data_9BTM
# 
_entry.id   9BTM 
# 
_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   9BTM         pdb_00009btm 10.2210/pdb9btm/pdb 
WWPDB D_1000283953 ?            ?                   
# 
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 2025-04-02 ? 
2 'Structure model' 1 1 2025-05-07 ? 
3 'Structure model' 1 2 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.title'                   
7  2 'Structure model' '_citation.year'                    
8  3 'Structure model' '_citation.pdbx_database_id_DOI'    
9  3 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 3 'Structure model' '_citation.title'                   
11 3 'Structure model' '_citation_author.identifier_ORCID' 
12 3 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BTM 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 zachary.hauseman@novartis.com Zachary Hauseman J 'principal investigator/group leader' 0000-0002-2581-2318 
3 dan.king@novartis.com         Daniel  King     A 'principal investigator/group leader' 0000-0002-2581-2318 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Hauseman, Z.J.' 1 0000-0002-0260-2326 
'King, D.'       2 0000-0002-2581-2318 
'Viscomi, J.'    3 ?                   
'Fodor, M.'      4 ?                   
# 
_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            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Targeting the SHOC2-RAS interaction in RAS-mutant cancers.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-025-08931-1 
_citation.pdbx_database_id_PubMed   40335703 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hauseman, Z.J.'        1  ?                   
primary 'Stauffer, F.'          2  ?                   
primary 'Beyer, K.S.'           3  0000-0002-3047-304X 
primary 'Molle, S.'             4  0009-0000-3288-7513 
primary 'Cavicchioli, E.'       5  ?                   
primary 'Marchand, J.R.'        6  0000-0002-8002-9457 
primary 'Fodor, M.'             7  ?                   
primary 'Viscomi, J.'           8  ?                   
primary 'Dhembi, A.'            9  ?                   
primary 'Katz, S.'              10 0009-0006-8730-9351 
primary 'Faggion, B.'           11 ?                   
primary 'Lanter, M.'            12 ?                   
primary 'Kerr, G.'              13 0009-0004-4231-518X 
primary 'Schildknecht, D.'      14 ?                   
primary 'Handl, C.'             15 ?                   
primary 'Maddalo, D.'           16 ?                   
primary 'Pissot Soldermann, C.' 17 ?                   
primary 'Brady, J.'             18 ?                   
primary 'Shrestha, O.'          19 ?                   
primary 'Nguyen, Z.'            20 ?                   
primary 'Leder, L.'             21 0009-0002-4378-6739 
primary 'Cremosnik, G.'         22 ?                   
primary 'Lopez Romero, S.'      23 ?                   
primary 'Hassiepen, U.'         24 ?                   
primary 'Stams, T.'             25 ?                   
primary 'Linder, M.'            26 ?                   
primary 'Galli, G.G.'           27 0000-0002-9401-060X 
primary 'Guthy, D.A.'           28 0000-0001-5324-8585 
primary 'King, D.A.'            29 ?                   
primary 'Maira, S.M.'           30 ?                   
primary 'Thoma, C.R.'           31 ?                   
primary 'Ehmke, V.'             32 ?                   
primary 'Tordella, L.'          33 0000-0002-0542-7834 
# 
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 'Leucine-rich repeat protein SHOC-2' 56583.418 1 ?       ?    ? ? 
2 polymer     man 'GTPase NRas'                        19243.855 1 3.6.5.2 Q61R ? ? 
3 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"          523.180   1 ?       ?    ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305    1 ?       ?    ? ? 
5 water       nat water                                18.015    9 ?       ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Protein soc-2 homolog,Protein sur-8 homolog' 
2 'Transforming protein N-Ras'                  
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLT
SLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCN
LITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI
STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFG
TWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLT
NNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ
IVAGGPSFIIQFLKMQGPYRAMV
;
;GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLT
SLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCN
LITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI
STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFG
TWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLT
NNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ
IVAGGPSFIIQFLKMQGPYRAMV
;
B ? 
2 'polypeptide(L)' no no 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGREEYSAMRDQYMRTGEGFLC
VFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLV
REIRQYRMK
;
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGREEYSAMRDQYMRTGEGFLC
VFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLV
REIRQYRMK
;
A ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "GUANOSINE-5'-TRIPHOSPHATE" GTP 
4 'MAGNESIUM ION'             MG  
5 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   THR n 
1 3   ARG n 
1 4   LYS n 
1 5   LYS n 
1 6   SER n 
1 7   SER n 
1 8   ASN n 
1 9   ALA n 
1 10  GLU n 
1 11  VAL n 
1 12  ILE n 
1 13  LYS n 
1 14  GLU n 
1 15  LEU n 
1 16  ASN n 
1 17  LYS n 
1 18  CYS n 
1 19  ARG n 
1 20  GLU n 
1 21  GLU n 
1 22  ASN n 
1 23  SER n 
1 24  MET n 
1 25  ARG n 
1 26  LEU n 
1 27  ASP n 
1 28  LEU n 
1 29  SER n 
1 30  LYS n 
1 31  ARG n 
1 32  SER n 
1 33  ILE n 
1 34  HIS n 
1 35  ILE n 
1 36  LEU n 
1 37  PRO n 
1 38  SER n 
1 39  SER n 
1 40  ILE n 
1 41  LYS n 
1 42  GLU n 
1 43  LEU n 
1 44  THR n 
1 45  GLN n 
1 46  LEU n 
1 47  THR n 
1 48  GLU n 
1 49  LEU n 
1 50  TYR n 
1 51  LEU n 
1 52  TYR n 
1 53  SER n 
1 54  ASN n 
1 55  LYS n 
1 56  LEU n 
1 57  GLN n 
1 58  SER n 
1 59  LEU n 
1 60  PRO n 
1 61  ALA n 
1 62  GLU n 
1 63  VAL n 
1 64  GLY n 
1 65  CYS n 
1 66  LEU n 
1 67  VAL n 
1 68  ASN n 
1 69  LEU n 
1 70  MET n 
1 71  THR n 
1 72  LEU n 
1 73  ALA n 
1 74  LEU n 
1 75  SER n 
1 76  GLU n 
1 77  ASN n 
1 78  SER n 
1 79  LEU n 
1 80  THR n 
1 81  SER n 
1 82  LEU n 
1 83  PRO n 
1 84  ASP n 
1 85  SER n 
1 86  LEU n 
1 87  ASP n 
1 88  ASN n 
1 89  LEU n 
1 90  LYS n 
1 91  LYS n 
1 92  LEU n 
1 93  ARG n 
1 94  MET n 
1 95  LEU n 
1 96  ASP n 
1 97  LEU n 
1 98  ARG n 
1 99  HIS n 
1 100 ASN n 
1 101 LYS n 
1 102 LEU n 
1 103 ARG n 
1 104 GLU n 
1 105 ILE n 
1 106 PRO n 
1 107 SER n 
1 108 VAL n 
1 109 VAL n 
1 110 TYR n 
1 111 ARG n 
1 112 LEU n 
1 113 ASP n 
1 114 SER n 
1 115 LEU n 
1 116 THR n 
1 117 THR n 
1 118 LEU n 
1 119 TYR n 
1 120 LEU n 
1 121 ARG n 
1 122 PHE n 
1 123 ASN n 
1 124 ARG n 
1 125 ILE n 
1 126 THR n 
1 127 THR n 
1 128 VAL n 
1 129 GLU n 
1 130 LYS n 
1 131 ASP n 
1 132 ILE n 
1 133 LYS n 
1 134 ASN n 
1 135 LEU n 
1 136 SER n 
1 137 LYS n 
1 138 LEU n 
1 139 SER n 
1 140 MET n 
1 141 LEU n 
1 142 SER n 
1 143 ILE n 
1 144 ARG n 
1 145 GLU n 
1 146 ASN n 
1 147 LYS n 
1 148 ILE n 
1 149 LYS n 
1 150 GLN n 
1 151 LEU n 
1 152 PRO n 
1 153 ALA n 
1 154 GLU n 
1 155 ILE n 
1 156 GLY n 
1 157 GLU n 
1 158 LEU n 
1 159 CYS n 
1 160 ASN n 
1 161 LEU n 
1 162 ILE n 
1 163 THR n 
1 164 LEU n 
1 165 ASP n 
1 166 VAL n 
1 167 ALA n 
1 168 HIS n 
1 169 ASN n 
1 170 GLN n 
1 171 LEU n 
1 172 GLU n 
1 173 HIS n 
1 174 LEU n 
1 175 PRO n 
1 176 LYS n 
1 177 GLU n 
1 178 ILE n 
1 179 GLY n 
1 180 ASN n 
1 181 CYS n 
1 182 THR n 
1 183 GLN n 
1 184 ILE n 
1 185 THR n 
1 186 ASN n 
1 187 LEU n 
1 188 ASP n 
1 189 LEU n 
1 190 GLN n 
1 191 HIS n 
1 192 ASN n 
1 193 GLU n 
1 194 LEU n 
1 195 LEU n 
1 196 ASP n 
1 197 LEU n 
1 198 PRO n 
1 199 ASP n 
1 200 THR n 
1 201 ILE n 
1 202 GLY n 
1 203 ASN n 
1 204 LEU n 
1 205 SER n 
1 206 SER n 
1 207 LEU n 
1 208 SER n 
1 209 ARG n 
1 210 LEU n 
1 211 GLY n 
1 212 LEU n 
1 213 ARG n 
1 214 TYR n 
1 215 ASN n 
1 216 ARG n 
1 217 LEU n 
1 218 SER n 
1 219 ALA n 
1 220 ILE n 
1 221 PRO n 
1 222 ARG n 
1 223 SER n 
1 224 LEU n 
1 225 ALA n 
1 226 LYS n 
1 227 CYS n 
1 228 SER n 
1 229 ALA n 
1 230 LEU n 
1 231 GLU n 
1 232 GLU n 
1 233 LEU n 
1 234 ASN n 
1 235 LEU n 
1 236 GLU n 
1 237 ASN n 
1 238 ASN n 
1 239 ASN n 
1 240 ILE n 
1 241 SER n 
1 242 THR n 
1 243 LEU n 
1 244 PRO n 
1 245 GLU n 
1 246 SER n 
1 247 LEU n 
1 248 LEU n 
1 249 SER n 
1 250 SER n 
1 251 LEU n 
1 252 VAL n 
1 253 LYS n 
1 254 LEU n 
1 255 ASN n 
1 256 SER n 
1 257 LEU n 
1 258 THR n 
1 259 LEU n 
1 260 ALA n 
1 261 ARG n 
1 262 ASN n 
1 263 CYS n 
1 264 PHE n 
1 265 GLN n 
1 266 LEU n 
1 267 TYR n 
1 268 PRO n 
1 269 VAL n 
1 270 GLY n 
1 271 GLY n 
1 272 PRO n 
1 273 SER n 
1 274 GLN n 
1 275 PHE n 
1 276 SER n 
1 277 THR n 
1 278 ILE n 
1 279 TYR n 
1 280 SER n 
1 281 LEU n 
1 282 ASN n 
1 283 MET n 
1 284 GLU n 
1 285 HIS n 
1 286 ASN n 
1 287 ARG n 
1 288 ILE n 
1 289 ASN n 
1 290 LYS n 
1 291 ILE n 
1 292 PRO n 
1 293 PHE n 
1 294 GLY n 
1 295 ILE n 
1 296 PHE n 
1 297 SER n 
1 298 ARG n 
1 299 ALA n 
1 300 LYS n 
1 301 VAL n 
1 302 LEU n 
1 303 SER n 
1 304 LYS n 
1 305 LEU n 
1 306 ASN n 
1 307 MET n 
1 308 LYS n 
1 309 ASP n 
1 310 ASN n 
1 311 GLN n 
1 312 LEU n 
1 313 THR n 
1 314 SER n 
1 315 LEU n 
1 316 PRO n 
1 317 LEU n 
1 318 ASP n 
1 319 PHE n 
1 320 GLY n 
1 321 THR n 
1 322 TRP n 
1 323 THR n 
1 324 SER n 
1 325 MET n 
1 326 VAL n 
1 327 GLU n 
1 328 LEU n 
1 329 ASN n 
1 330 LEU n 
1 331 ALA n 
1 332 THR n 
1 333 ASN n 
1 334 GLN n 
1 335 LEU n 
1 336 THR n 
1 337 LYS n 
1 338 ILE n 
1 339 PRO n 
1 340 GLU n 
1 341 ASP n 
1 342 VAL n 
1 343 SER n 
1 344 GLY n 
1 345 LEU n 
1 346 VAL n 
1 347 SER n 
1 348 LEU n 
1 349 GLU n 
1 350 VAL n 
1 351 LEU n 
1 352 ILE n 
1 353 LEU n 
1 354 SER n 
1 355 ASN n 
1 356 ASN n 
1 357 LEU n 
1 358 LEU n 
1 359 LYS n 
1 360 LYS n 
1 361 LEU n 
1 362 PRO n 
1 363 HIS n 
1 364 GLY n 
1 365 LEU n 
1 366 GLY n 
1 367 ASN n 
1 368 LEU n 
1 369 ARG n 
1 370 LYS n 
1 371 LEU n 
1 372 ARG n 
1 373 GLU n 
1 374 LEU n 
1 375 ASP n 
1 376 LEU n 
1 377 GLU n 
1 378 GLU n 
1 379 ASN n 
1 380 LYS n 
1 381 LEU n 
1 382 GLU n 
1 383 SER n 
1 384 LEU n 
1 385 PRO n 
1 386 ASN n 
1 387 GLU n 
1 388 ILE n 
1 389 ALA n 
1 390 TYR n 
1 391 LEU n 
1 392 LYS n 
1 393 ASP n 
1 394 LEU n 
1 395 GLN n 
1 396 LYS n 
1 397 LEU n 
1 398 VAL n 
1 399 LEU n 
1 400 THR n 
1 401 ASN n 
1 402 ASN n 
1 403 GLN n 
1 404 LEU n 
1 405 THR n 
1 406 THR n 
1 407 LEU n 
1 408 PRO n 
1 409 ARG n 
1 410 GLY n 
1 411 ILE n 
1 412 GLY n 
1 413 HIS n 
1 414 LEU n 
1 415 THR n 
1 416 ASN n 
1 417 LEU n 
1 418 THR n 
1 419 HIS n 
1 420 LEU n 
1 421 GLY n 
1 422 LEU n 
1 423 GLY n 
1 424 GLU n 
1 425 ASN n 
1 426 LEU n 
1 427 LEU n 
1 428 THR n 
1 429 HIS n 
1 430 LEU n 
1 431 PRO n 
1 432 GLU n 
1 433 GLU n 
1 434 ILE n 
1 435 GLY n 
1 436 THR n 
1 437 LEU n 
1 438 GLU n 
1 439 ASN n 
1 440 LEU n 
1 441 GLU n 
1 442 GLU n 
1 443 LEU n 
1 444 TYR n 
1 445 LEU n 
1 446 ASN n 
1 447 ASP n 
1 448 ASN n 
1 449 PRO n 
1 450 ASN n 
1 451 LEU n 
1 452 HIS n 
1 453 SER n 
1 454 LEU n 
1 455 PRO n 
1 456 PHE n 
1 457 GLU n 
1 458 LEU n 
1 459 ALA n 
1 460 LEU n 
1 461 CYS n 
1 462 SER n 
1 463 LYS n 
1 464 LEU n 
1 465 SER n 
1 466 ILE n 
1 467 MET n 
1 468 SER n 
1 469 ILE n 
1 470 GLU n 
1 471 ASN n 
1 472 CYS n 
1 473 PRO n 
1 474 LEU n 
1 475 SER n 
1 476 HIS n 
1 477 LEU n 
1 478 PRO n 
1 479 PRO n 
1 480 GLN n 
1 481 ILE n 
1 482 VAL n 
1 483 ALA n 
1 484 GLY n 
1 485 GLY n 
1 486 PRO n 
1 487 SER n 
1 488 PHE n 
1 489 ILE n 
1 490 ILE n 
1 491 GLN n 
1 492 PHE n 
1 493 LEU n 
1 494 LYS n 
1 495 MET n 
1 496 GLN n 
1 497 GLY n 
1 498 PRO n 
1 499 TYR n 
1 500 ARG n 
1 501 ALA n 
1 502 MET n 
1 503 VAL n 
2 1   MET n 
2 2   THR n 
2 3   GLU n 
2 4   TYR n 
2 5   LYS n 
2 6   LEU n 
2 7   VAL n 
2 8   VAL n 
2 9   VAL n 
2 10  GLY n 
2 11  ALA n 
2 12  GLY n 
2 13  GLY n 
2 14  VAL n 
2 15  GLY n 
2 16  LYS n 
2 17  SER n 
2 18  ALA n 
2 19  LEU n 
2 20  THR n 
2 21  ILE n 
2 22  GLN n 
2 23  LEU n 
2 24  ILE n 
2 25  GLN n 
2 26  ASN n 
2 27  HIS n 
2 28  PHE n 
2 29  VAL n 
2 30  ASP n 
2 31  GLU n 
2 32  TYR n 
2 33  ASP n 
2 34  PRO n 
2 35  THR n 
2 36  ILE n 
2 37  GLU n 
2 38  ASP n 
2 39  SER n 
2 40  TYR n 
2 41  ARG n 
2 42  LYS n 
2 43  GLN n 
2 44  VAL n 
2 45  VAL n 
2 46  ILE n 
2 47  ASP n 
2 48  GLY n 
2 49  GLU n 
2 50  THR n 
2 51  CYS n 
2 52  LEU n 
2 53  LEU n 
2 54  ASP n 
2 55  ILE n 
2 56  LEU n 
2 57  ASP n 
2 58  THR n 
2 59  ALA n 
2 60  GLY n 
2 61  ARG n 
2 62  GLU n 
2 63  GLU n 
2 64  TYR n 
2 65  SER n 
2 66  ALA n 
2 67  MET n 
2 68  ARG n 
2 69  ASP n 
2 70  GLN n 
2 71  TYR n 
2 72  MET n 
2 73  ARG n 
2 74  THR n 
2 75  GLY n 
2 76  GLU n 
2 77  GLY n 
2 78  PHE n 
2 79  LEU n 
2 80  CYS n 
2 81  VAL n 
2 82  PHE n 
2 83  ALA n 
2 84  ILE n 
2 85  ASN n 
2 86  ASN n 
2 87  SER n 
2 88  LYS n 
2 89  SER n 
2 90  PHE n 
2 91  ALA n 
2 92  ASP n 
2 93  ILE n 
2 94  ASN n 
2 95  LEU n 
2 96  TYR n 
2 97  ARG n 
2 98  GLU n 
2 99  GLN n 
2 100 ILE n 
2 101 LYS n 
2 102 ARG n 
2 103 VAL n 
2 104 LYS n 
2 105 ASP n 
2 106 SER n 
2 107 ASP n 
2 108 ASP n 
2 109 VAL n 
2 110 PRO n 
2 111 MET n 
2 112 VAL n 
2 113 LEU n 
2 114 VAL n 
2 115 GLY n 
2 116 ASN n 
2 117 LYS n 
2 118 CYS n 
2 119 ASP n 
2 120 LEU n 
2 121 PRO n 
2 122 THR n 
2 123 ARG n 
2 124 THR n 
2 125 VAL n 
2 126 ASP n 
2 127 THR n 
2 128 LYS n 
2 129 GLN n 
2 130 ALA n 
2 131 HIS n 
2 132 GLU n 
2 133 LEU n 
2 134 ALA n 
2 135 LYS n 
2 136 SER n 
2 137 TYR n 
2 138 GLY n 
2 139 ILE n 
2 140 PRO n 
2 141 PHE n 
2 142 ILE n 
2 143 GLU n 
2 144 THR n 
2 145 SER n 
2 146 ALA n 
2 147 LYS n 
2 148 THR n 
2 149 ARG n 
2 150 GLN n 
2 151 GLY n 
2 152 VAL n 
2 153 GLU n 
2 154 ASP n 
2 155 ALA n 
2 156 PHE n 
2 157 TYR n 
2 158 THR n 
2 159 LEU n 
2 160 VAL n 
2 161 ARG n 
2 162 GLU n 
2 163 ILE n 
2 164 ARG n 
2 165 GLN n 
2 166 TYR n 
2 167 ARG n 
2 168 MET n 
2 169 LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 503 human ? 'SHOC2, KIAA0862' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda'      7108   ? ? ? ? ? ? ? ? Sf21 ? ? ? ? ? ? ? ? ? pFastBac1 ? ? 
2 1 sample 'Biological sequence' 1 169 human ? 'NRAS, HRAS1'     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? ? ? ? pET13b    ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
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  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
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   80  ?   ?   ?   B . n 
A 1 2   THR 2   81  ?   ?   ?   B . n 
A 1 3   ARG 3   82  ?   ?   ?   B . n 
A 1 4   LYS 4   83  ?   ?   ?   B . n 
A 1 5   LYS 5   84  ?   ?   ?   B . n 
A 1 6   SER 6   85  ?   ?   ?   B . n 
A 1 7   SER 7   86  86  SER SER B . n 
A 1 8   ASN 8   87  87  ASN ASN B . n 
A 1 9   ALA 9   88  88  ALA ALA B . n 
A 1 10  GLU 10  89  89  GLU GLU B . n 
A 1 11  VAL 11  90  90  VAL VAL B . n 
A 1 12  ILE 12  91  91  ILE ILE B . n 
A 1 13  LYS 13  92  92  LYS LYS B . n 
A 1 14  GLU 14  93  93  GLU GLU B . n 
A 1 15  LEU 15  94  94  LEU LEU B . n 
A 1 16  ASN 16  95  95  ASN ASN B . n 
A 1 17  LYS 17  96  96  LYS LYS B . n 
A 1 18  CYS 18  97  97  CYS CYS B . n 
A 1 19  ARG 19  98  98  ARG ARG B . n 
A 1 20  GLU 20  99  99  GLU GLU B . n 
A 1 21  GLU 21  100 100 GLU GLU B . n 
A 1 22  ASN 22  101 101 ASN ASN B . n 
A 1 23  SER 23  102 102 SER SER B . n 
A 1 24  MET 24  103 103 MET MET B . n 
A 1 25  ARG 25  104 104 ARG ARG B . n 
A 1 26  LEU 26  105 105 LEU LEU B . n 
A 1 27  ASP 27  106 106 ASP ASP B . n 
A 1 28  LEU 28  107 107 LEU LEU B . n 
A 1 29  SER 29  108 108 SER SER B . n 
A 1 30  LYS 30  109 109 LYS LYS B . n 
A 1 31  ARG 31  110 110 ARG ARG B . n 
A 1 32  SER 32  111 111 SER SER B . n 
A 1 33  ILE 33  112 112 ILE ILE B . n 
A 1 34  HIS 34  113 113 HIS HIS B . n 
A 1 35  ILE 35  114 114 ILE ILE B . n 
A 1 36  LEU 36  115 115 LEU LEU B . n 
A 1 37  PRO 37  116 116 PRO PRO B . n 
A 1 38  SER 38  117 117 SER SER B . n 
A 1 39  SER 39  118 118 SER SER B . n 
A 1 40  ILE 40  119 119 ILE ILE B . n 
A 1 41  LYS 41  120 120 LYS LYS B . n 
A 1 42  GLU 42  121 121 GLU GLU B . n 
A 1 43  LEU 43  122 122 LEU LEU B . n 
A 1 44  THR 44  123 123 THR THR B . n 
A 1 45  GLN 45  124 124 GLN GLN B . n 
A 1 46  LEU 46  125 125 LEU LEU B . n 
A 1 47  THR 47  126 126 THR THR B . n 
A 1 48  GLU 48  127 127 GLU GLU B . n 
A 1 49  LEU 49  128 128 LEU LEU B . n 
A 1 50  TYR 50  129 129 TYR TYR B . n 
A 1 51  LEU 51  130 130 LEU LEU B . n 
A 1 52  TYR 52  131 131 TYR TYR B . n 
A 1 53  SER 53  132 132 SER SER B . n 
A 1 54  ASN 54  133 133 ASN ASN B . n 
A 1 55  LYS 55  134 134 LYS LYS B . n 
A 1 56  LEU 56  135 135 LEU LEU B . n 
A 1 57  GLN 57  136 136 GLN GLN B . n 
A 1 58  SER 58  137 137 SER SER B . n 
A 1 59  LEU 59  138 138 LEU LEU B . n 
A 1 60  PRO 60  139 139 PRO PRO B . n 
A 1 61  ALA 61  140 140 ALA ALA B . n 
A 1 62  GLU 62  141 141 GLU GLU B . n 
A 1 63  VAL 63  142 142 VAL VAL B . n 
A 1 64  GLY 64  143 143 GLY GLY B . n 
A 1 65  CYS 65  144 144 CYS CYS B . n 
A 1 66  LEU 66  145 145 LEU LEU B . n 
A 1 67  VAL 67  146 146 VAL VAL B . n 
A 1 68  ASN 68  147 147 ASN ASN B . n 
A 1 69  LEU 69  148 148 LEU LEU B . n 
A 1 70  MET 70  149 149 MET MET B . n 
A 1 71  THR 71  150 150 THR THR B . n 
A 1 72  LEU 72  151 151 LEU LEU B . n 
A 1 73  ALA 73  152 152 ALA ALA B . n 
A 1 74  LEU 74  153 153 LEU LEU B . n 
A 1 75  SER 75  154 154 SER SER B . n 
A 1 76  GLU 76  155 155 GLU GLU B . n 
A 1 77  ASN 77  156 156 ASN ASN B . n 
A 1 78  SER 78  157 157 SER SER B . n 
A 1 79  LEU 79  158 158 LEU LEU B . n 
A 1 80  THR 80  159 159 THR THR B . n 
A 1 81  SER 81  160 160 SER SER B . n 
A 1 82  LEU 82  161 161 LEU LEU B . n 
A 1 83  PRO 83  162 162 PRO PRO B . n 
A 1 84  ASP 84  163 163 ASP ASP B . n 
A 1 85  SER 85  164 164 SER SER B . n 
A 1 86  LEU 86  165 165 LEU LEU B . n 
A 1 87  ASP 87  166 166 ASP ASP B . n 
A 1 88  ASN 88  167 167 ASN ASN B . n 
A 1 89  LEU 89  168 168 LEU LEU B . n 
A 1 90  LYS 90  169 169 LYS LYS B . n 
A 1 91  LYS 91  170 170 LYS LYS B . n 
A 1 92  LEU 92  171 171 LEU LEU B . n 
A 1 93  ARG 93  172 172 ARG ARG B . n 
A 1 94  MET 94  173 173 MET MET B . n 
A 1 95  LEU 95  174 174 LEU LEU B . n 
A 1 96  ASP 96  175 175 ASP ASP B . n 
A 1 97  LEU 97  176 176 LEU LEU B . n 
A 1 98  ARG 98  177 177 ARG ARG B . n 
A 1 99  HIS 99  178 178 HIS HIS B . n 
A 1 100 ASN 100 179 179 ASN ASN B . n 
A 1 101 LYS 101 180 180 LYS LYS B . n 
A 1 102 LEU 102 181 181 LEU LEU B . n 
A 1 103 ARG 103 182 182 ARG ARG B . n 
A 1 104 GLU 104 183 183 GLU GLU B . n 
A 1 105 ILE 105 184 184 ILE ILE B . n 
A 1 106 PRO 106 185 185 PRO PRO B . n 
A 1 107 SER 107 186 186 SER SER B . n 
A 1 108 VAL 108 187 187 VAL VAL B . n 
A 1 109 VAL 109 188 188 VAL VAL B . n 
A 1 110 TYR 110 189 189 TYR TYR B . n 
A 1 111 ARG 111 190 190 ARG ARG B . n 
A 1 112 LEU 112 191 191 LEU LEU B . n 
A 1 113 ASP 113 192 192 ASP ASP B . n 
A 1 114 SER 114 193 193 SER SER B . n 
A 1 115 LEU 115 194 194 LEU LEU B . n 
A 1 116 THR 116 195 195 THR THR B . n 
A 1 117 THR 117 196 196 THR THR B . n 
A 1 118 LEU 118 197 197 LEU LEU B . n 
A 1 119 TYR 119 198 198 TYR TYR B . n 
A 1 120 LEU 120 199 199 LEU LEU B . n 
A 1 121 ARG 121 200 200 ARG ARG B . n 
A 1 122 PHE 122 201 201 PHE PHE B . n 
A 1 123 ASN 123 202 202 ASN ASN B . n 
A 1 124 ARG 124 203 203 ARG ARG B . n 
A 1 125 ILE 125 204 204 ILE ILE B . n 
A 1 126 THR 126 205 205 THR THR B . n 
A 1 127 THR 127 206 206 THR THR B . n 
A 1 128 VAL 128 207 207 VAL VAL B . n 
A 1 129 GLU 129 208 208 GLU GLU B . n 
A 1 130 LYS 130 209 209 LYS LYS B . n 
A 1 131 ASP 131 210 210 ASP ASP B . n 
A 1 132 ILE 132 211 211 ILE ILE B . n 
A 1 133 LYS 133 212 212 LYS LYS B . n 
A 1 134 ASN 134 213 213 ASN ASN B . n 
A 1 135 LEU 135 214 214 LEU LEU B . n 
A 1 136 SER 136 215 215 SER SER B . n 
A 1 137 LYS 137 216 216 LYS LYS B . n 
A 1 138 LEU 138 217 217 LEU LEU B . n 
A 1 139 SER 139 218 218 SER SER B . n 
A 1 140 MET 140 219 219 MET MET B . n 
A 1 141 LEU 141 220 220 LEU LEU B . n 
A 1 142 SER 142 221 221 SER SER B . n 
A 1 143 ILE 143 222 222 ILE ILE B . n 
A 1 144 ARG 144 223 223 ARG ARG B . n 
A 1 145 GLU 145 224 224 GLU GLU B . n 
A 1 146 ASN 146 225 225 ASN ASN B . n 
A 1 147 LYS 147 226 226 LYS LYS B . n 
A 1 148 ILE 148 227 227 ILE ILE B . n 
A 1 149 LYS 149 228 228 LYS LYS B . n 
A 1 150 GLN 150 229 229 GLN GLN B . n 
A 1 151 LEU 151 230 230 LEU LEU B . n 
A 1 152 PRO 152 231 231 PRO PRO B . n 
A 1 153 ALA 153 232 232 ALA ALA B . n 
A 1 154 GLU 154 233 233 GLU GLU B . n 
A 1 155 ILE 155 234 234 ILE ILE B . n 
A 1 156 GLY 156 235 235 GLY GLY B . n 
A 1 157 GLU 157 236 236 GLU GLU B . n 
A 1 158 LEU 158 237 237 LEU LEU B . n 
A 1 159 CYS 159 238 238 CYS CYS B . n 
A 1 160 ASN 160 239 239 ASN ASN B . n 
A 1 161 LEU 161 240 240 LEU LEU B . n 
A 1 162 ILE 162 241 241 ILE ILE B . n 
A 1 163 THR 163 242 242 THR THR B . n 
A 1 164 LEU 164 243 243 LEU LEU B . n 
A 1 165 ASP 165 244 244 ASP ASP B . n 
A 1 166 VAL 166 245 245 VAL VAL B . n 
A 1 167 ALA 167 246 246 ALA ALA B . n 
A 1 168 HIS 168 247 247 HIS HIS B . n 
A 1 169 ASN 169 248 248 ASN ASN B . n 
A 1 170 GLN 170 249 249 GLN GLN B . n 
A 1 171 LEU 171 250 250 LEU LEU B . n 
A 1 172 GLU 172 251 251 GLU GLU B . n 
A 1 173 HIS 173 252 252 HIS HIS B . n 
A 1 174 LEU 174 253 253 LEU LEU B . n 
A 1 175 PRO 175 254 254 PRO PRO B . n 
A 1 176 LYS 176 255 255 LYS LYS B . n 
A 1 177 GLU 177 256 256 GLU GLU B . n 
A 1 178 ILE 178 257 257 ILE ILE B . n 
A 1 179 GLY 179 258 258 GLY GLY B . n 
A 1 180 ASN 180 259 259 ASN ASN B . n 
A 1 181 CYS 181 260 260 CYS CYS B . n 
A 1 182 THR 182 261 261 THR THR B . n 
A 1 183 GLN 183 262 262 GLN GLN B . n 
A 1 184 ILE 184 263 263 ILE ILE B . n 
A 1 185 THR 185 264 264 THR THR B . n 
A 1 186 ASN 186 265 265 ASN ASN B . n 
A 1 187 LEU 187 266 266 LEU LEU B . n 
A 1 188 ASP 188 267 267 ASP ASP B . n 
A 1 189 LEU 189 268 268 LEU LEU B . n 
A 1 190 GLN 190 269 269 GLN GLN B . n 
A 1 191 HIS 191 270 270 HIS HIS B . n 
A 1 192 ASN 192 271 271 ASN ASN B . n 
A 1 193 GLU 193 272 272 GLU GLU B . n 
A 1 194 LEU 194 273 273 LEU LEU B . n 
A 1 195 LEU 195 274 274 LEU LEU B . n 
A 1 196 ASP 196 275 275 ASP ASP B . n 
A 1 197 LEU 197 276 276 LEU LEU B . n 
A 1 198 PRO 198 277 277 PRO PRO B . n 
A 1 199 ASP 199 278 278 ASP ASP B . n 
A 1 200 THR 200 279 279 THR THR B . n 
A 1 201 ILE 201 280 280 ILE ILE B . n 
A 1 202 GLY 202 281 281 GLY GLY B . n 
A 1 203 ASN 203 282 282 ASN ASN B . n 
A 1 204 LEU 204 283 283 LEU LEU B . n 
A 1 205 SER 205 284 284 SER SER B . n 
A 1 206 SER 206 285 285 SER SER B . n 
A 1 207 LEU 207 286 286 LEU LEU B . n 
A 1 208 SER 208 287 287 SER SER B . n 
A 1 209 ARG 209 288 288 ARG ARG B . n 
A 1 210 LEU 210 289 289 LEU LEU B . n 
A 1 211 GLY 211 290 290 GLY GLY B . n 
A 1 212 LEU 212 291 291 LEU LEU B . n 
A 1 213 ARG 213 292 292 ARG ARG B . n 
A 1 214 TYR 214 293 293 TYR TYR B . n 
A 1 215 ASN 215 294 294 ASN ASN B . n 
A 1 216 ARG 216 295 295 ARG ARG B . n 
A 1 217 LEU 217 296 296 LEU LEU B . n 
A 1 218 SER 218 297 297 SER SER B . n 
A 1 219 ALA 219 298 298 ALA ALA B . n 
A 1 220 ILE 220 299 299 ILE ILE B . n 
A 1 221 PRO 221 300 300 PRO PRO B . n 
A 1 222 ARG 222 301 301 ARG ARG B . n 
A 1 223 SER 223 302 302 SER SER B . n 
A 1 224 LEU 224 303 303 LEU LEU B . n 
A 1 225 ALA 225 304 304 ALA ALA B . n 
A 1 226 LYS 226 305 305 LYS LYS B . n 
A 1 227 CYS 227 306 306 CYS CYS B . n 
A 1 228 SER 228 307 307 SER SER B . n 
A 1 229 ALA 229 308 308 ALA ALA B . n 
A 1 230 LEU 230 309 309 LEU LEU B . n 
A 1 231 GLU 231 310 310 GLU GLU B . n 
A 1 232 GLU 232 311 311 GLU GLU B . n 
A 1 233 LEU 233 312 312 LEU LEU B . n 
A 1 234 ASN 234 313 313 ASN ASN B . n 
A 1 235 LEU 235 314 314 LEU LEU B . n 
A 1 236 GLU 236 315 315 GLU GLU B . n 
A 1 237 ASN 237 316 316 ASN ASN B . n 
A 1 238 ASN 238 317 317 ASN ASN B . n 
A 1 239 ASN 239 318 318 ASN ASN B . n 
A 1 240 ILE 240 319 319 ILE ILE B . n 
A 1 241 SER 241 320 320 SER SER B . n 
A 1 242 THR 242 321 321 THR THR B . n 
A 1 243 LEU 243 322 322 LEU LEU B . n 
A 1 244 PRO 244 323 323 PRO PRO B . n 
A 1 245 GLU 245 324 324 GLU GLU B . n 
A 1 246 SER 246 325 325 SER SER B . n 
A 1 247 LEU 247 326 326 LEU LEU B . n 
A 1 248 LEU 248 327 327 LEU LEU B . n 
A 1 249 SER 249 328 328 SER SER B . n 
A 1 250 SER 250 329 329 SER SER B . n 
A 1 251 LEU 251 330 330 LEU LEU B . n 
A 1 252 VAL 252 331 331 VAL VAL B . n 
A 1 253 LYS 253 332 332 LYS LYS B . n 
A 1 254 LEU 254 333 333 LEU LEU B . n 
A 1 255 ASN 255 334 334 ASN ASN B . n 
A 1 256 SER 256 335 335 SER SER B . n 
A 1 257 LEU 257 336 336 LEU LEU B . n 
A 1 258 THR 258 337 337 THR THR B . n 
A 1 259 LEU 259 338 338 LEU LEU B . n 
A 1 260 ALA 260 339 339 ALA ALA B . n 
A 1 261 ARG 261 340 340 ARG ARG B . n 
A 1 262 ASN 262 341 341 ASN ASN B . n 
A 1 263 CYS 263 342 342 CYS CYS B . n 
A 1 264 PHE 264 343 343 PHE PHE B . n 
A 1 265 GLN 265 344 344 GLN GLN B . n 
A 1 266 LEU 266 345 345 LEU LEU B . n 
A 1 267 TYR 267 346 346 TYR TYR B . n 
A 1 268 PRO 268 347 347 PRO PRO B . n 
A 1 269 VAL 269 348 348 VAL VAL B . n 
A 1 270 GLY 270 349 349 GLY GLY B . n 
A 1 271 GLY 271 350 350 GLY GLY B . n 
A 1 272 PRO 272 351 351 PRO PRO B . n 
A 1 273 SER 273 352 352 SER SER B . n 
A 1 274 GLN 274 353 353 GLN GLN B . n 
A 1 275 PHE 275 354 354 PHE PHE B . n 
A 1 276 SER 276 355 355 SER SER B . n 
A 1 277 THR 277 356 356 THR THR B . n 
A 1 278 ILE 278 357 357 ILE ILE B . n 
A 1 279 TYR 279 358 358 TYR TYR B . n 
A 1 280 SER 280 359 359 SER SER B . n 
A 1 281 LEU 281 360 360 LEU LEU B . n 
A 1 282 ASN 282 361 361 ASN ASN B . n 
A 1 283 MET 283 362 362 MET MET B . n 
A 1 284 GLU 284 363 363 GLU GLU B . n 
A 1 285 HIS 285 364 364 HIS HIS B . n 
A 1 286 ASN 286 365 365 ASN ASN B . n 
A 1 287 ARG 287 366 366 ARG ARG B . n 
A 1 288 ILE 288 367 367 ILE ILE B . n 
A 1 289 ASN 289 368 368 ASN ASN B . n 
A 1 290 LYS 290 369 369 LYS LYS B . n 
A 1 291 ILE 291 370 370 ILE ILE B . n 
A 1 292 PRO 292 371 371 PRO PRO B . n 
A 1 293 PHE 293 372 372 PHE PHE B . n 
A 1 294 GLY 294 373 373 GLY GLY B . n 
A 1 295 ILE 295 374 374 ILE ILE B . n 
A 1 296 PHE 296 375 375 PHE PHE B . n 
A 1 297 SER 297 376 376 SER SER B . n 
A 1 298 ARG 298 377 377 ARG ARG B . n 
A 1 299 ALA 299 378 378 ALA ALA B . n 
A 1 300 LYS 300 379 379 LYS LYS B . n 
A 1 301 VAL 301 380 380 VAL VAL B . n 
A 1 302 LEU 302 381 381 LEU LEU B . n 
A 1 303 SER 303 382 382 SER SER B . n 
A 1 304 LYS 304 383 383 LYS LYS B . n 
A 1 305 LEU 305 384 384 LEU LEU B . n 
A 1 306 ASN 306 385 385 ASN ASN B . n 
A 1 307 MET 307 386 386 MET MET B . n 
A 1 308 LYS 308 387 387 LYS LYS B . n 
A 1 309 ASP 309 388 388 ASP ASP B . n 
A 1 310 ASN 310 389 389 ASN ASN B . n 
A 1 311 GLN 311 390 390 GLN GLN B . n 
A 1 312 LEU 312 391 391 LEU LEU B . n 
A 1 313 THR 313 392 392 THR THR B . n 
A 1 314 SER 314 393 393 SER SER B . n 
A 1 315 LEU 315 394 394 LEU LEU B . n 
A 1 316 PRO 316 395 395 PRO PRO B . n 
A 1 317 LEU 317 396 396 LEU LEU B . n 
A 1 318 ASP 318 397 397 ASP ASP B . n 
A 1 319 PHE 319 398 398 PHE PHE B . n 
A 1 320 GLY 320 399 399 GLY GLY B . n 
A 1 321 THR 321 400 400 THR THR B . n 
A 1 322 TRP 322 401 401 TRP TRP B . n 
A 1 323 THR 323 402 402 THR THR B . n 
A 1 324 SER 324 403 403 SER SER B . n 
A 1 325 MET 325 404 404 MET MET B . n 
A 1 326 VAL 326 405 405 VAL VAL B . n 
A 1 327 GLU 327 406 406 GLU GLU B . n 
A 1 328 LEU 328 407 407 LEU LEU B . n 
A 1 329 ASN 329 408 408 ASN ASN B . n 
A 1 330 LEU 330 409 409 LEU LEU B . n 
A 1 331 ALA 331 410 410 ALA ALA B . n 
A 1 332 THR 332 411 411 THR THR B . n 
A 1 333 ASN 333 412 412 ASN ASN B . n 
A 1 334 GLN 334 413 413 GLN GLN B . n 
A 1 335 LEU 335 414 414 LEU LEU B . n 
A 1 336 THR 336 415 415 THR THR B . n 
A 1 337 LYS 337 416 416 LYS LYS B . n 
A 1 338 ILE 338 417 417 ILE ILE B . n 
A 1 339 PRO 339 418 418 PRO PRO B . n 
A 1 340 GLU 340 419 419 GLU GLU B . n 
A 1 341 ASP 341 420 420 ASP ASP B . n 
A 1 342 VAL 342 421 421 VAL VAL B . n 
A 1 343 SER 343 422 422 SER SER B . n 
A 1 344 GLY 344 423 423 GLY GLY B . n 
A 1 345 LEU 345 424 424 LEU LEU B . n 
A 1 346 VAL 346 425 425 VAL VAL B . n 
A 1 347 SER 347 426 426 SER SER B . n 
A 1 348 LEU 348 427 427 LEU LEU B . n 
A 1 349 GLU 349 428 428 GLU GLU B . n 
A 1 350 VAL 350 429 429 VAL VAL B . n 
A 1 351 LEU 351 430 430 LEU LEU B . n 
A 1 352 ILE 352 431 431 ILE ILE B . n 
A 1 353 LEU 353 432 432 LEU LEU B . n 
A 1 354 SER 354 433 433 SER SER B . n 
A 1 355 ASN 355 434 434 ASN ASN B . n 
A 1 356 ASN 356 435 435 ASN ASN B . n 
A 1 357 LEU 357 436 436 LEU LEU B . n 
A 1 358 LEU 358 437 437 LEU LEU B . n 
A 1 359 LYS 359 438 438 LYS LYS B . n 
A 1 360 LYS 360 439 439 LYS LYS B . n 
A 1 361 LEU 361 440 440 LEU LEU B . n 
A 1 362 PRO 362 441 441 PRO PRO B . n 
A 1 363 HIS 363 442 442 HIS HIS B . n 
A 1 364 GLY 364 443 443 GLY GLY B . n 
A 1 365 LEU 365 444 444 LEU LEU B . n 
A 1 366 GLY 366 445 445 GLY GLY B . n 
A 1 367 ASN 367 446 446 ASN ASN B . n 
A 1 368 LEU 368 447 447 LEU LEU B . n 
A 1 369 ARG 369 448 448 ARG ARG B . n 
A 1 370 LYS 370 449 449 LYS LYS B . n 
A 1 371 LEU 371 450 450 LEU LEU B . n 
A 1 372 ARG 372 451 451 ARG ARG B . n 
A 1 373 GLU 373 452 452 GLU GLU B . n 
A 1 374 LEU 374 453 453 LEU LEU B . n 
A 1 375 ASP 375 454 454 ASP ASP B . n 
A 1 376 LEU 376 455 455 LEU LEU B . n 
A 1 377 GLU 377 456 456 GLU GLU B . n 
A 1 378 GLU 378 457 457 GLU GLU B . n 
A 1 379 ASN 379 458 458 ASN ASN B . n 
A 1 380 LYS 380 459 459 LYS LYS B . n 
A 1 381 LEU 381 460 460 LEU LEU B . n 
A 1 382 GLU 382 461 461 GLU GLU B . n 
A 1 383 SER 383 462 462 SER SER B . n 
A 1 384 LEU 384 463 463 LEU LEU B . n 
A 1 385 PRO 385 464 464 PRO PRO B . n 
A 1 386 ASN 386 465 465 ASN ASN B . n 
A 1 387 GLU 387 466 466 GLU GLU B . n 
A 1 388 ILE 388 467 467 ILE ILE B . n 
A 1 389 ALA 389 468 468 ALA ALA B . n 
A 1 390 TYR 390 469 469 TYR TYR B . n 
A 1 391 LEU 391 470 470 LEU LEU B . n 
A 1 392 LYS 392 471 471 LYS LYS B . n 
A 1 393 ASP 393 472 472 ASP ASP B . n 
A 1 394 LEU 394 473 473 LEU LEU B . n 
A 1 395 GLN 395 474 474 GLN GLN B . n 
A 1 396 LYS 396 475 475 LYS LYS B . n 
A 1 397 LEU 397 476 476 LEU LEU B . n 
A 1 398 VAL 398 477 477 VAL VAL B . n 
A 1 399 LEU 399 478 478 LEU LEU B . n 
A 1 400 THR 400 479 479 THR THR B . n 
A 1 401 ASN 401 480 480 ASN ASN B . n 
A 1 402 ASN 402 481 481 ASN ASN B . n 
A 1 403 GLN 403 482 482 GLN GLN B . n 
A 1 404 LEU 404 483 483 LEU LEU B . n 
A 1 405 THR 405 484 484 THR THR B . n 
A 1 406 THR 406 485 485 THR THR B . n 
A 1 407 LEU 407 486 486 LEU LEU B . n 
A 1 408 PRO 408 487 487 PRO PRO B . n 
A 1 409 ARG 409 488 488 ARG ARG B . n 
A 1 410 GLY 410 489 489 GLY GLY B . n 
A 1 411 ILE 411 490 490 ILE ILE B . n 
A 1 412 GLY 412 491 491 GLY GLY B . n 
A 1 413 HIS 413 492 492 HIS HIS B . n 
A 1 414 LEU 414 493 493 LEU LEU B . n 
A 1 415 THR 415 494 494 THR THR B . n 
A 1 416 ASN 416 495 495 ASN ASN B . n 
A 1 417 LEU 417 496 496 LEU LEU B . n 
A 1 418 THR 418 497 497 THR THR B . n 
A 1 419 HIS 419 498 498 HIS HIS B . n 
A 1 420 LEU 420 499 499 LEU LEU B . n 
A 1 421 GLY 421 500 500 GLY GLY B . n 
A 1 422 LEU 422 501 501 LEU LEU B . n 
A 1 423 GLY 423 502 502 GLY GLY B . n 
A 1 424 GLU 424 503 503 GLU GLU B . n 
A 1 425 ASN 425 504 504 ASN ASN B . n 
A 1 426 LEU 426 505 505 LEU LEU B . n 
A 1 427 LEU 427 506 506 LEU LEU B . n 
A 1 428 THR 428 507 507 THR THR B . n 
A 1 429 HIS 429 508 508 HIS HIS B . n 
A 1 430 LEU 430 509 509 LEU LEU B . n 
A 1 431 PRO 431 510 510 PRO PRO B . n 
A 1 432 GLU 432 511 511 GLU GLU B . n 
A 1 433 GLU 433 512 512 GLU GLU B . n 
A 1 434 ILE 434 513 513 ILE ILE B . n 
A 1 435 GLY 435 514 514 GLY GLY B . n 
A 1 436 THR 436 515 515 THR THR B . n 
A 1 437 LEU 437 516 516 LEU LEU B . n 
A 1 438 GLU 438 517 517 GLU GLU B . n 
A 1 439 ASN 439 518 518 ASN ASN B . n 
A 1 440 LEU 440 519 519 LEU LEU B . n 
A 1 441 GLU 441 520 520 GLU GLU B . n 
A 1 442 GLU 442 521 521 GLU GLU B . n 
A 1 443 LEU 443 522 522 LEU LEU B . n 
A 1 444 TYR 444 523 523 TYR TYR B . n 
A 1 445 LEU 445 524 524 LEU LEU B . n 
A 1 446 ASN 446 525 525 ASN ASN B . n 
A 1 447 ASP 447 526 526 ASP ASP B . n 
A 1 448 ASN 448 527 527 ASN ASN B . n 
A 1 449 PRO 449 528 528 PRO PRO B . n 
A 1 450 ASN 450 529 529 ASN ASN B . n 
A 1 451 LEU 451 530 530 LEU LEU B . n 
A 1 452 HIS 452 531 531 HIS HIS B . n 
A 1 453 SER 453 532 532 SER SER B . n 
A 1 454 LEU 454 533 533 LEU LEU B . n 
A 1 455 PRO 455 534 534 PRO PRO B . n 
A 1 456 PHE 456 535 535 PHE PHE B . n 
A 1 457 GLU 457 536 536 GLU GLU B . n 
A 1 458 LEU 458 537 537 LEU LEU B . n 
A 1 459 ALA 459 538 538 ALA ALA B . n 
A 1 460 LEU 460 539 539 LEU LEU B . n 
A 1 461 CYS 461 540 540 CYS CYS B . n 
A 1 462 SER 462 541 541 SER SER B . n 
A 1 463 LYS 463 542 542 LYS LYS B . n 
A 1 464 LEU 464 543 543 LEU LEU B . n 
A 1 465 SER 465 544 544 SER SER B . n 
A 1 466 ILE 466 545 545 ILE ILE B . n 
A 1 467 MET 467 546 546 MET MET B . n 
A 1 468 SER 468 547 547 SER SER B . n 
A 1 469 ILE 469 548 548 ILE ILE B . n 
A 1 470 GLU 470 549 549 GLU GLU B . n 
A 1 471 ASN 471 550 550 ASN ASN B . n 
A 1 472 CYS 472 551 551 CYS CYS B . n 
A 1 473 PRO 473 552 552 PRO PRO B . n 
A 1 474 LEU 474 553 553 LEU LEU B . n 
A 1 475 SER 475 554 554 SER SER B . n 
A 1 476 HIS 476 555 555 HIS HIS B . n 
A 1 477 LEU 477 556 556 LEU LEU B . n 
A 1 478 PRO 478 557 557 PRO PRO B . n 
A 1 479 PRO 479 558 558 PRO PRO B . n 
A 1 480 GLN 480 559 559 GLN GLN B . n 
A 1 481 ILE 481 560 560 ILE ILE B . n 
A 1 482 VAL 482 561 561 VAL VAL B . n 
A 1 483 ALA 483 562 562 ALA ALA B . n 
A 1 484 GLY 484 563 563 GLY GLY B . n 
A 1 485 GLY 485 564 564 GLY GLY B . n 
A 1 486 PRO 486 565 565 PRO PRO B . n 
A 1 487 SER 487 566 566 SER SER B . n 
A 1 488 PHE 488 567 567 PHE PHE B . n 
A 1 489 ILE 489 568 568 ILE ILE B . n 
A 1 490 ILE 490 569 569 ILE ILE B . n 
A 1 491 GLN 491 570 570 GLN GLN B . n 
A 1 492 PHE 492 571 571 PHE PHE B . n 
A 1 493 LEU 493 572 572 LEU LEU B . n 
A 1 494 LYS 494 573 573 LYS LYS B . n 
A 1 495 MET 495 574 574 MET MET B . n 
A 1 496 GLN 496 575 575 GLN GLN B . n 
A 1 497 GLY 497 576 576 GLY GLY B . n 
A 1 498 PRO 498 577 ?   ?   ?   B . n 
A 1 499 TYR 499 578 ?   ?   ?   B . n 
A 1 500 ARG 500 579 ?   ?   ?   B . n 
A 1 501 ALA 501 580 ?   ?   ?   B . n 
A 1 502 MET 502 581 ?   ?   ?   B . n 
A 1 503 VAL 503 582 ?   ?   ?   B . n 
B 2 1   MET 1   1   1   MET MET A . n 
B 2 2   THR 2   2   2   THR THR A . n 
B 2 3   GLU 3   3   3   GLU GLU A . n 
B 2 4   TYR 4   4   4   TYR TYR A . n 
B 2 5   LYS 5   5   5   LYS LYS A . n 
B 2 6   LEU 6   6   6   LEU LEU A . n 
B 2 7   VAL 7   7   7   VAL VAL A . n 
B 2 8   VAL 8   8   8   VAL VAL A . n 
B 2 9   VAL 9   9   9   VAL VAL A . n 
B 2 10  GLY 10  10  10  GLY GLY A . n 
B 2 11  ALA 11  11  11  ALA ALA A . n 
B 2 12  GLY 12  12  12  GLY GLY A . n 
B 2 13  GLY 13  13  13  GLY GLY A . n 
B 2 14  VAL 14  14  14  VAL VAL A . n 
B 2 15  GLY 15  15  15  GLY GLY A . n 
B 2 16  LYS 16  16  16  LYS LYS A . n 
B 2 17  SER 17  17  17  SER SER A . n 
B 2 18  ALA 18  18  18  ALA ALA A . n 
B 2 19  LEU 19  19  19  LEU LEU A . n 
B 2 20  THR 20  20  20  THR THR A . n 
B 2 21  ILE 21  21  21  ILE ILE A . n 
B 2 22  GLN 22  22  22  GLN GLN A . n 
B 2 23  LEU 23  23  23  LEU LEU A . n 
B 2 24  ILE 24  24  24  ILE ILE A . n 
B 2 25  GLN 25  25  25  GLN GLN A . n 
B 2 26  ASN 26  26  26  ASN ASN A . n 
B 2 27  HIS 27  27  27  HIS HIS A . n 
B 2 28  PHE 28  28  28  PHE PHE A . n 
B 2 29  VAL 29  29  29  VAL VAL A . n 
B 2 30  ASP 30  30  30  ASP ASP A . n 
B 2 31  GLU 31  31  31  GLU GLU A . n 
B 2 32  TYR 32  32  32  TYR TYR A . n 
B 2 33  ASP 33  33  33  ASP ASP A . n 
B 2 34  PRO 34  34  34  PRO PRO A . n 
B 2 35  THR 35  35  35  THR THR A . n 
B 2 36  ILE 36  36  36  ILE ILE A . n 
B 2 37  GLU 37  37  37  GLU GLU A . n 
B 2 38  ASP 38  38  38  ASP ASP A . n 
B 2 39  SER 39  39  39  SER SER A . n 
B 2 40  TYR 40  40  40  TYR TYR A . n 
B 2 41  ARG 41  41  41  ARG ARG A . n 
B 2 42  LYS 42  42  42  LYS LYS A . n 
B 2 43  GLN 43  43  43  GLN GLN A . n 
B 2 44  VAL 44  44  44  VAL VAL A . n 
B 2 45  VAL 45  45  45  VAL VAL A . n 
B 2 46  ILE 46  46  46  ILE ILE A . n 
B 2 47  ASP 47  47  47  ASP ASP A . n 
B 2 48  GLY 48  48  48  GLY GLY A . n 
B 2 49  GLU 49  49  49  GLU GLU A . n 
B 2 50  THR 50  50  50  THR THR A . n 
B 2 51  CYS 51  51  51  CYS CYS A . n 
B 2 52  LEU 52  52  52  LEU LEU A . n 
B 2 53  LEU 53  53  53  LEU LEU A . n 
B 2 54  ASP 54  54  54  ASP ASP A . n 
B 2 55  ILE 55  55  55  ILE ILE A . n 
B 2 56  LEU 56  56  56  LEU LEU A . n 
B 2 57  ASP 57  57  57  ASP ASP A . n 
B 2 58  THR 58  58  58  THR THR A . n 
B 2 59  ALA 59  59  59  ALA ALA A . n 
B 2 60  GLY 60  60  60  GLY GLY A . n 
B 2 61  ARG 61  61  61  ARG ARG A . n 
B 2 62  GLU 62  62  62  GLU GLU A . n 
B 2 63  GLU 63  63  63  GLU GLU A . n 
B 2 64  TYR 64  64  64  TYR TYR A . n 
B 2 65  SER 65  65  65  SER SER A . n 
B 2 66  ALA 66  66  66  ALA ALA A . n 
B 2 67  MET 67  67  67  MET MET A . n 
B 2 68  ARG 68  68  68  ARG ARG A . n 
B 2 69  ASP 69  69  69  ASP ASP A . n 
B 2 70  GLN 70  70  70  GLN GLN A . n 
B 2 71  TYR 71  71  71  TYR TYR A . n 
B 2 72  MET 72  72  72  MET MET A . n 
B 2 73  ARG 73  73  73  ARG ARG A . n 
B 2 74  THR 74  74  74  THR THR A . n 
B 2 75  GLY 75  75  75  GLY GLY A . n 
B 2 76  GLU 76  76  76  GLU GLU A . n 
B 2 77  GLY 77  77  77  GLY GLY A . n 
B 2 78  PHE 78  78  78  PHE PHE A . n 
B 2 79  LEU 79  79  79  LEU LEU A . n 
B 2 80  CYS 80  80  80  CYS CYS A . n 
B 2 81  VAL 81  81  81  VAL VAL A . n 
B 2 82  PHE 82  82  82  PHE PHE A . n 
B 2 83  ALA 83  83  83  ALA ALA A . n 
B 2 84  ILE 84  84  84  ILE ILE A . n 
B 2 85  ASN 85  85  85  ASN ASN A . n 
B 2 86  ASN 86  86  86  ASN ASN A . n 
B 2 87  SER 87  87  87  SER SER A . n 
B 2 88  LYS 88  88  88  LYS LYS A . n 
B 2 89  SER 89  89  89  SER SER A . n 
B 2 90  PHE 90  90  90  PHE PHE A . n 
B 2 91  ALA 91  91  91  ALA ALA A . n 
B 2 92  ASP 92  92  92  ASP ASP A . n 
B 2 93  ILE 93  93  93  ILE ILE A . n 
B 2 94  ASN 94  94  94  ASN ASN A . n 
B 2 95  LEU 95  95  95  LEU LEU A . n 
B 2 96  TYR 96  96  96  TYR TYR A . n 
B 2 97  ARG 97  97  97  ARG ARG A . n 
B 2 98  GLU 98  98  98  GLU GLU A . n 
B 2 99  GLN 99  99  99  GLN GLN A . n 
B 2 100 ILE 100 100 100 ILE ILE A . n 
B 2 101 LYS 101 101 101 LYS LYS A . n 
B 2 102 ARG 102 102 102 ARG ARG A . n 
B 2 103 VAL 103 103 103 VAL VAL A . n 
B 2 104 LYS 104 104 104 LYS LYS A . n 
B 2 105 ASP 105 105 105 ASP ASP A . n 
B 2 106 SER 106 106 106 SER SER A . n 
B 2 107 ASP 107 107 107 ASP ASP A . n 
B 2 108 ASP 108 108 108 ASP ASP A . n 
B 2 109 VAL 109 109 109 VAL VAL A . n 
B 2 110 PRO 110 110 110 PRO PRO A . n 
B 2 111 MET 111 111 111 MET MET A . n 
B 2 112 VAL 112 112 112 VAL VAL A . n 
B 2 113 LEU 113 113 113 LEU LEU A . n 
B 2 114 VAL 114 114 114 VAL VAL A . n 
B 2 115 GLY 115 115 115 GLY GLY A . n 
B 2 116 ASN 116 116 116 ASN ASN A . n 
B 2 117 LYS 117 117 117 LYS LYS A . n 
B 2 118 CYS 118 118 118 CYS CYS A . n 
B 2 119 ASP 119 119 119 ASP ASP A . n 
B 2 120 LEU 120 120 120 LEU LEU A . n 
B 2 121 PRO 121 121 121 PRO PRO A . n 
B 2 122 THR 122 122 122 THR THR A . n 
B 2 123 ARG 123 123 123 ARG ARG A . n 
B 2 124 THR 124 124 124 THR THR A . n 
B 2 125 VAL 125 125 125 VAL VAL A . n 
B 2 126 ASP 126 126 126 ASP ASP A . n 
B 2 127 THR 127 127 127 THR THR A . n 
B 2 128 LYS 128 128 128 LYS LYS A . n 
B 2 129 GLN 129 129 129 GLN GLN A . n 
B 2 130 ALA 130 130 130 ALA ALA A . n 
B 2 131 HIS 131 131 131 HIS HIS A . n 
B 2 132 GLU 132 132 132 GLU GLU A . n 
B 2 133 LEU 133 133 133 LEU LEU A . n 
B 2 134 ALA 134 134 134 ALA ALA A . n 
B 2 135 LYS 135 135 135 LYS LYS A . n 
B 2 136 SER 136 136 136 SER SER A . n 
B 2 137 TYR 137 137 137 TYR TYR A . n 
B 2 138 GLY 138 138 138 GLY GLY A . n 
B 2 139 ILE 139 139 139 ILE ILE A . n 
B 2 140 PRO 140 140 140 PRO PRO A . n 
B 2 141 PHE 141 141 141 PHE PHE A . n 
B 2 142 ILE 142 142 142 ILE ILE A . n 
B 2 143 GLU 143 143 143 GLU GLU A . n 
B 2 144 THR 144 144 144 THR THR A . n 
B 2 145 SER 145 145 145 SER SER A . n 
B 2 146 ALA 146 146 146 ALA ALA A . n 
B 2 147 LYS 147 147 147 LYS LYS A . n 
B 2 148 THR 148 148 148 THR THR A . n 
B 2 149 ARG 149 149 149 ARG ARG A . n 
B 2 150 GLN 150 150 150 GLN GLN A . n 
B 2 151 GLY 151 151 151 GLY GLY A . n 
B 2 152 VAL 152 152 152 VAL VAL A . n 
B 2 153 GLU 153 153 153 GLU GLU A . n 
B 2 154 ASP 154 154 154 ASP ASP A . n 
B 2 155 ALA 155 155 155 ALA ALA A . n 
B 2 156 PHE 156 156 156 PHE PHE A . n 
B 2 157 TYR 157 157 157 TYR TYR A . n 
B 2 158 THR 158 158 158 THR THR A . n 
B 2 159 LEU 159 159 159 LEU LEU A . n 
B 2 160 VAL 160 160 160 VAL VAL A . n 
B 2 161 ARG 161 161 161 ARG ARG A . n 
B 2 162 GLU 162 162 162 GLU GLU A . n 
B 2 163 ILE 163 163 163 ILE ILE A . n 
B 2 164 ARG 164 164 164 ARG ARG A . n 
B 2 165 GLN 165 165 165 GLN GLN A . n 
B 2 166 TYR 166 166 166 TYR TYR A . n 
B 2 167 ARG 167 167 167 ARG ARG A . n 
B 2 168 MET 168 168 168 MET MET A . n 
B 2 169 LYS 169 169 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 GTP 1 201 201 GTP GTP A . 
D 4 MG  1 202 202 MG  MG  A . 
E 5 HOH 1 601 17  HOH HOH B . 
E 5 HOH 2 602 46  HOH HOH B . 
E 5 HOH 3 603 47  HOH HOH B . 
F 5 HOH 1 301 6   HOH HOH A . 
F 5 HOH 2 302 45  HOH HOH A . 
F 5 HOH 3 303 24  HOH HOH A . 
F 5 HOH 4 304 1   HOH HOH A . 
F 5 HOH 5 305 2   HOH HOH A . 
F 5 HOH 6 306 40  HOH HOH A . 
# 
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   ? ? ? 1.21.1_5286 1 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BTM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.884 
_cell.length_a_esd                 ? 
_cell.length_b                     89.339 
_cell.length_b_esd                 ? 
_cell.length_c                     119.768 
_cell.length_c_esd                 ? 
_cell.volume                       844048.006 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BTM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BTM 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.80 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Hepes pH 7, 15% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-13 
_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   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          82.58 
_reflns.entry_id                                       9BTM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.7 
_reflns.d_resolution_low                               71.58 
_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                                     23050 
_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                                15 
_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                                ? 
_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                              0.16 
_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                                    2.732 
_reflns_shell.d_res_low                                     2.741 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             225 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.359 
_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                                  ? 
_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                               85.23 
_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                                 9BTM 
_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                            2.73 
_refine.ls_d_res_low                             59.88 
_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                     22829 
_refine.ls_number_reflns_R_free                  1033 
_refine.ls_number_reflns_R_work                  21796 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.94 
_refine.ls_percent_reflns_R_free                 4.52 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2037 
_refine.ls_R_factor_R_free                       0.2382 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.6995 
_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                            0.4266 
_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                       2.73 
_refine_hist.d_res_low                        59.88 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               5247 
_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        5205 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.0020  ? 5320 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4967  ? 7211 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0394  ? 861  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0033  ? 919  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.6873 ? 2052 ? f_dihedral_angle_d ? ? 
# 
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' 2.73 2.88  . . 126 2890 92.77  . . . . 0.3408 . . . . . . . . . . . 0.4102 
'X-RAY DIFFRACTION' 2.88 3.06  . . 137 3104 99.97  . . . . 0.3085 . . . . . . . . . . . 0.3569 
'X-RAY DIFFRACTION' 3.06 3.29  . . 137 3107 100.00 . . . . 0.2792 . . . . . . . . . . . 0.3352 
'X-RAY DIFFRACTION' 3.29 3.62  . . 168 3094 99.97  . . . . 0.2491 . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 3.62 4.15  . . 168 3115 100.00 . . . . 0.1932 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 4.15 5.23  . . 151 3173 100.00 . . . . 0.1677 . . . . . . . . . . . 0.1923 
'X-RAY DIFFRACTION' 5.23 59.88 . . 146 3313 99.80  . . . . 0.1746 . . . . . . . . . . . 0.2019 
# 
_struct.entry_id                     9BTM 
_struct.title                        'NRas 1-169 Q61R in Complex with Shoc2 80-582' 
_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        9BTM 
_struct_keywords.text            'SHOC2, RAS, PP1C, MAPK, Complex, STRUCTURAL PROTEIN, SIGNALING PROTEIN-HYDROLASE complex' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN/HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SHOC2_HUMAN Q9UQ13 ? 1 
;GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLT
SLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCN
LITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI
STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFG
TWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLT
NNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ
IVAGGPSFIIQFLKMQGPYRAMV
;
80 
2 UNP RASN_HUMAN  P01111 ? 2 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLV
REIRQYRMK
;
1  
# 
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 9BTM B 1 ? 503 ? Q9UQ13 80 ? 582 ? 80 582 
2 2 9BTM A 1 ? 169 ? P01111 1  ? 169 ? 1  169 
# 
_struct_ref_seq_dif.align_id                     2 
_struct_ref_seq_dif.pdbx_pdb_id_code             9BTM 
_struct_ref_seq_dif.mon_id                       ARG 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      61 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P01111 
_struct_ref_seq_dif.db_mon_id                    GLN 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          61 
_struct_ref_seq_dif.details                      variant 
_struct_ref_seq_dif.pdbx_auth_seq_num            61 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 7   ? ASN A 22  ? SER B 86  ASN B 101 1 ? 16 
HELX_P HELX_P2  AA2 PRO A 37  ? LEU A 43  ? PRO B 116 LEU B 122 5 ? 7  
HELX_P HELX_P3  AA3 PRO A 60  ? LEU A 66  ? PRO B 139 LEU B 145 5 ? 7  
HELX_P HELX_P4  AA4 PRO A 83  ? LEU A 89  ? PRO B 162 LEU B 168 5 ? 7  
HELX_P HELX_P5  AA5 VAL A 108 ? LEU A 112 ? VAL B 187 LEU B 191 5 ? 5  
HELX_P HELX_P6  AA6 GLU A 129 ? LEU A 135 ? GLU B 208 LEU B 214 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 152 ? LEU A 158 ? PRO B 231 LEU B 237 5 ? 7  
HELX_P HELX_P8  AA8 PRO A 175 ? CYS A 181 ? PRO B 254 CYS B 260 5 ? 7  
HELX_P HELX_P9  AA9 PRO A 198 ? LEU A 204 ? PRO B 277 LEU B 283 5 ? 7  
HELX_P HELX_P10 AB1 PRO A 221 ? CYS A 227 ? PRO B 300 CYS B 306 5 ? 7  
HELX_P HELX_P11 AB2 GLY A 271 ? PHE A 275 ? GLY B 350 PHE B 354 5 ? 5  
HELX_P HELX_P12 AB3 PRO A 316 ? TRP A 322 ? PRO B 395 TRP B 401 5 ? 7  
HELX_P HELX_P13 AB4 PRO A 339 ? LEU A 345 ? PRO B 418 LEU B 424 5 ? 7  
HELX_P HELX_P14 AB5 PRO A 362 ? LEU A 368 ? PRO B 441 LEU B 447 5 ? 7  
HELX_P HELX_P15 AB6 PRO A 385 ? LEU A 391 ? PRO B 464 LEU B 470 5 ? 7  
HELX_P HELX_P16 AB7 PRO A 408 ? LEU A 414 ? PRO B 487 LEU B 493 5 ? 7  
HELX_P HELX_P17 AB8 PRO A 431 ? LEU A 437 ? PRO B 510 LEU B 516 5 ? 7  
HELX_P HELX_P18 AB9 PRO A 455 ? CYS A 461 ? PRO B 534 CYS B 540 5 ? 7  
HELX_P HELX_P19 AC1 PRO A 478 ? GLY A 485 ? PRO B 557 GLY B 564 1 ? 8  
HELX_P HELX_P20 AC2 GLY A 485 ? GLN A 496 ? GLY B 564 GLN B 575 1 ? 12 
HELX_P HELX_P21 AC3 GLY B 15  ? ASN B 26  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P22 AC4 MET B 67  ? GLY B 75  ? MET A 67  GLY A 75  1 ? 9  
HELX_P HELX_P23 AC5 ASN B 86  ? ASP B 92  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P24 AC6 ASP B 92  ? LYS B 104 ? ASP A 92  LYS A 104 1 ? 13 
HELX_P HELX_P25 AC7 ASP B 126 ? GLY B 138 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P26 AC8 GLY B 151 ? MET B 168 ? GLY A 151 MET A 168 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? B SER 17 OG  ? ? ? 1_555 D MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc2 metalc ? ? B THR 35 OG1 ? ? ? 1_555 D MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc3 metalc ? ? C GTP .  O2G ? ? ? 1_555 D MG  . MG ? ? A GTP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc4 metalc ? ? C GTP .  O1B ? ? ? 1_555 D MG  . MG ? ? A GTP 201 A MG  202 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc5 metalc ? ? D MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 303 1_555 ? ? ? ? ? ? ? 2.194 ? ? 
metalc6 metalc ? ? D MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 305 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? B SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 OG1 ? B THR 35 ? A THR 35  ? 1_555 85.3  ? 
2  OG  ? B SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O2G ? C GTP .  ? A GTP 201 ? 1_555 155.6 ? 
3  OG1 ? B THR 35 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O2G ? C GTP .  ? A GTP 201 ? 1_555 92.4  ? 
4  OG  ? B SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O1B ? C GTP .  ? A GTP 201 ? 1_555 84.6  ? 
5  OG1 ? B THR 35 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O1B ? C GTP .  ? A GTP 201 ? 1_555 157.3 ? 
6  O2G ? C GTP .  ? A GTP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O1B ? C GTP .  ? A GTP 201 ? 1_555 88.6  ? 
7  OG  ? B SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 303 ? 1_555 74.0  ? 
8  OG1 ? B THR 35 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 303 ? 1_555 73.7  ? 
9  O2G ? C GTP .  ? A GTP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 303 ? 1_555 82.0  ? 
10 O1B ? C GTP .  ? A GTP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 303 ? 1_555 84.0  ? 
11 OG  ? B SER 17 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 305 ? 1_555 88.4  ? 
12 OG1 ? B THR 35 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 305 ? 1_555 103.2 ? 
13 O2G ? C GTP .  ? A GTP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 305 ? 1_555 115.7 ? 
14 O1B ? C GTP .  ? A GTP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 305 ? 1_555 96.8  ? 
15 O   ? F HOH .  ? A HOH 303 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? F HOH .  ? A HOH 305 ? 1_555 162.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 20 ? 
AA2 ? 6  ? 
# 
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  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA1 14 15 ? parallel      
AA1 15 16 ? parallel      
AA1 16 17 ? parallel      
AA1 17 18 ? parallel      
AA1 18 19 ? parallel      
AA1 19 20 ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA2 5  6  ? 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  ARG A 25  ? ASP A 27  ? ARG B 104 ASP B 106 
AA1 2  GLU A 48  ? TYR A 50  ? GLU B 127 TYR B 129 
AA1 3  THR A 71  ? ALA A 73  ? THR B 150 ALA B 152 
AA1 4  MET A 94  ? ASP A 96  ? MET B 173 ASP B 175 
AA1 5  THR A 117 ? TYR A 119 ? THR B 196 TYR B 198 
AA1 6  MET A 140 ? SER A 142 ? MET B 219 SER B 221 
AA1 7  THR A 163 ? ASP A 165 ? THR B 242 ASP B 244 
AA1 8  ASN A 186 ? ASP A 188 ? ASN B 265 ASP B 267 
AA1 9  ARG A 209 ? GLY A 211 ? ARG B 288 GLY B 290 
AA1 10 GLU A 232 ? ASN A 234 ? GLU B 311 ASN B 313 
AA1 11 SER A 256 ? THR A 258 ? SER B 335 THR B 337 
AA1 12 SER A 280 ? ASN A 282 ? SER B 359 ASN B 361 
AA1 13 LYS A 304 ? ASN A 306 ? LYS B 383 ASN B 385 
AA1 14 GLU A 327 ? ASN A 329 ? GLU B 406 ASN B 408 
AA1 15 VAL A 350 ? ILE A 352 ? VAL B 429 ILE B 431 
AA1 16 GLU A 373 ? ASP A 375 ? GLU B 452 ASP B 454 
AA1 17 LYS A 396 ? VAL A 398 ? LYS B 475 VAL B 477 
AA1 18 HIS A 419 ? GLY A 421 ? HIS B 498 GLY B 500 
AA1 19 GLU A 442 ? TYR A 444 ? GLU B 521 TYR B 523 
AA1 20 ILE A 466 ? SER A 468 ? ILE B 545 SER B 547 
AA2 1  ASP B 38  ? ILE B 46  ? ASP A 38  ILE A 46  
AA2 2  GLU B 49  ? ASP B 57  ? GLU A 49  ASP A 57  
AA2 3  THR B 2   ? GLY B 10  ? THR A 2   GLY A 10  
AA2 4  GLY B 77  ? ALA B 83  ? GLY A 77  ALA A 83  
AA2 5  MET B 111 ? ASN B 116 ? MET A 111 ASN A 116 
AA2 6  PHE B 141 ? GLU B 143 ? PHE A 141 GLU A 143 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N LEU A 26  ? N LEU B 105 O TYR A 50  ? O TYR B 129 
AA1 2  3  N LEU A 49  ? N LEU B 128 O THR A 71  ? O THR B 150 
AA1 3  4  N LEU A 72  ? N LEU B 151 O ASP A 96  ? O ASP B 175 
AA1 4  5  N LEU A 95  ? N LEU B 174 O THR A 117 ? O THR B 196 
AA1 5  6  N LEU A 118 ? N LEU B 197 O SER A 142 ? O SER B 221 
AA1 6  7  N LEU A 141 ? N LEU B 220 O ASP A 165 ? O ASP B 244 
AA1 7  8  N LEU A 164 ? N LEU B 243 O ASN A 186 ? O ASN B 265 
AA1 8  9  N LEU A 187 ? N LEU B 266 O ARG A 209 ? O ARG B 288 
AA1 9  10 N LEU A 210 ? N LEU B 289 O GLU A 232 ? O GLU B 311 
AA1 10 11 N LEU A 233 ? N LEU B 312 O THR A 258 ? O THR B 337 
AA1 11 12 N LEU A 257 ? N LEU B 336 O ASN A 282 ? O ASN B 361 
AA1 12 13 N LEU A 281 ? N LEU B 360 O ASN A 306 ? O ASN B 385 
AA1 13 14 N LEU A 305 ? N LEU B 384 O GLU A 327 ? O GLU B 406 
AA1 14 15 N LEU A 328 ? N LEU B 407 O VAL A 350 ? O VAL B 429 
AA1 15 16 N LEU A 351 ? N LEU B 430 O GLU A 373 ? O GLU B 452 
AA1 16 17 N LEU A 374 ? N LEU B 453 O LYS A 396 ? O LYS B 475 
AA1 17 18 N LEU A 397 ? N LEU B 476 O GLY A 421 ? O GLY B 500 
AA1 18 19 N LEU A 420 ? N LEU B 499 O GLU A 442 ? O GLU B 521 
AA1 19 20 N LEU A 443 ? N LEU B 522 O ILE A 466 ? O ILE B 545 
AA2 1  2  N ASP B 38  ? N ASP A 38  O ASP B 57  ? O ASP A 57  
AA2 2  3  O ASP B 54  ? O ASP A 54  N LEU B 6   ? N LEU A 6   
AA2 3  4  N VAL B 9   ? N VAL A 9   O VAL B 81  ? O VAL A 81  
AA2 4  5  N PHE B 82  ? N PHE A 82  O ASN B 116 ? O ASN A 116 
AA2 5  6  N GLY B 115 ? N GLY A 115 O ILE B 142 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9BTM 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU B 155 ? ? 53.78   71.54   
2  1 ASN B 156 ? ? -139.31 -157.65 
3  1 ASN B 179 ? ? -130.29 -152.81 
4  1 LEU B 214 ? ? -91.36  51.75   
5  1 GLU B 224 ? ? 60.07   69.26   
6  1 LEU B 237 ? ? -92.21  59.12   
7  1 ASN B 248 ? ? -129.40 -153.05 
8  1 ASN B 271 ? ? -120.87 -145.85 
9  1 GLU B 272 ? ? -140.83 36.84   
10 1 LEU B 283 ? ? -68.86  72.63   
11 1 TYR B 293 ? ? 60.92   64.49   
12 1 ASN B 294 ? ? -132.57 -150.36 
13 1 SER B 307 ? ? -69.33  4.84    
14 1 ASN B 316 ? ? 64.10   73.74   
15 1 ARG B 340 ? ? 55.77   72.86   
16 1 HIS B 364 ? ? 60.74   68.32   
17 1 ASN B 365 ? ? -142.69 -153.04 
18 1 ASP B 388 ? ? 56.10   74.17   
19 1 ASN B 389 ? ? -144.66 -156.44 
20 1 TRP B 401 ? ? -68.57  66.18   
21 1 ASN B 412 ? ? -139.76 -159.03 
22 1 ASN B 434 ? ? 61.58   61.91   
23 1 ASN B 458 ? ? -117.08 -163.29 
24 1 ASN B 480 ? ? 67.86   71.90   
25 1 LEU B 506 ? ? 49.61   97.33   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.0379552148 
_pdbx_refine_tls.origin_y         -7.13818575464 
_pdbx_refine_tls.origin_z         -11.0340941251 
_pdbx_refine_tls.T[1][1]          0.571799528664 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0261388752888 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0384736700376 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.531626886097 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0911677359146 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.47563653373 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.76458554585 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.488483458848 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.55579660639 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.13794148698 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.162300491242 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.806084251152 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.179565048142 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0927641281009 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.134504695253 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0968053347539 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.156919056732 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0285614031328 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0861195559415 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.114608845283 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0117763831208 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    B 
_pdbx_refine_tls_group.beg_auth_seq_id     86 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   E 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     47 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 B GLY 80  ? A GLY 1   
2  1 Y 1 B THR 81  ? A THR 2   
3  1 Y 1 B ARG 82  ? A ARG 3   
4  1 Y 1 B LYS 83  ? A LYS 4   
5  1 Y 1 B LYS 84  ? A LYS 5   
6  1 Y 1 B SER 85  ? A SER 6   
7  1 Y 1 B PRO 577 ? A PRO 498 
8  1 Y 1 B TYR 578 ? A TYR 499 
9  1 Y 1 B ARG 579 ? A ARG 500 
10 1 Y 1 B ALA 580 ? A ALA 501 
11 1 Y 1 B MET 581 ? A MET 502 
12 1 Y 1 B VAL 582 ? A VAL 503 
13 1 Y 1 A LYS 169 ? B LYS 169 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GTP PG     P  N N 137 
GTP O1G    O  N N 138 
GTP O2G    O  N N 139 
GTP O3G    O  N N 140 
GTP O3B    O  N N 141 
GTP PB     P  N N 142 
GTP O1B    O  N N 143 
GTP O2B    O  N N 144 
GTP O3A    O  N N 145 
GTP PA     P  N N 146 
GTP O1A    O  N N 147 
GTP O2A    O  N N 148 
GTP "O5'"  O  N N 149 
GTP "C5'"  C  N N 150 
GTP "C4'"  C  N R 151 
GTP "O4'"  O  N N 152 
GTP "C3'"  C  N S 153 
GTP "O3'"  O  N N 154 
GTP "C2'"  C  N R 155 
GTP "O2'"  O  N N 156 
GTP "C1'"  C  N R 157 
GTP N9     N  Y N 158 
GTP C8     C  Y N 159 
GTP N7     N  Y N 160 
GTP C5     C  Y N 161 
GTP C6     C  N N 162 
GTP O6     O  N N 163 
GTP N1     N  N N 164 
GTP C2     C  N N 165 
GTP N2     N  N N 166 
GTP N3     N  N N 167 
GTP C4     C  Y N 168 
GTP HOG2   H  N N 169 
GTP HOG3   H  N N 170 
GTP HOB2   H  N N 171 
GTP HOA2   H  N N 172 
GTP "H5'"  H  N N 173 
GTP "H5''" H  N N 174 
GTP "H4'"  H  N N 175 
GTP "H3'"  H  N N 176 
GTP "HO3'" H  N N 177 
GTP "H2'"  H  N N 178 
GTP "HO2'" H  N N 179 
GTP "H1'"  H  N N 180 
GTP H8     H  N N 181 
GTP HN1    H  N N 182 
GTP HN21   H  N N 183 
GTP HN22   H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MG  MG     MG N N 298 
PHE N      N  N N 299 
PHE CA     C  N S 300 
PHE C      C  N N 301 
PHE O      O  N N 302 
PHE CB     C  N N 303 
PHE CG     C  Y N 304 
PHE CD1    C  Y N 305 
PHE CD2    C  Y N 306 
PHE CE1    C  Y N 307 
PHE CE2    C  Y N 308 
PHE CZ     C  Y N 309 
PHE OXT    O  N N 310 
PHE H      H  N N 311 
PHE H2     H  N N 312 
PHE HA     H  N N 313 
PHE HB2    H  N N 314 
PHE HB3    H  N N 315 
PHE HD1    H  N N 316 
PHE HD2    H  N N 317 
PHE HE1    H  N N 318 
PHE HE2    H  N N 319 
PHE HZ     H  N N 320 
PHE HXT    H  N N 321 
PRO N      N  N N 322 
PRO CA     C  N S 323 
PRO C      C  N N 324 
PRO O      O  N N 325 
PRO CB     C  N N 326 
PRO CG     C  N N 327 
PRO CD     C  N N 328 
PRO OXT    O  N N 329 
PRO H      H  N N 330 
PRO HA     H  N N 331 
PRO HB2    H  N N 332 
PRO HB3    H  N N 333 
PRO HG2    H  N N 334 
PRO HG3    H  N N 335 
PRO HD2    H  N N 336 
PRO HD3    H  N N 337 
PRO HXT    H  N N 338 
SER N      N  N N 339 
SER CA     C  N S 340 
SER C      C  N N 341 
SER O      O  N N 342 
SER CB     C  N N 343 
SER OG     O  N N 344 
SER OXT    O  N N 345 
SER H      H  N N 346 
SER H2     H  N N 347 
SER HA     H  N N 348 
SER HB2    H  N N 349 
SER HB3    H  N N 350 
SER HG     H  N N 351 
SER HXT    H  N N 352 
THR N      N  N N 353 
THR CA     C  N S 354 
THR C      C  N N 355 
THR O      O  N N 356 
THR CB     C  N R 357 
THR OG1    O  N N 358 
THR CG2    C  N N 359 
THR OXT    O  N N 360 
THR H      H  N N 361 
THR H2     H  N N 362 
THR HA     H  N N 363 
THR HB     H  N N 364 
THR HG1    H  N N 365 
THR HG21   H  N N 366 
THR HG22   H  N N 367 
THR HG23   H  N N 368 
THR HXT    H  N N 369 
TRP N      N  N N 370 
TRP CA     C  N S 371 
TRP C      C  N N 372 
TRP O      O  N N 373 
TRP CB     C  N N 374 
TRP CG     C  Y N 375 
TRP CD1    C  Y N 376 
TRP CD2    C  Y N 377 
TRP NE1    N  Y N 378 
TRP CE2    C  Y N 379 
TRP CE3    C  Y N 380 
TRP CZ2    C  Y N 381 
TRP CZ3    C  Y N 382 
TRP CH2    C  Y N 383 
TRP OXT    O  N N 384 
TRP H      H  N N 385 
TRP H2     H  N N 386 
TRP HA     H  N N 387 
TRP HB2    H  N N 388 
TRP HB3    H  N N 389 
TRP HD1    H  N N 390 
TRP HE1    H  N N 391 
TRP HE3    H  N N 392 
TRP HZ2    H  N N 393 
TRP HZ3    H  N N 394 
TRP HH2    H  N N 395 
TRP HXT    H  N N 396 
TYR N      N  N N 397 
TYR CA     C  N S 398 
TYR C      C  N N 399 
TYR O      O  N N 400 
TYR CB     C  N N 401 
TYR CG     C  Y N 402 
TYR CD1    C  Y N 403 
TYR CD2    C  Y N 404 
TYR CE1    C  Y N 405 
TYR CE2    C  Y N 406 
TYR CZ     C  Y N 407 
TYR OH     O  N N 408 
TYR OXT    O  N N 409 
TYR H      H  N N 410 
TYR H2     H  N N 411 
TYR HA     H  N N 412 
TYR HB2    H  N N 413 
TYR HB3    H  N N 414 
TYR HD1    H  N N 415 
TYR HD2    H  N N 416 
TYR HE1    H  N N 417 
TYR HE2    H  N N 418 
TYR HH     H  N N 419 
TYR HXT    H  N N 420 
VAL N      N  N N 421 
VAL CA     C  N S 422 
VAL C      C  N N 423 
VAL O      O  N N 424 
VAL CB     C  N N 425 
VAL CG1    C  N N 426 
VAL CG2    C  N N 427 
VAL OXT    O  N N 428 
VAL H      H  N N 429 
VAL H2     H  N N 430 
VAL HA     H  N N 431 
VAL HB     H  N N 432 
VAL HG11   H  N N 433 
VAL HG12   H  N N 434 
VAL HG13   H  N N 435 
VAL HG21   H  N N 436 
VAL HG22   H  N N 437 
VAL HG23   H  N N 438 
VAL HXT    H  N N 439 
# 
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  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GTP PG    O1G    doub N N 129 
GTP PG    O2G    sing N N 130 
GTP PG    O3G    sing N N 131 
GTP PG    O3B    sing N N 132 
GTP O2G   HOG2   sing N N 133 
GTP O3G   HOG3   sing N N 134 
GTP O3B   PB     sing N N 135 
GTP PB    O1B    doub N N 136 
GTP PB    O2B    sing N N 137 
GTP PB    O3A    sing N N 138 
GTP O2B   HOB2   sing N N 139 
GTP O3A   PA     sing N N 140 
GTP PA    O1A    doub N N 141 
GTP PA    O2A    sing N N 142 
GTP PA    "O5'"  sing N N 143 
GTP O2A   HOA2   sing N N 144 
GTP "O5'" "C5'"  sing N N 145 
GTP "C5'" "C4'"  sing N N 146 
GTP "C5'" "H5'"  sing N N 147 
GTP "C5'" "H5''" sing N N 148 
GTP "C4'" "O4'"  sing N N 149 
GTP "C4'" "C3'"  sing N N 150 
GTP "C4'" "H4'"  sing N N 151 
GTP "O4'" "C1'"  sing N N 152 
GTP "C3'" "O3'"  sing N N 153 
GTP "C3'" "C2'"  sing N N 154 
GTP "C3'" "H3'"  sing N N 155 
GTP "O3'" "HO3'" sing N N 156 
GTP "C2'" "O2'"  sing N N 157 
GTP "C2'" "C1'"  sing N N 158 
GTP "C2'" "H2'"  sing N N 159 
GTP "O2'" "HO2'" sing N N 160 
GTP "C1'" N9     sing N N 161 
GTP "C1'" "H1'"  sing N N 162 
GTP N9    C8     sing Y N 163 
GTP N9    C4     sing Y N 164 
GTP C8    N7     doub Y N 165 
GTP C8    H8     sing N N 166 
GTP N7    C5     sing Y N 167 
GTP C5    C6     sing N N 168 
GTP C5    C4     doub Y N 169 
GTP C6    O6     doub N N 170 
GTP C6    N1     sing N N 171 
GTP N1    C2     sing N N 172 
GTP N1    HN1    sing N N 173 
GTP C2    N2     sing N N 174 
GTP C2    N3     doub N N 175 
GTP N2    HN21   sing N N 176 
GTP N2    HN22   sing N N 177 
GTP N3    C4     sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TRP N     CA     sing N N 356 
TRP N     H      sing N N 357 
TRP N     H2     sing N N 358 
TRP CA    C      sing N N 359 
TRP CA    CB     sing N N 360 
TRP CA    HA     sing N N 361 
TRP C     O      doub N N 362 
TRP C     OXT    sing N N 363 
TRP CB    CG     sing N N 364 
TRP CB    HB2    sing N N 365 
TRP CB    HB3    sing N N 366 
TRP CG    CD1    doub Y N 367 
TRP CG    CD2    sing Y N 368 
TRP CD1   NE1    sing Y N 369 
TRP CD1   HD1    sing N N 370 
TRP CD2   CE2    doub Y N 371 
TRP CD2   CE3    sing Y N 372 
TRP NE1   CE2    sing Y N 373 
TRP NE1   HE1    sing N N 374 
TRP CE2   CZ2    sing Y N 375 
TRP CE3   CZ3    doub Y N 376 
TRP CE3   HE3    sing N N 377 
TRP CZ2   CH2    doub Y N 378 
TRP CZ2   HZ2    sing N N 379 
TRP CZ3   CH2    sing Y N 380 
TRP CZ3   HZ3    sing N N 381 
TRP CH2   HH2    sing N N 382 
TRP OXT   HXT    sing N N 383 
TYR N     CA     sing N N 384 
TYR N     H      sing N N 385 
TYR N     H2     sing N N 386 
TYR CA    C      sing N N 387 
TYR CA    CB     sing N N 388 
TYR CA    HA     sing N N 389 
TYR C     O      doub N N 390 
TYR C     OXT    sing N N 391 
TYR CB    CG     sing N N 392 
TYR CB    HB2    sing N N 393 
TYR CB    HB3    sing N N 394 
TYR CG    CD1    doub Y N 395 
TYR CG    CD2    sing Y N 396 
TYR CD1   CE1    sing Y N 397 
TYR CD1   HD1    sing N N 398 
TYR CD2   CE2    doub Y N 399 
TYR CD2   HD2    sing N N 400 
TYR CE1   CZ     doub Y N 401 
TYR CE1   HE1    sing N N 402 
TYR CE2   CZ     sing Y N 403 
TYR CE2   HE2    sing N N 404 
TYR CZ    OH     sing N N 405 
TYR OH    HH     sing N N 406 
TYR OXT   HXT    sing N N 407 
VAL N     CA     sing N N 408 
VAL N     H      sing N N 409 
VAL N     H2     sing N N 410 
VAL CA    C      sing N N 411 
VAL CA    CB     sing N N 412 
VAL CA    HA     sing N N 413 
VAL C     O      doub N N 414 
VAL C     OXT    sing N N 415 
VAL CB    CG1    sing N N 416 
VAL CB    CG2    sing N N 417 
VAL CB    HB     sing N N 418 
VAL CG1   HG11   sing N N 419 
VAL CG1   HG12   sing N N 420 
VAL CG1   HG13   sing N N 421 
VAL CG2   HG21   sing N N 422 
VAL CG2   HG22   sing N N 423 
VAL CG2   HG23   sing N N 424 
VAL OXT   HXT    sing N N 425 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 7YTG 'SHOC2 apo' 
2 ? 'experimental model' PDB 5UHV 'NRAS apo'  
# 
_atom_sites.entry_id                    9BTM 
_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]   0.012677 
_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]   0.011193 
_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]   0.008349 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
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 7   ? 26.56632  -40.00747 -0.35109  1.000 111.93853 ? 86  SER B N     1 
ATOM   2    C  CA    . SER A 1 7   ? 26.78154  -40.67972 0.92634   1.000 121.83025 ? 86  SER B CA    1 
ATOM   3    C  C     . SER A 1 7   ? 28.25850  -40.66369 1.30151   1.000 116.03228 ? 86  SER B C     1 
ATOM   4    O  O     . SER A 1 7   ? 29.08136  -40.09726 0.58351   1.000 119.72522 ? 86  SER B O     1 
ATOM   5    C  CB    . SER A 1 7   ? 26.27228  -42.12185 0.87538   1.000 117.64261 ? 86  SER B CB    1 
ATOM   6    O  OG    . SER A 1 7   ? 27.32441  -43.02297 0.57362   1.000 121.90647 ? 86  SER B OG    1 
ATOM   7    N  N     . ASN A 1 8   ? 28.58870  -41.30087 2.42824   1.000 114.58381 ? 87  ASN B N     1 
ATOM   8    C  CA    . ASN A 1 8   ? 29.96684  -41.31616 2.90667   1.000 120.82301 ? 87  ASN B CA    1 
ATOM   9    C  C     . ASN A 1 8   ? 30.85541  -42.25634 2.10086   1.000 131.12185 ? 87  ASN B C     1 
ATOM   10   O  O     . ASN A 1 8   ? 32.08233  -42.10582 2.13202   1.000 126.80509 ? 87  ASN B O     1 
ATOM   11   C  CB    . ASN A 1 8   ? 30.00327  -41.70473 4.38782   1.000 106.24174 ? 87  ASN B CB    1 
ATOM   12   C  CG    . ASN A 1 8   ? 31.40870  -41.68136 4.96629   1.000 115.74605 ? 87  ASN B CG    1 
ATOM   13   O  OD1   . ASN A 1 8   ? 32.11364  -42.69141 4.95724   1.000 107.68813 ? 87  ASN B OD1   1 
ATOM   14   N  ND2   . ASN A 1 8   ? 31.82312  -40.52398 5.46961   1.000 118.05131 ? 87  ASN B ND2   1 
ATOM   15   N  N     . ALA A 1 9   ? 30.26952  -43.21716 1.38117   1.000 129.46934 ? 88  ALA B N     1 
ATOM   16   C  CA    . ALA A 1 9   ? 31.07745  -44.15721 0.61023   1.000 126.31455 ? 88  ALA B CA    1 
ATOM   17   C  C     . ALA A 1 9   ? 31.89978  -43.43907 -0.45296  1.000 135.64125 ? 88  ALA B C     1 
ATOM   18   O  O     . ALA A 1 9   ? 33.08129  -43.74810 -0.64889  1.000 127.13542 ? 88  ALA B O     1 
ATOM   19   C  CB    . ALA A 1 9   ? 30.18215  -45.22002 -0.02601  1.000 118.12850 ? 88  ALA B CB    1 
ATOM   20   N  N     . GLU A 1 10  ? 31.29581  -42.46975 -1.14445  1.000 149.82087 ? 89  GLU B N     1 
ATOM   21   C  CA    . GLU A 1 10  ? 32.03430  -41.72249 -2.15646  1.000 151.88567 ? 89  GLU B CA    1 
ATOM   22   C  C     . GLU A 1 10  ? 33.02568  -40.74923 -1.53132  1.000 152.29302 ? 89  GLU B C     1 
ATOM   23   O  O     . GLU A 1 10  ? 34.03951  -40.41912 -2.15565  1.000 149.66375 ? 89  GLU B O     1 
ATOM   24   C  CB    . GLU A 1 10  ? 31.06982  -40.96485 -3.07223  1.000 148.43911 ? 89  GLU B CB    1 
ATOM   25   C  CG    . GLU A 1 10  ? 30.32992  -41.82226 -4.09215  1.000 144.41824 ? 89  GLU B CG    1 
ATOM   26   C  CD    . GLU A 1 10  ? 29.19743  -42.62587 -3.48189  1.000 148.06733 ? 89  GLU B CD    1 
ATOM   27   O  OE1   . GLU A 1 10  ? 29.47905  -43.60755 -2.76382  1.000 150.23435 ? 89  GLU B OE1   1 
ATOM   28   O  OE2   . GLU A 1 10  ? 28.02267  -42.27125 -3.71665  1.000 144.84162 ? 89  GLU B OE2   1 
ATOM   29   N  N     . VAL A 1 11  ? 32.75789  -40.28577 -0.30797  1.000 131.08575 ? 90  VAL B N     1 
ATOM   30   C  CA    . VAL A 1 11  ? 33.57688  -39.23215 0.29204   1.000 120.58424 ? 90  VAL B CA    1 
ATOM   31   C  C     . VAL A 1 11  ? 35.00324  -39.72252 0.51237   1.000 119.79888 ? 90  VAL B C     1 
ATOM   32   O  O     . VAL A 1 11  ? 35.96651  -39.14299 -0.00251  1.000 118.84182 ? 90  VAL B O     1 
ATOM   33   C  CB    . VAL A 1 11  ? 32.94591  -38.73703 1.60526   1.000 114.89410 ? 90  VAL B CB    1 
ATOM   34   C  CG1   . VAL A 1 11  ? 33.84413  -37.70350 2.26414   1.000 100.07361 ? 90  VAL B CG1   1 
ATOM   35   C  CG2   . VAL A 1 11  ? 31.56723  -38.15558 1.34574   1.000 105.55097 ? 90  VAL B CG2   1 
ATOM   36   N  N     . ILE A 1 12  ? 35.15850  -40.80006 1.28462   1.000 118.79058 ? 91  ILE B N     1 
ATOM   37   C  CA    . ILE A 1 12  ? 36.49832  -41.27974 1.60769   1.000 121.11695 ? 91  ILE B CA    1 
ATOM   38   C  C     . ILE A 1 12  ? 37.17933  -41.86476 0.37720   1.000 116.95520 ? 91  ILE B C     1 
ATOM   39   O  O     . ILE A 1 12  ? 38.40224  -41.75497 0.22619   1.000 116.29836 ? 91  ILE B O     1 
ATOM   40   C  CB    . ILE A 1 12  ? 36.43937  -42.30049 2.75972   1.000 118.67941 ? 91  ILE B CB    1 
ATOM   41   C  CG1   . ILE A 1 12  ? 35.66255  -41.71943 3.94301   1.000 115.24891 ? 91  ILE B CG1   1 
ATOM   42   C  CG2   . ILE A 1 12  ? 37.84215  -42.69438 3.19903   1.000 100.16921 ? 91  ILE B CG2   1 
ATOM   43   C  CD1   . ILE A 1 12  ? 35.66121  -42.60511 5.17146   1.000 111.66501 ? 91  ILE B CD1   1 
ATOM   44   N  N     . LYS A 1 13  ? 36.41460  -42.48227 -0.52591  1.000 119.63366 ? 92  LYS B N     1 
ATOM   45   C  CA    . LYS A 1 13  ? 37.03389  -43.10090 -1.69247  1.000 125.53955 ? 92  LYS B CA    1 
ATOM   46   C  C     . LYS A 1 13  ? 37.46961  -42.06636 -2.72249  1.000 120.79732 ? 92  LYS B C     1 
ATOM   47   O  O     . LYS A 1 13  ? 38.49853  -42.25298 -3.38210  1.000 121.35844 ? 92  LYS B O     1 
ATOM   48   C  CB    . LYS A 1 13  ? 36.08606  -44.12033 -2.32493  1.000 130.49938 ? 92  LYS B CB    1 
ATOM   49   C  CG    . LYS A 1 13  ? 36.22356  -45.52002 -1.74059  1.000 128.70368 ? 92  LYS B CG    1 
ATOM   50   C  CD    . LYS A 1 13  ? 35.73453  -46.58341 -2.71336  1.000 122.77622 ? 92  LYS B CD    1 
ATOM   51   C  CE    . LYS A 1 13  ? 36.05314  -47.98509 -2.21180  1.000 115.72340 ? 92  LYS B CE    1 
ATOM   52   N  NZ    . LYS A 1 13  ? 35.68830  -49.03524 -3.20440  1.000 111.82985 ? 92  LYS B NZ    1 
ATOM   53   N  N     . GLU A 1 14  ? 36.71353  -40.97746 -2.88278  1.000 117.75843 ? 93  GLU B N     1 
ATOM   54   C  CA    . GLU A 1 14  ? 37.12077  -39.94730 -3.83083  1.000 121.19483 ? 93  GLU B CA    1 
ATOM   55   C  C     . GLU A 1 14  ? 38.27058  -39.09414 -3.30691  1.000 117.60722 ? 93  GLU B C     1 
ATOM   56   O  O     . GLU A 1 14  ? 38.94119  -38.42385 -4.10116  1.000 112.34367 ? 93  GLU B O     1 
ATOM   57   C  CB    . GLU A 1 14  ? 35.93425  -39.05531 -4.20444  1.000 114.17920 ? 93  GLU B CB    1 
ATOM   58   C  CG    . GLU A 1 14  ? 36.16330  -38.25302 -5.47698  1.000 113.50660 ? 93  GLU B CG    1 
ATOM   59   C  CD    . GLU A 1 14  ? 34.94753  -37.46181 -5.90768  1.000 117.81450 ? 93  GLU B CD    1 
ATOM   60   O  OE1   . GLU A 1 14  ? 33.82472  -37.81231 -5.48716  1.000 117.37957 ? 93  GLU B OE1   1 
ATOM   61   O  OE2   . GLU A 1 14  ? 35.11759  -36.48715 -6.67053  1.000 113.48885 ? 93  GLU B OE2   1 
ATOM   62   N  N     . LEU A 1 15  ? 38.51700  -39.10118 -1.99525  1.000 113.04074 ? 94  LEU B N     1 
ATOM   63   C  CA    . LEU A 1 15  ? 39.72928  -38.47504 -1.47922  1.000 108.51589 ? 94  LEU B CA    1 
ATOM   64   C  C     . LEU A 1 15  ? 40.96631  -39.19602 -1.99849  1.000 118.52260 ? 94  LEU B C     1 
ATOM   65   O  O     . LEU A 1 15  ? 41.92158  -38.56159 -2.46047  1.000 111.63218 ? 94  LEU B O     1 
ATOM   66   C  CB    . LEU A 1 15  ? 39.70995  -38.45849 0.04886   1.000 109.10096 ? 94  LEU B CB    1 
ATOM   67   C  CG    . LEU A 1 15  ? 38.76257  -37.45370 0.70462   1.000 100.27275 ? 94  LEU B CG    1 
ATOM   68   C  CD1   . LEU A 1 15  ? 38.93103  -37.47912 2.20824   1.000 101.04841 ? 94  LEU B CD1   1 
ATOM   69   C  CD2   . LEU A 1 15  ? 39.01489  -36.05905 0.16884   1.000 98.65118  ? 94  LEU B CD2   1 
ATOM   70   N  N     . ASN A 1 16  ? 40.96164  -40.53169 -1.93670  1.000 138.11546 ? 95  ASN B N     1 
ATOM   71   C  CA    . ASN A 1 16  ? 42.03475  -41.30279 -2.55609  1.000 134.55089 ? 95  ASN B CA    1 
ATOM   72   C  C     . ASN A 1 16  ? 42.04008  -41.12887 -4.06780  1.000 132.26169 ? 95  ASN B C     1 
ATOM   73   O  O     . ASN A 1 16  ? 43.10775  -41.13965 -4.69143  1.000 126.16248 ? 95  ASN B O     1 
ATOM   74   C  CB    . ASN A 1 16  ? 41.90520  -42.78267 -2.19319  1.000 129.55559 ? 95  ASN B CB    1 
ATOM   75   C  CG    . ASN A 1 16  ? 42.53868  -43.11310 -0.85728  1.000 130.18962 ? 95  ASN B CG    1 
ATOM   76   O  OD1   . ASN A 1 16  ? 43.73062  -43.41194 -0.78147  1.000 131.83048 ? 95  ASN B OD1   1 
ATOM   77   N  ND2   . ASN A 1 16  ? 41.74317  -43.06437 0.20521   1.000 136.20246 ? 95  ASN B ND2   1 
ATOM   78   N  N     . LYS A 1 17  ? 40.86014  -40.96972 -4.67174  1.000 116.36274 ? 96  LYS B N     1 
ATOM   79   C  CA    . LYS A 1 17  ? 40.78734  -40.69762 -6.10246  1.000 115.06814 ? 96  LYS B CA    1 
ATOM   80   C  C     . LYS A 1 17  ? 41.44002  -39.36493 -6.44876  1.000 112.86007 ? 96  LYS B C     1 
ATOM   81   O  O     . LYS A 1 17  ? 42.04021  -39.22736 -7.52090  1.000 111.52163 ? 96  LYS B O     1 
ATOM   82   C  CB    . LYS A 1 17  ? 39.32571  -40.72814 -6.55672  1.000 109.84690 ? 96  LYS B CB    1 
ATOM   83   C  CG    . LYS A 1 17  ? 39.08648  -40.35555 -8.01069  1.000 102.97871 ? 96  LYS B CG    1 
ATOM   84   C  CD    . LYS A 1 17  ? 37.61732  -40.51829 -8.37524  1.000 103.71205 ? 96  LYS B CD    1 
ATOM   85   C  CE    . LYS A 1 17  ? 37.32750  -40.00289 -9.77512  1.000 103.71898 ? 96  LYS B CE    1 
ATOM   86   N  NZ    . LYS A 1 17  ? 37.49781  -38.52643 -9.86929  1.000 107.00081 ? 96  LYS B NZ    1 
ATOM   87   N  N     . CYS A 1 18  ? 41.35510  -38.38269 -5.54801  1.000 111.96009 ? 97  CYS B N     1 
ATOM   88   C  CA    . CYS A 1 18  ? 41.95921  -37.07929 -5.80219  1.000 110.75277 ? 97  CYS B CA    1 
ATOM   89   C  C     . CYS A 1 18  ? 43.47890  -37.12269 -5.68626  1.000 111.27991 ? 97  CYS B C     1 
ATOM   90   O  O     . CYS A 1 18  ? 44.18056  -36.55057 -6.52747  1.000 109.69633 ? 97  CYS B O     1 
ATOM   91   C  CB    . CYS A 1 18  ? 41.38874  -36.03616 -4.84251  1.000 110.62127 ? 97  CYS B CB    1 
ATOM   92   S  SG    . CYS A 1 18  ? 42.09733  -34.38570 -5.05618  1.000 105.26446 ? 97  CYS B SG    1 
ATOM   93   N  N     . ARG A 1 19  ? 44.00804  -37.78903 -4.65640  1.000 111.47739 ? 98  ARG B N     1 
ATOM   94   C  CA    . ARG A 1 19  ? 45.45640  -37.83705 -4.48294  1.000 114.06081 ? 98  ARG B CA    1 
ATOM   95   C  C     . ARG A 1 19  ? 46.12040  -38.79016 -5.46737  1.000 115.83055 ? 98  ARG B C     1 
ATOM   96   O  O     . ARG A 1 19  ? 47.28856  -38.58999 -5.81874  1.000 110.54506 ? 98  ARG B O     1 
ATOM   97   C  CB    . ARG A 1 19  ? 45.81167  -38.22417 -3.04517  1.000 113.61575 ? 98  ARG B CB    1 
ATOM   98   C  CG    . ARG A 1 19  ? 45.06670  -39.43407 -2.51450  1.000 123.88633 ? 98  ARG B CG    1 
ATOM   99   C  CD    . ARG A 1 19  ? 45.29567  -39.60942 -1.01913  1.000 129.46744 ? 98  ARG B CD    1 
ATOM   100  N  NE    . ARG A 1 19  ? 46.60621  -40.17171 -0.71391  1.000 120.79039 ? 98  ARG B NE    1 
ATOM   101  C  CZ    . ARG A 1 19  ? 46.79801  -41.39081 -0.22962  1.000 125.31556 ? 98  ARG B CZ    1 
ATOM   102  N  NH1   . ARG A 1 19  ? 45.78148  -42.19634 0.03427   1.000 130.59336 ? 98  ARG B NH1   1 
ATOM   103  N  NH2   . ARG A 1 19  ? 48.03928  -41.80999 0.00089   1.000 119.25135 ? 98  ARG B NH2   1 
ATOM   104  N  N     . GLU A 1 20  ? 45.40516  -39.82309 -5.92044  1.000 118.08935 ? 99  GLU B N     1 
ATOM   105  C  CA    . GLU A 1 20  ? 45.93974  -40.67716 -6.97626  1.000 122.69969 ? 99  GLU B CA    1 
ATOM   106  C  C     . GLU A 1 20  ? 46.05205  -39.90790 -8.28549  1.000 121.67606 ? 99  GLU B C     1 
ATOM   107  O  O     . GLU A 1 20  ? 47.10312  -39.91919 -8.93650  1.000 131.86842 ? 99  GLU B O     1 
ATOM   108  C  CB    . GLU A 1 20  ? 45.06625  -41.92242 -7.14813  1.000 129.74797 ? 99  GLU B CB    1 
ATOM   109  C  CG    . GLU A 1 20  ? 45.27432  -42.67236 -8.46459  1.000 142.49947 ? 99  GLU B CG    1 
ATOM   110  C  CD    . GLU A 1 20  ? 46.61434  -43.38998 -8.55483  1.000 152.44957 ? 99  GLU B CD    1 
ATOM   111  O  OE1   . GLU A 1 20  ? 47.39081  -43.36002 -7.57582  1.000 149.25961 ? 99  GLU B OE1   1 
ATOM   112  O  OE2   . GLU A 1 20  ? 46.88801  -43.99307 -9.61484  1.000 158.74415 ? 99  GLU B OE2   1 
ATOM   113  N  N     . GLU A 1 21  ? 44.97810  -39.22104 -8.68196  1.000 109.18876 ? 100 GLU B N     1 
ATOM   114  C  CA    . GLU A 1 21  ? 45.04614  -38.34424 -9.84366  1.000 107.78958 ? 100 GLU B CA    1 
ATOM   115  C  C     . GLU A 1 21  ? 45.94587  -37.13993 -9.60226  1.000 107.46341 ? 100 GLU B C     1 
ATOM   116  O  O     . GLU A 1 21  ? 46.35432  -36.48635 -10.56841 1.000 102.62211 ? 100 GLU B O     1 
ATOM   117  C  CB    . GLU A 1 21  ? 43.64559  -37.86856 -10.23120 1.000 107.07400 ? 100 GLU B CB    1 
ATOM   118  C  CG    . GLU A 1 21  ? 42.68834  -38.97964 -10.62122 1.000 107.50087 ? 100 GLU B CG    1 
ATOM   119  C  CD    . GLU A 1 21  ? 41.30546  -38.45682 -10.95650 1.000 111.57397 ? 100 GLU B CD    1 
ATOM   120  O  OE1   . GLU A 1 21  ? 41.18748  -37.25515 -11.27750 1.000 120.53474 ? 100 GLU B OE1   1 
ATOM   121  O  OE2   . GLU A 1 21  ? 40.33698  -39.24361 -10.89382 1.000 104.32480 ? 100 GLU B OE2   1 
ATOM   122  N  N     . ASN A 1 22  ? 46.26054  -36.83988 -8.33901  1.000 110.22524 ? 101 ASN B N     1 
ATOM   123  C  CA    . ASN A 1 22  ? 47.06898  -35.67718 -7.96589  1.000 101.88465 ? 101 ASN B CA    1 
ATOM   124  C  C     . ASN A 1 22  ? 46.47099  -34.39034 -8.53104  1.000 103.50829 ? 101 ASN B C     1 
ATOM   125  O  O     . ASN A 1 22  ? 47.18739  -33.47371 -8.93996  1.000 93.43113  ? 101 ASN B O     1 
ATOM   126  C  CB    . ASN A 1 22  ? 48.52656  -35.84779 -8.40188  1.000 100.66509 ? 101 ASN B CB    1 
ATOM   127  C  CG    . ASN A 1 22  ? 49.49436  -35.10570 -7.49938  1.000 99.81570  ? 101 ASN B CG    1 
ATOM   128  O  OD1   . ASN A 1 22  ? 49.79342  -35.55335 -6.39238  1.000 102.10466 ? 101 ASN B OD1   1 
ATOM   129  N  ND2   . ASN A 1 22  ? 49.99063  -33.96686 -7.96898  1.000 90.30753  ? 101 ASN B ND2   1 
ATOM   130  N  N     . SER A 1 23  ? 45.14182  -34.32516 -8.55082  1.000 105.35742 ? 102 SER B N     1 
ATOM   131  C  CA    . SER A 1 23  ? 44.45167  -33.15782 -9.07833  1.000 99.11476  ? 102 SER B CA    1 
ATOM   132  C  C     . SER A 1 23  ? 44.55348  -31.98989 -8.10687  1.000 98.26055  ? 102 SER B C     1 
ATOM   133  O  O     . SER A 1 23  ? 44.50003  -32.16657 -6.88659  1.000 95.89430  ? 102 SER B O     1 
ATOM   134  C  CB    . SER A 1 23  ? 42.98401  -33.48690 -9.34845  1.000 102.44077 ? 102 SER B CB    1 
ATOM   135  O  OG    . SER A 1 23  ? 42.27598  -32.34167 -9.79019  1.000 108.84795 ? 102 SER B OG    1 
ATOM   136  N  N     . MET A 1 24  ? 44.70101  -30.78490 -8.65968  1.000 95.95692  ? 103 MET B N     1 
ATOM   137  C  CA    . MET A 1 24  ? 44.76377  -29.56132 -7.87083  1.000 92.93399  ? 103 MET B CA    1 
ATOM   138  C  C     . MET A 1 24  ? 43.38613  -28.97293 -7.59724  1.000 86.39583  ? 103 MET B C     1 
ATOM   139  O  O     . MET A 1 24  ? 43.25738  -27.75287 -7.42691  1.000 86.14503  ? 103 MET B O     1 
ATOM   140  C  CB    . MET A 1 24  ? 45.65782  -28.53727 -8.57029  1.000 89.79846  ? 103 MET B CB    1 
ATOM   141  C  CG    . MET A 1 24  ? 47.12972  -28.91443 -8.57047  1.000 86.36066  ? 103 MET B CG    1 
ATOM   142  S  SD    . MET A 1 24  ? 48.10535  -27.94881 -9.73721  1.000 113.57746 ? 103 MET B SD    1 
ATOM   143  C  CE    . MET A 1 24  ? 47.55070  -26.28772 -9.35969  1.000 96.06361  ? 103 MET B CE    1 
ATOM   144  N  N     . ARG A 1 25  ? 42.35335  -29.81173 -7.54079  1.000 81.18980  ? 104 ARG B N     1 
ATOM   145  C  CA    . ARG A 1 25  ? 40.98845  -29.33800 -7.35872  1.000 79.90713  ? 104 ARG B CA    1 
ATOM   146  C  C     . ARG A 1 25  ? 40.11837  -30.50263 -6.91184  1.000 87.61089  ? 104 ARG B C     1 
ATOM   147  O  O     . ARG A 1 25  ? 40.08301  -31.54213 -7.57684  1.000 90.19163  ? 104 ARG B O     1 
ATOM   148  C  CB    . ARG A 1 25  ? 40.45254  -28.72134 -8.65641  1.000 84.03514  ? 104 ARG B CB    1 
ATOM   149  C  CG    . ARG A 1 25  ? 38.96985  -28.39323 -8.64423  1.000 89.20843  ? 104 ARG B CG    1 
ATOM   150  C  CD    . ARG A 1 25  ? 38.58838  -27.47239 -9.80157  1.000 85.75043  ? 104 ARG B CD    1 
ATOM   151  N  NE    . ARG A 1 25  ? 39.14188  -27.91004 -11.07871 1.000 87.97054  ? 104 ARG B NE    1 
ATOM   152  C  CZ    . ARG A 1 25  ? 40.17579  -27.33864 -11.68300 1.000 94.90552  ? 104 ARG B CZ    1 
ATOM   153  N  NH1   . ARG A 1 25  ? 40.79105  -26.29071 -11.15784 1.000 92.33874  ? 104 ARG B NH1   1 
ATOM   154  N  NH2   . ARG A 1 25  ? 40.60440  -27.83204 -12.84183 1.000 84.33836  ? 104 ARG B NH2   1 
ATOM   155  N  N     . LEU A 1 26  ? 39.42790  -30.32610 -5.78758  1.000 84.11812  ? 105 LEU B N     1 
ATOM   156  C  CA    . LEU A 1 26  ? 38.52019  -31.32463 -5.24050  1.000 75.50433  ? 105 LEU B CA    1 
ATOM   157  C  C     . LEU A 1 26  ? 37.13380  -30.71008 -5.11062  1.000 84.01771  ? 105 LEU B C     1 
ATOM   158  O  O     . LEU A 1 26  ? 36.98932  -29.60801 -4.57116  1.000 85.15520  ? 105 LEU B O     1 
ATOM   159  C  CB    . LEU A 1 26  ? 39.00933  -31.82782 -3.88005  1.000 76.01941  ? 105 LEU B CB    1 
ATOM   160  C  CG    . LEU A 1 26  ? 38.14041  -32.89545 -3.21393  1.000 81.89248  ? 105 LEU B CG    1 
ATOM   161  C  CD1   . LEU A 1 26  ? 38.26795  -34.22010 -3.94948  1.000 93.44911  ? 105 LEU B CD1   1 
ATOM   162  C  CD2   . LEU A 1 26  ? 38.50074  -33.05182 -1.74833  1.000 81.03629  ? 105 LEU B CD2   1 
ATOM   163  N  N     . ASP A 1 27  ? 36.11981  -31.42072 -5.60186  1.000 85.16666  ? 106 ASP B N     1 
ATOM   164  C  CA    . ASP A 1 27  ? 34.73738  -30.94223 -5.61093  1.000 75.32265  ? 106 ASP B CA    1 
ATOM   165  C  C     . ASP A 1 27  ? 33.87931  -31.94874 -4.84839  1.000 78.92375  ? 106 ASP B C     1 
ATOM   166  O  O     . ASP A 1 27  ? 33.49077  -32.98568 -5.39534  1.000 87.71882  ? 106 ASP B O     1 
ATOM   167  C  CB    . ASP A 1 27  ? 34.24021  -30.74845 -7.04411  1.000 74.93001  ? 106 ASP B CB    1 
ATOM   168  C  CG    . ASP A 1 27  ? 32.82648  -30.18245 -7.11179  1.000 87.16474  ? 106 ASP B CG    1 
ATOM   169  O  OD1   . ASP A 1 27  ? 32.30037  -29.72984 -6.07215  1.000 86.03684  ? 106 ASP B OD1   1 
ATOM   170  O  OD2   . ASP A 1 27  ? 32.23779  -30.19283 -8.21489  1.000 83.93296  ? 106 ASP B OD2   1 
ATOM   171  N  N     . LEU A 1 28  ? 33.58622  -31.64323 -3.58648  1.000 73.82614  ? 107 LEU B N     1 
ATOM   172  C  CA    . LEU A 1 28  ? 32.72709  -32.46719 -2.74296  1.000 75.85396  ? 107 LEU B CA    1 
ATOM   173  C  C     . LEU A 1 28  ? 31.41645  -31.75209 -2.42553  1.000 77.16955  ? 107 LEU B C     1 
ATOM   174  O  O     . LEU A 1 28  ? 30.91586  -31.80449 -1.30081  1.000 80.86801  ? 107 LEU B O     1 
ATOM   175  C  CB    . LEU A 1 28  ? 33.44489  -32.85878 -1.45344  1.000 81.44281  ? 107 LEU B CB    1 
ATOM   176  C  CG    . LEU A 1 28  ? 34.62054  -33.83311 -1.55203  1.000 82.18467  ? 107 LEU B CG    1 
ATOM   177  C  CD1   . LEU A 1 28  ? 35.26534  -34.02617 -0.19048  1.000 81.56471  ? 107 LEU B CD1   1 
ATOM   178  C  CD2   . LEU A 1 28  ? 34.16406  -35.16596 -2.11806  1.000 87.82103  ? 107 LEU B CD2   1 
ATOM   179  N  N     . SER A 1 29  ? 30.84368  -31.08085 -3.41779  1.000 75.55053  ? 108 SER B N     1 
ATOM   180  C  CA    . SER A 1 29  ? 29.63559  -30.29632 -3.21749  1.000 81.49292  ? 108 SER B CA    1 
ATOM   181  C  C     . SER A 1 29  ? 28.38549  -31.15804 -3.36641  1.000 81.72222  ? 108 SER B C     1 
ATOM   182  O  O     . SER A 1 29  ? 28.37039  -32.14692 -4.10448  1.000 85.92722  ? 108 SER B O     1 
ATOM   183  C  CB    . SER A 1 29  ? 29.58440  -29.13009 -4.20583  1.000 74.57953  ? 108 SER B CB    1 
ATOM   184  O  OG    . SER A 1 29  ? 29.60149  -29.59389 -5.54419  1.000 77.80414  ? 108 SER B OG    1 
ATOM   185  N  N     . LYS A 1 30  ? 27.33650  -30.77186 -2.63408  1.000 82.86421  ? 109 LYS B N     1 
ATOM   186  C  CA    . LYS A 1 30  ? 26.00272  -31.37620 -2.72925  1.000 83.80352  ? 109 LYS B CA    1 
ATOM   187  C  C     . LYS A 1 30  ? 26.00487  -32.86769 -2.39920  1.000 74.21688  ? 109 LYS B C     1 
ATOM   188  O  O     . LYS A 1 30  ? 25.15012  -33.61688 -2.87708  1.000 78.80110  ? 109 LYS B O     1 
ATOM   189  C  CB    . LYS A 1 30  ? 25.38183  -31.14200 -4.10966  1.000 86.72597  ? 109 LYS B CB    1 
ATOM   190  C  CG    . LYS A 1 30  ? 25.37523  -29.68729 -4.55144  1.000 78.70320  ? 109 LYS B CG    1 
ATOM   191  C  CD    . LYS A 1 30  ? 24.40291  -29.46792 -5.69838  1.000 75.32513  ? 109 LYS B CD    1 
ATOM   192  C  CE    . LYS A 1 30  ? 24.82887  -28.29876 -6.56909  1.000 88.43368  ? 109 LYS B CE    1 
ATOM   193  N  NZ    . LYS A 1 30  ? 26.14315  -28.55621 -7.23040  1.000 85.18836  ? 109 LYS B NZ    1 
ATOM   194  N  N     . ARG A 1 31  ? 26.94709  -33.31410 -1.57139  1.000 76.37526  ? 110 ARG B N     1 
ATOM   195  C  CA    . ARG A 1 31  ? 27.02878  -34.71120 -1.17070  1.000 66.74277  ? 110 ARG B CA    1 
ATOM   196  C  C     . ARG A 1 31  ? 26.50358  -34.94888 0.23871   1.000 79.83239  ? 110 ARG B C     1 
ATOM   197  O  O     . ARG A 1 31  ? 26.75292  -36.01734 0.80883   1.000 78.68213  ? 110 ARG B O     1 
ATOM   198  C  CB    . ARG A 1 31  ? 28.46876  -35.20843 -1.28140  1.000 61.57686  ? 110 ARG B CB    1 
ATOM   199  C  CG    . ARG A 1 31  ? 29.02128  -35.18156 -2.68866  1.000 73.20638  ? 110 ARG B CG    1 
ATOM   200  C  CD    . ARG A 1 31  ? 30.47242  -35.62122 -2.70096  1.000 89.56815  ? 110 ARG B CD    1 
ATOM   201  N  NE    . ARG A 1 31  ? 31.06382  -35.51991 -4.02900  1.000 96.08944  ? 110 ARG B NE    1 
ATOM   202  C  CZ    . ARG A 1 31  ? 31.14087  -36.52264 -4.89275  1.000 104.95661 ? 110 ARG B CZ    1 
ATOM   203  N  NH1   . ARG A 1 31  ? 30.66951  -37.72418 -4.60086  1.000 109.47421 ? 110 ARG B NH1   1 
ATOM   204  N  NH2   . ARG A 1 31  ? 31.70978  -36.31602 -6.07730  1.000 102.70542 ? 110 ARG B NH2   1 
ATOM   205  N  N     . SER A 1 32  ? 25.79027  -33.97539 0.81103   1.000 74.17962  ? 111 SER B N     1 
ATOM   206  C  CA    . SER A 1 32  ? 25.17626  -34.10780 2.13508   1.000 76.28615  ? 111 SER B CA    1 
ATOM   207  C  C     . SER A 1 32  ? 26.19953  -34.49759 3.19933   1.000 73.83581  ? 111 SER B C     1 
ATOM   208  O  O     . SER A 1 32  ? 25.87714  -35.19697 4.16168   1.000 83.28836  ? 111 SER B O     1 
ATOM   209  C  CB    . SER A 1 32  ? 24.02222  -35.11413 2.10719   1.000 80.21936  ? 111 SER B CB    1 
ATOM   210  O  OG    . SER A 1 32  ? 23.13498  -34.84422 1.03573   1.000 86.44904  ? 111 SER B OG    1 
ATOM   211  N  N     . ILE A 1 33  ? 27.44197  -34.04223 3.03339   1.000 76.02352  ? 112 ILE B N     1 
ATOM   212  C  CA    . ILE A 1 33  ? 28.51491  -34.41533 3.94833   1.000 74.43689  ? 112 ILE B CA    1 
ATOM   213  C  C     . ILE A 1 33  ? 28.31046  -33.72348 5.28906   1.000 77.37444  ? 112 ILE B C     1 
ATOM   214  O  O     . ILE A 1 33  ? 28.00890  -32.52446 5.34961   1.000 77.12540  ? 112 ILE B O     1 
ATOM   215  C  CB    . ILE A 1 33  ? 29.88183  -34.06160 3.34464   1.000 72.41779  ? 112 ILE B CB    1 
ATOM   216  C  CG1   . ILE A 1 33  ? 30.03766  -34.70515 1.96563   1.000 80.94289  ? 112 ILE B CG1   1 
ATOM   217  C  CG2   . ILE A 1 33  ? 31.00496  -34.50120 4.27103   1.000 81.86961  ? 112 ILE B CG2   1 
ATOM   218  C  CD1   . ILE A 1 33  ? 31.34763  -34.37893 1.28189   1.000 75.69849  ? 112 ILE B CD1   1 
ATOM   219  N  N     . HIS A 1 34  ? 28.47104  -34.48016 6.37440   1.000 84.88522  ? 113 HIS B N     1 
ATOM   220  C  CA    . HIS A 1 34  ? 28.35350  -33.95019 7.72844   1.000 82.08119  ? 113 HIS B CA    1 
ATOM   221  C  C     . HIS A 1 34  ? 29.70270  -33.69265 8.38406   1.000 89.64791  ? 113 HIS B C     1 
ATOM   222  O  O     . HIS A 1 34  ? 29.88250  -32.65742 9.03427   1.000 83.63834  ? 113 HIS B O     1 
ATOM   223  C  CB    . HIS A 1 34  ? 27.54339  -34.90743 8.61034   1.000 71.88488  ? 113 HIS B CB    1 
ATOM   224  C  CG    . HIS A 1 34  ? 26.07235  -34.90002 8.32807   1.000 82.87494  ? 113 HIS B CG    1 
ATOM   225  N  ND1   . HIS A 1 34  ? 25.52324  -35.49376 7.21173   1.000 79.54923  ? 113 HIS B ND1   1 
ATOM   226  C  CD2   . HIS A 1 34  ? 25.03481  -34.37784 9.02464   1.000 79.56933  ? 113 HIS B CD2   1 
ATOM   227  C  CE1   . HIS A 1 34  ? 24.21174  -35.33392 7.23090   1.000 88.82217  ? 113 HIS B CE1   1 
ATOM   228  N  NE2   . HIS A 1 34  ? 23.88973  -34.66073 8.32079   1.000 85.17347  ? 113 HIS B NE2   1 
ATOM   229  N  N     . ILE A 1 35  ? 30.65402  -34.61191 8.23510   1.000 82.84316  ? 114 ILE B N     1 
ATOM   230  C  CA    . ILE A 1 35  ? 31.97681  -34.48652 8.83547   1.000 78.15483  ? 114 ILE B CA    1 
ATOM   231  C  C     . ILE A 1 35  ? 33.01359  -34.81897 7.77308   1.000 78.69053  ? 114 ILE B C     1 
ATOM   232  O  O     . ILE A 1 35  ? 33.05717  -35.95035 7.27471   1.000 76.24153  ? 114 ILE B O     1 
ATOM   233  C  CB    . ILE A 1 35  ? 32.14616  -35.39800 10.06279  1.000 84.89123  ? 114 ILE B CB    1 
ATOM   234  C  CG1   . ILE A 1 35  ? 31.25831  -34.91457 11.21235  1.000 78.54630  ? 114 ILE B CG1   1 
ATOM   235  C  CG2   . ILE A 1 35  ? 33.60461  -35.44699 10.49407  1.000 79.21878  ? 114 ILE B CG2   1 
ATOM   236  C  CD1   . ILE A 1 35  ? 31.37177  -35.74967 12.46912  1.000 79.54370  ? 114 ILE B CD1   1 
ATOM   237  N  N     . LEU A 1 36  ? 33.83597  -33.84018 7.42562   1.000 87.46182  ? 115 LEU B N     1 
ATOM   238  C  CA    . LEU A 1 36  ? 34.90787  -34.05528 6.46345   1.000 79.65382  ? 115 LEU B CA    1 
ATOM   239  C  C     . LEU A 1 36  ? 35.99447  -34.91115 7.10086   1.000 79.02384  ? 115 LEU B C     1 
ATOM   240  O  O     . LEU A 1 36  ? 36.55414  -34.51405 8.13144   1.000 86.62397  ? 115 LEU B O     1 
ATOM   241  C  CB    . LEU A 1 36  ? 35.47819  -32.71717 6.00668   1.000 72.58289  ? 115 LEU B CB    1 
ATOM   242  C  CG    . LEU A 1 36  ? 36.50286  -32.75171 4.87346   1.000 81.08966  ? 115 LEU B CG    1 
ATOM   243  C  CD1   . LEU A 1 36  ? 35.85156  -33.21621 3.57850   1.000 76.73504  ? 115 LEU B CD1   1 
ATOM   244  C  CD2   . LEU A 1 36  ? 37.14560  -31.38560 4.70093   1.000 69.65202  ? 115 LEU B CD2   1 
ATOM   245  N  N     . PRO A 1 37  ? 36.32176  -36.07447 6.54287   1.000 75.96046  ? 116 PRO B N     1 
ATOM   246  C  CA    . PRO A 1 37  ? 37.33329  -36.93345 7.17052   1.000 79.26121  ? 116 PRO B CA    1 
ATOM   247  C  C     . PRO A 1 37  ? 38.70251  -36.26984 7.21218   1.000 85.98757  ? 116 PRO B C     1 
ATOM   248  O  O     . PRO A 1 37  ? 39.04638  -35.44215 6.36439   1.000 92.94632  ? 116 PRO B O     1 
ATOM   249  C  CB    . PRO A 1 37  ? 37.34632  -38.18124 6.27849   1.000 79.21774  ? 116 PRO B CB    1 
ATOM   250  C  CG    . PRO A 1 37  ? 36.75335  -37.73907 4.98288   1.000 86.14008  ? 116 PRO B CG    1 
ATOM   251  C  CD    . PRO A 1 37  ? 35.76551  -36.66553 5.31517   1.000 81.72624  ? 116 PRO B CD    1 
ATOM   252  N  N     . SER A 1 38  ? 39.48753  -36.65105 8.22652   1.000 90.47033  ? 117 SER B N     1 
ATOM   253  C  CA    . SER A 1 38  ? 40.82815  -36.11120 8.43472   1.000 85.55637  ? 117 SER B CA    1 
ATOM   254  C  C     . SER A 1 38  ? 41.81929  -36.50664 7.34265   1.000 84.20512  ? 117 SER B C     1 
ATOM   255  O  O     . SER A 1 38  ? 42.87368  -35.87256 7.23608   1.000 87.72930  ? 117 SER B O     1 
ATOM   256  C  CB    . SER A 1 38  ? 41.36324  -36.55206 9.80574   1.000 84.33296  ? 117 SER B CB    1 
ATOM   257  O  OG    . SER A 1 38  ? 40.53972  -36.08820 10.86720  1.000 94.46662  ? 117 SER B OG    1 
ATOM   258  N  N     . SER A 1 39  ? 41.51903  -37.52306 6.53150   1.000 89.64069  ? 118 SER B N     1 
ATOM   259  C  CA    . SER A 1 39  ? 42.41757  -37.94265 5.45536   1.000 85.99964  ? 118 SER B CA    1 
ATOM   260  C  C     . SER A 1 39  ? 42.61554  -36.87692 4.37572   1.000 79.89981  ? 118 SER B C     1 
ATOM   261  O  O     . SER A 1 39  ? 43.39970  -37.10965 3.45349   1.000 79.92147  ? 118 SER B O     1 
ATOM   262  C  CB    . SER A 1 39  ? 41.90232  -39.23519 4.82104   1.000 87.49443  ? 118 SER B CB    1 
ATOM   263  O  OG    . SER A 1 39  ? 40.52189  -39.13259 4.52396   1.000 84.36601  ? 118 SER B OG    1 
ATOM   264  N  N     . ILE A 1 40  ? 41.95331  -35.72030 4.46579   1.000 82.09621  ? 119 ILE B N     1 
ATOM   265  C  CA    . ILE A 1 40  ? 42.17167  -34.66164 3.48726   1.000 84.85729  ? 119 ILE B CA    1 
ATOM   266  C  C     . ILE A 1 40  ? 43.50960  -33.97095 3.68644   1.000 81.67657  ? 119 ILE B C     1 
ATOM   267  O  O     . ILE A 1 40  ? 43.93581  -33.20393 2.81704   1.000 77.68133  ? 119 ILE B O     1 
ATOM   268  C  CB    . ILE A 1 40  ? 41.02580  -33.62728 3.53885   1.000 79.19011  ? 119 ILE B CB    1 
ATOM   269  C  CG1   . ILE A 1 40  ? 40.92983  -32.80433 2.24583   1.000 82.46465  ? 119 ILE B CG1   1 
ATOM   270  C  CG2   . ILE A 1 40  ? 41.19206  -32.70844 4.73636   1.000 65.76168  ? 119 ILE B CG2   1 
ATOM   271  C  CD1   . ILE A 1 40  ? 39.67695  -31.92268 2.18649   1.000 72.22098  ? 119 ILE B CD1   1 
ATOM   272  N  N     . LYS A 1 41  ? 44.18123  -34.21961 4.81444   1.000 75.16660  ? 120 LYS B N     1 
ATOM   273  C  CA    . LYS A 1 41  ? 45.50201  -33.64908 5.04792   1.000 76.97636  ? 120 LYS B CA    1 
ATOM   274  C  C     . LYS A 1 41  ? 46.51820  -34.11763 4.01411   1.000 88.58867  ? 120 LYS B C     1 
ATOM   275  O  O     . LYS A 1 41  ? 47.52448  -33.43380 3.79094   1.000 73.41407  ? 120 LYS B O     1 
ATOM   276  C  CB    . LYS A 1 41  ? 45.97750  -34.00903 6.45744   1.000 75.50939  ? 120 LYS B CB    1 
ATOM   277  C  CG    . LYS A 1 41  ? 46.30568  -35.48369 6.64956   1.000 73.21136  ? 120 LYS B CG    1 
ATOM   278  C  CD    . LYS A 1 41  ? 46.47174  -35.83281 8.11913   1.000 71.40539  ? 120 LYS B CD    1 
ATOM   279  C  CE    . LYS A 1 41  ? 47.64209  -35.09347 8.74418   1.000 90.72201  ? 120 LYS B CE    1 
ATOM   280  N  NZ    . LYS A 1 41  ? 47.87163  -35.51507 10.15766  1.000 88.80261  ? 120 LYS B NZ    1 
ATOM   281  N  N     . GLU A 1 42  ? 46.27034  -35.26305 3.37309   1.000 85.94445  ? 121 GLU B N     1 
ATOM   282  C  CA    . GLU A 1 42  ? 47.19447  -35.79748 2.38159   1.000 81.54509  ? 121 GLU B CA    1 
ATOM   283  C  C     . GLU A 1 42  ? 47.17085  -35.01415 1.07715   1.000 83.11465  ? 121 GLU B C     1 
ATOM   284  O  O     . GLU A 1 42  ? 48.14484  -35.06929 0.31935   1.000 92.84651  ? 121 GLU B O     1 
ATOM   285  C  CB    . GLU A 1 42  ? 46.86738  -37.26607 2.10848   1.000 86.79794  ? 121 GLU B CB    1 
ATOM   286  C  CG    . GLU A 1 42  ? 47.19032  -38.19150 3.26565   1.000 99.55811  ? 121 GLU B CG    1 
ATOM   287  C  CD    . GLU A 1 42  ? 48.68378  -38.35690 3.46899   1.000 111.56228 ? 121 GLU B CD    1 
ATOM   288  O  OE1   . GLU A 1 42  ? 49.38670  -38.65899 2.48032   1.000 112.42105 ? 121 GLU B OE1   1 
ATOM   289  O  OE2   . GLU A 1 42  ? 49.15583  -38.17533 4.61221   1.000 107.78035 ? 121 GLU B OE2   1 
ATOM   290  N  N     . LEU A 1 43  ? 46.09470  -34.28430 0.80400   1.000 85.05501  ? 122 LEU B N     1 
ATOM   291  C  CA    . LEU A 1 43  ? 45.90134  -33.61651 -0.48366  1.000 82.17636  ? 122 LEU B CA    1 
ATOM   292  C  C     . LEU A 1 43  ? 46.54853  -32.23357 -0.50438  1.000 77.77246  ? 122 LEU B C     1 
ATOM   293  O  O     . LEU A 1 43  ? 45.90624  -31.23215 -0.81691  1.000 84.52706  ? 122 LEU B O     1 
ATOM   294  C  CB    . LEU A 1 43  ? 44.41067  -33.53084 -0.79722  1.000 84.66556  ? 122 LEU B CB    1 
ATOM   295  C  CG    . LEU A 1 43  ? 43.66439  -34.74480 -1.37208  1.000 86.92232  ? 122 LEU B CG    1 
ATOM   296  C  CD1   . LEU A 1 43  ? 43.89965  -36.02332 -0.57936  1.000 83.14738  ? 122 LEU B CD1   1 
ATOM   297  C  CD2   . LEU A 1 43  ? 42.17217  -34.45006 -1.45259  1.000 85.53392  ? 122 LEU B CD2   1 
ATOM   298  N  N     . THR A 1 44  ? 47.84341  -32.17221 -0.18150  1.000 71.24547  ? 123 THR B N     1 
ATOM   299  C  CA    . THR A 1 44  ? 48.53398  -30.89180 -0.05904  1.000 78.96118  ? 123 THR B CA    1 
ATOM   300  C  C     . THR A 1 44  ? 48.75575  -30.19607 -1.39583  1.000 79.44493  ? 123 THR B C     1 
ATOM   301  O  O     . THR A 1 44  ? 49.19020  -29.03894 -1.40315  1.000 81.34980  ? 123 THR B O     1 
ATOM   302  C  CB    . THR A 1 44  ? 49.88289  -31.07650 0.64353   1.000 78.70715  ? 123 THR B CB    1 
ATOM   303  O  OG1   . THR A 1 44  ? 50.66897  -32.04651 -0.06171  1.000 92.04109  ? 123 THR B OG1   1 
ATOM   304  C  CG2   . THR A 1 44  ? 49.67830  -31.53664 2.07615   1.000 71.77985  ? 123 THR B CG2   1 
ATOM   305  N  N     . GLN A 1 45  ? 48.47669  -30.85913 -2.51580  1.000 74.64826  ? 124 GLN B N     1 
ATOM   306  C  CA    . GLN A 1 45  ? 48.63151  -30.23783 -3.82471  1.000 81.01381  ? 124 GLN B CA    1 
ATOM   307  C  C     . GLN A 1 45  ? 47.41256  -29.42469 -4.24370  1.000 90.58702  ? 124 GLN B C     1 
ATOM   308  O  O     . GLN A 1 45  ? 47.42417  -28.84115 -5.33325  1.000 92.20422  ? 124 GLN B O     1 
ATOM   309  C  CB    . GLN A 1 45  ? 48.92298  -31.30552 -4.88472  1.000 84.88587  ? 124 GLN B CB    1 
ATOM   310  C  CG    . GLN A 1 45  ? 47.69034  -32.04015 -5.40500  1.000 87.30516  ? 124 GLN B CG    1 
ATOM   311  C  CD    . GLN A 1 45  ? 47.08693  -32.99179 -4.38795  1.000 88.83357  ? 124 GLN B CD    1 
ATOM   312  O  OE1   . GLN A 1 45  ? 47.70702  -33.31322 -3.37457  1.000 95.78388  ? 124 GLN B OE1   1 
ATOM   313  N  NE2   . GLN A 1 45  ? 45.86859  -33.45005 -4.65761  1.000 88.34613  ? 124 GLN B NE2   1 
ATOM   314  N  N     . LEU A 1 46  ? 46.37583  -29.36324 -3.41043  1.000 89.65129  ? 125 LEU B N     1 
ATOM   315  C  CA    . LEU A 1 46  ? 45.13424  -28.70656 -3.79652  1.000 83.45072  ? 125 LEU B CA    1 
ATOM   316  C  C     . LEU A 1 46  ? 45.28697  -27.19090 -3.80797  1.000 80.16246  ? 125 LEU B C     1 
ATOM   317  O  O     . LEU A 1 46  ? 45.91112  -26.60294 -2.92106  1.000 83.16491  ? 125 LEU B O     1 
ATOM   318  C  CB    . LEU A 1 46  ? 44.00575  -29.10237 -2.84406  1.000 72.75684  ? 125 LEU B CB    1 
ATOM   319  C  CG    . LEU A 1 46  ? 43.43270  -30.51314 -2.98786  1.000 79.88185  ? 125 LEU B CG    1 
ATOM   320  C  CD1   . LEU A 1 46  ? 42.30523  -30.74322 -1.99398  1.000 77.77907  ? 125 LEU B CD1   1 
ATOM   321  C  CD2   . LEU A 1 46  ? 42.94472  -30.74065 -4.40476  1.000 80.25758  ? 125 LEU B CD2   1 
ATOM   322  N  N     . THR A 1 47  ? 44.70850  -26.55863 -4.82892  1.000 83.35579  ? 126 THR B N     1 
ATOM   323  C  CA    . THR A 1 47  ? 44.57515  -25.11054 -4.87476  1.000 85.97049  ? 126 THR B CA    1 
ATOM   324  C  C     . THR A 1 47  ? 43.12736  -24.65022 -4.81503  1.000 80.04789  ? 126 THR B C     1 
ATOM   325  O  O     . THR A 1 47  ? 42.88164  -23.46220 -4.57858  1.000 76.96429  ? 126 THR B O     1 
ATOM   326  C  CB    . THR A 1 47  ? 45.22936  -24.54309 -6.14415  1.000 83.02642  ? 126 THR B CB    1 
ATOM   327  O  OG1   . THR A 1 47  ? 44.66207  -25.17129 -7.30055  1.000 88.96600  ? 126 THR B OG1   1 
ATOM   328  C  CG2   . THR A 1 47  ? 46.73067  -24.77846 -6.12242  1.000 76.71487  ? 126 THR B CG2   1 
ATOM   329  N  N     . GLU A 1 48  ? 42.17027  -25.55196 -5.02547  1.000 77.61526  ? 127 GLU B N     1 
ATOM   330  C  CA    . GLU A 1 48  ? 40.75153  -25.23525 -4.94378  1.000 77.08983  ? 127 GLU B CA    1 
ATOM   331  C  C     . GLU A 1 48  ? 40.04219  -26.37694 -4.23487  1.000 73.57585  ? 127 GLU B C     1 
ATOM   332  O  O     . GLU A 1 48  ? 40.24501  -27.54515 -4.57857  1.000 74.00711  ? 127 GLU B O     1 
ATOM   333  C  CB    . GLU A 1 48  ? 40.14594  -25.01386 -6.33591  1.000 78.94612  ? 127 GLU B CB    1 
ATOM   334  C  CG    . GLU A 1 48  ? 40.79946  -23.89213 -7.12982  1.000 82.80183  ? 127 GLU B CG    1 
ATOM   335  C  CD    . GLU A 1 48  ? 40.50484  -23.97958 -8.61473  1.000 92.27119  ? 127 GLU B CD    1 
ATOM   336  O  OE1   . GLU A 1 48  ? 39.39813  -24.43058 -8.97993  1.000 86.05195  ? 127 GLU B OE1   1 
ATOM   337  O  OE2   . GLU A 1 48  ? 41.38681  -23.60675 -9.41729  1.000 96.23520  ? 127 GLU B OE2   1 
ATOM   338  N  N     . LEU A 1 49  ? 39.22103  -26.03625 -3.24419  1.000 76.27650  ? 128 LEU B N     1 
ATOM   339  C  CA    . LEU A 1 49  ? 38.45068  -27.00976 -2.47608  1.000 65.95699  ? 128 LEU B CA    1 
ATOM   340  C  C     . LEU A 1 49  ? 37.01741  -26.50741 -2.38696  1.000 69.37633  ? 128 LEU B C     1 
ATOM   341  O  O     . LEU A 1 49  ? 36.75399  -25.48841 -1.74053  1.000 73.79122  ? 128 LEU B O     1 
ATOM   342  C  CB    . LEU A 1 49  ? 39.04711  -27.21178 -1.08334  1.000 64.66053  ? 128 LEU B CB    1 
ATOM   343  C  CG    . LEU A 1 49  ? 38.28875  -28.15322 -0.14849  1.000 71.26364  ? 128 LEU B CG    1 
ATOM   344  C  CD1   . LEU A 1 49  ? 38.19574  -29.54150 -0.75492  1.000 62.31781  ? 128 LEU B CD1   1 
ATOM   345  C  CD2   . LEU A 1 49  ? 38.95799  -28.20402 1.21685   1.000 68.59212  ? 128 LEU B CD2   1 
ATOM   346  N  N     . TYR A 1 50  ? 36.09557  -27.21531 -3.03444  1.000 76.45542  ? 129 TYR B N     1 
ATOM   347  C  CA    . TYR A 1 50  ? 34.69186  -26.82141 -3.09780  1.000 64.57149  ? 129 TYR B CA    1 
ATOM   348  C  C     . TYR A 1 50  ? 33.88650  -27.75427 -2.20249  1.000 68.30555  ? 129 TYR B C     1 
ATOM   349  O  O     . TYR A 1 50  ? 33.79831  -28.95761 -2.46957  1.000 81.57120  ? 129 TYR B O     1 
ATOM   350  C  CB    . TYR A 1 50  ? 34.18702  -26.85347 -4.53850  1.000 61.31156  ? 129 TYR B CB    1 
ATOM   351  C  CG    . TYR A 1 50  ? 35.00382  -25.99026 -5.47401  1.000 66.35691  ? 129 TYR B CG    1 
ATOM   352  C  CD1   . TYR A 1 50  ? 34.81252  -24.61707 -5.52416  1.000 72.54537  ? 129 TYR B CD1   1 
ATOM   353  C  CD2   . TYR A 1 50  ? 35.97019  -26.54716 -6.30160  1.000 68.46358  ? 129 TYR B CD2   1 
ATOM   354  C  CE1   . TYR A 1 50  ? 35.55777  -23.82135 -6.37261  1.000 78.52425  ? 129 TYR B CE1   1 
ATOM   355  C  CE2   . TYR A 1 50  ? 36.72124  -25.75891 -7.15464  1.000 77.79451  ? 129 TYR B CE2   1 
ATOM   356  C  CZ    . TYR A 1 50  ? 36.51039  -24.39575 -7.18512  1.000 81.29500  ? 129 TYR B CZ    1 
ATOM   357  O  OH    . TYR A 1 50  ? 37.25393  -23.60122 -8.02901  1.000 86.52226  ? 129 TYR B OH    1 
ATOM   358  N  N     . LEU A 1 51  ? 33.30493  -27.19711 -1.13829  1.000 58.47541  ? 130 LEU B N     1 
ATOM   359  C  CA    . LEU A 1 51  ? 32.51926  -27.96233 -0.17655  1.000 70.38371  ? 130 LEU B CA    1 
ATOM   360  C  C     . LEU A 1 51  ? 31.15327  -27.32391 0.04568   1.000 72.53105  ? 130 LEU B C     1 
ATOM   361  O  O     . LEU A 1 51  ? 30.57876  -27.43511 1.13239   1.000 68.13265  ? 130 LEU B O     1 
ATOM   362  C  CB    . LEU A 1 51  ? 33.26101  -28.09825 1.15445   1.000 57.98391  ? 130 LEU B CB    1 
ATOM   363  C  CG    . LEU A 1 51  ? 34.65326  -28.73519 1.14367   1.000 79.65157  ? 130 LEU B CG    1 
ATOM   364  C  CD1   . LEU A 1 51  ? 35.32939  -28.58182 2.50181   1.000 69.73544  ? 130 LEU B CD1   1 
ATOM   365  C  CD2   . LEU A 1 51  ? 34.57567  -30.20139 0.74961   1.000 80.33757  ? 130 LEU B CD2   1 
ATOM   366  N  N     . TYR A 1 52  ? 30.61889  -26.65185 -0.96880  1.000 67.52811  ? 131 TYR B N     1 
ATOM   367  C  CA    . TYR A 1 52  ? 29.37221  -25.93004 -0.78519  1.000 70.91503  ? 131 TYR B CA    1 
ATOM   368  C  C     . TYR A 1 52  ? 28.17335  -26.87092 -0.88287  1.000 79.50482  ? 131 TYR B C     1 
ATOM   369  O  O     . TYR A 1 52  ? 28.24422  -27.95839 -1.46261  1.000 81.26400  ? 131 TYR B O     1 
ATOM   370  C  CB    . TYR A 1 52  ? 29.24644  -24.79326 -1.80271  1.000 70.38326  ? 131 TYR B CB    1 
ATOM   371  C  CG    . TYR A 1 52  ? 29.41433  -25.20154 -3.24899  1.000 76.22718  ? 131 TYR B CG    1 
ATOM   372  C  CD1   . TYR A 1 52  ? 30.67109  -25.22886 -3.84114  1.000 77.19167  ? 131 TYR B CD1   1 
ATOM   373  C  CD2   . TYR A 1 52  ? 28.31443  -25.53563 -4.02986  1.000 74.77986  ? 131 TYR B CD2   1 
ATOM   374  C  CE1   . TYR A 1 52  ? 30.83079  -25.59246 -5.16593  1.000 80.66945  ? 131 TYR B CE1   1 
ATOM   375  C  CE2   . TYR A 1 52  ? 28.46351  -25.90019 -5.35731  1.000 74.51536  ? 131 TYR B CE2   1 
ATOM   376  C  CZ    . TYR A 1 52  ? 29.72449  -25.92675 -5.91903  1.000 84.52977  ? 131 TYR B CZ    1 
ATOM   377  O  OH    . TYR A 1 52  ? 29.88361  -26.28810 -7.23688  1.000 76.54969  ? 131 TYR B OH    1 
ATOM   378  N  N     . SER A 1 53  ? 27.06213  -26.43238 -0.28669  1.000 76.46958  ? 132 SER B N     1 
ATOM   379  C  CA    . SER A 1 53  ? 25.80314  -27.17885 -0.26441  1.000 75.99834  ? 132 SER B CA    1 
ATOM   380  C  C     . SER A 1 53  ? 25.98138  -28.54948 0.39415   1.000 86.23419  ? 132 SER B C     1 
ATOM   381  O  O     . SER A 1 53  ? 25.69979  -29.59589 -0.19112  1.000 94.42915  ? 132 SER B O     1 
ATOM   382  C  CB    . SER A 1 53  ? 25.21745  -27.31528 -1.67423  1.000 73.38833  ? 132 SER B CB    1 
ATOM   383  O  OG    . SER A 1 53  ? 24.90163  -26.04744 -2.21875  1.000 87.23442  ? 132 SER B OG    1 
ATOM   384  N  N     . ASN A 1 54  ? 26.45075  -28.52391 1.63625   1.000 74.03506  ? 133 ASN B N     1 
ATOM   385  C  CA    . ASN A 1 54  ? 26.57649  -29.73431 2.43890   1.000 68.41962  ? 133 ASN B CA    1 
ATOM   386  C  C     . ASN A 1 54  ? 25.93839  -29.46213 3.79938   1.000 71.51736  ? 133 ASN B C     1 
ATOM   387  O  O     . ASN A 1 54  ? 25.14291  -28.53072 3.97430   1.000 86.47917  ? 133 ASN B O     1 
ATOM   388  C  CB    . ASN A 1 54  ? 28.04259  -30.17380 2.53088   1.000 63.49973  ? 133 ASN B CB    1 
ATOM   389  C  CG    . ASN A 1 54  ? 28.53049  -30.83473 1.25745   1.000 75.61757  ? 133 ASN B CG    1 
ATOM   390  O  OD1   . ASN A 1 54  ? 27.82381  -31.64190 0.65469   1.000 77.38607  ? 133 ASN B OD1   1 
ATOM   391  N  ND2   . ASN A 1 54  ? 29.74258  -30.49092 0.83736   1.000 82.84690  ? 133 ASN B ND2   1 
ATOM   392  N  N     . LYS A 1 55  ? 26.27759  -30.28849 4.78799   1.000 72.05637  ? 134 LYS B N     1 
ATOM   393  C  CA    . LYS A 1 55  ? 25.69847  -30.19698 6.12364   1.000 85.22020  ? 134 LYS B CA    1 
ATOM   394  C  C     . LYS A 1 55  ? 26.77868  -30.05716 7.19315   1.000 75.58149  ? 134 LYS B C     1 
ATOM   395  O  O     . LYS A 1 55  ? 26.58307  -30.46393 8.34105   1.000 83.60248  ? 134 LYS B O     1 
ATOM   396  C  CB    . LYS A 1 55  ? 24.81425  -31.41184 6.41273   1.000 84.91096  ? 134 LYS B CB    1 
ATOM   397  C  CG    . LYS A 1 55  ? 23.86837  -31.79375 5.27916   1.000 84.67918  ? 134 LYS B CG    1 
ATOM   398  C  CD    . LYS A 1 55  ? 22.82894  -30.71385 5.01321   1.000 78.95256  ? 134 LYS B CD    1 
ATOM   399  C  CE    . LYS A 1 55  ? 21.86352  -30.57499 6.17759   1.000 92.43309  ? 134 LYS B CE    1 
ATOM   400  N  NZ    . LYS A 1 55  ? 20.78010  -29.59687 5.88149   1.000 94.73723  ? 134 LYS B NZ    1 
ATOM   401  N  N     . LEU A 1 56  ? 27.92064  -29.47976 6.82819   1.000 71.95694  ? 135 LEU B N     1 
ATOM   402  C  CA    . LEU A 1 56  ? 29.03399  -29.35585 7.75906   1.000 74.39213  ? 135 LEU B CA    1 
ATOM   403  C  C     . LEU A 1 56  ? 28.70305  -28.37551 8.87775   1.000 81.84807  ? 135 LEU B C     1 
ATOM   404  O  O     . LEU A 1 56  ? 28.12198  -27.31170 8.64487   1.000 81.82572  ? 135 LEU B O     1 
ATOM   405  C  CB    . LEU A 1 56  ? 30.29187  -28.89231 7.02302   1.000 67.99605  ? 135 LEU B CB    1 
ATOM   406  C  CG    . LEU A 1 56  ? 30.73940  -29.71197 5.81076   1.000 74.36958  ? 135 LEU B CG    1 
ATOM   407  C  CD1   . LEU A 1 56  ? 31.81950  -28.97519 5.03625   1.000 66.42824  ? 135 LEU B CD1   1 
ATOM   408  C  CD2   . LEU A 1 56  ? 31.22681  -31.09014 6.23670   1.000 75.12857  ? 135 LEU B CD2   1 
ATOM   409  N  N     . GLN A 1 57  ? 29.07630  -28.74273 10.10524  1.000 79.51924  ? 136 GLN B N     1 
ATOM   410  C  CA    . GLN A 1 57  ? 28.97026  -27.84033 11.24243  1.000 84.11155  ? 136 GLN B CA    1 
ATOM   411  C  C     . GLN A 1 57  ? 30.32170  -27.39320 11.77803  1.000 85.92169  ? 136 GLN B C     1 
ATOM   412  O  O     . GLN A 1 57  ? 30.37889  -26.41165 12.52631  1.000 85.71045  ? 136 GLN B O     1 
ATOM   413  C  CB    . GLN A 1 57  ? 28.16839  -28.49542 12.37714  1.000 80.56709  ? 136 GLN B CB    1 
ATOM   414  C  CG    . GLN A 1 57  ? 26.79534  -28.99198 11.95029  1.000 83.01947  ? 136 GLN B CG    1 
ATOM   415  C  CD    . GLN A 1 57  ? 25.93385  -29.41345 13.12435  1.000 91.41647  ? 136 GLN B CD    1 
ATOM   416  O  OE1   . GLN A 1 57  ? 26.00879  -28.82928 14.20509  1.000 88.67228  ? 136 GLN B OE1   1 
ATOM   417  N  NE2   . GLN A 1 57  ? 25.10870  -30.43355 12.91720  1.000 93.88380  ? 136 GLN B NE2   1 
ATOM   418  N  N     . SER A 1 58  ? 31.40031  -28.08195 11.41242  1.000 77.76125  ? 137 SER B N     1 
ATOM   419  C  CA    . SER A 1 58  ? 32.74744  -27.65932 11.75948  1.000 85.74627  ? 137 SER B CA    1 
ATOM   420  C  C     . SER A 1 58  ? 33.69986  -28.17693 10.69318  1.000 77.42403  ? 137 SER B C     1 
ATOM   421  O  O     . SER A 1 58  ? 33.38847  -29.11819 9.95942   1.000 78.69567  ? 137 SER B O     1 
ATOM   422  C  CB    . SER A 1 58  ? 33.16686  -28.16233 13.14747  1.000 87.62511  ? 137 SER B CB    1 
ATOM   423  O  OG    . SER A 1 58  ? 33.41882  -29.55718 13.13424  1.000 77.30600  ? 137 SER B OG    1 
ATOM   424  N  N     . LEU A 1 59  ? 34.86209  -27.54442 10.60669  1.000 75.90838  ? 138 LEU B N     1 
ATOM   425  C  CA    . LEU A 1 59  ? 35.86934  -28.03761 9.68346   1.000 81.34143  ? 138 LEU B CA    1 
ATOM   426  C  C     . LEU A 1 59  ? 37.00987  -28.69590 10.45024  1.000 72.22576  ? 138 LEU B C     1 
ATOM   427  O  O     . LEU A 1 59  ? 37.39378  -28.21244 11.52090  1.000 78.21258  ? 138 LEU B O     1 
ATOM   428  C  CB    . LEU A 1 59  ? 36.42783  -26.90526 8.81554   1.000 79.75826  ? 138 LEU B CB    1 
ATOM   429  C  CG    . LEU A 1 59  ? 36.44174  -27.15856 7.30933   1.000 72.83485  ? 138 LEU B CG    1 
ATOM   430  C  CD1   . LEU A 1 59  ? 35.07494  -27.62626 6.84110   1.000 71.63135  ? 138 LEU B CD1   1 
ATOM   431  C  CD2   . LEU A 1 59  ? 36.85178  -25.89385 6.57913   1.000 68.21043  ? 138 LEU B CD2   1 
ATOM   432  N  N     . PRO A 1 60  ? 37.55674  -29.79979 9.94938   1.000 71.04687  ? 139 PRO B N     1 
ATOM   433  C  CA    . PRO A 1 60  ? 38.66219  -30.45250 10.65729  1.000 72.80862  ? 139 PRO B CA    1 
ATOM   434  C  C     . PRO A 1 60  ? 39.92250  -29.60295 10.61904  1.000 73.24433  ? 139 PRO B C     1 
ATOM   435  O  O     . PRO A 1 60  ? 40.15625  -28.83487 9.68316   1.000 74.43011  ? 139 PRO B O     1 
ATOM   436  C  CB    . PRO A 1 60  ? 38.85066  -31.76585 9.88929   1.000 72.76070  ? 139 PRO B CB    1 
ATOM   437  C  CG    . PRO A 1 60  ? 38.31603  -31.48454 8.52658   1.000 73.97089  ? 139 PRO B CG    1 
ATOM   438  C  CD    . PRO A 1 60  ? 37.18323  -30.51443 8.71679   1.000 75.05540  ? 139 PRO B CD    1 
ATOM   439  N  N     . ALA A 1 61  ? 40.74075  -29.74457 11.66412  1.000 68.73545  ? 140 ALA B N     1 
ATOM   440  C  CA    . ALA A 1 61  ? 41.99226  -28.99873 11.72458  1.000 76.17890  ? 140 ALA B CA    1 
ATOM   441  C  C     . ALA A 1 61  ? 42.93270  -29.36422 10.58440  1.000 82.82110  ? 140 ALA B C     1 
ATOM   442  O  O     . ALA A 1 61  ? 43.75502  -28.53268 10.18399  1.000 71.81213  ? 140 ALA B O     1 
ATOM   443  C  CB    . ALA A 1 61  ? 42.68257  -29.23276 13.06845  1.000 69.53529  ? 140 ALA B CB    1 
ATOM   444  N  N     . GLU A 1 62  ? 42.81117  -30.57950 10.03956  1.000 81.96369  ? 141 GLU B N     1 
ATOM   445  C  CA    . GLU A 1 62  ? 43.70905  -31.03850 8.98481   1.000 75.45258  ? 141 GLU B CA    1 
ATOM   446  C  C     . GLU A 1 62  ? 43.60255  -30.20716 7.71142   1.000 77.70211  ? 141 GLU B C     1 
ATOM   447  O  O     . GLU A 1 62  ? 44.51380  -30.25887 6.87846   1.000 77.67528  ? 141 GLU B O     1 
ATOM   448  C  CB    . GLU A 1 62  ? 43.43337  -32.51070 8.66728   1.000 80.19126  ? 141 GLU B CB    1 
ATOM   449  C  CG    . GLU A 1 62  ? 44.04998  -33.50485 9.65009   1.000 83.72182  ? 141 GLU B CG    1 
ATOM   450  C  CD    . GLU A 1 62  ? 43.31180  -33.57876 10.97748  1.000 86.70126  ? 141 GLU B CD    1 
ATOM   451  O  OE1   . GLU A 1 62  ? 42.28777  -32.88152 11.13811  1.000 85.83887  ? 141 GLU B OE1   1 
ATOM   452  O  OE2   . GLU A 1 62  ? 43.75673  -34.34175 11.86254  1.000 86.09653  ? 141 GLU B OE2   1 
ATOM   453  N  N     . VAL A 1 63  ? 42.51796  -29.44638 7.53536   1.000 82.02140  ? 142 VAL B N     1 
ATOM   454  C  CA    . VAL A 1 63  ? 42.39980  -28.57284 6.37238   1.000 73.49814  ? 142 VAL B CA    1 
ATOM   455  C  C     . VAL A 1 63  ? 43.49185  -27.51082 6.36762   1.000 75.72725  ? 142 VAL B C     1 
ATOM   456  O  O     . VAL A 1 63  ? 43.84651  -26.98731 5.30546   1.000 73.36835  ? 142 VAL B O     1 
ATOM   457  C  CB    . VAL A 1 63  ? 40.99268  -27.93935 6.33015   1.000 70.20897  ? 142 VAL B CB    1 
ATOM   458  C  CG1   . VAL A 1 63  ? 40.80660  -27.10098 5.07287   1.000 70.75142  ? 142 VAL B CG1   1 
ATOM   459  C  CG2   . VAL A 1 63  ? 39.93301  -29.02258 6.39873   1.000 77.17278  ? 142 VAL B CG2   1 
ATOM   460  N  N     . GLY A 1 64  ? 44.05480  -27.19287 7.53349   1.000 75.89556  ? 143 GLY B N     1 
ATOM   461  C  CA    . GLY A 1 64  ? 45.17492  -26.27125 7.60342   1.000 70.47319  ? 143 GLY B CA    1 
ATOM   462  C  C     . GLY A 1 64  ? 46.45740  -26.78917 6.98279   1.000 80.18443  ? 143 GLY B C     1 
ATOM   463  O  O     . GLY A 1 64  ? 47.43122  -26.03228 6.89759   1.000 78.83063  ? 143 GLY B O     1 
ATOM   464  N  N     . CYS A 1 65  ? 46.48544  -28.05548 6.55941   1.000 74.58543  ? 144 CYS B N     1 
ATOM   465  C  CA    . CYS A 1 65  ? 47.63713  -28.58840 5.84398   1.000 66.48335  ? 144 CYS B CA    1 
ATOM   466  C  C     . CYS A 1 65  ? 47.68541  -28.13024 4.39341   1.000 76.15958  ? 144 CYS B C     1 
ATOM   467  O  O     . CYS A 1 65  ? 48.76970  -28.10388 3.80144   1.000 87.58322  ? 144 CYS B O     1 
ATOM   468  C  CB    . CYS A 1 65  ? 47.62990  -30.11793 5.89098   1.000 62.74330  ? 144 CYS B CB    1 
ATOM   469  S  SG    . CYS A 1 65  ? 47.63670  -30.81639 7.55601   1.000 80.41558  ? 144 CYS B SG    1 
ATOM   470  N  N     . LEU A 1 66  ? 46.54219  -27.76332 3.81279   1.000 71.97538  ? 145 LEU B N     1 
ATOM   471  C  CA    . LEU A 1 66  ? 46.46353  -27.37818 2.40342   1.000 72.72461  ? 145 LEU B CA    1 
ATOM   472  C  C     . LEU A 1 66  ? 46.99077  -25.95072 2.23383   1.000 78.91142  ? 145 LEU B C     1 
ATOM   473  O  O     . LEU A 1 66  ? 46.25270  -24.99609 1.98102   1.000 81.38845  ? 145 LEU B O     1 
ATOM   474  C  CB    . LEU A 1 66  ? 45.03307  -27.51710 1.90380   1.000 68.62344  ? 145 LEU B CB    1 
ATOM   475  C  CG    . LEU A 1 66  ? 44.26520  -28.72587 2.44797   1.000 68.23493  ? 145 LEU B CG    1 
ATOM   476  C  CD1   . LEU A 1 66  ? 42.82162  -28.71848 1.96499   1.000 69.30246  ? 145 LEU B CD1   1 
ATOM   477  C  CD2   . LEU A 1 66  ? 44.95033  -30.02765 2.07041   1.000 63.22324  ? 145 LEU B CD2   1 
ATOM   478  N  N     . VAL A 1 67  ? 48.31484  -25.82496 2.36886   1.000 77.48652  ? 146 VAL B N     1 
ATOM   479  C  CA    . VAL A 1 67  ? 48.97615  -24.52200 2.30333   1.000 79.96634  ? 146 VAL B CA    1 
ATOM   480  C  C     . VAL A 1 67  ? 48.79938  -23.87676 0.93454   1.000 76.20056  ? 146 VAL B C     1 
ATOM   481  O  O     . VAL A 1 67  ? 48.77550  -22.64468 0.81614   1.000 80.90848  ? 146 VAL B O     1 
ATOM   482  C  CB    . VAL A 1 67  ? 50.46887  -24.67660 2.66239   1.000 75.21540  ? 146 VAL B CB    1 
ATOM   483  C  CG1   . VAL A 1 67  ? 51.18992  -23.33679 2.58868   1.000 85.09656  ? 146 VAL B CG1   1 
ATOM   484  C  CG2   . VAL A 1 67  ? 50.62006  -25.29027 4.04346   1.000 77.28321  ? 146 VAL B CG2   1 
ATOM   485  N  N     . ASN A 1 68  ? 48.66973  -24.68284 -0.11418  1.000 75.98277  ? 147 ASN B N     1 
ATOM   486  C  CA    . ASN A 1 68  ? 48.56030  -24.16529 -1.47023  1.000 79.10902  ? 147 ASN B CA    1 
ATOM   487  C  C     . ASN A 1 68  ? 47.13701  -23.78289 -1.85215  1.000 78.99861  ? 147 ASN B C     1 
ATOM   488  O  O     . ASN A 1 68  ? 46.89179  -23.47718 -3.02321  1.000 83.20945  ? 147 ASN B O     1 
ATOM   489  C  CB    . ASN A 1 68  ? 49.10274  -25.19176 -2.46632  1.000 81.07430  ? 147 ASN B CB    1 
ATOM   490  C  CG    . ASN A 1 68  ? 50.56244  -25.50785 -2.23549  1.000 78.75921  ? 147 ASN B CG    1 
ATOM   491  O  OD1   . ASN A 1 68  ? 51.36453  -24.61854 -1.94740  1.000 84.15853  ? 147 ASN B OD1   1 
ATOM   492  N  ND2   . ASN A 1 68  ? 50.91618  -26.78200 -2.35200  1.000 87.73728  ? 147 ASN B ND2   1 
ATOM   493  N  N     . LEU A 1 69  ? 46.19930  -23.79115 -0.90992  1.000 75.23141  ? 148 LEU B N     1 
ATOM   494  C  CA    . LEU A 1 69  ? 44.81976  -23.46896 -1.24285  1.000 78.10907  ? 148 LEU B CA    1 
ATOM   495  C  C     . LEU A 1 69  ? 44.68860  -22.00692 -1.64947  1.000 83.29936  ? 148 LEU B C     1 
ATOM   496  O  O     . LEU A 1 69  ? 45.27255  -21.11330 -1.02874  1.000 80.88688  ? 148 LEU B O     1 
ATOM   497  C  CB    . LEU A 1 69  ? 43.89542  -23.76832 -0.06345  1.000 77.95810  ? 148 LEU B CB    1 
ATOM   498  C  CG    . LEU A 1 69  ? 43.13021  -25.09266 -0.10457  1.000 74.31784  ? 148 LEU B CG    1 
ATOM   499  C  CD1   . LEU A 1 69  ? 42.17750  -25.18285 1.07223   1.000 64.43446  ? 148 LEU B CD1   1 
ATOM   500  C  CD2   . LEU A 1 69  ? 42.37526  -25.24534 -1.41529  1.000 70.82697  ? 148 LEU B CD2   1 
ATOM   501  N  N     . MET A 1 70  ? 43.92183  -21.77325 -2.71532  1.000 77.67734  ? 149 MET B N     1 
ATOM   502  C  CA    . MET A 1 70  ? 43.58734  -20.43382 -3.17046  1.000 76.91639  ? 149 MET B CA    1 
ATOM   503  C  C     . MET A 1 70  ? 42.09412  -20.15895 -3.18784  1.000 72.45250  ? 149 MET B C     1 
ATOM   504  O  O     . MET A 1 70  ? 41.69992  -18.98858 -3.14434  1.000 75.12185  ? 149 MET B O     1 
ATOM   505  C  CB    . MET A 1 70  ? 44.14716  -20.18763 -4.58081  1.000 83.02463  ? 149 MET B CB    1 
ATOM   506  C  CG    . MET A 1 70  ? 45.65647  -20.03057 -4.63511  1.000 86.82370  ? 149 MET B CG    1 
ATOM   507  S  SD    . MET A 1 70  ? 46.30961  -20.15347 -6.31247  1.000 90.65234  ? 149 MET B SD    1 
ATOM   508  C  CE    . MET A 1 70  ? 45.34799  -18.90536 -7.16019  1.000 95.40231  ? 149 MET B CE    1 
ATOM   509  N  N     . THR A 1 71  ? 41.25948  -21.19299 -3.24685  1.000 72.66709  ? 150 THR B N     1 
ATOM   510  C  CA    . THR A 1 71  ? 39.81097  -21.04569 -3.27165  1.000 71.74017  ? 150 THR B CA    1 
ATOM   511  C  C     . THR A 1 71  ? 39.21279  -22.02911 -2.27951  1.000 68.33482  ? 150 THR B C     1 
ATOM   512  O  O     . THR A 1 71  ? 39.47587  -23.23305 -2.36237  1.000 69.84653  ? 150 THR B O     1 
ATOM   513  C  CB    . THR A 1 71  ? 39.25654  -21.29228 -4.67707  1.000 71.20537  ? 150 THR B CB    1 
ATOM   514  O  OG1   . THR A 1 71  ? 39.71607  -20.26036 -5.55844  1.000 79.59697  ? 150 THR B OG1   1 
ATOM   515  C  CG2   . THR A 1 71  ? 37.73647  -21.30376 -4.65912  1.000 70.14326  ? 150 THR B CG2   1 
ATOM   516  N  N     . LEU A 1 72  ? 38.42040  -21.51869 -1.34029  1.000 59.46118  ? 151 LEU B N     1 
ATOM   517  C  CA    . LEU A 1 72  ? 37.74472  -22.34598 -0.34277  1.000 58.54905  ? 151 LEU B CA    1 
ATOM   518  C  C     . LEU A 1 72  ? 36.26582  -21.96779 -0.35207  1.000 73.18127  ? 151 LEU B C     1 
ATOM   519  O  O     . LEU A 1 72  ? 35.87997  -20.91913 0.17585   1.000 61.45812  ? 151 LEU B O     1 
ATOM   520  C  CB    . LEU A 1 72  ? 38.36733  -22.16177 1.03652   1.000 63.89884  ? 151 LEU B CB    1 
ATOM   521  C  CG    . LEU A 1 72  ? 37.89040  -23.09206 2.15341   1.000 63.91523  ? 151 LEU B CG    1 
ATOM   522  C  CD1   . LEU A 1 72  ? 38.08199  -24.55030 1.76766   1.000 64.21301  ? 151 LEU B CD1   1 
ATOM   523  C  CD2   . LEU A 1 72  ? 38.63108  -22.77974 3.43977   1.000 52.45869  ? 151 LEU B CD2   1 
ATOM   524  N  N     . ALA A 1 73  ? 35.44285  -22.82272 -0.95885  1.000 73.62714  ? 152 ALA B N     1 
ATOM   525  C  CA    . ALA A 1 73  ? 34.01194  -22.57996 -1.10976  1.000 63.25305  ? 152 ALA B CA    1 
ATOM   526  C  C     . ALA A 1 73  ? 33.26221  -23.36043 -0.03593  1.000 60.07395  ? 152 ALA B C     1 
ATOM   527  O  O     . ALA A 1 73  ? 33.21808  -24.59419 -0.07269  1.000 62.07640  ? 152 ALA B O     1 
ATOM   528  C  CB    . ALA A 1 73  ? 33.54161  -22.97935 -2.50547  1.000 62.56981  ? 152 ALA B CB    1 
ATOM   529  N  N     . LEU A 1 74  ? 32.66163  -22.63808 0.91185   1.000 59.49052  ? 153 LEU B N     1 
ATOM   530  C  CA    . LEU A 1 74  ? 31.95064  -23.24331 2.03181   1.000 59.35781  ? 153 LEU B CA    1 
ATOM   531  C  C     . LEU A 1 74  ? 30.52805  -22.70611 2.14230   1.000 65.36874  ? 153 LEU B C     1 
ATOM   532  O  O     . LEU A 1 74  ? 29.94879  -22.68732 3.23153   1.000 67.53593  ? 153 LEU B O     1 
ATOM   533  C  CB    . LEU A 1 74  ? 32.70770  -23.01199 3.33905   1.000 67.66891  ? 153 LEU B CB    1 
ATOM   534  C  CG    . LEU A 1 74  ? 34.13582  -23.55751 3.39364   1.000 74.46247  ? 153 LEU B CG    1 
ATOM   535  C  CD1   . LEU A 1 74  ? 34.94311  -22.86955 4.48939   1.000 56.72176  ? 153 LEU B CD1   1 
ATOM   536  C  CD2   . LEU A 1 74  ? 34.11634  -25.06539 3.59845   1.000 63.14243  ? 153 LEU B CD2   1 
ATOM   537  N  N     . SER A 1 75  ? 29.95060  -22.26428 1.02965   1.000 69.92164  ? 154 SER B N     1 
ATOM   538  C  CA    . SER A 1 75  ? 28.61432  -21.69041 1.06857   1.000 68.33924  ? 154 SER B CA    1 
ATOM   539  C  C     . SER A 1 75  ? 27.56117  -22.76973 1.30305   1.000 77.61316  ? 154 SER B C     1 
ATOM   540  O  O     . SER A 1 75  ? 27.74369  -23.93832 0.95267   1.000 68.45477  ? 154 SER B O     1 
ATOM   541  C  CB    . SER A 1 75  ? 28.31939  -20.93717 -0.22749  1.000 62.40984  ? 154 SER B CB    1 
ATOM   542  O  OG    . SER A 1 75  ? 28.77097  -21.66841 -1.35158  1.000 76.91868  ? 154 SER B OG    1 
ATOM   543  N  N     . GLU A 1 76  ? 26.44917  -22.35918 1.90976   1.000 79.29395  ? 155 GLU B N     1 
ATOM   544  C  CA    . GLU A 1 76  ? 25.32858  -23.24156 2.23321   1.000 74.43089  ? 155 GLU B CA    1 
ATOM   545  C  C     . GLU A 1 76  ? 25.80158  -24.45329 3.04263   1.000 68.27177  ? 155 GLU B C     1 
ATOM   546  O  O     . GLU A 1 76  ? 25.86071  -25.58820 2.57006   1.000 70.09318  ? 155 GLU B O     1 
ATOM   547  C  CB    . GLU A 1 76  ? 24.57763  -23.65242 0.96156   1.000 73.46090  ? 155 GLU B CB    1 
ATOM   548  C  CG    . GLU A 1 76  ? 23.52214  -22.63209 0.54392   1.000 82.48869  ? 155 GLU B CG    1 
ATOM   549  C  CD    . GLU A 1 76  ? 23.05512  -22.79485 -0.89209  1.000 96.54525  ? 155 GLU B CD    1 
ATOM   550  O  OE1   . GLU A 1 76  ? 22.81549  -23.94291 -1.32362  1.000 93.82029  ? 155 GLU B OE1   1 
ATOM   551  O  OE2   . GLU A 1 76  ? 22.92888  -21.76570 -1.59089  1.000 98.80039  ? 155 GLU B OE2   1 
ATOM   552  N  N     . ASN A 1 77  ? 26.14975  -24.15824 4.28914   1.000 62.11485  ? 156 ASN B N     1 
ATOM   553  C  CA    . ASN A 1 77  ? 26.47329  -25.17259 5.28713   1.000 64.74584  ? 156 ASN B CA    1 
ATOM   554  C  C     . ASN A 1 77  ? 25.84691  -24.72406 6.60277   1.000 67.07923  ? 156 ASN B C     1 
ATOM   555  O  O     . ASN A 1 77  ? 24.90067  -23.92919 6.62804   1.000 84.59938  ? 156 ASN B O     1 
ATOM   556  C  CB    . ASN A 1 77  ? 27.99252  -25.38320 5.39744   1.000 70.31428  ? 156 ASN B CB    1 
ATOM   557  C  CG    . ASN A 1 77  ? 28.55238  -26.22206 4.26753   1.000 62.80323  ? 156 ASN B CG    1 
ATOM   558  O  OD1   . ASN A 1 77  ? 28.44110  -27.44476 4.27834   1.000 69.18741  ? 156 ASN B OD1   1 
ATOM   559  N  ND2   . ASN A 1 77  ? 29.16934  -25.56887 3.29101   1.000 68.01290  ? 156 ASN B ND2   1 
ATOM   560  N  N     . SER A 1 78  ? 26.37700  -25.22611 7.71469   1.000 71.09089  ? 157 SER B N     1 
ATOM   561  C  CA    . SER A 1 78  ? 25.92695  -24.82123 9.04233   1.000 74.87301  ? 157 SER B CA    1 
ATOM   562  C  C     . SER A 1 78  ? 27.12475  -24.57335 9.94733   1.000 82.60440  ? 157 SER B C     1 
ATOM   563  O  O     . SER A 1 78  ? 27.10888  -24.90466 11.13758  1.000 79.05747  ? 157 SER B O     1 
ATOM   564  C  CB    . SER A 1 78  ? 24.98986  -25.86396 9.65073   1.000 73.03504  ? 157 SER B CB    1 
ATOM   565  O  OG    . SER A 1 78  ? 23.81394  -26.00360 8.87031   1.000 80.36498  ? 157 SER B OG    1 
ATOM   566  N  N     . LEU A 1 79  ? 28.17962  -23.98356 9.38928   1.000 83.11312  ? 158 LEU B N     1 
ATOM   567  C  CA    . LEU A 1 79  ? 29.38924  -23.71723 10.15400  1.000 74.56848  ? 158 LEU B CA    1 
ATOM   568  C  C     . LEU A 1 79  ? 29.15614  -22.60397 11.16658  1.000 73.90199  ? 158 LEU B C     1 
ATOM   569  O  O     . LEU A 1 79  ? 28.45952  -21.62375 10.89015  1.000 79.40820  ? 158 LEU B O     1 
ATOM   570  C  CB    . LEU A 1 79  ? 30.53580  -23.33122 9.21857   1.000 69.30249  ? 158 LEU B CB    1 
ATOM   571  C  CG    . LEU A 1 79  ? 31.02838  -24.38208 8.22349   1.000 64.47491  ? 158 LEU B CG    1 
ATOM   572  C  CD1   . LEU A 1 79  ? 32.04801  -23.78118 7.27054   1.000 64.59202  ? 158 LEU B CD1   1 
ATOM   573  C  CD2   . LEU A 1 79  ? 31.61877  -25.56849 8.95609   1.000 67.18090  ? 158 LEU B CD2   1 
ATOM   574  N  N     . THR A 1 80  ? 29.74643  -22.76270 12.35162  1.000 72.12396  ? 159 THR B N     1 
ATOM   575  C  CA    . THR A 1 80  ? 29.74412  -21.71531 13.36076  1.000 75.21305  ? 159 THR B CA    1 
ATOM   576  C  C     . THR A 1 80  ? 31.12142  -21.12362 13.61285  1.000 78.01923  ? 159 THR B C     1 
ATOM   577  O  O     . THR A 1 80  ? 31.21162  -20.04664 14.21000  1.000 79.10218  ? 159 THR B O     1 
ATOM   578  C  CB    . THR A 1 80  ? 29.18171  -22.24399 14.68865  1.000 79.94283  ? 159 THR B CB    1 
ATOM   579  O  OG1   . THR A 1 80  ? 29.98880  -23.33433 15.15270  1.000 86.50563  ? 159 THR B OG1   1 
ATOM   580  C  CG2   . THR A 1 80  ? 27.74913  -22.71623 14.50697  1.000 63.16397  ? 159 THR B CG2   1 
ATOM   581  N  N     . SER A 1 81  ? 32.18425  -21.79256 13.17589  1.000 71.47538  ? 160 SER B N     1 
ATOM   582  C  CA    . SER A 1 81  ? 33.53665  -21.26516 13.29361  1.000 74.31236  ? 160 SER B CA    1 
ATOM   583  C  C     . SER A 1 81  ? 34.42448  -21.98883 12.28969  1.000 74.88048  ? 160 SER B C     1 
ATOM   584  O  O     . SER A 1 81  ? 33.97634  -22.87455 11.55604  1.000 75.03359  ? 160 SER B O     1 
ATOM   585  C  CB    . SER A 1 81  ? 34.07339  -21.41344 14.71883  1.000 88.86391  ? 160 SER B CB    1 
ATOM   586  O  OG    . SER A 1 81  ? 35.36714  -20.84496 14.82779  1.000 88.88474  ? 160 SER B OG    1 
ATOM   587  N  N     . LEU A 1 82  ? 35.69414  -21.59870 12.26365  1.000 76.53994  ? 161 LEU B N     1 
ATOM   588  C  CA    . LEU A 1 82  ? 36.69735  -22.18411 11.39072  1.000 74.48880  ? 161 LEU B CA    1 
ATOM   589  C  C     . LEU A 1 82  ? 37.94171  -22.52136 12.19710  1.000 70.67394  ? 161 LEU B C     1 
ATOM   590  O  O     . LEU A 1 82  ? 38.24118  -21.85242 13.19218  1.000 67.53196  ? 161 LEU B O     1 
ATOM   591  C  CB    . LEU A 1 82  ? 37.06242  -21.22776 10.24485  1.000 68.79563  ? 161 LEU B CB    1 
ATOM   592  C  CG    . LEU A 1 82  ? 35.95547  -20.96289 9.22252   1.000 70.20389  ? 161 LEU B CG    1 
ATOM   593  C  CD1   . LEU A 1 82  ? 36.36967  -19.87497 8.24489   1.000 70.50307  ? 161 LEU B CD1   1 
ATOM   594  C  CD2   . LEU A 1 82  ? 35.59699  -22.24303 8.48388   1.000 66.16326  ? 161 LEU B CD2   1 
ATOM   595  N  N     . PRO A 1 83  ? 38.68196  -23.55535 11.79506  1.000 71.54598  ? 162 PRO B N     1 
ATOM   596  C  CA    . PRO A 1 83  ? 39.84243  -23.98060 12.58771  1.000 53.86152  ? 162 PRO B CA    1 
ATOM   597  C  C     . PRO A 1 83  ? 40.93550  -22.92585 12.59293  1.000 65.40188  ? 162 PRO B C     1 
ATOM   598  O  O     . PRO A 1 83  ? 41.28356  -22.35841 11.55552  1.000 71.92035  ? 162 PRO B O     1 
ATOM   599  C  CB    . PRO A 1 83  ? 40.31240  -25.25776 11.87970  1.000 62.57966  ? 162 PRO B CB    1 
ATOM   600  C  CG    . PRO A 1 83  ? 39.17258  -25.67854 11.02035  1.000 66.33261  ? 162 PRO B CG    1 
ATOM   601  C  CD    . PRO A 1 83  ? 38.46769  -24.42341 10.62687  1.000 70.49227  ? 162 PRO B CD    1 
ATOM   602  N  N     . ASP A 1 84  ? 41.48884  -22.67579 13.78046  1.000 74.73228  ? 163 ASP B N     1 
ATOM   603  C  CA    . ASP A 1 84  ? 42.58689  -21.72650 13.90736  1.000 73.44221  ? 163 ASP B CA    1 
ATOM   604  C  C     . ASP A 1 84  ? 43.82833  -22.16264 13.14380  1.000 77.80446  ? 163 ASP B C     1 
ATOM   605  O  O     . ASP A 1 84  ? 44.75985  -21.36339 13.00367  1.000 85.93012  ? 163 ASP B O     1 
ATOM   606  C  CB    . ASP A 1 84  ? 42.92499  -21.51882 15.38351  1.000 82.65394  ? 163 ASP B CB    1 
ATOM   607  C  CG    . ASP A 1 84  ? 41.86448  -20.71683 16.11417  1.000 94.65077  ? 163 ASP B CG    1 
ATOM   608  O  OD1   . ASP A 1 84  ? 41.66182  -19.53493 15.75914  1.000 87.84595  ? 163 ASP B OD1   1 
ATOM   609  O  OD2   . ASP A 1 84  ? 41.22256  -21.27284 17.03159  1.000 93.28044  ? 163 ASP B OD2   1 
ATOM   610  N  N     . SER A 1 85  ? 43.86244  -23.39788 12.64565  1.000 78.84957  ? 164 SER B N     1 
ATOM   611  C  CA    . SER A 1 85  ? 44.97903  -23.89350 11.85341  1.000 71.69058  ? 164 SER B CA    1 
ATOM   612  C  C     . SER A 1 85  ? 44.97692  -23.36832 10.42383  1.000 76.71166  ? 164 SER B C     1 
ATOM   613  O  O     . SER A 1 85  ? 45.82773  -23.78578 9.63114   1.000 76.66910  ? 164 SER B O     1 
ATOM   614  C  CB    . SER A 1 85  ? 44.96447  -25.42421 11.83027  1.000 78.71384  ? 164 SER B CB    1 
ATOM   615  O  OG    . SER A 1 85  ? 43.81627  -25.91226 11.15295  1.000 74.79197  ? 164 SER B OG    1 
ATOM   616  N  N     . LEU A 1 86  ? 44.05314  -22.47493 10.07067  1.000 77.49515  ? 165 LEU B N     1 
ATOM   617  C  CA    . LEU A 1 86  ? 43.97418  -21.97255 8.70546   1.000 63.76653  ? 165 LEU B CA    1 
ATOM   618  C  C     . LEU A 1 86  ? 44.93184  -20.81880 8.43157   1.000 75.25064  ? 165 LEU B C     1 
ATOM   619  O  O     . LEU A 1 86  ? 44.96767  -20.33475 7.29523   1.000 72.92919  ? 165 LEU B O     1 
ATOM   620  C  CB    . LEU A 1 86  ? 42.54042  -21.54406 8.37742   1.000 69.39232  ? 165 LEU B CB    1 
ATOM   621  C  CG    . LEU A 1 86  ? 41.47754  -22.64435 8.28969   1.000 68.30486  ? 165 LEU B CG    1 
ATOM   622  C  CD1   . LEU A 1 86  ? 40.21958  -22.12902 7.60387   1.000 55.92612  ? 165 LEU B CD1   1 
ATOM   623  C  CD2   . LEU A 1 86  ? 42.01714  -23.86483 7.56736   1.000 76.46383  ? 165 LEU B CD2   1 
ATOM   624  N  N     . ASP A 1 87  ? 45.70277  -20.36711 9.43015   1.000 81.19557  ? 166 ASP B N     1 
ATOM   625  C  CA    . ASP A 1 87  ? 46.76108  -19.39445 9.16402   1.000 71.60421  ? 166 ASP B CA    1 
ATOM   626  C  C     . ASP A 1 87  ? 47.74947  -19.92195 8.13675   1.000 77.00680  ? 166 ASP B C     1 
ATOM   627  O  O     . ASP A 1 87  ? 48.30573  -19.14614 7.35071   1.000 75.09631  ? 166 ASP B O     1 
ATOM   628  C  CB    . ASP A 1 87  ? 47.52080  -19.04522 10.44453  1.000 77.73408  ? 166 ASP B CB    1 
ATOM   629  C  CG    . ASP A 1 87  ? 46.67250  -19.17331 11.68110  1.000 86.00974  ? 166 ASP B CG    1 
ATOM   630  O  OD1   . ASP A 1 87  ? 45.46366  -18.87847 11.60250  1.000 97.96150  ? 166 ASP B OD1   1 
ATOM   631  O  OD2   . ASP A 1 87  ? 47.21786  -19.56985 12.73263  1.000 70.34305  ? 166 ASP B OD2   1 
ATOM   632  N  N     . ASN A 1 88  ? 47.98700  -21.23539 8.13711   1.000 70.76495  ? 167 ASN B N     1 
ATOM   633  C  CA    . ASN A 1 88  ? 48.92691  -21.84810 7.20985   1.000 68.29868  ? 167 ASN B CA    1 
ATOM   634  C  C     . ASN A 1 88  ? 48.49021  -21.71808 5.75596   1.000 73.91061  ? 167 ASN B C     1 
ATOM   635  O  O     . ASN A 1 88  ? 49.28741  -22.01423 4.85991   1.000 86.32057  ? 167 ASN B O     1 
ATOM   636  C  CB    . ASN A 1 88  ? 49.12154  -23.32107 7.58044   1.000 75.25295  ? 167 ASN B CB    1 
ATOM   637  C  CG    . ASN A 1 88  ? 49.71247  -23.50121 8.97518   1.000 86.50700  ? 167 ASN B CG    1 
ATOM   638  O  OD1   . ASN A 1 88  ? 50.92261  -23.68540 9.13202   1.000 73.96080  ? 167 ASN B OD1   1 
ATOM   639  N  ND2   . ASN A 1 88  ? 48.85800  -23.44673 9.99407   1.000 74.65728  ? 167 ASN B ND2   1 
ATOM   640  N  N     . LEU A 1 89  ? 47.25736  -21.28235 5.49795   1.000 80.42971  ? 168 LEU B N     1 
ATOM   641  C  CA    . LEU A 1 89  ? 46.79104  -21.02920 4.13446   1.000 69.87783  ? 168 LEU B CA    1 
ATOM   642  C  C     . LEU A 1 89  ? 47.16722  -19.60044 3.73807   1.000 75.15938  ? 168 LEU B C     1 
ATOM   643  O  O     . LEU A 1 89  ? 46.32639  -18.72466 3.52961   1.000 71.09398  ? 168 LEU B O     1 
ATOM   644  C  CB    . LEU A 1 89  ? 45.28989  -21.27008 4.03043   1.000 70.05857  ? 168 LEU B CB    1 
ATOM   645  C  CG    . LEU A 1 89  ? 44.77413  -22.69621 3.80630   1.000 68.00895  ? 168 LEU B CG    1 
ATOM   646  C  CD1   . LEU A 1 89  ? 45.15139  -23.63395 4.94257   1.000 69.35550  ? 168 LEU B CD1   1 
ATOM   647  C  CD2   . LEU A 1 89  ? 43.26563  -22.68219 3.60786   1.000 65.03645  ? 168 LEU B CD2   1 
ATOM   648  N  N     . LYS A 1 90  ? 48.47624  -19.37500 3.63944   1.000 75.13568  ? 169 LYS B N     1 
ATOM   649  C  CA    . LYS A 1 90  ? 48.99508  -18.04033 3.36802   1.000 74.84882  ? 169 LYS B CA    1 
ATOM   650  C  C     . LYS A 1 90  ? 48.83956  -17.61741 1.91269   1.000 73.47443  ? 169 LYS B C     1 
ATOM   651  O  O     . LYS A 1 90  ? 49.30323  -16.53042 1.55038   1.000 65.78322  ? 169 LYS B O     1 
ATOM   652  C  CB    . LYS A 1 90  ? 50.46851  -17.95328 3.77930   1.000 71.12473  ? 169 LYS B CB    1 
ATOM   653  C  CG    . LYS A 1 90  ? 50.68563  -17.76137 5.27660   1.000 62.41827  ? 169 LYS B CG    1 
ATOM   654  C  CD    . LYS A 1 90  ? 51.43242  -18.93345 5.88806   1.000 69.52884  ? 169 LYS B CD    1 
ATOM   655  C  CE    . LYS A 1 90  ? 51.58919  -18.76944 7.39524   1.000 82.21483  ? 169 LYS B CE    1 
ATOM   656  N  NZ    . LYS A 1 90  ? 52.40775  -17.57958 7.76151   1.000 78.15703  ? 169 LYS B NZ    1 
ATOM   657  N  N     . LYS A 1 91  ? 48.19643  -18.43266 1.07498   1.000 75.74090  ? 170 LYS B N     1 
ATOM   658  C  CA    . LYS A 1 91  ? 47.97637  -18.09218 -0.32583  1.000 76.58349  ? 170 LYS B CA    1 
ATOM   659  C  C     . LYS A 1 91  ? 46.49831  -18.13869 -0.70233  1.000 83.70507  ? 170 LYS B C     1 
ATOM   660  O  O     . LYS A 1 91  ? 46.16668  -18.23052 -1.88861  1.000 89.58964  ? 170 LYS B O     1 
ATOM   661  C  CB    . LYS A 1 91  ? 48.79180  -19.01730 -1.23288  1.000 86.35510  ? 170 LYS B CB    1 
ATOM   662  C  CG    . LYS A 1 91  ? 50.29373  -18.97222 -0.96710  1.000 84.96283  ? 170 LYS B CG    1 
ATOM   663  C  CD    . LYS A 1 91  ? 51.08497  -19.73992 -2.01769  1.000 93.05961  ? 170 LYS B CD    1 
ATOM   664  C  CE    . LYS A 1 91  ? 50.68964  -21.20812 -2.05862  1.000 94.02318  ? 170 LYS B CE    1 
ATOM   665  N  NZ    . LYS A 1 91  ? 51.51946  -21.98526 -3.02470  1.000 96.30377  ? 170 LYS B NZ    1 
ATOM   666  N  N     . LEU A 1 92  ? 45.60354  -18.06519 0.28158   1.000 79.13660  ? 171 LEU B N     1 
ATOM   667  C  CA    . LEU A 1 92  ? 44.17143  -18.13435 0.02212   1.000 72.92741  ? 171 LEU B CA    1 
ATOM   668  C  C     . LEU A 1 92  ? 43.66278  -16.79141 -0.49138  1.000 77.11670  ? 171 LEU B C     1 
ATOM   669  O  O     . LEU A 1 92  ? 43.97380  -15.74141 0.08102   1.000 68.37505  ? 171 LEU B O     1 
ATOM   670  C  CB    . LEU A 1 92  ? 43.42424  -18.53623 1.29306   1.000 68.10470  ? 171 LEU B CB    1 
ATOM   671  C  CG    . LEU A 1 92  ? 41.94795  -18.89682 1.12975   1.000 70.87083  ? 171 LEU B CG    1 
ATOM   672  C  CD1   . LEU A 1 92  ? 41.79883  -20.18809 0.33848   1.000 67.44205  ? 171 LEU B CD1   1 
ATOM   673  C  CD2   . LEU A 1 92  ? 41.27602  -19.00848 2.48522   1.000 59.14326  ? 171 LEU B CD2   1 
ATOM   674  N  N     . ARG A 1 93  ? 42.86944  -16.82819 -1.56464  1.000 70.14384  ? 172 ARG B N     1 
ATOM   675  C  CA    . ARG A 1 93  ? 42.39513  -15.62450 -2.24058  1.000 69.97491  ? 172 ARG B CA    1 
ATOM   676  C  C     . ARG A 1 93  ? 40.91520  -15.34635 -2.02142  1.000 68.84064  ? 172 ARG B C     1 
ATOM   677  O  O     . ARG A 1 93  ? 40.55043  -14.22831 -1.64333  1.000 66.17764  ? 172 ARG B O     1 
ATOM   678  C  CB    . ARG A 1 93  ? 42.68224  -15.71848 -3.74537  1.000 66.70978  ? 172 ARG B CB    1 
ATOM   679  C  CG    . ARG A 1 93  ? 44.14768  -15.56006 -4.10554  1.000 82.84556  ? 172 ARG B CG    1 
ATOM   680  C  CD    . ARG A 1 93  ? 44.38555  -15.85813 -5.57648  1.000 91.66859  ? 172 ARG B CD    1 
ATOM   681  N  NE    . ARG A 1 93  ? 45.80138  -15.79934 -5.92054  1.000 110.67709 ? 172 ARG B NE    1 
ATOM   682  C  CZ    . ARG A 1 93  ? 46.37748  -14.78727 -6.55482  1.000 117.16663 ? 172 ARG B CZ    1 
ATOM   683  N  NH1   . ARG A 1 93  ? 45.68025  -13.73710 -6.95725  1.000 116.63173 ? 172 ARG B NH1   1 
ATOM   684  N  NH2   . ARG A 1 93  ? 47.68525  -14.83160 -6.79487  1.000 113.00668 ? 172 ARG B NH2   1 
ATOM   685  N  N     . MET A 1 94  ? 40.04198  -16.32126 -2.26253  1.000 50.50910  ? 173 MET B N     1 
ATOM   686  C  CA    . MET A 1 94  ? 38.61233  -16.13406 -2.06887  1.000 61.91997  ? 173 MET B CA    1 
ATOM   687  C  C     . MET A 1 94  ? 38.10177  -17.10819 -1.01576  1.000 67.33430  ? 173 MET B C     1 
ATOM   688  O  O     . MET A 1 94  ? 38.49272  -18.28088 -0.98961  1.000 55.35884  ? 173 MET B O     1 
ATOM   689  C  CB    . MET A 1 94  ? 37.83355  -16.29401 -3.39242  1.000 74.28031  ? 173 MET B CB    1 
ATOM   690  C  CG    . MET A 1 94  ? 37.46769  -17.71767 -3.79327  1.000 82.53283  ? 173 MET B CG    1 
ATOM   691  S  SD    . MET A 1 94  ? 35.86558  -18.25163 -3.14319  1.000 78.05818  ? 173 MET B SD    1 
ATOM   692  C  CE    . MET A 1 94  ? 34.80379  -16.94864 -3.75163  1.000 75.08423  ? 173 MET B CE    1 
ATOM   693  N  N     . LEU A 1 95  ? 37.23467  -16.60342 -0.13993  1.000 67.78116  ? 174 LEU B N     1 
ATOM   694  C  CA    . LEU A 1 95  ? 36.64587  -17.38060 0.94510   1.000 62.13878  ? 174 LEU B CA    1 
ATOM   695  C  C     . LEU A 1 95  ? 35.14005  -17.16868 0.90697   1.000 66.94150  ? 174 LEU B C     1 
ATOM   696  O  O     . LEU A 1 95  ? 34.65428  -16.08257 1.24162   1.000 61.33076  ? 174 LEU B O     1 
ATOM   697  C  CB    . LEU A 1 95  ? 37.22310  -16.96481 2.29753   1.000 57.60628  ? 174 LEU B CB    1 
ATOM   698  C  CG    . LEU A 1 95  ? 36.75810  -17.76890 3.50974   1.000 59.41883  ? 174 LEU B CG    1 
ATOM   699  C  CD1   . LEU A 1 95  ? 37.05437  -19.24407 3.30591   1.000 65.12185  ? 174 LEU B CD1   1 
ATOM   700  C  CD2   . LEU A 1 95  ? 37.42978  -17.25866 4.77179   1.000 52.95420  ? 174 LEU B CD2   1 
ATOM   701  N  N     . ASP A 1 96  ? 34.40640  -18.19802 0.49138   1.000 66.98200  ? 175 ASP B N     1 
ATOM   702  C  CA    . ASP A 1 96  ? 32.95470  -18.13529 0.36738   1.000 54.67753  ? 175 ASP B CA    1 
ATOM   703  C  C     . ASP A 1 96  ? 32.33869  -18.81657 1.58425   1.000 60.91748  ? 175 ASP B C     1 
ATOM   704  O  O     . ASP A 1 96  ? 32.36946  -20.04630 1.69845   1.000 59.82653  ? 175 ASP B O     1 
ATOM   705  C  CB    . ASP A 1 96  ? 32.49533  -18.79406 -0.93110  1.000 58.95168  ? 175 ASP B CB    1 
ATOM   706  C  CG    . ASP A 1 96  ? 31.00901  -18.61875 -1.18287  1.000 76.82240  ? 175 ASP B CG    1 
ATOM   707  O  OD1   . ASP A 1 96  ? 30.34708  -17.91663 -0.39011  1.000 66.36692  ? 175 ASP B OD1   1 
ATOM   708  O  OD2   . ASP A 1 96  ? 30.50131  -19.18449 -2.17615  1.000 87.32442  ? 175 ASP B OD2   1 
ATOM   709  N  N     . LEU A 1 97  ? 31.78293  -18.01337 2.49392   1.000 64.03842  ? 176 LEU B N     1 
ATOM   710  C  CA    . LEU A 1 97  ? 31.14457  -18.51513 3.70631   1.000 58.17451  ? 176 LEU B CA    1 
ATOM   711  C  C     . LEU A 1 97  ? 29.68100  -18.10375 3.79762   1.000 66.87093  ? 176 LEU B C     1 
ATOM   712  O  O     . LEU A 1 97  ? 29.11126  -18.09985 4.89346   1.000 68.49111  ? 176 LEU B O     1 
ATOM   713  C  CB    . LEU A 1 97  ? 31.89171  -18.02981 4.94858   1.000 52.30512  ? 176 LEU B CB    1 
ATOM   714  C  CG    . LEU A 1 97  ? 33.22049  -18.69559 5.29148   1.000 63.77911  ? 176 LEU B CG    1 
ATOM   715  C  CD1   . LEU A 1 97  ? 34.01631  -17.80528 6.22778   1.000 64.93125  ? 176 LEU B CD1   1 
ATOM   716  C  CD2   . LEU A 1 97  ? 32.97503  -20.05475 5.92431   1.000 74.50493  ? 176 LEU B CD2   1 
ATOM   717  N  N     . ARG A 1 98  ? 29.05837  -17.75057 2.67860   1.000 62.53403  ? 177 ARG B N     1 
ATOM   718  C  CA    . ARG A 1 98  ? 27.70211  -17.24026 2.75860   1.000 68.91550  ? 177 ARG B CA    1 
ATOM   719  C  C     . ARG A 1 98  ? 26.70571  -18.38130 2.94343   1.000 69.41851  ? 177 ARG B C     1 
ATOM   720  O  O     . ARG A 1 98  ? 26.98639  -19.54342 2.64122   1.000 67.60483  ? 177 ARG B O     1 
ATOM   721  C  CB    . ARG A 1 98  ? 27.35846  -16.41574 1.51894   1.000 65.86596  ? 177 ARG B CB    1 
ATOM   722  C  CG    . ARG A 1 98  ? 27.36237  -17.20191 0.24607   1.000 69.79518  ? 177 ARG B CG    1 
ATOM   723  C  CD    . ARG A 1 98  ? 27.58864  -16.30516 -0.94632  1.000 54.53274  ? 177 ARG B CD    1 
ATOM   724  N  NE    . ARG A 1 98  ? 28.26216  -17.05696 -1.99364  1.000 70.16146  ? 177 ARG B NE    1 
ATOM   725  C  CZ    . ARG A 1 98  ? 27.64004  -17.73671 -2.94469  1.000 60.27932  ? 177 ARG B CZ    1 
ATOM   726  N  NH1   . ARG A 1 98  ? 26.32437  -17.70414 -3.06850  1.000 61.89046  ? 177 ARG B NH1   1 
ATOM   727  N  NH2   . ARG A 1 98  ? 28.35707  -18.47042 -3.78951  1.000 81.15070  ? 177 ARG B NH2   1 
ATOM   728  N  N     . HIS A 1 99  ? 25.52697  -18.02592 3.45803   1.000 75.16154  ? 178 HIS B N     1 
ATOM   729  C  CA    . HIS A 1 99  ? 24.48451  -18.98404 3.82682   1.000 70.35846  ? 178 HIS B CA    1 
ATOM   730  C  C     . HIS A 1 99  ? 25.01877  -20.01823 4.82056   1.000 63.27111  ? 178 HIS B C     1 
ATOM   731  O  O     . HIS A 1 99  ? 25.02366  -21.22277 4.56823   1.000 67.74593  ? 178 HIS B O     1 
ATOM   732  C  CB    . HIS A 1 99  ? 23.88502  -19.66298 2.58921   1.000 67.08239  ? 178 HIS B CB    1 
ATOM   733  C  CG    . HIS A 1 99  ? 22.99941  -18.76971 1.77715   1.000 74.90193  ? 178 HIS B CG    1 
ATOM   734  N  ND1   . HIS A 1 99  ? 23.33877  -18.33013 0.51521   1.000 75.96592  ? 178 HIS B ND1   1 
ATOM   735  C  CD2   . HIS A 1 99  ? 21.78612  -18.23360 2.04816   1.000 60.07622  ? 178 HIS B CD2   1 
ATOM   736  C  CE1   . HIS A 1 99  ? 22.37274  -17.56202 0.04393   1.000 70.83876  ? 178 HIS B CE1   1 
ATOM   737  N  NE2   . HIS A 1 99  ? 21.41844  -17.48807 0.95435   1.000 72.01294  ? 178 HIS B NE2   1 
ATOM   738  N  N     . ASN A 1 100 ? 25.46976  -19.51811 5.97034   1.000 66.92441  ? 179 ASN B N     1 
ATOM   739  C  CA    . ASN A 1 100 ? 25.89427  -20.38416 7.06464   1.000 70.45803  ? 179 ASN B CA    1 
ATOM   740  C  C     . ASN A 1 100 ? 25.23967  -19.95838 8.37309   1.000 76.54172  ? 179 ASN B C     1 
ATOM   741  O  O     . ASN A 1 100 ? 24.14858  -19.37739 8.36994   1.000 73.97157  ? 179 ASN B O     1 
ATOM   742  C  CB    . ASN A 1 100 ? 27.41884  -20.37671 7.20736   1.000 70.30448  ? 179 ASN B CB    1 
ATOM   743  C  CG    . ASN A 1 100 ? 28.09507  -21.39406 6.31036   1.000 63.29960  ? 179 ASN B CG    1 
ATOM   744  O  OD1   . ASN A 1 100 ? 28.39102  -22.51046 6.73427   1.000 65.10319  ? 179 ASN B OD1   1 
ATOM   745  N  ND2   . ASN A 1 100 ? 28.34473  -21.01272 5.06382   1.000 67.05139  ? 179 ASN B ND2   1 
ATOM   746  N  N     . LYS A 1 101 ? 25.90014  -20.24092 9.49717   1.000 73.79436  ? 180 LYS B N     1 
ATOM   747  C  CA    . LYS A 1 101 ? 25.37699  -19.91641 10.81915  1.000 75.62246  ? 180 LYS B CA    1 
ATOM   748  C  C     . LYS A 1 101 ? 26.49933  -19.34891 11.69145  1.000 77.04708  ? 180 LYS B C     1 
ATOM   749  O  O     . LYS A 1 101 ? 26.85759  -19.89082 12.73264  1.000 90.59017  ? 180 LYS B O     1 
ATOM   750  C  CB    . LYS A 1 101 ? 24.73846  -21.14235 11.47077  1.000 86.22681  ? 180 LYS B CB    1 
ATOM   751  C  CG    . LYS A 1 101 ? 23.44943  -21.61252 10.80928  1.000 89.12615  ? 180 LYS B CG    1 
ATOM   752  C  CD    . LYS A 1 101 ? 22.84696  -22.79319 11.55828  1.000 93.07666  ? 180 LYS B CD    1 
ATOM   753  C  CE    . LYS A 1 101 ? 21.50404  -23.20421 10.97115  1.000 91.94299  ? 180 LYS B CE    1 
ATOM   754  N  NZ    . LYS A 1 101 ? 21.63058  -23.73327 9.58565   1.000 87.36205  ? 180 LYS B NZ    1 
ATOM   755  N  N     . LEU A 1 102 ? 27.06649  -18.22656 11.26098  1.000 73.92258  ? 181 LEU B N     1 
ATOM   756  C  CA    . LEU A 1 102 ? 28.13697  -17.55791 11.98819  1.000 68.44743  ? 181 LEU B CA    1 
ATOM   757  C  C     . LEU A 1 102 ? 27.56491  -16.38657 12.77390  1.000 75.35400  ? 181 LEU B C     1 
ATOM   758  O  O     . LEU A 1 102 ? 26.83944  -15.55888 12.21526  1.000 76.84588  ? 181 LEU B O     1 
ATOM   759  C  CB    . LEU A 1 102 ? 29.21859  -17.06035 11.02853  1.000 61.96708  ? 181 LEU B CB    1 
ATOM   760  C  CG    . LEU A 1 102 ? 29.88028  -18.07665 10.09764  1.000 65.36713  ? 181 LEU B CG    1 
ATOM   761  C  CD1   . LEU A 1 102 ? 30.64930  -17.35766 9.00217   1.000 63.79761  ? 181 LEU B CD1   1 
ATOM   762  C  CD2   . LEU A 1 102 ? 30.80278  -19.00239 10.87301  1.000 65.82486  ? 181 LEU B CD2   1 
ATOM   763  N  N     . ARG A 1 103 ? 27.88993  -16.31675 14.06535  1.000 68.65144  ? 182 ARG B N     1 
ATOM   764  C  CA    . ARG A 1 103 ? 27.50227  -15.16577 14.87278  1.000 75.24951  ? 182 ARG B CA    1 
ATOM   765  C  C     . ARG A 1 103 ? 28.54572  -14.05877 14.85392  1.000 82.01153  ? 182 ARG B C     1 
ATOM   766  O  O     . ARG A 1 103 ? 28.24631  -12.93054 15.26310  1.000 84.48709  ? 182 ARG B O     1 
ATOM   767  C  CB    . ARG A 1 103 ? 27.23571  -15.58074 16.32342  1.000 81.25392  ? 182 ARG B CB    1 
ATOM   768  C  CG    . ARG A 1 103 ? 27.53759  -17.03393 16.63423  1.000 100.33581 ? 182 ARG B CG    1 
ATOM   769  C  CD    . ARG A 1 103 ? 26.32512  -17.92476 16.40406  1.000 95.64602  ? 182 ARG B CD    1 
ATOM   770  N  NE    . ARG A 1 103 ? 26.68182  -19.33667 16.48416  1.000 115.34476 ? 182 ARG B NE    1 
ATOM   771  C  CZ    . ARG A 1 103 ? 26.74571  -20.02422 17.61557  1.000 106.17620 ? 182 ARG B CZ    1 
ATOM   772  N  NH1   . ARG A 1 103 ? 26.47353  -19.46017 18.78070  1.000 107.41469 ? 182 ARG B NH1   1 
ATOM   773  N  NH2   . ARG A 1 103 ? 27.09170  -21.30822 17.57726  1.000 105.10667 ? 182 ARG B NH2   1 
ATOM   774  N  N     . GLU A 1 104 ? 29.75889  -14.35744 14.40158  1.000 81.85844  ? 183 GLU B N     1 
ATOM   775  C  CA    . GLU A 1 104 ? 30.77751  -13.34070 14.19714  1.000 79.12813  ? 183 GLU B CA    1 
ATOM   776  C  C     . GLU A 1 104 ? 31.77671  -13.88386 13.19143  1.000 68.45825  ? 183 GLU B C     1 
ATOM   777  O  O     . GLU A 1 104 ? 31.80821  -15.08422 12.91027  1.000 69.28495  ? 183 GLU B O     1 
ATOM   778  C  CB    . GLU A 1 104 ? 31.47069  -12.94972 15.50973  1.000 86.07093  ? 183 GLU B CB    1 
ATOM   779  C  CG    . GLU A 1 104 ? 32.65232  -13.82980 15.90569  1.000 92.02248  ? 183 GLU B CG    1 
ATOM   780  C  CD    . GLU A 1 104 ? 32.24659  -15.07947 16.67095  1.000 98.78675  ? 183 GLU B CD    1 
ATOM   781  O  OE1   . GLU A 1 104 ? 31.14859  -15.61824 16.41303  1.000 100.63952 ? 183 GLU B OE1   1 
ATOM   782  O  OE2   . GLU A 1 104 ? 33.03296  -15.52272 17.53709  1.000 95.18532  ? 183 GLU B OE2   1 
ATOM   783  N  N     . ILE A 1 105 ? 32.57323  -12.98046 12.63221  1.000 76.31263  ? 184 ILE B N     1 
ATOM   784  C  CA    . ILE A 1 105 ? 33.62676  -13.43009 11.71875  1.000 71.44293  ? 184 ILE B CA    1 
ATOM   785  C  C     . ILE A 1 105 ? 34.62062  -14.27968 12.49968  1.000 72.57917  ? 184 ILE B C     1 
ATOM   786  O  O     . ILE A 1 105 ? 35.10933  -13.83770 13.55944  1.000 76.35868  ? 184 ILE B O     1 
ATOM   787  C  CB    . ILE A 1 105 ? 34.32341  -12.22639 11.06282  1.000 71.48809  ? 184 ILE B CB    1 
ATOM   788  C  CG1   . ILE A 1 105 ? 33.30288  -11.38179 10.29424  1.000 73.80407  ? 184 ILE B CG1   1 
ATOM   789  C  CG2   . ILE A 1 105 ? 35.43770  -12.69692 10.14313  1.000 64.12938  ? 184 ILE B CG2   1 
ATOM   790  C  CD1   . ILE A 1 105 ? 33.88538  -10.13696 9.67058   1.000 65.40241  ? 184 ILE B CD1   1 
ATOM   791  N  N     . PRO A 1 106 ? 34.92746  -15.50099 12.05959  1.000 70.12732  ? 185 PRO B N     1 
ATOM   792  C  CA    . PRO A 1 106 ? 35.87244  -16.33610 12.81067  1.000 70.54257  ? 185 PRO B CA    1 
ATOM   793  C  C     . PRO A 1 106 ? 37.21756  -15.64191 12.96065  1.000 78.92958  ? 185 PRO B C     1 
ATOM   794  O  O     . PRO A 1 106 ? 37.68323  -14.94928 12.05298  1.000 79.86262  ? 185 PRO B O     1 
ATOM   795  C  CB    . PRO A 1 106 ? 35.98254  -17.60455 11.95848  1.000 65.87937  ? 185 PRO B CB    1 
ATOM   796  C  CG    . PRO A 1 106 ? 34.71712  -17.63704 11.16123  1.000 72.71081  ? 185 PRO B CG    1 
ATOM   797  C  CD    . PRO A 1 106 ? 34.38049  -16.19882 10.88475  1.000 65.69574  ? 185 PRO B CD    1 
ATOM   798  N  N     . SER A 1 107 ? 37.84083  -15.83084 14.12884  1.000 70.08901  ? 186 SER B N     1 
ATOM   799  C  CA    . SER A 1 107 ? 39.08039  -15.11805 14.42261  1.000 75.90147  ? 186 SER B CA    1 
ATOM   800  C  C     . SER A 1 107 ? 40.17274  -15.44499 13.41279  1.000 75.10130  ? 186 SER B C     1 
ATOM   801  O  O     . SER A 1 107 ? 41.05544  -14.61529 13.16708  1.000 89.63363  ? 186 SER B O     1 
ATOM   802  C  CB    . SER A 1 107 ? 39.55431  -15.43717 15.84259  1.000 74.55653  ? 186 SER B CB    1 
ATOM   803  O  OG    . SER A 1 107 ? 40.01010  -16.77471 15.94808  1.000 81.77948  ? 186 SER B OG    1 
ATOM   804  N  N     . VAL A 1 108 ? 40.12711  -16.63385 12.80690  1.000 64.63654  ? 187 VAL B N     1 
ATOM   805  C  CA    . VAL A 1 108 ? 41.17282  -17.00120 11.85882  1.000 68.51012  ? 187 VAL B CA    1 
ATOM   806  C  C     . VAL A 1 108 ? 41.02638  -16.21989 10.55876  1.000 67.47811  ? 187 VAL B C     1 
ATOM   807  O  O     . VAL A 1 108 ? 42.01385  -15.99523 9.84923   1.000 70.64586  ? 187 VAL B O     1 
ATOM   808  C  CB    . VAL A 1 108 ? 41.16950  -18.52273 11.61436  1.000 63.05609  ? 187 VAL B CB    1 
ATOM   809  C  CG1   . VAL A 1 108 ? 39.90774  -18.95533 10.89003  1.000 68.23633  ? 187 VAL B CG1   1 
ATOM   810  C  CG2   . VAL A 1 108 ? 42.40197  -18.93699 10.83559  1.000 65.70455  ? 187 VAL B CG2   1 
ATOM   811  N  N     . VAL A 1 109 ? 39.81129  -15.77698 10.22756  1.000 69.79651  ? 188 VAL B N     1 
ATOM   812  C  CA    . VAL A 1 109 ? 39.62076  -15.05099 8.97568   1.000 70.16969  ? 188 VAL B CA    1 
ATOM   813  C  C     . VAL A 1 109 ? 40.28400  -13.67937 9.04015   1.000 70.47207  ? 188 VAL B C     1 
ATOM   814  O  O     . VAL A 1 109 ? 40.76495  -13.16720 8.02150   1.000 67.97452  ? 188 VAL B O     1 
ATOM   815  C  CB    . VAL A 1 109 ? 38.12086  -14.95180 8.63809   1.000 69.66381  ? 188 VAL B CB    1 
ATOM   816  C  CG1   . VAL A 1 109 ? 37.91776  -14.31077 7.26875   1.000 54.06669  ? 188 VAL B CG1   1 
ATOM   817  C  CG2   . VAL A 1 109 ? 37.48255  -16.33220 8.67696   1.000 57.88208  ? 188 VAL B CG2   1 
ATOM   818  N  N     . TYR A 1 110 ? 40.34703  -13.07188 10.22853  1.000 77.10398  ? 189 TYR B N     1 
ATOM   819  C  CA    . TYR A 1 110 ? 41.03051  -11.79191 10.38567  1.000 77.57339  ? 189 TYR B CA    1 
ATOM   820  C  C     . TYR A 1 110 ? 42.53958  -11.89917 10.19460  1.000 80.16570  ? 189 TYR B C     1 
ATOM   821  O  O     . TYR A 1 110 ? 43.21626  -10.86510 10.15842  1.000 80.30305  ? 189 TYR B O     1 
ATOM   822  C  CB    . TYR A 1 110 ? 40.73375  -11.19233 11.76521  1.000 73.26655  ? 189 TYR B CB    1 
ATOM   823  C  CG    . TYR A 1 110 ? 39.31216  -10.70007 11.95030  1.000 74.02768  ? 189 TYR B CG    1 
ATOM   824  C  CD1   . TYR A 1 110 ? 38.88346  -9.51450  11.36562  1.000 71.67878  ? 189 TYR B CD1   1 
ATOM   825  C  CD2   . TYR A 1 110 ? 38.40521  -11.41225 12.72477  1.000 71.98854  ? 189 TYR B CD2   1 
ATOM   826  C  CE1   . TYR A 1 110 ? 37.58607  -9.05912  11.53651  1.000 70.04184  ? 189 TYR B CE1   1 
ATOM   827  C  CE2   . TYR A 1 110 ? 37.10882  -10.96511 12.90302  1.000 67.61009  ? 189 TYR B CE2   1 
ATOM   828  C  CZ    . TYR A 1 110 ? 36.70278  -9.78928  12.30598  1.000 76.31669  ? 189 TYR B CZ    1 
ATOM   829  O  OH    . TYR A 1 110 ? 35.41062  -9.34358  12.48245  1.000 68.18049  ? 189 TYR B OH    1 
ATOM   830  N  N     . ARG A 1 111 ? 43.08009  -13.11147 10.07287  1.000 77.51625  ? 190 ARG B N     1 
ATOM   831  C  CA    . ARG A 1 111 ? 44.51046  -13.32088 9.89753   1.000 70.17405  ? 190 ARG B CA    1 
ATOM   832  C  C     . ARG A 1 111 ? 44.88772  -13.71774 8.47565   1.000 74.01572  ? 190 ARG B C     1 
ATOM   833  O  O     . ARG A 1 111 ? 46.08010  -13.86567 8.18554   1.000 78.55917  ? 190 ARG B O     1 
ATOM   834  C  CB    . ARG A 1 111 ? 45.01135  -14.38318 10.88382  1.000 66.70858  ? 190 ARG B CB    1 
ATOM   835  C  CG    . ARG A 1 111 ? 44.76251  -14.02892 12.34359  1.000 80.29438  ? 190 ARG B CG    1 
ATOM   836  C  CD    . ARG A 1 111 ? 45.59594  -14.88011 13.29511  1.000 70.31541  ? 190 ARG B CD    1 
ATOM   837  N  NE    . ARG A 1 111 ? 45.12540  -16.25770 13.38360  1.000 75.22931  ? 190 ARG B NE    1 
ATOM   838  C  CZ    . ARG A 1 111 ? 44.12457  -16.65857 14.15662  1.000 80.67593  ? 190 ARG B CZ    1 
ATOM   839  N  NH1   . ARG A 1 111 ? 43.42890  -15.80163 14.88686  1.000 77.11926  ? 190 ARG B NH1   1 
ATOM   840  N  NH2   . ARG A 1 111 ? 43.81416  -17.95161 14.19894  1.000 71.69824  ? 190 ARG B NH2   1 
ATOM   841  N  N     . LEU A 1 112 ? 43.91053  -13.88448 7.58181   1.000 77.23346  ? 191 LEU B N     1 
ATOM   842  C  CA    . LEU A 1 112 ? 44.16681  -14.30994 6.20299   1.000 70.05940  ? 191 LEU B CA    1 
ATOM   843  C  C     . LEU A 1 112 ? 44.33077  -13.08030 5.30754   1.000 70.46646  ? 191 LEU B C     1 
ATOM   844  O  O     . LEU A 1 112 ? 43.48796  -12.75785 4.46760   1.000 65.51132  ? 191 LEU B O     1 
ATOM   845  C  CB    . LEU A 1 112 ? 43.04212  -15.21222 5.71025   1.000 69.62901  ? 191 LEU B CB    1 
ATOM   846  C  CG    . LEU A 1 112 ? 42.66115  -16.40085 6.59510   1.000 66.35571  ? 191 LEU B CG    1 
ATOM   847  C  CD1   . LEU A 1 112 ? 41.51958  -17.18808 5.97132   1.000 49.36449  ? 191 LEU B CD1   1 
ATOM   848  C  CD2   . LEU A 1 112 ? 43.86681  -17.29263 6.83169   1.000 64.40332  ? 191 LEU B CD2   1 
ATOM   849  N  N     . ASP A 1 113 ? 45.46668  -12.39883 5.49191   1.000 70.69870  ? 192 ASP B N     1 
ATOM   850  C  CA    . ASP A 1 113 ? 45.70762  -11.11889 4.83289   1.000 60.98197  ? 192 ASP B CA    1 
ATOM   851  C  C     . ASP A 1 113 ? 45.88065  -11.23437 3.32356   1.000 63.98368  ? 192 ASP B C     1 
ATOM   852  O  O     . ASP A 1 113 ? 45.96058  -10.19994 2.65301   1.000 87.96211  ? 192 ASP B O     1 
ATOM   853  C  CB    . ASP A 1 113 ? 46.93542  -10.43232 5.43807   1.000 81.47602  ? 192 ASP B CB    1 
ATOM   854  C  CG    . ASP A 1 113 ? 48.14956  -11.34620 5.50998   1.000 86.63350  ? 192 ASP B CG    1 
ATOM   855  O  OD1   . ASP A 1 113 ? 48.53285  -11.92761 4.47083   1.000 85.09846  ? 192 ASP B OD1   1 
ATOM   856  O  OD2   . ASP A 1 113 ? 48.73291  -11.46734 6.60910   1.000 86.87438  ? 192 ASP B OD2   1 
ATOM   857  N  N     . SER A 1 114 ? 45.94173  -12.44308 2.77181   1.000 59.94274  ? 193 SER B N     1 
ATOM   858  C  CA    . SER A 1 114 ? 46.00663  -12.61352 1.32650   1.000 65.74299  ? 193 SER B CA    1 
ATOM   859  C  C     . SER A 1 114 ? 44.63424  -12.61333 0.66097   1.000 72.23267  ? 193 SER B C     1 
ATOM   860  O  O     . SER A 1 114 ? 44.56484  -12.64758 -0.57175  1.000 72.66317  ? 193 SER B O     1 
ATOM   861  C  CB    . SER A 1 114 ? 46.73905  -13.91280 0.97566   1.000 60.54624  ? 193 SER B CB    1 
ATOM   862  O  OG    . SER A 1 114 ? 46.01839  -15.04787 1.42220   1.000 72.28944  ? 193 SER B OG    1 
ATOM   863  N  N     . LEU A 1 115 ? 43.54980  -12.56943 1.43494   1.000 69.20531  ? 194 LEU B N     1 
ATOM   864  C  CA    . LEU A 1 115 ? 42.21108  -12.65069 0.86178   1.000 74.51344  ? 194 LEU B CA    1 
ATOM   865  C  C     . LEU A 1 115 ? 41.90811  -11.43471 -0.00624  1.000 70.96031  ? 194 LEU B C     1 
ATOM   866  O  O     . LEU A 1 115 ? 42.11846  -10.28988 0.40643   1.000 64.48893  ? 194 LEU B O     1 
ATOM   867  C  CB    . LEU A 1 115 ? 41.16102  -12.77385 1.96606   1.000 59.36753  ? 194 LEU B CB    1 
ATOM   868  C  CG    . LEU A 1 115 ? 40.96257  -14.15557 2.59145   1.000 67.47597  ? 194 LEU B CG    1 
ATOM   869  C  CD1   . LEU A 1 115 ? 39.89826  -14.10142 3.67600   1.000 59.70445  ? 194 LEU B CD1   1 
ATOM   870  C  CD2   . LEU A 1 115 ? 40.60035  -15.18880 1.53334   1.000 58.13773  ? 194 LEU B CD2   1 
ATOM   871  N  N     . THR A 1 116 ? 41.41051  -11.69220 -1.21738  1.000 67.33770  ? 195 THR B N     1 
ATOM   872  C  CA    . THR A 1 116 ? 40.91664  -10.64566 -2.09843  1.000 73.82157  ? 195 THR B CA    1 
ATOM   873  C  C     . THR A 1 116 ? 39.40383  -10.66323 -2.25480  1.000 71.19063  ? 195 THR B C     1 
ATOM   874  O  O     . THR A 1 116 ? 38.83453  -9.66871  -2.71506  1.000 67.67488  ? 195 THR B O     1 
ATOM   875  C  CB    . THR A 1 116 ? 41.56336  -10.76403 -3.48736  1.000 65.50210  ? 195 THR B CB    1 
ATOM   876  O  OG1   . THR A 1 116 ? 41.24238  -12.03610 -4.06220  1.000 66.49492  ? 195 THR B OG1   1 
ATOM   877  C  CG2   . THR A 1 116 ? 43.07338  -10.63387 -3.38067  1.000 69.40394  ? 195 THR B CG2   1 
ATOM   878  N  N     . THR A 1 117 ? 38.74730  -11.75423 -1.86444  1.000 67.51866  ? 196 THR B N     1 
ATOM   879  C  CA    . THR A 1 117 ? 37.30687  -11.91762 -1.99704  1.000 59.99261  ? 196 THR B CA    1 
ATOM   880  C  C     . THR A 1 117 ? 36.78128  -12.64289 -0.76736  1.000 65.28013  ? 196 THR B C     1 
ATOM   881  O  O     . THR A 1 117 ? 37.29201  -13.70919 -0.41144  1.000 58.35790  ? 196 THR B O     1 
ATOM   882  C  CB    . THR A 1 117 ? 36.96537  -12.69846 -3.27144  1.000 64.94970  ? 196 THR B CB    1 
ATOM   883  O  OG1   . THR A 1 117 ? 37.10084  -11.83846 -4.41006  1.000 76.33374  ? 196 THR B OG1   1 
ATOM   884  C  CG2   . THR A 1 117 ? 35.55295  -13.24646 -3.21100  1.000 70.25603  ? 196 THR B CG2   1 
ATOM   885  N  N     . LEU A 1 118 ? 35.77061  -12.06483 -0.11642  1.000 62.66003  ? 197 LEU B N     1 
ATOM   886  C  CA    . LEU A 1 118 ? 35.22496  -12.62370 1.11956   1.000 61.68784  ? 197 LEU B CA    1 
ATOM   887  C  C     . LEU A 1 118 ? 33.71364  -12.43853 1.12500   1.000 65.49442  ? 197 LEU B C     1 
ATOM   888  O  O     . LEU A 1 118 ? 33.22600  -11.30798 1.22174   1.000 64.99838  ? 197 LEU B O     1 
ATOM   889  C  CB    . LEU A 1 118 ? 35.85524  -11.96497 2.34530   1.000 54.89641  ? 197 LEU B CB    1 
ATOM   890  C  CG    . LEU A 1 118 ? 35.36571  -12.47418 3.70167   1.000 55.60839  ? 197 LEU B CG    1 
ATOM   891  C  CD1   . LEU A 1 118 ? 35.69870  -13.94594 3.87953   1.000 54.97147  ? 197 LEU B CD1   1 
ATOM   892  C  CD2   . LEU A 1 118 ? 35.96190  -11.64662 4.82427   1.000 47.16485  ? 197 LEU B CD2   1 
ATOM   893  N  N     . TYR A 1 119 ? 32.97571  -13.54559 1.03555   1.000 66.08356  ? 198 TYR B N     1 
ATOM   894  C  CA    . TYR A 1 119 ? 31.51483  -13.53746 1.04319   1.000 59.44453  ? 198 TYR B CA    1 
ATOM   895  C  C     . TYR A 1 119 ? 31.02975  -14.03899 2.39885   1.000 62.14878  ? 198 TYR B C     1 
ATOM   896  O  O     . TYR A 1 119 ? 31.21793  -15.21293 2.73628   1.000 52.82149  ? 198 TYR B O     1 
ATOM   897  C  CB    . TYR A 1 119 ? 30.95197  -14.40571 -0.07932  1.000 62.09561  ? 198 TYR B CB    1 
ATOM   898  C  CG    . TYR A 1 119 ? 31.40669  -14.02407 -1.46835  1.000 61.41379  ? 198 TYR B CG    1 
ATOM   899  C  CD1   . TYR A 1 119 ? 31.55045  -12.69422 -1.83685  1.000 59.20238  ? 198 TYR B CD1   1 
ATOM   900  C  CD2   . TYR A 1 119 ? 31.69611  -15.00076 -2.41256  1.000 64.02089  ? 198 TYR B CD2   1 
ATOM   901  C  CE1   . TYR A 1 119 ? 31.96572  -12.34975 -3.10854  1.000 58.35619  ? 198 TYR B CE1   1 
ATOM   902  C  CE2   . TYR A 1 119 ? 32.11390  -14.66540 -3.68390  1.000 51.56996  ? 198 TYR B CE2   1 
ATOM   903  C  CZ    . TYR A 1 119 ? 32.24508  -13.34051 -4.02774  1.000 60.66013  ? 198 TYR B CZ    1 
ATOM   904  O  OH    . TYR A 1 119 ? 32.66123  -13.00728 -5.29623  1.000 75.16785  ? 198 TYR B OH    1 
ATOM   905  N  N     . LEU A 1 120 ? 30.40172  -13.14988 3.17039   1.000 65.96805  ? 199 LEU B N     1 
ATOM   906  C  CA    . LEU A 1 120 ? 29.80304  -13.49817 4.45466   1.000 62.44492  ? 199 LEU B CA    1 
ATOM   907  C  C     . LEU A 1 120 ? 28.29090  -13.30018 4.43804   1.000 68.31729  ? 199 LEU B C     1 
ATOM   908  O  O     . LEU A 1 120 ? 27.67418  -13.12809 5.49508   1.000 68.81837  ? 199 LEU B O     1 
ATOM   909  C  CB    . LEU A 1 120 ? 30.43964  -12.67822 5.57826   1.000 58.31917  ? 199 LEU B CB    1 
ATOM   910  C  CG    . LEU A 1 120 ? 31.96463  -12.77683 5.67693   1.000 58.25763  ? 199 LEU B CG    1 
ATOM   911  C  CD1   . LEU A 1 120 ? 32.51565  -11.76603 6.66763   1.000 57.48985  ? 199 LEU B CD1   1 
ATOM   912  C  CD2   . LEU A 1 120 ? 32.38661  -14.18372 6.06114   1.000 55.92509  ? 199 LEU B CD2   1 
ATOM   913  N  N     . ARG A 1 121 ? 27.69011  -13.32834 3.25098   1.000 66.83846  ? 200 ARG B N     1 
ATOM   914  C  CA    . ARG A 1 121 ? 26.27326  -13.03951 3.08541   1.000 64.75190  ? 200 ARG B CA    1 
ATOM   915  C  C     . ARG A 1 121 ? 25.41728  -14.07549 3.81186   1.000 61.64277  ? 200 ARG B C     1 
ATOM   916  O  O     . ARG A 1 121 ? 25.80220  -15.23493 3.96075   1.000 59.00233  ? 200 ARG B O     1 
ATOM   917  C  CB    . ARG A 1 121 ? 25.93777  -13.00967 1.59221   1.000 66.97117  ? 200 ARG B CB    1 
ATOM   918  C  CG    . ARG A 1 121 ? 24.58478  -12.43677 1.23552   1.000 75.94200  ? 200 ARG B CG    1 
ATOM   919  C  CD    . ARG A 1 121 ? 24.25864  -12.74508 -0.21900  1.000 81.87258  ? 200 ARG B CD    1 
ATOM   920  N  NE    . ARG A 1 121 ? 25.12490  -12.01642 -1.13693  1.000 78.21948  ? 200 ARG B NE    1 
ATOM   921  C  CZ    . ARG A 1 121 ? 24.68970  -11.19573 -2.08236  1.000 75.22786  ? 200 ARG B CZ    1 
ATOM   922  N  NH1   . ARG A 1 121 ? 23.39740  -11.01620 -2.30009  1.000 87.52234  ? 200 ARG B NH1   1 
ATOM   923  N  NH2   . ARG A 1 121 ? 25.57316  -10.54475 -2.83349  1.000 83.02930  ? 200 ARG B NH2   1 
ATOM   924  N  N     . PHE A 1 122 ? 24.24748  -13.64125 4.27833   1.000 66.91167  ? 201 PHE B N     1 
ATOM   925  C  CA    . PHE A 1 122 ? 23.27896  -14.50401 4.96078   1.000 65.49783  ? 201 PHE B CA    1 
ATOM   926  C  C     . PHE A 1 122 ? 23.93131  -15.28780 6.10609   1.000 68.62358  ? 201 PHE B C     1 
ATOM   927  O  O     . PHE A 1 122 ? 24.11279  -16.50425 6.05597   1.000 63.95792  ? 201 PHE B O     1 
ATOM   928  C  CB    . PHE A 1 122 ? 22.59994  -15.45635 3.97175   1.000 62.75257  ? 201 PHE B CB    1 
ATOM   929  C  CG    . PHE A 1 122 ? 21.58320  -14.79404 3.09060   1.000 71.00262  ? 201 PHE B CG    1 
ATOM   930  C  CD1   . PHE A 1 122 ? 20.31797  -14.50003 3.57072   1.000 69.04948  ? 201 PHE B CD1   1 
ATOM   931  C  CD2   . PHE A 1 122 ? 21.88725  -14.47601 1.77776   1.000 68.57624  ? 201 PHE B CD2   1 
ATOM   932  C  CE1   . PHE A 1 122 ? 19.37776  -13.89103 2.75811   1.000 68.57130  ? 201 PHE B CE1   1 
ATOM   933  C  CE2   . PHE A 1 122 ? 20.95418  -13.86798 0.96077   1.000 70.02676  ? 201 PHE B CE2   1 
ATOM   934  C  CZ    . PHE A 1 122 ? 19.69686  -13.57468 1.45149   1.000 73.57476  ? 201 PHE B CZ    1 
ATOM   935  N  N     . ASN A 1 123 ? 24.28203  -14.54348 7.15052   1.000 69.31092  ? 202 ASN B N     1 
ATOM   936  C  CA    . ASN A 1 123 ? 24.73967  -15.12129 8.40515   1.000 68.80012  ? 202 ASN B CA    1 
ATOM   937  C  C     . ASN A 1 123 ? 24.12179  -14.32317 9.54363   1.000 65.61803  ? 202 ASN B C     1 
ATOM   938  O  O     . ASN A 1 123 ? 23.32465  -13.40640 9.32395   1.000 77.46647  ? 202 ASN B O     1 
ATOM   939  C  CB    . ASN A 1 123 ? 26.27110  -15.13741 8.49761   1.000 74.43579  ? 202 ASN B CB    1 
ATOM   940  C  CG    . ASN A 1 123 ? 26.89243  -16.29216 7.73550   1.000 68.28421  ? 202 ASN B CG    1 
ATOM   941  O  OD1   . ASN A 1 123 ? 26.98702  -17.40509 8.24852   1.000 63.57249  ? 202 ASN B OD1   1 
ATOM   942  N  ND2   . ASN A 1 123 ? 27.32916  -16.02977 6.50987   1.000 61.81499  ? 202 ASN B ND2   1 
ATOM   943  N  N     . ARG A 1 124 ? 24.49034  -14.67350 10.77096  1.000 70.09200  ? 203 ARG B N     1 
ATOM   944  C  CA    . ARG A 1 124 ? 24.00688  -13.98814 11.96431  1.000 77.13000  ? 203 ARG B CA    1 
ATOM   945  C  C     . ARG A 1 124 ? 25.11781  -13.16979 12.61701  1.000 74.20764  ? 203 ARG B C     1 
ATOM   946  O  O     . ARG A 1 124 ? 25.21530  -13.08789 13.84205  1.000 80.42889  ? 203 ARG B O     1 
ATOM   947  C  CB    . ARG A 1 124 ? 23.41609  -14.98497 12.95939  1.000 76.17491  ? 203 ARG B CB    1 
ATOM   948  C  CG    . ARG A 1 124 ? 22.28597  -15.83703 12.39306  1.000 87.36540  ? 203 ARG B CG    1 
ATOM   949  C  CD    . ARG A 1 124 ? 22.77320  -17.22675 12.00332  1.000 98.75391  ? 203 ARG B CD    1 
ATOM   950  N  NE    . ARG A 1 124 ? 22.32330  -18.24966 12.94106  1.000 96.06172  ? 203 ARG B NE    1 
ATOM   951  C  CZ    . ARG A 1 124 ? 21.31468  -19.08148 12.71527  1.000 101.30973 ? 203 ARG B CZ    1 
ATOM   952  N  NH1   . ARG A 1 124 ? 20.63689  -19.05490 11.57879  1.000 93.34455  ? 203 ARG B NH1   1 
ATOM   953  N  NH2   . ARG A 1 124 ? 20.98002  -19.96519 13.65151  1.000 106.88179 ? 203 ARG B NH2   1 
ATOM   954  N  N     . ILE A 1 125 ? 25.96953  -12.55333 11.79671  1.000 75.29180  ? 204 ILE B N     1 
ATOM   955  C  CA    . ILE A 1 125 ? 27.11797  -11.82070 12.31443  1.000 82.56630  ? 204 ILE B CA    1 
ATOM   956  C  C     . ILE A 1 125 ? 26.65939  -10.50358 12.92362  1.000 84.18224  ? 204 ILE B C     1 
ATOM   957  O  O     . ILE A 1 125 ? 25.81537  -9.79444  12.35859  1.000 83.50796  ? 204 ILE B O     1 
ATOM   958  C  CB    . ILE A 1 125 ? 28.15137  -11.59048 11.19835  1.000 80.79970  ? 204 ILE B CB    1 
ATOM   959  C  CG1   . ILE A 1 125 ? 28.61237  -12.92999 10.62155  1.000 65.40728  ? 204 ILE B CG1   1 
ATOM   960  C  CG2   . ILE A 1 125 ? 29.33768  -10.78675 11.71727  1.000 79.57395  ? 204 ILE B CG2   1 
ATOM   961  C  CD1   . ILE A 1 125 ? 29.58254  -12.79685 9.47702   1.000 70.79500  ? 204 ILE B CD1   1 
ATOM   962  N  N     . THR A 1 126 ? 27.21868  -10.16910 14.08936  1.000 84.93029  ? 205 THR B N     1 
ATOM   963  C  CA    . THR A 1 126 ? 26.87537  -8.94541  14.79719  1.000 87.29080  ? 205 THR B CA    1 
ATOM   964  C  C     . THR A 1 126 ? 28.03401  -7.97114  14.94343  1.000 80.80371  ? 205 THR B C     1 
ATOM   965  O  O     . THR A 1 126 ? 27.79635  -6.80937  15.29233  1.000 79.60053  ? 205 THR B O     1 
ATOM   966  C  CB    . THR A 1 126 ? 26.33681  -9.26770  16.20043  1.000 81.22462  ? 205 THR B CB    1 
ATOM   967  O  OG1   . THR A 1 126 ? 27.36995  -9.88809  16.97561  1.000 95.43697  ? 205 THR B OG1   1 
ATOM   968  C  CG2   . THR A 1 126 ? 25.14300  -10.20544 16.11514  1.000 84.67199  ? 205 THR B CG2   1 
ATOM   969  N  N     . THR A 1 127 ? 29.26905  -8.39715  14.68854  1.000 84.74783  ? 206 THR B N     1 
ATOM   970  C  CA    . THR A 1 127 ? 30.43578  -7.57166  14.96525  1.000 82.53185  ? 206 THR B CA    1 
ATOM   971  C  C     . THR A 1 127 ? 31.42442  -7.65356  13.81449  1.000 83.46643  ? 206 THR B C     1 
ATOM   972  O  O     . THR A 1 127 ? 31.73492  -8.74711  13.33288  1.000 86.28024  ? 206 THR B O     1 
ATOM   973  C  CB    . THR A 1 127 ? 31.12177  -8.01060  16.26362  1.000 89.44161  ? 206 THR B CB    1 
ATOM   974  O  OG1   . THR A 1 127 ? 30.16850  -8.00946  17.33273  1.000 102.62062 ? 206 THR B OG1   1 
ATOM   975  C  CG2   . THR A 1 127 ? 32.26878  -7.07061  16.60825  1.000 87.14011  ? 206 THR B CG2   1 
ATOM   976  N  N     . VAL A 1 128 ? 31.91442  -6.49792  13.38335  1.000 74.09111  ? 207 VAL B N     1 
ATOM   977  C  CA    . VAL A 1 128 ? 33.04204  -6.40406  12.46720  1.000 66.89654  ? 207 VAL B CA    1 
ATOM   978  C  C     . VAL A 1 128 ? 34.19948  -5.83816  13.27751  1.000 81.18312  ? 207 VAL B C     1 
ATOM   979  O  O     . VAL A 1 128 ? 34.23610  -4.63885  13.57496  1.000 89.73151  ? 207 VAL B O     1 
ATOM   980  C  CB    . VAL A 1 128 ? 32.72730  -5.53477  11.24646  1.000 78.06564  ? 207 VAL B CB    1 
ATOM   981  C  CG1   . VAL A 1 128 ? 33.95269  -5.41866  10.35194  1.000 67.61775  ? 207 VAL B CG1   1 
ATOM   982  C  CG2   . VAL A 1 128 ? 31.55523  -6.11786  10.47656  1.000 80.03934  ? 207 VAL B CG2   1 
ATOM   983  N  N     . GLU A 1 129 ? 35.14250  -6.70050  13.64669  1.000 78.86976  ? 208 GLU B N     1 
ATOM   984  C  CA    . GLU A 1 129 ? 36.23396  -6.29462  14.51715  1.000 73.86874  ? 208 GLU B CA    1 
ATOM   985  C  C     . GLU A 1 129 ? 37.17324  -5.32399  13.80661  1.000 76.68497  ? 208 GLU B C     1 
ATOM   986  O  O     . GLU A 1 129 ? 37.22492  -5.24948  12.57565  1.000 79.67232  ? 208 GLU B O     1 
ATOM   987  C  CB    . GLU A 1 129 ? 37.01590  -7.51601  14.99995  1.000 72.03234  ? 208 GLU B CB    1 
ATOM   988  C  CG    . GLU A 1 129 ? 36.21064  -8.46664  15.86817  1.000 79.20546  ? 208 GLU B CG    1 
ATOM   989  C  CD    . GLU A 1 129 ? 35.87453  -7.87949  17.22680  1.000 94.46137  ? 208 GLU B CD    1 
ATOM   990  O  OE1   . GLU A 1 129 ? 36.44905  -6.82902  17.58694  1.000 95.73763  ? 208 GLU B OE1   1 
ATOM   991  O  OE2   . GLU A 1 129 ? 35.03493  -8.47135  17.93770  1.000 96.35312  ? 208 GLU B OE2   1 
ATOM   992  N  N     . LYS A 1 130 ? 37.92830  -4.57090  14.61297  1.000 81.53366  ? 209 LYS B N     1 
ATOM   993  C  CA    . LYS A 1 130 ? 38.90169  -3.63054  14.06901  1.000 73.77334  ? 209 LYS B CA    1 
ATOM   994  C  C     . LYS A 1 130 ? 40.01351  -4.33005  13.30229  1.000 74.74414  ? 209 LYS B C     1 
ATOM   995  O  O     . LYS A 1 130 ? 40.68451  -3.69068  12.48471  1.000 83.01558  ? 209 LYS B O     1 
ATOM   996  C  CB    . LYS A 1 130 ? 39.50417  -2.78207  15.18940  1.000 74.38789  ? 209 LYS B CB    1 
ATOM   997  C  CG    . LYS A 1 130 ? 38.53234  -1.79963  15.81157  1.000 89.47623  ? 209 LYS B CG    1 
ATOM   998  C  CD    . LYS A 1 130 ? 39.25420  -0.78261  16.68065  1.000 79.48087  ? 209 LYS B CD    1 
ATOM   999  C  CE    . LYS A 1 130 ? 38.32423  0.35519   17.06518  1.000 105.96881 ? 209 LYS B CE    1 
ATOM   1000 N  NZ    . LYS A 1 130 ? 37.65328  0.94730   15.86818  1.000 104.95213 ? 209 LYS B NZ    1 
ATOM   1001 N  N     . ASP A 1 131 ? 40.22308  -5.62430  13.54508  1.000 73.97255  ? 210 ASP B N     1 
ATOM   1002 C  CA    . ASP A 1 131 ? 41.21721  -6.39905  12.81286  1.000 80.34355  ? 210 ASP B CA    1 
ATOM   1003 C  C     . ASP A 1 131 ? 40.87029  -6.57305  11.34311  1.000 75.65156  ? 210 ASP B C     1 
ATOM   1004 O  O     . ASP A 1 131 ? 41.67112  -7.15924  10.60654  1.000 80.74976  ? 210 ASP B O     1 
ATOM   1005 C  CB    . ASP A 1 131 ? 41.39222  -7.77216  13.46240  1.000 91.60988  ? 210 ASP B CB    1 
ATOM   1006 C  CG    . ASP A 1 131 ? 42.07320  -7.69503  14.81110  1.000 94.84375  ? 210 ASP B CG    1 
ATOM   1007 O  OD1   . ASP A 1 131 ? 43.22975  -7.22336  14.86902  1.000 92.04195  ? 210 ASP B OD1   1 
ATOM   1008 O  OD2   . ASP A 1 131 ? 41.44610  -8.09724  15.81417  1.000 105.18502 ? 210 ASP B OD2   1 
ATOM   1009 N  N     . ILE A 1 132 ? 39.70555  -6.09241  10.90052  1.000 75.94310  ? 211 ILE B N     1 
ATOM   1010 C  CA    . ILE A 1 132 ? 39.35270  -6.15381  9.48890   1.000 75.12387  ? 211 ILE B CA    1 
ATOM   1011 C  C     . ILE A 1 132 ? 40.38104  -5.42084  8.63720   1.000 82.02229  ? 211 ILE B C     1 
ATOM   1012 O  O     . ILE A 1 132 ? 40.53590  -5.72694  7.44897   1.000 77.76463  ? 211 ILE B O     1 
ATOM   1013 C  CB    . ILE A 1 132 ? 37.92825  -5.58874  9.28333   1.000 70.95753  ? 211 ILE B CB    1 
ATOM   1014 C  CG1   . ILE A 1 132 ? 37.39450  -5.93104  7.88842   1.000 63.45083  ? 211 ILE B CG1   1 
ATOM   1015 C  CG2   . ILE A 1 132 ? 37.89876  -4.08661  9.53629   1.000 68.60076  ? 211 ILE B CG2   1 
ATOM   1016 C  CD1   . ILE A 1 132 ? 37.09524  -7.40414  7.68849   1.000 50.67576  ? 211 ILE B CD1   1 
ATOM   1017 N  N     . LYS A 1 133 ? 41.11331  -4.47169  9.23031   1.000 76.88747  ? 212 LYS B N     1 
ATOM   1018 C  CA    . LYS A 1 133 ? 42.16670  -3.76117  8.51480   1.000 79.57494  ? 212 LYS B CA    1 
ATOM   1019 C  C     . LYS A 1 133 ? 43.25136  -4.69595  7.99573   1.000 76.62134  ? 212 LYS B C     1 
ATOM   1020 O  O     . LYS A 1 133 ? 43.94803  -4.34485  7.03694   1.000 75.38641  ? 212 LYS B O     1 
ATOM   1021 C  CB    . LYS A 1 133 ? 42.78978  -2.70117  9.42406   1.000 84.42025  ? 212 LYS B CB    1 
ATOM   1022 C  CG    . LYS A 1 133 ? 43.46173  -3.27350  10.66063  1.000 85.85969  ? 212 LYS B CG    1 
ATOM   1023 C  CD    . LYS A 1 133 ? 44.05815  -2.18228  11.52920  1.000 86.11483  ? 212 LYS B CD    1 
ATOM   1024 C  CE    . LYS A 1 133 ? 44.69694  -2.76656  12.77822  1.000 95.38467  ? 212 LYS B CE    1 
ATOM   1025 N  NZ    . LYS A 1 133 ? 45.20584  -1.69999  13.68499  1.000 98.45759  ? 212 LYS B NZ    1 
ATOM   1026 N  N     . ASN A 1 134 ? 43.41139  -5.87432  8.60406   1.000 74.20240  ? 213 ASN B N     1 
ATOM   1027 C  CA    . ASN A 1 134 ? 44.40762  -6.82910  8.13370   1.000 74.92044  ? 213 ASN B CA    1 
ATOM   1028 C  C     . ASN A 1 134 ? 44.06689  -7.39549  6.76430   1.000 74.43350  ? 213 ASN B C     1 
ATOM   1029 O  O     . ASN A 1 134 ? 44.97269  -7.82807  6.04562   1.000 77.68394  ? 213 ASN B O     1 
ATOM   1030 C  CB    . ASN A 1 134 ? 44.56225  -7.96878  9.13953   1.000 74.87646  ? 213 ASN B CB    1 
ATOM   1031 C  CG    . ASN A 1 134 ? 45.07354  -7.49085  10.48960  1.000 93.34085  ? 213 ASN B CG    1 
ATOM   1032 O  OD1   . ASN A 1 134 ? 45.94419  -6.62243  10.56523  1.000 97.89765  ? 213 ASN B OD1   1 
ATOM   1033 N  ND2   . ASN A 1 134 ? 44.53541  -8.05998  11.56334  1.000 101.70674 ? 213 ASN B ND2   1 
ATOM   1034 N  N     . LEU A 1 135 ? 42.79285  -7.40148  6.38731   1.000 84.02885  ? 214 LEU B N     1 
ATOM   1035 C  CA    . LEU A 1 135 ? 42.37344  -7.90345  5.07969   1.000 82.73831  ? 214 LEU B CA    1 
ATOM   1036 C  C     . LEU A 1 135 ? 42.34089  -6.78168  4.04747   1.000 82.30454  ? 214 LEU B C     1 
ATOM   1037 O  O     . LEU A 1 135 ? 41.35190  -6.58421  3.34515   1.000 78.66869  ? 214 LEU B O     1 
ATOM   1038 C  CB    . LEU A 1 135 ? 41.01421  -8.58403  5.19718   1.000 73.76341  ? 214 LEU B CB    1 
ATOM   1039 C  CG    . LEU A 1 135 ? 40.85623  -9.58072  6.35133   1.000 65.89506  ? 214 LEU B CG    1 
ATOM   1040 C  CD1   . LEU A 1 135 ? 39.47682  -10.21686 6.36003   1.000 49.81292  ? 214 LEU B CD1   1 
ATOM   1041 C  CD2   . LEU A 1 135 ? 41.93082  -10.64223 6.28347   1.000 56.77330  ? 214 LEU B CD2   1 
ATOM   1042 N  N     . SER A 1 136 ? 43.44669  -6.04199  3.94550   1.000 84.15731  ? 215 SER B N     1 
ATOM   1043 C  CA    . SER A 1 136 ? 43.50563  -4.85438  3.10274   1.000 83.20233  ? 215 SER B CA    1 
ATOM   1044 C  C     . SER A 1 136 ? 43.64328  -5.17058  1.62019   1.000 80.63399  ? 215 SER B C     1 
ATOM   1045 O  O     . SER A 1 136 ? 43.49462  -4.26144  0.79620   1.000 90.97099  ? 215 SER B O     1 
ATOM   1046 C  CB    . SER A 1 136 ? 44.66470  -3.96091  3.54179   1.000 79.34984  ? 215 SER B CB    1 
ATOM   1047 O  OG    . SER A 1 136 ? 45.88699  -4.67311  3.50385   1.000 99.30688  ? 215 SER B OG    1 
ATOM   1048 N  N     . LYS A 1 137 ? 43.92889  -6.41705  1.25821   1.000 64.89437  ? 216 LYS B N     1 
ATOM   1049 C  CA    . LYS A 1 137 ? 43.95150  -6.80754  -0.14370  1.000 68.89003  ? 216 LYS B CA    1 
ATOM   1050 C  C     . LYS A 1 137 ? 42.56267  -7.13343  -0.68137  1.000 75.61740  ? 216 LYS B C     1 
ATOM   1051 O  O     . LYS A 1 137 ? 42.44230  -7.56973  -1.83123  1.000 63.53776  ? 216 LYS B O     1 
ATOM   1052 C  CB    . LYS A 1 137 ? 44.89062  -8.00081  -0.33956  1.000 64.13225  ? 216 LYS B CB    1 
ATOM   1053 C  CG    . LYS A 1 137 ? 46.34047  -7.69847  0.02051   1.000 87.54107  ? 216 LYS B CG    1 
ATOM   1054 C  CD    . LYS A 1 137 ? 47.21113  -8.94274  -0.05084  1.000 88.62487  ? 216 LYS B CD    1 
ATOM   1055 C  CE    . LYS A 1 137 ? 48.58127  -8.69116  0.55923   1.000 79.63753  ? 216 LYS B CE    1 
ATOM   1056 N  NZ    . LYS A 1 137 ? 49.36050  -9.95408  0.71501   1.000 91.63130  ? 216 LYS B NZ    1 
ATOM   1057 N  N     . LEU A 1 138 ? 41.51892  -6.92378  0.11691   1.000 68.88960  ? 217 LEU B N     1 
ATOM   1058 C  CA    . LEU A 1 138 ? 40.16805  -7.24112  -0.31889  1.000 66.14781  ? 217 LEU B CA    1 
ATOM   1059 C  C     . LEU A 1 138 ? 39.70183  -6.26629  -1.38948  1.000 72.95212  ? 217 LEU B C     1 
ATOM   1060 O  O     . LEU A 1 138 ? 39.92097  -5.05522  -1.29285  1.000 82.67566  ? 217 LEU B O     1 
ATOM   1061 C  CB    . LEU A 1 138 ? 39.20100  -7.20818  0.86360   1.000 60.58679  ? 217 LEU B CB    1 
ATOM   1062 C  CG    . LEU A 1 138 ? 39.16365  -8.42669  1.78574   1.000 62.40218  ? 217 LEU B CG    1 
ATOM   1063 C  CD1   . LEU A 1 138 ? 38.19776  -8.18360  2.92849   1.000 60.22628  ? 217 LEU B CD1   1 
ATOM   1064 C  CD2   . LEU A 1 138 ? 38.77165  -9.67446  1.01114   1.000 63.54685  ? 217 LEU B CD2   1 
ATOM   1065 N  N     . SER A 1 139 ? 39.06164  -6.80897  -2.42277  1.000 69.48629  ? 218 SER B N     1 
ATOM   1066 C  CA    . SER A 1 139 ? 38.36871  -6.00803  -3.41796  1.000 72.13274  ? 218 SER B CA    1 
ATOM   1067 C  C     . SER A 1 139 ? 36.85997  -6.17437  -3.35036  1.000 63.01570  ? 218 SER B C     1 
ATOM   1068 O  O     . SER A 1 139 ? 36.13553  -5.36911  -3.94585  1.000 64.47676  ? 218 SER B O     1 
ATOM   1069 C  CB    . SER A 1 139 ? 38.85619  -6.36818  -4.82869  1.000 59.09742  ? 218 SER B CB    1 
ATOM   1070 O  OG    . SER A 1 139 ? 38.61532  -7.73473  -5.11019  1.000 70.98057  ? 218 SER B OG    1 
ATOM   1071 N  N     . MET A 1 140 ? 36.37599  -7.18695  -2.63454  1.000 62.01789  ? 219 MET B N     1 
ATOM   1072 C  CA    . MET A 1 140 ? 34.95002  -7.46461  -2.49890  1.000 63.09264  ? 219 MET B CA    1 
ATOM   1073 C  C     . MET A 1 140 ? 34.69052  -7.89382  -1.06172  1.000 64.82663  ? 219 MET B C     1 
ATOM   1074 O  O     . MET A 1 140 ? 35.15247  -8.95880  -0.63756  1.000 59.81147  ? 219 MET B O     1 
ATOM   1075 C  CB    . MET A 1 140 ? 34.50867  -8.54870  -3.48127  1.000 64.62940  ? 219 MET B CB    1 
ATOM   1076 C  CG    . MET A 1 140 ? 33.13802  -9.13782  -3.19801  1.000 72.34329  ? 219 MET B CG    1 
ATOM   1077 S  SD    . MET A 1 140 ? 31.78025  -8.09601  -3.75020  1.000 83.39601  ? 219 MET B SD    1 
ATOM   1078 C  CE    . MET A 1 140 ? 30.37172  -9.14378  -3.39331  1.000 68.15479  ? 219 MET B CE    1 
ATOM   1079 N  N     . LEU A 1 141 ? 33.96344  -7.06693  -0.31291  1.000 60.26548  ? 220 LEU B N     1 
ATOM   1080 C  CA    . LEU A 1 141 ? 33.54987  -7.38611  1.05098   1.000 65.69341  ? 220 LEU B CA    1 
ATOM   1081 C  C     . LEU A 1 141 ? 32.02734  -7.38592  1.09632   1.000 63.73753  ? 220 LEU B C     1 
ATOM   1082 O  O     . LEU A 1 141 ? 31.39926  -6.32901  0.97095   1.000 65.65123  ? 220 LEU B O     1 
ATOM   1083 C  CB    . LEU A 1 141 ? 34.13063  -6.38948  2.05281   1.000 65.93451  ? 220 LEU B CB    1 
ATOM   1084 C  CG    . LEU A 1 141 ? 33.84567  -6.67400  3.53045   1.000 72.09828  ? 220 LEU B CG    1 
ATOM   1085 C  CD1   . LEU A 1 141 ? 34.27817  -8.08480  3.89936   1.000 65.56544  ? 220 LEU B CD1   1 
ATOM   1086 C  CD2   . LEU A 1 141 ? 34.53959  -5.65252  4.42029   1.000 56.82298  ? 220 LEU B CD2   1 
ATOM   1087 N  N     . SER A 1 142 ? 31.43580  -8.56647  1.26742   1.000 66.08581  ? 221 SER B N     1 
ATOM   1088 C  CA    . SER A 1 142 ? 29.98253  -8.73381  1.28460   1.000 63.28932  ? 221 SER B CA    1 
ATOM   1089 C  C     . SER A 1 142 ? 29.56319  -9.29026  2.64088   1.000 61.68420  ? 221 SER B C     1 
ATOM   1090 O  O     . SER A 1 142 ? 29.73259  -10.48304 2.91108   1.000 60.86222  ? 221 SER B O     1 
ATOM   1091 C  CB    . SER A 1 142 ? 29.52083  -9.64909  0.15532   1.000 64.19311  ? 221 SER B CB    1 
ATOM   1092 O  OG    . SER A 1 142 ? 28.13356  -9.92376  0.26309   1.000 74.54562  ? 221 SER B OG    1 
ATOM   1093 N  N     . ILE A 1 143 ? 29.01336  -8.42778  3.49092   1.000 59.09794  ? 222 ILE B N     1 
ATOM   1094 C  CA    . ILE A 1 143 ? 28.44269  -8.85907  4.76099   1.000 64.41258  ? 222 ILE B CA    1 
ATOM   1095 C  C     . ILE A 1 143 ? 26.93989  -8.61961  4.71481   1.000 63.53177  ? 222 ILE B C     1 
ATOM   1096 O  O     . ILE A 1 143 ? 26.32434  -8.23849  5.71662   1.000 66.03476  ? 222 ILE B O     1 
ATOM   1097 C  CB    . ILE A 1 143 ? 29.09682  -8.13190  5.94845   1.000 62.62508  ? 222 ILE B CB    1 
ATOM   1098 C  CG1   . ILE A 1 143 ? 29.14980  -6.62787  5.68790   1.000 71.69084  ? 222 ILE B CG1   1 
ATOM   1099 C  CG2   . ILE A 1 143 ? 30.49276  -8.67244  6.20091   1.000 65.17301  ? 222 ILE B CG2   1 
ATOM   1100 C  CD1   . ILE A 1 143 ? 29.93151  -5.86215  6.73164   1.000 80.89459  ? 222 ILE B CD1   1 
ATOM   1101 N  N     . ARG A 1 144 ? 26.34708  -8.84265  3.54536   1.000 68.04432  ? 223 ARG B N     1 
ATOM   1102 C  CA    . ARG A 1 144 ? 24.91896  -8.64105  3.35421   1.000 66.61925  ? 223 ARG B CA    1 
ATOM   1103 C  C     . ARG A 1 144 ? 24.11804  -9.64379  4.17740   1.000 64.84697  ? 223 ARG B C     1 
ATOM   1104 O  O     . ARG A 1 144 ? 24.53347  -10.78823 4.37419   1.000 67.43421  ? 223 ARG B O     1 
ATOM   1105 C  CB    . ARG A 1 144 ? 24.56987  -8.78085  1.87236   1.000 67.27073  ? 223 ARG B CB    1 
ATOM   1106 C  CG    . ARG A 1 144 ? 23.16189  -8.36671  1.49516   1.000 74.01428  ? 223 ARG B CG    1 
ATOM   1107 C  CD    . ARG A 1 144 ? 22.80296  -8.91505  0.12399   1.000 72.18308  ? 223 ARG B CD    1 
ATOM   1108 N  NE    . ARG A 1 144 ? 21.72765  -8.16397  -0.50996  1.000 66.23012  ? 223 ARG B NE    1 
ATOM   1109 C  CZ    . ARG A 1 144 ? 21.91606  -7.10136  -1.27968  1.000 71.03464  ? 223 ARG B CZ    1 
ATOM   1110 N  NH1   . ARG A 1 144 ? 23.12887  -6.63387  -1.52736  1.000 77.12618  ? 223 ARG B NH1   1 
ATOM   1111 N  NH2   . ARG A 1 144 ? 20.86199  -6.49165  -1.81344  1.000 83.29909  ? 223 ARG B NH2   1 
ATOM   1112 N  N     . GLU A 1 145 ? 22.96097  -9.19484  4.66993   1.000 60.21228  ? 224 GLU B N     1 
ATOM   1113 C  CA    . GLU A 1 145 ? 22.02583  -10.03223 5.42242   1.000 67.19167  ? 224 GLU B CA    1 
ATOM   1114 C  C     . GLU A 1 145 ? 22.68497  -10.59270 6.68819   1.000 68.65826  ? 224 GLU B C     1 
ATOM   1115 O  O     . GLU A 1 145 ? 22.94983  -11.78944 6.82143   1.000 61.89237  ? 224 GLU B O     1 
ATOM   1116 C  CB    . GLU A 1 145 ? 21.47354  -11.15900 4.54121   1.000 72.36859  ? 224 GLU B CB    1 
ATOM   1117 C  CG    . GLU A 1 145 ? 20.60559  -10.68171 3.38749   1.000 74.97759  ? 224 GLU B CG    1 
ATOM   1118 C  CD    . GLU A 1 145 ? 19.15794  -10.48521 3.79311   1.000 80.68114  ? 224 GLU B CD    1 
ATOM   1119 O  OE1   . GLU A 1 145 ? 18.81428  -10.80964 4.95061   1.000 76.40815  ? 224 GLU B OE1   1 
ATOM   1120 O  OE2   . GLU A 1 145 ? 18.36386  -10.00826 2.95392   1.000 88.56073  ? 224 GLU B OE2   1 
ATOM   1121 N  N     . ASN A 1 146 ? 22.93895  -9.67906  7.62147   1.000 64.18386  ? 225 ASN B N     1 
ATOM   1122 C  CA    . ASN A 1 146 ? 23.50288  -10.01859 8.92053   1.000 60.98623  ? 225 ASN B CA    1 
ATOM   1123 C  C     . ASN A 1 146 ? 22.84734  -9.12680  9.96866   1.000 74.60490  ? 225 ASN B C     1 
ATOM   1124 O  O     . ASN A 1 146 ? 21.84380  -8.45710  9.70394   1.000 82.40575  ? 225 ASN B O     1 
ATOM   1125 C  CB    . ASN A 1 146 ? 25.03082  -9.87449  8.91207   1.000 75.25500  ? 225 ASN B CB    1 
ATOM   1126 C  CG    . ASN A 1 146 ? 25.72218  -11.01865 8.19616   1.000 73.26485  ? 225 ASN B CG    1 
ATOM   1127 O  OD1   . ASN A 1 146 ? 26.03146  -12.04360 8.80070   1.000 68.52169  ? 225 ASN B OD1   1 
ATOM   1128 N  ND2   . ASN A 1 146 ? 25.97388  -10.84632 6.90360   1.000 70.31551  ? 225 ASN B ND2   1 
ATOM   1129 N  N     . LYS A 1 147 ? 23.42359  -9.11614  11.16784  1.000 77.78505  ? 226 LYS B N     1 
ATOM   1130 C  CA    . LYS A 1 147 ? 22.92280  -8.33866  12.29505  1.000 87.58197  ? 226 LYS B CA    1 
ATOM   1131 C  C     . LYS A 1 147 ? 23.96953  -7.33815  12.77453  1.000 85.37920  ? 226 LYS B C     1 
ATOM   1132 O  O     . LYS A 1 147 ? 24.15748  -7.13038  13.97539  1.000 82.89831  ? 226 LYS B O     1 
ATOM   1133 C  CB    . LYS A 1 147 ? 22.49388  -9.25767  13.43604  1.000 84.78222  ? 226 LYS B CB    1 
ATOM   1134 C  CG    . LYS A 1 147 ? 21.36823  -10.21450 13.07795  1.000 80.07207  ? 226 LYS B CG    1 
ATOM   1135 C  CD    . LYS A 1 147 ? 21.08826  -11.17884 14.21987  1.000 92.82505  ? 226 LYS B CD    1 
ATOM   1136 C  CE    . LYS A 1 147 ? 20.77330  -10.43332 15.50921  1.000 100.96500 ? 226 LYS B CE    1 
ATOM   1137 N  NZ    . LYS A 1 147 ? 20.71831  -11.34594 16.68642  1.000 78.03482  ? 226 LYS B NZ    1 
ATOM   1138 N  N     . ILE A 1 148 ? 24.66318  -6.70629  11.83395  1.000 82.28608  ? 227 ILE B N     1 
ATOM   1139 C  CA    . ILE A 1 148 ? 25.73829  -5.77678  12.16282  1.000 84.85088  ? 227 ILE B CA    1 
ATOM   1140 C  C     . ILE A 1 148 ? 25.14362  -4.40597  12.45107  1.000 80.09246  ? 227 ILE B C     1 
ATOM   1141 O  O     . ILE A 1 148 ? 24.38012  -3.86320  11.64354  1.000 83.32723  ? 227 ILE B O     1 
ATOM   1142 C  CB    . ILE A 1 148 ? 26.76434  -5.71280  11.02040  1.000 84.80817  ? 227 ILE B CB    1 
ATOM   1143 C  CG1   . ILE A 1 148 ? 27.46215  -7.06602  10.86972  1.000 81.25432  ? 227 ILE B CG1   1 
ATOM   1144 C  CG2   . ILE A 1 148 ? 27.77490  -4.59859  11.26124  1.000 75.16674  ? 227 ILE B CG2   1 
ATOM   1145 C  CD1   . ILE A 1 148 ? 28.21614  -7.22121  9.57937   1.000 73.99036  ? 227 ILE B CD1   1 
ATOM   1146 N  N     . LYS A 1 149 ? 25.49195  -3.84140  13.60670  1.000 85.80812  ? 228 LYS B N     1 
ATOM   1147 C  CA    . LYS A 1 149 ? 24.98050  -2.54051  14.01179  1.000 79.06855  ? 228 LYS B CA    1 
ATOM   1148 C  C     . LYS A 1 149 ? 26.00157  -1.41993  13.87714  1.000 79.01100  ? 228 LYS B C     1 
ATOM   1149 O  O     . LYS A 1 149 ? 25.62459  -0.24883  13.99023  1.000 78.67648  ? 228 LYS B O     1 
ATOM   1150 C  CB    . LYS A 1 149 ? 24.47141  -2.59417  15.45832  1.000 74.21290  ? 228 LYS B CB    1 
ATOM   1151 C  CG    . LYS A 1 149 ? 23.11439  -3.26581  15.60058  1.000 97.08896  ? 228 LYS B CG    1 
ATOM   1152 C  CD    . LYS A 1 149 ? 22.45191  -2.91445  16.92337  1.000 106.51817 ? 228 LYS B CD    1 
ATOM   1153 C  CE    . LYS A 1 149 ? 20.93560  -3.02697  16.82354  1.000 113.49177 ? 228 LYS B CE    1 
ATOM   1154 N  NZ    . LYS A 1 149 ? 20.37063  -2.11104  15.78810  1.000 96.46964  ? 228 LYS B NZ    1 
ATOM   1155 N  N     . GLN A 1 150 ? 27.27125  -1.73901  13.63445  1.000 80.49737  ? 229 GLN B N     1 
ATOM   1156 C  CA    . GLN A 1 150 ? 28.28552  -0.70458  13.49721  1.000 82.70636  ? 229 GLN B CA    1 
ATOM   1157 C  C     . GLN A 1 150 ? 29.47534  -1.25733  12.72841  1.000 75.46670  ? 229 GLN B C     1 
ATOM   1158 O  O     . GLN A 1 150 ? 29.82445  -2.43142  12.87066  1.000 78.47516  ? 229 GLN B O     1 
ATOM   1159 C  CB    . GLN A 1 150 ? 28.74419  -0.18239  14.86308  1.000 77.92174  ? 229 GLN B CB    1 
ATOM   1160 C  CG    . GLN A 1 150 ? 29.63494  1.04482   14.78052  1.000 89.22475  ? 229 GLN B CG    1 
ATOM   1161 C  CD    . GLN A 1 150 ? 30.38856  1.30542   16.06776  1.000 110.31665 ? 229 GLN B CD    1 
ATOM   1162 O  OE1   . GLN A 1 150 ? 30.65195  0.38477   16.84243  1.000 112.36636 ? 229 GLN B OE1   1 
ATOM   1163 N  NE2   . GLN A 1 150 ? 30.74004  2.56532   16.30477  1.000 105.07579 ? 229 GLN B NE2   1 
ATOM   1164 N  N     . LEU A 1 151 ? 30.08847  -0.39885  11.91373  1.000 76.24282  ? 230 LEU B N     1 
ATOM   1165 C  CA    . LEU A 1 151 ? 31.34589  -0.68459  11.24962  1.000 74.16226  ? 230 LEU B CA    1 
ATOM   1166 C  C     . LEU A 1 151 ? 32.47603  0.09105   11.91139  1.000 88.04073  ? 230 LEU B C     1 
ATOM   1167 O  O     . LEU A 1 151 ? 32.30969  1.27409   12.22849  1.000 95.14449  ? 230 LEU B O     1 
ATOM   1168 C  CB    . LEU A 1 151 ? 31.29547  -0.31426  9.76442   1.000 77.55100  ? 230 LEU B CB    1 
ATOM   1169 C  CG    . LEU A 1 151 ? 30.37305  -1.14185  8.87545   1.000 84.05360  ? 230 LEU B CG    1 
ATOM   1170 C  CD1   . LEU A 1 151 ? 30.47000  -0.65614  7.43758   1.000 72.65178  ? 230 LEU B CD1   1 
ATOM   1171 C  CD2   . LEU A 1 151 ? 30.72097  -2.61859  8.98002   1.000 73.29548  ? 230 LEU B CD2   1 
ATOM   1172 N  N     . PRO A 1 152 ? 33.62696  -0.53595  12.13432  1.000 87.95636  ? 231 PRO B N     1 
ATOM   1173 C  CA    . PRO A 1 152 ? 34.75610  0.18974   12.72013  1.000 78.44136  ? 231 PRO B CA    1 
ATOM   1174 C  C     . PRO A 1 152 ? 35.34592  1.18556   11.73382  1.000 83.86751  ? 231 PRO B C     1 
ATOM   1175 O  O     . PRO A 1 152 ? 35.13863  1.10600   10.52090  1.000 89.01076  ? 231 PRO B O     1 
ATOM   1176 C  CB    . PRO A 1 152 ? 35.75599  -0.92153  13.05141  1.000 86.08738  ? 231 PRO B CB    1 
ATOM   1177 C  CG    . PRO A 1 152 ? 35.44311  -1.99779  12.06837  1.000 74.24217  ? 231 PRO B CG    1 
ATOM   1178 C  CD    . PRO A 1 152 ? 33.95503  -1.94645  11.86331  1.000 79.36124  ? 231 PRO B CD    1 
ATOM   1179 N  N     . ALA A 1 153 ? 36.09596  2.14381   12.28203  1.000 83.23078  ? 232 ALA B N     1 
ATOM   1180 C  CA    . ALA A 1 153 ? 36.77798  3.11906   11.44111  1.000 82.63296  ? 232 ALA B CA    1 
ATOM   1181 C  C     . ALA A 1 153 ? 37.84963  2.47105   10.57554  1.000 88.20719  ? 232 ALA B C     1 
ATOM   1182 O  O     . ALA A 1 153 ? 38.22256  3.03214   9.53939   1.000 86.89712  ? 232 ALA B O     1 
ATOM   1183 C  CB    . ALA A 1 153 ? 37.37979  4.22735   12.31021  1.000 86.55772  ? 232 ALA B CB    1 
ATOM   1184 N  N     . GLU A 1 154 ? 38.33837  1.29283   10.96544  1.000 85.93375  ? 233 GLU B N     1 
ATOM   1185 C  CA    . GLU A 1 154 ? 39.32534  0.55088   10.18326  1.000 84.89266  ? 233 GLU B CA    1 
ATOM   1186 C  C     . GLU A 1 154 ? 38.79658  0.11171   8.81744   1.000 89.56819  ? 233 GLU B C     1 
ATOM   1187 O  O     . GLU A 1 154 ? 39.55933  -0.46975  8.03962   1.000 84.74078  ? 233 GLU B O     1 
ATOM   1188 C  CB    . GLU A 1 154 ? 39.81294  -0.66714  10.97441  1.000 80.41735  ? 233 GLU B CB    1 
ATOM   1189 C  CG    . GLU A 1 154 ? 40.80402  -0.35849  12.09424  1.000 81.31389  ? 233 GLU B CG    1 
ATOM   1190 C  CD    . GLU A 1 154 ? 40.19371  0.45469   13.21631  1.000 96.66361  ? 233 GLU B CD    1 
ATOM   1191 O  OE1   . GLU A 1 154 ? 38.94865  0.51855   13.31872  1.000 87.08372  ? 233 GLU B OE1   1 
ATOM   1192 O  OE2   . GLU A 1 154 ? 40.96888  1.04101   13.99528  1.000 93.89044  ? 233 GLU B OE2   1 
ATOM   1193 N  N     . ILE A 1 155 ? 37.52783  0.39037   8.50401   1.000 85.49394  ? 234 ILE B N     1 
ATOM   1194 C  CA    . ILE A 1 155 ? 36.98895  0.08315   7.18776   1.000 73.73243  ? 234 ILE B CA    1 
ATOM   1195 C  C     . ILE A 1 155 ? 37.69447  0.88477   6.10316   1.000 86.74778  ? 234 ILE B C     1 
ATOM   1196 O  O     . ILE A 1 155 ? 37.70244  0.47343   4.93618   1.000 81.39846  ? 234 ILE B O     1 
ATOM   1197 C  CB    . ILE A 1 155 ? 35.45834  0.33663   7.17034   1.000 90.55943  ? 234 ILE B CB    1 
ATOM   1198 C  CG1   . ILE A 1 155 ? 34.71459  -0.82328  6.50474   1.000 80.67804  ? 234 ILE B CG1   1 
ATOM   1199 C  CG2   . ILE A 1 155 ? 35.11447  1.68269   6.52351   1.000 86.81878  ? 234 ILE B CG2   1 
ATOM   1200 C  CD1   . ILE A 1 155 ? 34.83490  -2.12096  7.26192   1.000 78.36092  ? 234 ILE B CD1   1 
ATOM   1201 N  N     . GLY A 1 156 ? 38.29069  2.02725   6.46418   1.000 90.34469  ? 235 GLY B N     1 
ATOM   1202 C  CA    . GLY A 1 156 ? 39.01509  2.91480   5.58034   1.000 87.72667  ? 235 GLY B CA    1 
ATOM   1203 C  C     . GLY A 1 156 ? 40.36306  2.41447   5.12708   1.000 82.57750  ? 235 GLY B C     1 
ATOM   1204 O  O     . GLY A 1 156 ? 40.96414  3.01858   4.23534   1.000 85.98792  ? 235 GLY B O     1 
ATOM   1205 N  N     . GLU A 1 157 ? 40.85641  1.32358   5.70743   1.000 74.42610  ? 236 GLU B N     1 
ATOM   1206 C  CA    . GLU A 1 157 ? 42.13295  0.75662   5.30519   1.000 77.87698  ? 236 GLU B CA    1 
ATOM   1207 C  C     . GLU A 1 157 ? 41.98750  -0.35478  4.27376   1.000 90.44284  ? 236 GLU B C     1 
ATOM   1208 O  O     . GLU A 1 157 ? 42.99389  -0.96038  3.89089   1.000 100.65572 ? 236 GLU B O     1 
ATOM   1209 C  CB    . GLU A 1 157 ? 42.89302  0.24600   6.53388   1.000 77.89123  ? 236 GLU B CB    1 
ATOM   1210 C  CG    . GLU A 1 157 ? 43.18050  1.33991   7.55411   1.000 88.55933  ? 236 GLU B CG    1 
ATOM   1211 C  CD    . GLU A 1 157 ? 43.95284  0.84502   8.75692   1.000 90.94649  ? 236 GLU B CD    1 
ATOM   1212 O  OE1   . GLU A 1 157 ? 44.65684  -0.17720  8.63282   1.000 96.59591  ? 236 GLU B OE1   1 
ATOM   1213 O  OE2   . GLU A 1 157 ? 43.85233  1.48027   9.82835   1.000 88.63144  ? 236 GLU B OE2   1 
ATOM   1214 N  N     . LEU A 1 158 ? 40.76984  -0.62927  3.80999   1.000 91.57807  ? 237 LEU B N     1 
ATOM   1215 C  CA    . LEU A 1 158 ? 40.54697  -1.56618  2.70878   1.000 83.09701  ? 237 LEU B CA    1 
ATOM   1216 C  C     . LEU A 1 158 ? 40.52893  -0.80833  1.38085   1.000 87.92055  ? 237 LEU B C     1 
ATOM   1217 O  O     . LEU A 1 158 ? 39.55843  -0.82376  0.62346   1.000 93.42960  ? 237 LEU B O     1 
ATOM   1218 C  CB    . LEU A 1 158 ? 39.25242  -2.34039  2.92348   1.000 81.50367  ? 237 LEU B CB    1 
ATOM   1219 C  CG    . LEU A 1 158 ? 39.05261  -2.98064  4.29755   1.000 83.90567  ? 237 LEU B CG    1 
ATOM   1220 C  CD1   . LEU A 1 158 ? 37.73653  -3.74188  4.34566   1.000 83.74789  ? 237 LEU B CD1   1 
ATOM   1221 C  CD2   . LEU A 1 158 ? 40.21783  -3.89077  4.64309   1.000 77.27164  ? 237 LEU B CD2   1 
ATOM   1222 N  N     . CYS A 1 159 ? 41.64852  -0.13544  1.11099   1.000 91.12051  ? 238 CYS B N     1 
ATOM   1223 C  CA    . CYS A 1 159 ? 41.76249  0.80311   0.00030   1.000 89.27120  ? 238 CYS B CA    1 
ATOM   1224 C  C     . CYS A 1 159 ? 41.67049  0.14264   -1.36937  1.000 78.83742  ? 238 CYS B C     1 
ATOM   1225 O  O     . CYS A 1 159 ? 41.75124  0.85366   -2.37720  1.000 83.15634  ? 238 CYS B O     1 
ATOM   1226 C  CB    . CYS A 1 159 ? 43.07649  1.57982   0.11466   1.000 93.25840  ? 238 CYS B CB    1 
ATOM   1227 S  SG    . CYS A 1 159 ? 44.55619  0.54358   0.23568   1.000 106.60257 ? 238 CYS B SG    1 
ATOM   1228 N  N     . ASN A 1 160 ? 41.50285  -1.17599  -1.44426  1.000 72.78460  ? 239 ASN B N     1 
ATOM   1229 C  CA    . ASN A 1 160 ? 41.34227  -1.86405  -2.71732  1.000 78.02208  ? 239 ASN B CA    1 
ATOM   1230 C  C     . ASN A 1 160 ? 39.90469  -2.30194  -2.96815  1.000 72.14851  ? 239 ASN B C     1 
ATOM   1231 O  O     . ASN A 1 160 ? 39.64327  -2.99731  -3.95498  1.000 69.05239  ? 239 ASN B O     1 
ATOM   1232 C  CB    . ASN A 1 160 ? 42.28061  -3.07067  -2.78697  1.000 83.31802  ? 239 ASN B CB    1 
ATOM   1233 C  CG    . ASN A 1 160 ? 43.74483  -2.67193  -2.76956  1.000 88.25894  ? 239 ASN B CG    1 
ATOM   1234 O  OD1   . ASN A 1 160 ? 44.34257  -2.41643  -3.81605  1.000 85.51458  ? 239 ASN B OD1   1 
ATOM   1235 N  ND2   . ASN A 1 160 ? 44.33088  -2.61814  -1.57779  1.000 73.42821  ? 239 ASN B ND2   1 
ATOM   1236 N  N     . LEU A 1 161 ? 38.96802  -1.90682  -2.10884  1.000 67.88899  ? 240 LEU B N     1 
ATOM   1237 C  CA    . LEU A 1 161 ? 37.58813  -2.35435  -2.24537  1.000 70.73182  ? 240 LEU B CA    1 
ATOM   1238 C  C     . LEU A 1 161 ? 36.93617  -1.74626  -3.47967  1.000 75.30749  ? 240 LEU B C     1 
ATOM   1239 O  O     . LEU A 1 161 ? 37.02017  -0.53611  -3.71164  1.000 70.74989  ? 240 LEU B O     1 
ATOM   1240 C  CB    . LEU A 1 161 ? 36.77881  -1.98707  -1.00325  1.000 60.99628  ? 240 LEU B CB    1 
ATOM   1241 C  CG    . LEU A 1 161 ? 36.87034  -2.93451  0.18870   1.000 60.55932  ? 240 LEU B CG    1 
ATOM   1242 C  CD1   . LEU A 1 161 ? 35.87071  -2.52819  1.25582   1.000 58.53565  ? 240 LEU B CD1   1 
ATOM   1243 C  CD2   . LEU A 1 161 ? 36.63732  -4.36521  -0.25531  1.000 64.19369  ? 240 LEU B CD2   1 
ATOM   1244 N  N     . ILE A 1 162 ? 36.28416  -2.59200  -4.27033  1.000 65.91336  ? 241 ILE B N     1 
ATOM   1245 C  CA    . ILE A 1 162 ? 35.42968  -2.13967  -5.35722  1.000 70.41168  ? 241 ILE B CA    1 
ATOM   1246 C  C     . ILE A 1 162 ? 33.95972  -2.18992  -4.96266  1.000 65.78654  ? 241 ILE B C     1 
ATOM   1247 O  O     . ILE A 1 162 ? 33.18073  -1.31398  -5.34039  1.000 63.40979  ? 241 ILE B O     1 
ATOM   1248 C  CB    . ILE A 1 162 ? 35.69202  -2.97441  -6.62860  1.000 64.05783  ? 241 ILE B CB    1 
ATOM   1249 C  CG1   . ILE A 1 162 ? 37.15219  -2.84737  -7.05939  1.000 59.64285  ? 241 ILE B CG1   1 
ATOM   1250 C  CG2   . ILE A 1 162 ? 34.76561  -2.54194  -7.75582  1.000 56.58608  ? 241 ILE B CG2   1 
ATOM   1251 C  CD1   . ILE A 1 162 ? 37.47456  -3.61341  -8.32160  1.000 59.03079  ? 241 ILE B CD1   1 
ATOM   1252 N  N     . THR A 1 163 ? 33.57443  -3.20297  -4.18981  1.000 57.27820  ? 242 THR B N     1 
ATOM   1253 C  CA    . THR A 1 163 ? 32.20826  -3.36132  -3.71456  1.000 61.14781  ? 242 THR B CA    1 
ATOM   1254 C  C     . THR A 1 163 ? 32.21788  -3.55646  -2.20736  1.000 61.98145  ? 242 THR B C     1 
ATOM   1255 O  O     . THR A 1 163 ? 32.92829  -4.42750  -1.69530  1.000 64.36363  ? 242 THR B O     1 
ATOM   1256 C  CB    . THR A 1 163 ? 31.51363  -4.55090  -4.38688  1.000 61.36890  ? 242 THR B CB    1 
ATOM   1257 O  OG1   . THR A 1 163 ? 31.22480  -4.23352  -5.75411  1.000 66.07593  ? 242 THR B OG1   1 
ATOM   1258 C  CG2   . THR A 1 163 ? 30.21986  -4.89073  -3.66263  1.000 55.31307  ? 242 THR B CG2   1 
ATOM   1259 N  N     . LEU A 1 164 ? 31.43561  -2.74420  -1.50292  1.000 64.04228  ? 243 LEU B N     1 
ATOM   1260 C  CA    . LEU A 1 164 ? 31.18740  -2.91923  -0.07410  1.000 62.11501  ? 243 LEU B CA    1 
ATOM   1261 C  C     . LEU A 1 164 ? 29.69012  -3.15908  0.09123   1.000 63.96177  ? 243 LEU B C     1 
ATOM   1262 O  O     . LEU A 1 164 ? 28.89053  -2.22122  0.00950   1.000 65.66138  ? 243 LEU B O     1 
ATOM   1263 C  CB    . LEU A 1 164 ? 31.65642  -1.71019  0.72806   1.000 51.09363  ? 243 LEU B CB    1 
ATOM   1264 C  CG    . LEU A 1 164 ? 31.49513  -1.84498  2.24379   1.000 64.66043  ? 243 LEU B CG    1 
ATOM   1265 C  CD1   . LEU A 1 164 ? 32.27750  -3.04469  2.76496   1.000 73.59798  ? 243 LEU B CD1   1 
ATOM   1266 C  CD2   . LEU A 1 164 ? 31.92860  -0.57728  2.95177   1.000 60.04067  ? 243 LEU B CD2   1 
ATOM   1267 N  N     . ASP A 1 165 ? 29.31232  -4.41539  0.31300   1.000 67.58274  ? 244 ASP B N     1 
ATOM   1268 C  CA    . ASP A 1 165 ? 27.91119  -4.81630  0.42736   1.000 61.25070  ? 244 ASP B CA    1 
ATOM   1269 C  C     . ASP A 1 165 ? 27.59579  -5.04241  1.90330   1.000 66.67410  ? 244 ASP B C     1 
ATOM   1270 O  O     . ASP A 1 165 ? 27.97026  -6.06728  2.47925   1.000 68.43768  ? 244 ASP B O     1 
ATOM   1271 C  CB    . ASP A 1 165 ? 27.64749  -6.06753  -0.40483  1.000 69.04109  ? 244 ASP B CB    1 
ATOM   1272 C  CG    . ASP A 1 165 ? 26.18996  -6.49591  -0.38162  1.000 77.63170  ? 244 ASP B CG    1 
ATOM   1273 O  OD1   . ASP A 1 165 ? 25.34194  -5.72261  0.11022   1.000 65.32510  ? 244 ASP B OD1   1 
ATOM   1274 O  OD2   . ASP A 1 165 ? 25.89429  -7.61465  -0.85684  1.000 85.89716  ? 244 ASP B OD2   1 
ATOM   1275 N  N     . VAL A 1 166 ? 26.91144  -4.07651  2.51624   1.000 67.38835  ? 245 VAL B N     1 
ATOM   1276 C  CA    . VAL A 1 166 ? 26.45419  -4.18080  3.89618   1.000 72.26680  ? 245 VAL B CA    1 
ATOM   1277 C  C     . VAL A 1 166 ? 24.93012  -4.09918  3.98055   1.000 71.99959  ? 245 VAL B C     1 
ATOM   1278 O  O     . VAL A 1 166 ? 24.37852  -3.76405  5.02549   1.000 67.28725  ? 245 VAL B O     1 
ATOM   1279 C  CB    . VAL A 1 166 ? 27.11935  -3.11611  4.79127   1.000 69.30086  ? 245 VAL B CB    1 
ATOM   1280 C  CG1   . VAL A 1 166 ? 28.63137  -3.19040  4.67445   1.000 77.45750  ? 245 VAL B CG1   1 
ATOM   1281 C  CG2   . VAL A 1 166 ? 26.62600  -1.72444  4.43417   1.000 75.25642  ? 245 VAL B CG2   1 
ATOM   1282 N  N     . ALA A 1 167 ? 24.24567  -4.41476  2.88418   1.000 71.13326  ? 246 ALA B N     1 
ATOM   1283 C  CA    . ALA A 1 167 ? 22.79625  -4.32106  2.84181   1.000 65.09581  ? 246 ALA B CA    1 
ATOM   1284 C  C     . ALA A 1 167 ? 22.15793  -5.31339  3.80894   1.000 70.06584  ? 246 ALA B C     1 
ATOM   1285 O  O     . ALA A 1 167 ? 22.74309  -6.33704  4.17438   1.000 66.68405  ? 246 ALA B O     1 
ATOM   1286 C  CB    . ALA A 1 167 ? 22.28533  -4.57135  1.42424   1.000 62.73183  ? 246 ALA B CB    1 
ATOM   1287 N  N     . HIS A 1 168 ? 20.93266  -4.98713  4.22336   1.000 69.10302  ? 247 HIS B N     1 
ATOM   1288 C  CA    . HIS A 1 168 ? 20.14604  -5.80439  5.14545   1.000 61.78095  ? 247 HIS B CA    1 
ATOM   1289 C  C     . HIS A 1 168 ? 20.90881  -6.05186  6.44928   1.000 68.45170  ? 247 HIS B C     1 
ATOM   1290 O  O     . HIS A 1 168 ? 21.15679  -7.18661  6.86108   1.000 68.09124  ? 247 HIS B O     1 
ATOM   1291 C  CB    . HIS A 1 168 ? 19.71442  -7.11618  4.48138   1.000 63.23316  ? 247 HIS B CB    1 
ATOM   1292 C  CG    . HIS A 1 168 ? 18.69456  -6.93209  3.39962   1.000 71.92133  ? 247 HIS B CG    1 
ATOM   1293 N  ND1   . HIS A 1 168 ? 19.03513  -6.65942  2.09216   1.000 74.41897  ? 247 HIS B ND1   1 
ATOM   1294 C  CD2   . HIS A 1 168 ? 17.34109  -6.96577  3.43556   1.000 75.26561  ? 247 HIS B CD2   1 
ATOM   1295 C  CE1   . HIS A 1 168 ? 17.93641  -6.53980  1.36818   1.000 72.05469  ? 247 HIS B CE1   1 
ATOM   1296 N  NE2   . HIS A 1 168 ? 16.89476  -6.72035  2.15963   1.000 65.32487  ? 247 HIS B NE2   1 
ATOM   1297 N  N     . ASN A 1 169 ? 21.28462  -4.94759  7.09234   1.000 68.86662  ? 248 ASN B N     1 
ATOM   1298 C  CA    . ASN A 1 169 ? 21.85587  -4.98454  8.43194   1.000 73.76405  ? 248 ASN B CA    1 
ATOM   1299 C  C     . ASN A 1 169 ? 21.11893  -3.99828  9.32772   1.000 78.67419  ? 248 ASN B C     1 
ATOM   1300 O  O     . ASN A 1 169 ? 19.94670  -3.69327  9.08777   1.000 81.67815  ? 248 ASN B O     1 
ATOM   1301 C  CB    . ASN A 1 169 ? 23.35351  -4.67038  8.40257   1.000 75.41557  ? 248 ASN B CB    1 
ATOM   1302 C  CG    . ASN A 1 169 ? 24.19294  -5.86196  7.98781   1.000 72.59761  ? 248 ASN B CG    1 
ATOM   1303 O  OD1   . ASN A 1 169 ? 24.45905  -6.75544  8.79085   1.000 68.70056  ? 248 ASN B OD1   1 
ATOM   1304 N  ND2   . ASN A 1 169 ? 24.62376  -5.87614  6.73166   1.000 75.25736  ? 248 ASN B ND2   1 
ATOM   1305 N  N     . GLN A 1 170 ? 21.79198  -3.49094  10.35638  1.000 84.42844  ? 249 GLN B N     1 
ATOM   1306 C  CA    . GLN A 1 170 ? 21.19283  -2.55216  11.29705  1.000 83.45636  ? 249 GLN B CA    1 
ATOM   1307 C  C     . GLN A 1 170 ? 22.12659  -1.38182  11.56070  1.000 81.24561  ? 249 GLN B C     1 
ATOM   1308 O  O     . GLN A 1 170 ? 22.22964  -0.88528  12.68623  1.000 88.95392  ? 249 GLN B O     1 
ATOM   1309 C  CB    . GLN A 1 170 ? 20.81511  -3.25225  12.60016  1.000 84.07134  ? 249 GLN B CB    1 
ATOM   1310 C  CG    . GLN A 1 170 ? 19.61457  -4.17480  12.46554  1.000 90.74672  ? 249 GLN B CG    1 
ATOM   1311 C  CD    . GLN A 1 170 ? 19.91931  -5.60031  12.87738  1.000 99.02556  ? 249 GLN B CD    1 
ATOM   1312 O  OE1   . GLN A 1 170 ? 20.38606  -5.85245  13.99011  1.000 105.16157 ? 249 GLN B OE1   1 
ATOM   1313 N  NE2   . GLN A 1 170 ? 19.65809  -6.54424  11.97750  1.000 90.17544  ? 249 GLN B NE2   1 
ATOM   1314 N  N     . LEU A 1 171 ? 22.81750  -0.91899  10.52172  1.000 76.86062  ? 250 LEU B N     1 
ATOM   1315 C  CA    . LEU A 1 171 ? 23.71343  0.21972   10.66690  1.000 81.82039  ? 250 LEU B CA    1 
ATOM   1316 C  C     . LEU A 1 171 ? 22.91732  1.48968   10.92788  1.000 84.87274  ? 250 LEU B C     1 
ATOM   1317 O  O     . LEU A 1 171 ? 21.95790  1.79016   10.21291  1.000 91.97068  ? 250 LEU B O     1 
ATOM   1318 C  CB    . LEU A 1 171 ? 24.56720  0.39308   9.41248   1.000 78.35490  ? 250 LEU B CB    1 
ATOM   1319 C  CG    . LEU A 1 171 ? 25.62201  -0.67204  9.12521   1.000 79.48757  ? 250 LEU B CG    1 
ATOM   1320 C  CD1   . LEU A 1 171 ? 26.39208  -0.31839  7.86433   1.000 76.12654  ? 250 LEU B CD1   1 
ATOM   1321 C  CD2   . LEU A 1 171 ? 26.56111  -0.81610  10.30806  1.000 79.67666  ? 250 LEU B CD2   1 
ATOM   1322 N  N     . GLU A 1 172 ? 23.31363  2.23359   11.95949  1.000 85.85357  ? 251 GLU B N     1 
ATOM   1323 C  CA    . GLU A 1 172 ? 22.76017  3.55784   12.20109  1.000 87.27413  ? 251 GLU B CA    1 
ATOM   1324 C  C     . GLU A 1 172 ? 23.65148  4.67685   11.68474  1.000 87.35064  ? 251 GLU B C     1 
ATOM   1325 O  O     . GLU A 1 172 ? 23.15054  5.77666   11.42656  1.000 84.61412  ? 251 GLU B O     1 
ATOM   1326 C  CB    . GLU A 1 172 ? 22.50418  3.77095   13.69765  1.000 88.97233  ? 251 GLU B CB    1 
ATOM   1327 C  CG    . GLU A 1 172 ? 21.16138  3.24935   14.17748  1.000 99.48046  ? 251 GLU B CG    1 
ATOM   1328 C  CD    . GLU A 1 172 ? 20.83520  3.70664   15.58504  1.000 116.53294 ? 251 GLU B CD    1 
ATOM   1329 O  OE1   . GLU A 1 172 ? 21.77797  3.88064   16.38731  1.000 116.55498 ? 251 GLU B OE1   1 
ATOM   1330 O  OE2   . GLU A 1 172 ? 19.63794  3.90187   15.88598  1.000 116.68704 ? 251 GLU B OE2   1 
ATOM   1331 N  N     . HIS A 1 173 ? 24.94893  4.42395   11.52625  1.000 88.93290  ? 252 HIS B N     1 
ATOM   1332 C  CA    . HIS A 1 173 ? 25.87164  5.41914   11.00427  1.000 90.37551  ? 252 HIS B CA    1 
ATOM   1333 C  C     . HIS A 1 173 ? 26.94770  4.72002   10.18911  1.000 85.67449  ? 252 HIS B C     1 
ATOM   1334 O  O     . HIS A 1 173 ? 27.33002  3.58404   10.48086  1.000 91.83996  ? 252 HIS B O     1 
ATOM   1335 C  CB    . HIS A 1 173 ? 26.51984  6.24214   12.12420  1.000 91.29964  ? 252 HIS B CB    1 
ATOM   1336 C  CG    . HIS A 1 173 ? 25.54059  6.99515   12.96826  1.000 92.85876  ? 252 HIS B CG    1 
ATOM   1337 N  ND1   . HIS A 1 173 ? 25.08304  8.25188   12.63552  1.000 97.60485  ? 252 HIS B ND1   1 
ATOM   1338 C  CD2   . HIS A 1 173 ? 24.93176  6.66900   14.13283  1.000 94.27345  ? 252 HIS B CD2   1 
ATOM   1339 C  CE1   . HIS A 1 173 ? 24.23418  8.66761   13.55851  1.000 96.09463  ? 252 HIS B CE1   1 
ATOM   1340 N  NE2   . HIS A 1 173 ? 24.12491  7.72583   14.47833  1.000 103.57679 ? 252 HIS B NE2   1 
ATOM   1341 N  N     . LEU A 1 174 ? 27.42894  5.41221   9.15917   1.000 87.75987  ? 253 LEU B N     1 
ATOM   1342 C  CA    . LEU A 1 174 ? 28.55442  4.93481   8.37320   1.000 88.71723  ? 253 LEU B CA    1 
ATOM   1343 C  C     . LEU A 1 174 ? 29.81126  5.63416   8.85829   1.000 94.41677  ? 253 LEU B C     1 
ATOM   1344 O  O     . LEU A 1 174 ? 29.82980  6.87511   8.89977   1.000 100.91087 ? 253 LEU B O     1 
ATOM   1345 C  CB    . LEU A 1 174 ? 28.33212  5.21768   6.89238   1.000 89.70213  ? 253 LEU B CB    1 
ATOM   1346 C  CG    . LEU A 1 174 ? 28.56259  4.11413   5.85745   1.000 83.59933  ? 253 LEU B CG    1 
ATOM   1347 C  CD1   . LEU A 1 174 ? 28.49812  4.70948   4.46474   1.000 86.36237  ? 253 LEU B CD1   1 
ATOM   1348 C  CD2   . LEU A 1 174 ? 29.88702  3.41065   6.06702   1.000 93.62167  ? 253 LEU B CD2   1 
ATOM   1349 N  N     . PRO A 1 175 ? 30.85922  4.91105   9.25402   1.000 95.81320  ? 254 PRO B N     1 
ATOM   1350 C  CA    . PRO A 1 175 ? 32.09301  5.58190   9.68707   1.000 86.10537  ? 254 PRO B CA    1 
ATOM   1351 C  C     . PRO A 1 175 ? 32.64878  6.48018   8.59149   1.000 91.07795  ? 254 PRO B C     1 
ATOM   1352 O  O     . PRO A 1 175 ? 32.76408  6.07815   7.43152   1.000 90.64275  ? 254 PRO B O     1 
ATOM   1353 C  CB    . PRO A 1 175 ? 33.04056  4.41757   10.00661  1.000 80.99559  ? 254 PRO B CB    1 
ATOM   1354 C  CG    . PRO A 1 175 ? 32.41789  3.20734   9.36884   1.000 91.21694  ? 254 PRO B CG    1 
ATOM   1355 C  CD    . PRO A 1 175 ? 30.94405  3.45166   9.42036   1.000 86.56683  ? 254 PRO B CD    1 
ATOM   1356 N  N     . LYS A 1 176 ? 32.99387  7.71211   8.97649   1.000 91.07794  ? 255 LYS B N     1 
ATOM   1357 C  CA    . LYS A 1 176 ? 33.45546  8.70883   8.01623   1.000 89.29615  ? 255 LYS B CA    1 
ATOM   1358 C  C     . LYS A 1 176 ? 34.70874  8.27089   7.26951   1.000 91.06009  ? 255 LYS B C     1 
ATOM   1359 O  O     . LYS A 1 176 ? 35.00871  8.82795   6.20752   1.000 89.71471  ? 255 LYS B O     1 
ATOM   1360 C  CB    . LYS A 1 176 ? 33.70768  10.03689  8.73172   1.000 85.02957  ? 255 LYS B CB    1 
ATOM   1361 C  CG    . LYS A 1 176 ? 34.54520  9.91240   9.99437   1.000 82.22449  ? 255 LYS B CG    1 
ATOM   1362 C  CD    . LYS A 1 176 ? 34.51595  11.20251  10.79915  1.000 100.45645 ? 255 LYS B CD    1 
ATOM   1363 C  CE    . LYS A 1 176 ? 35.28609  11.06731  12.10523  1.000 85.57183  ? 255 LYS B CE    1 
ATOM   1364 N  NZ    . LYS A 1 176 ? 36.73152  10.80659  11.87334  1.000 93.41540  ? 255 LYS B NZ    1 
ATOM   1365 N  N     . GLU A 1 177 ? 35.44094  7.28463   7.78984   1.000 83.47534  ? 256 GLU B N     1 
ATOM   1366 C  CA    . GLU A 1 177 ? 36.63763  6.78895   7.12037   1.000 90.45679  ? 256 GLU B CA    1 
ATOM   1367 C  C     . GLU A 1 177 ? 36.33326  6.04900   5.82202   1.000 92.86406  ? 256 GLU B C     1 
ATOM   1368 O  O     . GLU A 1 177 ? 37.27760  5.63276   5.13928   1.000 92.54680  ? 256 GLU B O     1 
ATOM   1369 C  CB    . GLU A 1 177 ? 37.43282  5.87987   8.06577   1.000 87.88048  ? 256 GLU B CB    1 
ATOM   1370 C  CG    . GLU A 1 177 ? 38.13882  6.60847   9.20888   1.000 82.23778  ? 256 GLU B CG    1 
ATOM   1371 C  CD    . GLU A 1 177 ? 37.18325  7.07769   10.29023  1.000 93.02490  ? 256 GLU B CD    1 
ATOM   1372 O  OE1   . GLU A 1 177 ? 36.03493  6.58860   10.32267  1.000 95.27594  ? 256 GLU B OE1   1 
ATOM   1373 O  OE2   . GLU A 1 177 ? 37.57860  7.93602   11.10745  1.000 95.78765  ? 256 GLU B OE2   1 
ATOM   1374 N  N     . ILE A 1 178 ? 35.05637  5.88258   5.46244   1.000 83.41729  ? 257 ILE B N     1 
ATOM   1375 C  CA    . ILE A 1 178 ? 34.69511  5.20900   4.22051   1.000 84.83387  ? 257 ILE B CA    1 
ATOM   1376 C  C     . ILE A 1 178 ? 35.18768  5.98053   3.00384   1.000 89.23731  ? 257 ILE B C     1 
ATOM   1377 O  O     . ILE A 1 178 ? 35.46277  5.37786   1.96125   1.000 89.81057  ? 257 ILE B O     1 
ATOM   1378 C  CB    . ILE A 1 178 ? 33.16662  4.98269   4.17068   1.000 88.72959  ? 257 ILE B CB    1 
ATOM   1379 C  CG1   . ILE A 1 178 ? 32.76952  4.16426   2.94093   1.000 72.99172  ? 257 ILE B CG1   1 
ATOM   1380 C  CG2   . ILE A 1 178 ? 32.42064  6.30866   4.17487   1.000 84.56829  ? 257 ILE B CG2   1 
ATOM   1381 C  CD1   . ILE A 1 178 ? 33.39489  2.78662   2.89129   1.000 80.06437  ? 257 ILE B CD1   1 
ATOM   1382 N  N     . GLY A 1 179 ? 35.33617  7.30197   3.11777   1.000 88.47514  ? 258 GLY B N     1 
ATOM   1383 C  CA    . GLY A 1 179 ? 35.87872  8.11317   2.04577   1.000 92.57957  ? 258 GLY B CA    1 
ATOM   1384 C  C     . GLY A 1 179 ? 37.31126  7.80985   1.66527   1.000 99.10343  ? 258 GLY B C     1 
ATOM   1385 O  O     . GLY A 1 179 ? 37.82259  8.43070   0.72961   1.000 92.60439  ? 258 GLY B O     1 
ATOM   1386 N  N     . ASN A 1 180 ? 37.97489  6.87857   2.35128   1.000 97.69557  ? 259 ASN B N     1 
ATOM   1387 C  CA    . ASN A 1 180 ? 39.33506  6.50449   1.99727   1.000 90.27525  ? 259 ASN B CA    1 
ATOM   1388 C  C     . ASN A 1 180 ? 39.39738  5.27662   1.10061   1.000 92.76527  ? 259 ASN B C     1 
ATOM   1389 O  O     . ASN A 1 180 ? 40.48100  4.95427   0.60575   1.000 96.73788  ? 259 ASN B O     1 
ATOM   1390 C  CB    . ASN A 1 180 ? 40.17519  6.25974   3.26040   1.000 98.29934  ? 259 ASN B CB    1 
ATOM   1391 C  CG    . ASN A 1 180 ? 40.26215  7.48946   4.15322   1.000 101.62432 ? 259 ASN B CG    1 
ATOM   1392 O  OD1   . ASN A 1 180 ? 39.57609  8.47999   3.91667   1.000 101.51763 ? 259 ASN B OD1   1 
ATOM   1393 N  ND2   . ASN A 1 180 ? 41.09109  7.42180   5.19666   1.000 104.52723 ? 259 ASN B ND2   1 
ATOM   1394 N  N     . CYS A 1 181 ? 38.27295  4.59002   0.88289   1.000 86.25005  ? 260 CYS B N     1 
ATOM   1395 C  CA    . CYS A 1 181 ? 38.19697  3.46237   -0.04992  1.000 82.69058  ? 260 CYS B CA    1 
ATOM   1396 C  C     . CYS A 1 181 ? 37.85118  3.99247   -1.44092  1.000 84.50454  ? 260 CYS B C     1 
ATOM   1397 O  O     . CYS A 1 181 ? 36.77997  3.74445   -1.99504  1.000 88.80695  ? 260 CYS B O     1 
ATOM   1398 C  CB    . CYS A 1 181 ? 37.16681  2.44774   0.42664   1.000 74.92591  ? 260 CYS B CB    1 
ATOM   1399 S  SG    . CYS A 1 181 ? 37.25180  2.06508   2.18398   1.000 77.60819  ? 260 CYS B SG    1 
ATOM   1400 N  N     . THR A 1 182 ? 38.79530  4.75412   -1.99712  1.000 93.30363  ? 261 THR B N     1 
ATOM   1401 C  CA    . THR A 1 182 ? 38.52277  5.50725   -3.21749  1.000 86.53077  ? 261 THR B CA    1 
ATOM   1402 C  C     . THR A 1 182 ? 38.15390  4.60006   -4.38404  1.000 73.47308  ? 261 THR B C     1 
ATOM   1403 O  O     . THR A 1 182 ? 37.35380  4.99175   -5.24073  1.000 87.91307  ? 261 THR B O     1 
ATOM   1404 C  CB    . THR A 1 182 ? 39.73291  6.36865   -3.57457  1.000 86.90084  ? 261 THR B CB    1 
ATOM   1405 O  OG1   . THR A 1 182 ? 40.88201  5.52955   -3.74730  1.000 75.07679  ? 261 THR B OG1   1 
ATOM   1406 C  CG2   . THR A 1 182 ? 40.00853  7.37013   -2.46061  1.000 85.74803  ? 261 THR B CG2   1 
ATOM   1407 N  N     . GLN A 1 183 ? 38.70503  3.38615   -4.43074  1.000 75.66102  ? 262 GLN B N     1 
ATOM   1408 C  CA    . GLN A 1 183 ? 38.43317  2.48423   -5.54537  1.000 73.91756  ? 262 GLN B CA    1 
ATOM   1409 C  C     . GLN A 1 183 ? 37.01304  1.93038   -5.54203  1.000 73.19541  ? 262 GLN B C     1 
ATOM   1410 O  O     . GLN A 1 183 ? 36.68764  1.12251   -6.41945  1.000 72.59609  ? 262 GLN B O     1 
ATOM   1411 C  CB    . GLN A 1 183 ? 39.42888  1.32270   -5.54180  1.000 78.69742  ? 262 GLN B CB    1 
ATOM   1412 C  CG    . GLN A 1 183 ? 40.85465  1.70292   -5.90394  1.000 83.31177  ? 262 GLN B CG    1 
ATOM   1413 C  CD    . GLN A 1 183 ? 41.74119  0.48352   -6.09538  1.000 100.67268 ? 262 GLN B CD    1 
ATOM   1414 O  OE1   . GLN A 1 183 ? 41.25283  -0.61101  -6.38220  1.000 102.22488 ? 262 GLN B OE1   1 
ATOM   1415 N  NE2   . GLN A 1 183 ? 43.04948  0.66488   -5.93224  1.000 88.03403  ? 262 GLN B NE2   1 
ATOM   1416 N  N     . ILE A 1 184 ? 36.16508  2.33517   -4.59666  1.000 73.03995  ? 263 ILE B N     1 
ATOM   1417 C  CA    . ILE A 1 184 ? 34.81704  1.78915   -4.51485  1.000 68.31746  ? 263 ILE B CA    1 
ATOM   1418 C  C     . ILE A 1 184 ? 33.97430  2.32079   -5.66521  1.000 75.85534  ? 263 ILE B C     1 
ATOM   1419 O  O     . ILE A 1 184 ? 33.86525  3.53718   -5.87018  1.000 77.76172  ? 263 ILE B O     1 
ATOM   1420 C  CB    . ILE A 1 184 ? 34.17977  2.12401   -3.15849  1.000 64.28137  ? 263 ILE B CB    1 
ATOM   1421 C  CG1   . ILE A 1 184 ? 34.71661  1.19364   -2.07229  1.000 65.55279  ? 263 ILE B CG1   1 
ATOM   1422 C  CG2   . ILE A 1 184 ? 32.66465  2.02604   -3.23808  1.000 65.61983  ? 263 ILE B CG2   1 
ATOM   1423 C  CD1   . ILE A 1 184 ? 33.98020  1.31733   -0.75861  1.000 67.33363  ? 263 ILE B CD1   1 
ATOM   1424 N  N     . THR A 1 185 ? 33.37775  1.40273   -6.42950  1.000 74.09530  ? 264 THR B N     1 
ATOM   1425 C  CA    . THR A 1 185 ? 32.38692  1.74986   -7.43619  1.000 68.81479  ? 264 THR B CA    1 
ATOM   1426 C  C     . THR A 1 185 ? 30.98115  1.30757   -7.06492  1.000 67.02215  ? 264 THR B C     1 
ATOM   1427 O  O     . THR A 1 185 ? 30.01792  1.80991   -7.65251  1.000 65.68192  ? 264 THR B O     1 
ATOM   1428 C  CB    . THR A 1 185 ? 32.75267  1.13213   -8.79533  1.000 68.51570  ? 264 THR B CB    1 
ATOM   1429 O  OG1   . THR A 1 185 ? 32.56426  -0.28709  -8.74572  1.000 69.48165  ? 264 THR B OG1   1 
ATOM   1430 C  CG2   . THR A 1 185 ? 34.20336  1.43140   -9.14683  1.000 68.15660  ? 264 THR B CG2   1 
ATOM   1431 N  N     . ASN A 1 186 ? 30.84174  0.39747   -6.10224  1.000 68.37713  ? 265 ASN B N     1 
ATOM   1432 C  CA    . ASN A 1 186 ? 29.54925  -0.15008  -5.70093  1.000 68.88514  ? 265 ASN B CA    1 
ATOM   1433 C  C     . ASN A 1 186 ? 29.47033  -0.15634  -4.17887  1.000 65.54648  ? 265 ASN B C     1 
ATOM   1434 O  O     . ASN A 1 186 ? 30.16155  -0.93963  -3.52007  1.000 59.77405  ? 265 ASN B O     1 
ATOM   1435 C  CB    . ASN A 1 186 ? 29.35769  -1.55829  -6.26366  1.000 63.02692  ? 265 ASN B CB    1 
ATOM   1436 C  CG    . ASN A 1 186 ? 28.03973  -2.17500  -5.85197  1.000 68.10750  ? 265 ASN B CG    1 
ATOM   1437 O  OD1   . ASN A 1 186 ? 27.04280  -1.47490  -5.67031  1.000 71.12315  ? 265 ASN B OD1   1 
ATOM   1438 N  ND2   . ASN A 1 186 ? 28.02737  -3.49488  -5.69766  1.000 65.96622  ? 265 ASN B ND2   1 
ATOM   1439 N  N     . LEU A 1 187 ? 28.63012  0.71270   -3.62221  1.000 70.45667  ? 266 LEU B N     1 
ATOM   1440 C  CA    . LEU A 1 187 ? 28.41046  0.80160   -2.18136  1.000 66.73398  ? 266 LEU B CA    1 
ATOM   1441 C  C     . LEU A 1 187 ? 26.92889  0.56384   -1.92038  1.000 74.50046  ? 266 LEU B C     1 
ATOM   1442 O  O     . LEU A 1 187 ? 26.08897  1.39707   -2.27954  1.000 74.40942  ? 266 LEU B O     1 
ATOM   1443 C  CB    . LEU A 1 187 ? 28.85585  2.15977   -1.64056  1.000 70.50916  ? 266 LEU B CB    1 
ATOM   1444 C  CG    . LEU A 1 187 ? 28.75703  2.37985   -0.12949  1.000 65.15660  ? 266 LEU B CG    1 
ATOM   1445 C  CD1   . LEU A 1 187 ? 29.74717  1.49551   0.61331   1.000 63.99317  ? 266 LEU B CD1   1 
ATOM   1446 C  CD2   . LEU A 1 187 ? 28.97674  3.84365   0.21551   1.000 65.06414  ? 266 LEU B CD2   1 
ATOM   1447 N  N     . ASP A 1 188 ? 26.60779  -0.56840  -1.30145  1.000 68.35029  ? 267 ASP B N     1 
ATOM   1448 C  CA    . ASP A 1 188 ? 25.22690  -0.97534  -1.06435  1.000 66.86049  ? 267 ASP B CA    1 
ATOM   1449 C  C     . ASP A 1 188 ? 24.94283  -0.87482  0.42987   1.000 70.16442  ? 267 ASP B C     1 
ATOM   1450 O  O     . ASP A 1 188 ? 25.47231  -1.66104  1.22329   1.000 66.10231  ? 267 ASP B O     1 
ATOM   1451 C  CB    . ASP A 1 188 ? 24.98459  -2.39096  -1.58260  1.000 68.07144  ? 267 ASP B CB    1 
ATOM   1452 C  CG    . ASP A 1 188 ? 23.51486  -2.68950  -1.80271  1.000 76.24403  ? 267 ASP B CG    1 
ATOM   1453 O  OD1   . ASP A 1 188 ? 22.67124  -2.08187  -1.11119  1.000 70.91456  ? 267 ASP B OD1   1 
ATOM   1454 O  OD2   . ASP A 1 188 ? 23.20287  -3.53284  -2.67167  1.000 84.07650  ? 267 ASP B OD2   1 
ATOM   1455 N  N     . LEU A 1 189 ? 24.10183  0.09167   0.80761   1.000 78.75543  ? 268 LEU B N     1 
ATOM   1456 C  CA    . LEU A 1 189 ? 23.73676  0.32779   2.20051   1.000 72.53967  ? 268 LEU B CA    1 
ATOM   1457 C  C     . LEU A 1 189 ? 22.23564  0.19414   2.42745   1.000 71.09950  ? 268 LEU B C     1 
ATOM   1458 O  O     . LEU A 1 189 ? 21.72414  0.66587   3.44770   1.000 81.51581  ? 268 LEU B O     1 
ATOM   1459 C  CB    . LEU A 1 189 ? 24.20339  1.71404   2.64900   1.000 66.05873  ? 268 LEU B CB    1 
ATOM   1460 C  CG    . LEU A 1 189 ? 25.56517  2.20058   2.15399   1.000 66.95809  ? 268 LEU B CG    1 
ATOM   1461 C  CD1   . LEU A 1 189 ? 25.73574  3.67810   2.45616   1.000 66.01425  ? 268 LEU B CD1   1 
ATOM   1462 C  CD2   . LEU A 1 189 ? 26.68072  1.39741   2.78320   1.000 61.18179  ? 268 LEU B CD2   1 
ATOM   1463 N  N     . GLN A 1 190 ? 21.51920  -0.43520  1.50015   1.000 70.78126  ? 269 GLN B N     1 
ATOM   1464 C  CA    . GLN A 1 190 ? 20.06719  -0.46593  1.57160   1.000 68.89549  ? 269 GLN B CA    1 
ATOM   1465 C  C     . GLN A 1 190 ? 19.59060  -1.37796  2.69940   1.000 69.43684  ? 269 GLN B C     1 
ATOM   1466 O  O     . GLN A 1 190 ? 20.31630  -2.25069  3.18307   1.000 74.96748  ? 269 GLN B O     1 
ATOM   1467 C  CB    . GLN A 1 190 ? 19.47348  -0.93055  0.24275   1.000 68.28529  ? 269 GLN B CB    1 
ATOM   1468 C  CG    . GLN A 1 190 ? 19.68290  -2.40439  -0.04328  1.000 67.79653  ? 269 GLN B CG    1 
ATOM   1469 C  CD    . GLN A 1 190 ? 19.12700  -2.81702  -1.38839  1.000 73.67569  ? 269 GLN B CD    1 
ATOM   1470 O  OE1   . GLN A 1 190 ? 17.92921  -3.05987  -1.52889  1.000 79.58169  ? 269 GLN B OE1   1 
ATOM   1471 N  NE2   . GLN A 1 190 ? 19.99563  -2.89354  -2.38930  1.000 68.69952  ? 269 GLN B NE2   1 
ATOM   1472 N  N     . HIS A 1 191 ? 18.34232  -1.15347  3.11626   1.000 72.94632  ? 270 HIS B N     1 
ATOM   1473 C  CA    . HIS A 1 191 ? 17.68185  -1.94373  4.15891   1.000 75.19781  ? 270 HIS B CA    1 
ATOM   1474 C  C     . HIS A 1 191 ? 18.49444  -1.96327  5.45468   1.000 76.98170  ? 270 HIS B C     1 
ATOM   1475 O  O     . HIS A 1 191 ? 18.75814  -3.01560  6.04069   1.000 72.12890  ? 270 HIS B O     1 
ATOM   1476 C  CB    . HIS A 1 191 ? 17.37961  -3.36017  3.66599   1.000 62.16568  ? 270 HIS B CB    1 
ATOM   1477 C  CG    . HIS A 1 191 ? 16.27055  -3.41750  2.66226   1.000 74.40530  ? 270 HIS B CG    1 
ATOM   1478 N  ND1   . HIS A 1 191 ? 14.94091  -3.43644  3.02423   1.000 71.04166  ? 270 HIS B ND1   1 
ATOM   1479 C  CD2   . HIS A 1 191 ? 16.29200  -3.44271  1.30851   1.000 77.27390  ? 270 HIS B CD2   1 
ATOM   1480 C  CE1   . HIS A 1 191 ? 14.19121  -3.47844  1.93747   1.000 76.34103  ? 270 HIS B CE1   1 
ATOM   1481 N  NE2   . HIS A 1 191 ? 14.98651  -3.48280  0.88288   1.000 77.91023  ? 270 HIS B NE2   1 
ATOM   1482 N  N     . ASN A 1 192 ? 18.88881  -0.77233  5.90263   1.000 74.66846  ? 271 ASN B N     1 
ATOM   1483 C  CA    . ASN A 1 192 ? 19.51702  -0.60576  7.20644   1.000 76.92213  ? 271 ASN B CA    1 
ATOM   1484 C  C     . ASN A 1 192 ? 18.69701  0.34844   8.06098   1.000 74.50143  ? 271 ASN B C     1 
ATOM   1485 O  O     . ASN A 1 192 ? 17.46651  0.37998   7.96344   1.000 91.42504  ? 271 ASN B O     1 
ATOM   1486 C  CB    . ASN A 1 192 ? 20.94845  -0.08641  7.06397   1.000 76.37736  ? 271 ASN B CB    1 
ATOM   1487 C  CG    . ASN A 1 192 ? 21.94510  -1.19226  6.81699   1.000 75.23978  ? 271 ASN B CG    1 
ATOM   1488 O  OD1   . ASN A 1 192 ? 22.56255  -1.70271  7.75059   1.000 74.24065  ? 271 ASN B OD1   1 
ATOM   1489 N  ND2   . ASN A 1 192 ? 22.10921  -1.57187  5.55551   1.000 77.00077  ? 271 ASN B ND2   1 
ATOM   1490 N  N     . GLU A 1 193 ? 19.37173  1.13262   8.89590   1.000 78.12298  ? 272 GLU B N     1 
ATOM   1491 C  CA    . GLU A 1 193 ? 18.72220  2.09831   9.77314   1.000 81.46264  ? 272 GLU B CA    1 
ATOM   1492 C  C     . GLU A 1 193 ? 19.54470  3.37340   9.83870   1.000 81.93220  ? 272 GLU B C     1 
ATOM   1493 O  O     . GLU A 1 193 ? 19.65816  4.00969   10.89192  1.000 83.25148  ? 272 GLU B O     1 
ATOM   1494 C  CB    . GLU A 1 193 ? 18.51238  1.51873   11.17107  1.000 85.33657  ? 272 GLU B CB    1 
ATOM   1495 C  CG    . GLU A 1 193 ? 17.52399  0.36733   11.22306  1.000 81.83802  ? 272 GLU B CG    1 
ATOM   1496 C  CD    . GLU A 1 193 ? 17.51900  -0.33668  12.56335  1.000 98.54983  ? 272 GLU B CD    1 
ATOM   1497 O  OE1   . GLU A 1 193 ? 18.41525  -0.05891  13.38945  1.000 103.03531 ? 272 GLU B OE1   1 
ATOM   1498 O  OE2   . GLU A 1 193 ? 16.61750  -1.17003  12.79029  1.000 109.55403 ? 272 GLU B OE2   1 
ATOM   1499 N  N     . LEU A 1 194 ? 20.14253  3.75144   8.71191   1.000 73.46571  ? 273 LEU B N     1 
ATOM   1500 C  CA    . LEU A 1 194 ? 21.03632  4.90040   8.67912   1.000 82.04273  ? 273 LEU B CA    1 
ATOM   1501 C  C     . LEU A 1 194 ? 20.27091  6.18711   8.95932   1.000 91.45271  ? 273 LEU B C     1 
ATOM   1502 O  O     . LEU A 1 194 ? 19.25553  6.47153   8.31740   1.000 86.58579  ? 273 LEU B O     1 
ATOM   1503 C  CB    . LEU A 1 194 ? 21.72967  4.98734   7.32121   1.000 72.34193  ? 273 LEU B CB    1 
ATOM   1504 C  CG    . LEU A 1 194 ? 22.64308  3.81965   6.95670   1.000 80.41703  ? 273 LEU B CG    1 
ATOM   1505 C  CD1   . LEU A 1 194 ? 23.16882  3.97839   5.53886   1.000 79.66360  ? 273 LEU B CD1   1 
ATOM   1506 C  CD2   . LEU A 1 194 ? 23.78895  3.72140   7.94977   1.000 80.00714  ? 273 LEU B CD2   1 
ATOM   1507 N  N     . LEU A 1 195 ? 20.76158  6.96515   9.92278   1.000 84.10911  ? 274 LEU B N     1 
ATOM   1508 C  CA    . LEU A 1 195 ? 20.16975  8.26003   10.23157  1.000 85.39870  ? 274 LEU B CA    1 
ATOM   1509 C  C     . LEU A 1 195 ? 20.79134  9.38958   9.42199   1.000 86.71971  ? 274 LEU B C     1 
ATOM   1510 O  O     . LEU A 1 195 ? 20.13536  10.41271  9.19140   1.000 85.70075  ? 274 LEU B O     1 
ATOM   1511 C  CB    . LEU A 1 195 ? 20.30764  8.55756   11.72800  1.000 81.54924  ? 274 LEU B CB    1 
ATOM   1512 C  CG    . LEU A 1 195 ? 19.72152  7.50732   12.67602  1.000 79.96769  ? 274 LEU B CG    1 
ATOM   1513 C  CD1   . LEU A 1 195 ? 20.07854  7.81822   14.11719  1.000 87.76061  ? 274 LEU B CD1   1 
ATOM   1514 C  CD2   . LEU A 1 195 ? 18.21611  7.41211   12.51021  1.000 85.62142  ? 274 LEU B CD2   1 
ATOM   1515 N  N     . ASP A 1 196 ? 22.03562  9.22377   8.98343   1.000 85.42676  ? 275 ASP B N     1 
ATOM   1516 C  CA    . ASP A 1 196 ? 22.71614  10.21329  8.15831   1.000 89.55540  ? 275 ASP B CA    1 
ATOM   1517 C  C     . ASP A 1 196 ? 23.80949  9.50494   7.36784   1.000 91.72729  ? 275 ASP B C     1 
ATOM   1518 O  O     . ASP A 1 196 ? 24.01864  8.29642   7.50301   1.000 97.75519  ? 275 ASP B O     1 
ATOM   1519 C  CB    . ASP A 1 196 ? 23.28645  11.35371  9.00936   1.000 93.44023  ? 275 ASP B CB    1 
ATOM   1520 C  CG    . ASP A 1 196 ? 24.23590  10.86294  10.08965  1.000 101.20350 ? 275 ASP B CG    1 
ATOM   1521 O  OD1   . ASP A 1 196 ? 25.34477  10.39540  9.75188   1.000 100.38897 ? 275 ASP B OD1   1 
ATOM   1522 O  OD2   . ASP A 1 196 ? 23.87427  10.95137  11.28199  1.000 108.66464 ? 275 ASP B OD2   1 
ATOM   1523 N  N     . LEU A 1 197 ? 24.51011  10.27395  6.53750   1.000 85.56284  ? 276 LEU B N     1 
ATOM   1524 C  CA    . LEU A 1 197 ? 25.62841  9.77632   5.75629   1.000 83.02095  ? 276 LEU B CA    1 
ATOM   1525 C  C     . LEU A 1 197 ? 26.83559  10.67924  5.96237   1.000 85.53057  ? 276 LEU B C     1 
ATOM   1526 O  O     . LEU A 1 197 ? 26.68757  11.90409  6.04968   1.000 96.15533  ? 276 LEU B O     1 
ATOM   1527 C  CB    . LEU A 1 197 ? 25.27951  9.71224   4.26274   1.000 81.28372  ? 276 LEU B CB    1 
ATOM   1528 C  CG    . LEU A 1 197 ? 24.40987  8.53930   3.81341   1.000 86.74622  ? 276 LEU B CG    1 
ATOM   1529 C  CD1   . LEU A 1 197 ? 23.72363  8.86659   2.49988   1.000 83.16924  ? 276 LEU B CD1   1 
ATOM   1530 C  CD2   . LEU A 1 197 ? 25.25171  7.28118   3.67690   1.000 82.56210  ? 276 LEU B CD2   1 
ATOM   1531 N  N     . PRO A 1 198 ? 28.03524  10.11144  6.04659   1.000 82.58350  ? 277 PRO B N     1 
ATOM   1532 C  CA    . PRO A 1 198 ? 29.22779  10.94373  6.22196   1.000 85.21184  ? 277 PRO B CA    1 
ATOM   1533 C  C     . PRO A 1 198 ? 29.47048  11.82523  5.00916   1.000 86.09131  ? 277 PRO B C     1 
ATOM   1534 O  O     . PRO A 1 198 ? 29.21054  11.44001  3.86706   1.000 88.68420  ? 277 PRO B O     1 
ATOM   1535 C  CB    . PRO A 1 198 ? 30.35325  9.91819   6.39922   1.000 91.47976  ? 277 PRO B CB    1 
ATOM   1536 C  CG    . PRO A 1 198 ? 29.84727  8.68997   5.71702   1.000 84.67701  ? 277 PRO B CG    1 
ATOM   1537 C  CD    . PRO A 1 198 ? 28.36703  8.67959   5.96687   1.000 86.40479  ? 277 PRO B CD    1 
ATOM   1538 N  N     . ASP A 1 199 ? 29.97280  13.03255  5.27513   1.000 87.61067  ? 278 ASP B N     1 
ATOM   1539 C  CA    . ASP A 1 199 ? 30.27739  13.96568  4.19804   1.000 86.65861  ? 278 ASP B CA    1 
ATOM   1540 C  C     . ASP A 1 199 ? 31.41537  13.47766  3.31209   1.000 92.37048  ? 278 ASP B C     1 
ATOM   1541 O  O     . ASP A 1 199 ? 31.49548  13.88690  2.14911   1.000 91.25541  ? 278 ASP B O     1 
ATOM   1542 C  CB    . ASP A 1 199 ? 30.61887  15.33926  4.77506   1.000 93.22357  ? 278 ASP B CB    1 
ATOM   1543 C  CG    . ASP A 1 199 ? 29.44879  15.97294  5.50285   1.000 101.36131 ? 278 ASP B CG    1 
ATOM   1544 O  OD1   . ASP A 1 199 ? 28.33257  15.41274  5.44446   1.000 91.58682  ? 278 ASP B OD1   1 
ATOM   1545 O  OD2   . ASP A 1 199 ? 29.64663  17.03148  6.13548   1.000 108.73862 ? 278 ASP B OD2   1 
ATOM   1546 N  N     . THR A 1 200 ? 32.28745  12.60796  3.82674   1.000 85.88461  ? 279 THR B N     1 
ATOM   1547 C  CA    . THR A 1 200 ? 33.39547  12.07854  3.03919   1.000 93.33024  ? 279 THR B CA    1 
ATOM   1548 C  C     . THR A 1 200 ? 32.94347  11.15623  1.91348   1.000 98.94333  ? 279 THR B C     1 
ATOM   1549 O  O     . THR A 1 200 ? 33.79839  10.65980  1.17024   1.000 95.60802  ? 279 THR B O     1 
ATOM   1550 C  CB    . THR A 1 200 ? 34.38092  11.33386  3.94456   1.000 100.89771 ? 279 THR B CB    1 
ATOM   1551 O  OG1   . THR A 1 200 ? 33.66375  10.44207  4.80778   1.000 99.43746  ? 279 THR B OG1   1 
ATOM   1552 C  CG2   . THR A 1 200 ? 35.18601  12.31540  4.78419   1.000 94.68938  ? 279 THR B CG2   1 
ATOM   1553 N  N     . ILE A 1 201 ? 31.63702  10.91866  1.76275   1.000 95.76722  ? 280 ILE B N     1 
ATOM   1554 C  CA    . ILE A 1 201 ? 31.14487  10.06798  0.68658   1.000 87.54091  ? 280 ILE B CA    1 
ATOM   1555 C  C     . ILE A 1 201 ? 31.45649  10.66790  -0.67693  1.000 94.22169  ? 280 ILE B C     1 
ATOM   1556 O  O     . ILE A 1 201 ? 31.47662  9.94836   -1.68187  1.000 96.68430  ? 280 ILE B O     1 
ATOM   1557 C  CB    . ILE A 1 201 ? 29.63075  9.81845   0.86122   1.000 91.39216  ? 280 ILE B CB    1 
ATOM   1558 C  CG1   . ILE A 1 201 ? 29.18421  8.60130   0.04836   1.000 89.75900  ? 280 ILE B CG1   1 
ATOM   1559 C  CG2   . ILE A 1 201 ? 28.83002  11.05230  0.46594   1.000 87.72155  ? 280 ILE B CG2   1 
ATOM   1560 C  CD1   . ILE A 1 201 ? 27.72208  8.25279   0.22873   1.000 82.40994  ? 280 ILE B CD1   1 
ATOM   1561 N  N     . GLY A 1 202 ? 31.71691  11.97458  -0.73580  1.000 92.23670  ? 281 GLY B N     1 
ATOM   1562 C  CA    . GLY A 1 202 ? 32.11401  12.61522  -1.97566  1.000 95.46155  ? 281 GLY B CA    1 
ATOM   1563 C  C     . GLY A 1 202 ? 33.51292  12.27055  -2.44275  1.000 98.20143  ? 281 GLY B C     1 
ATOM   1564 O  O     . GLY A 1 202 ? 33.87867  12.64112  -3.56391  1.000 90.37400  ? 281 GLY B O     1 
ATOM   1565 N  N     . ASN A 1 203 ? 34.30316  11.58069  -1.61591  1.000 88.06423  ? 282 ASN B N     1 
ATOM   1566 C  CA    . ASN A 1 203 ? 35.62446  11.15658  -2.06303  1.000 93.30332  ? 282 ASN B CA    1 
ATOM   1567 C  C     . ASN A 1 203 ? 35.53546  9.98045   -3.02475  1.000 91.63300  ? 282 ASN B C     1 
ATOM   1568 O  O     . ASN A 1 203 ? 36.39231  9.83428   -3.90418  1.000 95.64244  ? 282 ASN B O     1 
ATOM   1569 C  CB    . ASN A 1 203 ? 36.50334  10.79103  -0.86758  1.000 100.59414 ? 282 ASN B CB    1 
ATOM   1570 C  CG    . ASN A 1 203 ? 36.64861  11.92710  0.12053   1.000 108.43231 ? 282 ASN B CG    1 
ATOM   1571 O  OD1   . ASN A 1 203 ? 36.35378  13.08157  -0.19244  1.000 116.67660 ? 282 ASN B OD1   1 
ATOM   1572 N  ND2   . ASN A 1 203 ? 37.11052  11.60627  1.32382   1.000 105.70922 ? 282 ASN B ND2   1 
ATOM   1573 N  N     . LEU A 1 204 ? 34.51641  9.13515   -2.87699  1.000 85.40084  ? 283 LEU B N     1 
ATOM   1574 C  CA    . LEU A 1 204 ? 34.34381  8.00212   -3.77536  1.000 84.33577  ? 283 LEU B CA    1 
ATOM   1575 C  C     . LEU A 1 204 ? 33.96240  8.50140   -5.16144  1.000 85.23916  ? 283 LEU B C     1 
ATOM   1576 O  O     . LEU A 1 204 ? 32.80937  8.36951   -5.58175  1.000 89.32551  ? 283 LEU B O     1 
ATOM   1577 C  CB    . LEU A 1 204 ? 33.28398  7.04250   -3.23497  1.000 87.74905  ? 283 LEU B CB    1 
ATOM   1578 C  CG    . LEU A 1 204 ? 33.38588  6.69189   -1.75086  1.000 68.27115  ? 283 LEU B CG    1 
ATOM   1579 C  CD1   . LEU A 1 204 ? 32.30808  5.69223   -1.37625  1.000 71.76775  ? 283 LEU B CD1   1 
ATOM   1580 C  CD2   . LEU A 1 204 ? 34.76471  6.15236   -1.41478  1.000 81.25169  ? 283 LEU B CD2   1 
ATOM   1581 N  N     . SER A 1 205 ? 34.92459  9.09015   -5.87344  1.000 91.11157  ? 284 SER B N     1 
ATOM   1582 C  CA    . SER A 1 205 ? 34.63602  9.67061   -7.17809  1.000 84.86157  ? 284 SER B CA    1 
ATOM   1583 C  C     . SER A 1 205 ? 34.32169  8.61408   -8.22690  1.000 85.06619  ? 284 SER B C     1 
ATOM   1584 O  O     . SER A 1 205 ? 33.67376  8.93175   -9.22969  1.000 93.09425  ? 284 SER B O     1 
ATOM   1585 C  CB    . SER A 1 205 ? 35.81070  10.53211  -7.64008  1.000 80.86180  ? 284 SER B CB    1 
ATOM   1586 O  OG    . SER A 1 205 ? 37.00247  9.77042   -7.70363  1.000 94.76425  ? 284 SER B OG    1 
ATOM   1587 N  N     . SER A 1 206 ? 34.76388  7.37483   -8.02566  1.000 81.53221  ? 285 SER B N     1 
ATOM   1588 C  CA    . SER A 1 206 ? 34.42975  6.28361   -8.92969  1.000 83.60634  ? 285 SER B CA    1 
ATOM   1589 C  C     . SER A 1 206 ? 33.11836  5.60024   -8.57045  1.000 79.85008  ? 285 SER B C     1 
ATOM   1590 O  O     . SER A 1 206 ? 32.71625  4.66048   -9.26484  1.000 73.75614  ? 285 SER B O     1 
ATOM   1591 C  CB    . SER A 1 206 ? 35.55726  5.24868   -8.95549  1.000 73.02512  ? 285 SER B CB    1 
ATOM   1592 O  OG    . SER A 1 206 ? 36.65005  5.71657   -9.72481  1.000 92.00085  ? 285 SER B OG    1 
ATOM   1593 N  N     . LEU A 1 207 ? 32.44760  6.04461   -7.51163  1.000 69.21077  ? 286 LEU B N     1 
ATOM   1594 C  CA    . LEU A 1 207 ? 31.17778  5.44863   -7.12302  1.000 75.15280  ? 286 LEU B CA    1 
ATOM   1595 C  C     . LEU A 1 207 ? 30.14863  5.63048   -8.23083  1.000 78.88959  ? 286 LEU B C     1 
ATOM   1596 O  O     . LEU A 1 207 ? 29.81361  6.76115   -8.59791  1.000 87.67485  ? 286 LEU B O     1 
ATOM   1597 C  CB    . LEU A 1 207 ? 30.68245  6.08073   -5.82456  1.000 76.25176  ? 286 LEU B CB    1 
ATOM   1598 C  CG    . LEU A 1 207 ? 29.39519  5.50177   -5.24151  1.000 75.85384  ? 286 LEU B CG    1 
ATOM   1599 C  CD1   . LEU A 1 207 ? 29.63531  4.09277   -4.71935  1.000 65.19136  ? 286 LEU B CD1   1 
ATOM   1600 C  CD2   . LEU A 1 207 ? 28.85189  6.40625   -4.14850  1.000 69.49321  ? 286 LEU B CD2   1 
ATOM   1601 N  N     . SER A 1 208 ? 29.65455  4.51168   -8.76972  1.000 63.28177  ? 287 SER B N     1 
ATOM   1602 C  CA    . SER A 1 208 ? 28.63939  4.53153   -9.81287  1.000 70.64023  ? 287 SER B CA    1 
ATOM   1603 C  C     . SER A 1 208 ? 27.29938  3.95008   -9.38627  1.000 72.73040  ? 287 SER B C     1 
ATOM   1604 O  O     . SER A 1 208 ? 26.28471  4.26442   -10.01766 1.000 79.24354  ? 287 SER B O     1 
ATOM   1605 C  CB    . SER A 1 208 ? 29.12748  3.76902   -11.05612 1.000 74.70998  ? 287 SER B CB    1 
ATOM   1606 O  OG    . SER A 1 208 ? 29.33398  2.39564   -10.77120 1.000 67.38903  ? 287 SER B OG    1 
ATOM   1607 N  N     . ARG A 1 209 ? 27.26159  3.11996   -8.34717  1.000 67.94160  ? 288 ARG B N     1 
ATOM   1608 C  CA    . ARG A 1 209 ? 26.02793  2.50812   -7.86918  1.000 61.27955  ? 288 ARG B CA    1 
ATOM   1609 C  C     . ARG A 1 209 ? 25.98712  2.64411   -6.35504  1.000 69.48963  ? 288 ARG B C     1 
ATOM   1610 O  O     . ARG A 1 209 ? 26.91110  2.19980   -5.66547  1.000 68.08707  ? 288 ARG B O     1 
ATOM   1611 C  CB    . ARG A 1 209 ? 25.94680  1.03815   -8.29544  1.000 61.25645  ? 288 ARG B CB    1 
ATOM   1612 C  CG    . ARG A 1 209 ? 24.66478  0.31775   -7.90896  1.000 65.06483  ? 288 ARG B CG    1 
ATOM   1613 C  CD    . ARG A 1 209 ? 24.65248  -1.09888  -8.47426  1.000 66.77817  ? 288 ARG B CD    1 
ATOM   1614 N  NE    . ARG A 1 209 ? 23.42791  -1.81697  -8.14175  1.000 66.00486  ? 288 ARG B NE    1 
ATOM   1615 C  CZ    . ARG A 1 209 ? 23.24895  -2.51283  -7.02717  1.000 79.46179  ? 288 ARG B CZ    1 
ATOM   1616 N  NH1   . ARG A 1 209 ? 24.20357  -2.61625  -6.11530  1.000 67.70241  ? 288 ARG B NH1   1 
ATOM   1617 N  NH2   . ARG A 1 209 ? 22.08165  -3.11659  -6.81957  1.000 81.20569  ? 288 ARG B NH2   1 
ATOM   1618 N  N     . LEU A 1 210 ? 24.92731  3.26466   -5.83973  1.000 62.97368  ? 289 LEU B N     1 
ATOM   1619 C  CA    . LEU A 1 210 ? 24.80489  3.55242   -4.41345  1.000 68.92296  ? 289 LEU B CA    1 
ATOM   1620 C  C     . LEU A 1 210 ? 23.41314  3.15261   -3.94606  1.000 69.55828  ? 289 LEU B C     1 
ATOM   1621 O  O     . LEU A 1 210 ? 22.41832  3.75948   -4.35556  1.000 73.16105  ? 289 LEU B O     1 
ATOM   1622 C  CB    . LEU A 1 210 ? 25.07213  5.03061   -4.12521  1.000 67.80818  ? 289 LEU B CB    1 
ATOM   1623 C  CG    . LEU A 1 210 ? 24.91042  5.48308   -2.67220  1.000 63.84166  ? 289 LEU B CG    1 
ATOM   1624 C  CD1   . LEU A 1 210 ? 25.84867  4.71197   -1.74905  1.000 73.34484  ? 289 LEU B CD1   1 
ATOM   1625 C  CD2   . LEU A 1 210 ? 25.14573  6.98067   -2.54941  1.000 68.70568  ? 289 LEU B CD2   1 
ATOM   1626 N  N     . GLY A 1 211 ? 23.34548  2.14245   -3.08435  1.000 60.65378  ? 290 GLY B N     1 
ATOM   1627 C  CA    . GLY A 1 211 ? 22.07683  1.69328   -2.55126  1.000 61.51549  ? 290 GLY B CA    1 
ATOM   1628 C  C     . GLY A 1 211 ? 21.75614  2.32957   -1.21697  1.000 73.22062  ? 290 GLY B C     1 
ATOM   1629 O  O     . GLY A 1 211 ? 22.40473  2.03305   -0.20977  1.000 74.02126  ? 290 GLY B O     1 
ATOM   1630 N  N     . LEU A 1 212 ? 20.75720  3.20968   -1.19457  1.000 80.08610  ? 291 LEU B N     1 
ATOM   1631 C  CA    . LEU A 1 212 ? 20.37958  3.91443   0.02035   1.000 73.47624  ? 291 LEU B CA    1 
ATOM   1632 C  C     . LEU A 1 212 ? 18.94544  3.65924   0.44909   1.000 68.28970  ? 291 LEU B C     1 
ATOM   1633 O  O     . LEU A 1 212 ? 18.53051  4.17921   1.49091   1.000 70.49241  ? 291 LEU B O     1 
ATOM   1634 C  CB    . LEU A 1 212 ? 20.57957  5.42554   -0.15217  1.000 69.34175  ? 291 LEU B CB    1 
ATOM   1635 C  CG    . LEU A 1 212 ? 21.99560  5.90504   -0.45280  1.000 70.46772  ? 291 LEU B CG    1 
ATOM   1636 C  CD1   . LEU A 1 212 ? 22.01296  7.41888   -0.57845  1.000 71.09528  ? 291 LEU B CD1   1 
ATOM   1637 C  CD2   . LEU A 1 212 ? 22.95277  5.43876   0.62957   1.000 74.23050  ? 291 LEU B CD2   1 
ATOM   1638 N  N     . ARG A 1 213 ? 18.17775  2.88282   -0.30969  1.000 74.61907  ? 292 ARG B N     1 
ATOM   1639 C  CA    . ARG A 1 213 ? 16.75207  2.78432   -0.03993  1.000 68.18217  ? 292 ARG B CA    1 
ATOM   1640 C  C     . ARG A 1 213 ? 16.48440  1.97622   1.22476   1.000 72.63156  ? 292 ARG B C     1 
ATOM   1641 O  O     . ARG A 1 213 ? 17.28305  1.12884   1.63173   1.000 78.04088  ? 292 ARG B O     1 
ATOM   1642 C  CB    . ARG A 1 213 ? 16.01552  2.17036   -1.23087  1.000 72.85386  ? 292 ARG B CB    1 
ATOM   1643 C  CG    . ARG A 1 213 ? 16.30671  0.70795   -1.51136  1.000 71.38311  ? 292 ARG B CG    1 
ATOM   1644 C  CD    . ARG A 1 213 ? 15.20889  0.14562   -2.40171  1.000 70.55398  ? 292 ARG B CD    1 
ATOM   1645 N  NE    . ARG A 1 213 ? 15.69044  -0.84911  -3.35204  1.000 75.85982  ? 292 ARG B NE    1 
ATOM   1646 C  CZ    . ARG A 1 213 ? 15.48102  -2.15386  -3.24408  1.000 85.71127  ? 292 ARG B CZ    1 
ATOM   1647 N  NH1   . ARG A 1 213 ? 14.81858  -2.66527  -2.21934  1.000 92.14443  ? 292 ARG B NH1   1 
ATOM   1648 N  NH2   . ARG A 1 213 ? 15.94247  -2.96559  -4.19139  1.000 89.57545  ? 292 ARG B NH2   1 
ATOM   1649 N  N     . TYR A 1 214 ? 15.34556  2.27043   1.85420   1.000 74.61699  ? 293 TYR B N     1 
ATOM   1650 C  CA    . TYR A 1 214 ? 14.90746  1.62857   3.09391   1.000 76.85651  ? 293 TYR B CA    1 
ATOM   1651 C  C     . TYR A 1 214 ? 15.90546  1.86928   4.22972   1.000 78.69784  ? 293 TYR B C     1 
ATOM   1652 O  O     . TYR A 1 214 ? 16.53550  0.95355   4.76069   1.000 71.81475  ? 293 TYR B O     1 
ATOM   1653 C  CB    . TYR A 1 214 ? 14.63470  0.13670   2.87415   1.000 66.20567  ? 293 TYR B CB    1 
ATOM   1654 C  CG    . TYR A 1 214 ? 13.29410  -0.09296  2.21790   1.000 81.22337  ? 293 TYR B CG    1 
ATOM   1655 C  CD1   . TYR A 1 214 ? 13.17044  -0.12580  0.83484   1.000 83.60299  ? 293 TYR B CD1   1 
ATOM   1656 C  CD2   . TYR A 1 214 ? 12.14335  -0.23555  2.98283   1.000 82.60248  ? 293 TYR B CD2   1 
ATOM   1657 C  CE1   . TYR A 1 214 ? 11.93802  -0.31649  0.23151   1.000 93.81534  ? 293 TYR B CE1   1 
ATOM   1658 C  CE2   . TYR A 1 214 ? 10.90914  -0.42585  2.39047   1.000 89.99539  ? 293 TYR B CE2   1 
ATOM   1659 C  CZ    . TYR A 1 214 ? 10.81143  -0.46535  1.01538   1.000 95.78681  ? 293 TYR B CZ    1 
ATOM   1660 O  OH    . TYR A 1 214 ? 9.58393   -0.65576  0.42438   1.000 92.08653  ? 293 TYR B OH    1 
ATOM   1661 N  N     . ASN A 1 215 ? 16.02799  3.14326   4.59696   1.000 77.94542  ? 294 ASN B N     1 
ATOM   1662 C  CA    . ASN A 1 215 ? 16.79569  3.55162   5.76531   1.000 76.57491  ? 294 ASN B CA    1 
ATOM   1663 C  C     . ASN A 1 215 ? 15.97656  4.53247   6.59248   1.000 76.22003  ? 294 ASN B C     1 
ATOM   1664 O  O     . ASN A 1 215 ? 14.74331  4.46931   6.59827   1.000 86.01217  ? 294 ASN B O     1 
ATOM   1665 C  CB    . ASN A 1 215 ? 18.12891  4.18073   5.35217   1.000 80.26778  ? 294 ASN B CB    1 
ATOM   1666 C  CG    . ASN A 1 215 ? 19.15884  3.14867   4.93501   1.000 79.59265  ? 294 ASN B CG    1 
ATOM   1667 O  OD1   . ASN A 1 215 ? 19.32944  2.12811   5.59523   1.000 75.63004  ? 294 ASN B OD1   1 
ATOM   1668 N  ND2   . ASN A 1 215 ? 19.85200  3.41244   3.83373   1.000 76.56781  ? 294 ASN B ND2   1 
ATOM   1669 N  N     . ARG A 1 216 ? 16.65282  5.44049   7.29479   1.000 77.15874  ? 295 ARG B N     1 
ATOM   1670 C  CA    . ARG A 1 216 ? 16.00001  6.49217   8.06501   1.000 81.59274  ? 295 ARG B CA    1 
ATOM   1671 C  C     . ARG A 1 216 ? 16.66489  7.83785   7.80224   1.000 85.35502  ? 295 ARG B C     1 
ATOM   1672 O  O     . ARG A 1 216 ? 16.73023  8.69221   8.69086   1.000 83.84843  ? 295 ARG B O     1 
ATOM   1673 C  CB    . ARG A 1 216 ? 16.01383  6.16594   9.55831   1.000 82.80649  ? 295 ARG B CB    1 
ATOM   1674 C  CG    . ARG A 1 216 ? 15.42996  4.80378   9.89448   1.000 86.04586  ? 295 ARG B CG    1 
ATOM   1675 C  CD    . ARG A 1 216 ? 15.69166  4.42411   11.34097  1.000 95.42240  ? 295 ARG B CD    1 
ATOM   1676 N  NE    . ARG A 1 216 ? 15.45457  3.00436   11.57264  1.000 103.82251 ? 295 ARG B NE    1 
ATOM   1677 C  CZ    . ARG A 1 216 ? 14.31976  2.49688   12.03333  1.000 105.01739 ? 295 ARG B CZ    1 
ATOM   1678 N  NH1   . ARG A 1 216 ? 13.29072  3.27008   12.34040  1.000 112.97869 ? 295 ARG B NH1   1 
ATOM   1679 N  NH2   . ARG A 1 216 ? 14.21527  1.18027   12.19120  1.000 106.83082 ? 295 ARG B NH2   1 
ATOM   1680 N  N     . LEU A 1 217 ? 17.16589  8.03284   6.58448   1.000 77.70321  ? 296 LEU B N     1 
ATOM   1681 C  CA    . LEU A 1 217 ? 17.90521  9.24250   6.25286   1.000 85.47872  ? 296 LEU B CA    1 
ATOM   1682 C  C     . LEU A 1 217 ? 16.99449  10.46278  6.26726   1.000 91.91058  ? 296 LEU B C     1 
ATOM   1683 O  O     . LEU A 1 217 ? 15.85397  10.41557  5.79876   1.000 89.87588  ? 296 LEU B O     1 
ATOM   1684 C  CB    . LEU A 1 217 ? 18.55895  9.10380   4.87897   1.000 82.30888  ? 296 LEU B CB    1 
ATOM   1685 C  CG    . LEU A 1 217 ? 19.61395  8.01026   4.73075   1.000 84.24688  ? 296 LEU B CG    1 
ATOM   1686 C  CD1   . LEU A 1 217 ? 20.13361  7.97034   3.30503   1.000 85.74968  ? 296 LEU B CD1   1 
ATOM   1687 C  CD2   . LEU A 1 217 ? 20.74889  8.23916   5.71408   1.000 85.80819  ? 296 LEU B CD2   1 
ATOM   1688 N  N     . SER A 1 218 ? 17.51150  11.56668  6.80451   1.000 89.94313  ? 297 SER B N     1 
ATOM   1689 C  CA    . SER A 1 218 ? 16.79086  12.82911  6.81808   1.000 89.41318  ? 297 SER B CA    1 
ATOM   1690 C  C     . SER A 1 218 ? 17.34154  13.84383  5.82808   1.000 87.63003  ? 297 SER B C     1 
ATOM   1691 O  O     . SER A 1 218 ? 16.69943  14.87664  5.60847   1.000 90.48099  ? 297 SER B O     1 
ATOM   1692 C  CB    . SER A 1 218 ? 16.80582  13.43633  8.22898   1.000 87.33519  ? 297 SER B CB    1 
ATOM   1693 O  OG    . SER A 1 218 ? 16.30678  12.51330  9.18299   1.000 97.65758  ? 297 SER B OG    1 
ATOM   1694 N  N     . ALA A 1 219 ? 18.50072  13.58001  5.22767   1.000 84.40595  ? 298 ALA B N     1 
ATOM   1695 C  CA    . ALA A 1 219 ? 19.09460  14.48833  4.25700   1.000 79.77081  ? 298 ALA B CA    1 
ATOM   1696 C  C     . ALA A 1 219 ? 20.17425  13.74748  3.48363   1.000 92.03885  ? 298 ALA B C     1 
ATOM   1697 O  O     . ALA A 1 219 ? 20.62826  12.67301  3.88659   1.000 100.26515 ? 298 ALA B O     1 
ATOM   1698 C  CB    . ALA A 1 219 ? 19.67939  15.73453  4.93017   1.000 74.76169  ? 298 ALA B CB    1 
ATOM   1699 N  N     . ILE A 1 220 ? 20.57821  14.33957  2.37056   1.000 90.06832  ? 299 ILE B N     1 
ATOM   1700 C  CA    . ILE A 1 220 ? 21.65136  13.82225  1.52390   1.000 79.54550  ? 299 ILE B CA    1 
ATOM   1701 C  C     . ILE A 1 220 ? 22.81009  14.80657  1.58261   1.000 89.64035  ? 299 ILE B C     1 
ATOM   1702 O  O     . ILE A 1 220 ? 22.59341  16.01073  1.40204   1.000 90.32660  ? 299 ILE B O     1 
ATOM   1703 C  CB    . ILE A 1 220 ? 21.18594  13.61892  0.06906   1.000 83.69602  ? 299 ILE B CB    1 
ATOM   1704 C  CG1   . ILE A 1 220 ? 20.08081  12.56074  0.00056   1.000 83.88578  ? 299 ILE B CG1   1 
ATOM   1705 C  CG2   . ILE A 1 220 ? 22.35913  13.24576  -0.82139  1.000 71.07083  ? 299 ILE B CG2   1 
ATOM   1706 C  CD1   . ILE A 1 220 ? 20.49154  11.20739  0.53723   1.000 72.53714  ? 299 ILE B CD1   1 
ATOM   1707 N  N     . PRO A 1 221 ? 24.03649  14.35496  1.84294   1.000 87.35583  ? 300 PRO B N     1 
ATOM   1708 C  CA    . PRO A 1 221 ? 25.16871  15.28695  1.87947   1.000 92.45154  ? 300 PRO B CA    1 
ATOM   1709 C  C     . PRO A 1 221 ? 25.36933  15.96308  0.53155   1.000 88.33149  ? 300 PRO B C     1 
ATOM   1710 O  O     . PRO A 1 221 ? 25.28012  15.32850  -0.52104  1.000 87.22693  ? 300 PRO B O     1 
ATOM   1711 C  CB    . PRO A 1 221 ? 26.35743  14.38815  2.24067   1.000 90.83573  ? 300 PRO B CB    1 
ATOM   1712 C  CG    . PRO A 1 221 ? 25.74809  13.19288  2.89769   1.000 87.15798  ? 300 PRO B CG    1 
ATOM   1713 C  CD    . PRO A 1 221 ? 24.43385  12.98521  2.20896   1.000 87.42166  ? 300 PRO B CD    1 
ATOM   1714 N  N     . ARG A 1 222 ? 25.63882  17.27113  0.57198   1.000 94.07477  ? 301 ARG B N     1 
ATOM   1715 C  CA    . ARG A 1 222 ? 25.89903  18.00418  -0.66152  1.000 97.63597  ? 301 ARG B CA    1 
ATOM   1716 C  C     . ARG A 1 222 ? 27.10365  17.44571  -1.40448  1.000 94.92359  ? 301 ARG B C     1 
ATOM   1717 O  O     . ARG A 1 222 ? 27.18793  17.58797  -2.62954  1.000 94.75789  ? 301 ARG B O     1 
ATOM   1718 C  CB    . ARG A 1 222 ? 26.11194  19.49272  -0.37017  1.000 99.35554  ? 301 ARG B CB    1 
ATOM   1719 C  CG    . ARG A 1 222 ? 25.95502  20.37619  -1.60171  1.000 112.25381 ? 301 ARG B CG    1 
ATOM   1720 C  CD    . ARG A 1 222 ? 26.93558  21.54306  -1.62145  1.000 121.44352 ? 301 ARG B CD    1 
ATOM   1721 N  NE    . ARG A 1 222 ? 26.35275  22.78027  -1.11471  1.000 132.15201 ? 301 ARG B NE    1 
ATOM   1722 C  CZ    . ARG A 1 222 ? 26.80819  23.45191  -0.06565  1.000 138.80404 ? 301 ARG B CZ    1 
ATOM   1723 N  NH1   . ARG A 1 222 ? 27.86627  23.03920  0.61412   1.000 124.06679 ? 301 ARG B NH1   1 
ATOM   1724 N  NH2   . ARG A 1 222 ? 26.19240  24.57154  0.30472   1.000 135.35884 ? 301 ARG B NH2   1 
ATOM   1725 N  N     . SER A 1 223 ? 28.02861  16.80040  -0.69112  1.000 101.23557 ? 302 SER B N     1 
ATOM   1726 C  CA    . SER A 1 223 ? 29.21577  16.22710  -1.31044  1.000 102.14235 ? 302 SER B CA    1 
ATOM   1727 C  C     . SER A 1 223 ? 28.89780  15.07201  -2.25051  1.000 97.42410  ? 302 SER B C     1 
ATOM   1728 O  O     . SER A 1 223 ? 29.78345  14.65198  -3.00306  1.000 96.69051  ? 302 SER B O     1 
ATOM   1729 C  CB    . SER A 1 223 ? 30.19148  15.76049  -0.22986  1.000 95.27548  ? 302 SER B CB    1 
ATOM   1730 O  OG    . SER A 1 223 ? 29.57083  14.84087  0.65149   1.000 98.43606  ? 302 SER B OG    1 
ATOM   1731 N  N     . LEU A 1 224 ? 27.66831  14.54991  -2.23127  1.000 94.72064  ? 303 LEU B N     1 
ATOM   1732 C  CA    . LEU A 1 224 ? 27.30376  13.49800  -3.17241  1.000 93.58360  ? 303 LEU B CA    1 
ATOM   1733 C  C     . LEU A 1 224 ? 27.33704  13.99060  -4.61286  1.000 91.67427  ? 303 LEU B C     1 
ATOM   1734 O  O     . LEU A 1 224 ? 27.39318  13.17225  -5.53744  1.000 97.17927  ? 303 LEU B O     1 
ATOM   1735 C  CB    . LEU A 1 224 ? 25.91936  12.94000  -2.83504  1.000 79.57808  ? 303 LEU B CB    1 
ATOM   1736 C  CG    . LEU A 1 224 ? 25.55912  11.62099  -3.52336  1.000 82.16446  ? 303 LEU B CG    1 
ATOM   1737 C  CD1   . LEU A 1 224 ? 26.57926  10.54605  -3.17923  1.000 84.28289  ? 303 LEU B CD1   1 
ATOM   1738 C  CD2   . LEU A 1 224 ? 24.15382  11.17010  -3.16021  1.000 80.93950  ? 303 LEU B CD2   1 
ATOM   1739 N  N     . ALA A 1 225 ? 27.31901  15.30935  -4.82353  1.000 94.99721  ? 304 ALA B N     1 
ATOM   1740 C  CA    . ALA A 1 225 ? 27.46352  15.85449  -6.16772  1.000 97.11715  ? 304 ALA B CA    1 
ATOM   1741 C  C     . ALA A 1 225 ? 28.81056  15.50739  -6.78846  1.000 91.18034  ? 304 ALA B C     1 
ATOM   1742 O  O     . ALA A 1 225 ? 28.96503  15.61988  -8.00950  1.000 92.87666  ? 304 ALA B O     1 
ATOM   1743 C  CB    . ALA A 1 225 ? 27.27522  17.37198  -6.14122  1.000 89.68401  ? 304 ALA B CB    1 
ATOM   1744 N  N     . LYS A 1 226 ? 29.78749  15.09232  -5.97863  1.000 88.52046  ? 305 LYS B N     1 
ATOM   1745 C  CA    . LYS A 1 226 ? 31.08220  14.67916  -6.50319  1.000 91.39837  ? 305 LYS B CA    1 
ATOM   1746 C  C     . LYS A 1 226 ? 31.05405  13.27610  -7.09354  1.000 98.15146  ? 305 LYS B C     1 
ATOM   1747 O  O     . LYS A 1 226 ? 31.96058  12.92083  -7.85551  1.000 92.69409  ? 305 LYS B O     1 
ATOM   1748 C  CB    . LYS A 1 226 ? 32.14428  14.75045  -5.40383  1.000 93.05644  ? 305 LYS B CB    1 
ATOM   1749 C  CG    . LYS A 1 226 ? 32.32542  16.13323  -4.79906  1.000 89.09188  ? 305 LYS B CG    1 
ATOM   1750 C  CD    . LYS A 1 226 ? 33.42420  16.13384  -3.74893  1.000 91.09928  ? 305 LYS B CD    1 
ATOM   1751 C  CE    . LYS A 1 226 ? 33.60874  17.51476  -3.14544  1.000 98.68388  ? 305 LYS B CE    1 
ATOM   1752 N  NZ    . LYS A 1 226 ? 34.72100  17.54162  -2.15449  1.000 96.25414  ? 305 LYS B NZ    1 
ATOM   1753 N  N     . CYS A 1 227 ? 30.04456  12.47410  -6.75746  1.000 90.12742  ? 306 CYS B N     1 
ATOM   1754 C  CA    . CYS A 1 227 ? 29.90354  11.12629  -7.30781  1.000 85.44462  ? 306 CYS B CA    1 
ATOM   1755 C  C     . CYS A 1 227 ? 29.17143  11.18376  -8.64927  1.000 80.66228  ? 306 CYS B C     1 
ATOM   1756 O  O     . CYS A 1 227 ? 28.10920  10.59658  -8.84509  1.000 83.04519  ? 306 CYS B O     1 
ATOM   1757 C  CB    . CYS A 1 227 ? 29.18052  10.22196  -6.31536  1.000 90.26521  ? 306 CYS B CB    1 
ATOM   1758 S  SG    . CYS A 1 227 ? 29.92095  10.16456  -4.66707  1.000 85.13610  ? 306 CYS B SG    1 
ATOM   1759 N  N     . SER A 1 228 ? 29.77160  11.92074  -9.58352  1.000 86.37502  ? 307 SER B N     1 
ATOM   1760 C  CA    . SER A 1 228 ? 29.20534  12.17500  -10.90797 1.000 84.38704  ? 307 SER B CA    1 
ATOM   1761 C  C     . SER A 1 228 ? 29.17227  10.93953  -11.79906 1.000 79.37283  ? 307 SER B C     1 
ATOM   1762 O  O     . SER A 1 228 ? 28.80114  11.07593  -12.97381 1.000 82.50481  ? 307 SER B O     1 
ATOM   1763 C  CB    . SER A 1 228 ? 29.98429  13.29194  -11.60269 1.000 89.44466  ? 307 SER B CB    1 
ATOM   1764 O  OG    . SER A 1 228 ? 31.36585  12.98643  -11.66311 1.000 94.06704  ? 307 SER B OG    1 
ATOM   1765 N  N     . ALA A 1 229 ? 29.54534  9.76089   -11.30193 1.000 72.28937  ? 308 ALA B N     1 
ATOM   1766 C  CA    . ALA A 1 229 ? 29.41634  8.51947   -12.05160 1.000 76.00423  ? 308 ALA B CA    1 
ATOM   1767 C  C     . ALA A 1 229 ? 28.13748  7.76390   -11.71566 1.000 74.23981  ? 308 ALA B C     1 
ATOM   1768 O  O     . ALA A 1 229 ? 27.85643  6.73842   -12.34539 1.000 71.34333  ? 308 ALA B O     1 
ATOM   1769 C  CB    . ALA A 1 229 ? 30.63217  7.61983   -11.79963 1.000 71.89824  ? 308 ALA B CB    1 
ATOM   1770 N  N     . LEU A 1 230 ? 27.36061  8.24934   -10.74574 1.000 66.47448  ? 309 LEU B N     1 
ATOM   1771 C  CA    . LEU A 1 230 ? 26.11897  7.59033   -10.35866 1.000 76.48502  ? 309 LEU B CA    1 
ATOM   1772 C  C     . LEU A 1 230 ? 25.15301  7.51088   -11.53224 1.000 75.69460  ? 309 LEU B C     1 
ATOM   1773 O  O     . LEU A 1 230 ? 24.84534  8.52087   -12.17184 1.000 76.80317  ? 309 LEU B O     1 
ATOM   1774 C  CB    . LEU A 1 230 ? 25.46156  8.33760   -9.19840  1.000 65.70468  ? 309 LEU B CB    1 
ATOM   1775 C  CG    . LEU A 1 230 ? 25.91577  7.96521   -7.78988  1.000 72.54289  ? 309 LEU B CG    1 
ATOM   1776 C  CD1   . LEU A 1 230 ? 25.20487  8.82623   -6.76170  1.000 74.33161  ? 309 LEU B CD1   1 
ATOM   1777 C  CD2   . LEU A 1 230 ? 25.65454  6.49255   -7.53082  1.000 74.17067  ? 309 LEU B CD2   1 
ATOM   1778 N  N     . GLU A 1 231 ? 24.67159  6.30115   -11.81069 1.000 74.79998  ? 310 GLU B N     1 
ATOM   1779 C  CA    . GLU A 1 231 ? 23.67938  6.08634   -12.85257 1.000 80.16800  ? 310 GLU B CA    1 
ATOM   1780 C  C     . GLU A 1 231 ? 22.25850  6.00721   -12.31135 1.000 75.12882  ? 310 GLU B C     1 
ATOM   1781 O  O     . GLU A 1 231 ? 21.31040  6.03340   -13.10153 1.000 80.67196  ? 310 GLU B O     1 
ATOM   1782 C  CB    . GLU A 1 231 ? 23.99953  4.80566   -13.63481 1.000 82.60590  ? 310 GLU B CB    1 
ATOM   1783 C  CG    . GLU A 1 231 ? 25.40931  4.76168   -14.20248 1.000 87.55173  ? 310 GLU B CG    1 
ATOM   1784 C  CD    . GLU A 1 231 ? 25.69109  3.48630   -14.97690 1.000 98.60397  ? 310 GLU B CD    1 
ATOM   1785 O  OE1   . GLU A 1 231 ? 24.72408  2.83931   -15.43346 1.000 95.93119  ? 310 GLU B OE1   1 
ATOM   1786 O  OE2   . GLU A 1 231 ? 26.88061  3.12934   -15.12622 1.000 97.80486  ? 310 GLU B OE2   1 
ATOM   1787 N  N     . GLU A 1 232 ? 22.08779  5.92027   -10.99380 1.000 70.92897  ? 311 GLU B N     1 
ATOM   1788 C  CA    . GLU A 1 232 ? 20.76406  5.78979   -10.39983 1.000 67.54559  ? 311 GLU B CA    1 
ATOM   1789 C  C     . GLU A 1 232 ? 20.82378  6.27387   -8.96062  1.000 66.42676  ? 311 GLU B C     1 
ATOM   1790 O  O     . GLU A 1 232 ? 21.72027  5.87908   -8.20980  1.000 82.45617  ? 311 GLU B O     1 
ATOM   1791 C  CB    . GLU A 1 232 ? 20.27474  4.33733   -10.45823 1.000 66.38436  ? 311 GLU B CB    1 
ATOM   1792 C  CG    . GLU A 1 232 ? 18.97420  4.08644   -9.71140  1.000 81.42855  ? 311 GLU B CG    1 
ATOM   1793 C  CD    . GLU A 1 232 ? 18.53801  2.63211   -9.76386  1.000 95.08134  ? 311 GLU B CD    1 
ATOM   1794 O  OE1   . GLU A 1 232 ? 19.11533  1.86242   -10.56277 1.000 99.93341  ? 311 GLU B OE1   1 
ATOM   1795 O  OE2   . GLU A 1 232 ? 17.61807  2.25903   -9.00392  1.000 87.13651  ? 311 GLU B OE2   1 
ATOM   1796 N  N     . LEU A 1 233 ? 19.87599  7.12469   -8.58289  1.000 67.32485  ? 312 LEU B N     1 
ATOM   1797 C  CA    . LEU A 1 233 ? 19.75015  7.61575   -7.21359  1.000 65.40976  ? 312 LEU B CA    1 
ATOM   1798 C  C     . LEU A 1 233 ? 18.37958  7.18125   -6.70539  1.000 71.56590  ? 312 LEU B C     1 
ATOM   1799 O  O     . LEU A 1 233 ? 17.36091  7.78724   -7.05130  1.000 78.81305  ? 312 LEU B O     1 
ATOM   1800 C  CB    . LEU A 1 233 ? 19.92384  9.12978   -7.15300  1.000 69.93927  ? 312 LEU B CB    1 
ATOM   1801 C  CG    . LEU A 1 233 ? 20.01230  9.74430   -5.75588  1.000 71.20150  ? 312 LEU B CG    1 
ATOM   1802 C  CD1   . LEU A 1 233 ? 21.23229  9.20981   -5.02017  1.000 72.64485  ? 312 LEU B CD1   1 
ATOM   1803 C  CD2   . LEU A 1 233 ? 20.05109  11.26341  -5.83788  1.000 56.88845  ? 312 LEU B CD2   1 
ATOM   1804 N  N     . ASN A 1 234 ? 18.35541  6.12779   -5.89332  1.000 76.37835  ? 313 ASN B N     1 
ATOM   1805 C  CA    . ASN A 1 234 ? 17.11904  5.54050   -5.38012  1.000 70.36780  ? 313 ASN B CA    1 
ATOM   1806 C  C     . ASN A 1 234 ? 17.11008  5.70147   -3.86181  1.000 75.52280  ? 313 ASN B C     1 
ATOM   1807 O  O     . ASN A 1 234 ? 17.77986  4.95100   -3.14406  1.000 70.54385  ? 313 ASN B O     1 
ATOM   1808 C  CB    . ASN A 1 234 ? 17.00218  4.07656   -5.80047  1.000 62.21392  ? 313 ASN B CB    1 
ATOM   1809 C  CG    . ASN A 1 234 ? 15.72382  3.42369   -5.31200  1.000 63.47197  ? 313 ASN B CG    1 
ATOM   1810 O  OD1   . ASN A 1 234 ? 14.86415  4.07375   -4.71788  1.000 72.99129  ? 313 ASN B OD1   1 
ATOM   1811 N  ND2   . ASN A 1 234 ? 15.58877  2.12968   -5.57062  1.000 63.75680  ? 313 ASN B ND2   1 
ATOM   1812 N  N     . LEU A 1 235 ? 16.33933  6.67538   -3.37986  1.000 73.99020  ? 314 LEU B N     1 
ATOM   1813 C  CA    . LEU A 1 235 ? 16.23186  6.99294   -1.95990  1.000 70.42116  ? 314 LEU B CA    1 
ATOM   1814 C  C     . LEU A 1 235 ? 14.89373  6.53472   -1.38603  1.000 73.07273  ? 314 LEU B C     1 
ATOM   1815 O  O     . LEU A 1 235 ? 14.30885  7.20047   -0.52892  1.000 79.09235  ? 314 LEU B O     1 
ATOM   1816 C  CB    . LEU A 1 235 ? 16.41135  8.49107   -1.72993  1.000 67.45810  ? 314 LEU B CB    1 
ATOM   1817 C  CG    . LEU A 1 235 ? 17.47754  9.21716   -2.55354  1.000 80.05877  ? 314 LEU B CG    1 
ATOM   1818 C  CD1   . LEU A 1 235 ? 17.36712  10.72649  -2.36512  1.000 60.81340  ? 314 LEU B CD1   1 
ATOM   1819 C  CD2   . LEU A 1 235 ? 18.86869  8.73039   -2.18567  1.000 71.86602  ? 314 LEU B CD2   1 
ATOM   1820 N  N     . GLU A 1 236 ? 14.39810  5.39200   -1.85469  1.000 69.94642  ? 315 GLU B N     1 
ATOM   1821 C  CA    . GLU A 1 236 ? 13.06402  4.94151   -1.48359  1.000 76.48086  ? 315 GLU B CA    1 
ATOM   1822 C  C     . GLU A 1 236 ? 12.97703  4.62541   0.00469   1.000 79.45004  ? 315 GLU B C     1 
ATOM   1823 O  O     . GLU A 1 236 ? 13.89069  4.03430   0.58682   1.000 81.25940  ? 315 GLU B O     1 
ATOM   1824 C  CB    . GLU A 1 236 ? 12.67533  3.70736   -2.29568  1.000 79.76944  ? 315 GLU B CB    1 
ATOM   1825 C  CG    . GLU A 1 236 ? 11.26370  3.21283   -2.02728  1.000 80.54598  ? 315 GLU B CG    1 
ATOM   1826 C  CD    . GLU A 1 236 ? 10.96068  1.90714   -2.73127  1.000 84.98054  ? 315 GLU B CD    1 
ATOM   1827 O  OE1   . GLU A 1 236 ? 11.80746  1.44259   -3.52450  1.000 96.55982  ? 315 GLU B OE1   1 
ATOM   1828 O  OE2   . GLU A 1 236 ? 9.87502   1.34281   -2.48759  1.000 86.81226  ? 315 GLU B OE2   1 
ATOM   1829 N  N     . ASN A 1 237 ? 11.86486  5.04146   0.61595   1.000 81.59352  ? 316 ASN B N     1 
ATOM   1830 C  CA    . ASN A 1 237 ? 11.50135  4.71037   1.99482   1.000 77.38976  ? 316 ASN B CA    1 
ATOM   1831 C  C     . ASN A 1 237 ? 12.50940  5.29986   2.98792   1.000 74.30430  ? 316 ASN B C     1 
ATOM   1832 O  O     . ASN A 1 237 ? 13.32836  4.60495   3.59253   1.000 76.08954  ? 316 ASN B O     1 
ATOM   1833 C  CB    . ASN A 1 237 ? 11.35834  3.19360   2.16831   1.000 73.68032  ? 316 ASN B CB    1 
ATOM   1834 C  CG    . ASN A 1 237 ? 10.45613  2.82280   3.32694   1.000 84.40356  ? 316 ASN B CG    1 
ATOM   1835 O  OD1   . ASN A 1 237 ? 9.27515   2.52509   3.13924   1.000 93.10081  ? 316 ASN B OD1   1 
ATOM   1836 N  ND2   . ASN A 1 237 ? 11.00756  2.83896   4.53462   1.000 84.48794  ? 316 ASN B ND2   1 
ATOM   1837 N  N     . ASN A 1 238 ? 12.40813  6.61365   3.14790   1.000 72.68619  ? 317 ASN B N     1 
ATOM   1838 C  CA    . ASN A 1 238 ? 13.27501  7.35440   4.05541   1.000 78.01070  ? 317 ASN B CA    1 
ATOM   1839 C  C     . ASN A 1 238 ? 12.46729  8.49734   4.66422   1.000 87.65348  ? 317 ASN B C     1 
ATOM   1840 O  O     . ASN A 1 238 ? 11.23216  8.48753   4.63397   1.000 87.18299  ? 317 ASN B O     1 
ATOM   1841 C  CB    . ASN A 1 238 ? 14.53822  7.83159   3.31682   1.000 81.18855  ? 317 ASN B CB    1 
ATOM   1842 C  CG    . ASN A 1 238 ? 15.58214  6.73873   3.18522   1.000 84.64629  ? 317 ASN B CG    1 
ATOM   1843 O  OD1   . ASN A 1 238 ? 16.40605  6.54670   4.07949   1.000 88.36474  ? 317 ASN B OD1   1 
ATOM   1844 N  ND2   . ASN A 1 238 ? 15.54833  6.01164   2.07331   1.000 69.62765  ? 317 ASN B ND2   1 
ATOM   1845 N  N     . ASN A 1 239 ? 13.16933  9.47776   5.22611   1.000 84.95971  ? 318 ASN B N     1 
ATOM   1846 C  CA    A ASN A 1 239 ? 12.58057  10.65159  5.86482   0.416 92.07408  ? 318 ASN B CA    1 
ATOM   1847 C  CA    B ASN A 1 239 ? 12.57321  10.65150  5.85650   0.584 91.11024  ? 318 ASN B CA    1 
ATOM   1848 C  C     . ASN A 1 239 ? 13.20073  11.91839  5.28939   1.000 88.50920  ? 318 ASN B C     1 
ATOM   1849 O  O     . ASN A 1 239 ? 13.59738  12.83488  6.01183   1.000 92.78029  ? 318 ASN B O     1 
ATOM   1850 C  CB    A ASN A 1 239 ? 12.77186  10.58043  7.37974   0.416 91.00974  ? 318 ASN B CB    1 
ATOM   1851 C  CB    B ASN A 1 239 ? 12.73440  10.58988  7.37335   0.584 92.03885  ? 318 ASN B CB    1 
ATOM   1852 C  CG    A ASN A 1 239 ? 11.81474  11.48048  8.14262   0.416 88.04116  ? 318 ASN B CG    1 
ATOM   1853 C  CG    B ASN A 1 239 ? 12.11941  9.33933   7.97756   0.584 86.98738  ? 318 ASN B CG    1 
ATOM   1854 O  OD1   A ASN A 1 239 ? 11.43375  12.55092  7.67315   0.416 89.87851  ? 318 ASN B OD1   1 
ATOM   1855 O  OD1   B ASN A 1 239 ? 11.06096  8.88090   7.54719   0.584 92.47930  ? 318 ASN B OD1   1 
ATOM   1856 N  ND2   A ASN A 1 239 ? 11.42577  11.04508  9.33495   0.416 89.72230  ? 318 ASN B ND2   1 
ATOM   1857 N  ND2   B ASN A 1 239 ? 12.78280  8.78286   8.98386   0.584 82.63644  ? 318 ASN B ND2   1 
ATOM   1858 N  N     . ILE A 1 240 ? 13.30471  11.97252  3.96535   1.000 83.63233  ? 319 ILE B N     1 
ATOM   1859 C  CA    . ILE A 1 240 ? 13.93613  13.08106  3.25901   1.000 90.13825  ? 319 ILE B CA    1 
ATOM   1860 C  C     . ILE A 1 240 ? 12.85283  13.99259  2.70295   1.000 90.74096  ? 319 ILE B C     1 
ATOM   1861 O  O     . ILE A 1 240 ? 11.79731  13.52408  2.25854   1.000 87.34986  ? 319 ILE B O     1 
ATOM   1862 C  CB    . ILE A 1 240 ? 14.85966  12.55976  2.14027   1.000 83.80236  ? 319 ILE B CB    1 
ATOM   1863 C  CG1   . ILE A 1 240 ? 15.89070  11.58860  2.71975   1.000 86.75981  ? 319 ILE B CG1   1 
ATOM   1864 C  CG2   . ILE A 1 240 ? 15.55147  13.70895  1.42187   1.000 85.62649  ? 319 ILE B CG2   1 
ATOM   1865 C  CD1   . ILE A 1 240 ? 16.79319  10.95922  1.68269   1.000 90.24785  ? 319 ILE B CD1   1 
ATOM   1866 N  N     . SER A 1 241 ? 13.10696  15.29937  2.73422   1.000 90.71396  ? 320 SER B N     1 
ATOM   1867 C  CA    . SER A 1 241 ? 12.16297  16.28476  2.22842   1.000 89.65396  ? 320 SER B CA    1 
ATOM   1868 C  C     . SER A 1 241 ? 12.73025  17.18029  1.13762   1.000 97.32208  ? 320 SER B C     1 
ATOM   1869 O  O     . SER A 1 241 ? 11.95913  17.68417  0.31820   1.000 96.33395  ? 320 SER B O     1 
ATOM   1870 C  CB    . SER A 1 241 ? 11.64723  17.16930  3.37391   1.000 78.63250  ? 320 SER B CB    1 
ATOM   1871 O  OG    . SER A 1 241 ? 12.69198  17.95605  3.91465   1.000 82.74229  ? 320 SER B OG    1 
ATOM   1872 N  N     . THR A 1 242 ? 14.04507  17.40253  1.10710   1.000 96.79841  ? 321 THR B N     1 
ATOM   1873 C  CA    . THR A 1 242 ? 14.67498  18.23321  0.08841   1.000 96.48671  ? 321 THR B CA    1 
ATOM   1874 C  C     . THR A 1 242 ? 15.96293  17.57072  -0.38074  1.000 94.64853  ? 321 THR B C     1 
ATOM   1875 O  O     . THR A 1 242 ? 16.46361  16.62472  0.23229   1.000 106.50177 ? 321 THR B O     1 
ATOM   1876 C  CB    . THR A 1 242 ? 14.98778  19.64889  0.60203   1.000 93.74266  ? 321 THR B CB    1 
ATOM   1877 O  OG1   . THR A 1 242 ? 15.90817  19.57130  1.69812   1.000 101.22060 ? 321 THR B OG1   1 
ATOM   1878 C  CG2   . THR A 1 242 ? 13.72200  20.36645  1.05151   1.000 93.01542  ? 321 THR B CG2   1 
ATOM   1879 N  N     . LEU A 1 243 ? 16.50238  18.08748  -1.48437  1.000 95.50488  ? 322 LEU B N     1 
ATOM   1880 C  CA    . LEU A 1 243 ? 17.80204  17.68209  -1.98724  1.000 91.52982  ? 322 LEU B CA    1 
ATOM   1881 C  C     . LEU A 1 243 ? 18.74767  18.87714  -2.00642  1.000 94.96546  ? 322 LEU B C     1 
ATOM   1882 O  O     . LEU A 1 243 ? 18.31595  20.00078  -2.28616  1.000 104.66672 ? 322 LEU B O     1 
ATOM   1883 C  CB    . LEU A 1 243 ? 17.69403  17.08648  -3.39978  1.000 80.14997  ? 322 LEU B CB    1 
ATOM   1884 C  CG    . LEU A 1 243 ? 16.92365  15.76902  -3.50805  1.000 82.04925  ? 322 LEU B CG    1 
ATOM   1885 C  CD1   . LEU A 1 243 ? 16.86257  15.29167  -4.94854  1.000 78.16223  ? 322 LEU B CD1   1 
ATOM   1886 C  CD2   . LEU A 1 243 ? 17.54377  14.70665  -2.61558  1.000 75.09716  ? 322 LEU B CD2   1 
ATOM   1887 N  N     . PRO A 1 244 ? 20.03137  18.67289  -1.71330  1.000 91.06564  ? 323 PRO B N     1 
ATOM   1888 C  CA    . PRO A 1 244 ? 20.96670  19.80222  -1.64277  1.000 95.34164  ? 323 PRO B CA    1 
ATOM   1889 C  C     . PRO A 1 244 ? 21.09370  20.51457  -2.98043  1.000 105.55381 ? 323 PRO B C     1 
ATOM   1890 O  O     . PRO A 1 244 ? 20.69615  20.01516  -4.03572  1.000 110.97257 ? 323 PRO B O     1 
ATOM   1891 C  CB    . PRO A 1 244 ? 22.28940  19.14787  -1.22566  1.000 97.36131  ? 323 PRO B CB    1 
ATOM   1892 C  CG    . PRO A 1 244 ? 22.14125  17.71153  -1.60702  1.000 97.08924  ? 323 PRO B CG    1 
ATOM   1893 C  CD    . PRO A 1 244 ? 20.69132  17.39197  -1.41107  1.000 91.38069  ? 323 PRO B CD    1 
ATOM   1894 N  N     . GLU A 1 245 ? 21.67323  21.71211  -2.91728  1.000 117.12646 ? 324 GLU B N     1 
ATOM   1895 C  CA    . GLU A 1 245 ? 21.78027  22.56623  -4.09235  1.000 119.39873 ? 324 GLU B CA    1 
ATOM   1896 C  C     . GLU A 1 245 ? 22.64855  21.91865  -5.16306  1.000 118.50105 ? 324 GLU B C     1 
ATOM   1897 O  O     . GLU A 1 245 ? 23.74269  21.41998  -4.87963  1.000 115.08673 ? 324 GLU B O     1 
ATOM   1898 C  CB    . GLU A 1 245 ? 22.35807  23.92650  -3.70126  1.000 121.19691 ? 324 GLU B CB    1 
ATOM   1899 C  CG    . GLU A 1 245 ? 23.63611  23.83355  -2.88131  1.000 124.95521 ? 324 GLU B CG    1 
ATOM   1900 C  CD    . GLU A 1 245 ? 24.36313  25.15770  -2.77123  1.000 131.25586 ? 324 GLU B CD    1 
ATOM   1901 O  OE1   . GLU A 1 245 ? 23.71904  26.21078  -2.95817  1.000 126.33821 ? 324 GLU B OE1   1 
ATOM   1902 O  OE2   . GLU A 1 245 ? 25.58335  25.14351  -2.50428  1.000 137.33095 ? 324 GLU B OE2   1 
ATOM   1903 N  N     . SER A 1 246 ? 22.14196  21.92110  -6.39686  1.000 122.78773 ? 325 SER B N     1 
ATOM   1904 C  CA    . SER A 1 246 ? 22.88969  21.46043  -7.56679  1.000 124.73253 ? 325 SER B CA    1 
ATOM   1905 C  C     . SER A 1 246 ? 23.35628  20.01339  -7.41726  1.000 121.44390 ? 325 SER B C     1 
ATOM   1906 O  O     . SER A 1 246 ? 24.43439  19.64040  -7.88518  1.000 111.56565 ? 325 SER B O     1 
ATOM   1907 C  CB    . SER A 1 246 ? 24.07610  22.38243  -7.85448  1.000 118.90812 ? 325 SER B CB    1 
ATOM   1908 O  OG    . SER A 1 246 ? 23.63025  23.66884  -8.24233  1.000 124.10971 ? 325 SER B OG    1 
ATOM   1909 N  N     . LEU A 1 247 ? 22.54012  19.18801  -6.76018  1.000 105.51272 ? 326 LEU B N     1 
ATOM   1910 C  CA    . LEU A 1 247 ? 22.85547  17.76735  -6.65318  1.000 91.48754  ? 326 LEU B CA    1 
ATOM   1911 C  C     . LEU A 1 247 ? 22.43385  17.01779  -7.91180  1.000 96.76155  ? 326 LEU B C     1 
ATOM   1912 O  O     . LEU A 1 247 ? 23.25491  16.36286  -8.56252  1.000 93.49969  ? 326 LEU B O     1 
ATOM   1913 C  CB    . LEU A 1 247 ? 22.18144  17.16052  -5.41807  1.000 95.43497  ? 326 LEU B CB    1 
ATOM   1914 C  CG    . LEU A 1 247 ? 22.17788  15.62602  -5.39397  1.000 92.34104  ? 326 LEU B CG    1 
ATOM   1915 C  CD1   . LEU A 1 247 ? 23.59387  15.06722  -5.30140  1.000 89.93290  ? 326 LEU B CD1   1 
ATOM   1916 C  CD2   . LEU A 1 247 ? 21.30915  15.09182  -4.26718  1.000 92.12701  ? 326 LEU B CD2   1 
ATOM   1917 N  N     . LEU A 1 248 ? 21.15129  17.11410  -8.27227  1.000 100.72805 ? 327 LEU B N     1 
ATOM   1918 C  CA    . LEU A 1 248 ? 20.63960  16.35380  -9.40769  1.000 91.57012  ? 327 LEU B CA    1 
ATOM   1919 C  C     . LEU A 1 248 ? 21.28692  16.79665  -10.71231 1.000 96.97441  ? 327 LEU B C     1 
ATOM   1920 O  O     . LEU A 1 248 ? 21.53734  15.97230  -11.59892 1.000 100.13548 ? 327 LEU B O     1 
ATOM   1921 C  CB    . LEU A 1 248 ? 19.12113  16.49470  -9.49002  1.000 89.29755  ? 327 LEU B CB    1 
ATOM   1922 C  CG    . LEU A 1 248 ? 18.33821  15.96302  -8.29020  1.000 93.06983  ? 327 LEU B CG    1 
ATOM   1923 C  CD1   . LEU A 1 248 ? 16.84364  16.13842  -8.50884  1.000 88.42211  ? 327 LEU B CD1   1 
ATOM   1924 C  CD2   . LEU A 1 248 ? 18.68437  14.50310  -8.02735  1.000 91.42918  ? 327 LEU B CD2   1 
ATOM   1925 N  N     . SER A 1 249 ? 21.56384  18.09484  -10.85238 1.000 100.93392 ? 328 SER B N     1 
ATOM   1926 C  CA    . SER A 1 249 ? 22.21647  18.57041  -12.06645 1.000 93.59263  ? 328 SER B CA    1 
ATOM   1927 C  C     . SER A 1 249 ? 23.66188  18.09687  -12.14592 1.000 91.24257  ? 328 SER B C     1 
ATOM   1928 O  O     . SER A 1 249 ? 24.21362  17.97455  -13.24534 1.000 89.00290  ? 328 SER B O     1 
ATOM   1929 C  CB    . SER A 1 249 ? 22.14754  20.09555  -12.13863 1.000 100.26469 ? 328 SER B CB    1 
ATOM   1930 O  OG    . SER A 1 249 ? 22.77302  20.68596  -11.01333 1.000 118.07457 ? 328 SER B OG    1 
ATOM   1931 N  N     . SER A 1 250 ? 24.28588  17.81743  -11.00066 1.000 94.88223  ? 329 SER B N     1 
ATOM   1932 C  CA    . SER A 1 250 ? 25.67180  17.36605  -11.00075 1.000 94.85490  ? 329 SER B CA    1 
ATOM   1933 C  C     . SER A 1 250 ? 25.80333  15.91267  -11.43824 1.000 93.14035  ? 329 SER B C     1 
ATOM   1934 O  O     . SER A 1 250 ? 26.80290  15.54937  -12.06766 1.000 90.08323  ? 329 SER B O     1 
ATOM   1935 C  CB    . SER A 1 250 ? 26.28311  17.55354  -9.61200  1.000 93.98813  ? 329 SER B CB    1 
ATOM   1936 O  OG    . SER A 1 250 ? 26.18043  18.90265  -9.18982  1.000 97.47354  ? 329 SER B OG    1 
ATOM   1937 N  N     . LEU A 1 251 ? 24.81831  15.07238  -11.11767 1.000 89.59482  ? 330 LEU B N     1 
ATOM   1938 C  CA    . LEU A 1 251 ? 24.84336  13.65800  -11.49162 1.000 82.14705  ? 330 LEU B CA    1 
ATOM   1939 C  C     . LEU A 1 251 ? 24.50469  13.55579  -12.97688 1.000 86.73572  ? 330 LEU B C     1 
ATOM   1940 O  O     . LEU A 1 251 ? 23.37906  13.25332  -13.38071 1.000 91.10425  ? 330 LEU B O     1 
ATOM   1941 C  CB    . LEU A 1 251 ? 23.87783  12.85861  -10.62544 1.000 82.05777  ? 330 LEU B CB    1 
ATOM   1942 C  CG    . LEU A 1 251 ? 23.98751  13.09638  -9.11485  1.000 85.64680  ? 330 LEU B CG    1 
ATOM   1943 C  CD1   . LEU A 1 251 ? 22.99385  12.23473  -8.35124  1.000 82.89031  ? 330 LEU B CD1   1 
ATOM   1944 C  CD2   . LEU A 1 251 ? 25.40592  12.84925  -8.61992  1.000 80.82859  ? 330 LEU B CD2   1 
ATOM   1945 N  N     . VAL A 1 252 ? 25.51820  13.80383  -13.80540 1.000 87.79834  ? 331 VAL B N     1 
ATOM   1946 C  CA    . VAL A 1 252 ? 25.33506  13.97750  -15.24318 1.000 87.16536  ? 331 VAL B CA    1 
ATOM   1947 C  C     . VAL A 1 252 ? 25.06576  12.64845  -15.93705 1.000 87.87710  ? 331 VAL B C     1 
ATOM   1948 O  O     . VAL A 1 252 ? 24.82547  12.61088  -17.14932 1.000 90.88176  ? 331 VAL B O     1 
ATOM   1949 C  CB    . VAL A 1 252 ? 26.55939  14.67032  -15.86685 1.000 86.99728  ? 331 VAL B CB    1 
ATOM   1950 C  CG1   . VAL A 1 252 ? 26.75536  16.04900  -15.25703 1.000 80.71520  ? 331 VAL B CG1   1 
ATOM   1951 C  CG2   . VAL A 1 252 ? 27.79880  13.81423  -15.67654 1.000 81.18035  ? 331 VAL B CG2   1 
ATOM   1952 N  N     . LYS A 1 253 ? 25.10440  11.54879  -15.18337 1.000 90.98540  ? 332 LYS B N     1 
ATOM   1953 C  CA    . LYS A 1 253 ? 24.86428  10.22399  -15.74471 1.000 95.83775  ? 332 LYS B CA    1 
ATOM   1954 C  C     . LYS A 1 253 ? 23.66798  9.52869   -15.10288 1.000 89.38018  ? 332 LYS B C     1 
ATOM   1955 O  O     . LYS A 1 253 ? 23.54931  8.30269   -15.19010 1.000 92.55411  ? 332 LYS B O     1 
ATOM   1956 C  CB    . LYS A 1 253 ? 26.11403  9.35105   -15.61433 1.000 86.69355  ? 332 LYS B CB    1 
ATOM   1957 C  CG    . LYS A 1 253 ? 27.21804  9.69532   -16.59704 1.000 78.37366  ? 332 LYS B CG    1 
ATOM   1958 C  CD    . LYS A 1 253 ? 28.15215  8.51106   -16.79547 1.000 107.08219 ? 332 LYS B CD    1 
ATOM   1959 C  CE    . LYS A 1 253 ? 27.38212  7.27528   -17.25379 1.000 111.91852 ? 332 LYS B CE    1 
ATOM   1960 N  NZ    . LYS A 1 253 ? 28.24548  6.06432   -17.36612 1.000 94.99488  ? 332 LYS B NZ    1 
ATOM   1961 N  N     . LEU A 1 254 ? 22.77203  10.28438  -14.47423 1.000 84.53392  ? 333 LEU B N     1 
ATOM   1962 C  CA    . LEU A 1 254 ? 21.65240  9.69208   -13.75113 1.000 91.06410  ? 333 LEU B CA    1 
ATOM   1963 C  C     . LEU A 1 254 ? 20.59927  9.18073   -14.73031 1.000 83.42069  ? 333 LEU B C     1 
ATOM   1964 O  O     . LEU A 1 254 ? 20.10130  9.93975   -15.56821 1.000 82.25224  ? 333 LEU B O     1 
ATOM   1965 C  CB    . LEU A 1 254 ? 21.04680  10.72058  -12.79999 1.000 81.14410  ? 333 LEU B CB    1 
ATOM   1966 C  CG    . LEU A 1 254 ? 20.30132  10.17688  -11.58149 1.000 78.93163  ? 333 LEU B CG    1 
ATOM   1967 C  CD1   . LEU A 1 254 ? 21.27545  9.51288   -10.61966 1.000 73.81478  ? 333 LEU B CD1   1 
ATOM   1968 C  CD2   . LEU A 1 254 ? 19.52541  11.28663  -10.89022 1.000 73.79605  ? 333 LEU B CD2   1 
ATOM   1969 N  N     . ASN A 1 255 ? 20.25324  7.89539   -14.62022 1.000 81.15337  ? 334 ASN B N     1 
ATOM   1970 C  CA    . ASN A 1 255 ? 19.21482  7.30251   -15.45924 1.000 85.88722  ? 334 ASN B CA    1 
ATOM   1971 C  C     . ASN A 1 255 ? 17.83347  7.38028   -14.82145 1.000 78.33458  ? 334 ASN B C     1 
ATOM   1972 O  O     . ASN A 1 255 ? 16.83837  7.56624   -15.52844 1.000 78.38105  ? 334 ASN B O     1 
ATOM   1973 C  CB    . ASN A 1 255 ? 19.54154  5.83866   -15.76872 1.000 84.81191  ? 334 ASN B CB    1 
ATOM   1974 C  CG    . ASN A 1 255 ? 20.81703  5.68093   -16.56512 1.000 101.24042 ? 334 ASN B CG    1 
ATOM   1975 O  OD1   . ASN A 1 255 ? 21.17167  6.54448   -17.36895 1.000 99.28478  ? 334 ASN B OD1   1 
ATOM   1976 N  ND2   . ASN A 1 255 ? 21.51778  4.57222   -16.34594 1.000 101.11430 ? 334 ASN B ND2   1 
ATOM   1977 N  N     . SER A 1 256 ? 17.74672  7.22614   -13.50203 1.000 75.86194  ? 335 SER B N     1 
ATOM   1978 C  CA    . SER A 1 256 ? 16.46310  7.26991   -12.82074 1.000 76.24086  ? 335 SER B CA    1 
ATOM   1979 C  C     . SER A 1 256 ? 16.64282  7.88950   -11.44387 1.000 77.08911  ? 335 SER B C     1 
ATOM   1980 O  O     . SER A 1 256 ? 17.68580  7.73055   -10.80250 1.000 72.04702  ? 335 SER B O     1 
ATOM   1981 C  CB    . SER A 1 256 ? 15.83697  5.87480   -12.68935 1.000 76.13043  ? 335 SER B CB    1 
ATOM   1982 O  OG    . SER A 1 256 ? 16.51626  5.09755   -11.71740 1.000 85.73675  ? 335 SER B OG    1 
ATOM   1983 N  N     . LEU A 1 257 ? 15.61206  8.60577   -11.00494 1.000 68.40968  ? 336 LEU B N     1 
ATOM   1984 C  CA    . LEU A 1 257 ? 15.53561  9.16351   -9.66346  1.000 68.63621  ? 336 LEU B CA    1 
ATOM   1985 C  C     . LEU A 1 257 ? 14.29302  8.60653   -8.99008  1.000 73.77932  ? 336 LEU B C     1 
ATOM   1986 O  O     . LEU A 1 257 ? 13.21774  8.57245   -9.59746  1.000 72.52053  ? 336 LEU B O     1 
ATOM   1987 C  CB    . LEU A 1 257 ? 15.48271  10.69202  -9.69537  1.000 64.07952  ? 336 LEU B CB    1 
ATOM   1988 C  CG    . LEU A 1 257 ? 15.36651  11.37322  -8.33170  1.000 67.76762  ? 336 LEU B CG    1 
ATOM   1989 C  CD1   . LEU A 1 257 ? 16.59907  11.08502  -7.48683  1.000 76.02343  ? 336 LEU B CD1   1 
ATOM   1990 C  CD2   . LEU A 1 257 ? 15.16209  12.86651  -8.49737  1.000 69.27001  ? 336 LEU B CD2   1 
ATOM   1991 N  N     . THR A 1 258 ? 14.43920  8.16392   -7.74543  1.000 69.65940  ? 337 THR B N     1 
ATOM   1992 C  CA    . THR A 1 258 ? 13.33811  7.55205   -7.00631  1.000 72.18401  ? 337 THR B CA    1 
ATOM   1993 C  C     . THR A 1 258 ? 13.31260  8.15826   -5.60831  1.000 75.65269  ? 337 THR B C     1 
ATOM   1994 O  O     . THR A 1 258 ? 14.07687  7.74781   -4.72938  1.000 78.86834  ? 337 THR B O     1 
ATOM   1995 C  CB    . THR A 1 258 ? 13.48342  6.03620   -6.95534  1.000 69.11104  ? 337 THR B CB    1 
ATOM   1996 O  OG1   . THR A 1 258 ? 13.76173  5.54235   -8.27100  1.000 74.44264  ? 337 THR B OG1   1 
ATOM   1997 C  CG2   . THR A 1 258 ? 12.20107  5.39916   -6.44603  1.000 64.33040  ? 337 THR B CG2   1 
ATOM   1998 N  N     . LEU A 1 259 ? 12.43571  9.14242   -5.41274  1.000 72.64540  ? 338 LEU B N     1 
ATOM   1999 C  CA    . LEU A 1 259 ? 12.23909  9.78525   -4.12078  1.000 72.67263  ? 338 LEU B CA    1 
ATOM   2000 C  C     . LEU A 1 259 ? 10.99179  9.26661   -3.41363  1.000 74.86414  ? 338 LEU B C     1 
ATOM   2001 O  O     . LEU A 1 259 ? 10.40677  9.97239   -2.58485  1.000 77.74112  ? 338 LEU B O     1 
ATOM   2002 C  CB    . LEU A 1 259 ? 12.16300  11.30216  -4.29624  1.000 71.29861  ? 338 LEU B CB    1 
ATOM   2003 C  CG    . LEU A 1 259 ? 13.22724  11.94555  -5.18982  1.000 69.63683  ? 338 LEU B CG    1 
ATOM   2004 C  CD1   . LEU A 1 259 ? 12.82603  13.36279  -5.57234  1.000 85.81746  ? 338 LEU B CD1   1 
ATOM   2005 C  CD2   . LEU A 1 259 ? 14.57228  11.94903  -4.49950  1.000 73.68221  ? 338 LEU B CD2   1 
ATOM   2006 N  N     . ALA A 1 260 ? 10.57744  8.04087   -3.72664  1.000 75.45301  ? 339 ALA B N     1 
ATOM   2007 C  CA    . ALA A 1 260 ? 9.31891   7.51097   -3.22291  1.000 72.66982  ? 339 ALA B CA    1 
ATOM   2008 C  C     . ALA A 1 260 ? 9.39253   7.22577   -1.72646  1.000 81.95473  ? 339 ALA B C     1 
ATOM   2009 O  O     . ALA A 1 260 ? 10.45065  6.89734   -1.18220  1.000 81.17790  ? 339 ALA B O     1 
ATOM   2010 C  CB    . ALA A 1 260 ? 8.93835   6.23668   -3.97642  1.000 76.87391  ? 339 ALA B CB    1 
ATOM   2011 N  N     . ARG A 1 261 ? 8.23849   7.35104   -1.06587  1.000 81.74412  ? 340 ARG B N     1 
ATOM   2012 C  CA    . ARG A 1 261 ? 8.08415   7.11393   0.37019   1.000 72.28932  ? 340 ARG B CA    1 
ATOM   2013 C  C     . ARG A 1 261 ? 9.05667   7.98450   1.17237   1.000 81.56405  ? 340 ARG B C     1 
ATOM   2014 O  O     . ARG A 1 261 ? 10.04908  7.51943   1.73346   1.000 87.61959  ? 340 ARG B O     1 
ATOM   2015 C  CB    . ARG A 1 261 ? 8.26893   5.62951   0.70733   1.000 75.89996  ? 340 ARG B CB    1 
ATOM   2016 C  CG    . ARG A 1 261 ? 7.38728   4.68548   -0.08692  1.000 77.41267  ? 340 ARG B CG    1 
ATOM   2017 C  CD    . ARG A 1 261 ? 7.60869   3.24265   0.34526   1.000 86.94385  ? 340 ARG B CD    1 
ATOM   2018 N  NE    . ARG A 1 261 ? 6.88442   2.30291   -0.50216  1.000 108.76249 ? 340 ARG B NE    1 
ATOM   2019 C  CZ    . ARG A 1 261 ? 5.65127   1.87597   -0.26502  1.000 120.34534 ? 340 ARG B CZ    1 
ATOM   2020 N  NH1   . ARG A 1 261 ? 4.97408   2.27454   0.80014   1.000 106.38880 ? 340 ARG B NH1   1 
ATOM   2021 N  NH2   . ARG A 1 261 ? 5.08274   1.02835   -1.11839  1.000 123.19605 ? 340 ARG B NH2   1 
ATOM   2022 N  N     . ASN A 1 262 ? 8.73767   9.27150   1.20969   1.000 85.22315  ? 341 ASN B N     1 
ATOM   2023 C  CA    . ASN A 1 262 ? 9.55626   10.24033  1.92916   1.000 84.25526  ? 341 ASN B CA    1 
ATOM   2024 C  C     . ASN A 1 262 ? 8.63829   11.33685  2.45792   1.000 90.67856  ? 341 ASN B C     1 
ATOM   2025 O  O     . ASN A 1 262 ? 7.42333   11.14546  2.57414   1.000 95.27109  ? 341 ASN B O     1 
ATOM   2026 C  CB    . ASN A 1 262 ? 10.67418  10.78280  1.02097   1.000 83.51473  ? 341 ASN B CB    1 
ATOM   2027 C  CG    . ASN A 1 262 ? 11.90024  9.89076   1.00474   1.000 80.91045  ? 341 ASN B CG    1 
ATOM   2028 O  OD1   . ASN A 1 262 ? 12.83251  10.08960  1.78111   1.000 86.21793  ? 341 ASN B OD1   1 
ATOM   2029 N  ND2   . ASN A 1 262 ? 11.90626  8.90297   0.11680   1.000 78.95963  ? 341 ASN B ND2   1 
ATOM   2030 N  N     . CYS A 1 263 ? 9.21968   12.49036  2.78066   1.000 90.58508  ? 342 CYS B N     1 
ATOM   2031 C  CA    . CYS A 1 263 ? 8.47336   13.63505  3.28475   1.000 94.54247  ? 342 CYS B CA    1 
ATOM   2032 C  C     . CYS A 1 263 ? 8.49916   14.80349  2.30400   1.000 88.91508  ? 342 CYS B C     1 
ATOM   2033 O  O     . CYS A 1 263 ? 8.39640   15.96431  2.70766   1.000 89.78032  ? 342 CYS B O     1 
ATOM   2034 C  CB    . CYS A 1 263 ? 9.01407   14.06394  4.64743   1.000 89.43324  ? 342 CYS B CB    1 
ATOM   2035 S  SG    . CYS A 1 263 ? 8.89227   12.78292  5.91701   1.000 100.81455 ? 342 CYS B SG    1 
ATOM   2036 N  N     . PHE A 1 264 ? 8.64002   14.50868  1.01342   1.000 85.26127  ? 343 PHE B N     1 
ATOM   2037 C  CA    . PHE A 1 264 ? 8.63524   15.54408  -0.01492  1.000 95.11353  ? 343 PHE B CA    1 
ATOM   2038 C  C     . PHE A 1 264 ? 7.24227   16.15274  -0.11801  1.000 95.46900  ? 343 PHE B C     1 
ATOM   2039 O  O     . PHE A 1 264 ? 6.30905   15.50720  -0.60632  1.000 88.68014  ? 343 PHE B O     1 
ATOM   2040 C  CB    . PHE A 1 264 ? 9.06780   14.96281  -1.35845  1.000 93.71931  ? 343 PHE B CB    1 
ATOM   2041 C  CG    . PHE A 1 264 ? 10.55571  14.81094  -1.51218  1.000 88.16508  ? 343 PHE B CG    1 
ATOM   2042 C  CD1   . PHE A 1 264 ? 11.19621  13.65391  -1.09949  1.000 83.06870  ? 343 PHE B CD1   1 
ATOM   2043 C  CD2   . PHE A 1 264 ? 11.31086  15.81971  -2.08826  1.000 81.44486  ? 343 PHE B CD2   1 
ATOM   2044 C  CE1   . PHE A 1 264 ? 12.56347  13.51125  -1.24759  1.000 84.32317  ? 343 PHE B CE1   1 
ATOM   2045 C  CE2   . PHE A 1 264 ? 12.67811  15.68321  -2.23846  1.000 88.60110  ? 343 PHE B CE2   1 
ATOM   2046 C  CZ    . PHE A 1 264 ? 13.30527  14.52788  -1.81772  1.000 88.48071  ? 343 PHE B CZ    1 
ATOM   2047 N  N     . GLN A 1 265 ? 7.09388   17.39157  0.34886   1.000 94.46070  ? 344 GLN B N     1 
ATOM   2048 C  CA    . GLN A 1 265 ? 5.86822   18.14808  0.13744   1.000 98.65303  ? 344 GLN B CA    1 
ATOM   2049 C  C     . GLN A 1 265 ? 5.96217   19.08972  -1.05469  1.000 98.61757  ? 344 GLN B C     1 
ATOM   2050 O  O     . GLN A 1 265 ? 4.93274   19.60468  -1.50240  1.000 100.73351 ? 344 GLN B O     1 
ATOM   2051 C  CB    . GLN A 1 265 ? 5.50204   18.94469  1.39774   1.000 99.29831  ? 344 GLN B CB    1 
ATOM   2052 C  CG    . GLN A 1 265 ? 5.19161   18.07642  2.61204   1.000 108.13503 ? 344 GLN B CG    1 
ATOM   2053 C  CD    . GLN A 1 265 ? 4.58107   18.86339  3.75756   1.000 107.31350 ? 344 GLN B CD    1 
ATOM   2054 O  OE1   . GLN A 1 265 ? 4.28961   20.05200  3.62370   1.000 102.19914 ? 344 GLN B OE1   1 
ATOM   2055 N  NE2   . GLN A 1 265 ? 4.38249   18.20033  4.89202   1.000 103.52404 ? 344 GLN B NE2   1 
ATOM   2056 N  N     . LEU A 1 266 ? 7.16493   19.31869  -1.57630  1.000 102.23682 ? 345 LEU B N     1 
ATOM   2057 C  CA    . LEU A 1 266 ? 7.36988   20.12928  -2.76530  1.000 92.34790  ? 345 LEU B CA    1 
ATOM   2058 C  C     . LEU A 1 266 ? 8.38224   19.43910  -3.66492  1.000 87.36393  ? 345 LEU B C     1 
ATOM   2059 O  O     . LEU A 1 266 ? 9.11783   18.54684  -3.23736  1.000 91.51435  ? 345 LEU B O     1 
ATOM   2060 C  CB    . LEU A 1 266 ? 7.85765   21.54171  -2.41787  1.000 83.42969  ? 345 LEU B CB    1 
ATOM   2061 C  CG    . LEU A 1 266 ? 6.78984   22.61536  -2.22838  1.000 88.20226  ? 345 LEU B CG    1 
ATOM   2062 C  CD1   . LEU A 1 266 ? 7.43826   23.93784  -1.86455  1.000 87.37061  ? 345 LEU B CD1   1 
ATOM   2063 C  CD2   . LEU A 1 266 ? 5.95838   22.75293  -3.49283  1.000 102.01003 ? 345 LEU B CD2   1 
ATOM   2064 N  N     . TYR A 1 267 ? 8.40863   19.86160  -4.92367  1.000 93.08066  ? 346 TYR B N     1 
ATOM   2065 C  CA    . TYR A 1 267 ? 9.41730   19.36832  -5.84217  1.000 91.16416  ? 346 TYR B CA    1 
ATOM   2066 C  C     . TYR A 1 267 ? 10.79533  19.87973  -5.42474  1.000 87.55392  ? 346 TYR B C     1 
ATOM   2067 O  O     . TYR A 1 267 ? 10.92059  20.98820  -4.89769  1.000 91.56768  ? 346 TYR B O     1 
ATOM   2068 C  CB    . TYR A 1 267 ? 9.10200   19.80915  -7.26843  1.000 97.34999  ? 346 TYR B CB    1 
ATOM   2069 C  CG    . TYR A 1 267 ? 8.48634   18.72404  -8.12240  1.000 91.64725  ? 346 TYR B CG    1 
ATOM   2070 C  CD1   . TYR A 1 267 ? 7.25354   18.17270  -7.79851  1.000 93.28901  ? 346 TYR B CD1   1 
ATOM   2071 C  CD2   . TYR A 1 267 ? 9.13468   18.25737  -9.25876  1.000 92.18697  ? 346 TYR B CD2   1 
ATOM   2072 C  CE1   . TYR A 1 267 ? 6.68712   17.17938  -8.57763  1.000 93.32992  ? 346 TYR B CE1   1 
ATOM   2073 C  CE2   . TYR A 1 267 ? 8.57542   17.26686  -10.04559 1.000 92.22635  ? 346 TYR B CE2   1 
ATOM   2074 C  CZ    . TYR A 1 267 ? 7.35162   16.73090  -9.69964  1.000 91.45550  ? 346 TYR B CZ    1 
ATOM   2075 O  OH    . TYR A 1 267 ? 6.78969   15.74341  -10.47704 1.000 91.42965  ? 346 TYR B OH    1 
ATOM   2076 N  N     . PRO A 1 268 ? 11.84398  19.08552  -5.63473  1.000 100.45708 ? 347 PRO B N     1 
ATOM   2077 C  CA    . PRO A 1 268 ? 13.18599  19.52788  -5.23605  1.000 102.63129 ? 347 PRO B CA    1 
ATOM   2078 C  C     . PRO A 1 268 ? 13.64162  20.72187  -6.06090  1.000 97.71603  ? 347 PRO B C     1 
ATOM   2079 O  O     . PRO A 1 268 ? 13.39841  20.79716  -7.26754  1.000 97.93442  ? 347 PRO B O     1 
ATOM   2080 C  CB    . PRO A 1 268 ? 14.06038  18.29495  -5.49472  1.000 90.10275  ? 347 PRO B CB    1 
ATOM   2081 C  CG    . PRO A 1 268 ? 13.31347  17.51098  -6.52323  1.000 93.62426  ? 347 PRO B CG    1 
ATOM   2082 C  CD    . PRO A 1 268 ? 11.85684  17.74072  -6.23593  1.000 95.36172  ? 347 PRO B CD    1 
ATOM   2083 N  N     . VAL A 1 269 ? 14.30610  21.66595  -5.38873  1.000 99.84333  ? 348 VAL B N     1 
ATOM   2084 C  CA    . VAL A 1 269 ? 14.73901  22.88782  -6.05806  1.000 100.05767 ? 348 VAL B CA    1 
ATOM   2085 C  C     . VAL A 1 269 ? 15.88970  22.58679  -7.01405  1.000 102.95310 ? 348 VAL B C     1 
ATOM   2086 O  O     . VAL A 1 269 ? 16.63916  21.61560  -6.85801  1.000 115.28937 ? 348 VAL B O     1 
ATOM   2087 C  CB    . VAL A 1 269 ? 15.13581  23.96220  -5.03277  1.000 100.54031 ? 348 VAL B CB    1 
ATOM   2088 C  CG1   . VAL A 1 269 ? 13.97793  24.24517  -4.08939  1.000 102.78779 ? 348 VAL B CG1   1 
ATOM   2089 C  CG2   . VAL A 1 269 ? 16.36986  23.52765  -4.25709  1.000 103.58132 ? 348 VAL B CG2   1 
ATOM   2090 N  N     . GLY A 1 270 ? 16.02838  23.44311  -8.02232  1.000 108.65696 ? 349 GLY B N     1 
ATOM   2091 C  CA    . GLY A 1 270 ? 17.05120  23.26668  -9.03416  1.000 109.57740 ? 349 GLY B CA    1 
ATOM   2092 C  C     . GLY A 1 270 ? 16.58942  23.70357  -10.40903 1.000 114.33164 ? 349 GLY B C     1 
ATOM   2093 O  O     . GLY A 1 270 ? 17.40513  24.06008  -11.26511 1.000 109.75784 ? 349 GLY B O     1 
ATOM   2094 N  N     . GLY A 1 271 ? 15.27757  23.67824  -10.63118 1.000 112.03907 ? 350 GLY B N     1 
ATOM   2095 C  CA    . GLY A 1 271 ? 14.70747  24.10234  -11.88667 1.000 124.31028 ? 350 GLY B CA    1 
ATOM   2096 C  C     . GLY A 1 271 ? 14.59032  22.97143  -12.88751 1.000 121.45572 ? 350 GLY B C     1 
ATOM   2097 O  O     . GLY A 1 271 ? 14.67798  21.78953  -12.54169 1.000 114.40847 ? 350 GLY B O     1 
ATOM   2098 N  N     . PRO A 1 272 ? 14.37886  23.31894  -14.15992 1.000 127.22312 ? 351 PRO B N     1 
ATOM   2099 C  CA    . PRO A 1 272 ? 14.26453  22.27812  -15.19463 1.000 122.39571 ? 351 PRO B CA    1 
ATOM   2100 C  C     . PRO A 1 272 ? 15.58384  21.60797  -15.53903 1.000 125.51015 ? 351 PRO B C     1 
ATOM   2101 O  O     . PRO A 1 272 ? 15.56717  20.51912  -16.12703 1.000 117.79220 ? 351 PRO B O     1 
ATOM   2102 C  CB    . PRO A 1 272 ? 13.70128  23.04044  -16.40443 1.000 114.50961 ? 351 PRO B CB    1 
ATOM   2103 C  CG    . PRO A 1 272 ? 13.20414  24.35513  -15.85793 1.000 111.39761 ? 351 PRO B CG    1 
ATOM   2104 C  CD    . PRO A 1 272 ? 14.07521  24.65838  -14.68606 1.000 112.95544 ? 351 PRO B CD    1 
ATOM   2105 N  N     . SER A 1 273 ? 16.72021  22.21356  -15.19472 1.000 118.78767 ? 352 SER B N     1 
ATOM   2106 C  CA    . SER A 1 273 ? 18.02632  21.68609  -15.57084 1.000 108.13248 ? 352 SER B CA    1 
ATOM   2107 C  C     . SER A 1 273 ? 18.45311  20.48188  -14.74253 1.000 104.95344 ? 352 SER B C     1 
ATOM   2108 O  O     . SER A 1 273 ? 19.54871  19.95771  -14.96859 1.000 113.91245 ? 352 SER B O     1 
ATOM   2109 C  CB    . SER A 1 273 ? 19.08596  22.78370  -15.45379 1.000 109.44990 ? 352 SER B CB    1 
ATOM   2110 O  OG    . SER A 1 273 ? 19.12992  23.30503  -14.13738 1.000 116.24830 ? 352 SER B OG    1 
ATOM   2111 N  N     . GLN A 1 274 ? 17.63224  20.03256  -13.79628 1.000 99.70044  ? 353 GLN B N     1 
ATOM   2112 C  CA    . GLN A 1 274 ? 17.97544  18.90037  -12.94794 1.000 94.17713  ? 353 GLN B CA    1 
ATOM   2113 C  C     . GLN A 1 274 ? 17.31634  17.60184  -13.39235 1.000 94.30591  ? 353 GLN B C     1 
ATOM   2114 O  O     . GLN A 1 274 ? 17.56671  16.55746  -12.78416 1.000 91.31620  ? 353 GLN B O     1 
ATOM   2115 C  CB    . GLN A 1 274 ? 17.60063  19.19819  -11.49154 1.000 100.97184 ? 353 GLN B CB    1 
ATOM   2116 C  CG    . GLN A 1 274 ? 16.10867  19.33245  -11.24600 1.000 99.46404  ? 353 GLN B CG    1 
ATOM   2117 C  CD    . GLN A 1 274 ? 15.78210  19.73853  -9.82150  1.000 98.18098  ? 353 GLN B CD    1 
ATOM   2118 O  OE1   . GLN A 1 274 ? 16.57229  19.52139  -8.90403  1.000 102.29930 ? 353 GLN B OE1   1 
ATOM   2119 N  NE2   . GLN A 1 274 ? 14.61307  20.33625  -9.63126  1.000 100.68709 ? 353 GLN B NE2   1 
ATOM   2120 N  N     . PHE A 1 275 ? 16.48313  17.63728  -14.43366 1.000 98.58838  ? 354 PHE B N     1 
ATOM   2121 C  CA    . PHE A 1 275 ? 15.82363  16.44108  -14.94571 1.000 97.91674  ? 354 PHE B CA    1 
ATOM   2122 C  C     . PHE A 1 275 ? 16.19534  16.16172  -16.39786 1.000 95.65619  ? 354 PHE B C     1 
ATOM   2123 O  O     . PHE A 1 275 ? 15.46999  15.44417  -17.09426 1.000 91.72898  ? 354 PHE B O     1 
ATOM   2124 C  CB    . PHE A 1 275 ? 14.30425  16.56002  -14.80373 1.000 91.46136  ? 354 PHE B CB    1 
ATOM   2125 C  CG    . PHE A 1 275 ? 13.83639  16.73433  -13.38590 1.000 88.36086  ? 354 PHE B CG    1 
ATOM   2126 C  CD1   . PHE A 1 275 ? 13.95751  15.70308  -12.47001 1.000 91.33077  ? 354 PHE B CD1   1 
ATOM   2127 C  CD2   . PHE A 1 275 ? 13.26322  17.92459  -12.97295 1.000 91.11281  ? 354 PHE B CD2   1 
ATOM   2128 C  CE1   . PHE A 1 275 ? 13.52399  15.85856  -11.16596 1.000 90.82949  ? 354 PHE B CE1   1 
ATOM   2129 C  CE2   . PHE A 1 275 ? 12.82700  18.08542  -11.67170 1.000 93.07719  ? 354 PHE B CE2   1 
ATOM   2130 C  CZ    . PHE A 1 275 ? 12.95778  17.05111  -10.76713 1.000 89.77115  ? 354 PHE B CZ    1 
ATOM   2131 N  N     . SER A 1 276 ? 17.31844  16.70237  -16.86451 1.000 90.78908  ? 355 SER B N     1 
ATOM   2132 C  CA    . SER A 1 276 ? 17.70714  16.59299  -18.26408 1.000 88.60635  ? 355 SER B CA    1 
ATOM   2133 C  C     . SER A 1 276 ? 18.38705  15.27284  -18.60488 1.000 88.38612  ? 355 SER B C     1 
ATOM   2134 O  O     . SER A 1 276 ? 18.83260  15.10805  -19.74544 1.000 93.76567  ? 355 SER B O     1 
ATOM   2135 C  CB    . SER A 1 276 ? 18.63239  17.75362  -18.63799 1.000 100.37476 ? 355 SER B CB    1 
ATOM   2136 O  OG    . SER A 1 276 ? 17.99934  19.00106  -18.41361 1.000 114.51773 ? 355 SER B OG    1 
ATOM   2137 N  N     . THR A 1 277 ? 18.48083  14.33258  -17.66325 1.000 86.48754  ? 356 THR B N     1 
ATOM   2138 C  CA    . THR A 1 277 ? 19.17071  13.06989  -17.90964 1.000 90.69628  ? 356 THR B CA    1 
ATOM   2139 C  C     . THR A 1 277 ? 18.38731  11.82540  -17.51536 1.000 86.07527  ? 356 THR B C     1 
ATOM   2140 O  O     . THR A 1 277 ? 18.77045  10.72943  -17.94211 1.000 87.10956  ? 356 THR B O     1 
ATOM   2141 C  CB    . THR A 1 277 ? 20.52207  13.03519  -17.17473 1.000 92.08824  ? 356 THR B CB    1 
ATOM   2142 O  OG1   . THR A 1 277 ? 20.32056  13.29652  -15.77964 1.000 88.92610  ? 356 THR B OG1   1 
ATOM   2143 C  CG2   . THR A 1 277 ? 21.48421  14.06439  -17.75328 1.000 89.07984  ? 356 THR B CG2   1 
ATOM   2144 N  N     . ILE A 1 278 ? 17.32133  11.94061  -16.72916 1.000 89.17447  ? 357 ILE B N     1 
ATOM   2145 C  CA    . ILE A 1 278 ? 16.61601  10.76106  -16.23976 1.000 81.70241  ? 357 ILE B CA    1 
ATOM   2146 C  C     . ILE A 1 278 ? 15.62339  10.27451  -17.28632 1.000 81.12289  ? 357 ILE B C     1 
ATOM   2147 O  O     . ILE A 1 278 ? 14.94945  11.06939  -17.95358 1.000 90.20024  ? 357 ILE B O     1 
ATOM   2148 C  CB    . ILE A 1 278 ? 15.91097  11.05884  -14.90340 1.000 77.42828  ? 357 ILE B CB    1 
ATOM   2149 C  CG1   . ILE A 1 278 ? 14.93862  12.22956  -15.04801 1.000 76.76496  ? 357 ILE B CG1   1 
ATOM   2150 C  CG2   . ILE A 1 278 ? 16.92846  11.34064  -13.81030 1.000 82.80488  ? 357 ILE B CG2   1 
ATOM   2151 C  CD1   . ILE A 1 278 ? 14.07498  12.44448  -13.83036 1.000 81.79964  ? 357 ILE B CD1   1 
ATOM   2152 N  N     . TYR A 1 279 ? 15.54350  8.95474   -17.44079 1.000 79.15132  ? 358 TYR B N     1 
ATOM   2153 C  CA    . TYR A 1 279 ? 14.48991  8.32220   -18.21921 1.000 74.53296  ? 358 TYR B CA    1 
ATOM   2154 C  C     . TYR A 1 279 ? 13.27237  7.98480   -17.37456 1.000 76.44397  ? 358 TYR B C     1 
ATOM   2155 O  O     . TYR A 1 279 ? 12.20976  7.69177   -17.93208 1.000 83.17353  ? 358 TYR B O     1 
ATOM   2156 C  CB    . TYR A 1 279 ? 15.00782  7.03998   -18.88042 1.000 79.53715  ? 358 TYR B CB    1 
ATOM   2157 C  CG    . TYR A 1 279 ? 16.12672  7.25035   -19.87562 1.000 90.65967  ? 358 TYR B CG    1 
ATOM   2158 C  CD1   . TYR A 1 279 ? 17.44947  7.32645   -19.45924 1.000 93.54130  ? 358 TYR B CD1   1 
ATOM   2159 C  CD2   . TYR A 1 279 ? 15.86093  7.35785   -21.23356 1.000 96.17058  ? 358 TYR B CD2   1 
ATOM   2160 C  CE1   . TYR A 1 279 ? 18.47428  7.51326   -20.36675 1.000 100.73881 ? 358 TYR B CE1   1 
ATOM   2161 C  CE2   . TYR A 1 279 ? 16.87842  7.54426   -22.14833 1.000 100.25921 ? 358 TYR B CE2   1 
ATOM   2162 C  CZ    . TYR A 1 279 ? 18.18292  7.62085   -21.71051 1.000 107.37458 ? 358 TYR B CZ    1 
ATOM   2163 O  OH    . TYR A 1 279 ? 19.19912  7.80653   -22.62128 1.000 123.52936 ? 358 TYR B OH    1 
ATOM   2164 N  N     . SER A 1 280 ? 13.40500  8.02018   -16.05089 1.000 76.62198  ? 359 SER B N     1 
ATOM   2165 C  CA    . SER A 1 280 ? 12.33622  7.64424   -15.14137 1.000 73.03545  ? 359 SER B CA    1 
ATOM   2166 C  C     . SER A 1 280 ? 12.37492  8.54613   -13.91709 1.000 75.85491  ? 359 SER B C     1 
ATOM   2167 O  O     . SER A 1 280 ? 13.42026  9.09790   -13.56407 1.000 70.26808  ? 359 SER B O     1 
ATOM   2168 C  CB    . SER A 1 280 ? 12.45457  6.17463   -14.72070 1.000 63.44735  ? 359 SER B CB    1 
ATOM   2169 O  OG    . SER A 1 280 ? 11.54782  5.86812   -13.67878 1.000 85.48543  ? 359 SER B OG    1 
ATOM   2170 N  N     . LEU A 1 281 ? 11.21776  8.69300   -13.27592 1.000 81.93612  ? 360 LEU B N     1 
ATOM   2171 C  CA    . LEU A 1 281 ? 11.09380  9.52506   -12.08180 1.000 73.12102  ? 360 LEU B CA    1 
ATOM   2172 C  C     . LEU A 1 281 ? 9.92717   8.99059   -11.26584 1.000 69.15193  ? 360 LEU B C     1 
ATOM   2173 O  O     . LEU A 1 281 ? 8.78003   9.03923   -11.71803 1.000 79.56788  ? 360 LEU B O     1 
ATOM   2174 C  CB    . LEU A 1 281 ? 10.88172  10.99132  -12.44685 1.000 67.86943  ? 360 LEU B CB    1 
ATOM   2175 C  CG    . LEU A 1 281 ? 10.72416  11.95617  -11.27045 1.000 72.77149  ? 360 LEU B CG    1 
ATOM   2176 C  CD1   . LEU A 1 281 ? 11.95568  11.91994  -10.38328 1.000 74.70422  ? 360 LEU B CD1   1 
ATOM   2177 C  CD2   . LEU A 1 281 ? 10.46057  13.36987  -11.76637 1.000 82.37011  ? 360 LEU B CD2   1 
ATOM   2178 N  N     . ASN A 1 282 ? 10.21896  8.48035   -10.07405 1.000 72.22488  ? 361 ASN B N     1 
ATOM   2179 C  CA    . ASN A 1 282 ? 9.21045   7.92120   -9.18408  1.000 63.51599  ? 361 ASN B CA    1 
ATOM   2180 C  C     . ASN A 1 282 ? 9.17212   8.75585   -7.91224  1.000 74.89026  ? 361 ASN B C     1 
ATOM   2181 O  O     . ASN A 1 282 ? 10.18081  8.86322   -7.20590  1.000 76.53594  ? 361 ASN B O     1 
ATOM   2182 C  CB    . ASN A 1 282 ? 9.51555   6.45582   -8.86742  1.000 68.40900  ? 361 ASN B CB    1 
ATOM   2183 C  CG    . ASN A 1 282 ? 8.36352   5.75390   -8.18053  1.000 80.55364  ? 361 ASN B CG    1 
ATOM   2184 O  OD1   . ASN A 1 282 ? 7.40008   6.38862   -7.74981  1.000 80.53172  ? 361 ASN B OD1   1 
ATOM   2185 N  ND2   . ASN A 1 282 ? 8.45978   4.43386   -8.06840  1.000 84.21107  ? 361 ASN B ND2   1 
ATOM   2186 N  N     . MET A 1 283 ? 8.01055   9.34592   -7.62332  1.000 72.77851  ? 362 MET B N     1 
ATOM   2187 C  CA    . MET A 1 283 ? 7.82627   10.16431  -6.42975  1.000 72.75223  ? 362 MET B CA    1 
ATOM   2188 C  C     . MET A 1 283 ? 6.61561   9.70931   -5.62319  1.000 78.90483  ? 362 MET B C     1 
ATOM   2189 O  O     . MET A 1 283 ? 6.02535   10.50426  -4.88610  1.000 77.25588  ? 362 MET B O     1 
ATOM   2190 C  CB    . MET A 1 283 ? 7.68097   11.64255  -6.79534  1.000 69.47575  ? 362 MET B CB    1 
ATOM   2191 C  CG    . MET A 1 283 ? 8.90497   12.26080  -7.43918  1.000 81.22945  ? 362 MET B CG    1 
ATOM   2192 S  SD    . MET A 1 283 ? 8.67738   14.02554  -7.73293  1.000 100.92299 ? 362 MET B SD    1 
ATOM   2193 C  CE    . MET A 1 283 ? 10.32090  14.49889  -8.26438  1.000 93.66425  ? 362 MET B CE    1 
ATOM   2194 N  N     . GLU A 1 284 ? 6.23724   8.43918   -5.74145  1.000 74.94878  ? 363 GLU B N     1 
ATOM   2195 C  CA    . GLU A 1 284 ? 4.99370   7.98194   -5.14092  1.000 77.28042  ? 363 GLU B CA    1 
ATOM   2196 C  C     . GLU A 1 284 ? 5.09088   7.95172   -3.61992  1.000 81.65266  ? 363 GLU B C     1 
ATOM   2197 O  O     . GLU A 1 284 ? 6.17236   7.81524   -3.04416  1.000 85.15647  ? 363 GLU B O     1 
ATOM   2198 C  CB    . GLU A 1 284 ? 4.61155   6.59764   -5.66994  1.000 77.17109  ? 363 GLU B CB    1 
ATOM   2199 C  CG    . GLU A 1 284 ? 5.55755   5.48457   -5.27757  1.000 95.28856  ? 363 GLU B CG    1 
ATOM   2200 C  CD    . GLU A 1 284 ? 5.08826   4.12827   -5.77327  1.000 107.99458 ? 363 GLU B CD    1 
ATOM   2201 O  OE1   . GLU A 1 284 ? 3.91432   4.02315   -6.19165  1.000 88.12225  ? 363 GLU B OE1   1 
ATOM   2202 O  OE2   . GLU A 1 284 ? 5.89307   3.16990   -5.74586  1.000 117.74636 ? 363 GLU B OE2   1 
ATOM   2203 N  N     . HIS A 1 285 ? 3.93223   8.09538   -2.97312  1.000 84.52896  ? 364 HIS B N     1 
ATOM   2204 C  CA    . HIS A 1 285 ? 3.80334   8.10312   -1.51548  1.000 85.11664  ? 364 HIS B CA    1 
ATOM   2205 C  C     . HIS A 1 285 ? 4.60460   9.25690   -0.90263  1.000 82.75268  ? 364 HIS B C     1 
ATOM   2206 O  O     . HIS A 1 285 ? 5.61059   9.07533   -0.21584  1.000 89.60487  ? 364 HIS B O     1 
ATOM   2207 C  CB    . HIS A 1 285 ? 4.21388   6.74884   -0.92300  1.000 88.13423  ? 364 HIS B CB    1 
ATOM   2208 C  CG    . HIS A 1 285 ? 3.39329   5.60229   -1.42628  1.000 99.26311  ? 364 HIS B CG    1 
ATOM   2209 N  ND1   . HIS A 1 285 ? 2.12430   5.33484   -0.95947  1.000 104.67212 ? 364 HIS B ND1   1 
ATOM   2210 C  CD2   . HIS A 1 285 ? 3.65462   4.66184   -2.36495  1.000 98.67460  ? 364 HIS B CD2   1 
ATOM   2211 C  CE1   . HIS A 1 285 ? 1.64178   4.27551   -1.58416  1.000 105.16593 ? 364 HIS B CE1   1 
ATOM   2212 N  NE2   . HIS A 1 285 ? 2.55059   3.84801   -2.44216  1.000 103.56330 ? 364 HIS B NE2   1 
ATOM   2213 N  N     . ASN A 1 286 ? 4.11511   10.46380  -1.18018  1.000 85.76037  ? 365 ASN B N     1 
ATOM   2214 C  CA    . ASN A 1 286 ? 4.64919   11.67278  -0.56560  1.000 88.02759  ? 365 ASN B CA    1 
ATOM   2215 C  C     . ASN A 1 286 ? 3.51958   12.65152  -0.27378  1.000 88.11385  ? 365 ASN B C     1 
ATOM   2216 O  O     . ASN A 1 286 ? 2.37193   12.23963  -0.07398  1.000 88.30107  ? 365 ASN B O     1 
ATOM   2217 C  CB    . ASN A 1 286 ? 5.70781   12.32132  -1.46036  1.000 92.10216  ? 365 ASN B CB    1 
ATOM   2218 C  CG    . ASN A 1 286 ? 7.07234   11.67380  -1.31431  1.000 84.66855  ? 365 ASN B CG    1 
ATOM   2219 O  OD1   . ASN A 1 286 ? 7.87561   12.07575  -0.47343  1.000 81.22922  ? 365 ASN B OD1   1 
ATOM   2220 N  ND2   . ASN A 1 286 ? 7.34063   10.66643  -2.13474  1.000 91.06795  ? 365 ASN B ND2   1 
ATOM   2221 N  N     . ARG A 1 287 ? 3.83046   13.94561  -0.24355  1.000 91.27885  ? 366 ARG B N     1 
ATOM   2222 C  CA    . ARG A 1 287 ? 2.83717   14.97427  0.04679   1.000 91.85001  ? 366 ARG B CA    1 
ATOM   2223 C  C     . ARG A 1 287 ? 3.01412   16.16657  -0.88197  1.000 87.58030  ? 366 ARG B C     1 
ATOM   2224 O  O     . ARG A 1 287 ? 2.84002   17.32109  -0.47944  1.000 89.81497  ? 366 ARG B O     1 
ATOM   2225 C  CB    . ARG A 1 287 ? 2.91184   15.42106  1.50607   1.000 96.38132  ? 366 ARG B CB    1 
ATOM   2226 C  CG    . ARG A 1 287 ? 2.60986   14.33178  2.52306   1.000 94.97038  ? 366 ARG B CG    1 
ATOM   2227 C  CD    . ARG A 1 287 ? 2.16874   14.95651  3.82908   1.000 105.44915 ? 366 ARG B CD    1 
ATOM   2228 N  NE    . ARG A 1 287 ? 0.97181   15.76653  3.63593   1.000 122.52165 ? 366 ARG B NE    1 
ATOM   2229 C  CZ    . ARG A 1 287 ? 0.63635   16.80343  4.39094   1.000 127.28091 ? 366 ARG B CZ    1 
ATOM   2230 N  NH1   . ARG A 1 287 ? 1.39870   17.20106  5.39695   1.000 117.69032 ? 366 ARG B NH1   1 
ATOM   2231 N  NH2   . ARG A 1 287 ? -0.48822  17.46316  4.12462   1.000 115.52141 ? 366 ARG B NH2   1 
ATOM   2232 N  N     . ILE A 1 288 ? 3.35910   15.90230  -2.14021  1.000 91.34229  ? 367 ILE B N     1 
ATOM   2233 C  CA    . ILE A 1 288 ? 3.57494   16.97155  -3.10913  1.000 95.01400  ? 367 ILE B CA    1 
ATOM   2234 C  C     . ILE A 1 288 ? 2.22540   17.54465  -3.52164  1.000 99.82937  ? 367 ILE B C     1 
ATOM   2235 O  O     . ILE A 1 288 ? 1.34763   16.81861  -4.00162  1.000 105.35840 ? 367 ILE B O     1 
ATOM   2236 C  CB    . ILE A 1 288 ? 4.35908   16.45852  -4.32296  1.000 94.75550  ? 367 ILE B CB    1 
ATOM   2237 C  CG1   . ILE A 1 288 ? 5.69633   15.86432  -3.87102  1.000 95.21787  ? 367 ILE B CG1   1 
ATOM   2238 C  CG2   . ILE A 1 288 ? 4.56922   17.57972  -5.33136  1.000 95.03136  ? 367 ILE B CG2   1 
ATOM   2239 C  CD1   . ILE A 1 288 ? 6.46852   15.16491  -4.96942  1.000 89.50343  ? 367 ILE B CD1   1 
ATOM   2240 N  N     . ASN A 1 289 ? 2.05633   18.85435  -3.34096  1.000 97.81932  ? 368 ASN B N     1 
ATOM   2241 C  CA    . ASN A 1 289 ? 0.78278   19.51142  -3.60239  1.000 94.17366  ? 368 ASN B CA    1 
ATOM   2242 C  C     . ASN A 1 289 ? 0.68584   20.11657  -4.99746  1.000 102.69432 ? 368 ASN B C     1 
ATOM   2243 O  O     . ASN A 1 289 ? -0.41562  20.49792  -5.41076  1.000 103.32303 ? 368 ASN B O     1 
ATOM   2244 C  CB    . ASN A 1 289 ? 0.52980   20.60516  -2.55831  1.000 100.28768 ? 368 ASN B CB    1 
ATOM   2245 C  CG    . ASN A 1 289 ? 1.56142   21.71509  -2.61476  1.000 105.14824 ? 368 ASN B CG    1 
ATOM   2246 O  OD1   . ASN A 1 289 ? 2.71624   21.48754  -2.97409  1.000 105.20322 ? 368 ASN B OD1   1 
ATOM   2247 N  ND2   . ASN A 1 289 ? 1.14758   22.92634  -2.25981  1.000 106.75940 ? 368 ASN B ND2   1 
ATOM   2248 N  N     . LYS A 1 290 ? 1.79447   20.21706  -5.72964  1.000 97.89394  ? 369 LYS B N     1 
ATOM   2249 C  CA    . LYS A 1 290 ? 1.75888   20.78806  -7.06870  1.000 95.84549  ? 369 LYS B CA    1 
ATOM   2250 C  C     . LYS A 1 290 ? 3.01341   20.38844  -7.83233  1.000 99.39543  ? 369 LYS B C     1 
ATOM   2251 O  O     . LYS A 1 290 ? 4.10366   20.31940  -7.25799  1.000 97.87370  ? 369 LYS B O     1 
ATOM   2252 C  CB    . LYS A 1 290 ? 1.63554   22.31625  -7.02183  1.000 92.86776  ? 369 LYS B CB    1 
ATOM   2253 C  CG    . LYS A 1 290 ? 2.69263   23.00292  -6.17620  1.000 92.12363  ? 369 LYS B CG    1 
ATOM   2254 C  CD    . LYS A 1 290 ? 2.52017   24.51321  -6.20123  1.000 101.25265 ? 369 LYS B CD    1 
ATOM   2255 C  CE    . LYS A 1 290 ? 3.53774   25.20258  -5.30507  1.000 116.48447 ? 369 LYS B CE    1 
ATOM   2256 N  NZ    . LYS A 1 290 ? 3.39341   24.80144  -3.87738  1.000 109.88923 ? 369 LYS B NZ    1 
ATOM   2257 N  N     . ILE A 1 291 ? 2.84407   20.12241  -9.12438  1.000 98.04395  ? 370 ILE B N     1 
ATOM   2258 C  CA    . ILE A 1 291 ? 3.96463   19.91224  -10.03724 1.000 96.03853  ? 370 ILE B CA    1 
ATOM   2259 C  C     . ILE A 1 291 ? 4.32125   21.26636  -10.63851 1.000 89.42279  ? 370 ILE B C     1 
ATOM   2260 O  O     . ILE A 1 291 ? 3.43790   21.95808  -11.16596 1.000 90.71122  ? 370 ILE B O     1 
ATOM   2261 C  CB    . ILE A 1 291 ? 3.62493   18.88364  -11.12738 1.000 89.85710  ? 370 ILE B CB    1 
ATOM   2262 C  CG1   . ILE A 1 291 ? 3.28752   17.52959  -10.50249 1.000 81.70063  ? 370 ILE B CG1   1 
ATOM   2263 C  CG2   . ILE A 1 291 ? 4.78049   18.74003  -12.10759 1.000 82.06746  ? 370 ILE B CG2   1 
ATOM   2264 C  CD1   . ILE A 1 291 ? 2.87296   16.48171  -11.51356 1.000 77.80769  ? 370 ILE B CD1   1 
ATOM   2265 N  N     . PRO A 1 292 ? 5.58173   21.68814  -10.57662 1.000 89.20145  ? 371 PRO B N     1 
ATOM   2266 C  CA    . PRO A 1 292 ? 5.92803   23.04194  -11.02092 1.000 91.74863  ? 371 PRO B CA    1 
ATOM   2267 C  C     . PRO A 1 292 ? 5.72834   23.21855  -12.51587 1.000 95.41407  ? 371 PRO B C     1 
ATOM   2268 O  O     . PRO A 1 292 ? 5.94305   22.30115  -13.31250 1.000 100.59334 ? 371 PRO B O     1 
ATOM   2269 C  CB    . PRO A 1 292 ? 7.40992   23.17449  -10.64475 1.000 97.61836  ? 371 PRO B CB    1 
ATOM   2270 C  CG    . PRO A 1 292 ? 7.64962   22.11170  -9.62379  1.000 96.91703  ? 371 PRO B CG    1 
ATOM   2271 C  CD    . PRO A 1 292 ? 6.73597   20.98578  -9.99651  1.000 96.39642  ? 371 PRO B CD    1 
ATOM   2272 N  N     . PHE A 1 293 ? 5.30142   24.42233  -12.88652 1.000 97.13783  ? 372 PHE B N     1 
ATOM   2273 C  CA    . PHE A 1 293 ? 5.17224   24.77583  -14.29168 1.000 95.21553  ? 372 PHE B CA    1 
ATOM   2274 C  C     . PHE A 1 293 ? 6.54454   24.78326  -14.95266 1.000 100.82948 ? 372 PHE B C     1 
ATOM   2275 O  O     . PHE A 1 293 ? 7.46564   25.46230  -14.48908 1.000 110.10958 ? 372 PHE B O     1 
ATOM   2276 C  CB    . PHE A 1 293 ? 4.50787   26.14478  -14.42627 1.000 92.54984  ? 372 PHE B CB    1 
ATOM   2277 C  CG    . PHE A 1 293 ? 4.33676   26.60401  -15.84631 1.000 106.82990 ? 372 PHE B CG    1 
ATOM   2278 C  CD1   . PHE A 1 293 ? 3.18318   26.30125  -16.54988 1.000 97.34950  ? 372 PHE B CD1   1 
ATOM   2279 C  CD2   . PHE A 1 293 ? 5.32020   27.35557  -16.47211 1.000 102.08452 ? 372 PHE B CD2   1 
ATOM   2280 C  CE1   . PHE A 1 293 ? 3.01782   26.72906  -17.85242 1.000 92.00854  ? 372 PHE B CE1   1 
ATOM   2281 C  CE2   . PHE A 1 293 ? 5.16129   27.78387  -17.77573 1.000 101.41767 ? 372 PHE B CE2   1 
ATOM   2282 C  CZ    . PHE A 1 293 ? 4.00832   27.47046  -18.46740 1.000 92.41979  ? 372 PHE B CZ    1 
ATOM   2283 N  N     . GLY A 1 294 ? 6.68373   24.02279  -16.03431 1.000 98.35008  ? 373 GLY B N     1 
ATOM   2284 C  CA    . GLY A 1 294 ? 7.93885   24.01153  -16.75749 1.000 93.77433  ? 373 GLY B CA    1 
ATOM   2285 C  C     . GLY A 1 294 ? 9.03949   23.21437  -16.10417 1.000 98.22678  ? 373 GLY B C     1 
ATOM   2286 O  O     . GLY A 1 294 ? 10.20200  23.34672  -16.49370 1.000 102.09186 ? 373 GLY B O     1 
ATOM   2287 N  N     . ILE A 1 295 ? 8.70749   22.37991  -15.11673 1.000 97.70757  ? 374 ILE B N     1 
ATOM   2288 C  CA    . ILE A 1 295 ? 9.73148   21.58137  -14.45787 1.000 100.17935 ? 374 ILE B CA    1 
ATOM   2289 C  C     . ILE A 1 295 ? 10.30850  20.53112  -15.39783 1.000 95.54034  ? 374 ILE B C     1 
ATOM   2290 O  O     . ILE A 1 295 ? 11.42345  20.04504  -15.17344 1.000 96.18434  ? 374 ILE B O     1 
ATOM   2291 C  CB    . ILE A 1 295 ? 9.16289   20.93221  -13.18193 1.000 98.79685  ? 374 ILE B CB    1 
ATOM   2292 C  CG1   . ILE A 1 295 ? 10.29781  20.47665  -12.26468 1.000 101.14526 ? 374 ILE B CG1   1 
ATOM   2293 C  CG2   . ILE A 1 295 ? 8.24953   19.76584  -13.53409 1.000 93.83296  ? 374 ILE B CG2   1 
ATOM   2294 C  CD1   . ILE A 1 295 ? 11.22813  21.59788  -11.84685 1.000 96.31267  ? 374 ILE B CD1   1 
ATOM   2295 N  N     . PHE A 1 296 ? 9.58592   20.18200  -16.46235 1.000 92.85976  ? 375 PHE B N     1 
ATOM   2296 C  CA    . PHE A 1 296 ? 10.04216  19.19862  -17.43536 1.000 95.95318  ? 375 PHE B CA    1 
ATOM   2297 C  C     . PHE A 1 296 ? 10.35190  19.82678  -18.79187 1.000 98.47387  ? 375 PHE B C     1 
ATOM   2298 O  O     . PHE A 1 296 ? 10.38292  19.12119  -19.80544 1.000 95.34651  ? 375 PHE B O     1 
ATOM   2299 C  CB    . PHE A 1 296 ? 9.00343   18.08623  -17.58855 1.000 85.99251  ? 375 PHE B CB    1 
ATOM   2300 C  CG    . PHE A 1 296 ? 8.72949   17.32891  -16.31746 1.000 94.83863  ? 375 PHE B CG    1 
ATOM   2301 C  CD1   . PHE A 1 296 ? 9.76112   16.99701  -15.45289 1.000 93.49548  ? 375 PHE B CD1   1 
ATOM   2302 C  CD2   . PHE A 1 296 ? 7.43707   16.95367  -15.98476 1.000 89.57969  ? 375 PHE B CD2   1 
ATOM   2303 C  CE1   . PHE A 1 296 ? 9.50905   16.30059  -14.28262 1.000 87.92846  ? 375 PHE B CE1   1 
ATOM   2304 C  CE2   . PHE A 1 296 ? 7.17850   16.25781  -14.81529 1.000 88.55685  ? 375 PHE B CE2   1 
ATOM   2305 C  CZ    . PHE A 1 296 ? 8.21657   15.93071  -13.96401 1.000 89.46490  ? 375 PHE B CZ    1 
ATOM   2306 N  N     . SER A 1 297 ? 10.58463  21.14130  -18.83255 1.000 87.34451  ? 376 SER B N     1 
ATOM   2307 C  CA    . SER A 1 297 ? 10.92709  21.80493  -20.08491 1.000 95.17702  ? 376 SER B CA    1 
ATOM   2308 C  C     . SER A 1 297 ? 12.29804  21.40067  -20.61007 1.000 106.09767 ? 376 SER B C     1 
ATOM   2309 O  O     . SER A 1 297 ? 12.61218  21.70222  -21.76659 1.000 103.53589 ? 376 SER B O     1 
ATOM   2310 C  CB    . SER A 1 297 ? 10.87039  23.32345  -19.91041 1.000 96.04269  ? 376 SER B CB    1 
ATOM   2311 O  OG    . SER A 1 297 ? 11.82820  23.76630  -18.96598 1.000 100.08376 ? 376 SER B OG    1 
ATOM   2312 N  N     . ARG A 1 298 ? 13.11736  20.73676  -19.79514 1.000 101.49249 ? 377 ARG B N     1 
ATOM   2313 C  CA    . ARG A 1 298 ? 14.40625  20.22543  -20.23277 1.000 100.47540 ? 377 ARG B CA    1 
ATOM   2314 C  C     . ARG A 1 298 ? 14.52634  18.71544  -20.08001 1.000 100.56489 ? 377 ARG B C     1 
ATOM   2315 O  O     . ARG A 1 298 ? 15.59691  18.16295  -20.35960 1.000 99.62317  ? 377 ARG B O     1 
ATOM   2316 C  CB    . ARG A 1 298 ? 15.54304  20.91064  -19.46141 1.000 109.17052 ? 377 ARG B CB    1 
ATOM   2317 C  CG    . ARG A 1 298 ? 15.55201  22.42961  -19.56719 1.000 104.42932 ? 377 ARG B CG    1 
ATOM   2318 C  CD    . ARG A 1 298 ? 16.79163  23.01381  -18.90428 1.000 117.95360 ? 377 ARG B CD    1 
ATOM   2319 N  NE    . ARG A 1 298 ? 16.79983  24.47185  -18.92644 1.000 125.42356 ? 377 ARG B NE    1 
ATOM   2320 C  CZ    . ARG A 1 298 ? 17.82930  25.22029  -18.55271 1.000 127.73467 ? 377 ARG B CZ    1 
ATOM   2321 N  NH1   . ARG A 1 298 ? 18.96156  24.67910  -18.13279 1.000 120.38931 ? 377 ARG B NH1   1 
ATOM   2322 N  NH2   . ARG A 1 298 ? 17.72170  26.54498  -18.60526 1.000 117.54801 ? 377 ARG B NH2   1 
ATOM   2323 N  N     . ALA A 1 299 ? 13.46444  18.03258  -19.64826 1.000 88.40409  ? 378 ALA B N     1 
ATOM   2324 C  CA    . ALA A 1 299 ? 13.48822  16.58179  -19.45952 1.000 93.82831  ? 378 ALA B CA    1 
ATOM   2325 C  C     . ALA A 1 299 ? 13.00345  15.91210  -20.74181 1.000 92.14313  ? 378 ALA B C     1 
ATOM   2326 O  O     . ALA A 1 299 ? 11.86927  15.44142  -20.85063 1.000 96.14784  ? 378 ALA B O     1 
ATOM   2327 C  CB    . ALA A 1 299 ? 12.63570  16.18573  -18.26107 1.000 99.75496  ? 378 ALA B CB    1 
ATOM   2328 N  N     . LYS A 1 300 ? 13.89407  15.86082  -21.72970 1.000 82.07765  ? 379 LYS B N     1 
ATOM   2329 C  CA    . LYS A 1 300 ? 13.52963  15.36781  -23.05058 1.000 94.96026  ? 379 LYS B CA    1 
ATOM   2330 C  C     . LYS A 1 300 ? 13.63833  13.85372  -23.18620 1.000 90.53908  ? 379 LYS B C     1 
ATOM   2331 O  O     . LYS A 1 300 ? 13.13868  13.29959  -24.17121 1.000 91.99045  ? 379 LYS B O     1 
ATOM   2332 C  CB    . LYS A 1 300 ? 14.38960  16.05248  -24.11816 1.000 101.90691 ? 379 LYS B CB    1 
ATOM   2333 C  CG    . LYS A 1 300 ? 14.07997  17.53682  -24.27879 1.000 101.04426 ? 379 LYS B CG    1 
ATOM   2334 C  CD    . LYS A 1 300 ? 15.19045  18.27033  -25.01466 1.000 118.98635 ? 379 LYS B CD    1 
ATOM   2335 C  CE    . LYS A 1 300 ? 14.93551  19.77131  -25.04472 1.000 120.52821 ? 379 LYS B CE    1 
ATOM   2336 N  NZ    . LYS A 1 300 ? 16.11459  20.52490  -25.55944 1.000 123.04012 ? 379 LYS B NZ    1 
ATOM   2337 N  N     . VAL A 1 301 ? 14.26268  13.17151  -22.22827 1.000 89.02748  ? 380 VAL B N     1 
ATOM   2338 C  CA    . VAL A 1 301 ? 14.32712  11.71414  -22.21917 1.000 92.84518  ? 380 VAL B CA    1 
ATOM   2339 C  C     . VAL A 1 301 ? 13.44838  11.10051  -21.14468 1.000 91.19793  ? 380 VAL B C     1 
ATOM   2340 O  O     . VAL A 1 301 ? 13.34143  9.86661   -21.07683 1.000 84.14777  ? 380 VAL B O     1 
ATOM   2341 C  CB    . VAL A 1 301 ? 15.77610  11.21637  -22.06928 1.000 88.24316  ? 380 VAL B CB    1 
ATOM   2342 C  CG1   . VAL A 1 301 ? 16.50411  11.30650  -23.39725 1.000 87.82302  ? 380 VAL B CG1   1 
ATOM   2343 C  CG2   . VAL A 1 301 ? 16.49891  12.01853  -21.00280 1.000 84.17317  ? 380 VAL B CG2   1 
ATOM   2344 N  N     . LEU A 1 302 ? 12.82097  11.91581  -20.29954 1.000 91.48808  ? 381 LEU B N     1 
ATOM   2345 C  CA    . LEU A 1 302 ? 11.94463  11.41578  -19.24564 1.000 83.91906  ? 381 LEU B CA    1 
ATOM   2346 C  C     . LEU A 1 302 ? 10.71324  10.77397  -19.87391 1.000 84.83595  ? 381 LEU B C     1 
ATOM   2347 O  O     . LEU A 1 302 ? 9.88316   11.46244  -20.47589 1.000 85.02808  ? 381 LEU B O     1 
ATOM   2348 C  CB    . LEU A 1 302 ? 11.55793  12.55494  -18.30804 1.000 74.45994  ? 381 LEU B CB    1 
ATOM   2349 C  CG    . LEU A 1 302 ? 10.67810  12.20324  -17.10915 1.000 77.21555  ? 381 LEU B CG    1 
ATOM   2350 C  CD1   . LEU A 1 302 ? 11.37220  11.20093  -16.20172 1.000 81.84068  ? 381 LEU B CD1   1 
ATOM   2351 C  CD2   . LEU A 1 302 ? 10.30923  13.46048  -16.34146 1.000 85.61965  ? 381 LEU B CD2   1 
ATOM   2352 N  N     . SER A 1 303 ? 10.59885  9.44905   -19.75152 1.000 74.60861  ? 382 SER B N     1 
ATOM   2353 C  CA    . SER A 1 303 ? 9.49048   8.71508   -20.34314 1.000 72.09267  ? 382 SER B CA    1 
ATOM   2354 C  C     . SER A 1 303 ? 8.53138   8.12889   -19.32012 1.000 77.25946  ? 382 SER B C     1 
ATOM   2355 O  O     . SER A 1 303 ? 7.42148   7.73869   -19.69577 1.000 74.75494  ? 382 SER B O     1 
ATOM   2356 C  CB    . SER A 1 303 ? 10.01247  7.57628   -21.23323 1.000 73.70644  ? 382 SER B CB    1 
ATOM   2357 O  OG    . SER A 1 303 ? 10.37683  6.44688   -20.45876 1.000 79.48863  ? 382 SER B OG    1 
ATOM   2358 N  N     . LYS A 1 304 ? 8.92424   8.05358   -18.05024 1.000 69.94182  ? 383 LYS B N     1 
ATOM   2359 C  CA    . LYS A 1 304 ? 8.08634   7.48466   -17.00340 1.000 69.51477  ? 383 LYS B CA    1 
ATOM   2360 C  C     . LYS A 1 304 ? 7.99320   8.46172   -15.84302 1.000 69.59503  ? 383 LYS B C     1 
ATOM   2361 O  O     . LYS A 1 304 ? 9.01806   8.93456   -15.34179 1.000 68.11274  ? 383 LYS B O     1 
ATOM   2362 C  CB    . LYS A 1 304 ? 8.63868   6.14152   -16.51124 1.000 75.31516  ? 383 LYS B CB    1 
ATOM   2363 C  CG    . LYS A 1 304 ? 8.63320   5.03800   -17.55343 1.000 78.41776  ? 383 LYS B CG    1 
ATOM   2364 C  CD    . LYS A 1 304 ? 9.03302   3.70400   -16.94084 1.000 80.15986  ? 383 LYS B CD    1 
ATOM   2365 C  CE    . LYS A 1 304 ? 8.98375   2.58785   -17.97328 1.000 93.25571  ? 383 LYS B CE    1 
ATOM   2366 N  NZ    . LYS A 1 304 ? 9.30937   1.26327   -17.37759 1.000 105.59933 ? 383 LYS B NZ    1 
ATOM   2367 N  N     . LEU A 1 305 ? 6.76784   8.75779   -15.41747 1.000 72.76732  ? 384 LEU B N     1 
ATOM   2368 C  CA    . LEU A 1 305 ? 6.52298   9.59409   -14.25233 1.000 67.35933  ? 384 LEU B CA    1 
ATOM   2369 C  C     . LEU A 1 305 ? 5.52612   8.89963   -13.33862 1.000 75.81570  ? 384 LEU B C     1 
ATOM   2370 O  O     . LEU A 1 305 ? 4.51852   8.35654   -13.80267 1.000 77.80060  ? 384 LEU B O     1 
ATOM   2371 C  CB    . LEU A 1 305 ? 5.99660   10.97455  -14.64981 1.000 64.83235  ? 384 LEU B CB    1 
ATOM   2372 C  CG    . LEU A 1 305 ? 5.69305   11.92866  -13.49457 1.000 69.26180  ? 384 LEU B CG    1 
ATOM   2373 C  CD1   . LEU A 1 305 ? 6.91482   12.10188  -12.60980 1.000 70.83860  ? 384 LEU B CD1   1 
ATOM   2374 C  CD2   . LEU A 1 305 ? 5.21889   13.27122  -14.02640 1.000 73.47918  ? 384 LEU B CD2   1 
ATOM   2375 N  N     . ASN A 1 306 ? 5.81543   8.91490   -12.03946 1.000 68.47761  ? 385 ASN B N     1 
ATOM   2376 C  CA    . ASN A 1 306 ? 4.96405   8.28748   -11.03458 1.000 63.86714  ? 385 ASN B CA    1 
ATOM   2377 C  C     . ASN A 1 306 ? 4.70862   9.29825   -9.92553  1.000 74.45098  ? 385 ASN B C     1 
ATOM   2378 O  O     . ASN A 1 306 ? 5.60425   9.58668   -9.12521  1.000 78.78615  ? 385 ASN B O     1 
ATOM   2379 C  CB    . ASN A 1 306 ? 5.61102   7.01912   -10.48093 1.000 63.87439  ? 385 ASN B CB    1 
ATOM   2380 C  CG    . ASN A 1 306 ? 4.65918   6.19940   -9.63347  1.000 73.68206  ? 385 ASN B CG    1 
ATOM   2381 O  OD1   . ASN A 1 306 ? 3.64152   6.70086   -9.15919  1.000 74.16710  ? 385 ASN B OD1   1 
ATOM   2382 N  ND2   . ASN A 1 306 ? 4.98892   4.92695   -9.43672  1.000 78.47964  ? 385 ASN B ND2   1 
ATOM   2383 N  N     . MET A 1 307 ? 3.48941   9.83178   -9.87631  1.000 75.71288  ? 386 MET B N     1 
ATOM   2384 C  CA    . MET A 1 307 ? 3.07733   10.76275  -8.83472  1.000 71.42931  ? 386 MET B CA    1 
ATOM   2385 C  C     . MET A 1 307 ? 2.00335   10.16096  -7.93249  1.000 72.40332  ? 386 MET B C     1 
ATOM   2386 O  O     . MET A 1 307 ? 1.20689   10.89032  -7.33791  1.000 74.71177  ? 386 MET B O     1 
ATOM   2387 C  CB    . MET A 1 307 ? 2.58525   12.06820  -9.45577  1.000 70.50150  ? 386 MET B CB    1 
ATOM   2388 C  CG    . MET A 1 307 ? 3.66568   12.83727  -10.18553 1.000 77.73806  ? 386 MET B CG    1 
ATOM   2389 S  SD    . MET A 1 307 ? 4.98891   13.33106  -9.07537  1.000 79.99517  ? 386 MET B SD    1 
ATOM   2390 C  CE    . MET A 1 307 ? 4.07165   14.27499  -7.86078  1.000 86.32743  ? 386 MET B CE    1 
ATOM   2391 N  N     . LYS A 1 308 ? 1.98019   8.83305   -7.82018  1.000 73.34678  ? 387 LYS B N     1 
ATOM   2392 C  CA    . LYS A 1 308 ? 0.94137   8.15008   -7.06078  1.000 73.12934  ? 387 LYS B CA    1 
ATOM   2393 C  C     . LYS A 1 308 ? 0.98429   8.56220   -5.59345  1.000 75.95170  ? 387 LYS B C     1 
ATOM   2394 O  O     . LYS A 1 308 ? 2.05323   8.82808   -5.04145  1.000 79.95132  ? 387 LYS B O     1 
ATOM   2395 C  CB    . LYS A 1 308 ? 1.11787   6.63415   -7.18669  1.000 69.10603  ? 387 LYS B CB    1 
ATOM   2396 C  CG    . LYS A 1 308 ? -0.04125  5.80886   -6.65867  1.000 70.49909  ? 387 LYS B CG    1 
ATOM   2397 C  CD    . LYS A 1 308 ? 0.43287   4.43368   -6.22155  1.000 83.33991  ? 387 LYS B CD    1 
ATOM   2398 C  CE    . LYS A 1 308 ? -0.67703  3.39939   -6.28784  1.000 72.83313  ? 387 LYS B CE    1 
ATOM   2399 N  NZ    . LYS A 1 308 ? -0.95001  2.97989   -7.69011  1.000 78.03842  ? 387 LYS B NZ    1 
ATOM   2400 N  N     . ASP A 1 309 ? -0.19140  8.62841   -4.96355  1.000 75.72077  ? 388 ASP B N     1 
ATOM   2401 C  CA    . ASP A 1 309 ? -0.29431  8.91597   -3.53432  1.000 80.05267  ? 388 ASP B CA    1 
ATOM   2402 C  C     . ASP A 1 309 ? 0.39257   10.23203  -3.16813  1.000 82.00164  ? 388 ASP B C     1 
ATOM   2403 O  O     . ASP A 1 309 ? 1.47318   10.23653  -2.56430  1.000 80.94014  ? 388 ASP B O     1 
ATOM   2404 C  CB    . ASP A 1 309 ? 0.28409   7.74904   -2.71891  1.000 74.92482  ? 388 ASP B CB    1 
ATOM   2405 C  CG    . ASP A 1 309 ? -0.10096  7.81283   -1.25683  1.000 73.34467  ? 388 ASP B CG    1 
ATOM   2406 O  OD1   . ASP A 1 309 ? -1.31360  7.83094   -0.98043  1.000 97.36903  ? 388 ASP B OD1   1 
ATOM   2407 O  OD2   . ASP A 1 309 ? 0.79864   7.84725   -0.38745  1.000 87.93011  ? 388 ASP B OD2   1 
ATOM   2408 N  N     . ASN A 1 310 ? -0.23004  11.35296  -3.51640  1.000 82.57216  ? 389 ASN B N     1 
ATOM   2409 C  CA    . ASN A 1 310 ? 0.33284   12.67024  -3.21736  1.000 90.73240  ? 389 ASN B CA    1 
ATOM   2410 C  C     . ASN A 1 310 ? -0.79811  13.64563  -2.89258  1.000 92.90223  ? 389 ASN B C     1 
ATOM   2411 O  O     . ASN A 1 310 ? -1.88674  13.24170  -2.47179  1.000 92.06196  ? 389 ASN B O     1 
ATOM   2412 C  CB    . ASN A 1 310 ? 1.20322   13.16375  -4.38514  1.000 87.75352  ? 389 ASN B CB    1 
ATOM   2413 C  CG    . ASN A 1 310 ? 2.63103   12.65403  -4.31297  1.000 85.61687  ? 389 ASN B CG    1 
ATOM   2414 O  OD1   . ASN A 1 310 ? 3.46830   13.21006  -3.59889  1.000 83.11170  ? 389 ASN B OD1   1 
ATOM   2415 N  ND2   . ASN A 1 310 ? 2.92245   11.60854  -5.07691  1.000 78.53436  ? 389 ASN B ND2   1 
ATOM   2416 N  N     . GLN A 1 311 ? -0.53296  14.94289  -3.07388  1.000 90.17062  ? 390 GLN B N     1 
ATOM   2417 C  CA    . GLN A 1 311 ? -1.49793  15.99122  -2.75557  1.000 97.22157  ? 390 GLN B CA    1 
ATOM   2418 C  C     . GLN A 1 311 ? -1.88887  16.81554  -3.97842  1.000 92.03398  ? 390 GLN B C     1 
ATOM   2419 O  O     . GLN A 1 311 ? -2.33524  17.95856  -3.83292  1.000 94.58981  ? 390 GLN B O     1 
ATOM   2420 C  CB    . GLN A 1 311 ? -0.95181  16.91094  -1.66115  1.000 100.28910 ? 390 GLN B CB    1 
ATOM   2421 C  CG    . GLN A 1 311 ? -0.63480  16.20168  -0.35862  1.000 103.54376 ? 390 GLN B CG    1 
ATOM   2422 C  CD    . GLN A 1 311 ? -1.87838  15.86318  0.43045   1.000 110.17589 ? 390 GLN B CD    1 
ATOM   2423 O  OE1   . GLN A 1 311 ? -2.64381  16.74994  0.80968   1.000 115.46549 ? 390 GLN B OE1   1 
ATOM   2424 N  NE2   . GLN A 1 311 ? -2.09281  14.57561  0.67760   1.000 105.44141 ? 390 GLN B NE2   1 
ATOM   2425 N  N     . LEU A 1 312 ? -1.74636  16.25847  -5.17740  1.000 88.48665  ? 391 LEU B N     1 
ATOM   2426 C  CA    . LEU A 1 312 ? -2.03903  17.00057  -6.39693  1.000 83.09081  ? 391 LEU B CA    1 
ATOM   2427 C  C     . LEU A 1 312 ? -3.53989  17.23505  -6.52218  1.000 95.68536  ? 391 LEU B C     1 
ATOM   2428 O  O     . LEU A 1 312 ? -4.32656  16.28220  -6.53611  1.000 98.27512  ? 391 LEU B O     1 
ATOM   2429 C  CB    . LEU A 1 312 ? -1.51145  16.24114  -7.61079  1.000 73.96317  ? 391 LEU B CB    1 
ATOM   2430 C  CG    . LEU A 1 312 ? -0.00615  15.97555  -7.64310  1.000 80.74366  ? 391 LEU B CG    1 
ATOM   2431 C  CD1   . LEU A 1 312 ? 0.36212   15.13365  -8.85424  1.000 65.00005  ? 391 LEU B CD1   1 
ATOM   2432 C  CD2   . LEU A 1 312 ? 0.76638   17.28404  -7.64286  1.000 81.69774  ? 391 LEU B CD2   1 
ATOM   2433 N  N     . THR A 1 313 ? -3.93672  18.50458  -6.60333  1.000 90.46045  ? 392 THR B N     1 
ATOM   2434 C  CA    . THR A 1 313 ? -5.32793  18.86313  -6.83890  1.000 89.00930  ? 392 THR B CA    1 
ATOM   2435 C  C     . THR A 1 313 ? -5.58269  19.34700  -8.25788  1.000 84.97063  ? 392 THR B C     1 
ATOM   2436 O  O     . THR A 1 313 ? -6.73765  19.35618  -8.69649  1.000 97.88910  ? 392 THR B O     1 
ATOM   2437 C  CB    . THR A 1 313 ? -5.77558  19.95112  -5.85453  1.000 82.06499  ? 392 THR B CB    1 
ATOM   2438 O  OG1   . THR A 1 313 ? -4.88893  21.07347  -5.94275  1.000 93.55952  ? 392 THR B OG1   1 
ATOM   2439 C  CG2   . THR A 1 313 ? -5.77269  19.41447  -4.43441  1.000 87.93560  ? 392 THR B CG2   1 
ATOM   2440 N  N     . SER A 1 314 ? -4.53880  19.74560  -8.97747  1.000 83.04924  ? 393 SER B N     1 
ATOM   2441 C  CA    . SER A 1 314 ? -4.66529  20.17676  -10.35952 1.000 86.90884  ? 393 SER B CA    1 
ATOM   2442 C  C     . SER A 1 314 ? -3.33654  19.92729  -11.05400 1.000 85.04243  ? 393 SER B C     1 
ATOM   2443 O  O     . SER A 1 314 ? -2.33943  19.57015  -10.42233 1.000 82.23133  ? 393 SER B O     1 
ATOM   2444 C  CB    . SER A 1 314 ? -5.06877  21.65037  -10.45440 1.000 81.60018  ? 393 SER B CB    1 
ATOM   2445 O  OG    . SER A 1 314 ? -4.11664  22.46939  -9.79981  1.000 89.42239  ? 393 SER B OG    1 
ATOM   2446 N  N     . LEU A 1 315 ? -3.33186  20.11984  -12.36217 1.000 87.21774  ? 394 LEU B N     1 
ATOM   2447 C  CA    . LEU A 1 315 ? -2.13064  19.90072  -13.14418 1.000 82.95989  ? 394 LEU B CA    1 
ATOM   2448 C  C     . LEU A 1 315 ? -1.57900  21.22541  -13.66134 1.000 86.04931  ? 394 LEU B C     1 
ATOM   2449 O  O     . LEU A 1 315 ? -2.33170  22.18954  -13.83575 1.000 97.99195  ? 394 LEU B O     1 
ATOM   2450 C  CB    . LEU A 1 315 ? -2.41882  18.96548  -14.32441 1.000 77.03166  ? 394 LEU B CB    1 
ATOM   2451 C  CG    . LEU A 1 315 ? -2.89045  17.56832  -13.91567 1.000 82.20728  ? 394 LEU B CG    1 
ATOM   2452 C  CD1   . LEU A 1 315 ? -3.28054  16.74719  -15.13149 1.000 86.79710  ? 394 LEU B CD1   1 
ATOM   2453 C  CD2   . LEU A 1 315 ? -1.81277  16.85809  -13.10979 1.000 79.16195  ? 394 LEU B CD2   1 
ATOM   2454 N  N     . PRO A 1 316 ? -0.27021  21.31279  -13.89949 1.000 84.44838  ? 395 PRO B N     1 
ATOM   2455 C  CA    . PRO A 1 316 ? 0.29281   22.54422  -14.46226 1.000 86.97863  ? 395 PRO B CA    1 
ATOM   2456 C  C     . PRO A 1 316 ? -0.28202  22.83059  -15.84089 1.000 85.79313  ? 395 PRO B C     1 
ATOM   2457 O  O     . PRO A 1 316 ? -0.76059  21.93917  -16.54431 1.000 94.79695  ? 395 PRO B O     1 
ATOM   2458 C  CB    . PRO A 1 316 ? 1.79854   22.25456  -14.52876 1.000 90.04228  ? 395 PRO B CB    1 
ATOM   2459 C  CG    . PRO A 1 316 ? 1.90684   20.76401  -14.49423 1.000 89.71816  ? 395 PRO B CG    1 
ATOM   2460 C  CD    . PRO A 1 316 ? 0.76663   20.30022  -13.63943 1.000 89.63551  ? 395 PRO B CD    1 
ATOM   2461 N  N     . LEU A 1 317 ? -0.23726  24.10856  -16.22219 1.000 90.35894  ? 396 LEU B N     1 
ATOM   2462 C  CA    . LEU A 1 317 ? -0.85974  24.51718  -17.47724 1.000 99.07440  ? 396 LEU B CA    1 
ATOM   2463 C  C     . LEU A 1 317 ? -0.12013  23.95936  -18.68699 1.000 102.50103 ? 396 LEU B C     1 
ATOM   2464 O  O     . LEU A 1 317 ? -0.74656  23.67132  -19.71376 1.000 105.72092 ? 396 LEU B O     1 
ATOM   2465 C  CB    . LEU A 1 317 ? -0.94138  26.04176  -17.55396 1.000 98.69447  ? 396 LEU B CB    1 
ATOM   2466 C  CG    . LEU A 1 317 ? -1.77351  26.71244  -16.45775 1.000 101.94167 ? 396 LEU B CG    1 
ATOM   2467 C  CD1   . LEU A 1 317 ? -1.96111  28.19585  -16.74426 1.000 92.39425  ? 396 LEU B CD1   1 
ATOM   2468 C  CD2   . LEU A 1 317 ? -3.11681  26.01635  -16.29812 1.000 99.00532  ? 396 LEU B CD2   1 
ATOM   2469 N  N     . ASP A 1 318 ? 1.19925   23.79688  -18.59185 1.000 92.63962  ? 397 ASP B N     1 
ATOM   2470 C  CA    . ASP A 1 318 ? 1.98417   23.21385  -19.67006 1.000 95.93889  ? 397 ASP B CA    1 
ATOM   2471 C  C     . ASP A 1 318 ? 2.12329   21.70288  -19.53725 1.000 102.70710 ? 397 ASP B C     1 
ATOM   2472 O  O     . ASP A 1 318 ? 3.03882   21.11763  -20.12765 1.000 96.65526  ? 397 ASP B O     1 
ATOM   2473 C  CB    . ASP A 1 318 ? 3.36551   23.86862  -19.73685 1.000 94.07812  ? 397 ASP B CB    1 
ATOM   2474 C  CG    . ASP A 1 318 ? 4.21607   23.56816  -18.51849 1.000 93.33592  ? 397 ASP B CG    1 
ATOM   2475 O  OD1   . ASP A 1 318 ? 3.65769   23.17594  -17.47202 1.000 99.02149  ? 397 ASP B OD1   1 
ATOM   2476 O  OD2   . ASP A 1 318 ? 5.44904   23.73381  -18.60925 1.000 91.11937  ? 397 ASP B OD2   1 
ATOM   2477 N  N     . PHE A 1 319 ? 1.23890   21.06246  -18.76974 1.000 95.99454  ? 398 PHE B N     1 
ATOM   2478 C  CA    . PHE A 1 319 ? 1.27754   19.61204  -18.63690 1.000 98.15751  ? 398 PHE B CA    1 
ATOM   2479 C  C     . PHE A 1 319 ? 1.03724   18.91506  -19.97026 1.000 96.71264  ? 398 PHE B C     1 
ATOM   2480 O  O     . PHE A 1 319 ? 1.46900   17.77065  -20.14852 1.000 102.14892 ? 398 PHE B O     1 
ATOM   2481 C  CB    . PHE A 1 319 ? 0.25833   19.17261  -17.57681 1.000 97.26638  ? 398 PHE B CB    1 
ATOM   2482 C  CG    . PHE A 1 319 ? -0.64554  18.05631  -18.01188 1.000 91.29064  ? 398 PHE B CG    1 
ATOM   2483 C  CD1   . PHE A 1 319 ? -0.28493  16.73498  -17.80618 1.000 97.77234  ? 398 PHE B CD1   1 
ATOM   2484 C  CD2   . PHE A 1 319 ? -1.86879  18.32818  -18.60049 1.000 99.07445  ? 398 PHE B CD2   1 
ATOM   2485 C  CE1   . PHE A 1 319 ? -1.11714  15.70619  -18.20010 1.000 98.69774  ? 398 PHE B CE1   1 
ATOM   2486 C  CE2   . PHE A 1 319 ? -2.70590  17.30365  -18.99646 1.000 103.34309 ? 398 PHE B CE2   1 
ATOM   2487 C  CZ    . PHE A 1 319 ? -2.32984  15.99080  -18.79579 1.000 93.86349  ? 398 PHE B CZ    1 
ATOM   2488 N  N     . GLY A 1 320 ? 0.38186   19.58807  -20.91644 1.000 94.07513  ? 399 GLY B N     1 
ATOM   2489 C  CA    . GLY A 1 320 ? 0.17079   19.03996  -22.24177 1.000 95.61752  ? 399 GLY B CA    1 
ATOM   2490 C  C     . GLY A 1 320 ? 1.39621   18.99616  -23.12914 1.000 89.73324  ? 399 GLY B C     1 
ATOM   2491 O  O     . GLY A 1 320 ? 1.34770   18.36744  -24.19031 1.000 87.12593  ? 399 GLY B O     1 
ATOM   2492 N  N     . THR A 1 321 ? 2.48850   19.64450  -22.72867 1.000 77.64883  ? 400 THR B N     1 
ATOM   2493 C  CA    . THR A 1 321 ? 3.72282   19.62216  -23.50033 1.000 90.14091  ? 400 THR B CA    1 
ATOM   2494 C  C     . THR A 1 321 ? 4.63285   18.45805  -23.13090 1.000 83.80629  ? 400 THR B C     1 
ATOM   2495 O  O     . THR A 1 321 ? 5.68243   18.28957  -23.76005 1.000 84.35553  ? 400 THR B O     1 
ATOM   2496 C  CB    . THR A 1 321 ? 4.48605   20.93845  -23.32644 1.000 94.92942  ? 400 THR B CB    1 
ATOM   2497 O  OG1   . THR A 1 321 ? 4.90902   21.07114  -21.96417 1.000 91.76991  ? 400 THR B OG1   1 
ATOM   2498 C  CG2   . THR A 1 321 ? 3.60392   22.12133  -23.70146 1.000 86.36075  ? 400 THR B CG2   1 
ATOM   2499 N  N     . TRP A 1 322 ? 4.26027   17.65460  -22.13459 1.000 84.68873  ? 401 TRP B N     1 
ATOM   2500 C  CA    . TRP A 1 322 ? 5.03068   16.47441  -21.76238 1.000 72.88936  ? 401 TRP B CA    1 
ATOM   2501 C  C     . TRP A 1 322 ? 4.93849   15.42922  -22.86774 1.000 86.86637  ? 401 TRP B C     1 
ATOM   2502 O  O     . TRP A 1 322 ? 4.36978   14.35074  -22.66852 1.000 87.43473  ? 401 TRP B O     1 
ATOM   2503 C  CB    . TRP A 1 322 ? 4.52874   15.89885  -20.43420 1.000 76.67569  ? 401 TRP B CB    1 
ATOM   2504 C  CG    . TRP A 1 322 ? 4.57170   16.86537  -19.27745 1.000 80.75401  ? 401 TRP B CG    1 
ATOM   2505 C  CD1   . TRP A 1 322 ? 5.16429   18.09515  -19.25374 1.000 83.49151  ? 401 TRP B CD1   1 
ATOM   2506 C  CD2   . TRP A 1 322 ? 3.99248   16.67687  -17.97846 1.000 87.11032  ? 401 TRP B CD2   1 
ATOM   2507 N  NE1   . TRP A 1 322 ? 4.99158   18.68252  -18.02317 1.000 78.95937  ? 401 TRP B NE1   1 
ATOM   2508 C  CE2   . TRP A 1 322 ? 4.27621   17.83274  -17.22197 1.000 82.14418  ? 401 TRP B CE2   1 
ATOM   2509 C  CE3   . TRP A 1 322 ? 3.26303   15.64313  -17.38194 1.000 80.04361  ? 401 TRP B CE3   1 
ATOM   2510 C  CZ2   . TRP A 1 322 ? 3.85642   17.98347  -15.90101 1.000 78.56621  ? 401 TRP B CZ2   1 
ATOM   2511 C  CZ3   . TRP A 1 322 ? 2.84802   15.79475  -16.06917 1.000 80.81715  ? 401 TRP B CZ3   1 
ATOM   2512 C  CH2   . TRP A 1 322 ? 3.14601   16.95604  -15.34385 1.000 74.19553  ? 401 TRP B CH2   1 
ATOM   2513 N  N     . THR A 1 323 ? 5.50430   15.73879  -24.03532 1.000 84.08767  ? 402 THR B N     1 
ATOM   2514 C  CA    . THR A 1 323 ? 5.30659   14.91655  -25.22165 1.000 76.50392  ? 402 THR B CA    1 
ATOM   2515 C  C     . THR A 1 323 ? 6.14112   13.64281  -25.21821 1.000 82.42438  ? 402 THR B C     1 
ATOM   2516 O  O     . THR A 1 323 ? 5.79007   12.68927  -25.92178 1.000 85.62332  ? 402 THR B O     1 
ATOM   2517 C  CB    . THR A 1 323 ? 5.62166   15.73396  -26.47407 1.000 70.21366  ? 402 THR B CB    1 
ATOM   2518 O  OG1   . THR A 1 323 ? 6.95210   16.25891  -26.38082 1.000 74.91783  ? 402 THR B OG1   1 
ATOM   2519 C  CG2   . THR A 1 323 ? 4.64175   16.88511  -26.60507 1.000 69.63294  ? 402 THR B CG2   1 
ATOM   2520 N  N     . SER A 1 324 ? 7.22777   13.60070  -24.45348 1.000 78.43889  ? 403 SER B N     1 
ATOM   2521 C  CA    . SER A 1 324 ? 8.07246   12.41740  -24.38177 1.000 79.17042  ? 403 SER B CA    1 
ATOM   2522 C  C     . SER A 1 324 ? 7.59748   11.41467  -23.33879 1.000 79.05395  ? 403 SER B C     1 
ATOM   2523 O  O     . SER A 1 324 ? 8.25000   10.38288  -23.14909 1.000 83.60549  ? 403 SER B O     1 
ATOM   2524 C  CB    . SER A 1 324 ? 9.52118   12.82312  -24.08884 1.000 90.41465  ? 403 SER B CB    1 
ATOM   2525 O  OG    . SER A 1 324 ? 9.60778   13.57187  -22.88852 1.000 99.56218  ? 403 SER B OG    1 
ATOM   2526 N  N     . MET A 1 325 ? 6.48090   11.68762  -22.66870 1.000 85.29589  ? 404 MET B N     1 
ATOM   2527 C  CA    . MET A 1 325 ? 5.98016   10.81353  -21.61688 1.000 75.35148  ? 404 MET B CA    1 
ATOM   2528 C  C     . MET A 1 325 ? 5.30400   9.59059   -22.22361 1.000 68.92299  ? 404 MET B C     1 
ATOM   2529 O  O     . MET A 1 325 ? 4.42042   9.71782   -23.07699 1.000 77.41039  ? 404 MET B O     1 
ATOM   2530 C  CB    . MET A 1 325 ? 4.99647   11.57214  -20.72673 1.000 78.92560  ? 404 MET B CB    1 
ATOM   2531 C  CG    . MET A 1 325 ? 4.79695   10.96975  -19.34683 1.000 80.00336  ? 404 MET B CG    1 
ATOM   2532 S  SD    . MET A 1 325 ? 6.10523   11.44767  -18.20035 1.000 101.38783 ? 404 MET B SD    1 
ATOM   2533 C  CE    . MET A 1 325 ? 5.98651   13.23317  -18.26844 1.000 69.89326  ? 404 MET B CE    1 
ATOM   2534 N  N     . VAL A 1 326 ? 5.71551   8.40877   -21.77890 1.000 75.91210  ? 405 VAL B N     1 
ATOM   2535 C  CA    . VAL A 1 326 ? 5.13787   7.14945   -22.24070 1.000 74.04173  ? 405 VAL B CA    1 
ATOM   2536 C  C     . VAL A 1 326 ? 4.21055   6.54634   -21.19485 1.000 71.48566  ? 405 VAL B C     1 
ATOM   2537 O  O     . VAL A 1 326 ? 3.10490   6.10657   -21.51140 1.000 66.81144  ? 405 VAL B O     1 
ATOM   2538 C  CB    . VAL A 1 326 ? 6.25809   6.16115   -22.63511 1.000 68.77121  ? 405 VAL B CB    1 
ATOM   2539 C  CG1   . VAL A 1 326 ? 5.67457   4.79777   -22.97165 1.000 67.73262  ? 405 VAL B CG1   1 
ATOM   2540 C  CG2   . VAL A 1 326 ? 7.05251   6.70933   -23.80916 1.000 77.16244  ? 405 VAL B CG2   1 
ATOM   2541 N  N     . GLU A 1 327 ? 4.64727   6.51999   -19.93955 1.000 71.10778  ? 406 GLU B N     1 
ATOM   2542 C  CA    . GLU A 1 327 ? 3.85123   6.00993   -18.83379 1.000 64.02198  ? 406 GLU B CA    1 
ATOM   2543 C  C     . GLU A 1 327 ? 3.68190   7.11499   -17.80293 1.000 77.00839  ? 406 GLU B C     1 
ATOM   2544 O  O     . GLU A 1 327 ? 4.66589   7.73394   -17.38340 1.000 79.00805  ? 406 GLU B O     1 
ATOM   2545 C  CB    . GLU A 1 327 ? 4.50793   4.78015   -18.20283 1.000 63.82131  ? 406 GLU B CB    1 
ATOM   2546 C  CG    . GLU A 1 327 ? 4.77781   3.65382   -19.18806 1.000 71.11568  ? 406 GLU B CG    1 
ATOM   2547 C  CD    . GLU A 1 327 ? 5.38627   2.43157   -18.52709 1.000 86.91973  ? 406 GLU B CD    1 
ATOM   2548 O  OE1   . GLU A 1 327 ? 5.26846   2.30312   -17.28890 1.000 87.87029  ? 406 GLU B OE1   1 
ATOM   2549 O  OE2   . GLU A 1 327 ? 5.98493   1.60139   -19.24558 1.000 90.17001  ? 406 GLU B OE2   1 
ATOM   2550 N  N     . LEU A 1 328 ? 2.43606   7.36779   -17.40723 1.000 78.70036  ? 407 LEU B N     1 
ATOM   2551 C  CA    . LEU A 1 328 ? 2.11608   8.41057   -16.44235 1.000 71.66795  ? 407 LEU B CA    1 
ATOM   2552 C  C     . LEU A 1 328 ? 1.16397   7.84654   -15.40134 1.000 72.81662  ? 407 LEU B C     1 
ATOM   2553 O  O     . LEU A 1 328 ? 0.11771   7.29029   -15.75079 1.000 73.50298  ? 407 LEU B O     1 
ATOM   2554 C  CB    . LEU A 1 328 ? 1.49502   9.63164   -17.12926 1.000 73.41524  ? 407 LEU B CB    1 
ATOM   2555 C  CG    . LEU A 1 328 ? 1.10634   10.79727  -16.21763 1.000 71.29461  ? 407 LEU B CG    1 
ATOM   2556 C  CD1   . LEU A 1 328 ? 2.29232   11.24279  -15.37643 1.000 63.55724  ? 407 LEU B CD1   1 
ATOM   2557 C  CD2   . LEU A 1 328 ? 0.55835   11.95653  -17.03673 1.000 64.57872  ? 407 LEU B CD2   1 
ATOM   2558 N  N     . ASN A 1 329 ? 1.53037   7.98795   -14.12767 1.000 74.56709  ? 408 ASN B N     1 
ATOM   2559 C  CA    . ASN A 1 329 ? 0.74286   7.47689   -13.00911 1.000 67.67997  ? 408 ASN B CA    1 
ATOM   2560 C  C     . ASN A 1 329 ? 0.38924   8.64292   -12.09577 1.000 71.84044  ? 408 ASN B C     1 
ATOM   2561 O  O     . ASN A 1 329 ? 1.26702   9.21115   -11.43650 1.000 75.83271  ? 408 ASN B O     1 
ATOM   2562 C  CB    . ASN A 1 329 ? 1.50778   6.39717   -12.24414 1.000 57.70822  ? 408 ASN B CB    1 
ATOM   2563 C  CG    . ASN A 1 329 ? 0.63193   5.64802   -11.25581 1.000 65.36804  ? 408 ASN B CG    1 
ATOM   2564 O  OD1   . ASN A 1 329 ? -0.46803  6.08627   -10.92501 1.000 65.94587  ? 408 ASN B OD1   1 
ATOM   2565 N  ND2   . ASN A 1 329 ? 1.12098   4.51057   -10.77691 1.000 65.16252  ? 408 ASN B ND2   1 
ATOM   2566 N  N     . LEU A 1 330 ? -0.89512  8.99274   -12.05291 1.000 69.97322  ? 409 LEU B N     1 
ATOM   2567 C  CA    . LEU A 1 330 ? -1.39901  10.04005  -11.17386 1.000 66.96353  ? 409 LEU B CA    1 
ATOM   2568 C  C     . LEU A 1 330 ? -2.43403  9.48654   -10.20089 1.000 71.54052  ? 409 LEU B C     1 
ATOM   2569 O  O     . LEU A 1 330 ? -3.36441  10.19033  -9.80256  1.000 77.04866  ? 409 LEU B O     1 
ATOM   2570 C  CB    . LEU A 1 330 ? -1.98430  11.19397  -11.98696 1.000 61.90248  ? 409 LEU B CB    1 
ATOM   2571 C  CG    . LEU A 1 330 ? -0.99746  12.00616  -12.82896 1.000 65.73644  ? 409 LEU B CG    1 
ATOM   2572 C  CD1   . LEU A 1 330 ? -1.73495  12.93165  -13.77931 1.000 71.40459  ? 409 LEU B CD1   1 
ATOM   2573 C  CD2   . LEU A 1 330 ? -0.05845  12.79992  -11.93761 1.000 71.54292  ? 409 LEU B CD2   1 
ATOM   2574 N  N     . ALA A 1 331 ? -2.28000  8.22417   -9.81080  1.000 71.60505  ? 410 ALA B N     1 
ATOM   2575 C  CA    . ALA A 1 331 ? -3.25671  7.58504   -8.94555  1.000 73.08687  ? 410 ALA B CA    1 
ATOM   2576 C  C     . ALA A 1 331 ? -3.17209  8.13779   -7.52495  1.000 74.35150  ? 410 ALA B C     1 
ATOM   2577 O  O     . ALA A 1 331 ? -2.14115  8.65472   -7.08805  1.000 77.36927  ? 410 ALA B O     1 
ATOM   2578 C  CB    . ALA A 1 331 ? -3.05577  6.06937   -8.93166  1.000 61.91942  ? 410 ALA B CB    1 
ATOM   2579 N  N     . THR A 1 332 ? -4.28997  8.02838   -6.80906  1.000 77.93464  ? 411 THR B N     1 
ATOM   2580 C  CA    . THR A 1 332 ? -4.40525  8.43127   -5.40748  1.000 70.79476  ? 411 THR B CA    1 
ATOM   2581 C  C     . THR A 1 332 ? -3.97678  9.89098   -5.21737  1.000 73.42489  ? 411 THR B C     1 
ATOM   2582 O  O     . THR A 1 332 ? -2.95551  10.21061  -4.61056  1.000 72.09335  ? 411 THR B O     1 
ATOM   2583 C  CB    . THR A 1 332 ? -3.60532  7.48177   -4.50925  1.000 62.67146  ? 411 THR B CB    1 
ATOM   2584 O  OG1   . THR A 1 332 ? -3.94235  6.12680   -4.83362  1.000 69.45670  ? 411 THR B OG1   1 
ATOM   2585 C  CG2   . THR A 1 332 ? -3.92920  7.72860   -3.04278  1.000 67.59636  ? 411 THR B CG2   1 
ATOM   2586 N  N     . ASN A 1 333 ? -4.79932  10.77357  -5.77093  1.000 77.93201  ? 412 ASN B N     1 
ATOM   2587 C  CA    . ASN A 1 333 ? -4.63607  12.21274  -5.59197  1.000 80.89050  ? 412 ASN B CA    1 
ATOM   2588 C  C     . ASN A 1 333 ? -6.02652  12.81070  -5.40790  1.000 79.57815  ? 412 ASN B C     1 
ATOM   2589 O  O     . ASN A 1 333 ? -6.98267  12.11774  -5.04287  1.000 87.81235  ? 412 ASN B O     1 
ATOM   2590 C  CB    . ASN A 1 333 ? -3.86202  12.83103  -6.76740  1.000 82.13854  ? 412 ASN B CB    1 
ATOM   2591 C  CG    . ASN A 1 333 ? -2.36375  12.59431  -6.67099  1.000 82.01157  ? 412 ASN B CG    1 
ATOM   2592 O  OD1   . ASN A 1 333 ? -1.66199  13.28827  -5.93545  1.000 81.20909  ? 412 ASN B OD1   1 
ATOM   2593 N  ND2   . ASN A 1 333 ? -1.86606  11.61858  -7.42324  1.000 67.56543  ? 412 ASN B ND2   1 
ATOM   2594 N  N     . GLN A 1 334 ? -6.15299  14.11041  -5.65593  1.000 82.96225  ? 413 GLN B N     1 
ATOM   2595 C  CA    . GLN A 1 334 ? -7.42855  14.80523  -5.53541  1.000 86.80949  ? 413 GLN B CA    1 
ATOM   2596 C  C     . GLN A 1 334 ? -7.76781  15.52971  -6.82805  1.000 81.68520  ? 413 GLN B C     1 
ATOM   2597 O  O     . GLN A 1 334 ? -8.34558  16.62005  -6.81862  1.000 85.24382  ? 413 GLN B O     1 
ATOM   2598 C  CB    . GLN A 1 334 ? -7.42050  15.77961  -4.35894  1.000 90.38147  ? 413 GLN B CB    1 
ATOM   2599 C  CG    . GLN A 1 334 ? -7.01412  15.15965  -3.03197  1.000 87.82990  ? 413 GLN B CG    1 
ATOM   2600 C  CD    . GLN A 1 334 ? -5.52741  15.28388  -2.76663  1.000 105.09269 ? 413 GLN B CD    1 
ATOM   2601 O  OE1   . GLN A 1 334 ? -4.95717  16.37067  -2.87106  1.000 115.26968 ? 413 GLN B OE1   1 
ATOM   2602 N  NE2   . GLN A 1 334 ? -4.88926  14.16908  -2.42521  1.000 93.65884  ? 413 GLN B NE2   1 
ATOM   2603 N  N     . LEU A 1 335 ? -7.41387  14.93223  -7.96292  1.000 82.34160  ? 414 LEU B N     1 
ATOM   2604 C  CA    . LEU A 1 335 ? -7.68773  15.54670  -9.25554  1.000 78.25286  ? 414 LEU B CA    1 
ATOM   2605 C  C     . LEU A 1 335 ? -9.18072  15.49843  -9.54666  1.000 86.97695  ? 414 LEU B C     1 
ATOM   2606 O  O     . LEU A 1 335 ? -9.78016  14.41872  -9.58920  1.000 86.50775  ? 414 LEU B O     1 
ATOM   2607 C  CB    . LEU A 1 335 ? -6.90570  14.83906  -10.35737 1.000 76.53237  ? 414 LEU B CB    1 
ATOM   2608 C  CG    . LEU A 1 335 ? -5.38694  14.97783  -10.29187 1.000 87.34212  ? 414 LEU B CG    1 
ATOM   2609 C  CD1   . LEU A 1 335 ? -4.73559  14.15801  -11.39231 1.000 90.34700  ? 414 LEU B CD1   1 
ATOM   2610 C  CD2   . LEU A 1 335 ? -4.98425  16.44104  -10.39126 1.000 84.07396  ? 414 LEU B CD2   1 
ATOM   2611 N  N     . THR A 1 336 ? -9.77896  16.66947  -9.74782  1.000 94.15809  ? 415 THR B N     1 
ATOM   2612 C  CA    . THR A 1 336 ? -11.19760 16.77719  -10.04983 1.000 85.09937  ? 415 THR B CA    1 
ATOM   2613 C  C     . THR A 1 336 ? -11.47817 16.93204  -11.53648 1.000 87.47338  ? 415 THR B C     1 
ATOM   2614 O  O     . THR A 1 336 ? -12.64526 16.87704  -11.94041 1.000 87.13153  ? 415 THR B O     1 
ATOM   2615 C  CB    . THR A 1 336 ? -11.80556 17.96469  -9.29775  1.000 83.79706  ? 415 THR B CB    1 
ATOM   2616 O  OG1   . THR A 1 336 ? -11.19209 19.17754  -9.75091  1.000 94.98255  ? 415 THR B OG1   1 
ATOM   2617 C  CG2   . THR A 1 336 ? -11.56736 17.81718  -7.80408  1.000 96.51616  ? 415 THR B CG2   1 
ATOM   2618 N  N     . LYS A 1 337 ? -10.44597 17.11955  -12.35391 1.000 83.22721  ? 416 LYS B N     1 
ATOM   2619 C  CA    . LYS A 1 337 ? -10.63688 17.36423  -13.77341 1.000 79.58578  ? 416 LYS B CA    1 
ATOM   2620 C  C     . LYS A 1 337 ? -9.33675  17.06456  -14.50274 1.000 83.60715  ? 416 LYS B C     1 
ATOM   2621 O  O     . LYS A 1 337 ? -8.25097  17.36084  -13.99670 1.000 84.61020  ? 416 LYS B O     1 
ATOM   2622 C  CB    . LYS A 1 337 ? -11.08342 18.81111  -14.02470 1.000 80.66120  ? 416 LYS B CB    1 
ATOM   2623 C  CG    . LYS A 1 337 ? -10.25207 19.56937  -15.04953 1.000 92.98020  ? 416 LYS B CG    1 
ATOM   2624 C  CD    . LYS A 1 337 ? -9.79455  20.91647  -14.50459 1.000 100.25014 ? 416 LYS B CD    1 
ATOM   2625 C  CE    . LYS A 1 337 ? -8.90616  20.74741  -13.27849 1.000 101.98719 ? 416 LYS B CE    1 
ATOM   2626 N  NZ    . LYS A 1 337 ? -8.45197  22.05640  -12.72710 1.000 97.76919  ? 416 LYS B NZ    1 
ATOM   2627 N  N     . ILE A 1 338 ? -9.45879  16.46135  -15.67788 1.000 91.75719  ? 417 ILE B N     1 
ATOM   2628 C  CA    . ILE A 1 338 ? -8.33344  16.23992  -16.58106 1.000 84.21470  ? 417 ILE B CA    1 
ATOM   2629 C  C     . ILE A 1 338 ? -8.42779  17.27276  -17.69924 1.000 81.81318  ? 417 ILE B C     1 
ATOM   2630 O  O     . ILE A 1 338 ? -9.42818  17.28044  -18.43251 1.000 82.10520  ? 417 ILE B O     1 
ATOM   2631 C  CB    . ILE A 1 338 ? -8.33350  14.81418  -17.14908 1.000 85.42535  ? 417 ILE B CB    1 
ATOM   2632 C  CG1   . ILE A 1 338 ? -8.19178  13.79176  -16.02088 1.000 83.91382  ? 417 ILE B CG1   1 
ATOM   2633 C  CG2   . ILE A 1 338 ? -7.21897  14.65176  -18.17045 1.000 85.73401  ? 417 ILE B CG2   1 
ATOM   2634 C  CD1   . ILE A 1 338 ? -6.95069  13.98107  -15.17818 1.000 77.63481  ? 417 ILE B CD1   1 
ATOM   2635 N  N     . PRO A 1 339 ? -7.43789  18.14804  -17.86257 1.000 81.72177  ? 418 PRO B N     1 
ATOM   2636 C  CA    . PRO A 1 339 ? -7.55366  19.21952  -18.85738 1.000 73.72335  ? 418 PRO B CA    1 
ATOM   2637 C  C     . PRO A 1 339 ? -7.62230  18.67788  -20.27793 1.000 86.71296  ? 418 PRO B C     1 
ATOM   2638 O  O     . PRO A 1 339 ? -7.18287  17.56484  -20.57536 1.000 82.30703  ? 418 PRO B O     1 
ATOM   2639 C  CB    . PRO A 1 339 ? -6.27878  20.04612  -18.64170 1.000 82.39953  ? 418 PRO B CB    1 
ATOM   2640 C  CG    . PRO A 1 339 ? -5.80600  19.68217  -17.26539 1.000 92.91171  ? 418 PRO B CG    1 
ATOM   2641 C  CD    . PRO A 1 339 ? -6.19904  18.25195  -17.07457 1.000 89.53746  ? 418 PRO B CD    1 
ATOM   2642 N  N     . GLU A 1 340 ? -8.19424  19.49663  -21.16656 1.000 91.30936  ? 419 GLU B N     1 
ATOM   2643 C  CA    . GLU A 1 340 ? -8.24366  19.15182  -22.58241 1.000 89.16470  ? 419 GLU B CA    1 
ATOM   2644 C  C     . GLU A 1 340 ? -6.85905  19.09752  -23.21263 1.000 90.90812  ? 419 GLU B C     1 
ATOM   2645 O  O     . GLU A 1 340 ? -6.69363  18.46546  -24.26168 1.000 86.30920  ? 419 GLU B O     1 
ATOM   2646 C  CB    . GLU A 1 340 ? -9.11335  20.15465  -23.34219 1.000 83.45826  ? 419 GLU B CB    1 
ATOM   2647 C  CG    . GLU A 1 340 ? -10.59307 20.07957  -23.01805 1.000 95.49306  ? 419 GLU B CG    1 
ATOM   2648 C  CD    . GLU A 1 340 ? -11.26561 18.86260  -23.62502 1.000 95.60601  ? 419 GLU B CD    1 
ATOM   2649 O  OE1   . GLU A 1 340 ? -10.62505 18.17064  -24.44645 1.000 89.22670  ? 419 GLU B OE1   1 
ATOM   2650 O  OE2   . GLU A 1 340 ? -12.43579 18.59473  -23.27530 1.000 90.25159  ? 419 GLU B OE2   1 
ATOM   2651 N  N     . ASP A 1 341 ? -5.86482  19.74011  -22.59747 1.000 92.42532  ? 420 ASP B N     1 
ATOM   2652 C  CA    . ASP A 1 341 ? -4.49738  19.72941  -23.10377 1.000 90.02744  ? 420 ASP B CA    1 
ATOM   2653 C  C     . ASP A 1 341 ? -3.84844  18.35567  -23.03224 1.000 87.86398  ? 420 ASP B C     1 
ATOM   2654 O  O     . ASP A 1 341 ? -2.71259  18.20503  -23.49301 1.000 91.25660  ? 420 ASP B O     1 
ATOM   2655 C  CB    . ASP A 1 341 ? -3.64991  20.74143  -22.33127 1.000 99.68200  ? 420 ASP B CB    1 
ATOM   2656 C  CG    . ASP A 1 341 ? -4.27170  22.12339  -22.31014 1.000 120.42257 ? 420 ASP B CG    1 
ATOM   2657 O  OD1   . ASP A 1 341 ? -5.34941  22.28058  -21.69705 1.000 113.20844 ? 420 ASP B OD1   1 
ATOM   2658 O  OD2   . ASP A 1 341 ? -3.68502  23.05171  -22.90628 1.000 135.72486 ? 420 ASP B OD2   1 
ATOM   2659 N  N     . VAL A 1 342 ? -4.53143  17.35640  -22.47145 1.000 88.56621  ? 421 VAL B N     1 
ATOM   2660 C  CA    . VAL A 1 342 ? -4.01271  15.99841  -22.43262 1.000 78.00487  ? 421 VAL B CA    1 
ATOM   2661 C  C     . VAL A 1 342 ? -3.85789  15.39868  -23.82322 1.000 77.97290  ? 421 VAL B C     1 
ATOM   2662 O  O     . VAL A 1 342 ? -3.17521  14.38303  -23.98213 1.000 80.94020  ? 421 VAL B O     1 
ATOM   2663 C  CB    . VAL A 1 342 ? -4.92983  15.11807  -21.55385 1.000 83.69014  ? 421 VAL B CB    1 
ATOM   2664 C  CG1   . VAL A 1 342 ? -6.22683  14.79517  -22.28546 1.000 83.17931  ? 421 VAL B CG1   1 
ATOM   2665 C  CG2   . VAL A 1 342 ? -4.21042  13.84976  -21.11083 1.000 80.96759  ? 421 VAL B CG2   1 
ATOM   2666 N  N     . SER A 1 343 ? -4.46288  16.01320  -24.84176 1.000 81.12801  ? 422 SER B N     1 
ATOM   2667 C  CA    . SER A 1 343 ? -4.36599  15.49950  -26.20205 1.000 83.38254  ? 422 SER B CA    1 
ATOM   2668 C  C     . SER A 1 343 ? -2.96107  15.60584  -26.78076 1.000 80.49737  ? 422 SER B C     1 
ATOM   2669 O  O     . SER A 1 343 ? -2.69073  14.98447  -27.81366 1.000 83.88465  ? 422 SER B O     1 
ATOM   2670 C  CB    . SER A 1 343 ? -5.35383  16.23628  -27.10686 1.000 77.35254  ? 422 SER B CB    1 
ATOM   2671 O  OG    . SER A 1 343 ? -5.14776  17.63558  -27.04494 1.000 89.47246  ? 422 SER B OG    1 
ATOM   2672 N  N     . GLY A 1 344 ? -2.06722  16.36708  -26.14995 1.000 75.73751  ? 423 GLY B N     1 
ATOM   2673 C  CA    . GLY A 1 344 ? -0.71006  16.50020  -26.64539 1.000 79.68615  ? 423 GLY B CA    1 
ATOM   2674 C  C     . GLY A 1 344 ? 0.22827   15.37566  -26.27063 1.000 82.83110  ? 423 GLY B C     1 
ATOM   2675 O  O     . GLY A 1 344 ? 1.31170   15.27041  -26.85368 1.000 81.19957  ? 423 GLY B O     1 
ATOM   2676 N  N     . LEU A 1 345 ? -0.15874  14.53325  -25.31244 1.000 84.97793  ? 424 LEU B N     1 
ATOM   2677 C  CA    . LEU A 1 345 ? 0.67115   13.41257  -24.87294 1.000 74.14909  ? 424 LEU B CA    1 
ATOM   2678 C  C     . LEU A 1 345 ? 0.48663   12.22006  -25.81507 1.000 75.54389  ? 424 LEU B C     1 
ATOM   2679 O  O     . LEU A 1 345 ? 0.00893   11.15031  -25.43823 1.000 75.84303  ? 424 LEU B O     1 
ATOM   2680 C  CB    . LEU A 1 345 ? 0.33038   13.04116  -23.43560 1.000 77.30567  ? 424 LEU B CB    1 
ATOM   2681 C  CG    . LEU A 1 345 ? 0.08701   14.19245  -22.45642 1.000 79.17145  ? 424 LEU B CG    1 
ATOM   2682 C  CD1   . LEU A 1 345 ? -0.25167  13.65387  -21.07640 1.000 79.15217  ? 424 LEU B CD1   1 
ATOM   2683 C  CD2   . LEU A 1 345 ? 1.28808   15.11986  -22.38895 1.000 87.39156  ? 424 LEU B CD2   1 
ATOM   2684 N  N     . VAL A 1 346 ? 0.88501   12.42776  -27.07292 1.000 77.05656  ? 425 VAL B N     1 
ATOM   2685 C  CA    . VAL A 1 346 ? 0.62833   11.43408  -28.10923 1.000 81.88116  ? 425 VAL B CA    1 
ATOM   2686 C  C     . VAL A 1 346 ? 1.51547   10.20408  -27.96968 1.000 84.36264  ? 425 VAL B C     1 
ATOM   2687 O  O     . VAL A 1 346 ? 1.22623   9.16849   -28.57977 1.000 99.10096  ? 425 VAL B O     1 
ATOM   2688 C  CB    . VAL A 1 346 ? 0.79314   12.06488  -29.50511 1.000 76.77696  ? 425 VAL B CB    1 
ATOM   2689 C  CG1   . VAL A 1 346 ? -0.27340  13.12031  -29.73073 1.000 68.97680  ? 425 VAL B CG1   1 
ATOM   2690 C  CG2   . VAL A 1 346 ? 2.18028   12.66684  -29.65538 1.000 74.01436  ? 425 VAL B CG2   1 
ATOM   2691 N  N     . SER A 1 347 ? 2.58559   10.28022  -27.18357 1.000 81.83249  ? 426 SER B N     1 
ATOM   2692 C  CA    . SER A 1 347 ? 3.45764   9.13651   -26.95677 1.000 83.09697  ? 426 SER B CA    1 
ATOM   2693 C  C     . SER A 1 347 ? 3.09599   8.36279   -25.69637 1.000 72.78822  ? 426 SER B C     1 
ATOM   2694 O  O     . SER A 1 347 ? 3.85672   7.48062   -25.28547 1.000 80.35499  ? 426 SER B O     1 
ATOM   2695 C  CB    . SER A 1 347 ? 4.91766   9.59148   -26.88881 1.000 83.75019  ? 426 SER B CB    1 
ATOM   2696 O  OG    . SER A 1 347 ? 5.33021   10.14861  -28.12435 1.000 81.39152  ? 426 SER B OG    1 
ATOM   2697 N  N     . LEU A 1 348 ? 1.95449   8.66573   -25.08399 1.000 78.24435  ? 427 LEU B N     1 
ATOM   2698 C  CA    . LEU A 1 348 ? 1.55049   8.01623   -23.84494 1.000 72.95495  ? 427 LEU B CA    1 
ATOM   2699 C  C     . LEU A 1 348 ? 1.01618   6.61884   -24.13499 1.000 72.07630  ? 427 LEU B C     1 
ATOM   2700 O  O     . LEU A 1 348 ? 0.18046   6.43573   -25.02564 1.000 69.55012  ? 427 LEU B O     1 
ATOM   2701 C  CB    . LEU A 1 348 ? 0.48779   8.85375   -23.13377 1.000 71.83954  ? 427 LEU B CB    1 
ATOM   2702 C  CG    . LEU A 1 348 ? 0.25731   8.58040   -21.64805 1.000 74.49792  ? 427 LEU B CG    1 
ATOM   2703 C  CD1   . LEU A 1 348 ? 1.46660   9.01873   -20.83625 1.000 65.55526  ? 427 LEU B CD1   1 
ATOM   2704 C  CD2   . LEU A 1 348 ? -1.00364  9.27734   -21.16177 1.000 62.25914  ? 427 LEU B CD2   1 
ATOM   2705 N  N     . GLU A 1 349 ? 1.50250   5.63164   -23.38412 1.000 72.84186  ? 428 GLU B N     1 
ATOM   2706 C  CA    . GLU A 1 349 ? 1.05532   4.25409   -23.54052 1.000 72.66720  ? 428 GLU B CA    1 
ATOM   2707 C  C     . GLU A 1 349 ? 0.31800   3.71166   -22.32841 1.000 69.54756  ? 428 GLU B C     1 
ATOM   2708 O  O     . GLU A 1 349 ? -0.50821  2.80888   -22.47904 1.000 68.10775  ? 428 GLU B O     1 
ATOM   2709 C  CB    . GLU A 1 349 ? 2.24546   3.33670   -23.85182 1.000 71.67164  ? 428 GLU B CB    1 
ATOM   2710 C  CG    . GLU A 1 349 ? 2.92801   3.65050   -25.17485 1.000 79.88495  ? 428 GLU B CG    1 
ATOM   2711 C  CD    . GLU A 1 349 ? 4.03799   2.67479   -25.51618 1.000 80.62012  ? 428 GLU B CD    1 
ATOM   2712 O  OE1   . GLU A 1 349 ? 4.17060   1.64641   -24.81829 1.000 80.10478  ? 428 GLU B OE1   1 
ATOM   2713 O  OE2   . GLU A 1 349 ? 4.77815   2.93906   -26.48729 1.000 82.83339  ? 428 GLU B OE2   1 
ATOM   2714 N  N     . VAL A 1 350 ? 0.58880   4.23863   -21.13711 1.000 59.91564  ? 429 VAL B N     1 
ATOM   2715 C  CA    . VAL A 1 350 ? -0.08402  3.81722   -19.91527 1.000 70.58254  ? 429 VAL B CA    1 
ATOM   2716 C  C     . VAL A 1 350 ? -0.48090  5.05855   -19.13070 1.000 69.46333  ? 429 VAL B C     1 
ATOM   2717 O  O     . VAL A 1 350 ? 0.36449   5.91255   -18.84033 1.000 72.45995  ? 429 VAL B O     1 
ATOM   2718 C  CB    . VAL A 1 350 ? 0.80411   2.89614   -19.05806 1.000 61.30199  ? 429 VAL B CB    1 
ATOM   2719 C  CG1   . VAL A 1 350 ? 0.14004   2.63084   -17.71962 1.000 69.34984  ? 429 VAL B CG1   1 
ATOM   2720 C  CG2   . VAL A 1 350 ? 1.07566   1.59094   -19.78733 1.000 59.17461  ? 429 VAL B CG2   1 
ATOM   2721 N  N     . LEU A 1 351 ? -1.76303  5.15548   -18.78725 1.000 71.38616  ? 430 LEU B N     1 
ATOM   2722 C  CA    . LEU A 1 351 ? -2.29773  6.28536   -18.03342 1.000 73.30420  ? 430 LEU B CA    1 
ATOM   2723 C  C     . LEU A 1 351 ? -3.10360  5.74280   -16.86160 1.000 70.36046  ? 430 LEU B C     1 
ATOM   2724 O  O     . LEU A 1 351 ? -4.16562  5.14234   -17.05864 1.000 70.91872  ? 430 LEU B O     1 
ATOM   2725 C  CB    . LEU A 1 351 ? -3.15920  7.18206   -18.92188 1.000 67.22632  ? 430 LEU B CB    1 
ATOM   2726 C  CG    . LEU A 1 351 ? -3.72366  8.43665   -18.25740 1.000 76.94330  ? 430 LEU B CG    1 
ATOM   2727 C  CD1   . LEU A 1 351 ? -2.60316  9.25887   -17.64095 1.000 66.83434  ? 430 LEU B CD1   1 
ATOM   2728 C  CD2   . LEU A 1 351 ? -4.51470  9.26411   -19.26313 1.000 68.23719  ? 430 LEU B CD2   1 
ATOM   2729 N  N     . ILE A 1 352 ? -2.59943  5.95133   -15.64871 1.000 70.42688  ? 431 ILE B N     1 
ATOM   2730 C  CA    . ILE A 1 352 ? -3.23906  5.47829   -14.42646 1.000 71.25159  ? 431 ILE B CA    1 
ATOM   2731 C  C     . ILE A 1 352 ? -3.78585  6.68896   -13.68444 1.000 70.66448  ? 431 ILE B C     1 
ATOM   2732 O  O     . ILE A 1 352 ? -3.02062  7.56606   -13.26385 1.000 73.95538  ? 431 ILE B O     1 
ATOM   2733 C  CB    . ILE A 1 352 ? -2.26215  4.68789   -13.54355 1.000 68.35764  ? 431 ILE B CB    1 
ATOM   2734 C  CG1   . ILE A 1 352 ? -1.51446  3.64077   -14.37340 1.000 66.29354  ? 431 ILE B CG1   1 
ATOM   2735 C  CG2   . ILE A 1 352 ? -3.00436  4.03186   -12.38933 1.000 71.94673  ? 431 ILE B CG2   1 
ATOM   2736 C  CD1   . ILE A 1 352 ? -2.40559  2.58055   -14.97752 1.000 72.62589  ? 431 ILE B CD1   1 
ATOM   2737 N  N     . LEU A 1 353 ? -5.10893  6.73543   -13.51969 1.000 68.40376  ? 432 LEU B N     1 
ATOM   2738 C  CA    . LEU A 1 353 ? -5.77895  7.84082   -12.84406 1.000 70.40417  ? 432 LEU B CA    1 
ATOM   2739 C  C     . LEU A 1 353 ? -6.72059  7.33402   -11.75944 1.000 74.53871  ? 432 LEU B C     1 
ATOM   2740 O  O     . LEU A 1 353 ? -7.69858  8.00392   -11.41463 1.000 75.70610  ? 432 LEU B O     1 
ATOM   2741 C  CB    . LEU A 1 353 ? -6.54325  8.70773   -13.84309 1.000 67.96379  ? 432 LEU B CB    1 
ATOM   2742 C  CG    . LEU A 1 353 ? -5.72019  9.39976   -14.92736 1.000 67.10112  ? 432 LEU B CG    1 
ATOM   2743 C  CD1   . LEU A 1 353 ? -6.64131  10.06323  -15.93033 1.000 78.14100  ? 432 LEU B CD1   1 
ATOM   2744 C  CD2   . LEU A 1 353 ? -4.77251  10.41654  -14.31379 1.000 65.24154  ? 432 LEU B CD2   1 
ATOM   2745 N  N     . SER A 1 354 ? -6.44031  6.15535   -11.21288 1.000 79.05548  ? 433 SER B N     1 
ATOM   2746 C  CA    . SER A 1 354 ? -7.32774  5.56101   -10.22601 1.000 73.62269  ? 433 SER B CA    1 
ATOM   2747 C  C     . SER A 1 354 ? -7.27607  6.32681   -8.90587  1.000 81.92377  ? 433 SER B C     1 
ATOM   2748 O  O     . SER A 1 354 ? -6.25980  6.92554   -8.54617  1.000 75.76333  ? 433 SER B O     1 
ATOM   2749 C  CB    . SER A 1 354 ? -6.96727  4.09174   -10.00690 1.000 55.20031  ? 433 SER B CB    1 
ATOM   2750 O  OG    . SER A 1 354 ? -5.56874  3.89355   -10.09440 1.000 74.44471  ? 433 SER B OG    1 
ATOM   2751 N  N     . ASN A 1 355 ? -8.40574  6.31578   -8.19431  1.000 80.79777  ? 434 ASN B N     1 
ATOM   2752 C  CA    . ASN A 1 355 ? -8.55850  6.97192   -6.89335  1.000 69.56313  ? 434 ASN B CA    1 
ATOM   2753 C  C     . ASN A 1 355 ? -8.34506  8.48565   -6.99701  1.000 74.35956  ? 434 ASN B C     1 
ATOM   2754 O  O     . ASN A 1 355 ? -7.44596  9.06265   -6.38263  1.000 72.34907  ? 434 ASN B O     1 
ATOM   2755 C  CB    . ASN A 1 355 ? -7.62818  6.34476   -5.84914  1.000 70.99219  ? 434 ASN B CB    1 
ATOM   2756 C  CG    . ASN A 1 355 ? -8.03065  4.92394   -5.49193  1.000 84.44553  ? 434 ASN B CG    1 
ATOM   2757 O  OD1   . ASN A 1 355 ? -8.90829  4.70660   -4.65471  1.000 89.88197  ? 434 ASN B OD1   1 
ATOM   2758 N  ND2   . ASN A 1 355 ? -7.39243  3.94871   -6.12938  1.000 76.66219  ? 434 ASN B ND2   1 
ATOM   2759 N  N     . ASN A 1 356 ? -9.21112  9.12352   -7.78269  1.000 73.39288  ? 435 ASN B N     1 
ATOM   2760 C  CA    . ASN A 1 356 ? -9.26369  10.57810  -7.88748  1.000 76.94571  ? 435 ASN B CA    1 
ATOM   2761 C  C     . ASN A 1 356 ? -10.72680 11.01130  -7.84884  1.000 83.18062  ? 435 ASN B C     1 
ATOM   2762 O  O     . ASN A 1 356 ? -11.62739 10.20648  -7.59300  1.000 88.36391  ? 435 ASN B O     1 
ATOM   2763 C  CB    . ASN A 1 356 ? -8.55547  11.06861  -9.15626  1.000 74.72651  ? 435 ASN B CB    1 
ATOM   2764 C  CG    . ASN A 1 356 ? -7.05353  11.08743  -9.01338  1.000 77.02179  ? 435 ASN B CG    1 
ATOM   2765 O  OD1   . ASN A 1 356 ? -6.47642  12.07819  -8.56652  1.000 81.91969  ? 435 ASN B OD1   1 
ATOM   2766 N  ND2   . ASN A 1 356 ? -6.40728  9.99250   -9.39746  1.000 74.32235  ? 435 ASN B ND2   1 
ATOM   2767 N  N     . LEU A 1 357 ? -10.96828 12.29527  -8.10955  1.000 77.50303  ? 436 LEU B N     1 
ATOM   2768 C  CA    . LEU A 1 357 ? -12.31006 12.87052  -8.08760  1.000 81.64633  ? 436 LEU B CA    1 
ATOM   2769 C  C     . LEU A 1 357 ? -12.79428 13.23337  -9.48878  1.000 82.31612  ? 436 LEU B C     1 
ATOM   2770 O  O     . LEU A 1 357 ? -13.43790 14.26453  -9.69167  1.000 88.33752  ? 436 LEU B O     1 
ATOM   2771 C  CB    . LEU A 1 357 ? -12.36497 14.10225  -7.18537  1.000 88.07564  ? 436 LEU B CB    1 
ATOM   2772 C  CG    . LEU A 1 357 ? -12.28404 13.94675  -5.66207  1.000 81.92444  ? 436 LEU B CG    1 
ATOM   2773 C  CD1   . LEU A 1 357 ? -12.54046 12.51196  -5.21615  1.000 85.12630  ? 436 LEU B CD1   1 
ATOM   2774 C  CD2   . LEU A 1 357 ? -10.95488 14.45487  -5.13331  1.000 79.53340  ? 436 LEU B CD2   1 
ATOM   2775 N  N     . LEU A 1 358 ? -12.49981 12.38893  -10.47171 1.000 83.95111  ? 437 LEU B N     1 
ATOM   2776 C  CA    . LEU A 1 358 ? -12.86974 12.67936  -11.85081 1.000 87.14001  ? 437 LEU B CA    1 
ATOM   2777 C  C     . LEU A 1 358 ? -14.35437 12.41175  -12.05728 1.000 85.31148  ? 437 LEU B C     1 
ATOM   2778 O  O     . LEU A 1 358 ? -14.81425 11.27815  -11.88888 1.000 84.54871  ? 437 LEU B O     1 
ATOM   2779 C  CB    . LEU A 1 358 ? -12.03580 11.84286  -12.81686 1.000 83.38374  ? 437 LEU B CB    1 
ATOM   2780 C  CG    . LEU A 1 358 ? -10.54163 12.15806  -12.84502 1.000 79.60346  ? 437 LEU B CG    1 
ATOM   2781 C  CD1   . LEU A 1 358 ? -9.84852  11.31376  -13.89948 1.000 76.05995  ? 437 LEU B CD1   1 
ATOM   2782 C  CD2   . LEU A 1 358 ? -10.31320 13.64198  -13.09420 1.000 76.60348  ? 437 LEU B CD2   1 
ATOM   2783 N  N     . LYS A 1 359 ? -15.10115 13.45490  -12.42184 1.000 81.56977  ? 438 LYS B N     1 
ATOM   2784 C  CA    . LYS A 1 359 ? -16.50281 13.30537  -12.79392 1.000 86.04666  ? 438 LYS B CA    1 
ATOM   2785 C  C     . LYS A 1 359 ? -16.66789 12.92984  -14.26179 1.000 85.97752  ? 438 LYS B C     1 
ATOM   2786 O  O     . LYS A 1 359 ? -17.55921 12.14539  -14.60445 1.000 87.17825  ? 438 LYS B O     1 
ATOM   2787 C  CB    . LYS A 1 359 ? -17.27143 14.59836  -12.50617 1.000 98.00970  ? 438 LYS B CB    1 
ATOM   2788 C  CG    . LYS A 1 359 ? -18.26196 14.51288  -11.35179 1.000 97.28521  ? 438 LYS B CG    1 
ATOM   2789 C  CD    . LYS A 1 359 ? -17.68998 15.12357  -10.08076 1.000 104.09906 ? 438 LYS B CD    1 
ATOM   2790 C  CE    . LYS A 1 359 ? -18.77272 15.32846  -9.02871  1.000 109.73989 ? 438 LYS B CE    1 
ATOM   2791 N  NZ    . LYS A 1 359 ? -19.84638 16.25440  -9.49453  1.000 85.10502  ? 438 LYS B NZ    1 
ATOM   2792 N  N     . LYS A 1 360 ? -15.82982 13.48478  -15.13516 1.000 89.63382  ? 439 LYS B N     1 
ATOM   2793 C  CA    . LYS A 1 360 ? -15.86754 13.17817  -16.55761 1.000 91.99412  ? 439 LYS B CA    1 
ATOM   2794 C  C     . LYS A 1 360 ? -14.47460 13.38871  -17.13302 1.000 84.34784  ? 439 LYS B C     1 
ATOM   2795 O  O     . LYS A 1 360 ? -13.56694 13.88102  -16.45704 1.000 81.74957  ? 439 LYS B O     1 
ATOM   2796 C  CB    . LYS A 1 360 ? -16.91412 14.02973  -17.28978 1.000 87.24221  ? 439 LYS B CB    1 
ATOM   2797 C  CG    . LYS A 1 360 ? -16.92782 15.49296  -16.87520 1.000 86.53671  ? 439 LYS B CG    1 
ATOM   2798 C  CD    . LYS A 1 360 ? -18.23587 16.17490  -17.25593 1.000 86.73815  ? 439 LYS B CD    1 
ATOM   2799 C  CE    . LYS A 1 360 ? -18.12842 16.90686  -18.58695 1.000 99.38377  ? 439 LYS B CE    1 
ATOM   2800 N  NZ    . LYS A 1 360 ? -19.37642 17.66349  -18.90388 1.000 97.08889  ? 439 LYS B NZ    1 
ATOM   2801 N  N     . LEU A 1 361 ? -14.31079 13.00304  -18.39571 1.000 86.71012  ? 440 LEU B N     1 
ATOM   2802 C  CA    . LEU A 1 361 ? -13.00830 13.07113  -19.03608 1.000 87.96272  ? 440 LEU B CA    1 
ATOM   2803 C  C     . LEU A 1 361 ? -13.06091 13.96809  -20.26573 1.000 78.96257  ? 440 LEU B C     1 
ATOM   2804 O  O     . LEU A 1 361 ? -14.10543 14.07638  -20.91552 1.000 92.29157  ? 440 LEU B O     1 
ATOM   2805 C  CB    . LEU A 1 361 ? -12.52135 11.67661  -19.44377 1.000 80.74999  ? 440 LEU B CB    1 
ATOM   2806 C  CG    . LEU A 1 361 ? -12.30463 10.70933  -18.28533 1.000 75.69595  ? 440 LEU B CG    1 
ATOM   2807 C  CD1   . LEU A 1 361 ? -11.97434 9.32914   -18.81430 1.000 74.31976  ? 440 LEU B CD1   1 
ATOM   2808 C  CD2   . LEU A 1 361 ? -11.20164 11.22316  -17.37880 1.000 79.45145  ? 440 LEU B CD2   1 
ATOM   2809 N  N     . PRO A 1 362 ? -11.95353 14.62155  -20.60857 1.000 78.28439  ? 441 PRO B N     1 
ATOM   2810 C  CA    . PRO A 1 362 ? -11.96797 15.55602  -21.73702 1.000 77.00181  ? 441 PRO B CA    1 
ATOM   2811 C  C     . PRO A 1 362 ? -12.14145 14.83262  -23.06177 1.000 85.25889  ? 441 PRO B C     1 
ATOM   2812 O  O     . PRO A 1 362 ? -11.83253 13.64743  -23.20503 1.000 82.01862  ? 441 PRO B O     1 
ATOM   2813 C  CB    . PRO A 1 362 ? -10.59744 16.23332  -21.65199 1.000 82.48016  ? 441 PRO B CB    1 
ATOM   2814 C  CG    . PRO A 1 362 ? -9.73640  15.23768  -20.95597 1.000 79.41599  ? 441 PRO B CG    1 
ATOM   2815 C  CD    . PRO A 1 362 ? -10.63226 14.56355  -19.95947 1.000 78.05161  ? 441 PRO B CD    1 
ATOM   2816 N  N     . HIS A 1 363 ? -12.65621 15.57349  -24.04572 1.000 77.67661  ? 442 HIS B N     1 
ATOM   2817 C  CA    . HIS A 1 363 ? -12.82046 14.99649  -25.37288 1.000 85.39311  ? 442 HIS B CA    1 
ATOM   2818 C  C     . HIS A 1 363 ? -11.49073 14.86804  -26.10519 1.000 81.23897  ? 442 HIS B C     1 
ATOM   2819 O  O     . HIS A 1 363 ? -11.39679 14.09542  -27.06442 1.000 85.20889  ? 442 HIS B O     1 
ATOM   2820 C  CB    . HIS A 1 363 ? -13.82340 15.81822  -26.19489 1.000 84.78521  ? 442 HIS B CB    1 
ATOM   2821 C  CG    . HIS A 1 363 ? -13.50750 17.28054  -26.26705 1.000 98.47120  ? 442 HIS B CG    1 
ATOM   2822 N  ND1   . HIS A 1 363 ? -12.37291 17.77081  -26.87792 1.000 100.79411 ? 442 HIS B ND1   1 
ATOM   2823 C  CD2   . HIS A 1 363 ? -14.19012 18.36171  -25.82075 1.000 96.31235  ? 442 HIS B CD2   1 
ATOM   2824 C  CE1   . HIS A 1 363 ? -12.36608 19.08977  -26.79772 1.000 93.12442  ? 442 HIS B CE1   1 
ATOM   2825 N  NE2   . HIS A 1 363 ? -13.45748 19.47371  -26.16045 1.000 98.18688  ? 442 HIS B NE2   1 
ATOM   2826 N  N     . GLY A 1 364 ? -10.46120 15.58883  -25.66749 1.000 78.96301  ? 443 GLY B N     1 
ATOM   2827 C  CA    . GLY A 1 364 ? -9.13415  15.40099  -26.21564 1.000 80.68062  ? 443 GLY B CA    1 
ATOM   2828 C  C     . GLY A 1 364 ? -8.48531  14.07791  -25.87260 1.000 79.31081  ? 443 GLY B C     1 
ATOM   2829 O  O     . GLY A 1 364 ? -7.39778  13.79110  -26.38151 1.000 85.56999  ? 443 GLY B O     1 
ATOM   2830 N  N     . LEU A 1 365 ? -9.12328  13.26491  -25.02411 1.000 85.56118  ? 444 LEU B N     1 
ATOM   2831 C  CA    . LEU A 1 365 ? -8.56167  11.96748  -24.66440 1.000 81.52853  ? 444 LEU B CA    1 
ATOM   2832 C  C     . LEU A 1 365 ? -8.46049  11.04504  -25.87033 1.000 80.59660  ? 444 LEU B C     1 
ATOM   2833 O  O     . LEU A 1 365 ? -7.57253  10.18593  -25.92090 1.000 81.26138  ? 444 LEU B O     1 
ATOM   2834 C  CB    . LEU A 1 365 ? -9.40975  11.31115  -23.57234 1.000 77.29294  ? 444 LEU B CB    1 
ATOM   2835 C  CG    . LEU A 1 365 ? -8.91304  9.98467   -22.99660 1.000 75.82100  ? 444 LEU B CG    1 
ATOM   2836 C  CD1   . LEU A 1 365 ? -7.76532  10.21623  -22.03030 1.000 60.26924  ? 444 LEU B CD1   1 
ATOM   2837 C  CD2   . LEU A 1 365 ? -10.04936 9.23139   -22.32017 1.000 83.67588  ? 444 LEU B CD2   1 
ATOM   2838 N  N     . GLY A 1 366 ? -9.34938  11.20748  -26.84983 1.000 78.12765  ? 445 GLY B N     1 
ATOM   2839 C  CA    . GLY A 1 366 ? -9.31621  10.37519  -28.03891 1.000 75.53986  ? 445 GLY B CA    1 
ATOM   2840 C  C     . GLY A 1 366 ? -8.08451  10.55402  -28.90076 1.000 75.76430  ? 445 GLY B C     1 
ATOM   2841 O  O     . GLY A 1 366 ? -7.89126  9.77191   -29.83783 1.000 80.93641  ? 445 GLY B O     1 
ATOM   2842 N  N     . ASN A 1 367 ? -7.25614  11.55592  -28.61312 1.000 72.24355  ? 446 ASN B N     1 
ATOM   2843 C  CA    . ASN A 1 367 ? -6.04562  11.81375  -29.38071 1.000 83.20530  ? 446 ASN B CA    1 
ATOM   2844 C  C     . ASN A 1 367 ? -4.84902  11.00827  -28.88840 1.000 86.09179  ? 446 ASN B C     1 
ATOM   2845 O  O     . ASN A 1 367 ? -3.77916  11.07754  -29.50347 1.000 88.02144  ? 446 ASN B O     1 
ATOM   2846 C  CB    . ASN A 1 367 ? -5.70818  13.30989  -29.34965 1.000 81.48848  ? 446 ASN B CB    1 
ATOM   2847 C  CG    . ASN A 1 367 ? -4.76055  13.71915  -30.46441 1.000 81.40855  ? 446 ASN B CG    1 
ATOM   2848 O  OD1   . ASN A 1 367 ? -4.87856  13.25241  -31.59907 1.000 73.87834  ? 446 ASN B OD1   1 
ATOM   2849 N  ND2   . ASN A 1 367 ? -3.81017  14.59119  -30.14350 1.000 69.18385  ? 446 ASN B ND2   1 
ATOM   2850 N  N     . LEU A 1 368 ? -4.99755  10.25104  -27.79929 1.000 85.07361  ? 447 LEU B N     1 
ATOM   2851 C  CA    . LEU A 1 368 ? -3.92906  9.37995   -27.30835 1.000 75.17197  ? 447 LEU B CA    1 
ATOM   2852 C  C     . LEU A 1 368 ? -3.90863  8.12393   -28.17574 1.000 75.80541  ? 447 LEU B C     1 
ATOM   2853 O  O     . LEU A 1 368 ? -4.38553  7.04982   -27.79959 1.000 79.54074  ? 447 LEU B O     1 
ATOM   2854 C  CB    . LEU A 1 368 ? -4.12586  9.05352   -25.83370 1.000 63.66512  ? 447 LEU B CB    1 
ATOM   2855 C  CG    . LEU A 1 368 ? -4.24874  10.25407  -24.89278 1.000 63.34536  ? 447 LEU B CG    1 
ATOM   2856 C  CD1   . LEU A 1 368 ? -4.17631  9.81080   -23.44122 1.000 59.98609  ? 447 LEU B CD1   1 
ATOM   2857 C  CD2   . LEU A 1 368 ? -3.18100  11.29007  -25.19440 1.000 70.17801  ? 447 LEU B CD2   1 
ATOM   2858 N  N     . ARG A 1 369 ? -3.33251  8.28066   -29.37017 1.000 86.22550  ? 448 ARG B N     1 
ATOM   2859 C  CA    . ARG A 1 369 ? -3.28222  7.20099   -30.35105 1.000 80.44011  ? 448 ARG B CA    1 
ATOM   2860 C  C     . ARG A 1 369 ? -2.45921  6.01190   -29.86581 1.000 88.72105  ? 448 ARG B C     1 
ATOM   2861 O  O     . ARG A 1 369 ? -2.72587  4.87425   -30.26931 1.000 92.53545  ? 448 ARG B O     1 
ATOM   2862 C  CB    . ARG A 1 369 ? -2.71488  7.73752   -31.66571 1.000 87.62377  ? 448 ARG B CB    1 
ATOM   2863 C  CG    . ARG A 1 369 ? -1.62019  8.78579   -31.46286 1.000 98.87076  ? 448 ARG B CG    1 
ATOM   2864 C  CD    . ARG A 1 369 ? -1.08779  9.33996   -32.77830 1.000 112.98900 ? 448 ARG B CD    1 
ATOM   2865 N  NE    . ARG A 1 369 ? -0.29034  8.36027   -33.50656 1.000 128.40355 ? 448 ARG B NE    1 
ATOM   2866 C  CZ    . ARG A 1 369 ? 0.98809   8.10406   -33.26273 1.000 132.75506 ? 448 ARG B CZ    1 
ATOM   2867 N  NH1   . ARG A 1 369 ? 1.64755   8.72839   -32.29991 1.000 129.35470 ? 448 ARG B NH1   1 
ATOM   2868 N  NH2   . ARG A 1 369 ? 1.62034   7.19669   -34.00175 1.000 136.97255 ? 448 ARG B NH2   1 
ATOM   2869 N  N     . LYS A 1 370 ? -1.46442  6.24491   -29.01172 1.000 87.14437  ? 449 LYS B N     1 
ATOM   2870 C  CA    . LYS A 1 370 ? -0.58241  5.18439   -28.54196 1.000 81.20644  ? 449 LYS B CA    1 
ATOM   2871 C  C     . LYS A 1 370 ? -1.01858  4.58667   -27.21138 1.000 74.54749  ? 449 LYS B C     1 
ATOM   2872 O  O     . LYS A 1 370 ? -0.33510  3.69368   -26.70026 1.000 70.13232  ? 449 LYS B O     1 
ATOM   2873 C  CB    . LYS A 1 370 ? 0.85274   5.70863   -28.41319 1.000 85.76902  ? 449 LYS B CB    1 
ATOM   2874 C  CG    . LYS A 1 370 ? 1.52160   6.06896   -29.72957 1.000 83.08165  ? 449 LYS B CG    1 
ATOM   2875 C  CD    . LYS A 1 370 ? 1.66926   4.85188   -30.62718 1.000 97.27550  ? 449 LYS B CD    1 
ATOM   2876 C  CE    . LYS A 1 370 ? 2.67380   5.10694   -31.73966 1.000 103.37578 ? 449 LYS B CE    1 
ATOM   2877 N  NZ    . LYS A 1 370 ? 2.78338   3.94885   -32.66982 1.000 96.56929  ? 449 LYS B NZ    1 
ATOM   2878 N  N     . LEU A 1 371 ? -2.13149  5.04836   -26.64488 1.000 79.03557  ? 450 LEU B N     1 
ATOM   2879 C  CA    . LEU A 1 371 ? -2.53973  4.60944   -25.31653 1.000 77.17325  ? 450 LEU B CA    1 
ATOM   2880 C  C     . LEU A 1 371 ? -2.89413  3.12756   -25.32613 1.000 75.88588  ? 450 LEU B C     1 
ATOM   2881 O  O     . LEU A 1 371 ? -3.72541  2.68135   -26.12177 1.000 77.33168  ? 450 LEU B O     1 
ATOM   2882 C  CB    . LEU A 1 371 ? -3.72970  5.43366   -24.82755 1.000 73.58118  ? 450 LEU B CB    1 
ATOM   2883 C  CG    . LEU A 1 371 ? -4.02664  5.30880   -23.33114 1.000 74.92658  ? 450 LEU B CG    1 
ATOM   2884 C  CD1   . LEU A 1 371 ? -2.87908  5.88998   -22.51898 1.000 66.83865  ? 450 LEU B CD1   1 
ATOM   2885 C  CD2   . LEU A 1 371 ? -5.34252  5.97884   -22.96598 1.000 62.92655  ? 450 LEU B CD2   1 
ATOM   2886 N  N     . ARG A 1 372 ? -2.26253  2.36563   -24.43007 1.000 75.02484  ? 451 ARG B N     1 
ATOM   2887 C  CA    . ARG A 1 372 ? -2.47333  0.92904   -24.34240 1.000 66.65261  ? 451 ARG B CA    1 
ATOM   2888 C  C     . ARG A 1 372 ? -3.20761  0.49535   -23.08242 1.000 68.74692  ? 451 ARG B C     1 
ATOM   2889 O  O     . ARG A 1 372 ? -3.85000  -0.55864  -23.09660 1.000 72.04342  ? 451 ARG B O     1 
ATOM   2890 C  CB    . ARG A 1 372 ? -1.12592  0.19145   -24.41238 1.000 69.24062  ? 451 ARG B CB    1 
ATOM   2891 C  CG    . ARG A 1 372 ? -1.23558  -1.30269  -24.68883 1.000 90.58406  ? 451 ARG B CG    1 
ATOM   2892 C  CD    . ARG A 1 372 ? 0.12706   -1.99505  -24.67317 1.000 95.47887  ? 451 ARG B CD    1 
ATOM   2893 N  NE    . ARG A 1 372 ? 0.70431   -2.05633  -23.33475 1.000 91.27399  ? 451 ARG B NE    1 
ATOM   2894 C  CZ    . ARG A 1 372 ? 1.67446   -1.26409  -22.89835 1.000 91.37578  ? 451 ARG B CZ    1 
ATOM   2895 N  NH1   . ARG A 1 372 ? 2.22025   -0.34526  -23.67880 1.000 87.60962  ? 451 ARG B NH1   1 
ATOM   2896 N  NH2   . ARG A 1 372 ? 2.11045   -1.39957  -21.64848 1.000 81.37655  ? 451 ARG B NH2   1 
ATOM   2897 N  N     . GLU A 1 373 ? -3.14426  1.27828   -22.00760 1.000 66.26145  ? 452 GLU B N     1 
ATOM   2898 C  CA    . GLU A 1 373 ? -3.73543  0.88196   -20.73337 1.000 67.18281  ? 452 GLU B CA    1 
ATOM   2899 C  C     . GLU A 1 373 ? -4.24680  2.12163   -20.01662 1.000 74.72081  ? 452 GLU B C     1 
ATOM   2900 O  O     . GLU A 1 373 ? -3.47019  3.03888   -19.73250 1.000 72.72935  ? 452 GLU B O     1 
ATOM   2901 C  CB    . GLU A 1 373 ? -2.71255  0.13915   -19.87137 1.000 72.89463  ? 452 GLU B CB    1 
ATOM   2902 C  CG    . GLU A 1 373 ? -3.19465  -0.20603  -18.47515 1.000 83.26693  ? 452 GLU B CG    1 
ATOM   2903 C  CD    . GLU A 1 373 ? -2.15377  -0.97047  -17.67784 1.000 95.66364  ? 452 GLU B CD    1 
ATOM   2904 O  OE1   . GLU A 1 373 ? -1.08166  -1.28260  -18.24280 1.000 88.52104  ? 452 GLU B OE1   1 
ATOM   2905 O  OE2   . GLU A 1 373 ? -2.40699  -1.25806  -16.48785 1.000 96.44793  ? 452 GLU B OE2   1 
ATOM   2906 N  N     . LEU A 1 374 ? -5.54566  2.14302   -19.71908 1.000 73.46142  ? 453 LEU B N     1 
ATOM   2907 C  CA    . LEU A 1 374 ? -6.19477  3.27899   -19.06968 1.000 69.85127  ? 453 LEU B CA    1 
ATOM   2908 C  C     . LEU A 1 374 ? -6.92094  2.78049   -17.82785 1.000 71.74577  ? 453 LEU B C     1 
ATOM   2909 O  O     . LEU A 1 374 ? -7.88031  2.00982   -17.93533 1.000 78.90554  ? 453 LEU B O     1 
ATOM   2910 C  CB    . LEU A 1 374 ? -7.16355  3.97472   -20.02631 1.000 66.60606  ? 453 LEU B CB    1 
ATOM   2911 C  CG    . LEU A 1 374 ? -7.98106  5.14043   -19.46977 1.000 69.50304  ? 453 LEU B CG    1 
ATOM   2912 C  CD1   . LEU A 1 374 ? -7.07611  6.17959   -18.82582 1.000 67.69594  ? 453 LEU B CD1   1 
ATOM   2913 C  CD2   . LEU A 1 374 ? -8.81663  5.76764   -20.57461 1.000 59.96381  ? 453 LEU B CD2   1 
ATOM   2914 N  N     . ASP A 1 375 ? -6.46868  3.22020   -16.65488 1.000 70.86060  ? 454 ASP B N     1 
ATOM   2915 C  CA    . ASP A 1 375 ? -7.05013  2.82463   -15.37635 1.000 68.27650  ? 454 ASP B CA    1 
ATOM   2916 C  C     . ASP A 1 375 ? -7.71577  4.03962   -14.74195 1.000 72.52862  ? 454 ASP B C     1 
ATOM   2917 O  O     . ASP A 1 375 ? -7.06178  5.06458   -14.51826 1.000 74.07823  ? 454 ASP B O     1 
ATOM   2918 C  CB    . ASP A 1 375 ? -5.98150  2.24464   -14.44756 1.000 72.59038  ? 454 ASP B CB    1 
ATOM   2919 C  CG    . ASP A 1 375 ? -6.57027  1.52918   -13.23754 1.000 82.15516  ? 454 ASP B CG    1 
ATOM   2920 O  OD1   . ASP A 1 375 ? -7.65638  1.92394   -12.76157 1.000 80.60797  ? 454 ASP B OD1   1 
ATOM   2921 O  OD2   . ASP A 1 375 ? -5.93616  0.56618   -12.75543 1.000 82.52393  ? 454 ASP B OD2   1 
ATOM   2922 N  N     . LEU A 1 376 ? -9.01233  3.91909   -14.44914 1.000 66.67680  ? 455 LEU B N     1 
ATOM   2923 C  CA    . LEU A 1 376 ? -9.78815  4.98831   -13.82988 1.000 74.55388  ? 455 LEU B CA    1 
ATOM   2924 C  C     . LEU A 1 376 ? -10.59200 4.46614   -12.64454 1.000 74.82912  ? 455 LEU B C     1 
ATOM   2925 O  O     . LEU A 1 376 ? -11.68436 4.96336   -12.35823 1.000 77.81179  ? 455 LEU B O     1 
ATOM   2926 C  CB    . LEU A 1 376 ? -10.71298 5.65069   -14.85028 1.000 73.07909  ? 455 LEU B CB    1 
ATOM   2927 C  CG    . LEU A 1 376 ? -10.04137 6.43915   -15.97288 1.000 69.04957  ? 455 LEU B CG    1 
ATOM   2928 C  CD1   . LEU A 1 376 ? -10.83813 6.29834   -17.25268 1.000 62.87475  ? 455 LEU B CD1   1 
ATOM   2929 C  CD2   . LEU A 1 376 ? -9.90243  7.90206   -15.58453 1.000 64.47303  ? 455 LEU B CD2   1 
ATOM   2930 N  N     . GLU A 1 377 ? -10.06009 3.46781   -11.94635 1.000 71.64279  ? 456 GLU B N     1 
ATOM   2931 C  CA    . GLU A 1 377 ? -10.79158 2.82597   -10.86461 1.000 71.86007  ? 456 GLU B CA    1 
ATOM   2932 C  C     . GLU A 1 377 ? -10.98459 3.78076   -9.69080  1.000 78.82796  ? 456 GLU B C     1 
ATOM   2933 O  O     . GLU A 1 377 ? -10.09669 4.56727   -9.35535  1.000 77.18526  ? 456 GLU B O     1 
ATOM   2934 C  CB    . GLU A 1 377 ? -10.04813 1.56919   -10.41322 1.000 83.59311  ? 456 GLU B CB    1 
ATOM   2935 C  CG    . GLU A 1 377 ? -10.71297 0.80383   -9.28308  1.000 94.57947  ? 456 GLU B CG    1 
ATOM   2936 C  CD    . GLU A 1 377 ? -9.96638  -0.46829  -8.93155  1.000 90.41121  ? 456 GLU B CD    1 
ATOM   2937 O  OE1   . GLU A 1 377 ? -9.38018  -1.08712  -9.84561  1.000 77.96296  ? 456 GLU B OE1   1 
ATOM   2938 O  OE2   . GLU A 1 377 ? -9.96046  -0.84409  -7.74040  1.000 98.92311  ? 456 GLU B OE2   1 
ATOM   2939 N  N     . GLU A 1 378 ? -12.16470 3.71399   -9.07384  1.000 73.24925  ? 457 GLU B N     1 
ATOM   2940 C  CA    . GLU A 1 378 ? -12.49242 4.49278   -7.87866  1.000 80.60807  ? 457 GLU B CA    1 
ATOM   2941 C  C     . GLU A 1 378 ? -12.41374 5.99786   -8.14877  1.000 73.46037  ? 457 GLU B C     1 
ATOM   2942 O  O     . GLU A 1 378 ? -11.69099 6.74430   -7.48725  1.000 69.70356  ? 457 GLU B O     1 
ATOM   2943 C  CB    . GLU A 1 378 ? -11.59749 4.09908   -6.69696  1.000 80.55376  ? 457 GLU B CB    1 
ATOM   2944 C  CG    . GLU A 1 378 ? -11.85224 2.70169   -6.15324  1.000 93.43852  ? 457 GLU B CG    1 
ATOM   2945 C  CD    . GLU A 1 378 ? -11.65715 2.61813   -4.64815  1.000 99.90758  ? 457 GLU B CD    1 
ATOM   2946 O  OE1   . GLU A 1 378 ? -12.39983 3.30458   -3.91330  1.000 92.87986  ? 457 GLU B OE1   1 
ATOM   2947 O  OE2   . GLU A 1 378 ? -10.75730 1.87383   -4.20074  1.000 100.55143 ? 457 GLU B OE2   1 
ATOM   2948 N  N     . ASN A 1 379 ? -13.18375 6.43467   -9.14144  1.000 82.60357  ? 458 ASN B N     1 
ATOM   2949 C  CA    . ASN A 1 379 ? -13.39656 7.85933   -9.35788  1.000 77.87500  ? 458 ASN B CA    1 
ATOM   2950 C  C     . ASN A 1 379 ? -14.87226 8.18026   -9.16964  1.000 81.75292  ? 458 ASN B C     1 
ATOM   2951 O  O     . ASN A 1 379 ? -15.61572 7.38383   -8.58703  1.000 86.96282  ? 458 ASN B O     1 
ATOM   2952 C  CB    . ASN A 1 379 ? -12.92000 8.28237   -10.74889 1.000 77.37633  ? 458 ASN B CB    1 
ATOM   2953 C  CG    . ASN A 1 379 ? -11.42655 8.53396   -10.80119 1.000 78.17056  ? 458 ASN B CG    1 
ATOM   2954 O  OD1   . ASN A 1 379 ? -10.97524 9.66874   -10.65933 1.000 75.59167  ? 458 ASN B OD1   1 
ATOM   2955 N  ND2   . ASN A 1 379 ? -10.65125 7.47516   -11.00313 1.000 67.94338  ? 458 ASN B ND2   1 
ATOM   2956 N  N     . LYS A 1 380 ? -15.30582 9.33823   -9.65172  1.000 78.38643  ? 459 LYS B N     1 
ATOM   2957 C  CA    . LYS A 1 380 ? -16.70482 9.73892   -9.59897  1.000 86.66862  ? 459 LYS B CA    1 
ATOM   2958 C  C     . LYS A 1 380 ? -17.26172 9.90592   -11.00799 1.000 90.10673  ? 459 LYS B C     1 
ATOM   2959 O  O     . LYS A 1 380 ? -18.05354 10.81046  -11.28390 1.000 93.18466  ? 459 LYS B O     1 
ATOM   2960 C  CB    . LYS A 1 380 ? -16.87263 11.02158  -8.78634  1.000 94.51640  ? 459 LYS B CB    1 
ATOM   2961 C  CG    . LYS A 1 380 ? -16.26911 10.95810  -7.38658  1.000 79.27102  ? 459 LYS B CG    1 
ATOM   2962 C  CD    . LYS A 1 380 ? -16.88030 9.83342   -6.56363  1.000 84.14011  ? 459 LYS B CD    1 
ATOM   2963 C  CE    . LYS A 1 380 ? -16.14758 9.64577   -5.23915  1.000 87.78036  ? 459 LYS B CE    1 
ATOM   2964 N  NZ    . LYS A 1 380 ? -16.23606 10.84596  -4.36095  1.000 98.48519  ? 459 LYS B NZ    1 
ATOM   2965 N  N     . LEU A 1 381 ? -16.84557 9.02472   -11.91709 1.000 83.06633  ? 460 LEU B N     1 
ATOM   2966 C  CA    . LEU A 1 381 ? -17.18014 9.15347   -13.33257 1.000 85.31647  ? 460 LEU B CA    1 
ATOM   2967 C  C     . LEU A 1 381 ? -18.67578 8.95585   -13.54250 1.000 91.38286  ? 460 LEU B C     1 
ATOM   2968 O  O     . LEU A 1 381 ? -19.20273 7.85981   -13.32927 1.000 86.16343  ? 460 LEU B O     1 
ATOM   2969 C  CB    . LEU A 1 381 ? -16.38536 8.14711   -14.15779 1.000 82.17178  ? 460 LEU B CB    1 
ATOM   2970 C  CG    . LEU A 1 381 ? -14.94962 8.51553   -14.52696 1.000 84.53071  ? 460 LEU B CG    1 
ATOM   2971 C  CD1   . LEU A 1 381 ? -14.41171 7.51746   -15.53365 1.000 77.73205  ? 460 LEU B CD1   1 
ATOM   2972 C  CD2   . LEU A 1 381 ? -14.88053 9.92978   -15.08093 1.000 84.82130  ? 460 LEU B CD2   1 
ATOM   2973 N  N     . GLU A 1 382 ? -19.35912 10.01505  -13.97348 1.000 87.06603  ? 461 GLU B N     1 
ATOM   2974 C  CA    . GLU A 1 382 ? -20.76577 9.92302   -14.33553 1.000 88.89915  ? 461 GLU B CA    1 
ATOM   2975 C  C     . GLU A 1 382 ? -20.97412 9.49436   -15.77948 1.000 87.61033  ? 461 GLU B C     1 
ATOM   2976 O  O     . GLU A 1 382 ? -22.04888 8.98044   -16.11092 1.000 84.58200  ? 461 GLU B O     1 
ATOM   2977 C  CB    . GLU A 1 382 ? -21.46339 11.26887  -14.10924 1.000 85.46646  ? 461 GLU B CB    1 
ATOM   2978 C  CG    . GLU A 1 382 ? -21.31893 11.82253  -12.70128 1.000 100.82556 ? 461 GLU B CG    1 
ATOM   2979 C  CD    . GLU A 1 382 ? -21.86031 13.23511  -12.57056 1.000 107.62521 ? 461 GLU B CD    1 
ATOM   2980 O  OE1   . GLU A 1 382 ? -22.60181 13.67939  -13.47494 1.000 97.47762  ? 461 GLU B OE1   1 
ATOM   2981 O  OE2   . GLU A 1 382 ? -21.53831 13.90366  -11.56443 1.000 108.66520 ? 461 GLU B OE2   1 
ATOM   2982 N  N     . SER A 1 383 ? -19.97777 9.68768   -16.63977 1.000 88.52724  ? 462 SER B N     1 
ATOM   2983 C  CA    . SER A 1 383 ? -20.12930 9.38121   -18.05323 1.000 83.89002  ? 462 SER B CA    1 
ATOM   2984 C  C     . SER A 1 383 ? -18.75575 9.19992   -18.67873 1.000 88.18295  ? 462 SER B C     1 
ATOM   2985 O  O     . SER A 1 383 ? -17.77016 9.79519   -18.23421 1.000 87.94401  ? 462 SER B O     1 
ATOM   2986 C  CB    . SER A 1 383 ? -20.90030 10.48541  -18.78449 1.000 82.06544  ? 462 SER B CB    1 
ATOM   2987 O  OG    . SER A 1 383 ? -20.22083 11.72582  -18.69056 1.000 81.12692  ? 462 SER B OG    1 
ATOM   2988 N  N     . LEU A 1 384 ? -18.70531 8.36244   -19.70884 1.000 90.01264  ? 463 LEU B N     1 
ATOM   2989 C  CA    . LEU A 1 384 ? -17.48524 8.27803   -20.49782 1.000 89.18278  ? 463 LEU B CA    1 
ATOM   2990 C  C     . LEU A 1 384 ? -17.55690 9.24733   -21.67220 1.000 85.17368  ? 463 LEU B C     1 
ATOM   2991 O  O     . LEU A 1 384 ? -18.62091 9.41019   -22.27738 1.000 84.66258  ? 463 LEU B O     1 
ATOM   2992 C  CB    . LEU A 1 384 ? -17.27269 6.86494   -21.02724 1.000 76.70143  ? 463 LEU B CB    1 
ATOM   2993 C  CG    . LEU A 1 384 ? -16.54149 5.86897   -20.13255 1.000 81.98213  ? 463 LEU B CG    1 
ATOM   2994 C  CD1   . LEU A 1 384 ? -16.40416 4.54121   -20.85506 1.000 79.37361  ? 463 LEU B CD1   1 
ATOM   2995 C  CD2   . LEU A 1 384 ? -15.17680 6.41035   -19.73811 1.000 85.90215  ? 463 LEU B CD2   1 
ATOM   2996 N  N     . PRO A 1 385 ? -16.45257 9.90958   -22.00656 1.000 90.67482  ? 464 PRO B N     1 
ATOM   2997 C  CA    . PRO A 1 385 ? -16.44091 10.73425  -23.21753 1.000 84.56439  ? 464 PRO B CA    1 
ATOM   2998 C  C     . PRO A 1 385 ? -16.58503 9.86024   -24.45022 1.000 82.40808  ? 464 PRO B C     1 
ATOM   2999 O  O     . PRO A 1 385 ? -16.00436 8.77697   -24.53342 1.000 81.95788  ? 464 PRO B O     1 
ATOM   3000 C  CB    . PRO A 1 385 ? -15.07225 11.42091  -23.16885 1.000 77.87303  ? 464 PRO B CB    1 
ATOM   3001 C  CG    . PRO A 1 385 ? -14.23048 10.50426  -22.34909 1.000 79.97570  ? 464 PRO B CG    1 
ATOM   3002 C  CD    . PRO A 1 385 ? -15.15112 9.91718   -21.31789 1.000 73.28593  ? 464 PRO B CD    1 
ATOM   3003 N  N     . ASN A 1 386 ? -17.37862 10.33785  -25.41091 1.000 83.96239  ? 465 ASN B N     1 
ATOM   3004 C  CA    . ASN A 1 386 ? -17.60060 9.57629   -26.63478 1.000 89.93565  ? 465 ASN B CA    1 
ATOM   3005 C  C     . ASN A 1 386 ? -16.30611 9.29562   -27.38580 1.000 80.53657  ? 465 ASN B C     1 
ATOM   3006 O  O     . ASN A 1 386 ? -16.26381 8.37651   -28.21016 1.000 78.05611  ? 465 ASN B O     1 
ATOM   3007 C  CB    . ASN A 1 386 ? -18.57659 10.32252  -27.54502 1.000 91.92534  ? 465 ASN B CB    1 
ATOM   3008 C  CG    . ASN A 1 386 ? -19.96100 10.43957  -26.94219 1.000 94.81517  ? 465 ASN B CG    1 
ATOM   3009 O  OD1   . ASN A 1 386 ? -20.75125 9.49829   -26.99162 1.000 98.65105  ? 465 ASN B OD1   1 
ATOM   3010 N  ND2   . ASN A 1 386 ? -20.26407 11.60008  -26.37194 1.000 102.08463 ? 465 ASN B ND2   1 
ATOM   3011 N  N     . GLU A 1 387 ? -15.24869 10.04967  -27.10669 1.000 87.18090  ? 466 GLU B N     1 
ATOM   3012 C  CA    . GLU A 1 387 ? -14.00767 9.95247   -27.85913 1.000 82.44378  ? 466 GLU B CA    1 
ATOM   3013 C  C     . GLU A 1 387 ? -13.14988 8.75314   -27.47076 1.000 78.72034  ? 466 GLU B C     1 
ATOM   3014 O  O     . GLU A 1 387 ? -12.07277 8.58053   -28.05097 1.000 86.17876  ? 466 GLU B O     1 
ATOM   3015 C  CB    . GLU A 1 387 ? -13.20230 11.24627  -27.69685 1.000 84.51824  ? 466 GLU B CB    1 
ATOM   3016 C  CG    . GLU A 1 387 ? -13.75970 12.43248  -28.48028 1.000 82.43806  ? 466 GLU B CG    1 
ATOM   3017 C  CD    . GLU A 1 387 ? -15.05853 12.97552  -27.90896 1.000 85.77205  ? 466 GLU B CD    1 
ATOM   3018 O  OE1   . GLU A 1 387 ? -15.28268 12.82800  -26.68944 1.000 93.41127  ? 466 GLU B OE1   1 
ATOM   3019 O  OE2   . GLU A 1 387 ? -15.85662 13.54932  -28.68270 1.000 83.37297  ? 466 GLU B OE2   1 
ATOM   3020 N  N     . ILE A 1 388 ? -13.58567 7.91755   -26.52216 1.000 78.97591  ? 467 ILE B N     1 
ATOM   3021 C  CA    . ILE A 1 388 ? -12.81594 6.71605   -26.21048 1.000 81.30198  ? 467 ILE B CA    1 
ATOM   3022 C  C     . ILE A 1 388 ? -12.79368 5.75239   -27.38650 1.000 80.01287  ? 467 ILE B C     1 
ATOM   3023 O  O     . ILE A 1 388 ? -11.93066 4.87005   -27.44308 1.000 82.63464  ? 467 ILE B O     1 
ATOM   3024 C  CB    . ILE A 1 388 ? -13.35115 6.00139   -24.95042 1.000 82.87639  ? 467 ILE B CB    1 
ATOM   3025 C  CG1   . ILE A 1 388 ? -14.88391 5.94332   -24.94873 1.000 83.06781  ? 467 ILE B CG1   1 
ATOM   3026 C  CG2   . ILE A 1 388 ? -12.80926 6.65856   -23.68607 1.000 74.70168  ? 467 ILE B CG2   1 
ATOM   3027 C  CD1   . ILE A 1 388 ? -15.47708 4.77116   -25.70772 1.000 88.30330  ? 467 ILE B CD1   1 
ATOM   3028 N  N     . ALA A 1 389 ? -13.72598 5.89880   -28.33049 1.000 77.14202  ? 468 ALA B N     1 
ATOM   3029 C  CA    . ALA A 1 389 ? -13.76390 5.02039   -29.49218 1.000 81.34814  ? 468 ALA B CA    1 
ATOM   3030 C  C     . ALA A 1 389 ? -12.50961 5.13334   -30.34686 1.000 77.86681  ? 468 ALA B C     1 
ATOM   3031 O  O     . ALA A 1 389 ? -12.19089 4.19743   -31.08786 1.000 87.24687  ? 468 ALA B O     1 
ATOM   3032 C  CB    . ALA A 1 389 ? -14.99661 5.33305   -30.34063 1.000 83.21001  ? 468 ALA B CB    1 
ATOM   3033 N  N     . TYR A 1 390 ? -11.78979 6.24852   -30.25872 1.000 66.08775  ? 469 TYR B N     1 
ATOM   3034 C  CA    . TYR A 1 390 ? -10.64248 6.50575   -31.11504 1.000 81.56475  ? 469 TYR B CA    1 
ATOM   3035 C  C     . TYR A 1 390 ? -9.32214  6.10403   -30.46771 1.000 84.88822  ? 469 TYR B C     1 
ATOM   3036 O  O     . TYR A 1 390 ? -8.25664  6.43980   -30.99442 1.000 87.67338  ? 469 TYR B O     1 
ATOM   3037 C  CB    . TYR A 1 390 ? -10.62451 7.98127   -31.51861 1.000 80.52314  ? 469 TYR B CB    1 
ATOM   3038 C  CG    . TYR A 1 390 ? -11.99969 8.49820   -31.89037 1.000 75.16669  ? 469 TYR B CG    1 
ATOM   3039 C  CD1   . TYR A 1 390 ? -12.72356 7.91704   -32.92424 1.000 68.04256  ? 469 TYR B CD1   1 
ATOM   3040 C  CD2   . TYR A 1 390 ? -12.57778 9.55792   -31.20210 1.000 73.41729  ? 469 TYR B CD2   1 
ATOM   3041 C  CE1   . TYR A 1 390 ? -13.98208 8.37609   -33.26258 1.000 67.84992  ? 469 TYR B CE1   1 
ATOM   3042 C  CE2   . TYR A 1 390 ? -13.83574 10.02707  -31.53675 1.000 72.54363  ? 469 TYR B CE2   1 
ATOM   3043 C  CZ    . TYR A 1 390 ? -14.53340 9.43226   -32.56798 1.000 68.36467  ? 469 TYR B CZ    1 
ATOM   3044 O  OH    . TYR A 1 390 ? -15.78691 9.89237   -32.90576 1.000 69.81341  ? 469 TYR B OH    1 
ATOM   3045 N  N     . LEU A 1 391 ? -9.36994  5.39106   -29.34199 1.000 81.67878  ? 470 LEU B N     1 
ATOM   3046 C  CA    . LEU A 1 391 ? -8.17094  4.83402   -28.71391 1.000 81.20175  ? 470 LEU B CA    1 
ATOM   3047 C  C     . LEU A 1 391 ? -7.88737  3.45904   -29.32161 1.000 82.68349  ? 470 LEU B C     1 
ATOM   3048 O  O     . LEU A 1 391 ? -8.09314  2.40773   -28.71089 1.000 77.18524  ? 470 LEU B O     1 
ATOM   3049 C  CB    . LEU A 1 391 ? -8.34601  4.75880   -27.20192 1.000 75.59828  ? 470 LEU B CB    1 
ATOM   3050 C  CG    . LEU A 1 391 ? -8.62619  6.07294   -26.47000 1.000 70.48067  ? 470 LEU B CG    1 
ATOM   3051 C  CD1   . LEU A 1 391 ? -8.76998  5.83597   -24.97600 1.000 65.47433  ? 470 LEU B CD1   1 
ATOM   3052 C  CD2   . LEU A 1 391 ? -7.53142  7.08494   -26.74780 1.000 68.10477  ? 470 LEU B CD2   1 
ATOM   3053 N  N     . LYS A 1 392 ? -7.39438  3.49372   -30.56346 1.000 79.50436  ? 471 LYS B N     1 
ATOM   3054 C  CA    . LYS A 1 392 ? -7.24537  2.27102   -31.34766 1.000 87.05541  ? 471 LYS B CA    1 
ATOM   3055 C  C     . LYS A 1 392 ? -6.29483  1.27658   -30.69044 1.000 89.96271  ? 471 LYS B C     1 
ATOM   3056 O  O     . LYS A 1 392 ? -6.46313  0.06242   -30.85261 1.000 89.47451  ? 471 LYS B O     1 
ATOM   3057 C  CB    . LYS A 1 392 ? -6.76185  2.61411   -32.75846 1.000 94.07982  ? 471 LYS B CB    1 
ATOM   3058 C  CG    . LYS A 1 392 ? -7.57131  3.70630   -33.44977 1.000 101.55339 ? 471 LYS B CG    1 
ATOM   3059 C  CD    . LYS A 1 392 ? -9.02396  3.29210   -33.64761 1.000 109.14174 ? 471 LYS B CD    1 
ATOM   3060 C  CE    . LYS A 1 392 ? -9.87259  4.45573   -34.15265 1.000 100.70852 ? 471 LYS B CE    1 
ATOM   3061 N  NZ    . LYS A 1 392 ? -9.33674  5.06295   -35.40602 1.000 93.32496  ? 471 LYS B NZ    1 
ATOM   3062 N  N     . ASP A 1 393 ? -5.30423  1.76201   -29.94345 1.000 89.55181  ? 472 ASP B N     1 
ATOM   3063 C  CA    . ASP A 1 393 ? -4.27789  0.91389   -29.34978 1.000 79.98068  ? 472 ASP B CA    1 
ATOM   3064 C  C     . ASP A 1 393 ? -4.59795  0.48417   -27.92179 1.000 78.49889  ? 472 ASP B C     1 
ATOM   3065 O  O     . ASP A 1 393 ? -3.75341  -0.14523  -27.27630 1.000 77.54631  ? 472 ASP B O     1 
ATOM   3066 C  CB    . ASP A 1 393 ? -2.92511  1.63292   -29.37113 1.000 83.62409  ? 472 ASP B CB    1 
ATOM   3067 C  CG    . ASP A 1 393 ? -2.29319  1.65102   -30.74825 1.000 82.81016  ? 472 ASP B CG    1 
ATOM   3068 O  OD1   . ASP A 1 393 ? -2.92344  2.17837   -31.68809 1.000 105.13080 ? 472 ASP B OD1   1 
ATOM   3069 O  OD2   . ASP A 1 393 ? -1.15934  1.14567   -30.88870 1.000 94.89320  ? 472 ASP B OD2   1 
ATOM   3070 N  N     . LEU A 1 394 ? -5.78203  0.80896   -27.41048 1.000 89.02857  ? 473 LEU B N     1 
ATOM   3071 C  CA    . LEU A 1 394 ? -6.10720  0.48183   -26.02811 1.000 79.21613  ? 473 LEU B CA    1 
ATOM   3072 C  C     . LEU A 1 394 ? -6.34555  -1.01639  -25.87793 1.000 78.88848  ? 473 LEU B C     1 
ATOM   3073 O  O     . LEU A 1 394 ? -7.06320  -1.62673  -26.67660 1.000 83.10255  ? 473 LEU B O     1 
ATOM   3074 C  CB    . LEU A 1 394 ? -7.33879  1.26268   -25.57150 1.000 77.18680  ? 473 LEU B CB    1 
ATOM   3075 C  CG    . LEU A 1 394 ? -7.59342  1.28016   -24.06242 1.000 70.64288  ? 473 LEU B CG    1 
ATOM   3076 C  CD1   . LEU A 1 394 ? -6.57404  2.16283   -23.36381 1.000 68.95547  ? 473 LEU B CD1   1 
ATOM   3077 C  CD2   . LEU A 1 394 ? -9.00935  1.73885   -23.75167 1.000 68.89401  ? 473 LEU B CD2   1 
ATOM   3078 N  N     . GLN A 1 395 ? -5.73766  -1.60804  -24.85185 1.000 80.69992  ? 474 GLN B N     1 
ATOM   3079 C  CA    . GLN A 1 395 ? -5.91218  -3.02050  -24.54264 1.000 80.55972  ? 474 GLN B CA    1 
ATOM   3080 C  C     . GLN A 1 395 ? -6.52982  -3.27538  -23.17885 1.000 74.67143  ? 474 GLN B C     1 
ATOM   3081 O  O     . GLN A 1 395 ? -7.20699  -4.29039  -23.00756 1.000 81.81356  ? 474 GLN B O     1 
ATOM   3082 C  CB    . GLN A 1 395 ? -4.56640  -3.75931  -24.60784 1.000 83.50228  ? 474 GLN B CB    1 
ATOM   3083 C  CG    . GLN A 1 395 ? -3.83481  -3.62117  -25.92848 1.000 80.38675  ? 474 GLN B CG    1 
ATOM   3084 C  CD    . GLN A 1 395 ? -2.50478  -4.34539  -25.92737 1.000 84.69118  ? 474 GLN B CD    1 
ATOM   3085 O  OE1   . GLN A 1 395 ? -2.27032  -5.23591  -25.10947 1.000 91.14639  ? 474 GLN B OE1   1 
ATOM   3086 N  NE2   . GLN A 1 395 ? -1.62205  -3.96254  -26.84245 1.000 94.22279  ? 474 GLN B NE2   1 
ATOM   3087 N  N     . LYS A 1 396 ? -6.31499  -2.39043  -22.20809 1.000 68.38273  ? 475 LYS B N     1 
ATOM   3088 C  CA    . LYS A 1 396 ? -6.82098  -2.56544  -20.85244 1.000 73.41677  ? 475 LYS B CA    1 
ATOM   3089 C  C     . LYS A 1 396 ? -7.53645  -1.29116  -20.43167 1.000 78.93412  ? 475 LYS B C     1 
ATOM   3090 O  O     . LYS A 1 396 ? -6.93514  -0.21166  -20.42785 1.000 74.99391  ? 475 LYS B O     1 
ATOM   3091 C  CB    . LYS A 1 396 ? -5.68282  -2.89226  -19.87943 1.000 72.16306  ? 475 LYS B CB    1 
ATOM   3092 C  CG    . LYS A 1 396 ? -6.13175  -3.29410  -18.48006 1.000 77.90050  ? 475 LYS B CG    1 
ATOM   3093 C  CD    . LYS A 1 396 ? -4.96343  -3.23288  -17.50343 1.000 90.79669  ? 475 LYS B CD    1 
ATOM   3094 C  CE    . LYS A 1 396 ? -5.31582  -3.83008  -16.14930 1.000 92.06935  ? 475 LYS B CE    1 
ATOM   3095 N  NZ    . LYS A 1 396 ? -5.39162  -5.31677  -16.19762 1.000 96.64643  ? 475 LYS B NZ    1 
ATOM   3096 N  N     . LEU A 1 397 ? -8.81585  -1.41543  -20.08430 1.000 76.58091  ? 476 LEU B N     1 
ATOM   3097 C  CA    . LEU A 1 397 ? -9.61084  -0.29945  -19.58572 1.000 69.70259  ? 476 LEU B CA    1 
ATOM   3098 C  C     . LEU A 1 397 ? -10.23933 -0.71529  -18.26506 1.000 79.00610  ? 476 LEU B C     1 
ATOM   3099 O  O     . LEU A 1 397 ? -11.04432 -1.65200  -18.22665 1.000 79.68187  ? 476 LEU B O     1 
ATOM   3100 C  CB    . LEU A 1 397 ? -10.68571 0.11154   -20.59668 1.000 78.12234  ? 476 LEU B CB    1 
ATOM   3101 C  CG    . LEU A 1 397 ? -11.58346 1.29716   -20.23381 1.000 71.91215  ? 476 LEU B CG    1 
ATOM   3102 C  CD1   . LEU A 1 397 ? -10.75445 2.54297   -19.96262 1.000 70.63229  ? 476 LEU B CD1   1 
ATOM   3103 C  CD2   . LEU A 1 397 ? -12.59226 1.55610   -21.33945 1.000 58.19299  ? 476 LEU B CD2   1 
ATOM   3104 N  N     . VAL A 1 398 ? -9.86770  -0.02842  -17.18862 1.000 74.59115  ? 477 VAL B N     1 
ATOM   3105 C  CA    . VAL A 1 398 ? -10.34014 -0.33852  -15.84332 1.000 77.71178  ? 477 VAL B CA    1 
ATOM   3106 C  C     . VAL A 1 398 ? -11.23016 0.80787   -15.38414 1.000 81.58682  ? 477 VAL B C     1 
ATOM   3107 O  O     . VAL A 1 398 ? -10.74631 1.91288   -15.10651 1.000 73.56327  ? 477 VAL B O     1 
ATOM   3108 C  CB    . VAL A 1 398 ? -9.17955  -0.56237  -14.86612 1.000 66.16273  ? 477 VAL B CB    1 
ATOM   3109 C  CG1   . VAL A 1 398 ? -9.70908  -0.75022  -13.45228 1.000 75.89068  ? 477 VAL B CG1   1 
ATOM   3110 C  CG2   . VAL A 1 398 ? -8.35662  -1.76111  -15.29437 1.000 79.73421  ? 477 VAL B CG2   1 
ATOM   3111 N  N     . LEU A 1 399 ? -12.53419 0.54194   -15.29422 1.000 81.21333  ? 478 LEU B N     1 
ATOM   3112 C  CA    . LEU A 1 399 ? -13.51594 1.53216   -14.86643 1.000 84.24393  ? 478 LEU B CA    1 
ATOM   3113 C  C     . LEU A 1 399 ? -14.23465 1.10627   -13.59042 1.000 79.34724  ? 478 LEU B C     1 
ATOM   3114 O  O     . LEU A 1 399 ? -15.35203 1.56366   -13.33004 1.000 73.71261  ? 478 LEU B O     1 
ATOM   3115 C  CB    . LEU A 1 399 ? -14.52834 1.79172   -15.98419 1.000 88.49711  ? 478 LEU B CB    1 
ATOM   3116 C  CG    . LEU A 1 399 ? -13.97626 2.35684   -17.29378 1.000 78.18701  ? 478 LEU B CG    1 
ATOM   3117 C  CD1   . LEU A 1 399 ? -15.00923 2.24155   -18.40156 1.000 65.14461  ? 478 LEU B CD1   1 
ATOM   3118 C  CD2   . LEU A 1 399 ? -13.55560 3.80366   -17.10777 1.000 80.37263  ? 478 LEU B CD2   1 
ATOM   3119 N  N     . THR A 1 400 ? -13.61168 0.24513   -12.78888 1.000 80.18401  ? 479 THR B N     1 
ATOM   3120 C  CA    . THR A 1 400 ? -14.26676 -0.30043  -11.60821 1.000 81.48729  ? 479 THR B CA    1 
ATOM   3121 C  C     . THR A 1 400 ? -14.52172 0.78660   -10.56884 1.000 85.84247  ? 479 THR B C     1 
ATOM   3122 O  O     . THR A 1 400 ? -13.67996 1.66048   -10.34090 1.000 81.27007  ? 479 THR B O     1 
ATOM   3123 C  CB    . THR A 1 400 ? -13.41621 -1.41916  -11.00533 1.000 82.37255  ? 479 THR B CB    1 
ATOM   3124 O  OG1   . THR A 1 400 ? -13.15614 -2.41165  -12.00614 1.000 83.98183  ? 479 THR B OG1   1 
ATOM   3125 C  CG2   . THR A 1 400 ? -14.13723 -2.07369  -9.83570  1.000 90.76000  ? 479 THR B CG2   1 
ATOM   3126 N  N     . ASN A 1 401 ? -15.70688 0.73003   -9.95285  1.000 83.82190  ? 480 ASN B N     1 
ATOM   3127 C  CA    . ASN A 1 401 ? -16.12162 1.63044   -8.87963  1.000 85.21098  ? 480 ASN B CA    1 
ATOM   3128 C  C     . ASN A 1 401 ? -16.31261 3.05782   -9.38436  1.000 84.89185  ? 480 ASN B C     1 
ATOM   3129 O  O     . ASN A 1 401 ? -15.51373 3.94668   -9.07049  1.000 78.65761  ? 480 ASN B O     1 
ATOM   3130 C  CB    . ASN A 1 401 ? -15.11497 1.59537   -7.72494  1.000 80.66525  ? 480 ASN B CB    1 
ATOM   3131 C  CG    . ASN A 1 401 ? -15.70726 2.07982   -6.41713  1.000 88.15623  ? 480 ASN B CG    1 
ATOM   3132 O  OD1   . ASN A 1 401 ? -16.70177 2.80551   -6.40002  1.000 94.57839  ? 480 ASN B OD1   1 
ATOM   3133 N  ND2   . ASN A 1 401 ? -15.09384 1.67988   -5.30928  1.000 94.18729  ? 480 ASN B ND2   1 
ATOM   3134 N  N     . ASN A 1 402 ? -17.37389 3.28561   -10.15067 1.000 88.20596  ? 481 ASN B N     1 
ATOM   3135 C  CA    . ASN A 1 402 ? -17.70947 4.61479   -10.65520 1.000 87.51526  ? 481 ASN B CA    1 
ATOM   3136 C  C     . ASN A 1 402 ? -19.23144 4.74309   -10.70617 1.000 88.89601  ? 481 ASN B C     1 
ATOM   3137 O  O     . ASN A 1 402 ? -19.95747 3.94263   -10.10693 1.000 94.70834  ? 481 ASN B O     1 
ATOM   3138 C  CB    . ASN A 1 402 ? -17.04473 4.85927   -12.02158 1.000 86.49015  ? 481 ASN B CB    1 
ATOM   3139 C  CG    . ASN A 1 402 ? -15.56810 5.18455   -11.90368 1.000 82.09219  ? 481 ASN B CG    1 
ATOM   3140 O  OD1   . ASN A 1 402 ? -15.19639 6.31558   -11.59665 1.000 76.10859  ? 481 ASN B OD1   1 
ATOM   3141 N  ND2   . ASN A 1 402 ? -14.71814 4.19546   -12.15953 1.000 80.93023  ? 481 ASN B ND2   1 
ATOM   3142 N  N     . GLN A 1 403 ? -19.71805 5.75440   -11.42755 1.000 89.49527  ? 482 GLN B N     1 
ATOM   3143 C  CA    . GLN A 1 403 ? -21.14385 6.04107   -11.52905 1.000 99.62033  ? 482 GLN B CA    1 
ATOM   3144 C  C     . GLN A 1 403 ? -21.67532 5.85025   -12.94647 1.000 93.76123  ? 482 GLN B C     1 
ATOM   3145 O  O     . GLN A 1 403 ? -22.69949 6.44142   -13.30431 1.000 100.00811 ? 482 GLN B O     1 
ATOM   3146 C  CB    . GLN A 1 403 ? -21.43063 7.46760   -11.05821 1.000 104.54130 ? 482 GLN B CB    1 
ATOM   3147 C  CG    . GLN A 1 403 ? -20.61122 7.91783   -9.86203  1.000 96.35665  ? 482 GLN B CG    1 
ATOM   3148 C  CD    . GLN A 1 403 ? -21.25667 7.55662   -8.54270  1.000 105.49058 ? 482 GLN B CD    1 
ATOM   3149 O  OE1   . GLN A 1 403 ? -21.83146 8.41133   -7.86800  1.000 125.90328 ? 482 GLN B OE1   1 
ATOM   3150 N  NE2   . GLN A 1 403 ? -21.16291 6.28726   -8.16343  1.000 101.16563 ? 482 GLN B NE2   1 
ATOM   3151 N  N     . LEU A 1 404 ? -21.00451 5.03780   -13.75878 1.000 87.58469  ? 483 LEU B N     1 
ATOM   3152 C  CA    . LEU A 1 404 ? -21.37997 4.90178   -15.16026 1.000 90.77861  ? 483 LEU B CA    1 
ATOM   3153 C  C     . LEU A 1 404 ? -22.69505 4.14372   -15.29826 1.000 85.05389  ? 483 LEU B C     1 
ATOM   3154 O  O     . LEU A 1 404 ? -22.83381 3.02281   -14.79986 1.000 93.59268  ? 483 LEU B O     1 
ATOM   3155 C  CB    . LEU A 1 404 ? -20.27726 4.18302   -15.93581 1.000 82.53037  ? 483 LEU B CB    1 
ATOM   3156 C  CG    . LEU A 1 404 ? -18.89311 4.83042   -15.94717 1.000 83.68934  ? 483 LEU B CG    1 
ATOM   3157 C  CD1   . LEU A 1 404 ? -17.93885 3.99974   -16.78545 1.000 84.93511  ? 483 LEU B CD1   1 
ATOM   3158 C  CD2   . LEU A 1 404 ? -18.96765 6.25750   -16.46812 1.000 86.69886  ? 483 LEU B CD2   1 
ATOM   3159 N  N     . THR A 1 405 ? -23.66102 4.75587   -15.98210 1.000 77.46688  ? 484 THR B N     1 
ATOM   3160 C  CA    . THR A 1 405 ? -24.92457 4.09490   -16.28356 1.000 93.73612  ? 484 THR B CA    1 
ATOM   3161 C  C     . THR A 1 405 ? -24.98928 3.55713   -17.70410 1.000 94.94506  ? 484 THR B C     1 
ATOM   3162 O  O     . THR A 1 405 ? -25.72488 2.59760   -17.95879 1.000 85.36276  ? 484 THR B O     1 
ATOM   3163 C  CB    . THR A 1 405 ? -26.10372 5.05060   -16.06029 1.000 83.85985  ? 484 THR B CB    1 
ATOM   3164 O  OG1   . THR A 1 405 ? -26.03636 6.13274   -16.99780 1.000 87.54882  ? 484 THR B OG1   1 
ATOM   3165 C  CG2   . THR A 1 405 ? -26.07470 5.60756   -14.64768 1.000 90.67446  ? 484 THR B CG2   1 
ATOM   3166 N  N     . THR A 1 406 ? -24.24560 4.15523   -18.63288 1.000 91.87895  ? 485 THR B N     1 
ATOM   3167 C  CA    . THR A 1 406 ? -24.19951 3.69915   -20.01309 1.000 88.88316  ? 485 THR B CA    1 
ATOM   3168 C  C     . THR A 1 406 ? -22.78111 3.83898   -20.54028 1.000 92.52987  ? 485 THR B C     1 
ATOM   3169 O  O     . THR A 1 406 ? -22.02300 4.71318   -20.11109 1.000 92.94503  ? 485 THR B O     1 
ATOM   3170 C  CB    . THR A 1 406 ? -25.14881 4.49083   -20.92761 1.000 88.88502  ? 485 THR B CB    1 
ATOM   3171 O  OG1   . THR A 1 406 ? -24.84413 5.88834   -20.83898 1.000 89.98549  ? 485 THR B OG1   1 
ATOM   3172 C  CG2   . THR A 1 406 ? -26.60455 4.26018   -20.54544 1.000 85.12559  ? 485 THR B CG2   1 
ATOM   3173 N  N     . LEU A 1 407 ? -22.43247 2.96446   -21.47447 1.000 96.50484  ? 486 LEU B N     1 
ATOM   3174 C  CA    . LEU A 1 407 ? -21.19198 3.07621   -22.22257 1.000 88.74922  ? 486 LEU B CA    1 
ATOM   3175 C  C     . LEU A 1 407 ? -21.46245 3.70805   -23.57858 1.000 82.29873  ? 486 LEU B C     1 
ATOM   3176 O  O     . LEU A 1 407 ? -22.50452 3.44094   -24.18656 1.000 95.92578  ? 486 LEU B O     1 
ATOM   3177 C  CB    . LEU A 1 407 ? -20.55411 1.70286   -22.42882 1.000 90.43131  ? 486 LEU B CB    1 
ATOM   3178 C  CG    . LEU A 1 407 ? -20.12186 0.93297   -21.18393 1.000 84.62780  ? 486 LEU B CG    1 
ATOM   3179 C  CD1   . LEU A 1 407 ? -19.85461 -0.51372  -21.54987 1.000 81.67762  ? 486 LEU B CD1   1 
ATOM   3180 C  CD2   . LEU A 1 407 ? -18.88580 1.57105   -20.57099 1.000 70.35831  ? 486 LEU B CD2   1 
ATOM   3181 N  N     . PRO A 1 408 ? -20.56634 4.55720   -24.07693 1.000 91.40923  ? 487 PRO B N     1 
ATOM   3182 C  CA    . PRO A 1 408 ? -20.75262 5.10247   -25.42646 1.000 92.83624  ? 487 PRO B CA    1 
ATOM   3183 C  C     . PRO A 1 408 ? -20.76414 3.98288   -26.45673 1.000 91.01637  ? 487 PRO B C     1 
ATOM   3184 O  O     . PRO A 1 408 ? -19.99162 3.02634   -26.36785 1.000 94.14932  ? 487 PRO B O     1 
ATOM   3185 C  CB    . PRO A 1 408 ? -19.54605 6.03078   -25.60636 1.000 81.20383  ? 487 PRO B CB    1 
ATOM   3186 C  CG    . PRO A 1 408 ? -19.09756 6.34947   -24.21641 1.000 89.03818  ? 487 PRO B CG    1 
ATOM   3187 C  CD    . PRO A 1 408 ? -19.37696 5.11390   -23.41283 1.000 86.12107  ? 487 PRO B CD    1 
ATOM   3188 N  N     . ARG A 1 409 ? -21.66484 4.10337   -27.43628 1.000 84.78276  ? 488 ARG B N     1 
ATOM   3189 C  CA    . ARG A 1 409 ? -21.82723 3.03613   -28.41895 1.000 89.33545  ? 488 ARG B CA    1 
ATOM   3190 C  C     . ARG A 1 409 ? -20.54841 2.80058   -29.21161 1.000 95.56114  ? 488 ARG B C     1 
ATOM   3191 O  O     . ARG A 1 409 ? -20.31214 1.68577   -29.69029 1.000 95.89264  ? 488 ARG B O     1 
ATOM   3192 C  CB    . ARG A 1 409 ? -22.98858 3.35783   -29.35860 1.000 86.97733  ? 488 ARG B CB    1 
ATOM   3193 C  CG    . ARG A 1 409 ? -24.27136 3.73885   -28.64012 1.000 93.83277  ? 488 ARG B CG    1 
ATOM   3194 C  CD    . ARG A 1 409 ? -25.44587 3.82179   -29.60087 1.000 88.12173  ? 488 ARG B CD    1 
ATOM   3195 N  NE    . ARG A 1 409 ? -25.90913 2.49821   -29.99863 1.000 98.43103  ? 488 ARG B NE    1 
ATOM   3196 C  CZ    . ARG A 1 409 ? -26.95172 2.27375   -30.78646 1.000 114.59001 ? 488 ARG B CZ    1 
ATOM   3197 N  NH1   . ARG A 1 409 ? -27.65968 3.26874   -31.29730 1.000 113.29175 ? 488 ARG B NH1   1 
ATOM   3198 N  NH2   . ARG A 1 409 ? -27.29395 1.01946   -31.06762 1.000 113.66440 ? 488 ARG B NH2   1 
ATOM   3199 N  N     . GLY A 1 410 ? -19.70845 3.82515   -29.34871 1.000 95.64424  ? 489 GLY B N     1 
ATOM   3200 C  CA    . GLY A 1 410 ? -18.42772 3.68210   -30.01117 1.000 90.09004  ? 489 GLY B CA    1 
ATOM   3201 C  C     . GLY A 1 410 ? -17.42394 2.80562   -29.29541 1.000 95.63443  ? 489 GLY B C     1 
ATOM   3202 O  O     . GLY A 1 410 ? -16.34078 2.57139   -29.83885 1.000 106.68701 ? 489 GLY B O     1 
ATOM   3203 N  N     . ILE A 1 411 ? -17.75169 2.30575   -28.09938 1.000 88.62822  ? 490 ILE B N     1 
ATOM   3204 C  CA    . ILE A 1 411 ? -16.84577 1.42700   -27.36601 1.000 91.01755  ? 490 ILE B CA    1 
ATOM   3205 C  C     . ILE A 1 411 ? -16.45081 0.21251   -28.19746 1.000 94.23299  ? 490 ILE B C     1 
ATOM   3206 O  O     . ILE A 1 411 ? -15.39473 -0.38412  -27.96056 1.000 94.37353  ? 490 ILE B O     1 
ATOM   3207 C  CB    . ILE A 1 411 ? -17.48930 1.00166   -26.02561 1.000 93.22133  ? 490 ILE B CB    1 
ATOM   3208 C  CG1   . ILE A 1 411 ? -16.45541 0.36523   -25.09132 1.000 81.32283  ? 490 ILE B CG1   1 
ATOM   3209 C  CG2   . ILE A 1 411 ? -18.65054 0.04876   -26.26161 1.000 94.26447  ? 490 ILE B CG2   1 
ATOM   3210 C  CD1   . ILE A 1 411 ? -15.66828 1.36556   -24.27648 1.000 74.16071  ? 490 ILE B CD1   1 
ATOM   3211 N  N     . GLY A 1 412 ? -17.26724 -0.15969  -29.18448 1.000 92.78803  ? 491 GLY B N     1 
ATOM   3212 C  CA    . GLY A 1 412 ? -16.94677 -1.27361  -30.05673 1.000 95.03260  ? 491 GLY B CA    1 
ATOM   3213 C  C     . GLY A 1 412 ? -15.80962 -1.01458  -31.02226 1.000 89.62545  ? 491 GLY B C     1 
ATOM   3214 O  O     . GLY A 1 412 ? -15.32796 -1.96434  -31.64935 1.000 90.95551  ? 491 GLY B O     1 
ATOM   3215 N  N     . HIS A 1 413 ? -15.37444 0.23658   -31.16049 1.000 92.52126  ? 492 HIS B N     1 
ATOM   3216 C  CA    . HIS A 1 413 ? -14.23196 0.56352   -32.00432 1.000 90.51858  ? 492 HIS B CA    1 
ATOM   3217 C  C     . HIS A 1 413 ? -12.89595 0.22568   -31.35236 1.000 88.55944  ? 492 HIS B C     1 
ATOM   3218 O  O     . HIS A 1 413 ? -11.84948 0.47259   -31.96192 1.000 90.62491  ? 492 HIS B O     1 
ATOM   3219 C  CB    . HIS A 1 413 ? -14.26251 2.04855   -32.38222 1.000 80.76041  ? 492 HIS B CB    1 
ATOM   3220 C  CG    . HIS A 1 413 ? -15.34665 2.40447   -33.35266 1.000 93.06202  ? 492 HIS B CG    1 
ATOM   3221 N  ND1   . HIS A 1 413 ? -15.69905 3.70787   -33.63137 1.000 93.05348  ? 492 HIS B ND1   1 
ATOM   3222 C  CD2   . HIS A 1 413 ? -16.15156 1.62698   -34.11521 1.000 97.82782  ? 492 HIS B CD2   1 
ATOM   3223 C  CE1   . HIS A 1 413 ? -16.67639 3.71810   -34.52016 1.000 86.71337  ? 492 HIS B CE1   1 
ATOM   3224 N  NE2   . HIS A 1 413 ? -16.96980 2.46805   -34.83034 1.000 106.20798 ? 492 HIS B NE2   1 
ATOM   3225 N  N     . LEU A 1 414 ? -12.90249 -0.32979  -30.13992 1.000 82.22631  ? 493 LEU B N     1 
ATOM   3226 C  CA    . LEU A 1 414 ? -11.66997 -0.70944  -29.44748 1.000 76.97202  ? 493 LEU B CA    1 
ATOM   3227 C  C     . LEU A 1 414 ? -11.26542 -2.12102  -29.87385 1.000 82.44714  ? 493 LEU B C     1 
ATOM   3228 O  O     . LEU A 1 414 ? -11.27745 -3.08030  -29.09966 1.000 79.76477  ? 493 LEU B O     1 
ATOM   3229 C  CB    . LEU A 1 414 ? -11.85554 -0.60537  -27.94006 1.000 88.63106  ? 493 LEU B CB    1 
ATOM   3230 C  CG    . LEU A 1 414 ? -12.26119 0.77595   -27.42677 1.000 78.41947  ? 493 LEU B CG    1 
ATOM   3231 C  CD1   . LEU A 1 414 ? -12.46560 0.74721   -25.92370 1.000 79.85156  ? 493 LEU B CD1   1 
ATOM   3232 C  CD2   . LEU A 1 414 ? -11.21773 1.80621   -27.80898 1.000 61.74667  ? 493 LEU B CD2   1 
ATOM   3233 N  N     . THR A 1 415 ? -10.87988 -2.22266  -31.14702 1.000 86.47476  ? 494 THR B N     1 
ATOM   3234 C  CA    . THR A 1 415 ? -10.62285 -3.51289  -31.77536 1.000 88.31328  ? 494 THR B CA    1 
ATOM   3235 C  C     . THR A 1 415 ? -9.47863  -4.28320  -31.12643 1.000 84.76660  ? 494 THR B C     1 
ATOM   3236 O  O     . THR A 1 415 ? -9.34072  -5.48228  -31.39050 1.000 94.65386  ? 494 THR B O     1 
ATOM   3237 C  CB    . THR A 1 415 ? -10.33472 -3.31183  -33.26600 1.000 95.99343  ? 494 THR B CB    1 
ATOM   3238 O  OG1   . THR A 1 415 ? -10.45282 -4.56402  -33.95124 1.000 115.43525 ? 494 THR B OG1   1 
ATOM   3239 C  CG2   . THR A 1 415 ? -8.93118  -2.75643  -33.47073 1.000 90.76994  ? 494 THR B CG2   1 
ATOM   3240 N  N     . ASN A 1 416 ? -8.66395  -3.63982  -30.28965 1.000 89.95888  ? 495 ASN B N     1 
ATOM   3241 C  CA    . ASN A 1 416 ? -7.56557  -4.30531  -29.59920 1.000 85.50237  ? 495 ASN B CA    1 
ATOM   3242 C  C     . ASN A 1 416 ? -7.81412  -4.45040  -28.10279 1.000 86.95545  ? 495 ASN B C     1 
ATOM   3243 O  O     . ASN A 1 416 ? -6.90833  -4.86454  -27.37107 1.000 78.50934  ? 495 ASN B O     1 
ATOM   3244 C  CB    . ASN A 1 416 ? -6.25270  -3.55330  -29.83444 1.000 76.25090  ? 495 ASN B CB    1 
ATOM   3245 C  CG    . ASN A 1 416 ? -5.80502  -3.59161  -31.28480 1.000 87.59465  ? 495 ASN B CG    1 
ATOM   3246 O  OD1   . ASN A 1 416 ? -6.03400  -4.57052  -31.99453 1.000 90.77972  ? 495 ASN B OD1   1 
ATOM   3247 N  ND2   . ASN A 1 416 ? -5.15812  -2.52170  -31.73038 1.000 86.50865  ? 495 ASN B ND2   1 
ATOM   3248 N  N     . LEU A 1 417 ? -9.01365  -4.12208  -27.62988 1.000 90.07560  ? 496 LEU B N     1 
ATOM   3249 C  CA    . LEU A 1 417 ? -9.29886  -4.19450  -26.20327 1.000 90.61626  ? 496 LEU B CA    1 
ATOM   3250 C  C     . LEU A 1 417 ? -9.37826  -5.64839  -25.75229 1.000 87.02610  ? 496 LEU B C     1 
ATOM   3251 O  O     . LEU A 1 417 ? -10.09428 -6.45734  -26.35015 1.000 96.27701  ? 496 LEU B O     1 
ATOM   3252 C  CB    . LEU A 1 417 ? -10.60490 -3.46593  -25.88645 1.000 84.79954  ? 496 LEU B CB    1 
ATOM   3253 C  CG    . LEU A 1 417 ? -10.92198 -3.23935  -24.40577 1.000 81.36225  ? 496 LEU B CG    1 
ATOM   3254 C  CD1   . LEU A 1 417 ? -9.89274  -2.31669  -23.76636 1.000 82.97961  ? 496 LEU B CD1   1 
ATOM   3255 C  CD2   . LEU A 1 417 ? -12.32202 -2.67989  -24.23561 1.000 77.96466  ? 496 LEU B CD2   1 
ATOM   3256 N  N     . THR A 1 418 ? -8.63179  -5.98025  -24.69571 1.000 87.96343  ? 497 THR B N     1 
ATOM   3257 C  CA    . THR A 1 418 ? -8.63567  -7.31960  -24.12436 1.000 97.24203  ? 497 THR B CA    1 
ATOM   3258 C  C     . THR A 1 418 ? -9.14796  -7.37704  -22.69315 1.000 92.41462  ? 497 THR B C     1 
ATOM   3259 O  O     . THR A 1 418 ? -9.56817  -8.45271  -22.25226 1.000 84.50055  ? 497 THR B O     1 
ATOM   3260 C  CB    . THR A 1 418 ? -7.22270  -7.92851  -24.15483 1.000 94.34070  ? 497 THR B CB    1 
ATOM   3261 O  OG1   . THR A 1 418 ? -6.37889  -7.23331  -23.22833 1.000 82.22130  ? 497 THR B OG1   1 
ATOM   3262 C  CG2   . THR A 1 418 ? -6.62442  -7.82705  -25.55004 1.000 91.08109  ? 497 THR B CG2   1 
ATOM   3263 N  N     . HIS A 1 419 ? -9.12530  -6.26493  -21.96099 1.000 91.52472  ? 498 HIS B N     1 
ATOM   3264 C  CA    . HIS A 1 419 ? -9.55535  -6.21942  -20.56865 1.000 87.71169  ? 498 HIS B CA    1 
ATOM   3265 C  C     . HIS A 1 419 ? -10.48759 -5.03182  -20.38738 1.000 88.25973  ? 498 HIS B C     1 
ATOM   3266 O  O     . HIS A 1 419 ? -10.11465 -3.89495  -20.69619 1.000 86.49934  ? 498 HIS B O     1 
ATOM   3267 C  CB    . HIS A 1 419 ? -8.35361  -6.10799  -19.62500 1.000 83.53067  ? 498 HIS B CB    1 
ATOM   3268 C  CG    . HIS A 1 419 ? -8.71771  -6.13543  -18.17259 1.000 89.90117  ? 498 HIS B CG    1 
ATOM   3269 N  ND1   . HIS A 1 419 ? -8.46518  -7.22210  -17.36325 1.000 97.19797  ? 498 HIS B ND1   1 
ATOM   3270 C  CD2   . HIS A 1 419 ? -9.31516  -5.21037  -17.38390 1.000 91.16463  ? 498 HIS B CD2   1 
ATOM   3271 C  CE1   . HIS A 1 419 ? -8.89101  -6.96542  -16.13910 1.000 95.80248  ? 498 HIS B CE1   1 
ATOM   3272 N  NE2   . HIS A 1 419 ? -9.41177  -5.75161  -16.12488 1.000 88.13421  ? 498 HIS B NE2   1 
ATOM   3273 N  N     . LEU A 1 420 ? -11.69178 -5.29222  -19.88405 1.000 81.46060  ? 499 LEU B N     1 
ATOM   3274 C  CA    . LEU A 1 420 ? -12.67891 -4.24886  -19.62633 1.000 79.30465  ? 499 LEU B CA    1 
ATOM   3275 C  C     . LEU A 1 420 ? -13.28317 -4.49516  -18.25007 1.000 85.53549  ? 499 LEU B C     1 
ATOM   3276 O  O     . LEU A 1 420 ? -14.05199 -5.44477  -18.06555 1.000 76.68270  ? 499 LEU B O     1 
ATOM   3277 C  CB    . LEU A 1 420 ? -13.75782 -4.22924  -20.71066 1.000 77.66359  ? 499 LEU B CB    1 
ATOM   3278 C  CG    . LEU A 1 420 ? -14.78009 -3.09152  -20.64547 1.000 82.61390  ? 499 LEU B CG    1 
ATOM   3279 C  CD1   . LEU A 1 420 ? -14.08057 -1.74163  -20.66515 1.000 76.02836  ? 499 LEU B CD1   1 
ATOM   3280 C  CD2   . LEU A 1 420 ? -15.78053 -3.19737  -21.78778 1.000 63.35209  ? 499 LEU B CD2   1 
ATOM   3281 N  N     . GLY A 1 421 ? -12.93216 -3.64589  -17.28708 1.000 82.38288  ? 500 GLY B N     1 
ATOM   3282 C  CA    . GLY A 1 421 ? -13.44095 -3.77821  -15.93620 1.000 82.02040  ? 500 GLY B CA    1 
ATOM   3283 C  C     . GLY A 1 421 ? -14.54472 -2.79225  -15.61603 1.000 73.89508  ? 500 GLY B C     1 
ATOM   3284 O  O     . GLY A 1 421 ? -14.28018 -1.62008  -15.33609 1.000 74.67648  ? 500 GLY B O     1 
ATOM   3285 N  N     . LEU A 1 422 ? -15.79118 -3.26000  -15.65025 1.000 81.67293  ? 501 LEU B N     1 
ATOM   3286 C  CA    . LEU A 1 422 ? -16.95940 -2.42351  -15.40550 1.000 92.17654  ? 501 LEU B CA    1 
ATOM   3287 C  C     . LEU A 1 422 ? -17.63537 -2.75905  -14.07857 1.000 87.89700  ? 501 LEU B C     1 
ATOM   3288 O  O     . LEU A 1 422 ? -18.84903 -2.59374  -13.93306 1.000 88.10609  ? 501 LEU B O     1 
ATOM   3289 C  CB    . LEU A 1 422 ? -17.95412 -2.55641  -16.55702 1.000 93.31339  ? 501 LEU B CB    1 
ATOM   3290 C  CG    . LEU A 1 422 ? -17.42153 -2.19652  -17.94386 1.000 85.63526  ? 501 LEU B CG    1 
ATOM   3291 C  CD1   . LEU A 1 422 ? -18.40895 -2.61544  -19.01466 1.000 84.95160  ? 501 LEU B CD1   1 
ATOM   3292 C  CD2   . LEU A 1 422 ? -17.13559 -0.70842  -18.03146 1.000 85.46590  ? 501 LEU B CD2   1 
ATOM   3293 N  N     . GLY A 1 423 ? -16.86070 -3.22945  -13.10224 1.000 90.93132  ? 502 GLY B N     1 
ATOM   3294 C  CA    . GLY A 1 423 ? -17.43061 -3.61107  -11.83095 1.000 89.60664  ? 502 GLY B CA    1 
ATOM   3295 C  C     . GLY A 1 423 ? -17.75661 -2.42301  -10.94549 1.000 89.33809  ? 502 GLY B C     1 
ATOM   3296 O  O     . GLY A 1 423 ? -17.19214 -1.33798  -11.07754 1.000 80.30414  ? 502 GLY B O     1 
ATOM   3297 N  N     . GLU A 1 424 ? -18.70112 -2.65220  -10.03072 1.000 89.72856  ? 503 GLU B N     1 
ATOM   3298 C  CA    . GLU A 1 424 ? -19.10422 -1.66417  -9.02715  1.000 90.70831  ? 503 GLU B CA    1 
ATOM   3299 C  C     . GLU A 1 424 ? -19.53457 -0.34592  -9.67482  1.000 93.76240  ? 503 GLU B C     1 
ATOM   3300 O  O     . GLU A 1 424 ? -19.13527 0.74304   -9.25717  1.000 86.44144  ? 503 GLU B O     1 
ATOM   3301 C  CB    . GLU A 1 424 ? -17.98778 -1.44680  -8.00170  1.000 87.87285  ? 503 GLU B CB    1 
ATOM   3302 C  CG    . GLU A 1 424 ? -17.74467 -2.65865  -7.10623  1.000 98.01132  ? 503 GLU B CG    1 
ATOM   3303 C  CD    . GLU A 1 424 ? -16.31639 -2.74546  -6.60140  1.000 107.04591 ? 503 GLU B CD    1 
ATOM   3304 O  OE1   . GLU A 1 424 ? -15.62560 -1.70518  -6.58255  1.000 112.34855 ? 503 GLU B OE1   1 
ATOM   3305 O  OE2   . GLU A 1 424 ? -15.88173 -3.85829  -6.23279  1.000 104.82901 ? 503 GLU B OE2   1 
ATOM   3306 N  N     . ASN A 1 425 ? -20.36371 -0.45567  -10.70611 1.000 90.52689  ? 504 ASN B N     1 
ATOM   3307 C  CA    . ASN A 1 425 ? -20.95819 0.68284   -11.39478 1.000 91.47506  ? 504 ASN B CA    1 
ATOM   3308 C  C     . ASN A 1 425 ? -22.47732 0.55202   -11.36916 1.000 99.09539  ? 504 ASN B C     1 
ATOM   3309 O  O     . ASN A 1 425 ? -23.03322 -0.40439  -10.82539 1.000 100.60581 ? 504 ASN B O     1 
ATOM   3310 C  CB    . ASN A 1 425 ? -20.44642 0.78511   -12.83422 1.000 86.38283  ? 504 ASN B CB    1 
ATOM   3311 C  CG    . ASN A 1 425 ? -19.18046 1.60115   -12.94256 1.000 90.00524  ? 504 ASN B CG    1 
ATOM   3312 O  OD1   . ASN A 1 425 ? -19.22623 2.80579   -13.19327 1.000 91.48770  ? 504 ASN B OD1   1 
ATOM   3313 N  ND2   . ASN A 1 425 ? -18.03893 0.95184   -12.74784 1.000 86.99378  ? 504 ASN B ND2   1 
ATOM   3314 N  N     . LEU A 1 426 ? -23.15362 1.53117   -11.96754 1.000 80.99057  ? 505 LEU B N     1 
ATOM   3315 C  CA    . LEU A 1 426 ? -24.61199 1.47517   -12.05059 1.000 93.27012  ? 505 LEU B CA    1 
ATOM   3316 C  C     . LEU A 1 426 ? -25.03796 0.64672   -13.26014 1.000 100.78203 ? 505 LEU B C     1 
ATOM   3317 O  O     . LEU A 1 426 ? -25.62325 -0.42995  -13.11167 1.000 102.29760 ? 505 LEU B O     1 
ATOM   3318 C  CB    . LEU A 1 426 ? -25.18716 2.89439   -12.09827 1.000 91.85732  ? 505 LEU B CB    1 
ATOM   3319 C  CG    . LEU A 1 426 ? -24.69247 3.79786   -10.96022 1.000 85.54016  ? 505 LEU B CG    1 
ATOM   3320 C  CD1   . LEU A 1 426 ? -25.35489 5.16351   -11.01794 1.000 93.73833  ? 505 LEU B CD1   1 
ATOM   3321 C  CD2   . LEU A 1 426 ? -24.91994 3.14457   -9.60475  1.000 75.03313  ? 505 LEU B CD2   1 
ATOM   3322 N  N     . LEU A 1 427 ? -24.74111 1.14378   -14.46423 1.000 96.54438  ? 506 LEU B N     1 
ATOM   3323 C  CA    . LEU A 1 427 ? -24.89186 0.41968   -15.72629 1.000 95.01932  ? 506 LEU B CA    1 
ATOM   3324 C  C     . LEU A 1 427 ? -26.25312 -0.23956  -15.90736 1.000 95.58540  ? 506 LEU B C     1 
ATOM   3325 O  O     . LEU A 1 427 ? -26.48263 -1.35325  -15.42505 1.000 92.93353  ? 506 LEU B O     1 
ATOM   3326 C  CB    . LEU A 1 427 ? -23.79822 -0.64118  -15.87001 1.000 91.10361  ? 506 LEU B CB    1 
ATOM   3327 C  CG    . LEU A 1 427 ? -22.43887 -0.16726  -16.38465 1.000 79.47458  ? 506 LEU B CG    1 
ATOM   3328 C  CD1   . LEU A 1 427 ? -21.66486 -1.34745  -16.93762 1.000 70.70410  ? 506 LEU B CD1   1 
ATOM   3329 C  CD2   . LEU A 1 427 ? -22.60120 0.91574   -17.43993 1.000 87.88114  ? 506 LEU B CD2   1 
ATOM   3330 N  N     . THR A 1 428 ? -27.15343 0.42788   -16.62831 1.000 98.76757  ? 507 THR B N     1 
ATOM   3331 C  CA    . THR A 1 428 ? -28.43899 -0.18304  -16.94333 1.000 99.40353  ? 507 THR B CA    1 
ATOM   3332 C  C     . THR A 1 428 ? -28.31966 -1.22717  -18.04719 1.000 99.92958  ? 507 THR B C     1 
ATOM   3333 O  O     . THR A 1 428 ? -29.09636 -2.18911  -18.06658 1.000 96.11526  ? 507 THR B O     1 
ATOM   3334 C  CB    . THR A 1 428 ? -29.45571 0.88834   -17.34583 1.000 87.37700  ? 507 THR B CB    1 
ATOM   3335 O  OG1   . THR A 1 428 ? -28.97979 1.59857   -18.49680 1.000 95.88351  ? 507 THR B OG1   1 
ATOM   3336 C  CG2   . THR A 1 428 ? -29.67278 1.86742   -16.20376 1.000 77.86728  ? 507 THR B CG2   1 
ATOM   3337 N  N     . HIS A 1 429 ? -27.36260 -1.06609  -18.95909 1.000 94.61063  ? 508 HIS B N     1 
ATOM   3338 C  CA    . HIS A 1 429 ? -27.18767 -2.00756  -20.05809 1.000 99.77011  ? 508 HIS B CA    1 
ATOM   3339 C  C     . HIS A 1 429 ? -25.84566 -1.75227  -20.72733 1.000 102.97943 ? 508 HIS B C     1 
ATOM   3340 O  O     . HIS A 1 429 ? -25.22881 -0.69800  -20.54616 1.000 99.55876  ? 508 HIS B O     1 
ATOM   3341 C  CB    . HIS A 1 429 ? -28.31892 -1.89357  -21.08559 1.000 97.36663  ? 508 HIS B CB    1 
ATOM   3342 C  CG    . HIS A 1 429 ? -28.34739 -0.58299  -21.80864 1.000 99.33377  ? 508 HIS B CG    1 
ATOM   3343 N  ND1   . HIS A 1 429 ? -28.37696 0.62879   -21.15253 1.000 95.43767  ? 508 HIS B ND1   1 
ATOM   3344 C  CD2   . HIS A 1 429 ? -28.35716 -0.29446  -23.13162 1.000 101.97191 ? 508 HIS B CD2   1 
ATOM   3345 C  CE1   . HIS A 1 429 ? -28.40073 1.60719   -22.03980 1.000 102.62854 ? 508 HIS B CE1   1 
ATOM   3346 N  NE2   . HIS A 1 429 ? -28.38941 1.07406   -23.24822 1.000 104.77131 ? 508 HIS B NE2   1 
ATOM   3347 N  N     . LEU A 1 430 ? -25.40082 -2.74698  -21.51128 1.000 98.04451  ? 509 LEU B N     1 
ATOM   3348 C  CA    . LEU A 1 430 ? -24.24138 -2.65846  -22.37897 1.000 97.72112  ? 509 LEU B CA    1 
ATOM   3349 C  C     . LEU A 1 430 ? -24.67579 -2.33727  -23.80411 1.000 102.86680 ? 509 LEU B C     1 
ATOM   3350 O  O     . LEU A 1 430 ? -25.76402 -2.73477  -24.23160 1.000 94.25613  ? 509 LEU B O     1 
ATOM   3351 C  CB    . LEU A 1 430 ? -23.45392 -3.97265  -22.37750 1.000 90.12397  ? 509 LEU B CB    1 
ATOM   3352 C  CG    . LEU A 1 430 ? -22.96271 -4.49700  -21.03000 1.000 86.72825  ? 509 LEU B CG    1 
ATOM   3353 C  CD1   . LEU A 1 430 ? -22.09964 -5.73326  -21.23215 1.000 90.23172  ? 509 LEU B CD1   1 
ATOM   3354 C  CD2   . LEU A 1 430 ? -22.19916 -3.41892  -20.27823 1.000 97.69747  ? 509 LEU B CD2   1 
ATOM   3355 N  N     . PRO A 1 431 ? -23.85748 -1.61211  -24.56282 1.000 100.08638 ? 510 PRO B N     1 
ATOM   3356 C  CA    . PRO A 1 431 ? -24.22625 -1.30552  -25.94777 1.000 87.61605  ? 510 PRO B CA    1 
ATOM   3357 C  C     . PRO A 1 431 ? -24.23122 -2.55542  -26.81181 1.000 93.82545  ? 510 PRO B C     1 
ATOM   3358 O  O     . PRO A 1 431 ? -23.50725 -3.52199  -26.55942 1.000 97.96751  ? 510 PRO B O     1 
ATOM   3359 C  CB    . PRO A 1 431 ? -23.13714 -0.32481  -26.40179 1.000 97.75237  ? 510 PRO B CB    1 
ATOM   3360 C  CG    . PRO A 1 431 ? -22.50507 0.17654   -25.14087 1.000 98.65091  ? 510 PRO B CG    1 
ATOM   3361 C  CD    . PRO A 1 431 ? -22.60260 -0.95302  -24.16689 1.000 99.02445  ? 510 PRO B CD    1 
ATOM   3362 N  N     . GLU A 1 432 ? -25.07132 -2.52507  -27.84761 1.000 101.03818 ? 511 GLU B N     1 
ATOM   3363 C  CA    . GLU A 1 432 ? -25.10198 -3.61662  -28.81224 1.000 103.25502 ? 511 GLU B CA    1 
ATOM   3364 C  C     . GLU A 1 432 ? -23.81750 -3.69466  -29.62824 1.000 108.98898 ? 511 GLU B C     1 
ATOM   3365 O  O     . GLU A 1 432 ? -23.51843 -4.75214  -30.19327 1.000 102.78115 ? 511 GLU B O     1 
ATOM   3366 C  CB    . GLU A 1 432 ? -26.31114 -3.45986  -29.73636 1.000 102.73113 ? 511 GLU B CB    1 
ATOM   3367 C  CG    . GLU A 1 432 ? -27.65127 -3.49031  -29.01226 1.000 99.31783  ? 511 GLU B CG    1 
ATOM   3368 C  CD    . GLU A 1 432 ? -28.77371 -2.88279  -29.83330 1.000 126.35961 ? 511 GLU B CD    1 
ATOM   3369 O  OE1   . GLU A 1 432 ? -28.48042 -2.06369  -30.73020 1.000 129.72344 ? 511 GLU B OE1   1 
ATOM   3370 O  OE2   . GLU A 1 432 ? -29.94974 -3.22281  -29.58305 1.000 138.98356 ? 511 GLU B OE2   1 
ATOM   3371 N  N     . GLU A 1 433 ? -23.04893 -2.60714  -29.69213 1.000 108.01843 ? 512 GLU B N     1 
ATOM   3372 C  CA    . GLU A 1 433 ? -21.77234 -2.58268  -30.39506 1.000 98.89913  ? 512 GLU B CA    1 
ATOM   3373 C  C     . GLU A 1 433 ? -20.65599 -3.27355  -29.62001 1.000 99.74248  ? 512 GLU B C     1 
ATOM   3374 O  O     . GLU A 1 433 ? -19.49035 -3.17079  -30.01671 1.000 100.28720 ? 512 GLU B O     1 
ATOM   3375 C  CB    . GLU A 1 433 ? -21.36702 -1.13831  -30.70727 1.000 93.14545  ? 512 GLU B CB    1 
ATOM   3376 C  CG    . GLU A 1 433 ? -22.19421 -0.46385  -31.79684 1.000 97.02397  ? 512 GLU B CG    1 
ATOM   3377 C  CD    . GLU A 1 433 ? -23.57892 -0.05380  -31.32853 1.000 103.73348 ? 512 GLU B CD    1 
ATOM   3378 O  OE1   . GLU A 1 433 ? -23.81113 -0.01795  -30.10136 1.000 99.77958  ? 512 GLU B OE1   1 
ATOM   3379 O  OE2   . GLU A 1 433 ? -24.43654 0.23302   -32.19073 1.000 105.48736 ? 512 GLU B OE2   1 
ATOM   3380 N  N     . ILE A 1 434 ? -20.98380 -3.96989  -28.52871 1.000 91.45452  ? 513 ILE B N     1 
ATOM   3381 C  CA    . ILE A 1 434 ? -19.97755 -4.70537  -27.77470 1.000 93.14550  ? 513 ILE B CA    1 
ATOM   3382 C  C     . ILE A 1 434 ? -19.44317 -5.89352  -28.56597 1.000 92.56421  ? 513 ILE B C     1 
ATOM   3383 O  O     . ILE A 1 434 ? -18.38189 -6.43171  -28.23104 1.000 98.46897  ? 513 ILE B O     1 
ATOM   3384 C  CB    . ILE A 1 434 ? -20.56690 -5.16196  -26.42459 1.000 98.52948  ? 513 ILE B CB    1 
ATOM   3385 C  CG1   . ILE A 1 434 ? -19.45875 -5.46271  -25.41267 1.000 90.35708  ? 513 ILE B CG1   1 
ATOM   3386 C  CG2   . ILE A 1 434 ? -21.47149 -6.37169  -26.61195 1.000 100.55621 ? 513 ILE B CG2   1 
ATOM   3387 C  CD1   . ILE A 1 434 ? -18.91924 -4.23011  -24.72371 1.000 86.76926  ? 513 ILE B CD1   1 
ATOM   3388 N  N     . GLY A 1 435 ? -20.14621 -6.31017  -29.62078 1.000 102.45197 ? 514 GLY B N     1 
ATOM   3389 C  CA    . GLY A 1 435 ? -19.78072 -7.49480  -30.37457 1.000 98.22024  ? 514 GLY B CA    1 
ATOM   3390 C  C     . GLY A 1 435 ? -18.60357 -7.33899  -31.30791 1.000 99.11126  ? 514 GLY B C     1 
ATOM   3391 O  O     . GLY A 1 435 ? -18.07133 -8.34851  -31.77937 1.000 108.90600 ? 514 GLY B O     1 
ATOM   3392 N  N     . THR A 1 436 ? -18.18746 -6.10867  -31.59380 1.000 96.16827  ? 515 THR B N     1 
ATOM   3393 C  CA    . THR A 1 436 ? -17.02560 -5.86598  -32.43710 1.000 98.64665  ? 515 THR B CA    1 
ATOM   3394 C  C     . THR A 1 436 ? -15.71688 -5.88526  -31.65761 1.000 104.40562 ? 515 THR B C     1 
ATOM   3395 O  O     . THR A 1 436 ? -14.65313 -5.69216  -32.25603 1.000 106.36101 ? 515 THR B O     1 
ATOM   3396 C  CB    . THR A 1 436 ? -17.17176 -4.52893  -33.17051 1.000 103.70821 ? 515 THR B CB    1 
ATOM   3397 O  OG1   . THR A 1 436 ? -17.48930 -3.49881  -32.22806 1.000 109.49263 ? 515 THR B OG1   1 
ATOM   3398 C  CG2   . THR A 1 436 ? -18.27652 -4.61093  -34.21701 1.000 94.84613  ? 515 THR B CG2   1 
ATOM   3399 N  N     . LEU A 1 437 ? -15.76784 -6.10956  -30.34303 1.000 102.77911 ? 516 LEU B N     1 
ATOM   3400 C  CA    . LEU A 1 437 ? -14.56256 -6.26138  -29.52793 1.000 97.96834  ? 516 LEU B CA    1 
ATOM   3401 C  C     . LEU A 1 437 ? -14.01749 -7.66814  -29.75620 1.000 104.23425 ? 516 LEU B C     1 
ATOM   3402 O  O     . LEU A 1 437 ? -14.28140 -8.61005  -29.00408 1.000 104.57058 ? 516 LEU B O     1 
ATOM   3403 C  CB    . LEU A 1 437 ? -14.86486 -6.00059  -28.05838 1.000 91.00502  ? 516 LEU B CB    1 
ATOM   3404 C  CG    . LEU A 1 437 ? -15.41586 -4.61464  -27.72174 1.000 92.86701  ? 516 LEU B CG    1 
ATOM   3405 C  CD1   . LEU A 1 437 ? -15.64369 -4.48123  -26.22687 1.000 85.74353  ? 516 LEU B CD1   1 
ATOM   3406 C  CD2   . LEU A 1 437 ? -14.48054 -3.52697  -28.22492 1.000 84.44848  ? 516 LEU B CD2   1 
ATOM   3407 N  N     . GLU A 1 438 ? -13.23646 -7.80074  -30.83028 1.000 106.11574 ? 517 GLU B N     1 
ATOM   3408 C  CA    . GLU A 1 438 ? -12.75808 -9.11235  -31.25628 1.000 106.11104 ? 517 GLU B CA    1 
ATOM   3409 C  C     . GLU A 1 438 ? -11.86359 -9.74676  -30.19886 1.000 108.30664 ? 517 GLU B C     1 
ATOM   3410 O  O     . GLU A 1 438 ? -12.05343 -10.90930 -29.82188 1.000 108.72852 ? 517 GLU B O     1 
ATOM   3411 C  CB    . GLU A 1 438 ? -12.00793 -8.98051  -32.58157 1.000 107.70518 ? 517 GLU B CB    1 
ATOM   3412 C  CG    . GLU A 1 438 ? -12.70724 -8.10051  -33.60421 1.000 115.67094 ? 517 GLU B CG    1 
ATOM   3413 C  CD    . GLU A 1 438 ? -11.74755 -7.53263  -34.63162 1.000 114.01117 ? 517 GLU B CD    1 
ATOM   3414 O  OE1   . GLU A 1 438 ? -10.52514 -7.74127  -34.47995 1.000 106.95009 ? 517 GLU B OE1   1 
ATOM   3415 O  OE2   . GLU A 1 438 ? -12.21376 -6.87564  -35.58696 1.000 107.09447 ? 517 GLU B OE2   1 
ATOM   3416 N  N     . ASN A 1 439 ? -10.88703 -8.99281  -29.70220 1.000 102.37306 ? 518 ASN B N     1 
ATOM   3417 C  CA    . ASN A 1 439 ? -9.86451  -9.52383  -28.81367 1.000 109.68068 ? 518 ASN B CA    1 
ATOM   3418 C  C     . ASN A 1 439 ? -10.23260 -9.41334  -27.33786 1.000 104.45125 ? 518 ASN B C     1 
ATOM   3419 O  O     . ASN A 1 439 ? -9.35393  -9.57161  -26.48410 1.000 103.85370 ? 518 ASN B O     1 
ATOM   3420 C  CB    . ASN A 1 439 ? -8.53329  -8.81447  -29.07349 1.000 106.05101 ? 518 ASN B CB    1 
ATOM   3421 C  CG    . ASN A 1 439 ? -8.10904  -8.89069  -30.52742 1.000 107.83915 ? 518 ASN B CG    1 
ATOM   3422 O  OD1   . ASN A 1 439 ? -8.26903  -9.92244  -31.17959 1.000 112.00329 ? 518 ASN B OD1   1 
ATOM   3423 N  ND2   . ASN A 1 439 ? -7.57188  -7.79284  -31.04560 1.000 101.57124 ? 518 ASN B ND2   1 
ATOM   3424 N  N     . LEU A 1 440 ? -11.49910 -9.15074  -27.01707 1.000 97.90553  ? 519 LEU B N     1 
ATOM   3425 C  CA    . LEU A 1 440 ? -11.91174 -9.08057  -25.62053 1.000 99.36450  ? 519 LEU B CA    1 
ATOM   3426 C  C     . LEU A 1 440 ? -11.75583 -10.44275 -24.95461 1.000 102.21470 ? 519 LEU B C     1 
ATOM   3427 O  O     . LEU A 1 440 ? -12.13819 -11.47141 -25.51933 1.000 106.20674 ? 519 LEU B O     1 
ATOM   3428 C  CB    . LEU A 1 440 ? -13.35969 -8.59669  -25.51777 1.000 97.49202  ? 519 LEU B CB    1 
ATOM   3429 C  CG    . LEU A 1 440 ? -13.93333 -8.48862  -24.10117 1.000 94.52521  ? 519 LEU B CG    1 
ATOM   3430 C  CD1   . LEU A 1 440 ? -13.14572 -7.48200  -23.27446 1.000 80.59326  ? 519 LEU B CD1   1 
ATOM   3431 C  CD2   . LEU A 1 440 ? -15.41218 -8.12468  -24.13343 1.000 93.79461  ? 519 LEU B CD2   1 
ATOM   3432 N  N     . GLU A 1 441 ? -11.18418 -10.44855 -23.75001 1.000 96.13341  ? 520 GLU B N     1 
ATOM   3433 C  CA    . GLU A 1 441 ? -10.90830 -11.70138 -23.05674 1.000 89.72201  ? 520 GLU B CA    1 
ATOM   3434 C  C     . GLU A 1 441 ? -11.42981 -11.69077 -21.62422 1.000 91.83353  ? 520 GLU B C     1 
ATOM   3435 O  O     . GLU A 1 441 ? -11.77559 -12.74547 -21.08249 1.000 92.64174  ? 520 GLU B O     1 
ATOM   3436 C  CB    . GLU A 1 441 ? -9.40598  -11.99207 -23.06729 1.000 94.51836  ? 520 GLU B CB    1 
ATOM   3437 C  CG    . GLU A 1 441 ? -8.81213  -12.12156 -24.46364 1.000 102.33477 ? 520 GLU B CG    1 
ATOM   3438 C  CD    . GLU A 1 441 ? -7.30258  -12.28206 -24.44917 1.000 100.20150 ? 520 GLU B CD    1 
ATOM   3439 O  OE1   . GLU A 1 441 ? -6.72482  -12.39028 -23.34582 1.000 93.07047  ? 520 GLU B OE1   1 
ATOM   3440 O  OE2   . GLU A 1 441 ? -6.69480  -12.29787 -25.54230 1.000 92.73618  ? 520 GLU B OE2   1 
ATOM   3441 N  N     . GLU A 1 442 ? -11.48760 -10.51444 -20.99960 1.000 94.36539  ? 521 GLU B N     1 
ATOM   3442 C  CA    . GLU A 1 442 ? -11.93831 -10.37844 -19.61770 1.000 87.90221  ? 521 GLU B CA    1 
ATOM   3443 C  C     . GLU A 1 442 ? -12.96021 -9.25525  -19.53874 1.000 84.63693  ? 521 GLU B C     1 
ATOM   3444 O  O     . GLU A 1 442 ? -12.67250 -8.12318  -19.94056 1.000 85.49576  ? 521 GLU B O     1 
ATOM   3445 C  CB    . GLU A 1 442 ? -10.76059 -10.10255 -18.67746 1.000 90.06026  ? 521 GLU B CB    1 
ATOM   3446 C  CG    . GLU A 1 442 ? -9.69354  -11.18897 -18.69113 1.000 96.04568  ? 521 GLU B CG    1 
ATOM   3447 C  CD    . GLU A 1 442 ? -8.47019  -10.82786 -17.86972 1.000 93.82434  ? 521 GLU B CD    1 
ATOM   3448 O  OE1   . GLU A 1 442 ? -8.59931  -10.02727 -16.91962 1.000 96.95944  ? 521 GLU B OE1   1 
ATOM   3449 O  OE2   . GLU A 1 442 ? -7.37575  -11.34424 -18.17857 1.000 102.23897 ? 521 GLU B OE2   1 
ATOM   3450 N  N     . LEU A 1 443 ? -14.14861 -9.56768  -19.02372 1.000 90.13087  ? 522 LEU B N     1 
ATOM   3451 C  CA    . LEU A 1 443 ? -15.23318 -8.59644  -18.87790 1.000 89.89816  ? 522 LEU B CA    1 
ATOM   3452 C  C     . LEU A 1 443 ? -15.81271 -8.73537  -17.47302 1.000 88.26218  ? 522 LEU B C     1 
ATOM   3453 O  O     . LEU A 1 443 ? -16.59816 -9.64960  -17.20597 1.000 80.91806  ? 522 LEU B O     1 
ATOM   3454 C  CB    . LEU A 1 443 ? -16.30665 -8.80189  -19.94376 1.000 89.60453  ? 522 LEU B CB    1 
ATOM   3455 C  CG    . LEU A 1 443 ? -17.51745 -7.86522  -19.88857 1.000 89.06031  ? 522 LEU B CG    1 
ATOM   3456 C  CD1   . LEU A 1 443 ? -17.08637 -6.41456  -20.02973 1.000 78.85507  ? 522 LEU B CD1   1 
ATOM   3457 C  CD2   . LEU A 1 443 ? -18.53514 -8.23060  -20.96030 1.000 85.87037  ? 522 LEU B CD2   1 
ATOM   3458 N  N     . TYR A 1 444 ? -15.42950 -7.82574  -16.57925 1.000 85.04786  ? 523 TYR B N     1 
ATOM   3459 C  CA    . TYR A 1 444 ? -15.88931 -7.83589  -15.19431 1.000 88.88974  ? 523 TYR B CA    1 
ATOM   3460 C  C     . TYR A 1 444 ? -17.09524 -6.91117  -15.06771 1.000 89.34982  ? 523 TYR B C     1 
ATOM   3461 O  O     . TYR A 1 444 ? -16.96967 -5.69063  -15.21122 1.000 84.83847  ? 523 TYR B O     1 
ATOM   3462 C  CB    . TYR A 1 444 ? -14.76836 -7.41327  -14.24807 1.000 80.11658  ? 523 TYR B CB    1 
ATOM   3463 C  CG    . TYR A 1 444 ? -13.60634 -8.37664  -14.22243 1.000 83.16599  ? 523 TYR B CG    1 
ATOM   3464 C  CD1   . TYR A 1 444 ? -12.56466 -8.26063  -15.13288 1.000 93.77272  ? 523 TYR B CD1   1 
ATOM   3465 C  CD2   . TYR A 1 444 ? -13.55183 -9.40534  -13.29080 1.000 74.99261  ? 523 TYR B CD2   1 
ATOM   3466 C  CE1   . TYR A 1 444 ? -11.49867 -9.14077  -15.11646 1.000 93.47553  ? 523 TYR B CE1   1 
ATOM   3467 C  CE2   . TYR A 1 444 ? -12.48943 -10.29081 -13.26596 1.000 82.84082  ? 523 TYR B CE2   1 
ATOM   3468 C  CZ    . TYR A 1 444 ? -11.46549 -10.15328 -14.18194 1.000 92.13338  ? 523 TYR B CZ    1 
ATOM   3469 O  OH    . TYR A 1 444 ? -10.40212 -11.02764 -14.16834 1.000 93.05513  ? 523 TYR B OH    1 
ATOM   3470 N  N     . LEU A 1 445 ? -18.26204 -7.49594  -14.79563 1.000 94.15069  ? 524 LEU B N     1 
ATOM   3471 C  CA    . LEU A 1 445 ? -19.50084 -6.74229  -14.64455 1.000 96.77374  ? 524 LEU B CA    1 
ATOM   3472 C  C     . LEU A 1 445 ? -20.08879 -6.85752  -13.24402 1.000 98.09216  ? 524 LEU B C     1 
ATOM   3473 O  O     . LEU A 1 445 ? -21.22234 -6.41672  -13.02518 1.000 93.94469  ? 524 LEU B O     1 
ATOM   3474 C  CB    . LEU A 1 445 ? -20.53443 -7.20377  -15.67760 1.000 85.42881  ? 524 LEU B CB    1 
ATOM   3475 C  CG    . LEU A 1 445 ? -20.16905 -7.03885  -17.15397 1.000 95.29046  ? 524 LEU B CG    1 
ATOM   3476 C  CD1   . LEU A 1 445 ? -21.25690 -7.62259  -18.04290 1.000 95.23943  ? 524 LEU B CD1   1 
ATOM   3477 C  CD2   . LEU A 1 445 ? -19.93315 -5.57614  -17.48792 1.000 94.95668  ? 524 LEU B CD2   1 
ATOM   3478 N  N     . ASN A 1 446 ? -19.34885 -7.42538  -12.29303 1.000 100.42457 ? 525 ASN B N     1 
ATOM   3479 C  CA    . ASN A 1 446 ? -19.89316 -7.69105  -10.96797 1.000 98.73625  ? 525 ASN B CA    1 
ATOM   3480 C  C     . ASN A 1 446 ? -20.31602 -6.40007  -10.27528 1.000 101.98199 ? 525 ASN B C     1 
ATOM   3481 O  O     . ASN A 1 446 ? -19.77726 -5.32078  -10.53540 1.000 100.45023 ? 525 ASN B O     1 
ATOM   3482 C  CB    . ASN A 1 446 ? -18.86535 -8.43099  -10.10879 1.000 103.87137 ? 525 ASN B CB    1 
ATOM   3483 C  CG    . ASN A 1 446 ? -17.61281 -7.61091  -9.85623  1.000 97.17134  ? 525 ASN B CG    1 
ATOM   3484 O  OD1   . ASN A 1 446 ? -17.53054 -6.86502  -8.88025  1.000 95.73338  ? 525 ASN B OD1   1 
ATOM   3485 N  ND2   . ASN A 1 446 ? -16.62704 -7.75162  -10.73370 1.000 85.31903  ? 525 ASN B ND2   1 
ATOM   3486 N  N     . ASP A 1 447 ? -21.30348 -6.52811  -9.38723  1.000 102.73130 ? 526 ASP B N     1 
ATOM   3487 C  CA    . ASP A 1 447 ? -21.81763 -5.42198  -8.57910  1.000 96.89958  ? 526 ASP B CA    1 
ATOM   3488 C  C     . ASP A 1 447 ? -22.40231 -4.31450  -9.46010  1.000 100.29284 ? 526 ASP B C     1 
ATOM   3489 O  O     . ASP A 1 447 ? -21.99209 -3.15345  -9.40890  1.000 103.63649 ? 526 ASP B O     1 
ATOM   3490 C  CB    . ASP A 1 447 ? -20.73371 -4.87573  -7.64184  1.000 97.74718  ? 526 ASP B CB    1 
ATOM   3491 C  CG    . ASP A 1 447 ? -20.31752 -5.88012  -6.58320  1.000 104.96972 ? 526 ASP B CG    1 
ATOM   3492 O  OD1   . ASP A 1 447 ? -20.87323 -6.99825  -6.56865  1.000 102.28301 ? 526 ASP B OD1   1 
ATOM   3493 O  OD2   . ASP A 1 447 ? -19.43484 -5.55108  -5.76309  1.000 115.95540 ? 526 ASP B OD2   1 
ATOM   3494 N  N     . ASN A 1 448 ? -23.38549 -4.70020  -10.27356 1.000 106.21443 ? 527 ASN B N     1 
ATOM   3495 C  CA    . ASN A 1 448 ? -24.16071 -3.76593  -11.09045 1.000 106.68187 ? 527 ASN B CA    1 
ATOM   3496 C  C     . ASN A 1 448 ? -25.63665 -4.03532  -10.83238 1.000 109.76241 ? 527 ASN B C     1 
ATOM   3497 O  O     . ASN A 1 448 ? -26.26374 -4.84910  -11.52523 1.000 112.62514 ? 527 ASN B O     1 
ATOM   3498 C  CB    . ASN A 1 448 ? -23.81637 -3.89682  -12.57286 1.000 106.25440 ? 527 ASN B CB    1 
ATOM   3499 C  CG    . ASN A 1 448 ? -22.53205 -3.17737  -12.93772 1.000 95.92812  ? 527 ASN B CG    1 
ATOM   3500 O  OD1   . ASN A 1 448 ? -22.54117 -1.98245  -13.23293 1.000 91.98374  ? 527 ASN B OD1   1 
ATOM   3501 N  ND2   . ASN A 1 448 ? -21.41864 -3.90185  -12.91700 1.000 98.92700  ? 527 ASN B ND2   1 
ATOM   3502 N  N     . PRO A 1 449 ? -26.22860 -3.36476  -9.83843  1.000 108.85558 ? 528 PRO B N     1 
ATOM   3503 C  CA    . PRO A 1 449 ? -27.61047 -3.68732  -9.44483  1.000 114.00942 ? 528 PRO B CA    1 
ATOM   3504 C  C     . PRO A 1 449 ? -28.66373 -3.30047  -10.47299 1.000 115.18787 ? 528 PRO B C     1 
ATOM   3505 O  O     . PRO A 1 449 ? -29.82525 -3.69620  -10.31060 1.000 111.35380 ? 528 PRO B O     1 
ATOM   3506 C  CB    . PRO A 1 449 ? -27.79914 -2.89439  -8.14174  1.000 119.03988 ? 528 PRO B CB    1 
ATOM   3507 C  CG    . PRO A 1 449 ? -26.40672 -2.54359  -7.68465  1.000 103.01409 ? 528 PRO B CG    1 
ATOM   3508 C  CD    . PRO A 1 449 ? -25.61655 -2.37376  -8.93968  1.000 104.53732 ? 528 PRO B CD    1 
ATOM   3509 N  N     . ASN A 1 450 ? -28.31136 -2.54707  -11.51268 1.000 118.56493 ? 529 ASN B N     1 
ATOM   3510 C  CA    . ASN A 1 450 ? -29.27016 -2.13348  -12.52872 1.000 117.57564 ? 529 ASN B CA    1 
ATOM   3511 C  C     . ASN A 1 450 ? -29.16786 -2.94830  -13.81213 1.000 111.09287 ? 529 ASN B C     1 
ATOM   3512 O  O     . ASN A 1 450 ? -29.97572 -2.74555  -14.72396 1.000 106.63027 ? 529 ASN B O     1 
ATOM   3513 C  CB    . ASN A 1 450 ? -29.09300 -0.64436  -12.84978 1.000 115.38808 ? 529 ASN B CB    1 
ATOM   3514 C  CG    . ASN A 1 450 ? -29.21012 0.23739   -11.62012 1.000 116.56981 ? 529 ASN B CG    1 
ATOM   3515 O  OD1   . ASN A 1 450 ? -29.85966 -0.12661  -10.63817 1.000 102.68716 ? 529 ASN B OD1   1 
ATOM   3516 N  ND2   . ASN A 1 450 ? -28.57881 1.40682   -11.66921 1.000 114.56586 ? 529 ASN B ND2   1 
ATOM   3517 N  N     . LEU A 1 451 ? -28.20383 -3.86193  -13.90597 1.000 109.98855 ? 530 LEU B N     1 
ATOM   3518 C  CA    . LEU A 1 451 ? -27.99952 -4.65833  -15.11538 1.000 110.84105 ? 530 LEU B CA    1 
ATOM   3519 C  C     . LEU A 1 451 ? -28.94516 -5.85223  -15.07677 1.000 110.64859 ? 530 LEU B C     1 
ATOM   3520 O  O     . LEU A 1 451 ? -28.62710 -6.91329  -14.53763 1.000 114.54928 ? 530 LEU B O     1 
ATOM   3521 C  CB    . LEU A 1 451 ? -26.54652 -5.10182  -15.22996 1.000 106.30844 ? 530 LEU B CB    1 
ATOM   3522 C  CG    . LEU A 1 451 ? -26.13590 -5.72737  -16.56446 1.000 103.34875 ? 530 LEU B CG    1 
ATOM   3523 C  CD1   . LEU A 1 451 ? -26.19586 -4.69256  -17.67869 1.000 99.70695  ? 530 LEU B CD1   1 
ATOM   3524 C  CD2   . LEU A 1 451 ? -24.74897 -6.34093  -16.47042 1.000 101.58483 ? 530 LEU B CD2   1 
ATOM   3525 N  N     . HIS A 1 452 ? -30.12830 -5.67514  -15.65855 1.000 110.30332 ? 531 HIS B N     1 
ATOM   3526 C  CA    . HIS A 1 452 ? -31.12219 -6.73509  -15.74566 1.000 118.91691 ? 531 HIS B CA    1 
ATOM   3527 C  C     . HIS A 1 452 ? -31.08363 -7.47318  -17.07522 1.000 115.66935 ? 531 HIS B C     1 
ATOM   3528 O  O     . HIS A 1 452 ? -31.92815 -8.34201  -17.30941 1.000 117.43780 ? 531 HIS B O     1 
ATOM   3529 C  CB    . HIS A 1 452 ? -32.52603 -6.16775  -15.51826 1.000 111.22080 ? 531 HIS B CB    1 
ATOM   3530 C  CG    . HIS A 1 452 ? -32.73531 -5.60063  -14.14912 1.000 116.46826 ? 531 HIS B CG    1 
ATOM   3531 N  ND1   . HIS A 1 452 ? -33.22249 -6.35004  -13.09999 1.000 111.27455 ? 531 HIS B ND1   1 
ATOM   3532 C  CD2   . HIS A 1 452 ? -32.52582 -4.35644  -13.65738 1.000 118.71003 ? 531 HIS B CD2   1 
ATOM   3533 C  CE1   . HIS A 1 452 ? -33.30398 -5.59219  -12.02097 1.000 116.59829 ? 531 HIS B CE1   1 
ATOM   3534 N  NE2   . HIS A 1 452 ? -32.88680 -4.37808  -12.33211 1.000 118.76226 ? 531 HIS B NE2   1 
ATOM   3535 N  N     . SER A 1 453 ? -30.13195 -7.15155  -17.94807 1.000 116.88449 ? 532 SER B N     1 
ATOM   3536 C  CA    . SER A 1 453 ? -30.06162 -7.77712  -19.25885 1.000 118.49565 ? 532 SER B CA    1 
ATOM   3537 C  C     . SER A 1 453 ? -28.62178 -7.78128  -19.74337 1.000 110.37202 ? 532 SER B C     1 
ATOM   3538 O  O     . SER A 1 453 ? -27.78013 -7.01754  -19.26482 1.000 111.13682 ? 532 SER B O     1 
ATOM   3539 C  CB    . SER A 1 453 ? -30.95644 -7.05739  -20.27587 1.000 122.21124 ? 532 SER B CB    1 
ATOM   3540 O  OG    . SER A 1 453 ? -30.74935 -7.56804  -21.58191 1.000 122.57508 ? 532 SER B OG    1 
ATOM   3541 N  N     . LEU A 1 454 ? -28.35313 -8.65787  -20.70827 1.000 115.81280 ? 533 LEU B N     1 
ATOM   3542 C  CA    . LEU A 1 454 ? -27.06142 -8.74279  -21.36521 1.000 109.37669 ? 533 LEU B CA    1 
ATOM   3543 C  C     . LEU A 1 454 ? -27.27097 -8.71071  -22.87260 1.000 108.14090 ? 533 LEU B C     1 
ATOM   3544 O  O     . LEU A 1 454 ? -28.16719 -9.38990  -23.38881 1.000 126.51882 ? 533 LEU B O     1 
ATOM   3545 C  CB    . LEU A 1 454 ? -26.31404 -10.01942 -20.96140 1.000 109.31131 ? 533 LEU B CB    1 
ATOM   3546 C  CG    . LEU A 1 454 ? -24.90735 -9.82610  -20.39855 1.000 111.20825 ? 533 LEU B CG    1 
ATOM   3547 C  CD1   . LEU A 1 454 ? -24.91012 -8.77000  -19.30095 1.000 102.81720 ? 533 LEU B CD1   1 
ATOM   3548 C  CD2   . LEU A 1 454 ? -24.37017 -11.14583 -19.87207 1.000 108.94672 ? 533 LEU B CD2   1 
ATOM   3549 N  N     . PRO A 1 455 ? -26.47928 -7.92207  -23.59845 1.000 108.92865 ? 534 PRO B N     1 
ATOM   3550 C  CA    . PRO A 1 455 ? -26.69295 -7.79620  -25.04584 1.000 110.89580 ? 534 PRO B CA    1 
ATOM   3551 C  C     . PRO A 1 455 ? -26.45743 -9.11523  -25.76564 1.000 115.99259 ? 534 PRO B C     1 
ATOM   3552 O  O     . PRO A 1 455 ? -25.51645 -9.85343  -25.46526 1.000 119.98308 ? 534 PRO B O     1 
ATOM   3553 C  CB    . PRO A 1 455 ? -25.67005 -6.73518  -25.46521 1.000 112.86156 ? 534 PRO B CB    1 
ATOM   3554 C  CG    . PRO A 1 455 ? -24.61472 -6.79223  -24.40790 1.000 107.71717 ? 534 PRO B CG    1 
ATOM   3555 C  CD    . PRO A 1 455 ? -25.32748 -7.13339  -23.13236 1.000 110.00027 ? 534 PRO B CD    1 
ATOM   3556 N  N     . PHE A 1 456 ? -27.33744 -9.40862  -26.72485 1.000 127.55904 ? 535 PHE B N     1 
ATOM   3557 C  CA    . PHE A 1 456 ? -27.24391 -10.66807 -27.45366 1.000 133.39694 ? 535 PHE B CA    1 
ATOM   3558 C  C     . PHE A 1 456 ? -26.01528 -10.70939 -28.35153 1.000 131.57418 ? 535 PHE B C     1 
ATOM   3559 O  O     . PHE A 1 456 ? -25.50220 -11.79439 -28.64710 1.000 136.04185 ? 535 PHE B O     1 
ATOM   3560 C  CB    . PHE A 1 456 ? -28.51374 -10.89054 -28.27373 1.000 143.66616 ? 535 PHE B CB    1 
ATOM   3561 C  CG    . PHE A 1 456 ? -29.75483 -11.03812 -27.43976 1.000 151.22701 ? 535 PHE B CG    1 
ATOM   3562 C  CD1   . PHE A 1 456 ? -29.68881 -11.56711 -26.16042 1.000 150.79017 ? 535 PHE B CD1   1 
ATOM   3563 C  CD2   . PHE A 1 456 ? -30.98734 -10.64627 -27.93447 1.000 153.29944 ? 535 PHE B CD2   1 
ATOM   3564 C  CE1   . PHE A 1 456 ? -30.82980 -11.70553 -25.39114 1.000 151.76835 ? 535 PHE B CE1   1 
ATOM   3565 C  CE2   . PHE A 1 456 ? -32.13160 -10.78167 -27.17061 1.000 155.87122 ? 535 PHE B CE2   1 
ATOM   3566 C  CZ    . PHE A 1 456 ? -32.05263 -11.31201 -25.89762 1.000 156.51453 ? 535 PHE B CZ    1 
ATOM   3567 N  N     . GLU A 1 457 ? -25.52583 -9.54804  -28.78674 1.000 125.43779 ? 536 GLU B N     1 
ATOM   3568 C  CA    . GLU A 1 457 ? -24.35132 -9.49279  -29.64889 1.000 124.51765 ? 536 GLU B CA    1 
ATOM   3569 C  C     . GLU A 1 457 ? -23.05402 -9.77057  -28.90198 1.000 120.49453 ? 536 GLU B C     1 
ATOM   3570 O  O     . GLU A 1 457 ? -21.99086 -9.77182  -29.53265 1.000 116.07838 ? 536 GLU B O     1 
ATOM   3571 C  CB    . GLU A 1 457 ? -24.26485 -8.12731  -30.33454 1.000 116.15442 ? 536 GLU B CB    1 
ATOM   3572 C  CG    . GLU A 1 457 ? -25.48573 -7.24363  -30.12982 1.000 121.74077 ? 536 GLU B CG    1 
ATOM   3573 C  CD    . GLU A 1 457 ? -26.67119 -7.66815  -30.97141 1.000 122.14494 ? 536 GLU B CD    1 
ATOM   3574 O  OE1   . GLU A 1 457 ? -26.45954 -8.30808  -32.02290 1.000 130.69286 ? 536 GLU B OE1   1 
ATOM   3575 O  OE2   . GLU A 1 457 ? -27.81597 -7.36167  -30.57815 1.000 124.16507 ? 536 GLU B OE2   1 
ATOM   3576 N  N     . LEU A 1 458 ? -23.10964 -10.00091 -27.58711 1.000 112.83768 ? 537 LEU B N     1 
ATOM   3577 C  CA    . LEU A 1 458 ? -21.90118 -10.28665 -26.82204 1.000 120.32325 ? 537 LEU B CA    1 
ATOM   3578 C  C     . LEU A 1 458 ? -21.26979 -11.61685 -27.21439 1.000 118.23984 ? 537 LEU B C     1 
ATOM   3579 O  O     . LEU A 1 458 ? -20.07084 -11.81119 -26.98567 1.000 109.65255 ? 537 LEU B O     1 
ATOM   3580 C  CB    . LEU A 1 458 ? -22.21719 -10.27542 -25.32264 1.000 118.75106 ? 537 LEU B CB    1 
ATOM   3581 C  CG    . LEU A 1 458 ? -21.05275 -10.34760 -24.32850 1.000 99.18584  ? 537 LEU B CG    1 
ATOM   3582 C  CD1   . LEU A 1 458 ? -20.15608 -9.12544  -24.44669 1.000 98.90822  ? 537 LEU B CD1   1 
ATOM   3583 C  CD2   . LEU A 1 458 ? -21.56853 -10.49748 -22.90645 1.000 98.66385  ? 537 LEU B CD2   1 
ATOM   3584 N  N     . ALA A 1 459 ? -22.04345 -12.52836 -27.81055 1.000 121.38992 ? 538 ALA B N     1 
ATOM   3585 C  CA    . ALA A 1 459 ? -21.51435 -13.83291 -28.19033 1.000 112.10947 ? 538 ALA B CA    1 
ATOM   3586 C  C     . ALA A 1 459 ? -20.47689 -13.74552 -29.30309 1.000 111.38829 ? 538 ALA B C     1 
ATOM   3587 O  O     . ALA A 1 459 ? -19.68977 -14.68301 -29.47008 1.000 118.08874 ? 538 ALA B O     1 
ATOM   3588 C  CB    . ALA A 1 459 ? -22.65559 -14.75822 -28.61423 1.000 123.94964 ? 538 ALA B CB    1 
ATOM   3589 N  N     . LEU A 1 460 ? -20.45351 -12.64792 -30.06357 1.000 112.04954 ? 539 LEU B N     1 
ATOM   3590 C  CA    . LEU A 1 460 ? -19.47031 -12.48430 -31.12893 1.000 110.90033 ? 539 LEU B CA    1 
ATOM   3591 C  C     . LEU A 1 460 ? -18.05362 -12.28402 -30.60336 1.000 110.26295 ? 539 LEU B C     1 
ATOM   3592 O  O     . LEU A 1 460 ? -17.10494 -12.35873 -31.39220 1.000 116.37440 ? 539 LEU B O     1 
ATOM   3593 C  CB    . LEU A 1 460 ? -19.86706 -11.31101 -32.02956 1.000 112.99262 ? 539 LEU B CB    1 
ATOM   3594 C  CG    . LEU A 1 460 ? -21.07359 -11.54681 -32.94530 1.000 112.05259 ? 539 LEU B CG    1 
ATOM   3595 C  CD1   . LEU A 1 460 ? -21.82201 -10.24869 -33.21711 1.000 103.45322 ? 539 LEU B CD1   1 
ATOM   3596 C  CD2   . LEU A 1 460 ? -20.63654 -12.19210 -34.25440 1.000 98.82422  ? 539 LEU B CD2   1 
ATOM   3597 N  N     . CYS A 1 461 ? -17.88590 -12.03353 -29.30595 1.000 106.47588 ? 540 CYS B N     1 
ATOM   3598 C  CA    . CYS A 1 461 ? -16.56103 -11.94144 -28.69478 1.000 111.04293 ? 540 CYS B CA    1 
ATOM   3599 C  C     . CYS A 1 461 ? -16.04391 -13.35809 -28.48643 1.000 107.46757 ? 540 CYS B C     1 
ATOM   3600 O  O     . CYS A 1 461 ? -16.37702 -14.01625 -27.49880 1.000 110.13577 ? 540 CYS B O     1 
ATOM   3601 C  CB    . CYS A 1 461 ? -16.62286 -11.17094 -27.38097 1.000 108.96635 ? 540 CYS B CB    1 
ATOM   3602 S  SG    . CYS A 1 461 ? -17.32212 -9.50709  -27.51865 1.000 111.09538 ? 540 CYS B SG    1 
ATOM   3603 N  N     . SER A 1 462 ? -15.21874 -13.83074 -29.42214 1.000 108.48833 ? 541 SER B N     1 
ATOM   3604 C  CA    . SER A 1 462 ? -14.80968 -15.23160 -29.40914 1.000 113.89775 ? 541 SER B CA    1 
ATOM   3605 C  C     . SER A 1 462 ? -13.87148 -15.53766 -28.24722 1.000 117.09586 ? 541 SER B C     1 
ATOM   3606 O  O     . SER A 1 462 ? -13.99005 -16.59066 -27.61028 1.000 126.10267 ? 541 SER B O     1 
ATOM   3607 C  CB    . SER A 1 462 ? -14.14788 -15.59402 -30.73790 1.000 121.57997 ? 541 SER B CB    1 
ATOM   3608 O  OG    . SER A 1 462 ? -12.98280 -14.81668 -30.95460 1.000 125.79170 ? 541 SER B OG    1 
ATOM   3609 N  N     . LYS A 1 463 ? -12.93455 -14.63945 -27.95526 1.000 108.99421 ? 542 LYS B N     1 
ATOM   3610 C  CA    . LYS A 1 463 ? -11.90527 -14.89964 -26.95807 1.000 107.63828 ? 542 LYS B CA    1 
ATOM   3611 C  C     . LYS A 1 463 ? -12.34604 -14.56253 -25.53703 1.000 103.92494 ? 542 LYS B C     1 
ATOM   3612 O  O     . LYS A 1 463 ? -11.51472 -14.58983 -24.62367 1.000 104.69650 ? 542 LYS B O     1 
ATOM   3613 C  CB    . LYS A 1 463 ? -10.63316 -14.12192 -27.30326 1.000 106.49192 ? 542 LYS B CB    1 
ATOM   3614 C  CG    . LYS A 1 463 ? -10.29854 -14.11440 -28.78393 1.000 105.13731 ? 542 LYS B CG    1 
ATOM   3615 C  CD    . LYS A 1 463 ? -8.93344  -13.49645 -29.03693 1.000 108.58872 ? 542 LYS B CD    1 
ATOM   3616 C  CE    . LYS A 1 463 ? -8.79627  -13.03842 -30.47920 1.000 108.88271 ? 542 LYS B CE    1 
ATOM   3617 N  NZ    . LYS A 1 463 ? -9.24067  -14.08012 -31.44631 1.000 105.84478 ? 542 LYS B NZ    1 
ATOM   3618 N  N     . LEU A 1 464 ? -13.62372 -14.25389 -25.32701 1.000 104.01365 ? 543 LEU B N     1 
ATOM   3619 C  CA    . LEU A 1 464 ? -14.12036 -13.86894 -24.00615 1.000 105.49798 ? 543 LEU B CA    1 
ATOM   3620 C  C     . LEU A 1 464 ? -14.19266 -15.10436 -23.11665 1.000 105.17130 ? 543 LEU B C     1 
ATOM   3621 O  O     . LEU A 1 464 ? -15.14704 -15.88195 -23.18410 1.000 119.88693 ? 543 LEU B O     1 
ATOM   3622 C  CB    . LEU A 1 464 ? -15.48242 -13.19328 -24.12553 1.000 103.56326 ? 543 LEU B CB    1 
ATOM   3623 C  CG    . LEU A 1 464 ? -16.11673 -12.71607 -22.81573 1.000 99.59839  ? 543 LEU B CG    1 
ATOM   3624 C  CD1   . LEU A 1 464 ? -15.18814 -11.75438 -22.08362 1.000 96.23503  ? 543 LEU B CD1   1 
ATOM   3625 C  CD2   . LEU A 1 464 ? -17.46991 -12.07020 -23.07149 1.000 93.21089  ? 543 LEU B CD2   1 
ATOM   3626 N  N     . SER A 1 465 ? -13.18310 -15.28535 -22.26620 1.000 101.27881 ? 544 SER B N     1 
ATOM   3627 C  CA    . SER A 1 465 ? -13.10263 -16.44364 -21.38428 1.000 102.00179 ? 544 SER B CA    1 
ATOM   3628 C  C     . SER A 1 465 ? -13.47707 -16.11479 -19.94419 1.000 103.77354 ? 544 SER B C     1 
ATOM   3629 O  O     . SER A 1 465 ? -14.27757 -16.82895 -19.33275 1.000 113.46121 ? 544 SER B O     1 
ATOM   3630 C  CB    . SER A 1 465 ? -11.69051 -17.04059 -21.43112 1.000 107.82488 ? 544 SER B CB    1 
ATOM   3631 O  OG    . SER A 1 465 ? -10.72022 -16.09336 -21.01814 1.000 111.73543 ? 544 SER B OG    1 
ATOM   3632 N  N     . ILE A 1 466 ? -12.91368 -15.04515 -19.38992 1.000 97.97911  ? 545 ILE B N     1 
ATOM   3633 C  CA    . ILE A 1 466 ? -13.12941 -14.66422 -17.99924 1.000 99.46115  ? 545 ILE B CA    1 
ATOM   3634 C  C     . ILE A 1 466 ? -14.24261 -13.62760 -17.93978 1.000 96.84889  ? 545 ILE B C     1 
ATOM   3635 O  O     . ILE A 1 466 ? -14.25700 -12.67221 -18.72704 1.000 93.65198  ? 545 ILE B O     1 
ATOM   3636 C  CB    . ILE A 1 466 ? -11.83433 -14.12532 -17.36793 1.000 89.33537  ? 545 ILE B CB    1 
ATOM   3637 C  CG1   . ILE A 1 466 ? -10.77877 -15.22876 -17.30270 1.000 89.09283  ? 545 ILE B CG1   1 
ATOM   3638 C  CG2   . ILE A 1 466 ? -12.09938 -13.55694 -15.98376 1.000 87.73719  ? 545 ILE B CG2   1 
ATOM   3639 C  CD1   . ILE A 1 466 ? -9.48868  -14.79614 -16.63957 1.000 99.56660  ? 545 ILE B CD1   1 
ATOM   3640 N  N     . MET A 1 467 ? -15.17686 -13.81637 -17.00986 1.000 85.42353  ? 546 MET B N     1 
ATOM   3641 C  CA    . MET A 1 467 ? -16.27252 -12.87787 -16.82128 1.000 83.48997  ? 546 MET B CA    1 
ATOM   3642 C  C     . MET A 1 467 ? -16.88390 -13.11213 -15.44801 1.000 93.21434  ? 546 MET B C     1 
ATOM   3643 O  O     . MET A 1 467 ? -17.02874 -14.25866 -15.01628 1.000 108.76772 ? 546 MET B O     1 
ATOM   3644 C  CB    . MET A 1 467 ? -17.33098 -13.03049 -17.92051 1.000 90.38447  ? 546 MET B CB    1 
ATOM   3645 C  CG    . MET A 1 467 ? -18.55393 -12.14537 -17.74631 1.000 92.99598  ? 546 MET B CG    1 
ATOM   3646 S  SD    . MET A 1 467 ? -19.67130 -12.23526 -19.15936 1.000 116.73395 ? 546 MET B SD    1 
ATOM   3647 C  CE    . MET A 1 467 ? -19.92975 -14.00534 -19.27077 1.000 113.93888 ? 546 MET B CE    1 
ATOM   3648 N  N     . SER A 1 468 ? -17.22787 -12.02145 -14.76693 1.000 93.32777  ? 547 SER B N     1 
ATOM   3649 C  CA    . SER A 1 468 ? -17.85190 -12.06853 -13.45135 1.000 103.63935 ? 547 SER B CA    1 
ATOM   3650 C  C     . SER A 1 468 ? -19.18456 -11.33512 -13.50360 1.000 94.81579  ? 547 SER B C     1 
ATOM   3651 O  O     . SER A 1 468 ? -19.27404 -10.23968 -14.06838 1.000 95.43557  ? 547 SER B O     1 
ATOM   3652 C  CB    . SER A 1 468 ? -16.94272 -11.44708 -12.38582 1.000 96.86744  ? 547 SER B CB    1 
ATOM   3653 O  OG    . SER A 1 468 ? -16.78479 -10.05528 -12.59820 1.000 93.85056  ? 547 SER B OG    1 
ATOM   3654 N  N     . ILE A 1 469 ? -20.21843 -11.94043 -12.92070 1.000 101.39348 ? 548 ILE B N     1 
ATOM   3655 C  CA    . ILE A 1 469 ? -21.55641 -11.35845 -12.95113 1.000 102.67968 ? 548 ILE B CA    1 
ATOM   3656 C  C     . ILE A 1 469 ? -22.20943 -11.45197 -11.57882 1.000 99.92577  ? 548 ILE B C     1 
ATOM   3657 O  O     . ILE A 1 469 ? -23.42878 -11.29225 -11.45424 1.000 107.63773 ? 548 ILE B O     1 
ATOM   3658 C  CB    . ILE A 1 469 ? -22.44207 -12.03826 -14.01482 1.000 106.51689 ? 548 ILE B CB    1 
ATOM   3659 C  CG1   . ILE A 1 469 ? -22.58672 -13.53650 -13.72617 1.000 109.31789 ? 548 ILE B CG1   1 
ATOM   3660 C  CG2   . ILE A 1 469 ? -21.89162 -11.80365 -15.41596 1.000 98.54940  ? 548 ILE B CG2   1 
ATOM   3661 C  CD1   . ILE A 1 469 ? -23.95619 -13.93857 -13.20101 1.000 111.01655 ? 548 ILE B CD1   1 
ATOM   3662 N  N     . GLU A 1 470 ? -21.41529 -11.71439 -10.54254 1.000 101.35999 ? 549 GLU B N     1 
ATOM   3663 C  CA    . GLU A 1 470 ? -21.97616 -11.81955 -9.20152  1.000 109.28549 ? 549 GLU B CA    1 
ATOM   3664 C  C     . GLU A 1 470 ? -22.57402 -10.48601 -8.76829  1.000 107.40149 ? 549 GLU B C     1 
ATOM   3665 O  O     . GLU A 1 470 ? -22.01357 -9.41887  -9.03514  1.000 114.64788 ? 549 GLU B O     1 
ATOM   3666 C  CB    . GLU A 1 470 ? -20.91266 -12.27931 -8.20085  1.000 103.94386 ? 549 GLU B CB    1 
ATOM   3667 C  CG    . GLU A 1 470 ? -19.56777 -11.58657 -8.32700  1.000 103.78855 ? 549 GLU B CG    1 
ATOM   3668 C  CD    . GLU A 1 470 ? -18.60030 -12.35734 -9.20212  1.000 106.64976 ? 549 GLU B CD    1 
ATOM   3669 O  OE1   . GLU A 1 470 ? -19.05998 -13.22197 -9.97742  1.000 113.85561 ? 549 GLU B OE1   1 
ATOM   3670 O  OE2   . GLU A 1 470 ? -17.37999 -12.10612 -9.10849  1.000 110.52101 ? 549 GLU B OE2   1 
ATOM   3671 N  N     . ASN A 1 471 ? -23.73264 -10.56286 -8.10582  1.000 111.17246 ? 550 ASN B N     1 
ATOM   3672 C  CA    . ASN A 1 471 ? -24.51928 -9.40286  -7.68323  1.000 100.12701 ? 550 ASN B CA    1 
ATOM   3673 C  C     . ASN A 1 471 ? -25.07025 -8.61599  -8.87051  1.000 95.95084  ? 550 ASN B C     1 
ATOM   3674 O  O     . ASN A 1 471 ? -25.22043 -7.39463  -8.79874  1.000 94.48189  ? 550 ASN B O     1 
ATOM   3675 C  CB    . ASN A 1 471 ? -23.71959 -8.48107  -6.75575  1.000 104.07378 ? 550 ASN B CB    1 
ATOM   3676 C  CG    . ASN A 1 471 ? -23.22986 -9.19176  -5.50957  1.000 112.11316 ? 550 ASN B CG    1 
ATOM   3677 O  OD1   . ASN A 1 471 ? -23.97147 -9.94463  -4.87665  1.000 111.00848 ? 550 ASN B OD1   1 
ATOM   3678 N  ND2   . ASN A 1 471 ? -21.97072 -8.96133  -5.15439  1.000 111.51186 ? 550 ASN B ND2   1 
ATOM   3679 N  N     . CYS A 1 472 ? -25.37397 -9.30615  -9.96948  1.000 108.45036 ? 551 CYS B N     1 
ATOM   3680 C  CA    . CYS A 1 472 ? -26.07826 -8.72090  -11.10010 1.000 110.23744 ? 551 CYS B CA    1 
ATOM   3681 C  C     . CYS A 1 472 ? -27.44168 -9.37188  -11.23921 1.000 112.32017 ? 551 CYS B C     1 
ATOM   3682 O  O     . CYS A 1 472 ? -27.52360 -10.60603 -11.29767 1.000 120.96361 ? 551 CYS B O     1 
ATOM   3683 C  CB    . CYS A 1 472 ? -25.28795 -8.90190  -12.39788 1.000 112.17902 ? 551 CYS B CB    1 
ATOM   3684 S  SG    . CYS A 1 472 ? -23.78258 -7.93251  -12.48811 1.000 119.07448 ? 551 CYS B SG    1 
ATOM   3685 N  N     . PRO A 1 473 ? -28.52325 -8.59406  -11.29254 1.000 107.12349 ? 552 PRO B N     1 
ATOM   3686 C  CA    . PRO A 1 473 ? -29.86132 -9.19499  -11.37512 1.000 103.29996 ? 552 PRO B CA    1 
ATOM   3687 C  C     . PRO A 1 473 ? -30.02747 -10.10306 -12.58411 1.000 115.56979 ? 552 PRO B C     1 
ATOM   3688 O  O     . PRO A 1 473 ? -30.26775 -11.30453 -12.42646 1.000 112.95357 ? 552 PRO B O     1 
ATOM   3689 C  CB    . PRO A 1 473 ? -30.78729 -7.97429  -11.45411 1.000 109.05669 ? 552 PRO B CB    1 
ATOM   3690 C  CG    . PRO A 1 473 ? -30.00831 -6.87104  -10.81717 1.000 108.89851 ? 552 PRO B CG    1 
ATOM   3691 C  CD    . PRO A 1 473 ? -28.58019 -7.12589  -11.20079 1.000 108.91897 ? 552 PRO B CD    1 
ATOM   3692 N  N     . LEU A 1 474 ? -29.88545 -9.54310  -13.78862 1.000 119.93639 ? 553 LEU B N     1 
ATOM   3693 C  CA    . LEU A 1 474 ? -30.07036 -10.28655 -15.03766 1.000 120.38420 ? 553 LEU B CA    1 
ATOM   3694 C  C     . LEU A 1 474 ? -31.44647 -10.95294 -15.07722 1.000 125.33996 ? 553 LEU B C     1 
ATOM   3695 O  O     . LEU A 1 474 ? -31.58627 -12.12932 -15.41913 1.000 128.65319 ? 553 LEU B O     1 
ATOM   3696 C  CB    . LEU A 1 474 ? -28.95242 -11.31444 -15.23828 1.000 115.72300 ? 553 LEU B CB    1 
ATOM   3697 C  CG    . LEU A 1 474 ? -27.52898 -10.76499 -15.35133 1.000 114.38662 ? 553 LEU B CG    1 
ATOM   3698 C  CD1   . LEU A 1 474 ? -26.50372 -11.87771 -15.20026 1.000 111.19693 ? 553 LEU B CD1   1 
ATOM   3699 C  CD2   . LEU A 1 474 ? -27.34372 -10.04482 -16.67662 1.000 117.31366 ? 553 LEU B CD2   1 
ATOM   3700 N  N     . SER A 1 475 ? -32.47578 -10.17925 -14.71949 1.000 113.56705 ? 554 SER B N     1 
ATOM   3701 C  CA    . SER A 1 475 ? -33.82380 -10.72731 -14.61720 1.000 116.32656 ? 554 SER B CA    1 
ATOM   3702 C  C     . SER A 1 475 ? -34.44709 -11.01231 -15.97756 1.000 125.50690 ? 554 SER B C     1 
ATOM   3703 O  O     . SER A 1 475 ? -35.34467 -11.85705 -16.06609 1.000 126.00315 ? 554 SER B O     1 
ATOM   3704 C  CB    . SER A 1 475 ? -34.72246 -9.77591  -13.82528 1.000 118.33281 ? 554 SER B CB    1 
ATOM   3705 O  OG    . SER A 1 475 ? -34.90997 -8.55217  -14.51390 1.000 129.50198 ? 554 SER B OG    1 
ATOM   3706 N  N     . HIS A 1 476 ? -34.00305 -10.32664 -17.03438 1.000 126.79345 ? 555 HIS B N     1 
ATOM   3707 C  CA    . HIS A 1 476 ? -34.52225 -10.60249 -18.36914 1.000 119.00053 ? 555 HIS B CA    1 
ATOM   3708 C  C     . HIS A 1 476 ? -34.05047 -11.94996 -18.89792 1.000 123.49076 ? 555 HIS B C     1 
ATOM   3709 O  O     . HIS A 1 476 ? -34.70832 -12.52645 -19.77076 1.000 127.28948 ? 555 HIS B O     1 
ATOM   3710 C  CB    . HIS A 1 476 ? -34.11897 -9.48626  -19.33442 1.000 113.52642 ? 555 HIS B CB    1 
ATOM   3711 C  CG    . HIS A 1 476 ? -34.67508 -8.14335  -18.97224 1.000 117.04931 ? 555 HIS B CG    1 
ATOM   3712 N  ND1   . HIS A 1 476 ? -35.48454 -7.94283  -17.87445 1.000 116.98100 ? 555 HIS B ND1   1 
ATOM   3713 C  CD2   . HIS A 1 476 ? -34.53977 -6.93318  -19.56478 1.000 115.34769 ? 555 HIS B CD2   1 
ATOM   3714 C  CE1   . HIS A 1 476 ? -35.82228 -6.66751  -17.80521 1.000 115.38485 ? 555 HIS B CE1   1 
ATOM   3715 N  NE2   . HIS A 1 476 ? -35.26239 -6.03302  -18.81946 1.000 115.44634 ? 555 HIS B NE2   1 
ATOM   3716 N  N     . LEU A 1 477 ? -32.93210 -12.45873 -18.39182 1.000 125.95209 ? 556 LEU B N     1 
ATOM   3717 C  CA    . LEU A 1 477 ? -32.41242 -13.78679 -18.66745 1.000 132.70002 ? 556 LEU B CA    1 
ATOM   3718 C  C     . LEU A 1 477 ? -33.01152 -14.79401 -17.68894 1.000 142.87599 ? 556 LEU B C     1 
ATOM   3719 O  O     . LEU A 1 477 ? -33.39402 -14.42902 -16.57153 1.000 131.23226 ? 556 LEU B O     1 
ATOM   3720 C  CB    . LEU A 1 477 ? -30.88991 -13.79463 -18.55429 1.000 127.33782 ? 556 LEU B CB    1 
ATOM   3721 C  CG    . LEU A 1 477 ? -30.15614 -12.71645 -19.35665 1.000 130.62911 ? 556 LEU B CG    1 
ATOM   3722 C  CD1   . LEU A 1 477 ? -28.64900 -12.85407 -19.19913 1.000 124.94225 ? 556 LEU B CD1   1 
ATOM   3723 C  CD2   . LEU A 1 477 ? -30.55369 -12.76424 -20.82508 1.000 133.37568 ? 556 LEU B CD2   1 
ATOM   3724 N  N     . PRO A 1 478 ? -33.12146 -16.06164 -18.08386 1.000 147.27752 ? 557 PRO B N     1 
ATOM   3725 C  CA    . PRO A 1 478 ? -33.75174 -17.04280 -17.20555 1.000 146.68371 ? 557 PRO B CA    1 
ATOM   3726 C  C     . PRO A 1 478 ? -32.95390 -17.21525 -15.92827 1.000 146.46317 ? 557 PRO B C     1 
ATOM   3727 O  O     . PRO A 1 478 ? -31.71309 -17.10825 -15.93023 1.000 146.28891 ? 557 PRO B O     1 
ATOM   3728 C  CB    . PRO A 1 478 ? -33.74965 -18.32539 -18.04938 1.000 145.65066 ? 557 PRO B CB    1 
ATOM   3729 C  CG    . PRO A 1 478 ? -33.65512 -17.85269 -19.46131 1.000 141.77576 ? 557 PRO B CG    1 
ATOM   3730 C  CD    . PRO A 1 478 ? -32.79989 -16.62678 -19.40586 1.000 139.81280 ? 557 PRO B CD    1 
ATOM   3731 N  N     . PRO A 1 479 ? -33.62861 -17.47544 -14.80498 1.000 147.83830 ? 558 PRO B N     1 
ATOM   3732 C  CA    . PRO A 1 479 ? -32.89377 -17.67182 -13.54426 1.000 144.20018 ? 558 PRO B CA    1 
ATOM   3733 C  C     . PRO A 1 479 ? -31.99576 -18.89492 -13.55620 1.000 148.34262 ? 558 PRO B C     1 
ATOM   3734 O  O     . PRO A 1 479 ? -30.96803 -18.90347 -12.86761 1.000 151.03772 ? 558 PRO B O     1 
ATOM   3735 C  CB    . PRO A 1 479 ? -34.01398 -17.80423 -12.50092 1.000 134.19815 ? 558 PRO B CB    1 
ATOM   3736 C  CG    . PRO A 1 479 ? -35.22124 -17.19534 -13.14420 1.000 135.20206 ? 558 PRO B CG    1 
ATOM   3737 C  CD    . PRO A 1 479 ? -35.08640 -17.49492 -14.60435 1.000 142.46342 ? 558 PRO B CD    1 
ATOM   3738 N  N     . GLN A 1 480 ? -32.35093 -19.93168 -14.31925 1.000 159.90691 ? 559 GLN B N     1 
ATOM   3739 C  CA    . GLN A 1 480 ? -31.51437 -21.12572 -14.37788 1.000 159.03731 ? 559 GLN B CA    1 
ATOM   3740 C  C     . GLN A 1 480 ? -30.24388 -20.88670 -15.18430 1.000 155.75423 ? 559 GLN B C     1 
ATOM   3741 O  O     . GLN A 1 480 ? -29.20316 -21.48606 -14.88979 1.000 148.67997 ? 559 GLN B O     1 
ATOM   3742 C  CB    . GLN A 1 480 ? -32.30705 -22.29402 -14.96513 1.000 163.36283 ? 559 GLN B CB    1 
ATOM   3743 C  CG    . GLN A 1 480 ? -33.02402 -21.96977 -16.26653 1.000 164.17206 ? 559 GLN B CG    1 
ATOM   3744 C  CD    . GLN A 1 480 ? -32.64437 -22.91164 -17.39178 1.000 169.00912 ? 559 GLN B CD    1 
ATOM   3745 O  OE1   . GLN A 1 480 ? -31.60834 -23.57489 -17.33902 1.000 169.43883 ? 559 GLN B OE1   1 
ATOM   3746 N  NE2   . GLN A 1 480 ? -33.48522 -22.97702 -18.41773 1.000 166.28033 ? 559 GLN B NE2   1 
ATOM   3747 N  N     . ILE A 1 481 ? -30.30489 -20.02022 -16.19741 1.000 156.56930 ? 560 ILE B N     1 
ATOM   3748 C  CA    . ILE A 1 481 ? -29.11878 -19.73334 -16.99744 1.000 150.71265 ? 560 ILE B CA    1 
ATOM   3749 C  C     . ILE A 1 481 ? -28.14572 -18.85994 -16.21582 1.000 151.22919 ? 560 ILE B C     1 
ATOM   3750 O  O     . ILE A 1 481 ? -26.92945 -19.08590 -16.24004 1.000 143.80117 ? 560 ILE B O     1 
ATOM   3751 C  CB    . ILE A 1 481 ? -29.52089 -19.08269 -18.33352 1.000 146.27724 ? 560 ILE B CB    1 
ATOM   3752 C  CG1   . ILE A 1 481 ? -30.41246 -20.02928 -19.13737 1.000 149.66618 ? 560 ILE B CG1   1 
ATOM   3753 C  CG2   . ILE A 1 481 ? -28.28749 -18.70764 -19.14045 1.000 149.94336 ? 560 ILE B CG2   1 
ATOM   3754 C  CD1   . ILE A 1 481 ? -29.75339 -21.35080 -19.46571 1.000 148.28824 ? 560 ILE B CD1   1 
ATOM   3755 N  N     . VAL A 1 482 ? -28.66132 -17.85434 -15.50389 1.000 146.81822 ? 561 VAL B N     1 
ATOM   3756 C  CA    . VAL A 1 482 ? -27.79169 -16.97003 -14.73931 1.000 145.20579 ? 561 VAL B CA    1 
ATOM   3757 C  C     . VAL A 1 482 ? -27.26827 -17.64337 -13.47700 1.000 147.73692 ? 561 VAL B C     1 
ATOM   3758 O  O     . VAL A 1 482 ? -26.24026 -17.21950 -12.93493 1.000 142.50545 ? 561 VAL B O     1 
ATOM   3759 C  CB    . VAL A 1 482 ? -28.52511 -15.65961 -14.39559 1.000 127.96930 ? 561 VAL B CB    1 
ATOM   3760 C  CG1   . VAL A 1 482 ? -29.03777 -14.99501 -15.66186 1.000 129.21119 ? 561 VAL B CG1   1 
ATOM   3761 C  CG2   . VAL A 1 482 ? -29.66428 -15.92053 -13.42625 1.000 132.48545 ? 561 VAL B CG2   1 
ATOM   3762 N  N     . ALA A 1 483 ? -27.94310 -18.69034 -12.99400 1.000 138.60530 ? 562 ALA B N     1 
ATOM   3763 C  CA    . ALA A 1 483 ? -27.47235 -19.37694 -11.79601 1.000 139.45501 ? 562 ALA B CA    1 
ATOM   3764 C  C     . ALA A 1 483 ? -26.20553 -20.17664 -12.06587 1.000 141.57566 ? 562 ALA B C     1 
ATOM   3765 O  O     . ALA A 1 483 ? -25.39075 -20.36759 -11.15578 1.000 139.10850 ? 562 ALA B O     1 
ATOM   3766 C  CB    . ALA A 1 483 ? -28.56565 -20.29109 -11.24494 1.000 140.99777 ? 562 ALA B CB    1 
ATOM   3767 N  N     . GLY A 1 484 ? -26.02261 -20.64762 -13.29726 1.000 140.74177 ? 563 GLY B N     1 
ATOM   3768 C  CA    . GLY A 1 484 ? -24.85378 -21.42920 -13.64736 1.000 137.81019 ? 563 GLY B CA    1 
ATOM   3769 C  C     . GLY A 1 484 ? -23.55736 -20.66033 -13.50788 1.000 142.50231 ? 563 GLY B C     1 
ATOM   3770 O  O     . GLY A 1 484 ? -22.89416 -20.73157 -12.46865 1.000 144.40230 ? 563 GLY B O     1 
ATOM   3771 N  N     . GLY A 1 485 ? -23.18646 -19.91915 -14.54766 1.000 144.71559 ? 564 GLY B N     1 
ATOM   3772 C  CA    . GLY A 1 485 ? -21.96783 -19.14804 -14.53324 1.000 146.57403 ? 564 GLY B CA    1 
ATOM   3773 C  C     . GLY A 1 485 ? -21.72894 -18.42877 -15.84357 1.000 148.48217 ? 564 GLY B C     1 
ATOM   3774 O  O     . GLY A 1 485 ? -22.66200 -18.13865 -16.59935 1.000 139.85984 ? 564 GLY B O     1 
ATOM   3775 N  N     . PRO A 1 486 ? -20.46240 -18.12080 -16.13620 1.000 158.24797 ? 565 PRO B N     1 
ATOM   3776 C  CA    . PRO A 1 486 ? -20.16309 -17.43139 -17.40432 1.000 153.12281 ? 565 PRO B CA    1 
ATOM   3777 C  C     . PRO A 1 486 ? -20.51497 -18.26130 -18.62533 1.000 153.62840 ? 565 PRO B C     1 
ATOM   3778 O  O     . PRO A 1 486 ? -21.19968 -17.77011 -19.53151 1.000 151.88851 ? 565 PRO B O     1 
ATOM   3779 C  CB    . PRO A 1 486 ? -18.65305 -17.16096 -17.30580 1.000 147.76021 ? 565 PRO B CB    1 
ATOM   3780 C  CG    . PRO A 1 486 ? -18.32557 -17.27666 -15.84760 1.000 150.45270 ? 565 PRO B CG    1 
ATOM   3781 C  CD    . PRO A 1 486 ? -19.25961 -18.31301 -15.31077 1.000 152.74588 ? 565 PRO B CD    1 
ATOM   3782 N  N     . SER A 1 487 ? -20.07533 -19.52198 -18.66443 1.000 150.77459 ? 566 SER B N     1 
ATOM   3783 C  CA    . SER A 1 487 ? -20.30256 -20.35347 -19.84152 1.000 150.20179 ? 566 SER B CA    1 
ATOM   3784 C  C     . SER A 1 487 ? -21.78534 -20.60851 -20.08211 1.000 149.17400 ? 566 SER B C     1 
ATOM   3785 O  O     . SER A 1 487 ? -22.19122 -20.86168 -21.22228 1.000 153.79126 ? 566 SER B O     1 
ATOM   3786 C  CB    . SER A 1 487 ? -19.55221 -21.67731 -19.69805 1.000 143.87422 ? 566 SER B CB    1 
ATOM   3787 O  OG    . SER A 1 487 ? -19.70935 -22.47810 -20.85554 1.000 143.70779 ? 566 SER B OG    1 
ATOM   3788 N  N     . PHE A 1 488 ? -22.60714 -20.54574 -19.03127 1.000 144.74360 ? 567 PHE B N     1 
ATOM   3789 C  CA    . PHE A 1 488 ? -24.04069 -20.76899 -19.19803 1.000 143.62001 ? 567 PHE B CA    1 
ATOM   3790 C  C     . PHE A 1 488 ? -24.67309 -19.67473 -20.04938 1.000 146.38982 ? 567 PHE B C     1 
ATOM   3791 O  O     . PHE A 1 488 ? -25.42593 -19.96071 -20.98783 1.000 145.97381 ? 567 PHE B O     1 
ATOM   3792 C  CB    . PHE A 1 488 ? -24.72246 -20.85404 -17.83253 1.000 141.53972 ? 567 PHE B CB    1 
ATOM   3793 C  CG    . PHE A 1 488 ? -25.11580 -22.24802 -17.43891 1.000 138.19786 ? 567 PHE B CG    1 
ATOM   3794 C  CD1   . PHE A 1 488 ? -24.21669 -23.08038 -16.79344 1.000 125.79291 ? 567 PHE B CD1   1 
ATOM   3795 C  CD2   . PHE A 1 488 ? -26.38617 -22.72695 -17.71682 1.000 136.96858 ? 567 PHE B CD2   1 
ATOM   3796 C  CE1   . PHE A 1 488 ? -24.57717 -24.36451 -16.43193 1.000 132.91491 ? 567 PHE B CE1   1 
ATOM   3797 C  CE2   . PHE A 1 488 ? -26.75345 -24.01006 -17.35753 1.000 124.13498 ? 567 PHE B CE2   1 
ATOM   3798 C  CZ    . PHE A 1 488 ? -25.84781 -24.82991 -16.71395 1.000 130.33456 ? 567 PHE B CZ    1 
ATOM   3799 N  N     . ILE A 1 489 ? -24.38082 -18.41058 -19.73455 1.000 149.77176 ? 568 ILE B N     1 
ATOM   3800 C  CA    . ILE A 1 489 ? -24.88243 -17.31204 -20.54917 1.000 153.02559 ? 568 ILE B CA    1 
ATOM   3801 C  C     . ILE A 1 489 ? -24.11699 -17.20734 -21.86308 1.000 155.61248 ? 568 ILE B C     1 
ATOM   3802 O  O     . ILE A 1 489 ? -24.64148 -16.66228 -22.84217 1.000 152.03822 ? 568 ILE B O     1 
ATOM   3803 C  CB    . ILE A 1 489 ? -24.82046 -15.99291 -19.75452 1.000 150.76663 ? 568 ILE B CB    1 
ATOM   3804 C  CG1   . ILE A 1 489 ? -25.38210 -16.19741 -18.34558 1.000 145.16816 ? 568 ILE B CG1   1 
ATOM   3805 C  CG2   . ILE A 1 489 ? -25.60045 -14.89449 -20.46422 1.000 156.87804 ? 568 ILE B CG2   1 
ATOM   3806 C  CD1   . ILE A 1 489 ? -25.40033 -14.93957 -17.50231 1.000 135.98826 ? 568 ILE B CD1   1 
ATOM   3807 N  N     . ILE A 1 490 ? -22.88857 -17.73095 -21.91291 1.000 154.42171 ? 569 ILE B N     1 
ATOM   3808 C  CA    . ILE A 1 490 ? -22.11770 -17.72611 -23.15534 1.000 156.33639 ? 569 ILE B CA    1 
ATOM   3809 C  C     . ILE A 1 490 ? -22.84296 -18.52430 -24.23259 1.000 156.92046 ? 569 ILE B C     1 
ATOM   3810 O  O     . ILE A 1 490 ? -22.99985 -18.06803 -25.37169 1.000 156.20244 ? 569 ILE B O     1 
ATOM   3811 C  CB    . ILE A 1 490 ? -20.69693 -18.26796 -22.90761 1.000 158.25357 ? 569 ILE B CB    1 
ATOM   3812 C  CG1   . ILE A 1 490 ? -19.81247 -17.19139 -22.27049 1.000 161.41362 ? 569 ILE B CG1   1 
ATOM   3813 C  CG2   . ILE A 1 490 ? -20.07820 -18.78015 -24.20231 1.000 157.17411 ? 569 ILE B CG2   1 
ATOM   3814 C  CD1   . ILE A 1 490 ? -18.44746 -17.69274 -21.83059 1.000 151.50798 ? 569 ILE B CD1   1 
ATOM   3815 N  N     . GLN A 1 491 ? -23.30363 -19.72793 -23.88594 1.000 153.91432 ? 570 GLN B N     1 
ATOM   3816 C  CA    . GLN A 1 491 ? -24.03618 -20.53762 -24.85286 1.000 154.92062 ? 570 GLN B CA    1 
ATOM   3817 C  C     . GLN A 1 491 ? -25.44267 -20.00172 -25.08634 1.000 150.27394 ? 570 GLN B C     1 
ATOM   3818 O  O     . GLN A 1 491 ? -25.98291 -20.14673 -26.18856 1.000 143.73049 ? 570 GLN B O     1 
ATOM   3819 C  CB    . GLN A 1 491 ? -24.09494 -21.99159 -24.38517 1.000 155.39834 ? 570 GLN B CB    1 
ATOM   3820 C  CG    . GLN A 1 491 ? -23.43985 -22.97306 -25.34066 1.000 157.71950 ? 570 GLN B CG    1 
ATOM   3821 C  CD    . GLN A 1 491 ? -21.95495 -22.71691 -25.50898 1.000 156.02262 ? 570 GLN B CD    1 
ATOM   3822 O  OE1   . GLN A 1 491 ? -21.24254 -22.46243 -24.53761 1.000 152.08233 ? 570 GLN B OE1   1 
ATOM   3823 N  NE2   . GLN A 1 491 ? -21.48128 -22.77686 -26.74795 1.000 153.46326 ? 570 GLN B NE2   1 
ATOM   3824 N  N     . PHE A 1 492 ? -26.04468 -19.37684 -24.07101 1.000 148.86258 ? 571 PHE B N     1 
ATOM   3825 C  CA    . PHE A 1 492 ? -27.41743 -18.89744 -24.20103 1.000 151.51239 ? 571 PHE B CA    1 
ATOM   3826 C  C     . PHE A 1 492 ? -27.52185 -17.76925 -25.21943 1.000 154.25776 ? 571 PHE B C     1 
ATOM   3827 O  O     . PHE A 1 492 ? -28.50750 -17.68643 -25.96157 1.000 153.87190 ? 571 PHE B O     1 
ATOM   3828 C  CB    . PHE A 1 492 ? -27.94419 -18.44427 -22.83887 1.000 154.88321 ? 571 PHE B CB    1 
ATOM   3829 C  CG    . PHE A 1 492 ? -29.30538 -17.80634 -22.89344 1.000 160.29551 ? 571 PHE B CG    1 
ATOM   3830 C  CD1   . PHE A 1 492 ? -30.40505 -18.52290 -23.33728 1.000 158.35257 ? 571 PHE B CD1   1 
ATOM   3831 C  CD2   . PHE A 1 492 ? -29.48761 -16.49418 -22.48727 1.000 158.84711 ? 571 PHE B CD2   1 
ATOM   3832 C  CE1   . PHE A 1 492 ? -31.65885 -17.93967 -23.38543 1.000 151.95932 ? 571 PHE B CE1   1 
ATOM   3833 C  CE2   . PHE A 1 492 ? -30.73972 -15.90644 -22.53146 1.000 156.20476 ? 571 PHE B CE2   1 
ATOM   3834 C  CZ    . PHE A 1 492 ? -31.82594 -16.63055 -22.98080 1.000 148.47225 ? 571 PHE B CZ    1 
ATOM   3835 N  N     . LEU A 1 493 ? -26.51735 -16.89165 -25.27279 1.000 161.88809 ? 572 LEU B N     1 
ATOM   3836 C  CA    . LEU A 1 493 ? -26.56374 -15.78413 -26.22138 1.000 167.46791 ? 572 LEU B CA    1 
ATOM   3837 C  C     . LEU A 1 493 ? -26.32793 -16.25544 -27.65083 1.000 167.79667 ? 572 LEU B C     1 
ATOM   3838 O  O     . LEU A 1 493 ? -26.78050 -15.60275 -28.59854 1.000 162.17594 ? 572 LEU B O     1 
ATOM   3839 C  CB    . LEU A 1 493 ? -25.54104 -14.71560 -25.83474 1.000 156.37247 ? 572 LEU B CB    1 
ATOM   3840 C  CG    . LEU A 1 493 ? -25.77554 -14.01223 -24.49552 1.000 153.14164 ? 572 LEU B CG    1 
ATOM   3841 C  CD1   . LEU A 1 493 ? -24.71732 -12.94797 -24.25409 1.000 153.21784 ? 572 LEU B CD1   1 
ATOM   3842 C  CD2   . LEU A 1 493 ? -27.16897 -13.40704 -24.43821 1.000 147.55486 ? 572 LEU B CD2   1 
ATOM   3843 N  N     . LYS A 1 494 ? -25.62911 -17.37976 -27.82813 1.000 151.91994 ? 573 LYS B N     1 
ATOM   3844 C  CA    . LYS A 1 494 ? -25.41163 -17.90688 -29.17103 1.000 146.43230 ? 573 LYS B CA    1 
ATOM   3845 C  C     . LYS A 1 494 ? -26.70731 -18.40581 -29.79742 1.000 155.17594 ? 573 LYS B C     1 
ATOM   3846 O  O     . LYS A 1 494 ? -26.85586 -18.36674 -31.02469 1.000 151.78771 ? 573 LYS B O     1 
ATOM   3847 C  CB    . LYS A 1 494 ? -24.37888 -19.03325 -29.13592 1.000 129.75210 ? 573 LYS B CB    1 
ATOM   3848 C  CG    . LYS A 1 494 ? -22.98793 -18.59729 -28.71751 1.000 128.32903 ? 573 LYS B CG    1 
ATOM   3849 C  CD    . LYS A 1 494 ? -22.02125 -19.76828 -28.75607 1.000 131.49093 ? 573 LYS B CD    1 
ATOM   3850 C  CE    . LYS A 1 494 ? -20.61545 -19.34550 -28.36614 1.000 121.47882 ? 573 LYS B CE    1 
ATOM   3851 N  NZ    . LYS A 1 494 ? -19.67124 -20.49701 -28.38450 1.000 119.72881 ? 573 LYS B NZ    1 
ATOM   3852 N  N     . MET A 1 495 ? -27.65041 -18.87420 -28.97768 1.000 157.17692 ? 574 MET B N     1 
ATOM   3853 C  CA    . MET A 1 495 ? -28.89506 -19.42326 -29.50562 1.000 152.64395 ? 574 MET B CA    1 
ATOM   3854 C  C     . MET A 1 495 ? -29.72940 -18.33940 -30.17746 1.000 154.00111 ? 574 MET B C     1 
ATOM   3855 O  O     . MET A 1 495 ? -30.04826 -18.43052 -31.36860 1.000 160.90955 ? 574 MET B O     1 
ATOM   3856 C  CB    . MET A 1 495 ? -29.68607 -20.09830 -28.38281 1.000 150.56971 ? 574 MET B CB    1 
ATOM   3857 C  CG    . MET A 1 495 ? -28.84723 -20.98404 -27.47198 1.000 154.54381 ? 574 MET B CG    1 
ATOM   3858 S  SD    . MET A 1 495 ? -27.91648 -22.24816 -28.36012 1.000 166.01248 ? 574 MET B SD    1 
ATOM   3859 C  CE    . MET A 1 495 ? -27.06577 -23.06672 -27.01089 1.000 142.02470 ? 574 MET B CE    1 
ATOM   3860 N  N     . GLN A 1 496 ? -30.08807 -17.29959 -29.42739 1.000 152.41062 ? 575 GLN B N     1 
ATOM   3861 C  CA    . GLN A 1 496 ? -30.91864 -16.21294 -29.94482 1.000 160.73408 ? 575 GLN B CA    1 
ATOM   3862 C  C     . GLN A 1 496 ? -30.01840 -15.20843 -30.65399 1.000 158.69710 ? 575 GLN B C     1 
ATOM   3863 O  O     . GLN A 1 496 ? -29.57147 -14.21694 -30.07467 1.000 156.73286 ? 575 GLN B O     1 
ATOM   3864 C  CB    . GLN A 1 496 ? -31.71376 -15.56167 -28.81955 1.000 160.55891 ? 575 GLN B CB    1 
ATOM   3865 C  CG    . GLN A 1 496 ? -32.57040 -16.53553 -28.02210 1.000 166.04722 ? 575 GLN B CG    1 
ATOM   3866 C  CD    . GLN A 1 496 ? -33.64568 -17.19625 -28.86362 1.000 176.42525 ? 575 GLN B CD    1 
ATOM   3867 O  OE1   . GLN A 1 496 ? -34.13070 -16.62023 -29.83746 1.000 179.75447 ? 575 GLN B OE1   1 
ATOM   3868 N  NE2   . GLN A 1 496 ? -34.02172 -18.41473 -28.49236 1.000 173.44464 ? 575 GLN B NE2   1 
ATOM   3869 N  N     . GLY A 1 497 ? -29.75258 -15.46927 -31.93044 1.000 151.67922 ? 576 GLY B N     1 
ATOM   3870 C  CA    . GLY A 1 497 ? -28.91364 -14.59545 -32.72947 1.000 136.21185 ? 576 GLY B CA    1 
ATOM   3871 C  C     . GLY A 1 497 ? -28.59435 -15.14774 -34.10501 1.000 120.58271 ? 576 GLY B C     1 
ATOM   3872 O  O     . GLY A 1 497 ? -27.58486 -15.82705 -34.29306 1.000 119.32329 ? 576 GLY B O     1 
ATOM   3873 N  N     . MET B 2 1   ? 14.38164  -38.61922 -15.40611 1.000 69.80309  ? 1   MET A N     1 
ATOM   3874 C  CA    . MET B 2 1   ? 14.24280  -37.93838 -16.68871 1.000 76.57265  ? 1   MET A CA    1 
ATOM   3875 C  C     . MET B 2 1   ? 15.54277  -37.24874 -17.09751 1.000 76.52193  ? 1   MET A C     1 
ATOM   3876 O  O     . MET B 2 1   ? 16.48196  -37.14130 -16.30636 1.000 62.55953  ? 1   MET A O     1 
ATOM   3877 C  CB    . MET B 2 1   ? 13.10493  -36.91466 -16.63876 1.000 62.45831  ? 1   MET A CB    1 
ATOM   3878 C  CG    . MET B 2 1   ? 13.37809  -35.72045 -15.74032 1.000 64.55824  ? 1   MET A CG    1 
ATOM   3879 S  SD    . MET B 2 1   ? 12.11337  -34.43572 -15.86845 1.000 81.95373  ? 1   MET A SD    1 
ATOM   3880 C  CE    . MET B 2 1   ? 10.68963  -35.27930 -15.19057 1.000 77.81563  ? 1   MET A CE    1 
ATOM   3881 N  N     . THR B 2 2   ? 15.57886  -36.77612 -18.34046 1.000 76.51071  ? 2   THR A N     1 
ATOM   3882 C  CA    . THR B 2 2   ? 16.77783  -36.14990 -18.88038 1.000 67.12291  ? 2   THR A CA    1 
ATOM   3883 C  C     . THR B 2 2   ? 16.98561  -34.76639 -18.27420 1.000 67.75823  ? 2   THR A C     1 
ATOM   3884 O  O     . THR B 2 2   ? 16.02740  -34.03253 -18.01902 1.000 75.74690  ? 2   THR A O     1 
ATOM   3885 C  CB    . THR B 2 2   ? 16.67305  -36.04657 -20.40301 1.000 66.55166  ? 2   THR A CB    1 
ATOM   3886 O  OG1   . THR B 2 2   ? 16.37548  -37.33735 -20.95098 1.000 69.98781  ? 2   THR A OG1   1 
ATOM   3887 C  CG2   . THR B 2 2   ? 17.97447  -35.53614 -21.00508 1.000 69.30677  ? 2   THR A CG2   1 
ATOM   3888 N  N     . GLU B 2 3   ? 18.24922  -34.41229 -18.04246 1.000 65.97814  ? 3   GLU A N     1 
ATOM   3889 C  CA    . GLU B 2 3   ? 18.61935  -33.11105 -17.50768 1.000 65.51460  ? 3   GLU A CA    1 
ATOM   3890 C  C     . GLU B 2 3   ? 19.57061  -32.39976 -18.46169 1.000 65.20238  ? 3   GLU A C     1 
ATOM   3891 O  O     . GLU B 2 3   ? 20.28503  -33.03670 -19.24108 1.000 73.32407  ? 3   GLU A O     1 
ATOM   3892 C  CB    . GLU B 2 3   ? 19.27558  -33.24399 -16.13033 1.000 65.89412  ? 3   GLU A CB    1 
ATOM   3893 C  CG    . GLU B 2 3   ? 18.41829  -33.96299 -15.10754 1.000 75.54033  ? 3   GLU A CG    1 
ATOM   3894 C  CD    . GLU B 2 3   ? 19.05157  -33.98659 -13.73230 1.000 86.59434  ? 3   GLU A CD    1 
ATOM   3895 O  OE1   . GLU B 2 3   ? 19.99546  -33.20187 -13.49814 1.000 91.17423  ? 3   GLU A OE1   1 
ATOM   3896 O  OE2   . GLU B 2 3   ? 18.60614  -34.79076 -12.88615 1.000 94.02316  ? 3   GLU A OE2   1 
ATOM   3897 N  N     . TYR B 2 4   ? 19.57326  -31.06803 -18.39298 1.000 66.29150  ? 4   TYR A N     1 
ATOM   3898 C  CA    . TYR B 2 4   ? 20.46954  -30.23052 -19.18831 1.000 63.09477  ? 4   TYR A CA    1 
ATOM   3899 C  C     . TYR B 2 4   ? 21.07537  -29.16881 -18.27780 1.000 59.32376  ? 4   TYR A C     1 
ATOM   3900 O  O     . TYR B 2 4   ? 20.35830  -28.29679 -17.77623 1.000 60.47259  ? 4   TYR A O     1 
ATOM   3901 C  CB    . TYR B 2 4   ? 19.73100  -29.58143 -20.36090 1.000 55.22757  ? 4   TYR A CB    1 
ATOM   3902 C  CG    . TYR B 2 4   ? 19.16889  -30.56182 -21.36743 1.000 71.52168  ? 4   TYR A CG    1 
ATOM   3903 C  CD1   . TYR B 2 4   ? 19.95246  -31.04513 -22.40943 1.000 72.79820  ? 4   TYR A CD1   1 
ATOM   3904 C  CD2   . TYR B 2 4   ? 17.85138  -30.99617 -21.28358 1.000 68.32418  ? 4   TYR A CD2   1 
ATOM   3905 C  CE1   . TYR B 2 4   ? 19.44061  -31.93883 -23.33514 1.000 73.27890  ? 4   TYR A CE1   1 
ATOM   3906 C  CE2   . TYR B 2 4   ? 17.33302  -31.89133 -22.20404 1.000 65.56041  ? 4   TYR A CE2   1 
ATOM   3907 C  CZ    . TYR B 2 4   ? 18.13153  -32.35834 -23.22641 1.000 66.66424  ? 4   TYR A CZ    1 
ATOM   3908 O  OH    . TYR B 2 4   ? 17.61972  -33.24728 -24.14357 1.000 72.82934  ? 4   TYR A OH    1 
ATOM   3909 N  N     . LYS B 2 5   ? 22.39003  -29.23920 -18.06534 1.000 64.05423  ? 5   LYS A N     1 
ATOM   3910 C  CA    . LYS B 2 5   ? 23.09366  -28.28110 -17.21401 1.000 59.41294  ? 5   LYS A CA    1 
ATOM   3911 C  C     . LYS B 2 5   ? 23.41025  -27.02867 -18.02525 1.000 61.60888  ? 5   LYS A C     1 
ATOM   3912 O  O     . LYS B 2 5   ? 24.26630  -27.05619 -18.91566 1.000 65.78131  ? 5   LYS A O     1 
ATOM   3913 C  CB    . LYS B 2 5   ? 24.37018  -28.89945 -16.64941 1.000 64.45590  ? 5   LYS A CB    1 
ATOM   3914 C  CG    . LYS B 2 5   ? 24.15593  -29.99140 -15.60769 1.000 71.93507  ? 5   LYS A CG    1 
ATOM   3915 C  CD    . LYS B 2 5   ? 25.48282  -30.64620 -15.22167 1.000 85.97955  ? 5   LYS A CD    1 
ATOM   3916 C  CE    . LYS B 2 5   ? 25.38787  -31.40574 -13.90188 1.000 89.17363  ? 5   LYS A CE    1 
ATOM   3917 N  NZ    . LYS B 2 5   ? 24.38104  -32.50444 -13.92720 1.000 84.71808  ? 5   LYS A NZ    1 
ATOM   3918 N  N     . LEU B 2 6   ? 22.73423  -25.92711 -17.71258 1.000 58.84410  ? 6   LEU A N     1 
ATOM   3919 C  CA    . LEU B 2 6   ? 22.88395  -24.67521 -18.44002 1.000 59.26103  ? 6   LEU A CA    1 
ATOM   3920 C  C     . LEU B 2 6   ? 23.55639  -23.63106 -17.55750 1.000 67.49095  ? 6   LEU A C     1 
ATOM   3921 O  O     . LEU B 2 6   ? 23.28714  -23.55419 -16.35388 1.000 68.20281  ? 6   LEU A O     1 
ATOM   3922 C  CB    . LEU B 2 6   ? 21.52470  -24.15726 -18.91615 1.000 59.71069  ? 6   LEU A CB    1 
ATOM   3923 C  CG    . LEU B 2 6   ? 20.63695  -25.15897 -19.65902 1.000 63.21431  ? 6   LEU A CG    1 
ATOM   3924 C  CD1   . LEU B 2 6   ? 19.32936  -24.50733 -20.06944 1.000 54.17660  ? 6   LEU A CD1   1 
ATOM   3925 C  CD2   . LEU B 2 6   ? 21.35751  -25.73102 -20.87068 1.000 59.61076  ? 6   LEU A CD2   1 
ATOM   3926 N  N     . VAL B 2 7   ? 24.43267  -22.82951 -18.16170 1.000 59.01425  ? 7   VAL A N     1 
ATOM   3927 C  CA    . VAL B 2 7   ? 25.14475  -21.76059 -17.47033 1.000 62.03007  ? 7   VAL A CA    1 
ATOM   3928 C  C     . VAL B 2 7   ? 24.93586  -20.46895 -18.24819 1.000 58.75648  ? 7   VAL A C     1 
ATOM   3929 O  O     . VAL B 2 7   ? 25.07352  -20.45245 -19.47623 1.000 59.34654  ? 7   VAL A O     1 
ATOM   3930 C  CB    . VAL B 2 7   ? 26.64824  -22.07131 -17.32769 1.000 65.06940  ? 7   VAL A CB    1 
ATOM   3931 C  CG1   . VAL B 2 7   ? 27.37151  -20.92141 -16.64192 1.000 55.32765  ? 7   VAL A CG1   1 
ATOM   3932 C  CG2   . VAL B 2 7   ? 26.85221  -23.36239 -16.55712 1.000 57.00459  ? 7   VAL A CG2   1 
ATOM   3933 N  N     . VAL B 2 8   ? 24.60217  -19.39311 -17.53918 1.000 52.21870  ? 8   VAL A N     1 
ATOM   3934 C  CA    . VAL B 2 8   ? 24.35556  -18.08877 -18.14599 1.000 55.68639  ? 8   VAL A CA    1 
ATOM   3935 C  C     . VAL B 2 8   ? 25.53330  -17.18553 -17.80402 1.000 62.86481  ? 8   VAL A C     1 
ATOM   3936 O  O     . VAL B 2 8   ? 25.72003  -16.80855 -16.64026 1.000 61.66073  ? 8   VAL A O     1 
ATOM   3937 C  CB    . VAL B 2 8   ? 23.03467  -17.47204 -17.66760 1.000 52.23765  ? 8   VAL A CB    1 
ATOM   3938 C  CG1   . VAL B 2 8   ? 22.69847  -16.25632 -18.50466 1.000 62.63631  ? 8   VAL A CG1   1 
ATOM   3939 C  CG2   . VAL B 2 8   ? 21.90640  -18.49348 -17.72334 1.000 52.30616  ? 8   VAL A CG2   1 
ATOM   3940 N  N     . VAL B 2 9   ? 26.32393  -16.82644 -18.81512 1.000 61.28768  ? 9   VAL A N     1 
ATOM   3941 C  CA    . VAL B 2 9   ? 27.48425  -15.96679 -18.63017 1.000 67.84042  ? 9   VAL A CA    1 
ATOM   3942 C  C     . VAL B 2 9   ? 27.29421  -14.68877 -19.43857 1.000 67.53668  ? 9   VAL A C     1 
ATOM   3943 O  O     . VAL B 2 9   ? 26.55209  -14.64332 -20.42360 1.000 65.90500  ? 9   VAL A O     1 
ATOM   3944 C  CB    . VAL B 2 9   ? 28.80281  -16.66660 -19.02355 1.000 56.36685  ? 9   VAL A CB    1 
ATOM   3945 C  CG1   . VAL B 2 9   ? 28.95516  -17.96767 -18.26055 1.000 59.70024  ? 9   VAL A CG1   1 
ATOM   3946 C  CG2   . VAL B 2 9   ? 28.85379  -16.91086 -20.52539 1.000 57.32885  ? 9   VAL A CG2   1 
ATOM   3947 N  N     . GLY B 2 10  ? 27.97732  -13.64599 -19.00418 1.000 68.71737  ? 10  GLY A N     1 
ATOM   3948 C  CA    . GLY B 2 10  ? 27.91227  -12.34669 -19.64296 1.000 61.07592  ? 10  GLY A CA    1 
ATOM   3949 C  C     . GLY B 2 10  ? 28.24815  -11.25011 -18.65733 1.000 63.48511  ? 10  GLY A C     1 
ATOM   3950 O  O     . GLY B 2 10  ? 28.26583  -11.44656 -17.44433 1.000 64.99824  ? 10  GLY A O     1 
ATOM   3951 N  N     . ALA B 2 11  ? 28.51699  -10.06287 -19.20060 1.000 66.20750  ? 11  ALA A N     1 
ATOM   3952 C  CA    . ALA B 2 11  ? 28.88528  -8.91755  -18.38193 1.000 57.83732  ? 11  ALA A CA    1 
ATOM   3953 C  C     . ALA B 2 11  ? 27.77484  -8.57862  -17.39003 1.000 67.60044  ? 11  ALA A C     1 
ATOM   3954 O  O     . ALA B 2 11  ? 26.63355  -9.03302  -17.50980 1.000 65.91579  ? 11  ALA A O     1 
ATOM   3955 C  CB    . ALA B 2 11  ? 29.18867  -7.70690  -19.26182 1.000 59.11959  ? 11  ALA A CB    1 
ATOM   3956 N  N     . GLY B 2 12  ? 28.12793  -7.77453  -16.39025 1.000 64.55501  ? 12  GLY A N     1 
ATOM   3957 C  CA    . GLY B 2 12  ? 27.15884  -7.39838  -15.37638 1.000 51.40553  ? 12  GLY A CA    1 
ATOM   3958 C  C     . GLY B 2 12  ? 26.13721  -6.41785  -15.92239 1.000 54.60953  ? 12  GLY A C     1 
ATOM   3959 O  O     . GLY B 2 12  ? 26.47300  -5.45937  -16.61902 1.000 63.62851  ? 12  GLY A O     1 
ATOM   3960 N  N     . GLY B 2 13  ? 24.87088  -6.66913  -15.59930 1.000 61.72986  ? 13  GLY A N     1 
ATOM   3961 C  CA    . GLY B 2 13  ? 23.78736  -5.79023  -15.98974 1.000 61.56271  ? 13  GLY A CA    1 
ATOM   3962 C  C     . GLY B 2 13  ? 23.17242  -6.06100  -17.34522 1.000 62.53760  ? 13  GLY A C     1 
ATOM   3963 O  O     . GLY B 2 13  ? 22.32028  -5.27901  -17.78498 1.000 67.03934  ? 13  GLY A O     1 
ATOM   3964 N  N     . VAL B 2 14  ? 23.56713  -7.14135  -18.02227 1.000 64.43420  ? 14  VAL A N     1 
ATOM   3965 C  CA    . VAL B 2 14  ? 23.02905  -7.41512  -19.35085 1.000 63.93453  ? 14  VAL A CA    1 
ATOM   3966 C  C     . VAL B 2 14  ? 21.65088  -8.05792  -19.29309 1.000 63.77870  ? 14  VAL A C     1 
ATOM   3967 O  O     . VAL B 2 14  ? 20.89709  -7.97538  -20.27073 1.000 67.73809  ? 14  VAL A O     1 
ATOM   3968 C  CB    . VAL B 2 14  ? 23.98485  -8.30696  -20.16139 1.000 65.72898  ? 14  VAL A CB    1 
ATOM   3969 C  CG1   . VAL B 2 14  ? 25.34750  -7.63974  -20.29804 1.000 64.51955  ? 14  VAL A CG1   1 
ATOM   3970 C  CG2   . VAL B 2 14  ? 24.11436  -9.67421  -19.51261 1.000 57.30995  ? 14  VAL A CG2   1 
ATOM   3971 N  N     . GLY B 2 15  ? 21.29783  -8.69622  -18.18144 1.000 62.76283  ? 15  GLY A N     1 
ATOM   3972 C  CA    . GLY B 2 15  ? 19.97829  -9.27646  -18.04686 1.000 62.88367  ? 15  GLY A CA    1 
ATOM   3973 C  C     . GLY B 2 15  ? 19.97705  -10.77421 -17.82479 1.000 63.35758  ? 15  GLY A C     1 
ATOM   3974 O  O     . GLY B 2 15  ? 18.95284  -11.42935 -18.03696 1.000 64.62135  ? 15  GLY A O     1 
ATOM   3975 N  N     . LYS B 2 16  ? 21.11231  -11.32519 -17.38357 1.000 56.12809  ? 16  LYS A N     1 
ATOM   3976 C  CA    . LYS B 2 16  ? 21.21053  -12.76826 -17.17762 1.000 49.19144  ? 16  LYS A CA    1 
ATOM   3977 C  C     . LYS B 2 16  ? 20.21818  -13.25419 -16.12819 1.000 55.17826  ? 16  LYS A C     1 
ATOM   3978 O  O     . LYS B 2 16  ? 19.62767  -14.33093 -16.27298 1.000 56.05157  ? 16  LYS A O     1 
ATOM   3979 C  CB    . LYS B 2 16  ? 22.63290  -13.14686 -16.76916 1.000 58.71430  ? 16  LYS A CB    1 
ATOM   3980 C  CG    . LYS B 2 16  ? 23.69664  -12.82705 -17.80014 1.000 51.23769  ? 16  LYS A CG    1 
ATOM   3981 C  CD    . LYS B 2 16  ? 25.05103  -13.33011 -17.34296 1.000 60.57892  ? 16  LYS A CD    1 
ATOM   3982 C  CE    . LYS B 2 16  ? 25.43101  -12.75604 -15.98581 1.000 58.34078  ? 16  LYS A CE    1 
ATOM   3983 N  NZ    . LYS B 2 16  ? 25.59700  -11.27745 -16.03199 1.000 59.17792  ? 16  LYS A NZ    1 
ATOM   3984 N  N     . SER B 2 17  ? 20.02913  -12.48213 -15.05740 1.000 58.75172  ? 17  SER A N     1 
ATOM   3985 C  CA    . SER B 2 17  ? 19.08617  -12.88319 -14.01966 1.000 57.51191  ? 17  SER A CA    1 
ATOM   3986 C  C     . SER B 2 17  ? 17.64463  -12.64643 -14.45361 1.000 65.08670  ? 17  SER A C     1 
ATOM   3987 O  O     . SER B 2 17  ? 16.75290  -13.43535 -14.11775 1.000 56.89614  ? 17  SER A O     1 
ATOM   3988 C  CB    . SER B 2 17  ? 19.38229  -12.13167 -12.72133 1.000 63.40042  ? 17  SER A CB    1 
ATOM   3989 O  OG    . SER B 2 17  ? 20.70419  -12.38242 -12.27368 1.000 64.56283  ? 17  SER A OG    1 
ATOM   3990 N  N     . ALA B 2 18  ? 17.39791  -11.56699 -15.19825 1.000 64.87354  ? 18  ALA A N     1 
ATOM   3991 C  CA    . ALA B 2 18  ? 16.04547  -11.29535 -15.67035 1.000 57.55758  ? 18  ALA A CA    1 
ATOM   3992 C  C     . ALA B 2 18  ? 15.60195  -12.33104 -16.69588 1.000 62.99174  ? 18  ALA A C     1 
ATOM   3993 O  O     . ALA B 2 18  ? 14.42770  -12.71307 -16.72864 1.000 66.59463  ? 18  ALA A O     1 
ATOM   3994 C  CB    . ALA B 2 18  ? 15.96634  -9.88500  -16.25189 1.000 59.87870  ? 18  ALA A CB    1 
ATOM   3995 N  N     . LEU B 2 19  ? 16.52663  -12.79948 -17.53892 1.000 58.57595  ? 19  LEU A N     1 
ATOM   3996 C  CA    . LEU B 2 19  ? 16.18844  -13.83987 -18.50576 1.000 58.08205  ? 19  LEU A CA    1 
ATOM   3997 C  C     . LEU B 2 19  ? 15.86210  -15.15250 -17.80795 1.000 62.71136  ? 19  LEU A C     1 
ATOM   3998 O  O     . LEU B 2 19  ? 14.88595  -15.82662 -18.16066 1.000 62.91843  ? 19  LEU A O     1 
ATOM   3999 C  CB    . LEU B 2 19  ? 17.33892  -14.03779 -19.49070 1.000 49.87609  ? 19  LEU A CB    1 
ATOM   4000 C  CG    . LEU B 2 19  ? 17.63324  -12.90378 -20.47095 1.000 57.95733  ? 19  LEU A CG    1 
ATOM   4001 C  CD1   . LEU B 2 19  ? 18.94886  -13.15715 -21.17809 1.000 55.76374  ? 19  LEU A CD1   1 
ATOM   4002 C  CD2   . LEU B 2 19  ? 16.50072  -12.74240 -21.47812 1.000 64.74007  ? 19  LEU A CD2   1 
ATOM   4003 N  N     . THR B 2 20  ? 16.67180  -15.53123 -16.81740 1.000 53.50862  ? 20  THR A N     1 
ATOM   4004 C  CA    . THR B 2 20  ? 16.44488  -16.78577 -16.11023 1.000 54.88016  ? 20  THR A CA    1 
ATOM   4005 C  C     . THR B 2 20  ? 15.11705  -16.75778 -15.36738 1.000 59.97626  ? 20  THR A C     1 
ATOM   4006 O  O     . THR B 2 20  ? 14.29429  -17.67085 -15.50638 1.000 65.43814  ? 20  THR A O     1 
ATOM   4007 C  CB    . THR B 2 20  ? 17.59925  -17.05773 -15.14379 1.000 52.61685  ? 20  THR A CB    1 
ATOM   4008 O  OG1   . THR B 2 20  ? 18.82166  -17.18187 -15.88019 1.000 57.81340  ? 20  THR A OG1   1 
ATOM   4009 C  CG2   . THR B 2 20  ? 17.35436  -18.33375 -14.35746 1.000 53.01600  ? 20  THR A CG2   1 
ATOM   4010 N  N     . ILE B 2 21  ? 14.88592  -15.70421 -14.58045 1.000 53.41011  ? 21  ILE A N     1 
ATOM   4011 C  CA    . ILE B 2 21  ? 13.65987  -15.62060 -13.79509 1.000 61.16183  ? 21  ILE A CA    1 
ATOM   4012 C  C     . ILE B 2 21  ? 12.44220  -15.50402 -14.70386 1.000 61.69749  ? 21  ILE A C     1 
ATOM   4013 O  O     . ILE B 2 21  ? 11.37296  -16.04127 -14.39020 1.000 60.80850  ? 21  ILE A O     1 
ATOM   4014 C  CB    . ILE B 2 21  ? 13.76081  -14.45223 -12.79690 1.000 56.72236  ? 21  ILE A CB    1 
ATOM   4015 C  CG1   . ILE B 2 21  ? 14.87969  -14.72452 -11.79004 1.000 53.39420  ? 21  ILE A CG1   1 
ATOM   4016 C  CG2   . ILE B 2 21  ? 12.44723  -14.23848 -12.06997 1.000 58.10793  ? 21  ILE A CG2   1 
ATOM   4017 C  CD1   . ILE B 2 21  ? 15.10738  -13.60065 -10.80326 1.000 80.17902  ? 21  ILE A CD1   1 
ATOM   4018 N  N     . GLN B 2 22  ? 12.58130  -14.82862 -15.84803 1.000 63.10008  ? 22  GLN A N     1 
ATOM   4019 C  CA    . GLN B 2 22  ? 11.48272  -14.77047 -16.80869 1.000 65.32125  ? 22  GLN A CA    1 
ATOM   4020 C  C     . GLN B 2 22  ? 11.10428  -16.16335 -17.29759 1.000 64.20833  ? 22  GLN A C     1 
ATOM   4021 O  O     . GLN B 2 22  ? 9.91786   -16.49473 -17.39367 1.000 70.48736  ? 22  GLN A O     1 
ATOM   4022 C  CB    . GLN B 2 22  ? 11.86130  -13.87333 -17.98728 1.000 58.79196  ? 22  GLN A CB    1 
ATOM   4023 C  CG    . GLN B 2 22  ? 10.78764  -13.74774 -19.05083 1.000 73.29752  ? 22  GLN A CG    1 
ATOM   4024 C  CD    . GLN B 2 22  ? 9.52507   -13.07969 -18.53753 1.000 70.96799  ? 22  GLN A CD    1 
ATOM   4025 O  OE1   . GLN B 2 22  ? 8.46089   -13.69642 -18.48902 1.000 76.39482  ? 22  GLN A OE1   1 
ATOM   4026 N  NE2   . GLN B 2 22  ? 9.63543   -11.81017 -18.16089 1.000 56.20800  ? 22  GLN A NE2   1 
ATOM   4027 N  N     . LEU B 2 23  ? 12.09976  -16.99676 -17.60398 1.000 66.28691  ? 23  LEU A N     1 
ATOM   4028 C  CA    . LEU B 2 23  ? 11.81311  -18.35698 -18.04701 1.000 61.59483  ? 23  LEU A CA    1 
ATOM   4029 C  C     . LEU B 2 23  ? 11.32084  -19.22300 -16.89473 1.000 64.09969  ? 23  LEU A C     1 
ATOM   4030 O  O     . LEU B 2 23  ? 10.44824  -20.07942 -17.08034 1.000 71.95618  ? 23  LEU A O     1 
ATOM   4031 C  CB    . LEU B 2 23  ? 13.06109  -18.97360 -18.67777 1.000 65.37831  ? 23  LEU A CB    1 
ATOM   4032 C  CG    . LEU B 2 23  ? 12.97759  -20.46724 -18.99725 1.000 61.53622  ? 23  LEU A CG    1 
ATOM   4033 C  CD1   . LEU B 2 23  ? 12.21200  -20.70180 -20.28742 1.000 65.09759  ? 23  LEU A CD1   1 
ATOM   4034 C  CD2   . LEU B 2 23  ? 14.36243  -21.08415 -19.06169 1.000 70.86313  ? 23  LEU A CD2   1 
ATOM   4035 N  N     . ILE B 2 24  ? 11.85982  -19.00646 -15.69848 1.000 66.26486  ? 24  ILE A N     1 
ATOM   4036 C  CA    . ILE B 2 24  ? 11.59272  -19.89617 -14.57499 1.000 64.90152  ? 24  ILE A CA    1 
ATOM   4037 C  C     . ILE B 2 24  ? 10.32821  -19.50422 -13.80808 1.000 63.75845  ? 24  ILE A C     1 
ATOM   4038 O  O     . ILE B 2 24  ? 9.61624   -20.38072 -13.30508 1.000 67.47897  ? 24  ILE A O     1 
ATOM   4039 C  CB    . ILE B 2 24  ? 12.83482  -19.93772 -13.65935 1.000 63.61513  ? 24  ILE A CB    1 
ATOM   4040 C  CG1   . ILE B 2 24  ? 13.64908  -21.20449 -13.92418 1.000 62.06122  ? 24  ILE A CG1   1 
ATOM   4041 C  CG2   . ILE B 2 24  ? 12.46841  -19.84660 -12.18622 1.000 61.84921  ? 24  ILE A CG2   1 
ATOM   4042 C  CD1   . ILE B 2 24  ? 14.02681  -21.39729 -15.37232 1.000 72.65890  ? 24  ILE A CD1   1 
ATOM   4043 N  N     . GLN B 2 25  ? 10.01369  -18.20819 -13.72912 1.000 65.29245  ? 25  GLN A N     1 
ATOM   4044 C  CA    . GLN B 2 25  ? 8.88457   -17.73720 -12.93880 1.000 72.38202  ? 25  GLN A CA    1 
ATOM   4045 C  C     . GLN B 2 25  ? 7.90650   -16.85959 -13.71053 1.000 70.18000  ? 25  GLN A C     1 
ATOM   4046 O  O     . GLN B 2 25  ? 6.94521   -16.36664 -13.10984 1.000 72.43638  ? 25  GLN A O     1 
ATOM   4047 C  CB    . GLN B 2 25  ? 9.38251   -16.97148 -11.70235 1.000 65.35483  ? 25  GLN A CB    1 
ATOM   4048 C  CG    . GLN B 2 25  ? 9.96926   -17.86176 -10.62217 1.000 56.28162  ? 25  GLN A CG    1 
ATOM   4049 C  CD    . GLN B 2 25  ? 10.76820  -17.08643 -9.59375  1.000 66.09971  ? 25  GLN A CD    1 
ATOM   4050 O  OE1   . GLN B 2 25  ? 10.78138  -15.85572 -9.59878  1.000 70.27398  ? 25  GLN A OE1   1 
ATOM   4051 N  NE2   . GLN B 2 25  ? 11.44723  -17.80575 -8.70786  1.000 63.39009  ? 25  GLN A NE2   1 
ATOM   4052 N  N     . ASN B 2 26  ? 8.13011   -16.63617 -15.00741 1.000 68.91538  ? 26  ASN A N     1 
ATOM   4053 C  CA    . ASN B 2 26  ? 7.16093   -15.97338 -15.88468 1.000 71.39242  ? 26  ASN A CA    1 
ATOM   4054 C  C     . ASN B 2 26  ? 6.81996   -14.56249 -15.40280 1.000 66.31969  ? 26  ASN A C     1 
ATOM   4055 O  O     . ASN B 2 26  ? 5.65371   -14.16915 -15.34125 1.000 70.03427  ? 26  ASN A O     1 
ATOM   4056 C  CB    . ASN B 2 26  ? 5.89359   -16.81954 -16.03107 1.000 66.13572  ? 26  ASN A CB    1 
ATOM   4057 C  CG    . ASN B 2 26  ? 6.16778   -18.17823 -16.64371 1.000 77.73056  ? 26  ASN A CG    1 
ATOM   4058 O  OD1   . ASN B 2 26  ? 6.19354   -18.32688 -17.86724 1.000 90.66688  ? 26  ASN A OD1   1 
ATOM   4059 N  ND2   . ASN B 2 26  ? 6.37108   -19.18047 -15.79530 1.000 73.90265  ? 26  ASN A ND2   1 
ATOM   4060 N  N     . HIS B 2 27  ? 7.85328   -13.79493 -15.06376 1.000 69.74180  ? 27  HIS A N     1 
ATOM   4061 C  CA    . HIS B 2 27  ? 7.67243   -12.39671 -14.69495 1.000 70.70190  ? 27  HIS A CA    1 
ATOM   4062 C  C     . HIS B 2 27  ? 9.01508   -11.68749 -14.78945 1.000 65.30105  ? 27  HIS A C     1 
ATOM   4063 O  O     . HIS B 2 27  ? 10.07494  -12.30429 -14.65790 1.000 68.44514  ? 27  HIS A O     1 
ATOM   4064 C  CB    . HIS B 2 27  ? 7.07661   -12.24917 -13.29028 1.000 64.70478  ? 27  HIS A CB    1 
ATOM   4065 C  CG    . HIS B 2 27  ? 8.03117   -12.58281 -12.18779 1.000 75.93817  ? 27  HIS A CG    1 
ATOM   4066 N  ND1   . HIS B 2 27  ? 8.92771   -11.66871 -11.67738 1.000 81.65747  ? 27  HIS A ND1   1 
ATOM   4067 C  CD2   . HIS B 2 27  ? 8.22651   -13.72902 -11.49418 1.000 74.40163  ? 27  HIS A CD2   1 
ATOM   4068 C  CE1   . HIS B 2 27  ? 9.63575   -12.23803 -10.71815 1.000 80.44861  ? 27  HIS A CE1   1 
ATOM   4069 N  NE2   . HIS B 2 27  ? 9.22958   -13.48819 -10.58673 1.000 78.10194  ? 27  HIS A NE2   1 
ATOM   4070 N  N     . PHE B 2 28  ? 8.95303   -10.37872 -15.01413 1.000 61.06776  ? 28  PHE A N     1 
ATOM   4071 C  CA    . PHE B 2 28  ? 10.13610  -9.56115  -15.24792 1.000 69.13767  ? 28  PHE A CA    1 
ATOM   4072 C  C     . PHE B 2 28  ? 10.56380  -8.88586  -13.95069 1.000 81.06218  ? 28  PHE A C     1 
ATOM   4073 O  O     . PHE B 2 28  ? 9.77302   -8.16689  -13.32901 1.000 73.05076  ? 28  PHE A O     1 
ATOM   4074 C  CB    . PHE B 2 28  ? 9.86297   -8.51899  -16.33107 1.000 66.08672  ? 28  PHE A CB    1 
ATOM   4075 C  CG    . PHE B 2 28  ? 10.93181  -7.47248  -16.45142 1.000 71.80955  ? 28  PHE A CG    1 
ATOM   4076 C  CD1   . PHE B 2 28  ? 12.22295  -7.81843  -16.81311 1.000 74.86627  ? 28  PHE A CD1   1 
ATOM   4077 C  CD2   . PHE B 2 28  ? 10.64162  -6.13919  -16.21749 1.000 74.61844  ? 28  PHE A CD2   1 
ATOM   4078 C  CE1   . PHE B 2 28  ? 13.20733  -6.85480  -16.92924 1.000 72.95599  ? 28  PHE A CE1   1 
ATOM   4079 C  CE2   . PHE B 2 28  ? 11.62068  -5.17101  -16.33384 1.000 72.51855  ? 28  PHE A CE2   1 
ATOM   4080 C  CZ    . PHE B 2 28  ? 12.90540  -5.52969  -16.68873 1.000 71.74236  ? 28  PHE A CZ    1 
ATOM   4081 N  N     . VAL B 2 29  ? 11.81053  -9.11751  -13.54802 1.000 79.84209  ? 29  VAL A N     1 
ATOM   4082 C  CA    . VAL B 2 29  ? 12.37534  -8.44350  -12.38393 1.000 81.95795  ? 29  VAL A CA    1 
ATOM   4083 C  C     . VAL B 2 29  ? 12.84872  -7.05874  -12.81162 1.000 82.56325  ? 29  VAL A C     1 
ATOM   4084 O  O     . VAL B 2 29  ? 13.67611  -6.92129  -13.71913 1.000 73.48167  ? 29  VAL A O     1 
ATOM   4085 C  CB    . VAL B 2 29  ? 13.51560  -9.26304  -11.75850 1.000 75.23496  ? 29  VAL A CB    1 
ATOM   4086 C  CG1   . VAL B 2 29  ? 12.95835  -10.49558 -11.06743 1.000 75.53092  ? 29  VAL A CG1   1 
ATOM   4087 C  CG2   . VAL B 2 29  ? 14.53261  -9.67604  -12.80667 1.000 79.78266  ? 29  VAL A CG2   1 
ATOM   4088 N  N     . ASP B 2 30  ? 12.30641  -6.02553  -12.17098 1.000 88.64964  ? 30  ASP A N     1 
ATOM   4089 C  CA    . ASP B 2 30  ? 12.63787  -4.65587  -12.53766 1.000 76.42559  ? 30  ASP A CA    1 
ATOM   4090 C  C     . ASP B 2 30  ? 13.87509  -4.14835  -11.80788 1.000 75.57125  ? 30  ASP A C     1 
ATOM   4091 O  O     . ASP B 2 30  ? 14.67990  -3.41754  -12.39519 1.000 77.08137  ? 30  ASP A O     1 
ATOM   4092 C  CB    . ASP B 2 30  ? 11.44448  -3.73854  -12.25896 1.000 79.54383  ? 30  ASP A CB    1 
ATOM   4093 C  CG    . ASP B 2 30  ? 11.49179  -2.45750  -13.06868 1.000 99.65079  ? 30  ASP A CG    1 
ATOM   4094 O  OD1   . ASP B 2 30  ? 12.52271  -1.75419  -13.02248 1.000 99.05737  ? 30  ASP A OD1   1 
ATOM   4095 O  OD2   . ASP B 2 30  ? 10.49795  -2.15839  -13.76400 1.000 115.22045 ? 30  ASP A OD2   1 
ATOM   4096 N  N     . GLU B 2 31  ? 14.04692  -4.52656  -10.54278 1.000 82.64511  ? 31  GLU A N     1 
ATOM   4097 C  CA    . GLU B 2 31  ? 15.19721  -4.08225  -9.76910  1.000 87.89350  ? 31  GLU A CA    1 
ATOM   4098 C  C     . GLU B 2 31  ? 16.47551  -4.75189  -10.26632 1.000 73.73748  ? 31  GLU A C     1 
ATOM   4099 O  O     . GLU B 2 31  ? 16.44977  -5.79834  -10.91903 1.000 75.04799  ? 31  GLU A O     1 
ATOM   4100 C  CB    . GLU B 2 31  ? 15.00571  -4.39624  -8.28516  1.000 87.20569  ? 31  GLU A CB    1 
ATOM   4101 C  CG    . GLU B 2 31  ? 13.68351  -3.93537  -7.70125  1.000 92.49302  ? 31  GLU A CG    1 
ATOM   4102 C  CD    . GLU B 2 31  ? 13.46026  -4.46543  -6.29630  1.000 104.59261 ? 31  GLU A CD    1 
ATOM   4103 O  OE1   . GLU B 2 31  ? 14.44578  -4.89502  -5.65775  1.000 93.43059  ? 31  GLU A OE1   1 
ATOM   4104 O  OE2   . GLU B 2 31  ? 12.29933  -4.46036  -5.83342  1.000 110.59356 ? 31  GLU A OE2   1 
ATOM   4105 N  N     . TYR B 2 32  ? 17.60875  -4.13763  -9.93908  1.000 70.71494  ? 32  TYR A N     1 
ATOM   4106 C  CA    . TYR B 2 32  ? 18.91930  -4.69338  -10.25322 1.000 73.80106  ? 32  TYR A CA    1 
ATOM   4107 C  C     . TYR B 2 32  ? 19.61988  -5.09417  -8.96194  1.000 69.41760  ? 32  TYR A C     1 
ATOM   4108 O  O     . TYR B 2 32  ? 19.95627  -4.23468  -8.13969  1.000 68.21219  ? 32  TYR A O     1 
ATOM   4109 C  CB    . TYR B 2 32  ? 19.77656  -3.70076  -11.03647 1.000 68.02378  ? 32  TYR A CB    1 
ATOM   4110 C  CG    . TYR B 2 32  ? 21.17603  -4.20998  -11.30079 1.000 74.31646  ? 32  TYR A CG    1 
ATOM   4111 C  CD1   . TYR B 2 32  ? 21.38964  -5.51446  -11.73242 1.000 72.22326  ? 32  TYR A CD1   1 
ATOM   4112 C  CD2   . TYR B 2 32  ? 22.28268  -3.38912  -11.12404 1.000 74.46027  ? 32  TYR A CD2   1 
ATOM   4113 C  CE1   . TYR B 2 32  ? 22.66653  -5.98896  -11.97316 1.000 71.92264  ? 32  TYR A CE1   1 
ATOM   4114 C  CE2   . TYR B 2 32  ? 23.56331  -3.85379  -11.36681 1.000 65.68536  ? 32  TYR A CE2   1 
ATOM   4115 C  CZ    . TYR B 2 32  ? 23.74879  -5.15358  -11.79111 1.000 71.49151  ? 32  TYR A CZ    1 
ATOM   4116 O  OH    . TYR B 2 32  ? 25.02025  -5.62046  -12.03317 1.000 68.70713  ? 32  TYR A OH    1 
ATOM   4117 N  N     . ASP B 2 33  ? 19.84151  -6.39283  -8.79525  1.000 67.11324  ? 33  ASP A N     1 
ATOM   4118 C  CA    . ASP B 2 33  ? 20.58395  -6.93490  -7.65879  1.000 62.68684  ? 33  ASP A CA    1 
ATOM   4119 C  C     . ASP B 2 33  ? 21.72026  -7.78909  -8.20511  1.000 68.23213  ? 33  ASP A C     1 
ATOM   4120 O  O     . ASP B 2 33  ? 21.45876  -8.89021  -8.73330  1.000 62.11330  ? 33  ASP A O     1 
ATOM   4121 C  CB    . ASP B 2 33  ? 19.66845  -7.74965  -6.75000  1.000 62.04639  ? 33  ASP A CB    1 
ATOM   4122 C  CG    . ASP B 2 33  ? 20.29629  -8.05216  -5.40385  1.000 72.94502  ? 33  ASP A CG    1 
ATOM   4123 O  OD1   . ASP B 2 33  ? 21.36033  -7.47499  -5.09323  1.000 69.02137  ? 33  ASP A OD1   1 
ATOM   4124 O  OD2   . ASP B 2 33  ? 19.72035  -8.86890  -4.65308  1.000 82.30065  ? 33  ASP A OD2   1 
ATOM   4125 N  N     . PRO B 2 34  ? 22.97104  -7.33169  -8.11798  1.000 60.92305  ? 34  PRO A N     1 
ATOM   4126 C  CA    . PRO B 2 34  ? 24.08066  -8.08600  -8.71677  1.000 67.18615  ? 34  PRO A CA    1 
ATOM   4127 C  C     . PRO B 2 34  ? 24.18329  -9.49491  -8.15242  1.000 61.08542  ? 34  PRO A C     1 
ATOM   4128 O  O     . PRO B 2 34  ? 23.97229  -9.72731  -6.95980  1.000 64.59056  ? 34  PRO A O     1 
ATOM   4129 C  CB    . PRO B 2 34  ? 25.31249  -7.24695  -8.35830  1.000 58.19552  ? 34  PRO A CB    1 
ATOM   4130 C  CG    . PRO B 2 34  ? 24.78125  -5.87217  -8.16694  1.000 59.08148  ? 34  PRO A CG    1 
ATOM   4131 C  CD    . PRO B 2 34  ? 23.41744  -6.04500  -7.56109  1.000 55.73027  ? 34  PRO A CD    1 
ATOM   4132 N  N     . THR B 2 35  ? 24.52048  -10.43559 -9.02847  1.000 54.84734  ? 35  THR A N     1 
ATOM   4133 C  CA    . THR B 2 35  ? 24.52782  -11.85256 -8.70037  1.000 55.34903  ? 35  THR A CA    1 
ATOM   4134 C  C     . THR B 2 35  ? 25.93420  -12.31532 -8.34558  1.000 59.86744  ? 35  THR A C     1 
ATOM   4135 O  O     . THR B 2 35  ? 26.90885  -11.94128 -9.00375  1.000 59.57489  ? 35  THR A O     1 
ATOM   4136 C  CB    . THR B 2 35  ? 23.99316  -12.67881 -9.87345  1.000 50.56805  ? 35  THR A CB    1 
ATOM   4137 O  OG1   . THR B 2 35  ? 22.65242  -12.27264 -10.17566 1.000 59.14087  ? 35  THR A OG1   1 
ATOM   4138 C  CG2   . THR B 2 35  ? 24.00346  -14.16184 -9.54005  1.000 58.18129  ? 35  THR A CG2   1 
ATOM   4139 N  N     . ILE B 2 36  ? 26.03398  -13.11766 -7.28833  1.000 59.55389  ? 36  ILE A N     1 
ATOM   4140 C  CA    . ILE B 2 36  ? 27.24538  -13.88142 -7.01967  1.000 58.61581  ? 36  ILE A CA    1 
ATOM   4141 C  C     . ILE B 2 36  ? 27.09447  -15.21061 -7.74559  1.000 60.98691  ? 36  ILE A C     1 
ATOM   4142 O  O     . ILE B 2 36  ? 27.83858  -15.50776 -8.68696  1.000 68.99204  ? 36  ILE A O     1 
ATOM   4143 C  CB    . ILE B 2 36  ? 27.47597  -14.07352 -5.50992  1.000 56.33632  ? 36  ILE A CB    1 
ATOM   4144 C  CG1   . ILE B 2 36  ? 27.77565  -12.72696 -4.84697  1.000 54.49619  ? 36  ILE A CG1   1 
ATOM   4145 C  CG2   . ILE B 2 36  ? 28.59913  -15.06348 -5.26246  1.000 49.92735  ? 36  ILE A CG2   1 
ATOM   4146 C  CD1   . ILE B 2 36  ? 27.98869  -12.81033 -3.35459  1.000 66.79333  ? 36  ILE A CD1   1 
ATOM   4147 N  N     . GLU B 2 37  ? 26.11399  -16.00540 -7.32418  1.000 61.39195  ? 37  GLU A N     1 
ATOM   4148 C  CA    . GLU B 2 37  ? 25.70149  -17.19132 -8.05894  1.000 58.48149  ? 37  GLU A CA    1 
ATOM   4149 C  C     . GLU B 2 37  ? 24.29484  -17.56153 -7.61322  1.000 61.83507  ? 37  GLU A C     1 
ATOM   4150 O  O     . GLU B 2 37  ? 23.92369  -17.36396 -6.45300  1.000 62.31305  ? 37  GLU A O     1 
ATOM   4151 C  CB    . GLU B 2 37  ? 26.66489  -18.36684 -7.84628  1.000 59.41053  ? 37  GLU A CB    1 
ATOM   4152 C  CG    . GLU B 2 37  ? 26.68694  -18.91927 -6.42998  1.000 72.35715  ? 37  GLU A CG    1 
ATOM   4153 C  CD    . GLU B 2 37  ? 25.63699  -19.98786 -6.19225  1.000 75.75676  ? 37  GLU A CD    1 
ATOM   4154 O  OE1   . GLU B 2 37  ? 25.29693  -20.71249 -7.15158  1.000 83.22915  ? 37  GLU A OE1   1 
ATOM   4155 O  OE2   . GLU B 2 37  ? 25.14558  -20.09489 -5.04822  1.000 87.62363  ? 37  GLU A OE2   1 
ATOM   4156 N  N     . ASP B 2 38  ? 23.51830  -18.09470 -8.55075  1.000 56.14588  ? 38  ASP A N     1 
ATOM   4157 C  CA    . ASP B 2 38  ? 22.17740  -18.57913 -8.25882  1.000 64.67204  ? 38  ASP A CA    1 
ATOM   4158 C  C     . ASP B 2 38  ? 21.90519  -19.78120 -9.14742  1.000 68.54521  ? 38  ASP A C     1 
ATOM   4159 O  O     . ASP B 2 38  ? 22.20722  -19.75090 -10.34435 1.000 65.41208  ? 38  ASP A O     1 
ATOM   4160 C  CB    . ASP B 2 38  ? 21.12628  -17.48654 -8.48232  1.000 57.95601  ? 38  ASP A CB    1 
ATOM   4161 C  CG    . ASP B 2 38  ? 21.14311  -16.42875 -7.39111  1.000 63.98818  ? 38  ASP A CG    1 
ATOM   4162 O  OD1   . ASP B 2 38  ? 20.99918  -16.79089 -6.20247  1.000 65.31530  ? 38  ASP A OD1   1 
ATOM   4163 O  OD2   . ASP B 2 38  ? 21.30955  -15.23502 -7.72119  1.000 59.01461  ? 38  ASP A OD2   1 
ATOM   4164 N  N     . SER B 2 39  ? 21.35488  -20.83653 -8.55657  1.000 62.96783  ? 39  SER A N     1 
ATOM   4165 C  CA    . SER B 2 39  ? 21.08500  -22.07998 -9.25869  1.000 61.02747  ? 39  SER A CA    1 
ATOM   4166 C  C     . SER B 2 39  ? 19.59638  -22.38270 -9.19850  1.000 63.95309  ? 39  SER A C     1 
ATOM   4167 O  O     . SER B 2 39  ? 18.93590  -22.10552 -8.19278  1.000 59.03576  ? 39  SER A O     1 
ATOM   4168 C  CB    . SER B 2 39  ? 21.88383  -23.23964 -8.65631  1.000 62.60746  ? 39  SER A CB    1 
ATOM   4169 O  OG    . SER B 2 39  ? 21.51964  -23.45600 -7.30419  1.000 72.52279  ? 39  SER A OG    1 
ATOM   4170 N  N     . TYR B 2 40  ? 19.07542  -22.95566 -10.28001 1.000 64.99536  ? 40  TYR A N     1 
ATOM   4171 C  CA    . TYR B 2 40  ? 17.65956  -23.26111 -10.39163 1.000 56.59175  ? 40  TYR A CA    1 
ATOM   4172 C  C     . TYR B 2 40  ? 17.48437  -24.61196 -11.06736 1.000 62.92751  ? 40  TYR A C     1 
ATOM   4173 O  O     . TYR B 2 40  ? 18.30501  -25.02007 -11.89319 1.000 65.72742  ? 40  TYR A O     1 
ATOM   4174 C  CB    . TYR B 2 40  ? 16.91367  -22.18345 -11.18908 1.000 61.17860  ? 40  TYR A CB    1 
ATOM   4175 C  CG    . TYR B 2 40  ? 17.09636  -20.77917 -10.65879 1.000 65.71429  ? 40  TYR A CG    1 
ATOM   4176 C  CD1   . TYR B 2 40  ? 16.29961  -20.29640 -9.62872  1.000 63.26939  ? 40  TYR A CD1   1 
ATOM   4177 C  CD2   . TYR B 2 40  ? 18.06006  -19.93316 -11.19371 1.000 62.98314  ? 40  TYR A CD2   1 
ATOM   4178 C  CE1   . TYR B 2 40  ? 16.45946  -19.01303 -9.14308  1.000 45.29196  ? 40  TYR A CE1   1 
ATOM   4179 C  CE2   . TYR B 2 40  ? 18.22544  -18.64800 -10.71592 1.000 58.28607  ? 40  TYR A CE2   1 
ATOM   4180 C  CZ    . TYR B 2 40  ? 17.42250  -18.19397 -9.69082  1.000 54.62043  ? 40  TYR A CZ    1 
ATOM   4181 O  OH    . TYR B 2 40  ? 17.58533  -16.91575 -9.21093  1.000 65.58671  ? 40  TYR A OH    1 
ATOM   4182 N  N     . ARG B 2 41  ? 16.40491  -25.30475 -10.70463 1.000 65.98345  ? 41  ARG A N     1 
ATOM   4183 C  CA    . ARG B 2 41  ? 15.99824  -26.54051 -11.36625 1.000 66.31745  ? 41  ARG A CA    1 
ATOM   4184 C  C     . ARG B 2 41  ? 14.53570  -26.39974 -11.75976 1.000 59.35889  ? 41  ARG A C     1 
ATOM   4185 O  O     . ARG B 2 41  ? 13.66872  -26.27480 -10.88849 1.000 70.86551  ? 41  ARG A O     1 
ATOM   4186 C  CB    . ARG B 2 41  ? 16.21299  -27.76162 -10.46189 1.000 59.73060  ? 41  ARG A CB    1 
ATOM   4187 C  CG    . ARG B 2 41  ? 17.62331  -27.85060 -9.87503  1.000 78.33649  ? 41  ARG A CG    1 
ATOM   4188 C  CD    . ARG B 2 41  ? 17.89552  -29.17991 -9.17319  1.000 78.05845  ? 41  ARG A CD    1 
ATOM   4189 N  NE    . ARG B 2 41  ? 18.31651  -30.22519 -10.09997 1.000 82.09278  ? 41  ARG A NE    1 
ATOM   4190 C  CZ    . ARG B 2 41  ? 17.57061  -31.26467 -10.45044 1.000 87.98347  ? 41  ARG A CZ    1 
ATOM   4191 N  NH1   . ARG B 2 41  ? 16.35783  -31.44488 -9.95333  1.000 92.74872  ? 41  ARG A NH1   1 
ATOM   4192 N  NH2   . ARG B 2 41  ? 18.05571  -32.14843 -11.31791 1.000 78.43389  ? 41  ARG A NH2   1 
ATOM   4193 N  N     . LYS B 2 42  ? 14.26571  -26.41395 -13.06670 1.000 57.30029  ? 42  LYS A N     1 
ATOM   4194 C  CA    . LYS B 2 42  ? 12.94073  -26.12883 -13.61125 1.000 61.03933  ? 42  LYS A CA    1 
ATOM   4195 C  C     . LYS B 2 42  ? 12.58228  -27.17952 -14.65110 1.000 65.56011  ? 42  LYS A C     1 
ATOM   4196 O  O     . LYS B 2 42  ? 13.29897  -27.33821 -15.64454 1.000 63.87266  ? 42  LYS A O     1 
ATOM   4197 C  CB    . LYS B 2 42  ? 12.90101  -24.73078 -14.23595 1.000 60.94693  ? 42  LYS A CB    1 
ATOM   4198 C  CG    . LYS B 2 42  ? 11.67657  -24.44416 -15.08855 1.000 62.52436  ? 42  LYS A CG    1 
ATOM   4199 C  CD    . LYS B 2 42  ? 10.49019  -24.01481 -14.24787 1.000 62.55568  ? 42  LYS A CD    1 
ATOM   4200 C  CE    . LYS B 2 42  ? 9.33236   -23.57507 -15.12909 1.000 73.04121  ? 42  LYS A CE    1 
ATOM   4201 N  NZ    . LYS B 2 42  ? 8.18527   -23.05950 -14.33341 1.000 73.91437  ? 42  LYS A NZ    1 
ATOM   4202 N  N     . GLN B 2 43  ? 11.47318  -27.88480 -14.43147 1.000 64.35666  ? 43  GLN A N     1 
ATOM   4203 C  CA    . GLN B 2 43  ? 11.00377  -28.87196 -15.39435 1.000 61.30818  ? 43  GLN A CA    1 
ATOM   4204 C  C     . GLN B 2 43  ? 10.23982  -28.18990 -16.52027 1.000 62.42438  ? 43  GLN A C     1 
ATOM   4205 O  O     . GLN B 2 43  ? 9.48970   -27.23705 -16.29444 1.000 74.88824  ? 43  GLN A O     1 
ATOM   4206 C  CB    . GLN B 2 43  ? 10.11104  -29.91072 -14.71735 1.000 55.63849  ? 43  GLN A CB    1 
ATOM   4207 C  CG    . GLN B 2 43  ? 9.61183   -30.99040 -15.66230 1.000 62.58018  ? 43  GLN A CG    1 
ATOM   4208 C  CD    . GLN B 2 43  ? 8.63414   -31.94235 -15.00435 1.000 75.75535  ? 43  GLN A CD    1 
ATOM   4209 O  OE1   . GLN B 2 43  ? 8.89783   -32.47663 -13.92654 1.000 69.88231  ? 43  GLN A OE1   1 
ATOM   4210 N  NE2   . GLN B 2 43  ? 7.49172   -32.15561 -15.65052 1.000 76.32572  ? 43  GLN A NE2   1 
ATOM   4211 N  N     . VAL B 2 44  ? 10.43164  -28.68463 -17.73954 1.000 65.47399  ? 44  VAL A N     1 
ATOM   4212 C  CA    . VAL B 2 44  ? 9.81806   -28.06909 -18.90871 1.000 60.30404  ? 44  VAL A CA    1 
ATOM   4213 C  C     . VAL B 2 44  ? 9.73318   -29.10590 -20.02122 1.000 62.83146  ? 44  VAL A C     1 
ATOM   4214 O  O     . VAL B 2 44  ? 10.35780  -30.16966 -19.94070 1.000 62.52301  ? 44  VAL A O     1 
ATOM   4215 C  CB    . VAL B 2 44  ? 10.61150  -26.82353 -19.34721 1.000 59.44764  ? 44  VAL A CB    1 
ATOM   4216 C  CG1   . VAL B 2 44  ? 11.82023  -27.22223 -20.17797 1.000 58.47414  ? 44  VAL A CG1   1 
ATOM   4217 C  CG2   . VAL B 2 44  ? 9.71713   -25.85100 -20.09682 1.000 88.57313  ? 44  VAL A CG2   1 
ATOM   4218 N  N     . VAL B 2 45  ? 8.95169   -28.81809 -21.05788 1.000 63.75630  ? 45  VAL A N     1 
ATOM   4219 C  CA    . VAL B 2 45  ? 8.80592   -29.71303 -22.20002 1.000 70.30964  ? 45  VAL A CA    1 
ATOM   4220 C  C     . VAL B 2 45  ? 9.26845   -28.97213 -23.44776 1.000 62.07990  ? 45  VAL A C     1 
ATOM   4221 O  O     . VAL B 2 45  ? 8.67431   -27.95849 -23.83699 1.000 68.62320  ? 45  VAL A O     1 
ATOM   4222 C  CB    . VAL B 2 45  ? 7.36529   -30.22921 -22.35285 1.000 62.48353  ? 45  VAL A CB    1 
ATOM   4223 C  CG1   . VAL B 2 45  ? 6.35674   -29.10098 -22.17435 1.000 69.53952  ? 45  VAL A CG1   1 
ATOM   4224 C  CG2   . VAL B 2 45  ? 7.19315   -30.90268 -23.70107 1.000 59.91658  ? 45  VAL A CG2   1 
ATOM   4225 N  N     . ILE B 2 46  ? 10.33207  -29.47496 -24.06596 1.000 62.41020  ? 46  ILE A N     1 
ATOM   4226 C  CA    . ILE B 2 46  ? 10.94282  -28.86208 -25.23848 1.000 64.36130  ? 46  ILE A CA    1 
ATOM   4227 C  C     . ILE B 2 46  ? 10.86069  -29.86469 -26.37840 1.000 63.08095  ? 46  ILE A C     1 
ATOM   4228 O  O     . ILE B 2 46  ? 11.34101  -30.99790 -26.24743 1.000 66.28976  ? 46  ILE A O     1 
ATOM   4229 C  CB    . ILE B 2 46  ? 12.40080  -28.45328 -24.97219 1.000 66.44984  ? 46  ILE A CB    1 
ATOM   4230 C  CG1   . ILE B 2 46  ? 12.47815  -27.49950 -23.77738 1.000 70.54060  ? 46  ILE A CG1   1 
ATOM   4231 C  CG2   . ILE B 2 46  ? 13.01770  -27.82214 -26.21352 1.000 62.04178  ? 46  ILE A CG2   1 
ATOM   4232 C  CD1   . ILE B 2 46  ? 13.88828  -27.25085 -23.28442 1.000 67.62351  ? 46  ILE A CD1   1 
ATOM   4233 N  N     . ASP B 2 47  ? 10.24514  -29.45207 -27.48843 1.000 60.92844  ? 47  ASP A N     1 
ATOM   4234 C  CA    . ASP B 2 47  ? 10.11632  -30.29299 -28.68120 1.000 60.69820  ? 47  ASP A CA    1 
ATOM   4235 C  C     . ASP B 2 47  ? 9.54080   -31.66614 -28.34772 1.000 68.93608  ? 47  ASP A C     1 
ATOM   4236 O  O     . ASP B 2 47  ? 9.87988   -32.66680 -28.98280 1.000 77.62809  ? 47  ASP A O     1 
ATOM   4237 C  CB    . ASP B 2 47  ? 11.45780  -30.43910 -29.40045 1.000 68.26432  ? 47  ASP A CB    1 
ATOM   4238 C  CG    . ASP B 2 47  ? 12.01602  -29.11286 -29.86402 1.000 72.47005  ? 47  ASP A CG    1 
ATOM   4239 O  OD1   . ASP B 2 47  ? 11.23543  -28.28647 -30.38044 1.000 88.22793  ? 47  ASP A OD1   1 
ATOM   4240 O  OD2   . ASP B 2 47  ? 13.23403  -28.89498 -29.70583 1.000 74.14950  ? 47  ASP A OD2   1 
ATOM   4241 N  N     . GLY B 2 48  ? 8.67378   -31.72578 -27.33784 1.000 70.00837  ? 48  GLY A N     1 
ATOM   4242 C  CA    . GLY B 2 48  ? 8.01734   -32.95437 -26.94903 1.000 67.74335  ? 48  GLY A CA    1 
ATOM   4243 C  C     . GLY B 2 48  ? 8.67170   -33.70531 -25.80749 1.000 69.66381  ? 48  GLY A C     1 
ATOM   4244 O  O     . GLY B 2 48  ? 8.06714   -34.65259 -25.28913 1.000 70.75343  ? 48  GLY A O     1 
ATOM   4245 N  N     . GLU B 2 49  ? 9.87601   -33.31747 -25.39628 1.000 71.26713  ? 49  GLU A N     1 
ATOM   4246 C  CA    . GLU B 2 49  ? 10.60873  -34.02522 -24.35382 1.000 72.03570  ? 49  GLU A CA    1 
ATOM   4247 C  C     . GLU B 2 49  ? 10.38672  -33.33589 -23.01472 1.000 74.86250  ? 49  GLU A C     1 
ATOM   4248 O  O     . GLU B 2 49  ? 10.68817  -32.14636 -22.86665 1.000 71.42901  ? 49  GLU A O     1 
ATOM   4249 C  CB    . GLU B 2 49  ? 12.10382  -34.08510 -24.66766 1.000 64.16643  ? 49  GLU A CB    1 
ATOM   4250 C  CG    . GLU B 2 49  ? 12.92148  -34.77325 -23.57979 1.000 64.40299  ? 49  GLU A CG    1 
ATOM   4251 C  CD    . GLU B 2 49  ? 14.41970  -34.58945 -23.75174 1.000 75.69545  ? 49  GLU A CD    1 
ATOM   4252 O  OE1   . GLU B 2 49  ? 14.83325  -33.56889 -24.34374 1.000 75.53090  ? 49  GLU A OE1   1 
ATOM   4253 O  OE2   . GLU B 2 49  ? 15.18493  -35.46853 -23.29586 1.000 67.79898  ? 49  GLU A OE2   1 
ATOM   4254 N  N     . THR B 2 50  ? 9.86628   -34.08206 -22.04396 1.000 69.81500  ? 50  THR A N     1 
ATOM   4255 C  CA    . THR B 2 50  ? 9.82725   -33.61167 -20.66447 1.000 67.67995  ? 50  THR A CA    1 
ATOM   4256 C  C     . THR B 2 50  ? 11.23093  -33.73899 -20.08877 1.000 66.21573  ? 50  THR A C     1 
ATOM   4257 O  O     . THR B 2 50  ? 11.73460  -34.85053 -19.89856 1.000 80.72247  ? 50  THR A O     1 
ATOM   4258 C  CB    . THR B 2 50  ? 8.81976   -34.40785 -19.84086 1.000 61.45960  ? 50  THR A CB    1 
ATOM   4259 O  OG1   . THR B 2 50  ? 7.51570   -34.27009 -20.41831 1.000 75.43044  ? 50  THR A OG1   1 
ATOM   4260 C  CG2   . THR B 2 50  ? 8.78898   -33.89548 -18.40850 1.000 55.81697  ? 50  THR A CG2   1 
ATOM   4261 N  N     . CYS B 2 51  ? 11.87013  -32.60611 -19.82013 1.000 67.52027  ? 51  CYS A N     1 
ATOM   4262 C  CA    . CYS B 2 51  ? 13.23675  -32.59796 -19.32833 1.000 65.12674  ? 51  CYS A CA    1 
ATOM   4263 C  C     . CYS B 2 51  ? 13.34805  -31.59911 -18.19014 1.000 59.88727  ? 51  CYS A C     1 
ATOM   4264 O  O     . CYS B 2 51  ? 12.47227  -30.75601 -17.98093 1.000 67.85330  ? 51  CYS A O     1 
ATOM   4265 C  CB    . CYS B 2 51  ? 14.23406  -32.25849 -20.44138 1.000 68.04050  ? 51  CYS A CB    1 
ATOM   4266 S  SG    . CYS B 2 51  ? 13.89187  -30.69805 -21.28462 1.000 71.18418  ? 51  CYS A SG    1 
ATOM   4267 N  N     . LEU B 2 52  ? 14.44694  -31.70250 -17.45560 1.000 58.98930  ? 52  LEU A N     1 
ATOM   4268 C  CA    . LEU B 2 52  ? 14.71197  -30.86399 -16.29724 1.000 61.11518  ? 52  LEU A CA    1 
ATOM   4269 C  C     . LEU B 2 52  ? 15.87216  -29.93670 -16.63480 1.000 65.61793  ? 52  LEU A C     1 
ATOM   4270 O  O     . LEU B 2 52  ? 16.95988  -30.40373 -16.98833 1.000 67.38275  ? 52  LEU A O     1 
ATOM   4271 C  CB    . LEU B 2 52  ? 15.02703  -31.72852 -15.07675 1.000 63.18291  ? 52  LEU A CB    1 
ATOM   4272 C  CG    . LEU B 2 52  ? 14.51871  -31.25930 -13.71396 1.000 77.37303  ? 52  LEU A CG    1 
ATOM   4273 C  CD1   . LEU B 2 52  ? 14.40644  -32.44206 -12.75855 1.000 85.88769  ? 52  LEU A CD1   1 
ATOM   4274 C  CD2   . LEU B 2 52  ? 15.43916  -30.19389 -13.13949 1.000 72.94923  ? 52  LEU A CD2   1 
ATOM   4275 N  N     . LEU B 2 53  ? 15.63454  -28.63067 -16.55021 1.000 58.70249  ? 53  LEU A N     1 
ATOM   4276 C  CA    . LEU B 2 53  ? 16.66501  -27.64172 -16.83130 1.000 56.54432  ? 53  LEU A CA    1 
ATOM   4277 C  C     . LEU B 2 53  ? 17.36240  -27.25008 -15.53692 1.000 64.11882  ? 53  LEU A C     1 
ATOM   4278 O  O     . LEU B 2 53  ? 16.70706  -26.86449 -14.56391 1.000 63.64528  ? 53  LEU A O     1 
ATOM   4279 C  CB    . LEU B 2 53  ? 16.07009  -26.40160 -17.49889 1.000 55.49727  ? 53  LEU A CB    1 
ATOM   4280 C  CG    . LEU B 2 53  ? 15.38535  -26.59078 -18.85077 1.000 54.96211  ? 53  LEU A CG    1 
ATOM   4281 C  CD1   . LEU B 2 53  ? 15.03399  -25.24286 -19.45804 1.000 53.48744  ? 53  LEU A CD1   1 
ATOM   4282 C  CD2   . LEU B 2 53  ? 16.27017  -27.39014 -19.78889 1.000 69.66635  ? 53  LEU A CD2   1 
ATOM   4283 N  N     . ASP B 2 54  ? 18.68608  -27.34671 -15.52893 1.000 57.93554  ? 54  ASP A N     1 
ATOM   4284 C  CA    . ASP B 2 54  ? 19.49657  -26.96084 -14.37891 1.000 60.19184  ? 54  ASP A CA    1 
ATOM   4285 C  C     . ASP B 2 54  ? 20.27666  -25.70845 -14.76923 1.000 56.68904  ? 54  ASP A C     1 
ATOM   4286 O  O     . ASP B 2 54  ? 21.34174  -25.79484 -15.38614 1.000 62.61888  ? 54  ASP A O     1 
ATOM   4287 C  CB    . ASP B 2 54  ? 20.41425  -28.10229 -13.95635 1.000 56.87031  ? 54  ASP A CB    1 
ATOM   4288 C  CG    . ASP B 2 54  ? 20.79005  -28.03064 -12.49356 1.000 75.12692  ? 54  ASP A CG    1 
ATOM   4289 O  OD1   . ASP B 2 54  ? 21.34524  -26.99418 -12.07178 1.000 74.10911  ? 54  ASP A OD1   1 
ATOM   4290 O  OD2   . ASP B 2 54  ? 20.51078  -29.00362 -11.76051 1.000 92.16722  ? 54  ASP A OD2   1 
ATOM   4291 N  N     . ILE B 2 55  ? 19.74187  -24.54495 -14.40697 1.000 56.81583  ? 55  ILE A N     1 
ATOM   4292 C  CA    . ILE B 2 55  ? 20.27223  -23.25817 -14.84289 1.000 57.61027  ? 55  ILE A CA    1 
ATOM   4293 C  C     . ILE B 2 55  ? 21.18121  -22.69409 -13.76015 1.000 59.24238  ? 55  ILE A C     1 
ATOM   4294 O  O     . ILE B 2 55  ? 20.79083  -22.60559 -12.58899 1.000 54.74287  ? 55  ILE A O     1 
ATOM   4295 C  CB    . ILE B 2 55  ? 19.13606  -22.27681 -15.17629 1.000 57.40967  ? 55  ILE A CB    1 
ATOM   4296 C  CG1   . ILE B 2 55  ? 18.26228  -22.85014 -16.29282 1.000 57.17070  ? 55  ILE A CG1   1 
ATOM   4297 C  CG2   . ILE B 2 55  ? 19.69670  -20.91946 -15.57507 1.000 56.39856  ? 55  ILE A CG2   1 
ATOM   4298 C  CD1   . ILE B 2 55  ? 17.28254  -21.86078 -16.87034 1.000 65.44960  ? 55  ILE A CD1   1 
ATOM   4299 N  N     . LEU B 2 56  ? 22.39332  -22.31222 -14.15033 1.000 59.96710  ? 56  LEU A N     1 
ATOM   4300 C  CA    . LEU B 2 56  ? 23.35077  -21.67405 -13.25770 1.000 55.44545  ? 56  LEU A CA    1 
ATOM   4301 C  C     . LEU B 2 56  ? 23.48574  -20.21574 -13.67334 1.000 58.77696  ? 56  LEU A C     1 
ATOM   4302 O  O     . LEU B 2 56  ? 23.91912  -19.92143 -14.79297 1.000 55.27121  ? 56  LEU A O     1 
ATOM   4303 C  CB    . LEU B 2 56  ? 24.70494  -22.38351 -13.30199 1.000 56.81347  ? 56  LEU A CB    1 
ATOM   4304 C  CG    . LEU B 2 56  ? 25.53846  -22.42026 -12.01523 1.000 71.73688  ? 56  LEU A CG    1 
ATOM   4305 C  CD1   . LEU B 2 56  ? 26.79940  -23.24736 -12.22725 1.000 76.78362  ? 56  LEU A CD1   1 
ATOM   4306 C  CD2   . LEU B 2 56  ? 25.89248  -21.02252 -11.51252 1.000 62.84696  ? 56  LEU A CD2   1 
ATOM   4307 N  N     . ASP B 2 57  ? 23.11348  -19.31225 -12.77511 1.000 56.07723  ? 57  ASP A N     1 
ATOM   4308 C  CA    . ASP B 2 57  ? 23.15189  -17.87784 -13.02848 1.000 55.15713  ? 57  ASP A CA    1 
ATOM   4309 C  C     . ASP B 2 57  ? 24.42110  -17.32339 -12.38718 1.000 56.77624  ? 57  ASP A C     1 
ATOM   4310 O  O     . ASP B 2 57  ? 24.52593  -17.26283 -11.15818 1.000 69.85320  ? 57  ASP A O     1 
ATOM   4311 C  CB    . ASP B 2 57  ? 21.89670  -17.21440 -12.46571 1.000 53.47310  ? 57  ASP A CB    1 
ATOM   4312 C  CG    . ASP B 2 57  ? 21.69189  -15.80761 -12.98209 1.000 64.26575  ? 57  ASP A CG    1 
ATOM   4313 O  OD1   . ASP B 2 57  ? 22.32090  -15.43819 -13.99614 1.000 66.04986  ? 57  ASP A OD1   1 
ATOM   4314 O  OD2   . ASP B 2 57  ? 20.89580  -15.06874 -12.36510 1.000 67.55279  ? 57  ASP A OD2   1 
ATOM   4315 N  N     . THR B 2 58  ? 25.38749  -16.92784 -13.21224 1.000 62.12104  ? 58  THR A N     1 
ATOM   4316 C  CA    . THR B 2 58  ? 26.69422  -16.52200 -12.71734 1.000 64.19059  ? 58  THR A CA    1 
ATOM   4317 C  C     . THR B 2 58  ? 26.79828  -15.00161 -12.62199 1.000 61.46151  ? 58  THR A C     1 
ATOM   4318 O  O     . THR B 2 58  ? 25.86134  -14.25900 -12.92556 1.000 64.97558  ? 58  THR A O     1 
ATOM   4319 C  CB    . THR B 2 58  ? 27.81029  -17.07463 -13.60541 1.000 50.62096  ? 58  THR A CB    1 
ATOM   4320 O  OG1   . THR B 2 58  ? 27.78941  -16.40937 -14.87365 1.000 58.13234  ? 58  THR A OG1   1 
ATOM   4321 C  CG2   . THR B 2 58  ? 27.63236  -18.56694 -13.81318 1.000 65.81190  ? 58  THR A CG2   1 
ATOM   4322 N  N     . ALA B 2 59  ? 27.97275  -14.54215 -12.19946 1.000 68.57794  ? 59  ALA A N     1 
ATOM   4323 C  CA    . ALA B 2 59  ? 28.24362  -13.13189 -11.97460 1.000 53.70906  ? 59  ALA A CA    1 
ATOM   4324 C  C     . ALA B 2 59  ? 28.79976  -12.47213 -13.22941 1.000 56.60360  ? 59  ALA A C     1 
ATOM   4325 O  O     . ALA B 2 59  ? 29.49862  -13.09837 -14.03032 1.000 70.25133  ? 59  ALA A O     1 
ATOM   4326 C  CB    . ALA B 2 59  ? 29.23520  -12.95838 -10.82480 1.000 57.24473  ? 59  ALA A CB    1 
ATOM   4327 N  N     . GLY B 2 60  ? 28.48490  -11.19040 -13.38831 1.000 57.61087  ? 60  GLY A N     1 
ATOM   4328 C  CA    . GLY B 2 60  ? 29.03464  -10.40432 -14.47416 1.000 64.53918  ? 60  GLY A CA    1 
ATOM   4329 C  C     . GLY B 2 60  ? 30.10985  -9.44864  -14.00055 1.000 59.13609  ? 60  GLY A C     1 
ATOM   4330 O  O     . GLY B 2 60  ? 31.12312  -9.25685  -14.67842 1.000 70.52535  ? 60  GLY A O     1 
ATOM   4331 N  N     . ARG B 2 61  ? 29.89291  -8.83882  -12.83722 1.000 64.23034  ? 61  ARG A N     1 
ATOM   4332 C  CA    . ARG B 2 61  ? 30.91132  -7.99811  -12.22570 1.000 60.17421  ? 61  ARG A CA    1 
ATOM   4333 C  C     . ARG B 2 61  ? 32.09628  -8.85075  -11.79339 1.000 68.87721  ? 61  ARG A C     1 
ATOM   4334 O  O     . ARG B 2 61  ? 31.92725  -9.96689  -11.29633 1.000 67.10223  ? 61  ARG A O     1 
ATOM   4335 C  CB    . ARG B 2 61  ? 30.33205  -7.25156  -11.02558 1.000 57.31025  ? 61  ARG A CB    1 
ATOM   4336 C  CG    . ARG B 2 61  ? 29.16661  -6.34170  -11.36521 1.000 51.75149  ? 61  ARG A CG    1 
ATOM   4337 C  CD    . ARG B 2 61  ? 28.61739  -5.66802  -10.12046 1.000 59.81587  ? 61  ARG A CD    1 
ATOM   4338 N  NE    . ARG B 2 61  ? 29.62693  -4.86703  -9.43888  1.000 61.81667  ? 61  ARG A NE    1 
ATOM   4339 C  CZ    . ARG B 2 61  ? 29.80246  -3.56589  -9.62553  1.000 68.38216  ? 61  ARG A CZ    1 
ATOM   4340 N  NH1   . ARG B 2 61  ? 29.04333  -2.87911  -10.46484 1.000 63.63495  ? 61  ARG A NH1   1 
ATOM   4341 N  NH2   . ARG B 2 61  ? 30.76254  -2.93785  -8.95225  1.000 60.57705  ? 61  ARG A NH2   1 
ATOM   4342 N  N     . GLU B 2 62  ? 33.30490  -8.31648  -11.97850 1.000 64.29848  ? 62  GLU A N     1 
ATOM   4343 C  CA    . GLU B 2 62  ? 34.49839  -9.12663  -11.76142 1.000 63.62768  ? 62  GLU A CA    1 
ATOM   4344 C  C     . GLU B 2 62  ? 34.69075  -9.45990  -10.28656 1.000 65.02649  ? 62  GLU A C     1 
ATOM   4345 O  O     . GLU B 2 62  ? 35.03443  -10.59787 -9.94634  1.000 73.32901  ? 62  GLU A O     1 
ATOM   4346 C  CB    . GLU B 2 62  ? 35.72826  -8.41339  -12.32138 1.000 72.01462  ? 62  GLU A CB    1 
ATOM   4347 C  CG    . GLU B 2 62  ? 36.82037  -9.36122  -12.80448 1.000 91.31749  ? 62  GLU A CG    1 
ATOM   4348 C  CD    . GLU B 2 62  ? 36.35397  -10.26758 -13.93787 1.000 111.12165 ? 62  GLU A CD    1 
ATOM   4349 O  OE1   . GLU B 2 62  ? 35.48223  -9.84386  -14.73178 1.000 98.42984  ? 62  GLU A OE1   1 
ATOM   4350 O  OE2   . GLU B 2 62  ? 36.85879  -11.40806 -14.03192 1.000 110.23568 ? 62  GLU A OE2   1 
ATOM   4351 N  N     . GLU B 2 63  ? 34.46943  -8.48833  -9.39484  1.000 57.63023  ? 63  GLU A N     1 
ATOM   4352 C  CA    . GLU B 2 63  ? 34.65589  -8.74422  -7.96775  1.000 65.30365  ? 63  GLU A CA    1 
ATOM   4353 C  C     . GLU B 2 63  ? 33.68459  -9.79760  -7.45696  1.000 64.68803  ? 63  GLU A C     1 
ATOM   4354 O  O     . GLU B 2 63  ? 33.99875  -10.52773 -6.50996  1.000 70.74796  ? 63  GLU A O     1 
ATOM   4355 C  CB    . GLU B 2 63  ? 34.49618  -7.45215  -7.16759  1.000 60.19435  ? 63  GLU A CB    1 
ATOM   4356 C  CG    . GLU B 2 63  ? 34.55350  -6.19896  -8.01014  1.000 69.39122  ? 63  GLU A CG    1 
ATOM   4357 C  CD    . GLU B 2 63  ? 33.20131  -5.82212  -8.57633  1.000 66.79650  ? 63  GLU A CD    1 
ATOM   4358 O  OE1   . GLU B 2 63  ? 32.24631  -5.67786  -7.78357  1.000 61.40422  ? 63  GLU A OE1   1 
ATOM   4359 O  OE2   . GLU B 2 63  ? 33.09243  -5.68030  -9.81317  1.000 74.62564  ? 63  GLU A OE2   1 
ATOM   4360 N  N     . TYR B 2 64  ? 32.49869  -9.87842  -8.05706  1.000 67.82166  ? 64  TYR A N     1 
ATOM   4361 C  CA    . TYR B 2 64  ? 31.56556  -10.95354 -7.75965  1.000 59.28641  ? 64  TYR A CA    1 
ATOM   4362 C  C     . TYR B 2 64  ? 31.94787  -12.25172 -8.45541  1.000 77.71969  ? 64  TYR A C     1 
ATOM   4363 O  O     . TYR B 2 64  ? 31.48670  -13.32179 -8.04328  1.000 72.54440  ? 64  TYR A O     1 
ATOM   4364 C  CB    . TYR B 2 64  ? 30.14986  -10.55637 -8.18786  1.000 52.63554  ? 64  TYR A CB    1 
ATOM   4365 C  CG    . TYR B 2 64  ? 29.51519  -9.42456  -7.40190  1.000 59.43804  ? 64  TYR A CG    1 
ATOM   4366 C  CD1   . TYR B 2 64  ? 30.02130  -8.13164  -7.45979  1.000 55.64204  ? 64  TYR A CD1   1 
ATOM   4367 C  CD2   . TYR B 2 64  ? 28.38351  -9.64717  -6.63049  1.000 60.14676  ? 64  TYR A CD2   1 
ATOM   4368 C  CE1   . TYR B 2 64  ? 29.43225  -7.10235  -6.75093  1.000 57.26395  ? 64  TYR A CE1   1 
ATOM   4369 C  CE2   . TYR B 2 64  ? 27.78771  -8.62657  -5.92352  1.000 56.62138  ? 64  TYR A CE2   1 
ATOM   4370 C  CZ    . TYR B 2 64  ? 28.31357  -7.35667  -5.98512  1.000 62.36346  ? 64  TYR A CZ    1 
ATOM   4371 O  OH    . TYR B 2 64  ? 27.71221  -6.33982  -5.27616  1.000 68.72380  ? 64  TYR A OH    1 
ATOM   4372 N  N     . SER B 2 65  ? 32.78969  -12.17826 -9.48840  1.000 74.29282  ? 65  SER A N     1 
ATOM   4373 C  CA    . SER B 2 65  ? 33.03266  -13.28599 -10.40008 1.000 70.92859  ? 65  SER A CA    1 
ATOM   4374 C  C     . SER B 2 65  ? 34.11296  -14.24093 -9.91357  1.000 77.40083  ? 65  SER A C     1 
ATOM   4375 O  O     . SER B 2 65  ? 34.64579  -15.01402 -10.71804 1.000 85.01882  ? 65  SER A O     1 
ATOM   4376 C  CB    . SER B 2 65  ? 33.40021  -12.75471 -11.78693 1.000 88.18224  ? 65  SER A CB    1 
ATOM   4377 O  OG    . SER B 2 65  ? 32.50264  -13.24138 -12.77029 1.000 99.69193  ? 65  SER A OG    1 
ATOM   4378 N  N     . ALA B 2 66  ? 34.46272  -14.20150 -8.63177  1.000 79.72050  ? 66  ALA A N     1 
ATOM   4379 C  CA    . ALA B 2 66  ? 35.31341  -15.24946 -8.08994  1.000 82.00482  ? 66  ALA A CA    1 
ATOM   4380 C  C     . ALA B 2 66  ? 34.57860  -16.58021 -8.18111  1.000 87.35299  ? 66  ALA A C     1 
ATOM   4381 O  O     . ALA B 2 66  ? 33.35361  -16.63774 -8.03340  1.000 85.78593  ? 66  ALA A O     1 
ATOM   4382 C  CB    . ALA B 2 66  ? 35.69922  -14.93939 -6.64396  1.000 73.66350  ? 66  ALA A CB    1 
ATOM   4383 N  N     . MET B 2 67  ? 35.33365  -17.64525 -8.46087  1.000 80.67443  ? 67  MET A N     1 
ATOM   4384 C  CA    . MET B 2 67  ? 34.81743  -18.99538 -8.68700  1.000 84.02124  ? 67  MET A CA    1 
ATOM   4385 C  C     . MET B 2 67  ? 34.05707  -19.13597 -9.99909  1.000 87.98226  ? 67  MET A C     1 
ATOM   4386 O  O     . MET B 2 67  ? 33.27427  -20.07781 -10.15696 1.000 91.58499  ? 67  MET A O     1 
ATOM   4387 C  CB    . MET B 2 67  ? 33.91432  -19.46881 -7.54288  1.000 80.11590  ? 67  MET A CB    1 
ATOM   4388 C  CG    . MET B 2 67  ? 34.62463  -20.11725 -6.38741  1.000 84.78543  ? 67  MET A CG    1 
ATOM   4389 S  SD    . MET B 2 67  ? 33.39956  -20.79227 -5.25856  1.000 103.79238 ? 67  MET A SD    1 
ATOM   4390 C  CE    . MET B 2 67  ? 32.46282  -21.84128 -6.37094  1.000 84.31122  ? 67  MET A CE    1 
ATOM   4391 N  N     . ARG B 2 68  ? 34.25494  -18.22675 -10.95505 1.000 90.44825  ? 68  ARG A N     1 
ATOM   4392 C  CA    . ARG B 2 68  ? 33.54322  -18.35944 -12.22181 1.000 87.36065  ? 68  ARG A CA    1 
ATOM   4393 C  C     . ARG B 2 68  ? 34.05771  -19.54396 -13.03180 1.000 88.19753  ? 68  ARG A C     1 
ATOM   4394 O  O     . ARG B 2 68  ? 33.29888  -20.13659 -13.80703 1.000 92.67230  ? 68  ARG A O     1 
ATOM   4395 C  CB    . ARG B 2 68  ? 33.64928  -17.06547 -13.03038 1.000 94.08684  ? 68  ARG A CB    1 
ATOM   4396 C  CG    . ARG B 2 68  ? 32.78871  -17.04957 -14.28687 1.000 98.33210  ? 68  ARG A CG    1 
ATOM   4397 C  CD    . ARG B 2 68  ? 32.59830  -15.63945 -14.82140 1.000 91.64037  ? 68  ARG A CD    1 
ATOM   4398 N  NE    . ARG B 2 68  ? 33.85644  -15.02603 -15.22815 1.000 92.03553  ? 68  ARG A NE    1 
ATOM   4399 C  CZ    . ARG B 2 68  ? 33.98985  -13.75296 -15.57407 1.000 94.44621  ? 68  ARG A CZ    1 
ATOM   4400 N  NH1   . ARG B 2 68  ? 32.96027  -12.92059 -15.55849 1.000 77.63175  ? 68  ARG A NH1   1 
ATOM   4401 N  NH2   . ARG B 2 68  ? 35.18649  -13.30285 -15.94235 1.000 99.77393  ? 68  ARG A NH2   1 
ATOM   4402 N  N     . ASP B 2 69  ? 35.32986  -19.91430 -12.85624 1.000 91.09941  ? 69  ASP A N     1 
ATOM   4403 C  CA    . ASP B 2 69  ? 35.87712  -21.05007 -13.59349 1.000 83.70293  ? 69  ASP A CA    1 
ATOM   4404 C  C     . ASP B 2 69  ? 35.18353  -22.35098 -13.20869 1.000 73.60597  ? 69  ASP A C     1 
ATOM   4405 O  O     . ASP B 2 69  ? 34.88798  -23.18303 -14.07428 1.000 80.45423  ? 69  ASP A O     1 
ATOM   4406 C  CB    . ASP B 2 69  ? 37.38451  -21.16105 -13.35704 1.000 84.74312  ? 69  ASP A CB    1 
ATOM   4407 C  CG    . ASP B 2 69  ? 38.19453  -20.38056 -14.37389 1.000 91.22962  ? 69  ASP A CG    1 
ATOM   4408 O  OD1   . ASP B 2 69  ? 37.58517  -19.68133 -15.21003 1.000 95.92098  ? 69  ASP A OD1   1 
ATOM   4409 O  OD2   . ASP B 2 69  ? 39.44127  -20.47195 -14.34268 1.000 98.36540  ? 69  ASP A OD2   1 
ATOM   4410 N  N     . GLN B 2 70  ? 34.91597  -22.54668 -11.91544 1.000 68.18898  ? 70  GLN A N     1 
ATOM   4411 C  CA    . GLN B 2 70  ? 34.30758  -23.79724 -11.47248 1.000 71.53532  ? 70  GLN A CA    1 
ATOM   4412 C  C     . GLN B 2 70  ? 32.87752  -23.93036 -11.98005 1.000 74.41167  ? 70  GLN A C     1 
ATOM   4413 O  O     . GLN B 2 70  ? 32.45794  -25.02068 -12.38691 1.000 76.57239  ? 70  GLN A O     1 
ATOM   4414 C  CB    . GLN B 2 70  ? 34.35082  -23.89387 -9.94726  1.000 77.24818  ? 70  GLN A CB    1 
ATOM   4415 C  CG    . GLN B 2 70  ? 33.66055  -25.12659 -9.37574  1.000 71.18888  ? 70  GLN A CG    1 
ATOM   4416 C  CD    . GLN B 2 70  ? 34.33302  -26.42900 -9.77805  1.000 78.07611  ? 70  GLN A CD    1 
ATOM   4417 O  OE1   . GLN B 2 70  ? 35.46902  -26.43889 -10.25367 1.000 77.67546  ? 70  GLN A OE1   1 
ATOM   4418 N  NE2   . GLN B 2 70  ? 33.62959  -27.53893 -9.58477  1.000 83.72396  ? 70  GLN A NE2   1 
ATOM   4419 N  N     . TYR B 2 71  ? 32.11520  -22.83345 -11.96482 1.000 81.59721  ? 71  TYR A N     1 
ATOM   4420 C  CA    . TYR B 2 71  ? 30.75809  -22.86805 -12.50140 1.000 72.86327  ? 71  TYR A CA    1 
ATOM   4421 C  C     . TYR B 2 71  ? 30.76427  -23.23198 -13.98016 1.000 74.81346  ? 71  TYR A C     1 
ATOM   4422 O  O     . TYR B 2 71  ? 29.96308  -24.06175 -14.42712 1.000 70.77117  ? 71  TYR A O     1 
ATOM   4423 C  CB    . TYR B 2 71  ? 30.07237  -21.51982 -12.27522 1.000 70.54272  ? 71  TYR A CB    1 
ATOM   4424 C  CG    . TYR B 2 71  ? 29.94098  -21.15248 -10.81307 1.000 85.34755  ? 71  TYR A CG    1 
ATOM   4425 C  CD1   . TYR B 2 71  ? 29.68747  -22.12828 -9.85629  1.000 83.63547  ? 71  TYR A CD1   1 
ATOM   4426 C  CD2   . TYR B 2 71  ? 30.08392  -19.83602 -10.38604 1.000 77.78359  ? 71  TYR A CD2   1 
ATOM   4427 C  CE1   . TYR B 2 71  ? 29.57172  -21.80642 -8.51810  1.000 80.44647  ? 71  TYR A CE1   1 
ATOM   4428 C  CE2   . TYR B 2 71  ? 29.97061  -19.50375 -9.04600  1.000 73.94023  ? 71  TYR A CE2   1 
ATOM   4429 C  CZ    . TYR B 2 71  ? 29.71368  -20.49535 -8.11733  1.000 85.23052  ? 71  TYR A CZ    1 
ATOM   4430 O  OH    . TYR B 2 71  ? 29.59731  -20.18251 -6.78196  1.000 86.92598  ? 71  TYR A OH    1 
ATOM   4431 N  N     . MET B 2 72  ? 31.67443  -22.63288 -14.75263 1.000 68.11371  ? 72  MET A N     1 
ATOM   4432 C  CA    . MET B 2 72  ? 31.78606  -22.97670 -16.16492 1.000 61.72585  ? 72  MET A CA    1 
ATOM   4433 C  C     . MET B 2 72  ? 32.24853  -24.41368 -16.36122 1.000 72.66688  ? 72  MET A C     1 
ATOM   4434 O  O     . MET B 2 72  ? 31.91095  -25.03884 -17.37251 1.000 77.26763  ? 72  MET A O     1 
ATOM   4435 C  CB    . MET B 2 72  ? 32.74981  -22.02072 -16.86483 1.000 68.78666  ? 72  MET A CB    1 
ATOM   4436 C  CG    . MET B 2 72  ? 32.29271  -20.57310 -16.90657 1.000 81.18360  ? 72  MET A CG    1 
ATOM   4437 S  SD    . MET B 2 72  ? 33.52273  -19.52744 -17.71006 1.000 85.30336  ? 72  MET A SD    1 
ATOM   4438 C  CE    . MET B 2 72  ? 32.65223  -17.96477 -17.80558 1.000 85.57631  ? 72  MET A CE    1 
ATOM   4439 N  N     . ARG B 2 73  ? 33.01397  -24.95488 -15.41164 1.000 71.89042  ? 73  ARG A N     1 
ATOM   4440 C  CA    . ARG B 2 73  ? 33.58652  -26.28292 -15.59824 1.000 74.65869  ? 73  ARG A CA    1 
ATOM   4441 C  C     . ARG B 2 73  ? 32.51886  -27.37124 -15.56669 1.000 77.04243  ? 73  ARG A C     1 
ATOM   4442 O  O     . ARG B 2 73  ? 32.67124  -28.40647 -16.22618 1.000 77.47292  ? 73  ARG A O     1 
ATOM   4443 C  CB    . ARG B 2 73  ? 34.65464  -26.53698 -14.53475 1.000 74.30039  ? 73  ARG A CB    1 
ATOM   4444 C  CG    . ARG B 2 73  ? 35.51404  -27.76106 -14.78870 1.000 74.95062  ? 73  ARG A CG    1 
ATOM   4445 C  CD    . ARG B 2 73  ? 36.71981  -27.79711 -13.86142 1.000 69.86170  ? 73  ARG A CD    1 
ATOM   4446 N  NE    . ARG B 2 73  ? 37.67321  -26.73163 -14.15031 1.000 73.31507  ? 73  ARG A NE    1 
ATOM   4447 C  CZ    . ARG B 2 73  ? 37.84785  -25.65297 -13.39865 1.000 81.17790  ? 73  ARG A CZ    1 
ATOM   4448 N  NH1   . ARG B 2 73  ? 37.14997  -25.46124 -12.29115 1.000 79.87021  ? 73  ARG A NH1   1 
ATOM   4449 N  NH2   . ARG B 2 73  ? 38.75149  -24.74734 -13.76336 1.000 83.55992  ? 73  ARG A NH2   1 
ATOM   4450 N  N     . THR B 2 74  ? 31.42947  -27.15143 -14.83196 1.000 73.47202  ? 74  THR A N     1 
ATOM   4451 C  CA    . THR B 2 74  ? 30.38366  -28.15654 -14.69305 1.000 73.17008  ? 74  THR A CA    1 
ATOM   4452 C  C     . THR B 2 74  ? 29.26507  -28.01711 -15.71848 1.000 83.36830  ? 74  THR A C     1 
ATOM   4453 O  O     . THR B 2 74  ? 28.50317  -28.97198 -15.91468 1.000 86.47820  ? 74  THR A O     1 
ATOM   4454 C  CB    . THR B 2 74  ? 29.77976  -28.09582 -13.28616 1.000 74.15472  ? 74  THR A CB    1 
ATOM   4455 O  OG1   . THR B 2 74  ? 29.28769  -26.77322 -13.03359 1.000 68.59973  ? 74  THR A OG1   1 
ATOM   4456 C  CG2   . THR B 2 74  ? 30.82822  -28.44807 -12.24093 1.000 77.02221  ? 74  THR A CG2   1 
ATOM   4457 N  N     . GLY B 2 75  ? 29.14607  -26.86558 -16.37460 1.000 75.60553  ? 75  GLY A N     1 
ATOM   4458 C  CA    . GLY B 2 75  ? 28.05081  -26.66298 -17.30201 1.000 67.46319  ? 75  GLY A CA    1 
ATOM   4459 C  C     . GLY B 2 75  ? 28.21633  -27.46499 -18.57869 1.000 66.15561  ? 75  GLY A C     1 
ATOM   4460 O  O     . GLY B 2 75  ? 29.32305  -27.81020 -18.99053 1.000 74.16106  ? 75  GLY A O     1 
ATOM   4461 N  N     . GLU B 2 76  ? 27.08355  -27.76733 -19.21332 1.000 65.82075  ? 76  GLU A N     1 
ATOM   4462 C  CA    . GLU B 2 76  ? 27.07527  -28.45029 -20.50101 1.000 58.36778  ? 76  GLU A CA    1 
ATOM   4463 C  C     . GLU B 2 76  ? 26.74436  -27.52672 -21.66196 1.000 56.29022  ? 76  GLU A C     1 
ATOM   4464 O  O     . GLU B 2 76  ? 27.14885  -27.80317 -22.79571 1.000 71.11581  ? 76  GLU A O     1 
ATOM   4465 C  CB    . GLU B 2 76  ? 26.07206  -29.60651 -20.48550 1.000 61.11001  ? 76  GLU A CB    1 
ATOM   4466 C  CG    . GLU B 2 76  ? 26.22531  -30.54393 -19.30783 1.000 61.61147  ? 76  GLU A CG    1 
ATOM   4467 C  CD    . GLU B 2 76  ? 25.27625  -31.72174 -19.38588 1.000 85.84317  ? 76  GLU A CD    1 
ATOM   4468 O  OE1   . GLU B 2 76  ? 25.25169  -32.39444 -20.44039 1.000 90.17524  ? 76  GLU A OE1   1 
ATOM   4469 O  OE2   . GLU B 2 76  ? 24.54638  -31.96713 -18.40025 1.000 79.72971  ? 76  GLU A OE2   1 
ATOM   4470 N  N     . GLY B 2 77  ? 26.01367  -26.45288 -21.40536 1.000 57.94989  ? 77  GLY A N     1 
ATOM   4471 C  CA    . GLY B 2 77  ? 25.72781  -25.46106 -22.42475 1.000 62.24106  ? 77  GLY A CA    1 
ATOM   4472 C  C     . GLY B 2 77  ? 25.75738  -24.07931 -21.81044 1.000 59.15803  ? 77  GLY A C     1 
ATOM   4473 O  O     . GLY B 2 77  ? 25.51433  -23.90456 -20.61421 1.000 62.00799  ? 77  GLY A O     1 
ATOM   4474 N  N     . PHE B 2 78  ? 26.05981  -23.08791 -22.64443 1.000 55.43068  ? 78  PHE A N     1 
ATOM   4475 C  CA    . PHE B 2 78  ? 26.31697  -21.73916 -22.15939 1.000 58.59980  ? 78  PHE A CA    1 
ATOM   4476 C  C     . PHE B 2 78  ? 25.51812  -20.72495 -22.95983 1.000 58.25334  ? 78  PHE A C     1 
ATOM   4477 O  O     . PHE B 2 78  ? 25.53907  -20.74511 -24.19440 1.000 69.39215  ? 78  PHE A O     1 
ATOM   4478 C  CB    . PHE B 2 78  ? 27.81338  -21.41800 -22.22533 1.000 58.60043  ? 78  PHE A CB    1 
ATOM   4479 C  CG    . PHE B 2 78  ? 28.64896  -22.29032 -21.33563 1.000 62.90546  ? 78  PHE A CG    1 
ATOM   4480 C  CD1   . PHE B 2 78  ? 29.08983  -23.52941 -21.77179 1.000 58.70906  ? 78  PHE A CD1   1 
ATOM   4481 C  CD2   . PHE B 2 78  ? 28.97241  -21.88255 -20.05299 1.000 62.73218  ? 78  PHE A CD2   1 
ATOM   4482 C  CE1   . PHE B 2 78  ? 29.84515  -24.33823 -20.94883 1.000 66.97872  ? 78  PHE A CE1   1 
ATOM   4483 C  CE2   . PHE B 2 78  ? 29.72915  -22.68649 -19.22659 1.000 57.18011  ? 78  PHE A CE2   1 
ATOM   4484 C  CZ    . PHE B 2 78  ? 30.16561  -23.91509 -19.67490 1.000 67.99817  ? 78  PHE A CZ    1 
ATOM   4485 N  N     . LEU B 2 79  ? 24.80859  -19.84997 -22.25075 1.000 52.55554  ? 79  LEU A N     1 
ATOM   4486 C  CA    . LEU B 2 79  ? 24.15109  -18.68979 -22.84569 1.000 61.87079  ? 79  LEU A CA    1 
ATOM   4487 C  C     . LEU B 2 79  ? 25.08572  -17.50157 -22.67191 1.000 65.52144  ? 79  LEU A C     1 
ATOM   4488 O  O     . LEU B 2 79  ? 25.21107  -16.95244 -21.57455 1.000 70.98936  ? 79  LEU A O     1 
ATOM   4489 C  CB    . LEU B 2 79  ? 22.79733  -18.41759 -22.19924 1.000 56.30821  ? 79  LEU A CB    1 
ATOM   4490 C  CG    . LEU B 2 79  ? 21.59193  -19.20192 -22.71005 1.000 53.12354  ? 79  LEU A CG    1 
ATOM   4491 C  CD1   . LEU B 2 79  ? 20.31994  -18.59830 -22.15686 1.000 55.81326  ? 79  LEU A CD1   1 
ATOM   4492 C  CD2   . LEU B 2 79  ? 21.56341  -19.21582 -24.22406 1.000 65.02143  ? 79  LEU A CD2   1 
ATOM   4493 N  N     . CYS B 2 80  ? 25.74805  -17.10896 -23.75378 1.000 61.28255  ? 80  CYS A N     1 
ATOM   4494 C  CA    . CYS B 2 80  ? 26.60946  -15.93405 -23.74533 1.000 62.51749  ? 80  CYS A CA    1 
ATOM   4495 C  C     . CYS B 2 80  ? 25.73979  -14.71759 -24.03693 1.000 59.65701  ? 80  CYS A C     1 
ATOM   4496 O  O     . CYS B 2 80  ? 25.23188  -14.56099 -25.15179 1.000 67.18668  ? 80  CYS A O     1 
ATOM   4497 C  CB    . CYS B 2 80  ? 27.73753  -16.09248 -24.75883 1.000 65.40686  ? 80  CYS A CB    1 
ATOM   4498 S  SG    . CYS B 2 80  ? 28.81788  -17.50474 -24.39579 1.000 71.74696  ? 80  CYS A SG    1 
ATOM   4499 N  N     . VAL B 2 81  ? 25.55659  -13.86624 -23.03052 1.000 54.81288  ? 81  VAL A N     1 
ATOM   4500 C  CA    . VAL B 2 81  ? 24.56601  -12.79789 -23.06548 1.000 62.73797  ? 81  VAL A CA    1 
ATOM   4501 C  C     . VAL B 2 81  ? 25.27028  -11.44945 -23.10637 1.000 72.70860  ? 81  VAL A C     1 
ATOM   4502 O  O     . VAL B 2 81  ? 26.26994  -11.23492 -22.41050 1.000 79.27276  ? 81  VAL A O     1 
ATOM   4503 C  CB    . VAL B 2 81  ? 23.61826  -12.87463 -21.85154 1.000 65.70862  ? 81  VAL A CB    1 
ATOM   4504 C  CG1   . VAL B 2 81  ? 22.44339  -11.92414 -22.03150 1.000 66.42161  ? 81  VAL A CG1   1 
ATOM   4505 C  CG2   . VAL B 2 81  ? 23.13578  -14.30199 -21.62989 1.000 54.39502  ? 81  VAL A CG2   1 
ATOM   4506 N  N     . PHE B 2 82  ? 24.74083  -10.54104 -23.92465 1.000 70.47575  ? 82  PHE A N     1 
ATOM   4507 C  CA    . PHE B 2 82  ? 25.14026  -9.14191  -23.92063 1.000 67.73593  ? 82  PHE A CA    1 
ATOM   4508 C  C     . PHE B 2 82  ? 23.89154  -8.28604  -24.08076 1.000 71.25547  ? 82  PHE A C     1 
ATOM   4509 O  O     . PHE B 2 82  ? 22.84693  -8.75883  -24.53590 1.000 67.87945  ? 82  PHE A O     1 
ATOM   4510 C  CB    . PHE B 2 82  ? 26.15542  -8.82806  -25.03268 1.000 71.52841  ? 82  PHE A CB    1 
ATOM   4511 C  CG    . PHE B 2 82  ? 25.58410  -8.91324  -26.41982 1.000 74.07190  ? 82  PHE A CG    1 
ATOM   4512 C  CD1   . PHE B 2 82  ? 25.56714  -10.11703 -27.10345 1.000 81.91727  ? 82  PHE A CD1   1 
ATOM   4513 C  CD2   . PHE B 2 82  ? 25.06765  -7.78735  -27.04313 1.000 80.15608  ? 82  PHE A CD2   1 
ATOM   4514 C  CE1   . PHE B 2 82  ? 25.03892  -10.19835 -28.38099 1.000 82.26653  ? 82  PHE A CE1   1 
ATOM   4515 C  CE2   . PHE B 2 82  ? 24.53851  -7.86286  -28.31820 1.000 78.41678  ? 82  PHE A CE2   1 
ATOM   4516 C  CZ    . PHE B 2 82  ? 24.52490  -9.06914  -28.98796 1.000 73.07723  ? 82  PHE A CZ    1 
ATOM   4517 N  N     . ALA B 2 83  ? 24.00584  -7.01667  -23.70043 1.000 77.81557  ? 83  ALA A N     1 
ATOM   4518 C  CA    . ALA B 2 83  ? 22.92167  -6.05461  -23.85560 1.000 79.00180  ? 83  ALA A CA    1 
ATOM   4519 C  C     . ALA B 2 83  ? 23.16011  -5.22762  -25.11234 1.000 79.63255  ? 83  ALA A C     1 
ATOM   4520 O  O     . ALA B 2 83  ? 24.28089  -4.76812  -25.35331 1.000 84.13662  ? 83  ALA A O     1 
ATOM   4521 C  CB    . ALA B 2 83  ? 22.81280  -5.14664  -22.62991 1.000 75.66902  ? 83  ALA A CB    1 
ATOM   4522 N  N     . ILE B 2 84  ? 22.10659  -5.03975  -25.91223 1.000 82.01639  ? 84  ILE A N     1 
ATOM   4523 C  CA    . ILE B 2 84  ? 22.25203  -4.33391  -27.18157 1.000 84.80935  ? 84  ILE A CA    1 
ATOM   4524 C  C     . ILE B 2 84  ? 22.49332  -2.84361  -27.00851 1.000 87.18948  ? 84  ILE A C     1 
ATOM   4525 O  O     . ILE B 2 84  ? 22.80479  -2.16135  -27.99010 1.000 90.73610  ? 84  ILE A O     1 
ATOM   4526 C  CB    . ILE B 2 84  ? 21.01714  -4.53612  -28.08254 1.000 82.80337  ? 84  ILE A CB    1 
ATOM   4527 C  CG1   . ILE B 2 84  ? 19.79336  -3.85844  -27.46927 1.000 81.83890  ? 84  ILE A CG1   1 
ATOM   4528 C  CG2   . ILE B 2 84  ? 20.75836  -6.01552  -28.31318 1.000 73.15974  ? 84  ILE A CG2   1 
ATOM   4529 C  CD1   . ILE B 2 84  ? 18.59134  -3.86798  -28.37211 1.000 94.52131  ? 84  ILE A CD1   1 
ATOM   4530 N  N     . ASN B 2 85  ? 22.34816  -2.31586  -25.79235 1.000 87.60437  ? 85  ASN A N     1 
ATOM   4531 C  CA    . ASN B 2 85  ? 22.65393  -0.92094  -25.50279 1.000 85.63774  ? 85  ASN A CA    1 
ATOM   4532 C  C     . ASN B 2 85  ? 23.94573  -0.77592  -24.70634 1.000 83.90275  ? 85  ASN A C     1 
ATOM   4533 O  O     . ASN B 2 85  ? 24.14942  0.24076   -24.03592 1.000 90.67817  ? 85  ASN A O     1 
ATOM   4534 C  CB    . ASN B 2 85  ? 21.48970  -0.25888  -24.76279 1.000 88.15570  ? 85  ASN A CB    1 
ATOM   4535 C  CG    . ASN B 2 85  ? 21.29465  -0.80573  -23.35904 1.000 88.93311  ? 85  ASN A CG    1 
ATOM   4536 O  OD1   . ASN B 2 85  ? 21.61238  -1.96192  -23.07652 1.000 93.62675  ? 85  ASN A OD1   1 
ATOM   4537 N  ND2   . ASN B 2 85  ? 20.76501  0.02770   -22.47114 1.000 87.64172  ? 85  ASN A ND2   1 
ATOM   4538 N  N     . ASN B 2 86  ? 24.82411  -1.77599  -24.77249 1.000 85.46387  ? 86  ASN A N     1 
ATOM   4539 C  CA    . ASN B 2 86  ? 26.08219  -1.78221  -24.02534 1.000 86.61569  ? 86  ASN A CA    1 
ATOM   4540 C  C     . ASN B 2 86  ? 27.14054  -2.40570  -24.93034 1.000 86.28282  ? 86  ASN A C     1 
ATOM   4541 O  O     . ASN B 2 86  ? 27.27950  -3.63101  -24.98151 1.000 85.88621  ? 86  ASN A O     1 
ATOM   4542 C  CB    . ASN B 2 86  ? 25.93657  -2.54529  -22.71311 1.000 88.00740  ? 86  ASN A CB    1 
ATOM   4543 C  CG    . ASN B 2 86  ? 27.22135  -2.58272  -21.90766 1.000 81.92917  ? 86  ASN A CG    1 
ATOM   4544 O  OD1   . ASN B 2 86  ? 28.19632  -1.90603  -22.23293 1.000 81.73153  ? 86  ASN A OD1   1 
ATOM   4545 N  ND2   . ASN B 2 86  ? 27.22341  -3.37290  -20.84130 1.000 72.67460  ? 86  ASN A ND2   1 
ATOM   4546 N  N     . SER B 2 87  ? 27.88523  -1.55642  -25.64162 1.000 90.43483  ? 87  SER A N     1 
ATOM   4547 C  CA    . SER B 2 87  ? 28.87417  -2.05981  -26.58834 1.000 93.07244  ? 87  SER A CA    1 
ATOM   4548 C  C     . SER B 2 87  ? 30.02715  -2.76394  -25.88449 1.000 93.31406  ? 87  SER A C     1 
ATOM   4549 O  O     . SER B 2 87  ? 30.66484  -3.64339  -26.47543 1.000 91.23097  ? 87  SER A O     1 
ATOM   4550 C  CB    . SER B 2 87  ? 29.39695  -0.91728  -27.45842 1.000 97.82045  ? 87  SER A CB    1 
ATOM   4551 O  OG    . SER B 2 87  ? 28.35045  -0.34279  -28.22284 1.000 93.86713  ? 87  SER A OG    1 
ATOM   4552 N  N     . LYS B 2 88  ? 30.31069  -2.39796  -24.63202 1.000 91.19668  ? 88  LYS A N     1 
ATOM   4553 C  CA    . LYS B 2 88  ? 31.37110  -3.07695  -23.89438 1.000 92.03588  ? 88  LYS A CA    1 
ATOM   4554 C  C     . LYS B 2 88  ? 31.01638  -4.53720  -23.64032 1.000 94.73459  ? 88  LYS A C     1 
ATOM   4555 O  O     . LYS B 2 88  ? 31.88647  -5.41337  -23.71033 1.000 91.52249  ? 88  LYS A O     1 
ATOM   4556 C  CB    . LYS B 2 88  ? 31.64498  -2.35308  -22.57604 1.000 90.88454  ? 88  LYS A CB    1 
ATOM   4557 C  CG    . LYS B 2 88  ? 32.72675  -3.00301  -21.72399 1.000 97.81801  ? 88  LYS A CG    1 
ATOM   4558 C  CD    . LYS B 2 88  ? 34.01523  -2.20291  -21.75414 1.000 101.44546 ? 88  LYS A CD    1 
ATOM   4559 C  CE    . LYS B 2 88  ? 33.81311  -0.82529  -21.14211 1.000 117.78327 ? 88  LYS A CE    1 
ATOM   4560 N  NZ    . LYS B 2 88  ? 35.07060  -0.02864  -21.12163 1.000 117.61495 ? 88  LYS A NZ    1 
ATOM   4561 N  N     . SER B 2 89  ? 29.74127  -4.81976  -23.35293 1.000 93.95823  ? 89  SER A N     1 
ATOM   4562 C  CA    . SER B 2 89  ? 29.32929  -6.19616  -23.09433 1.000 90.56610  ? 89  SER A CA    1 
ATOM   4563 C  C     . SER B 2 89  ? 29.43237  -7.06110  -24.34409 1.000 83.04544  ? 89  SER A C     1 
ATOM   4564 O  O     . SER B 2 89  ? 29.75552  -8.25023  -24.24686 1.000 86.11097  ? 89  SER A O     1 
ATOM   4565 C  CB    . SER B 2 89  ? 27.90332  -6.22867  -22.53945 1.000 78.50182  ? 89  SER A CB    1 
ATOM   4566 O  OG    . SER B 2 89  ? 26.96940  -5.71242  -23.47034 1.000 73.40321  ? 89  SER A OG    1 
ATOM   4567 N  N     . PHE B 2 90  ? 29.16686  -6.49012  -25.52067 1.000 86.34013  ? 90  PHE A N     1 
ATOM   4568 C  CA    . PHE B 2 90  ? 29.30085  -7.25968  -26.75237 1.000 87.97742  ? 90  PHE A CA    1 
ATOM   4569 C  C     . PHE B 2 90  ? 30.76294  -7.49367  -27.10974 1.000 82.89846  ? 90  PHE A C     1 
ATOM   4570 O  O     . PHE B 2 90  ? 31.09667  -8.52849  -27.69773 1.000 89.55473  ? 90  PHE A O     1 
ATOM   4571 C  CB    . PHE B 2 90  ? 28.57123  -6.55496  -27.89712 1.000 88.26129  ? 90  PHE A CB    1 
ATOM   4572 C  CG    . PHE B 2 90  ? 28.70714  -7.25000  -29.22506 1.000 92.59477  ? 90  PHE A CG    1 
ATOM   4573 C  CD1   . PHE B 2 90  ? 28.13453  -8.49497  -29.43398 1.000 84.90378  ? 90  PHE A CD1   1 
ATOM   4574 C  CD2   . PHE B 2 90  ? 29.39917  -6.65310  -30.26759 1.000 86.03454  ? 90  PHE A CD2   1 
ATOM   4575 C  CE1   . PHE B 2 90  ? 28.25696  -9.13425  -30.65521 1.000 86.61943  ? 90  PHE A CE1   1 
ATOM   4576 C  CE2   . PHE B 2 90  ? 29.52243  -7.28602  -31.48959 1.000 85.02617  ? 90  PHE A CE2   1 
ATOM   4577 C  CZ    . PHE B 2 90  ? 28.95090  -8.52738  -31.68426 1.000 84.26988  ? 90  PHE A CZ    1 
ATOM   4578 N  N     . ALA B 2 91  ? 31.64665  -6.55387  -26.76656 1.000 83.86772  ? 91  ALA A N     1 
ATOM   4579 C  CA    . ALA B 2 91  ? 33.07087  -6.77937  -26.98444 1.000 87.22664  ? 91  ALA A CA    1 
ATOM   4580 C  C     . ALA B 2 91  ? 33.60346  -7.88107  -26.07919 1.000 85.98927  ? 91  ALA A C     1 
ATOM   4581 O  O     . ALA B 2 91  ? 34.48727  -8.64384  -26.48571 1.000 88.27119  ? 91  ALA A O     1 
ATOM   4582 C  CB    . ALA B 2 91  ? 33.85049  -5.48382  -26.76257 1.000 83.27308  ? 91  ALA A CB    1 
ATOM   4583 N  N     . ASP B 2 92  ? 33.07028  -7.98709  -24.85995 1.000 96.59226  ? 92  ASP A N     1 
ATOM   4584 C  CA    . ASP B 2 92  ? 33.49439  -9.01287  -23.91554 1.000 97.40830  ? 92  ASP A CA    1 
ATOM   4585 C  C     . ASP B 2 92  ? 33.06157  -10.41365 -24.32438 1.000 92.92672  ? 92  ASP A C     1 
ATOM   4586 O  O     . ASP B 2 92  ? 33.53085  -11.38304 -23.71863 1.000 97.41212  ? 92  ASP A O     1 
ATOM   4587 C  CB    . ASP B 2 92  ? 32.94351  -8.70482  -22.52084 1.000 95.89148  ? 92  ASP A CB    1 
ATOM   4588 C  CG    . ASP B 2 92  ? 33.43676  -7.37838  -21.97358 1.000 104.63928 ? 92  ASP A CG    1 
ATOM   4589 O  OD1   . ASP B 2 92  ? 34.28642  -6.73560  -22.62698 1.000 99.91227  ? 92  ASP A OD1   1 
ATOM   4590 O  OD2   . ASP B 2 92  ? 32.96841  -6.97700  -20.88673 1.000 108.65952 ? 92  ASP A OD2   1 
ATOM   4591 N  N     . ILE B 2 93  ? 32.18518  -10.54135 -25.32488 1.000 85.93458  ? 93  ILE A N     1 
ATOM   4592 C  CA    . ILE B 2 93  ? 31.66254  -11.85157 -25.70659 1.000 76.75706  ? 93  ILE A CA    1 
ATOM   4593 C  C     . ILE B 2 93  ? 32.79609  -12.79676 -26.08486 1.000 86.87663  ? 93  ILE A C     1 
ATOM   4594 O  O     . ILE B 2 93  ? 32.79236  -13.97503 -25.70702 1.000 88.02878  ? 93  ILE A O     1 
ATOM   4595 C  CB    . ILE B 2 93  ? 30.64020  -11.70628 -26.84898 1.000 75.36149  ? 93  ILE A CB    1 
ATOM   4596 C  CG1   . ILE B 2 93  ? 29.37895  -11.00121 -26.35085 1.000 80.58262  ? 93  ILE A CG1   1 
ATOM   4597 C  CG2   . ILE B 2 93  ? 30.28751  -13.06385 -27.42977 1.000 70.22943  ? 93  ILE A CG2   1 
ATOM   4598 C  CD1   . ILE B 2 93  ? 28.59735  -11.80035 -25.33131 1.000 83.52056  ? 93  ILE A CD1   1 
ATOM   4599 N  N     . ASN B 2 94  ? 33.79056  -12.29972 -26.82345 1.000 80.78070  ? 94  ASN A N     1 
ATOM   4600 C  CA    . ASN B 2 94  ? 34.89588  -13.16857 -27.20985 1.000 82.67444  ? 94  ASN A CA    1 
ATOM   4601 C  C     . ASN B 2 94  ? 35.71568  -13.60999 -26.00398 1.000 80.96777  ? 94  ASN A C     1 
ATOM   4602 O  O     . ASN B 2 94  ? 36.30349  -14.69731 -26.02303 1.000 85.15037  ? 94  ASN A O     1 
ATOM   4603 C  CB    . ASN B 2 94  ? 35.79299  -12.47565 -28.23092 1.000 74.57643  ? 94  ASN A CB    1 
ATOM   4604 C  CG    . ASN B 2 94  ? 36.90724  -13.37675 -28.71854 1.000 88.74996  ? 94  ASN A CG    1 
ATOM   4605 O  OD1   . ASN B 2 94  ? 36.71609  -14.17874 -29.63266 1.000 94.59030  ? 94  ASN A OD1   1 
ATOM   4606 N  ND2   . ASN B 2 94  ? 38.07587  -13.26263 -28.09838 1.000 87.00299  ? 94  ASN A ND2   1 
ATOM   4607 N  N     . LEU B 2 95  ? 35.76673  -12.79193 -24.95039 1.000 82.20041  ? 95  LEU A N     1 
ATOM   4608 C  CA    . LEU B 2 95  ? 36.49039  -13.19394 -23.74899 1.000 76.34567  ? 95  LEU A CA    1 
ATOM   4609 C  C     . LEU B 2 95  ? 35.79749  -14.35662 -23.05162 1.000 76.97842  ? 95  LEU A C     1 
ATOM   4610 O  O     . LEU B 2 95  ? 36.45773  -15.29994 -22.59956 1.000 77.73476  ? 95  LEU A O     1 
ATOM   4611 C  CB    . LEU B 2 95  ? 36.63484  -12.00927 -22.79431 1.000 80.38573  ? 95  LEU A CB    1 
ATOM   4612 C  CG    . LEU B 2 95  ? 37.54086  -10.86253 -23.24498 1.000 87.12354  ? 95  LEU A CG    1 
ATOM   4613 C  CD1   . LEU B 2 95  ? 37.74521  -9.87362  -22.10848 1.000 78.30361  ? 95  LEU A CD1   1 
ATOM   4614 C  CD2   . LEU B 2 95  ? 38.87411  -11.39156 -23.75055 1.000 75.34385  ? 95  LEU A CD2   1 
ATOM   4615 N  N     . TYR B 2 96  ? 34.46676  -14.31056 -22.96018 1.000 82.72697  ? 96  TYR A N     1 
ATOM   4616 C  CA    . TYR B 2 96  ? 33.73736  -15.37529 -22.27909 1.000 76.51523  ? 96  TYR A CA    1 
ATOM   4617 C  C     . TYR B 2 96  ? 33.82781  -16.69130 -23.04246 1.000 74.47666  ? 96  TYR A C     1 
ATOM   4618 O  O     . TYR B 2 96  ? 33.94827  -17.75875 -22.43050 1.000 71.87180  ? 96  TYR A O     1 
ATOM   4619 C  CB    . TYR B 2 96  ? 32.28035  -14.96235 -22.07023 1.000 61.77515  ? 96  TYR A CB    1 
ATOM   4620 C  CG    . TYR B 2 96  ? 32.10462  -13.93873 -20.97034 1.000 68.48180  ? 96  TYR A CG    1 
ATOM   4621 C  CD1   . TYR B 2 96  ? 32.03917  -14.32908 -19.63992 1.000 74.16586  ? 96  TYR A CD1   1 
ATOM   4622 C  CD2   . TYR B 2 96  ? 32.01362  -12.58405 -21.25951 1.000 71.51621  ? 96  TYR A CD2   1 
ATOM   4623 C  CE1   . TYR B 2 96  ? 31.88376  -13.40132 -18.62868 1.000 73.29845  ? 96  TYR A CE1   1 
ATOM   4624 C  CE2   . TYR B 2 96  ? 31.85896  -11.64692 -20.25338 1.000 71.10380  ? 96  TYR A CE2   1 
ATOM   4625 C  CZ    . TYR B 2 96  ? 31.79497  -12.06210 -18.94018 1.000 73.15315  ? 96  TYR A CZ    1 
ATOM   4626 O  OH    . TYR B 2 96  ? 31.64048  -11.13704 -17.93231 1.000 75.42303  ? 96  TYR A OH    1 
ATOM   4627 N  N     . ARG B 2 97  ? 33.78481  -16.63934 -24.37698 1.000 74.10422  ? 97  ARG A N     1 
ATOM   4628 C  CA    . ARG B 2 97  ? 33.87699  -17.87028 -25.15647 1.000 75.52307  ? 97  ARG A CA    1 
ATOM   4629 C  C     . ARG B 2 97  ? 35.24061  -18.52899 -24.99376 1.000 81.45919  ? 97  ARG A C     1 
ATOM   4630 O  O     . ARG B 2 97  ? 35.33183  -19.75584 -24.86882 1.000 85.98042  ? 97  ARG A O     1 
ATOM   4631 C  CB    . ARG B 2 97  ? 33.59477  -17.59447 -26.63328 1.000 75.32060  ? 97  ARG A CB    1 
ATOM   4632 C  CG    . ARG B 2 97  ? 33.68476  -18.84498 -27.50067 1.000 82.98695  ? 97  ARG A CG    1 
ATOM   4633 C  CD    . ARG B 2 97  ? 33.19296  -18.60076 -28.91442 1.000 89.08721  ? 97  ARG A CD    1 
ATOM   4634 N  NE    . ARG B 2 97  ? 32.99322  -19.84959 -29.64105 1.000 98.37072  ? 97  ARG A NE    1 
ATOM   4635 C  CZ    . ARG B 2 97  ? 33.89850  -20.41590 -30.42762 1.000 110.84921 ? 97  ARG A CZ    1 
ATOM   4636 N  NH1   . ARG B 2 97  ? 35.08560  -19.86413 -30.62613 1.000 105.22288 ? 97  ARG A NH1   1 
ATOM   4637 N  NH2   . ARG B 2 97  ? 33.60486  -21.56432 -31.03170 1.000 113.27853 ? 97  ARG A NH2   1 
ATOM   4638 N  N     . GLU B 2 98  ? 36.31178  -17.73360 -24.99351 1.000 80.09862  ? 98  GLU A N     1 
ATOM   4639 C  CA    . GLU B 2 98  ? 37.64552  -18.30378 -24.83947 1.000 80.91319  ? 98  GLU A CA    1 
ATOM   4640 C  C     . GLU B 2 98  ? 37.85254  -18.85002 -23.43245 1.000 73.69689  ? 98  GLU A C     1 
ATOM   4641 O  O     . GLU B 2 98  ? 38.50696  -19.88363 -23.25256 1.000 77.99605  ? 98  GLU A O     1 
ATOM   4642 C  CB    . GLU B 2 98  ? 38.70398  -17.25707 -25.18512 1.000 83.53771  ? 98  GLU A CB    1 
ATOM   4643 C  CG    . GLU B 2 98  ? 38.74155  -16.90033 -26.66562 1.000 82.70352  ? 98  GLU A CG    1 
ATOM   4644 C  CD    . GLU B 2 98  ? 39.13074  -18.08327 -27.53658 1.000 101.20045 ? 98  GLU A CD    1 
ATOM   4645 O  OE1   . GLU B 2 98  ? 40.03257  -18.84880 -27.13140 1.000 101.23499 ? 98  GLU A OE1   1 
ATOM   4646 O  OE2   . GLU B 2 98  ? 38.53234  -18.25236 -28.62105 1.000 100.87751 ? 98  GLU A OE2   1 
ATOM   4647 N  N     . GLN B 2 99  ? 37.29314  -18.17928 -22.42296 1.000 75.97765  ? 99  GLN A N     1 
ATOM   4648 C  CA    . GLN B 2 99  ? 37.37071  -18.70548 -21.06419 1.000 79.48923  ? 99  GLN A CA    1 
ATOM   4649 C  C     . GLN B 2 99  ? 36.60514  -20.01875 -20.93931 1.000 80.80044  ? 99  GLN A C     1 
ATOM   4650 O  O     . GLN B 2 99  ? 37.03623  -20.92830 -20.22130 1.000 80.08991  ? 99  GLN A O     1 
ATOM   4651 C  CB    . GLN B 2 99  ? 36.84341  -17.67296 -20.06771 1.000 74.19688  ? 99  GLN A CB    1 
ATOM   4652 C  CG    . GLN B 2 99  ? 37.08459  -18.04678 -18.61316 1.000 86.93442  ? 99  GLN A CG    1 
ATOM   4653 C  CD    . GLN B 2 99  ? 36.52647  -17.02437 -17.64165 1.000 93.38305  ? 99  GLN A CD    1 
ATOM   4654 O  OE1   . GLN B 2 99  ? 35.88231  -16.05282 -18.04142 1.000 86.53454  ? 99  GLN A OE1   1 
ATOM   4655 N  NE2   . GLN B 2 99  ? 36.77304  -17.23911 -16.35484 1.000 95.59971  ? 99  GLN A NE2   1 
ATOM   4656 N  N     . ILE B 2 100 ? 35.47451  -20.14104 -21.64027 1.000 71.07982  ? 100 ILE A N     1 
ATOM   4657 C  CA    . ILE B 2 100 ? 34.72223  -21.39267 -21.62645 1.000 78.92362  ? 100 ILE A CA    1 
ATOM   4658 C  C     . ILE B 2 100 ? 35.50421  -22.49622 -22.32816 1.000 77.14881  ? 100 ILE A C     1 
ATOM   4659 O  O     . ILE B 2 100 ? 35.60430  -23.62160 -21.82410 1.000 78.71651  ? 100 ILE A O     1 
ATOM   4660 C  CB    . ILE B 2 100 ? 33.33357  -21.19307 -22.26369 1.000 80.42378  ? 100 ILE A CB    1 
ATOM   4661 C  CG1   . ILE B 2 100 ? 32.44241  -20.33461 -21.36480 1.000 75.58607  ? 100 ILE A CG1   1 
ATOM   4662 C  CG2   . ILE B 2 100 ? 32.66902  -22.53415 -22.53179 1.000 74.71435  ? 100 ILE A CG2   1 
ATOM   4663 C  CD1   . ILE B 2 100 ? 31.16647  -19.87457 -22.04006 1.000 71.54699  ? 100 ILE A CD1   1 
ATOM   4664 N  N     . LYS B 2 101 ? 36.07610  -22.19301 -23.49660 1.000 79.59252  ? 101 LYS A N     1 
ATOM   4665 C  CA    . LYS B 2 101 ? 36.79752  -23.21023 -24.25508 1.000 80.59073  ? 101 LYS A CA    1 
ATOM   4666 C  C     . LYS B 2 101 ? 38.00203  -23.74686 -23.49004 1.000 87.82119  ? 101 LYS A C     1 
ATOM   4667 O  O     . LYS B 2 101 ? 38.38278  -24.90764 -23.67670 1.000 91.22950  ? 101 LYS A O     1 
ATOM   4668 C  CB    . LYS B 2 101 ? 37.23575  -22.64636 -25.60727 1.000 77.71602  ? 101 LYS A CB    1 
ATOM   4669 C  CG    . LYS B 2 101 ? 36.08789  -22.39895 -26.57676 1.000 88.79342  ? 101 LYS A CG    1 
ATOM   4670 C  CD    . LYS B 2 101 ? 36.51914  -21.52757 -27.75145 1.000 103.30019 ? 101 LYS A CD    1 
ATOM   4671 C  CE    . LYS B 2 101 ? 37.70586  -22.12532 -28.49192 1.000 107.21773 ? 101 LYS A CE    1 
ATOM   4672 N  NZ    . LYS B 2 101 ? 38.22205  -21.21140 -29.54921 1.000 92.86837  ? 101 LYS A NZ    1 
ATOM   4673 N  N     . ARG B 2 102 ? 38.61015  -22.93502 -22.62274 1.000 79.77699  ? 102 ARG A N     1 
ATOM   4674 C  CA    . ARG B 2 102 ? 39.78689  -23.40472 -21.90080 1.000 85.76147  ? 102 ARG A CA    1 
ATOM   4675 C  C     . ARG B 2 102 ? 39.42759  -24.16401 -20.62642 1.000 88.48854  ? 102 ARG A C     1 
ATOM   4676 O  O     . ARG B 2 102 ? 40.11435  -25.12928 -20.27311 1.000 102.35944 ? 102 ARG A O     1 
ATOM   4677 C  CB    . ARG B 2 102 ? 40.72627  -22.23685 -21.57738 1.000 94.37951  ? 102 ARG A CB    1 
ATOM   4678 C  CG    . ARG B 2 102 ? 40.18050  -21.21203 -20.59781 1.000 99.71947  ? 102 ARG A CG    1 
ATOM   4679 C  CD    . ARG B 2 102 ? 41.27305  -20.26115 -20.12112 1.000 97.58697  ? 102 ARG A CD    1 
ATOM   4680 N  NE    . ARG B 2 102 ? 40.75163  -19.24295 -19.21585 1.000 110.05248 ? 102 ARG A NE    1 
ATOM   4681 C  CZ    . ARG B 2 102 ? 40.67621  -19.37602 -17.89798 1.000 110.72904 ? 102 ARG A CZ    1 
ATOM   4682 N  NH1   . ARG B 2 102 ? 41.09555  -20.47294 -17.28800 1.000 105.63639 ? 102 ARG A NH1   1 
ATOM   4683 N  NH2   . ARG B 2 102 ? 40.16615  -18.38370 -17.17359 1.000 107.63381 ? 102 ARG A NH2   1 
ATOM   4684 N  N     . VAL B 2 103 ? 38.36490  -23.76319 -19.92528 1.000 83.31765  ? 103 VAL A N     1 
ATOM   4685 C  CA    . VAL B 2 103 ? 37.99724  -24.48741 -18.71163 1.000 84.42933  ? 103 VAL A CA    1 
ATOM   4686 C  C     . VAL B 2 103 ? 37.33676  -25.81799 -19.05253 1.000 77.75332  ? 103 VAL A C     1 
ATOM   4687 O  O     . VAL B 2 103 ? 37.49146  -26.79723 -18.31416 1.000 76.15817  ? 103 VAL A O     1 
ATOM   4688 C  CB    . VAL B 2 103 ? 37.09841  -23.62587 -17.80620 1.000 78.33122  ? 103 VAL A CB    1 
ATOM   4689 C  CG1   . VAL B 2 103 ? 37.81892  -22.34759 -17.40726 1.000 83.08569  ? 103 VAL A CG1   1 
ATOM   4690 C  CG2   . VAL B 2 103 ? 35.77817  -23.31009 -18.49171 1.000 86.26533  ? 103 VAL A CG2   1 
ATOM   4691 N  N     . LYS B 2 104 ? 36.59976  -25.88434 -20.16110 1.000 74.94465  ? 104 LYS A N     1 
ATOM   4692 C  CA    . LYS B 2 104 ? 36.06237  -27.15244 -20.63207 1.000 85.84117  ? 104 LYS A CA    1 
ATOM   4693 C  C     . LYS B 2 104 ? 37.08512  -27.95246 -21.42432 1.000 90.51511  ? 104 LYS A C     1 
ATOM   4694 O  O     . LYS B 2 104 ? 36.87392  -29.15101 -21.64144 1.000 99.64865  ? 104 LYS A O     1 
ATOM   4695 C  CB    . LYS B 2 104 ? 34.81311  -26.91747 -21.48959 1.000 86.79286  ? 104 LYS A CB    1 
ATOM   4696 C  CG    . LYS B 2 104 ? 33.67560  -26.19582 -20.77250 1.000 75.66655  ? 104 LYS A CG    1 
ATOM   4697 C  CD    . LYS B 2 104 ? 33.04504  -27.06092 -19.69281 1.000 71.74733  ? 104 LYS A CD    1 
ATOM   4698 C  CE    . LYS B 2 104 ? 32.27242  -28.22208 -20.29122 1.000 63.33743  ? 104 LYS A CE    1 
ATOM   4699 N  NZ    . LYS B 2 104 ? 31.68383  -29.08564 -19.23165 1.000 70.43286  ? 104 LYS A NZ    1 
ATOM   4700 N  N     . ASP B 2 105 ? 38.18009  -27.31857 -21.84667 1.000 80.21247  ? 105 ASP A N     1 
ATOM   4701 C  CA    . ASP B 2 105 ? 39.24682  -27.97562 -22.59879 1.000 85.48994  ? 105 ASP A CA    1 
ATOM   4702 C  C     . ASP B 2 105 ? 38.68893  -28.66147 -23.84359 1.000 95.81538  ? 105 ASP A C     1 
ATOM   4703 O  O     . ASP B 2 105 ? 38.98767  -29.82062 -24.14024 1.000 96.40773  ? 105 ASP A O     1 
ATOM   4704 C  CB    . ASP B 2 105 ? 40.00843  -28.96316 -21.71462 1.000 97.44809  ? 105 ASP A CB    1 
ATOM   4705 C  CG    . ASP B 2 105 ? 41.34956  -29.35372 -22.30012 1.000 105.48056 ? 105 ASP A CG    1 
ATOM   4706 O  OD1   . ASP B 2 105 ? 42.18189  -28.45076 -22.53552 1.000 110.14429 ? 105 ASP A OD1   1 
ATOM   4707 O  OD2   . ASP B 2 105 ? 41.57367  -30.56319 -22.51806 1.000 106.59269 ? 105 ASP A OD2   1 
ATOM   4708 N  N     . SER B 2 106 ? 37.85452  -27.92541 -24.57334 1.000 93.23682  ? 106 SER A N     1 
ATOM   4709 C  CA    . SER B 2 106 ? 37.21202  -28.44787 -25.76729 1.000 90.61590  ? 106 SER A CA    1 
ATOM   4710 C  C     . SER B 2 106 ? 37.04059  -27.32104 -26.77188 1.000 89.05526  ? 106 SER A C     1 
ATOM   4711 O  O     . SER B 2 106 ? 36.90617  -26.15220 -26.39941 1.000 85.05372  ? 106 SER A O     1 
ATOM   4712 C  CB    . SER B 2 106 ? 35.85335  -29.08051 -25.44660 1.000 88.06905  ? 106 SER A CB    1 
ATOM   4713 O  OG    . SER B 2 106 ? 35.19694  -29.49286 -26.63275 1.000 99.42823  ? 106 SER A OG    1 
ATOM   4714 N  N     . ASP B 2 107 ? 37.04802  -27.68600 -28.05315 1.000 92.63418  ? 107 ASP A N     1 
ATOM   4715 C  CA    . ASP B 2 107 ? 36.84193  -26.70837 -29.11326 1.000 95.04728  ? 107 ASP A CA    1 
ATOM   4716 C  C     . ASP B 2 107 ? 35.36325  -26.47665 -29.40217 1.000 94.71817  ? 107 ASP A C     1 
ATOM   4717 O  O     . ASP B 2 107 ? 34.94270  -25.32687 -29.56956 1.000 97.55100  ? 107 ASP A O     1 
ATOM   4718 C  CB    . ASP B 2 107 ? 37.55866  -27.14744 -30.39176 1.000 101.99415 ? 107 ASP A CB    1 
ATOM   4719 C  CG    . ASP B 2 107 ? 37.61763  -26.04322 -31.43020 1.000 123.91250 ? 107 ASP A CG    1 
ATOM   4720 O  OD1   . ASP B 2 107 ? 37.36562  -24.87371 -31.06741 1.000 118.82155 ? 107 ASP A OD1   1 
ATOM   4721 O  OD2   . ASP B 2 107 ? 37.90810  -26.34300 -32.60821 1.000 133.21464 ? 107 ASP A OD2   1 
ATOM   4722 N  N     . ASP B 2 108 ? 34.56141  -27.53933 -29.46704 1.000 93.02650  ? 108 ASP A N     1 
ATOM   4723 C  CA    . ASP B 2 108 ? 33.12023  -27.41074 -29.64452 1.000 97.92538  ? 108 ASP A CA    1 
ATOM   4724 C  C     . ASP B 2 108 ? 32.44075  -27.56490 -28.28633 1.000 87.47671  ? 108 ASP A C     1 
ATOM   4725 O  O     . ASP B 2 108 ? 32.53034  -28.61923 -27.64705 1.000 81.65995  ? 108 ASP A O     1 
ATOM   4726 C  CB    . ASP B 2 108 ? 32.57728  -28.41939 -30.66392 1.000 98.66610  ? 108 ASP A CB    1 
ATOM   4727 C  CG    . ASP B 2 108 ? 32.55201  -29.84350 -30.13967 1.000 101.65396 ? 108 ASP A CG    1 
ATOM   4728 O  OD1   . ASP B 2 108 ? 33.58107  -30.30023 -29.59634 1.000 102.05011 ? 108 ASP A OD1   1 
ATOM   4729 O  OD2   . ASP B 2 108 ? 31.49420  -30.50012 -30.25888 1.000 85.49409  ? 108 ASP A OD2   1 
ATOM   4730 N  N     . VAL B 2 109 ? 31.80527  -26.49326 -27.82952 1.000 85.15623  ? 109 VAL A N     1 
ATOM   4731 C  CA    . VAL B 2 109 ? 31.04953  -26.50153 -26.58156 1.000 82.29693  ? 109 VAL A CA    1 
ATOM   4732 C  C     . VAL B 2 109 ? 29.67369  -25.92501 -26.88864 1.000 75.40977  ? 109 VAL A C     1 
ATOM   4733 O  O     . VAL B 2 109 ? 29.58467  -24.84995 -27.49911 1.000 79.28570  ? 109 VAL A O     1 
ATOM   4734 C  CB    . VAL B 2 109 ? 31.76872  -25.70295 -25.48364 1.000 73.01172  ? 109 VAL A CB    1 
ATOM   4735 C  CG1   . VAL B 2 109 ? 30.94432  -25.68701 -24.20963 1.000 74.27671  ? 109 VAL A CG1   1 
ATOM   4736 C  CG2   . VAL B 2 109 ? 33.14476  -26.28650 -25.22267 1.000 86.47163  ? 109 VAL A CG2   1 
ATOM   4737 N  N     . PRO B 2 110 ? 28.58251  -26.60790 -26.51920 1.000 72.38444  ? 110 PRO A N     1 
ATOM   4738 C  CA    . PRO B 2 110 ? 27.24217  -26.07818 -26.81166 1.000 66.29514  ? 110 PRO A CA    1 
ATOM   4739 C  C     . PRO B 2 110 ? 27.06446  -24.65616 -26.30298 1.000 69.97873  ? 110 PRO A C     1 
ATOM   4740 O  O     . PRO B 2 110 ? 27.21829  -24.38684 -25.10738 1.000 71.12077  ? 110 PRO A O     1 
ATOM   4741 C  CB    . PRO B 2 110 ? 26.31478  -27.06404 -26.09195 1.000 70.18431  ? 110 PRO A CB    1 
ATOM   4742 C  CG    . PRO B 2 110 ? 27.09253  -28.34229 -26.06971 1.000 73.58215  ? 110 PRO A CG    1 
ATOM   4743 C  CD    . PRO B 2 110 ? 28.52759  -27.93392 -25.88002 1.000 68.42052  ? 110 PRO A CD    1 
ATOM   4744 N  N     . MET B 2 111 ? 26.75025  -23.73543 -27.21069 1.000 63.76867  ? 111 MET A N     1 
ATOM   4745 C  CA    . MET B 2 111 ? 26.80580  -22.31725 -26.89733 1.000 67.30409  ? 111 MET A CA    1 
ATOM   4746 C  C     . MET B 2 111 ? 25.81853  -21.56683 -27.77756 1.000 65.96156  ? 111 MET A C     1 
ATOM   4747 O  O     . MET B 2 111 ? 25.58207  -21.94184 -28.92900 1.000 71.85363  ? 111 MET A O     1 
ATOM   4748 C  CB    . MET B 2 111 ? 28.22739  -21.78006 -27.09842 1.000 70.79555  ? 111 MET A CB    1 
ATOM   4749 C  CG    . MET B 2 111 ? 28.50755  -20.43643 -26.46782 1.000 70.44440  ? 111 MET A CG    1 
ATOM   4750 S  SD    . MET B 2 111 ? 30.24650  -20.00513 -26.67054 1.000 87.98819  ? 111 MET A SD    1 
ATOM   4751 C  CE    . MET B 2 111 ? 31.03221  -21.47568 -26.00959 1.000 72.06392  ? 111 MET A CE    1 
ATOM   4752 N  N     . VAL B 2 112 ? 25.24663  -20.50015 -27.22336 1.000 60.70458  ? 112 VAL A N     1 
ATOM   4753 C  CA    . VAL B 2 112 ? 24.27402  -19.66739 -27.92357 1.000 67.31479  ? 112 VAL A CA    1 
ATOM   4754 C  C     . VAL B 2 112 ? 24.54392  -18.21066 -27.57650 1.000 63.68808  ? 112 VAL A C     1 
ATOM   4755 O  O     . VAL B 2 112 ? 24.60569  -17.85031 -26.39628 1.000 71.63412  ? 112 VAL A O     1 
ATOM   4756 C  CB    . VAL B 2 112 ? 22.82266  -20.04109 -27.55861 1.000 68.13984  ? 112 VAL A CB    1 
ATOM   4757 C  CG1   . VAL B 2 112 ? 21.86246  -18.96066 -28.03160 1.000 63.95055  ? 112 VAL A CG1   1 
ATOM   4758 C  CG2   . VAL B 2 112 ? 22.44568  -21.38879 -28.15681 1.000 68.74376  ? 112 VAL A CG2   1 
ATOM   4759 N  N     . LEU B 2 113 ? 24.69982  -17.37444 -28.60000 1.000 65.31007  ? 113 LEU A N     1 
ATOM   4760 C  CA    . LEU B 2 113 ? 24.85609  -15.94045 -28.39607 1.000 74.20645  ? 113 LEU A CA    1 
ATOM   4761 C  C     . LEU B 2 113 ? 23.48552  -15.28887 -28.23755 1.000 70.59272  ? 113 LEU A C     1 
ATOM   4762 O  O     . LEU B 2 113 ? 22.57110  -15.54927 -29.02569 1.000 69.00996  ? 113 LEU A O     1 
ATOM   4763 C  CB    . LEU B 2 113 ? 25.61463  -15.31905 -29.56762 1.000 69.38796  ? 113 LEU A CB    1 
ATOM   4764 C  CG    . LEU B 2 113 ? 25.86072  -13.81223 -29.50402 1.000 72.83082  ? 113 LEU A CG    1 
ATOM   4765 C  CD1   . LEU B 2 113 ? 26.73315  -13.46242 -28.31128 1.000 58.35326  ? 113 LEU A CD1   1 
ATOM   4766 C  CD2   . LEU B 2 113 ? 26.48629  -13.32052 -30.80200 1.000 79.88018  ? 113 LEU A CD2   1 
ATOM   4767 N  N     . VAL B 2 114 ? 23.34348  -14.44322 -27.21762 1.000 59.46543  ? 114 VAL A N     1 
ATOM   4768 C  CA    . VAL B 2 114 ? 22.06365  -13.84128 -26.86067 1.000 60.28446  ? 114 VAL A CA    1 
ATOM   4769 C  C     . VAL B 2 114 ? 22.22473  -12.32872 -26.79635 1.000 74.80484  ? 114 VAL A C     1 
ATOM   4770 O  O     . VAL B 2 114 ? 23.11582  -11.82455 -26.10424 1.000 76.79548  ? 114 VAL A O     1 
ATOM   4771 C  CB    . VAL B 2 114 ? 21.53769  -14.38066 -25.51573 1.000 68.22045  ? 114 VAL A CB    1 
ATOM   4772 C  CG1   . VAL B 2 114 ? 20.29353  -13.61556 -25.07726 1.000 62.96365  ? 114 VAL A CG1   1 
ATOM   4773 C  CG2   . VAL B 2 114 ? 21.24654  -15.87010 -25.61602 1.000 59.51168  ? 114 VAL A CG2   1 
ATOM   4774 N  N     . GLY B 2 115 ? 21.36007  -11.60890 -27.51059 1.000 74.59695  ? 115 GLY A N     1 
ATOM   4775 C  CA    . GLY B 2 115 ? 21.30177  -10.16274 -27.41075 1.000 65.82516  ? 115 GLY A CA    1 
ATOM   4776 C  C     . GLY B 2 115 ? 20.05925  -9.69946  -26.67705 1.000 70.32712  ? 115 GLY A C     1 
ATOM   4777 O  O     . GLY B 2 115 ? 18.95340  -9.76008  -27.22232 1.000 78.10679  ? 115 GLY A O     1 
ATOM   4778 N  N     . ASN B 2 116 ? 20.22531  -9.23461  -25.44253 1.000 74.15273  ? 116 ASN A N     1 
ATOM   4779 C  CA    . ASN B 2 116 ? 19.10029  -8.91714  -24.57630 1.000 73.39267  ? 116 ASN A CA    1 
ATOM   4780 C  C     . ASN B 2 116 ? 18.73089  -7.43689  -24.67500 1.000 81.46992  ? 116 ASN A C     1 
ATOM   4781 O  O     . ASN B 2 116 ? 19.42816  -6.63212  -25.29769 1.000 80.87154  ? 116 ASN A O     1 
ATOM   4782 C  CB    . ASN B 2 116 ? 19.42541  -9.29083  -23.12737 1.000 65.44915  ? 116 ASN A CB    1 
ATOM   4783 C  CG    . ASN B 2 116 ? 18.18902  -9.36835  -22.25002 1.000 68.14200  ? 116 ASN A CG    1 
ATOM   4784 O  OD1   . ASN B 2 116 ? 17.10478  -9.71506  -22.71802 1.000 72.67868  ? 116 ASN A OD1   1 
ATOM   4785 N  ND2   . ASN B 2 116 ? 18.34430  -9.03330  -20.97342 1.000 66.69498  ? 116 ASN A ND2   1 
ATOM   4786 N  N     . LYS B 2 117 ? 17.60207  -7.09258  -24.04552 1.000 82.06079  ? 117 LYS A N     1 
ATOM   4787 C  CA    . LYS B 2 117 ? 17.10646  -5.71713  -23.95529 1.000 76.93533  ? 117 LYS A CA    1 
ATOM   4788 C  C     . LYS B 2 117 ? 16.72457  -5.16754  -25.32778 1.000 79.49365  ? 117 LYS A C     1 
ATOM   4789 O  O     . LYS B 2 117 ? 17.00620  -4.01407  -25.65666 1.000 89.39236  ? 117 LYS A O     1 
ATOM   4790 C  CB    . LYS B 2 117 ? 18.11790  -4.80213  -23.25811 1.000 72.03885  ? 117 LYS A CB    1 
ATOM   4791 C  CG    . LYS B 2 117 ? 18.32056  -5.11919  -21.78495 1.000 76.65779  ? 117 LYS A CG    1 
ATOM   4792 C  CD    . LYS B 2 117 ? 19.36271  -4.20941  -21.14956 1.000 84.51167  ? 117 LYS A CD    1 
ATOM   4793 C  CE    . LYS B 2 117 ? 19.47145  -4.44529  -19.64899 1.000 64.87163  ? 117 LYS A CE    1 
ATOM   4794 N  NZ    . LYS B 2 117 ? 20.46557  -3.52598  -19.02516 1.000 81.65233  ? 117 LYS A NZ    1 
ATOM   4795 N  N     . CYS B 2 118 ? 16.06499  -5.99901  -26.13382 1.000 81.85095  ? 118 CYS A N     1 
ATOM   4796 C  CA    . CYS B 2 118 ? 15.54941  -5.55302  -27.42074 1.000 89.78804  ? 118 CYS A CA    1 
ATOM   4797 C  C     . CYS B 2 118 ? 14.27146  -4.73621  -27.29506 1.000 90.29392  ? 118 CYS A C     1 
ATOM   4798 O  O     . CYS B 2 118 ? 13.87623  -4.08115  -28.26573 1.000 90.88586  ? 118 CYS A O     1 
ATOM   4799 C  CB    . CYS B 2 118 ? 15.31234  -6.75412  -28.33560 1.000 89.87221  ? 118 CYS A CB    1 
ATOM   4800 S  SG    . CYS B 2 118 ? 16.84463  -7.47532  -28.95299 1.000 96.91790  ? 118 CYS A SG    1 
ATOM   4801 N  N     . ASP B 2 119 ? 13.62144  -4.75695  -26.13037 1.000 86.47789  ? 119 ASP A N     1 
ATOM   4802 C  CA    . ASP B 2 119 ? 12.47454  -3.88981  -25.89741 1.000 87.13509  ? 119 ASP A CA    1 
ATOM   4803 C  C     . ASP B 2 119 ? 12.86628  -2.42084  -25.84631 1.000 95.90195  ? 119 ASP A C     1 
ATOM   4804 O  O     . ASP B 2 119 ? 12.00012  -1.55557  -26.01357 1.000 90.80658  ? 119 ASP A O     1 
ATOM   4805 C  CB    . ASP B 2 119 ? 11.78175  -4.27647  -24.59279 1.000 93.75220  ? 119 ASP A CB    1 
ATOM   4806 C  CG    . ASP B 2 119 ? 12.74104  -4.31922  -23.42016 1.000 84.90137  ? 119 ASP A CG    1 
ATOM   4807 O  OD1   . ASP B 2 119 ? 13.71130  -5.10322  -23.47550 1.000 81.07096  ? 119 ASP A OD1   1 
ATOM   4808 O  OD2   . ASP B 2 119 ? 12.53643  -3.55771  -22.45216 1.000 89.65721  ? 119 ASP A OD2   1 
ATOM   4809 N  N     . LEU B 2 120 ? 14.14201  -2.12500  -25.61486 1.000 93.66792  ? 120 LEU A N     1 
ATOM   4810 C  CA    . LEU B 2 120 ? 14.58097  -0.74301  -25.51520 1.000 101.61791 ? 120 LEU A CA    1 
ATOM   4811 C  C     . LEU B 2 120 ? 14.46940  -0.05234  -26.87288 1.000 110.09657 ? 120 LEU A C     1 
ATOM   4812 O  O     . LEU B 2 120 ? 14.71416  -0.67515  -27.91160 1.000 105.27665 ? 120 LEU A O     1 
ATOM   4813 C  CB    . LEU B 2 120 ? 16.01911  -0.67411  -25.00495 1.000 100.41497 ? 120 LEU A CB    1 
ATOM   4814 C  CG    . LEU B 2 120 ? 16.21178  -1.13082  -23.55783 1.000 89.02041  ? 120 LEU A CG    1 
ATOM   4815 C  CD1   . LEU B 2 120 ? 17.65821  -0.96254  -23.12731 1.000 78.30473  ? 120 LEU A CD1   1 
ATOM   4816 C  CD2   . LEU B 2 120 ? 15.27853  -0.36608  -22.63094 1.000 83.90268  ? 120 LEU A CD2   1 
ATOM   4817 N  N     . PRO B 2 121 ? 14.10429  1.23256   -26.89751 1.000 122.77815 ? 121 PRO A N     1 
ATOM   4818 C  CA    . PRO B 2 121 ? 13.90184  1.89840   -28.19393 1.000 111.30015 ? 121 PRO A CA    1 
ATOM   4819 C  C     . PRO B 2 121 ? 15.19033  2.13654   -28.95794 1.000 110.06604 ? 121 PRO A C     1 
ATOM   4820 O  O     . PRO B 2 121 ? 15.21594  1.96328   -30.18279 1.000 123.16024 ? 121 PRO A O     1 
ATOM   4821 C  CB    . PRO B 2 121 ? 13.21790  3.21463   -27.80077 1.000 122.32531 ? 121 PRO A CB    1 
ATOM   4822 C  CG    . PRO B 2 121 ? 13.69037  3.47466   -26.40673 1.000 123.44797 ? 121 PRO A CG    1 
ATOM   4823 C  CD    . PRO B 2 121 ? 13.82169  2.12481   -25.75939 1.000 115.40635 ? 121 PRO A CD    1 
ATOM   4824 N  N     . THR B 2 122 ? 16.26246  2.52971   -28.27583 1.000 106.62707 ? 122 THR A N     1 
ATOM   4825 C  CA    . THR B 2 122 ? 17.52785  2.85554   -28.91913 1.000 107.25942 ? 122 THR A CA    1 
ATOM   4826 C  C     . THR B 2 122 ? 18.59861  1.87392   -28.46982 1.000 103.93162 ? 122 THR A C     1 
ATOM   4827 O  O     . THR B 2 122 ? 18.73900  1.60456   -27.27200 1.000 106.66268 ? 122 THR A O     1 
ATOM   4828 C  CB    . THR B 2 122 ? 17.96312  4.28575   -28.59462 1.000 110.52518 ? 122 THR A CB    1 
ATOM   4829 O  OG1   . THR B 2 122 ? 18.19853  4.40495   -27.18627 1.000 110.77864 ? 122 THR A OG1   1 
ATOM   4830 C  CG2   . THR B 2 122 ? 16.88591  5.27519   -29.01083 1.000 114.38896 ? 122 THR A CG2   1 
ATOM   4831 N  N     . ARG B 2 123 ? 19.35564  1.35408   -29.43010 1.000 101.08053 ? 123 ARG A N     1 
ATOM   4832 C  CA    . ARG B 2 123 ? 20.42370  0.40520   -29.16823 1.000 98.11765  ? 123 ARG A CA    1 
ATOM   4833 C  C     . ARG B 2 123 ? 21.75256  0.96805   -29.65596 1.000 94.87175  ? 123 ARG A C     1 
ATOM   4834 O  O     . ARG B 2 123 ? 21.79889  1.93790   -30.41713 1.000 113.10728 ? 123 ARG A O     1 
ATOM   4835 C  CB    . ARG B 2 123 ? 20.14455  -0.93971  -29.84715 1.000 102.19287 ? 123 ARG A CB    1 
ATOM   4836 C  CG    . ARG B 2 123 ? 19.88932  -0.83296  -31.33855 1.000 100.66671 ? 123 ARG A CG    1 
ATOM   4837 C  CD    . ARG B 2 123 ? 20.09112  -2.17376  -32.01625 1.000 104.69099 ? 123 ARG A CD    1 
ATOM   4838 N  NE    . ARG B 2 123 ? 19.11807  -3.16897  -31.58352 1.000 100.48162 ? 123 ARG A NE    1 
ATOM   4839 C  CZ    . ARG B 2 123 ? 19.25588  -4.47487  -31.76844 1.000 103.90912 ? 123 ARG A CZ    1 
ATOM   4840 N  NH1   . ARG B 2 123 ? 20.33853  -4.98191  -32.33558 1.000 95.06188  ? 123 ARG A NH1   1 
ATOM   4841 N  NH2   . ARG B 2 123 ? 18.28457  -5.29292  -31.37260 1.000 109.34098 ? 123 ARG A NH2   1 
ATOM   4842 N  N     . THR B 2 124 ? 22.84191  0.34509   -29.20079 1.000 94.53143  ? 124 THR A N     1 
ATOM   4843 C  CA    . THR B 2 124 ? 24.18994  0.73711   -29.59097 1.000 90.68653  ? 124 THR A CA    1 
ATOM   4844 C  C     . THR B 2 124 ? 24.98023  -0.39159  -30.23837 1.000 93.40823  ? 124 THR A C     1 
ATOM   4845 O  O     . THR B 2 124 ? 26.12912  -0.17018  -30.63963 1.000 86.72956  ? 124 THR A O     1 
ATOM   4846 C  CB    . THR B 2 124 ? 24.97722  1.26031   -28.37902 1.000 96.09669  ? 124 THR A CB    1 
ATOM   4847 O  OG1   . THR B 2 124 ? 25.29167  0.17140   -27.50089 1.000 103.86839 ? 124 THR A OG1   1 
ATOM   4848 C  CG2   . THR B 2 124 ? 24.17001  2.30135   -27.61791 1.000 97.38792  ? 124 THR A CG2   1 
ATOM   4849 N  N     . VAL B 2 125 ? 24.41267  -1.59067  -30.34070 1.000 94.17544  ? 125 VAL A N     1 
ATOM   4850 C  CA    . VAL B 2 125 ? 25.07709  -2.73926  -30.94570 1.000 95.04645  ? 125 VAL A CA    1 
ATOM   4851 C  C     . VAL B 2 125 ? 24.35352  -3.07760  -32.24084 1.000 93.30682  ? 125 VAL A C     1 
ATOM   4852 O  O     . VAL B 2 125 ? 23.11790  -3.13266  -32.27321 1.000 91.39500  ? 125 VAL A O     1 
ATOM   4853 C  CB    . VAL B 2 125 ? 25.09952  -3.94867  -29.99341 1.000 93.53283  ? 125 VAL A CB    1 
ATOM   4854 C  CG1   . VAL B 2 125 ? 25.87697  -5.10022  -30.61386 1.000 83.73632  ? 125 VAL A CG1   1 
ATOM   4855 C  CG2   . VAL B 2 125 ? 25.69526  -3.56034  -28.64667 1.000 86.38186  ? 125 VAL A CG2   1 
ATOM   4856 N  N     . ASP B 2 126 ? 25.12076  -3.30276  -33.30457 1.000 96.41902  ? 126 ASP A N     1 
ATOM   4857 C  CA    . ASP B 2 126 ? 24.55140  -3.61026  -34.61095 1.000 104.70699 ? 126 ASP A CA    1 
ATOM   4858 C  C     . ASP B 2 126 ? 24.19198  -5.09088  -34.67544 1.000 95.42374  ? 126 ASP A C     1 
ATOM   4859 O  O     . ASP B 2 126 ? 25.05002  -5.95252  -34.45425 1.000 102.00435 ? 126 ASP A O     1 
ATOM   4860 C  CB    . ASP B 2 126 ? 25.54031  -3.23969  -35.71586 1.000 103.17949 ? 126 ASP A CB    1 
ATOM   4861 C  CG    . ASP B 2 126 ? 24.90620  -3.22889  -37.09639 1.000 104.27974 ? 126 ASP A CG    1 
ATOM   4862 O  OD1   . ASP B 2 126 ? 23.69859  -3.52996  -37.20965 1.000 109.55505 ? 126 ASP A OD1   1 
ATOM   4863 O  OD2   . ASP B 2 126 ? 25.62021  -2.91282  -38.07148 1.000 98.05292  ? 126 ASP A OD2   1 
ATOM   4864 N  N     . THR B 2 127 ? 22.92186  -5.38341  -34.97521 1.000 89.42771  ? 127 THR A N     1 
ATOM   4865 C  CA    . THR B 2 127 ? 22.48957  -6.77012  -35.13291 1.000 96.37487  ? 127 THR A CA    1 
ATOM   4866 C  C     . THR B 2 127 ? 23.28610  -7.48343  -36.21978 1.000 93.79560  ? 127 THR A C     1 
ATOM   4867 O  O     . THR B 2 127 ? 23.52426  -8.69381  -36.12414 1.000 89.42693  ? 127 THR A O     1 
ATOM   4868 C  CB    . THR B 2 127 ? 20.98817  -6.81743  -35.44123 1.000 108.63065 ? 127 THR A CB    1 
ATOM   4869 O  OG1   . THR B 2 127 ? 20.25151  -6.31210  -34.32019 1.000 107.80493 ? 127 THR A OG1   1 
ATOM   4870 C  CG2   . THR B 2 127 ? 20.52709  -8.24065  -35.73632 1.000 87.83160  ? 127 THR A CG2   1 
ATOM   4871 N  N     . LYS B 2 128 ? 23.72136  -6.75032  -37.24794 1.000 96.17426  ? 128 LYS A N     1 
ATOM   4872 C  CA    . LYS B 2 128 ? 24.56471  -7.34721  -38.27852 1.000 97.71582  ? 128 LYS A CA    1 
ATOM   4873 C  C     . LYS B 2 128 ? 25.87174  -7.86882  -37.69154 1.000 94.94200  ? 128 LYS A C     1 
ATOM   4874 O  O     . LYS B 2 128 ? 26.39886  -8.89166  -38.14403 1.000 101.96398 ? 128 LYS A O     1 
ATOM   4875 C  CB    . LYS B 2 128 ? 24.84421  -6.32856  -39.38374 1.000 113.47976 ? 128 LYS A CB    1 
ATOM   4876 C  CG    . LYS B 2 128 ? 23.60285  -5.82233  -40.10231 1.000 112.73042 ? 128 LYS A CG    1 
ATOM   4877 C  CD    . LYS B 2 128 ? 23.97311  -4.83219  -41.19741 1.000 120.97487 ? 128 LYS A CD    1 
ATOM   4878 C  CE    . LYS B 2 128 ? 22.74564  -4.35866  -41.96020 1.000 116.96845 ? 128 LYS A CE    1 
ATOM   4879 N  NZ    . LYS B 2 128 ? 23.10375  -3.38643  -43.03003 1.000 115.58442 ? 128 LYS A NZ    1 
ATOM   4880 N  N     . GLN B 2 129 ? 26.41117  -7.18071  -36.68237 1.000 88.34825  ? 129 GLN A N     1 
ATOM   4881 C  CA    . GLN B 2 129 ? 27.65053  -7.64002  -36.06316 1.000 98.40760  ? 129 GLN A CA    1 
ATOM   4882 C  C     . GLN B 2 129 ? 27.43808  -8.93730  -35.29317 1.000 93.96052  ? 129 GLN A C     1 
ATOM   4883 O  O     . GLN B 2 129 ? 28.28073  -9.84141  -35.34416 1.000 95.10117  ? 129 GLN A O     1 
ATOM   4884 C  CB    . GLN B 2 129 ? 28.21120  -6.56344  -35.13494 1.000 108.71413 ? 129 GLN A CB    1 
ATOM   4885 C  CG    . GLN B 2 129 ? 28.62592  -5.27815  -35.82200 1.000 98.12251  ? 129 GLN A CG    1 
ATOM   4886 C  CD    . GLN B 2 129 ? 29.17969  -4.26356  -34.84123 1.000 111.07589 ? 129 GLN A CD    1 
ATOM   4887 O  OE1   . GLN B 2 129 ? 28.43104  -3.49380  -34.23789 1.000 108.49042 ? 129 GLN A OE1   1 
ATOM   4888 N  NE2   . GLN B 2 129 ? 30.49721  -4.26533  -34.66757 1.000 104.28600 ? 129 GLN A NE2   1 
ATOM   4889 N  N     . ALA B 2 130 ? 26.31891  -9.04562  -34.57305 1.000 95.03433  ? 130 ALA A N     1 
ATOM   4890 C  CA    . ALA B 2 130 ? 26.07525  -10.22787 -33.75254 1.000 85.83669  ? 130 ALA A CA    1 
ATOM   4891 C  C     . ALA B 2 130 ? 25.83561  -11.46414 -34.61090 1.000 91.93951  ? 130 ALA A C     1 
ATOM   4892 O  O     . ALA B 2 130 ? 26.35901  -12.54357 -34.30899 1.000 89.54323  ? 130 ALA A O     1 
ATOM   4893 C  CB    . ALA B 2 130 ? 24.89286  -9.98140  -32.81810 1.000 83.10393  ? 130 ALA A CB    1 
ATOM   4894 N  N     . HIS B 2 131 ? 25.03642  -11.33241 -35.67513 1.000 94.77605  ? 131 HIS A N     1 
ATOM   4895 C  CA    . HIS B 2 131 ? 24.87538  -12.43805 -36.61507 1.000 87.23302  ? 131 HIS A CA    1 
ATOM   4896 C  C     . HIS B 2 131 ? 26.21916  -12.85874 -37.19328 1.000 88.05494  ? 131 HIS A C     1 
ATOM   4897 O  O     . HIS B 2 131 ? 26.52339  -14.05421 -37.27730 1.000 93.63259  ? 131 HIS A O     1 
ATOM   4898 C  CB    . HIS B 2 131 ? 23.91432  -12.04760 -37.73916 1.000 84.56064  ? 131 HIS A CB    1 
ATOM   4899 C  CG    . HIS B 2 131 ? 22.46835  -12.23515 -37.39713 1.000 99.68251  ? 131 HIS A CG    1 
ATOM   4900 N  ND1   . HIS B 2 131 ? 21.68704  -11.22449 -36.87910 1.000 100.28919 ? 131 HIS A ND1   1 
ATOM   4901 C  CD2   . HIS B 2 131 ? 21.65931  -13.31596 -37.50775 1.000 93.11665  ? 131 HIS A CD2   1 
ATOM   4902 C  CE1   . HIS B 2 131 ? 20.46066  -11.67524 -36.68174 1.000 85.00713  ? 131 HIS A CE1   1 
ATOM   4903 N  NE2   . HIS B 2 131 ? 20.41732  -12.94156 -37.05513 1.000 84.85731  ? 131 HIS A NE2   1 
ATOM   4904 N  N     . GLU B 2 132 ? 27.04220  -11.88416 -37.58433 1.000 86.24439  ? 132 GLU A N     1 
ATOM   4905 C  CA    . GLU B 2 132 ? 28.34748  -12.19193 -38.15670 1.000 90.39200  ? 132 GLU A CA    1 
ATOM   4906 C  C     . GLU B 2 132 ? 29.25409  -12.86166 -37.13224 1.000 85.59142  ? 132 GLU A C     1 
ATOM   4907 O  O     . GLU B 2 132 ? 29.95867  -13.82535 -37.45440 1.000 86.63196  ? 132 GLU A O     1 
ATOM   4908 C  CB    . GLU B 2 132 ? 28.98663  -10.91155 -38.69316 1.000 97.89674  ? 132 GLU A CB    1 
ATOM   4909 C  CG    . GLU B 2 132 ? 30.13100  -11.12808 -39.66563 1.000 116.17658 ? 132 GLU A CG    1 
ATOM   4910 C  CD    . GLU B 2 132 ? 30.73202  -9.81935  -40.14762 1.000 135.27431 ? 132 GLU A CD    1 
ATOM   4911 O  OE1   . GLU B 2 132 ? 30.64761  -8.81723  -39.40550 1.000 132.60228 ? 132 GLU A OE1   1 
ATOM   4912 O  OE2   . GLU B 2 132 ? 31.28183  -9.78993  -41.26964 1.000 138.14170 ? 132 GLU A OE2   1 
ATOM   4913 N  N     . LEU B 2 133 ? 29.24209  -12.37201 -35.89082 1.000 83.74629  ? 133 LEU A N     1 
ATOM   4914 C  CA    . LEU B 2 133 ? 30.10080  -12.94513 -34.85937 1.000 89.42509  ? 133 LEU A CA    1 
ATOM   4915 C  C     . LEU B 2 133 ? 29.68408  -14.37167 -34.52656 1.000 93.35273  ? 133 LEU A C     1 
ATOM   4916 O  O     . LEU B 2 133 ? 30.52420  -15.27853 -34.47484 1.000 89.61807  ? 133 LEU A O     1 
ATOM   4917 C  CB    . LEU B 2 133 ? 30.07251  -12.07113 -33.60559 1.000 85.46085  ? 133 LEU A CB    1 
ATOM   4918 C  CG    . LEU B 2 133 ? 30.88145  -12.59254 -32.41622 1.000 77.06252  ? 133 LEU A CG    1 
ATOM   4919 C  CD1   . LEU B 2 133 ? 32.32642  -12.81956 -32.81493 1.000 75.94573  ? 133 LEU A CD1   1 
ATOM   4920 C  CD2   . LEU B 2 133 ? 30.79390  -11.63075 -31.24424 1.000 73.90557  ? 133 LEU A CD2   1 
ATOM   4921 N  N     . ALA B 2 134 ? 28.38646  -14.58758 -34.29082 1.000 93.24178  ? 134 ALA A N     1 
ATOM   4922 C  CA    . ALA B 2 134 ? 27.90336  -15.93047 -33.98885 1.000 82.33251  ? 134 ALA A CA    1 
ATOM   4923 C  C     . ALA B 2 134 ? 28.12333  -16.87830 -35.15755 1.000 92.70916  ? 134 ALA A C     1 
ATOM   4924 O  O     . ALA B 2 134 ? 28.35754  -18.07507 -34.95127 1.000 89.50120  ? 134 ALA A O     1 
ATOM   4925 C  CB    . ALA B 2 134 ? 26.42300  -15.88646 -33.61595 1.000 71.60635  ? 134 ALA A CB    1 
ATOM   4926 N  N     . LYS B 2 135 ? 28.05428  -16.36485 -36.38761 1.000 91.63745  ? 135 LYS A N     1 
ATOM   4927 C  CA    . LYS B 2 135 ? 28.29323  -17.20955 -37.55115 1.000 86.76193  ? 135 LYS A CA    1 
ATOM   4928 C  C     . LYS B 2 135 ? 29.72250  -17.73338 -37.56328 1.000 84.19008  ? 135 LYS A C     1 
ATOM   4929 O  O     . LYS B 2 135 ? 29.95912  -18.90399 -37.88244 1.000 88.22694  ? 135 LYS A O     1 
ATOM   4930 C  CB    . LYS B 2 135 ? 27.99110  -16.43329 -38.83177 1.000 78.05871  ? 135 LYS A CB    1 
ATOM   4931 C  CG    . LYS B 2 135 ? 28.19707  -17.22974 -40.10632 1.000 86.04260  ? 135 LYS A CG    1 
ATOM   4932 C  CD    . LYS B 2 135 ? 27.88425  -16.38597 -41.33134 1.000 101.32903 ? 135 LYS A CD    1 
ATOM   4933 C  CE    . LYS B 2 135 ? 28.11084  -17.16353 -42.61678 1.000 100.24278 ? 135 LYS A CE    1 
ATOM   4934 N  NZ    . LYS B 2 135 ? 27.84322  -16.32922 -43.82171 1.000 106.29483 ? 135 LYS A NZ    1 
ATOM   4935 N  N     . SER B 2 136 ? 30.68988  -16.88440 -37.20826 1.000 85.38537  ? 136 SER A N     1 
ATOM   4936 C  CA    . SER B 2 136 ? 32.08357  -17.31381 -37.19643 1.000 96.59284  ? 136 SER A CA    1 
ATOM   4937 C  C     . SER B 2 136 ? 32.36969  -18.31577 -36.08574 1.000 90.93914  ? 136 SER A C     1 
ATOM   4938 O  O     . SER B 2 136 ? 33.34392  -19.06912 -36.18319 1.000 92.86196  ? 136 SER A O     1 
ATOM   4939 C  CB    . SER B 2 136 ? 33.01037  -16.10410 -37.05838 1.000 94.49208  ? 136 SER A CB    1 
ATOM   4940 O  OG    . SER B 2 136 ? 32.85138  -15.47803 -35.79712 1.000 91.65622  ? 136 SER A OG    1 
ATOM   4941 N  N     . TYR B 2 137 ? 31.54862  -18.34155 -35.03559 1.000 86.51314  ? 137 TYR A N     1 
ATOM   4942 C  CA    . TYR B 2 137 ? 31.72265  -19.31925 -33.97003 1.000 89.00501  ? 137 TYR A CA    1 
ATOM   4943 C  C     . TYR B 2 137 ? 31.09512  -20.66654 -34.29866 1.000 83.44924  ? 137 TYR A C     1 
ATOM   4944 O  O     . TYR B 2 137 ? 31.48523  -21.67773 -33.70477 1.000 80.76637  ? 137 TYR A O     1 
ATOM   4945 C  CB    . TYR B 2 137 ? 31.12076  -18.79458 -32.66500 1.000 90.38930  ? 137 TYR A CB    1 
ATOM   4946 C  CG    . TYR B 2 137 ? 31.88021  -17.65085 -32.03497 1.000 94.52188  ? 137 TYR A CG    1 
ATOM   4947 C  CD1   . TYR B 2 137 ? 33.24137  -17.48685 -32.25360 1.000 96.11252  ? 137 TYR A CD1   1 
ATOM   4948 C  CD2   . TYR B 2 137 ? 31.23339  -16.73693 -31.21355 1.000 94.41743  ? 137 TYR A CD2   1 
ATOM   4949 C  CE1   . TYR B 2 137 ? 33.93617  -16.44140 -31.67180 1.000 91.09882  ? 137 TYR A CE1   1 
ATOM   4950 C  CE2   . TYR B 2 137 ? 31.91835  -15.69079 -30.62836 1.000 85.66030  ? 137 TYR A CE2   1 
ATOM   4951 C  CZ    . TYR B 2 137 ? 33.26815  -15.54714 -30.86024 1.000 88.13142  ? 137 TYR A CZ    1 
ATOM   4952 O  OH    . TYR B 2 137 ? 33.95003  -14.50280 -30.27788 1.000 90.88250  ? 137 TYR A OH    1 
ATOM   4953 N  N     . GLY B 2 138 ? 30.14175  -20.70583 -35.22579 1.000 74.32517  ? 138 GLY A N     1 
ATOM   4954 C  CA    . GLY B 2 138 ? 29.38629  -21.91825 -35.46265 1.000 70.49349  ? 138 GLY A CA    1 
ATOM   4955 C  C     . GLY B 2 138 ? 28.20875  -22.10419 -34.53671 1.000 86.24106  ? 138 GLY A C     1 
ATOM   4956 O  O     . GLY B 2 138 ? 27.70240  -23.22341 -34.40941 1.000 87.82877  ? 138 GLY A O     1 
ATOM   4957 N  N     . ILE B 2 139 ? 27.75696  -21.04054 -33.88648 1.000 80.61837  ? 139 ILE A N     1 
ATOM   4958 C  CA    . ILE B 2 139 ? 26.67754  -21.11634 -32.90599 1.000 78.89543  ? 139 ILE A CA    1 
ATOM   4959 C  C     . ILE B 2 139 ? 25.57792  -20.16404 -33.35220 1.000 74.25490  ? 139 ILE A C     1 
ATOM   4960 O  O     . ILE B 2 139 ? 25.82603  -19.21902 -34.12128 1.000 76.86115  ? 139 ILE A O     1 
ATOM   4961 C  CB    . ILE B 2 139 ? 27.17421  -20.78522 -31.47963 1.000 72.77529  ? 139 ILE A CB    1 
ATOM   4962 C  CG1   . ILE B 2 139 ? 27.40054  -19.28094 -31.32819 1.000 77.70020  ? 139 ILE A CG1   1 
ATOM   4963 C  CG2   . ILE B 2 139 ? 28.45304  -21.54712 -31.16926 1.000 66.28033  ? 139 ILE A CG2   1 
ATOM   4964 C  CD1   . ILE B 2 139 ? 27.65438  -18.84867 -29.90429 1.000 67.94642  ? 139 ILE A CD1   1 
ATOM   4965 N  N     . PRO B 2 140 ? 24.34617  -20.38467 -32.90222 1.000 65.24652  ? 140 PRO A N     1 
ATOM   4966 C  CA    . PRO B 2 140 ? 23.25476  -19.47765 -33.26467 1.000 74.16510  ? 140 PRO A CA    1 
ATOM   4967 C  C     . PRO B 2 140 ? 23.27144  -18.19953 -32.43807 1.000 73.97626  ? 140 PRO A C     1 
ATOM   4968 O  O     . PRO B 2 140 ? 23.92031  -18.09994 -31.39588 1.000 69.59252  ? 140 PRO A O     1 
ATOM   4969 C  CB    . PRO B 2 140 ? 21.99826  -20.30363 -32.96856 1.000 63.60646  ? 140 PRO A CB    1 
ATOM   4970 C  CG    . PRO B 2 140 ? 22.42032  -21.23315 -31.89427 1.000 66.47985  ? 140 PRO A CG    1 
ATOM   4971 C  CD    . PRO B 2 140 ? 23.85440  -21.57341 -32.18218 1.000 71.95250  ? 140 PRO A CD    1 
ATOM   4972 N  N     . PHE B 2 141 ? 22.53246  -17.20986 -32.93529 1.000 75.81438  ? 141 PHE A N     1 
ATOM   4973 C  CA    . PHE B 2 141 ? 22.33654  -15.93859 -32.25401 1.000 68.83132  ? 141 PHE A CA    1 
ATOM   4974 C  C     . PHE B 2 141 ? 20.84652  -15.64792 -32.16143 1.000 77.88844  ? 141 PHE A C     1 
ATOM   4975 O  O     . PHE B 2 141 ? 20.09870  -15.89968 -33.11085 1.000 83.60284  ? 141 PHE A O     1 
ATOM   4976 C  CB    . PHE B 2 141 ? 23.04750  -14.79600 -32.97894 1.000 79.08427  ? 141 PHE A CB    1 
ATOM   4977 C  CG    . PHE B 2 141 ? 22.56277  -13.43637 -32.57714 1.000 85.01163  ? 141 PHE A CG    1 
ATOM   4978 C  CD1   . PHE B 2 141 ? 22.83589  -12.93464 -31.31577 1.000 78.84690  ? 141 PHE A CD1   1 
ATOM   4979 C  CD2   . PHE B 2 141 ? 21.83051  -12.65985 -33.45919 1.000 82.34897  ? 141 PHE A CD2   1 
ATOM   4980 C  CE1   . PHE B 2 141 ? 22.38579  -11.68391 -30.94054 1.000 81.88038  ? 141 PHE A CE1   1 
ATOM   4981 C  CE2   . PHE B 2 141 ? 21.37828  -11.40772 -33.08990 1.000 85.09757  ? 141 PHE A CE2   1 
ATOM   4982 C  CZ    . PHE B 2 141 ? 21.65529  -10.91954 -31.82958 1.000 81.67590  ? 141 PHE A CZ    1 
ATOM   4983 N  N     . ILE B 2 142 ? 20.41722  -15.11905 -31.01640 1.000 82.20860  ? 142 ILE A N     1 
ATOM   4984 C  CA    . ILE B 2 142 ? 19.00021  -14.92852 -30.72217 1.000 73.67126  ? 142 ILE A CA    1 
ATOM   4985 C  C     . ILE B 2 142 ? 18.81546  -13.59317 -30.01491 1.000 79.47807  ? 142 ILE A C     1 
ATOM   4986 O  O     . ILE B 2 142 ? 19.45152  -13.33725 -28.98722 1.000 75.73520  ? 142 ILE A O     1 
ATOM   4987 C  CB    . ILE B 2 142 ? 18.44046  -16.07178 -29.85254 1.000 71.61730  ? 142 ILE A CB    1 
ATOM   4988 C  CG1   . ILE B 2 142 ? 18.54364  -17.40613 -30.59181 1.000 73.94884  ? 142 ILE A CG1   1 
ATOM   4989 C  CG2   . ILE B 2 142 ? 16.99995  -15.78573 -29.45098 1.000 71.23202  ? 142 ILE A CG2   1 
ATOM   4990 C  CD1   . ILE B 2 142 ? 18.17022  -18.59402 -29.75275 1.000 79.59632  ? 142 ILE A CD1   1 
ATOM   4991 N  N     . GLU B 2 143 ? 17.94460  -12.74407 -30.56067 1.000 84.02492  ? 143 GLU A N     1 
ATOM   4992 C  CA    . GLU B 2 143 ? 17.57582  -11.49904 -29.89802 1.000 78.45244  ? 143 GLU A CA    1 
ATOM   4993 C  C     . GLU B 2 143 ? 16.47176  -11.77125 -28.88698 1.000 75.73429  ? 143 GLU A C     1 
ATOM   4994 O  O     . GLU B 2 143 ? 15.45785  -12.39297 -29.21865 1.000 82.41578  ? 143 GLU A O     1 
ATOM   4995 C  CB    . GLU B 2 143 ? 17.10624  -10.45905 -30.91437 1.000 89.19094  ? 143 GLU A CB    1 
ATOM   4996 C  CG    . GLU B 2 143 ? 18.16565  -9.99317  -31.89614 1.000 100.70469 ? 143 GLU A CG    1 
ATOM   4997 C  CD    . GLU B 2 143 ? 17.65707  -8.89179  -32.80763 1.000 113.27242 ? 143 GLU A CD    1 
ATOM   4998 O  OE1   . GLU B 2 143 ? 16.95416  -7.98520  -32.31102 1.000 110.52178 ? 143 GLU A OE1   1 
ATOM   4999 O  OE2   . GLU B 2 143 ? 17.94775  -8.93942  -34.02157 1.000 116.62314 ? 143 GLU A OE2   1 
ATOM   5000 N  N     . THR B 2 144 ? 16.66408  -11.30718 -27.65481 1.000 76.40675  ? 144 THR A N     1 
ATOM   5001 C  CA    . THR B 2 144 ? 15.71333  -11.56181 -26.58283 1.000 78.39072  ? 144 THR A CA    1 
ATOM   5002 C  C     . THR B 2 144 ? 15.33728  -10.25947 -25.88808 1.000 80.28061  ? 144 THR A C     1 
ATOM   5003 O  O     . THR B 2 144 ? 15.89445  -9.19174  -26.15728 1.000 75.27788  ? 144 THR A O     1 
ATOM   5004 C  CB    . THR B 2 144 ? 16.26957  -12.55358 -25.55004 1.000 66.26782  ? 144 THR A CB    1 
ATOM   5005 O  OG1   . THR B 2 144 ? 17.38148  -11.96065 -24.86969 1.000 78.14932  ? 144 THR A OG1   1 
ATOM   5006 C  CG2   . THR B 2 144 ? 16.71760  -13.84471 -26.22359 1.000 67.07921  ? 144 THR A CG2   1 
ATOM   5007 N  N     . SER B 2 145 ? 14.36618  -10.37186 -24.98325 1.000 75.02318  ? 145 SER A N     1 
ATOM   5008 C  CA    . SER B 2 145 ? 13.94458  -9.25472  -24.14199 1.000 74.93953  ? 145 SER A CA    1 
ATOM   5009 C  C     . SER B 2 145 ? 13.27070  -9.84723  -22.91323 1.000 75.66753  ? 145 SER A C     1 
ATOM   5010 O  O     . SER B 2 145 ? 12.17230  -10.40093 -23.02082 1.000 83.17203  ? 145 SER A O     1 
ATOM   5011 C  CB    . SER B 2 145 ? 13.00000  -8.32362  -24.89073 1.000 83.99911  ? 145 SER A CB    1 
ATOM   5012 O  OG    . SER B 2 145 ? 12.30935  -7.47635  -23.98623 1.000 77.55528  ? 145 SER A OG    1 
ATOM   5013 N  N     . ALA B 2 146 ? 13.92651  -9.73696  -21.75678 1.000 68.51646  ? 146 ALA A N     1 
ATOM   5014 C  CA    . ALA B 2 146 ? 13.36816  -10.29767 -20.53352 1.000 65.82204  ? 146 ALA A CA    1 
ATOM   5015 C  C     . ALA B 2 146 ? 12.15716  -9.51939  -20.03580 1.000 75.13530  ? 146 ALA A C     1 
ATOM   5016 O  O     . ALA B 2 146 ? 11.35756  -10.06715 -19.26933 1.000 72.99466  ? 146 ALA A O     1 
ATOM   5017 C  CB    . ALA B 2 146 ? 14.43886  -10.34994 -19.44611 1.000 60.61923  ? 146 ALA A CB    1 
ATOM   5018 N  N     . LYS B 2 147 ? 12.00216  -8.26068  -20.45112 1.000 75.44531  ? 147 LYS A N     1 
ATOM   5019 C  CA    . LYS B 2 147 ? 10.84021  -7.48269  -20.03326 1.000 78.18620  ? 147 LYS A CA    1 
ATOM   5020 C  C     . LYS B 2 147 ? 9.58040   -7.95575  -20.74717 1.000 73.15591  ? 147 LYS A C     1 
ATOM   5021 O  O     . LYS B 2 147 ? 8.54994   -8.20677  -20.11145 1.000 72.15014  ? 147 LYS A O     1 
ATOM   5022 C  CB    . LYS B 2 147 ? 11.08235  -5.99488  -20.29454 1.000 81.96659  ? 147 LYS A CB    1 
ATOM   5023 C  CG    . LYS B 2 147 ? 9.96503   -5.08336  -19.80350 1.000 75.23618  ? 147 LYS A CG    1 
ATOM   5024 C  CD    . LYS B 2 147 ? 10.25117  -3.62836  -20.14411 1.000 74.52532  ? 147 LYS A CD    1 
ATOM   5025 C  CE    . LYS B 2 147 ? 9.18493   -2.70184  -19.58368 1.000 72.00905  ? 147 LYS A CE    1 
ATOM   5026 N  NZ    . LYS B 2 147 ? 9.43322   -1.28398  -19.96786 1.000 81.13967  ? 147 LYS A NZ    1 
ATOM   5027 N  N     . THR B 2 148 ? 9.64579   -8.08639  -22.06913 1.000 76.23956  ? 148 THR A N     1 
ATOM   5028 C  CA    . THR B 2 148 ? 8.50161   -8.49202  -22.87229 1.000 68.64716  ? 148 THR A CA    1 
ATOM   5029 C  C     . THR B 2 148 ? 8.45309   -9.99308  -23.12452 1.000 72.67143  ? 148 THR A C     1 
ATOM   5030 O  O     . THR B 2 148 ? 7.53312   -10.46011 -23.80386 1.000 78.44255  ? 148 THR A O     1 
ATOM   5031 C  CB    . THR B 2 148 ? 8.51211   -7.74875  -24.21129 1.000 65.47362  ? 148 THR A CB    1 
ATOM   5032 O  OG1   . THR B 2 148 ? 9.68584   -8.10851  -24.95052 1.000 74.15684  ? 148 THR A OG1   1 
ATOM   5033 C  CG2   . THR B 2 148 ? 8.50948   -6.24641  -23.98137 1.000 67.94635  ? 148 THR A CG2   1 
ATOM   5034 N  N     . ARG B 2 149 ? 9.41512   -10.75050 -22.59850 1.000 70.96856  ? 149 ARG A N     1 
ATOM   5035 C  CA    . ARG B 2 149 ? 9.53612   -12.19722 -22.76716 1.000 70.88962  ? 149 ARG A CA    1 
ATOM   5036 C  C     . ARG B 2 149 ? 9.78708   -12.60214 -24.21624 1.000 69.47144  ? 149 ARG A C     1 
ATOM   5037 O  O     . ARG B 2 149 ? 9.75058   -13.79668 -24.53863 1.000 70.58031  ? 149 ARG A O     1 
ATOM   5038 C  CB    . ARG B 2 149 ? 8.30617   -12.94082 -22.22197 1.000 67.47603  ? 149 ARG A CB    1 
ATOM   5039 C  CG    . ARG B 2 149 ? 8.59664   -14.37753 -21.80857 1.000 83.15426  ? 149 ARG A CG    1 
ATOM   5040 C  CD    . ARG B 2 149 ? 7.33325   -15.19779 -21.61750 1.000 84.27294  ? 149 ARG A CD    1 
ATOM   5041 N  NE    . ARG B 2 149 ? 7.63179   -16.62513 -21.62349 1.000 73.91620  ? 149 ARG A NE    1 
ATOM   5042 C  CZ    . ARG B 2 149 ? 8.08688   -17.29928 -20.57668 1.000 67.16766  ? 149 ARG A CZ    1 
ATOM   5043 N  NH1   . ARG B 2 149 ? 8.29520   -16.70804 -19.41207 1.000 70.27500  ? 149 ARG A NH1   1 
ATOM   5044 N  NH2   . ARG B 2 149 ? 8.34005   -18.59915 -20.70187 1.000 68.50092  ? 149 ARG A NH2   1 
ATOM   5045 N  N     . GLN B 2 150 ? 10.04622  -11.64184 -25.09886 1.000 61.87619  ? 150 GLN A N     1 
ATOM   5046 C  CA    . GLN B 2 150 ? 10.32008  -11.95535 -26.49450 1.000 69.65571  ? 150 GLN A CA    1 
ATOM   5047 C  C     . GLN B 2 150 ? 11.60601  -12.76523 -26.61115 1.000 76.03628  ? 150 GLN A C     1 
ATOM   5048 O  O     . GLN B 2 150 ? 12.66350  -12.33899 -26.13763 1.000 73.17073  ? 150 GLN A O     1 
ATOM   5049 C  CB    . GLN B 2 150 ? 10.42279  -10.66401 -27.30435 1.000 73.75117  ? 150 GLN A CB    1 
ATOM   5050 C  CG    . GLN B 2 150 ? 11.09356  -10.82499 -28.65513 1.000 82.17822  ? 150 GLN A CG    1 
ATOM   5051 C  CD    . GLN B 2 150 ? 11.75545  -9.54321  -29.12900 1.000 98.51482  ? 150 GLN A CD    1 
ATOM   5052 O  OE1   . GLN B 2 150 ? 12.96140  -9.35431  -28.95902 1.000 91.43547  ? 150 GLN A OE1   1 
ATOM   5053 N  NE2   . GLN B 2 150 ? 10.96807  -8.65416  -29.72471 1.000 102.81480 ? 150 GLN A NE2   1 
ATOM   5054 N  N     . GLY B 2 151 ? 11.50881  -13.94221 -27.22714 1.000 76.41727  ? 151 GLY A N     1 
ATOM   5055 C  CA    . GLY B 2 151 ? 12.67134  -14.77067 -27.47972 1.000 60.04343  ? 151 GLY A CA    1 
ATOM   5056 C  C     . GLY B 2 151 ? 13.26619  -15.46341 -26.27473 1.000 66.48335  ? 151 GLY A C     1 
ATOM   5057 O  O     . GLY B 2 151 ? 14.31092  -16.10788 -26.40864 1.000 62.58547  ? 151 GLY A O     1 
ATOM   5058 N  N     . VAL B 2 152 ? 12.63843  -15.36175 -25.10077 1.000 70.38060  ? 152 VAL A N     1 
ATOM   5059 C  CA    . VAL B 2 152 ? 13.22010  -15.95333 -23.89797 1.000 58.99054  ? 152 VAL A CA    1 
ATOM   5060 C  C     . VAL B 2 152 ? 13.17929  -17.47503 -23.97527 1.000 64.44019  ? 152 VAL A C     1 
ATOM   5061 O  O     . VAL B 2 152 ? 14.17901  -18.15086 -23.70968 1.000 67.02164  ? 152 VAL A O     1 
ATOM   5062 C  CB    . VAL B 2 152 ? 12.50928  -15.42882 -22.63882 1.000 50.96853  ? 152 VAL A CB    1 
ATOM   5063 C  CG1   . VAL B 2 152 ? 12.95163  -16.21263 -21.41852 1.000 56.56738  ? 152 VAL A CG1   1 
ATOM   5064 C  CG2   . VAL B 2 152 ? 12.80089  -13.95140 -22.45278 1.000 55.50086  ? 152 VAL A CG2   1 
ATOM   5065 N  N     . GLU B 2 153 ? 12.02619  -18.04086 -24.33727 1.000 70.94509  ? 153 GLU A N     1 
ATOM   5066 C  CA    . GLU B 2 153 ? 11.96354  -19.48585 -24.52865 1.000 67.44771  ? 153 GLU A CA    1 
ATOM   5067 C  C     . GLU B 2 153 ? 12.84554  -19.91890 -25.69061 1.000 64.42375  ? 153 GLU A C     1 
ATOM   5068 O  O     . GLU B 2 153 ? 13.48360  -20.97624 -25.63488 1.000 67.75225  ? 153 GLU A O     1 
ATOM   5069 C  CB    . GLU B 2 153 ? 10.52038  -19.93475 -24.75688 1.000 63.70305  ? 153 GLU A CB    1 
ATOM   5070 C  CG    . GLU B 2 153 ? 9.65397   -19.90797 -23.51324 1.000 64.25074  ? 153 GLU A CG    1 
ATOM   5071 C  CD    . GLU B 2 153 ? 8.33646   -20.62368 -23.72070 1.000 79.39977  ? 153 GLU A CD    1 
ATOM   5072 O  OE1   . GLU B 2 153 ? 8.25078   -21.44766 -24.65659 1.000 82.86605  ? 153 GLU A OE1   1 
ATOM   5073 O  OE2   . GLU B 2 153 ? 7.38647   -20.36170 -22.95357 1.000 88.29416  ? 153 GLU A OE2   1 
ATOM   5074 N  N     . ASP B 2 154 ? 12.90197  -19.10491 -26.74794 1.000 67.87132  ? 154 ASP A N     1 
ATOM   5075 C  CA    . ASP B 2 154 ? 13.71319  -19.44625 -27.91167 1.000 65.78373  ? 154 ASP A CA    1 
ATOM   5076 C  C     . ASP B 2 154 ? 15.17696  -19.63055 -27.53025 1.000 69.85844  ? 154 ASP A C     1 
ATOM   5077 O  O     . ASP B 2 154 ? 15.83784  -20.56242 -28.00476 1.000 66.64321  ? 154 ASP A O     1 
ATOM   5078 C  CB    . ASP B 2 154 ? 13.56696  -18.36138 -28.97993 1.000 60.19711  ? 154 ASP A CB    1 
ATOM   5079 C  CG    . ASP B 2 154 ? 14.11432  -18.78846 -30.33177 1.000 75.24241  ? 154 ASP A CG    1 
ATOM   5080 O  OD1   . ASP B 2 154 ? 14.57594  -19.94284 -30.45921 1.000 84.19644  ? 154 ASP A OD1   1 
ATOM   5081 O  OD2   . ASP B 2 154 ? 14.07772  -17.96704 -31.27321 1.000 74.12285  ? 154 ASP A OD2   1 
ATOM   5082 N  N     . ALA B 2 155 ? 15.69340  -18.76292 -26.65717 1.000 69.59626  ? 155 ALA A N     1 
ATOM   5083 C  CA    . ALA B 2 155 ? 17.11204  -18.79741 -26.31838 1.000 63.09693  ? 155 ALA A CA    1 
ATOM   5084 C  C     . ALA B 2 155 ? 17.47365  -20.07356 -25.56961 1.000 67.88807  ? 155 ALA A C     1 
ATOM   5085 O  O     . ALA B 2 155 ? 18.38310  -20.80772 -25.97554 1.000 59.66912  ? 155 ALA A O     1 
ATOM   5086 C  CB    . ALA B 2 155 ? 17.48022  -17.56506 -25.49304 1.000 63.22732  ? 155 ALA A CB    1 
ATOM   5087 N  N     . PHE B 2 156 ? 16.77210  -20.35383 -24.46994 1.000 62.35220  ? 156 PHE A N     1 
ATOM   5088 C  CA    . PHE B 2 156 ? 17.10525  -21.52286 -23.66418 1.000 58.52552  ? 156 PHE A CA    1 
ATOM   5089 C  C     . PHE B 2 156 ? 16.81947  -22.81619 -24.41596 1.000 69.18852  ? 156 PHE A C     1 
ATOM   5090 O  O     . PHE B 2 156 ? 17.55622  -23.79837 -24.26869 1.000 71.08543  ? 156 PHE A O     1 
ATOM   5091 C  CB    . PHE B 2 156 ? 16.33753  -21.48907 -22.34292 1.000 57.78700  ? 156 PHE A CB    1 
ATOM   5092 C  CG    . PHE B 2 156 ? 16.77092  -20.38848 -21.41396 1.000 65.30948  ? 156 PHE A CG    1 
ATOM   5093 C  CD1   . PHE B 2 156 ? 16.21413  -19.12320 -21.50611 1.000 65.26670  ? 156 PHE A CD1   1 
ATOM   5094 C  CD2   . PHE B 2 156 ? 17.72779  -20.62255 -20.44061 1.000 67.91719  ? 156 PHE A CD2   1 
ATOM   5095 C  CE1   . PHE B 2 156 ? 16.60757  -18.11153 -20.65123 1.000 47.53014  ? 156 PHE A CE1   1 
ATOM   5096 C  CE2   . PHE B 2 156 ? 18.12313  -19.61355 -19.58066 1.000 66.82153  ? 156 PHE A CE2   1 
ATOM   5097 C  CZ    . PHE B 2 156 ? 17.56089  -18.35652 -19.68831 1.000 45.25303  ? 156 PHE A CZ    1 
ATOM   5098 N  N     . TYR B 2 157 ? 15.76015  -22.83825 -25.23042 1.000 65.35492  ? 157 TYR A N     1 
ATOM   5099 C  CA    . TYR B 2 157 ? 15.41432  -24.06759 -25.93820 1.000 65.53945  ? 157 TYR A CA    1 
ATOM   5100 C  C     . TYR B 2 157 ? 16.41146  -24.35835 -27.05342 1.000 69.51458  ? 157 TYR A C     1 
ATOM   5101 O  O     . TYR B 2 157 ? 16.76953  -25.51911 -27.28478 1.000 66.21076  ? 157 TYR A O     1 
ATOM   5102 C  CB    . TYR B 2 157 ? 13.99137  -23.98665 -26.49677 1.000 73.22527  ? 157 TYR A CB    1 
ATOM   5103 C  CG    . TYR B 2 157 ? 12.89361  -23.96383 -25.44827 1.000 72.24666  ? 157 TYR A CG    1 
ATOM   5104 C  CD1   . TYR B 2 157 ? 13.19335  -23.94182 -24.09056 1.000 65.12063  ? 157 TYR A CD1   1 
ATOM   5105 C  CD2   . TYR B 2 157 ? 11.55500  -23.97199 -25.82018 1.000 65.74066  ? 157 TYR A CD2   1 
ATOM   5106 C  CE1   . TYR B 2 157 ? 12.19492  -23.92202 -23.13615 1.000 68.95045  ? 157 TYR A CE1   1 
ATOM   5107 C  CE2   . TYR B 2 157 ? 10.54788  -23.95370 -24.87081 1.000 67.33844  ? 157 TYR A CE2   1 
ATOM   5108 C  CZ    . TYR B 2 157 ? 10.87472  -23.92944 -23.53099 1.000 68.31416  ? 157 TYR A CZ    1 
ATOM   5109 O  OH    . TYR B 2 157 ? 9.88015   -23.91036 -22.58183 1.000 68.52206  ? 157 TYR A OH    1 
ATOM   5110 N  N     . THR B 2 158 ? 16.87203  -23.31759 -27.75398 1.000 70.10203  ? 158 THR A N     1 
ATOM   5111 C  CA    . THR B 2 158 ? 17.89478  -23.51011 -28.77829 1.000 67.54789  ? 158 THR A CA    1 
ATOM   5112 C  C     . THR B 2 158 ? 19.17862  -24.06115 -28.17361 1.000 60.22677  ? 158 THR A C     1 
ATOM   5113 O  O     . THR B 2 158 ? 19.84172  -24.91392 -28.77458 1.000 66.02978  ? 158 THR A O     1 
ATOM   5114 C  CB    . THR B 2 158 ? 18.17090  -22.19304 -29.50330 1.000 66.23828  ? 158 THR A CB    1 
ATOM   5115 O  OG1   . THR B 2 158 ? 16.97121  -21.73176 -30.13772 1.000 64.46912  ? 158 THR A OG1   1 
ATOM   5116 C  CG2   . THR B 2 158 ? 19.25579  -22.37378 -30.55077 1.000 52.77299  ? 158 THR A CG2   1 
ATOM   5117 N  N     . LEU B 2 159 ? 19.54110  -23.58991 -26.97938 1.000 57.17600  ? 159 LEU A N     1 
ATOM   5118 C  CA    . LEU B 2 159 ? 20.72043  -24.11914 -26.30448 1.000 56.49886  ? 159 LEU A CA    1 
ATOM   5119 C  C     . LEU B 2 159 ? 20.54932  -25.59613 -25.97947 1.000 59.35642  ? 159 LEU A C     1 
ATOM   5120 O  O     . LEU B 2 159 ? 21.48419  -26.38770 -26.14630 1.000 69.24414  ? 159 LEU A O     1 
ATOM   5121 C  CB    . LEU B 2 159 ? 21.00204  -23.31549 -25.03510 1.000 58.92128  ? 159 LEU A CB    1 
ATOM   5122 C  CG    . LEU B 2 159 ? 22.16395  -23.80347 -24.17085 1.000 58.68485  ? 159 LEU A CG    1 
ATOM   5123 C  CD1   . LEU B 2 159 ? 23.43602  -23.91094 -24.99641 1.000 60.44587  ? 159 LEU A CD1   1 
ATOM   5124 C  CD2   . LEU B 2 159 ? 22.36636  -22.88008 -22.97970 1.000 55.24204  ? 159 LEU A CD2   1 
ATOM   5125 N  N     . VAL B 2 160 ? 19.35870  -25.98669 -25.51840 1.000 64.83914  ? 160 VAL A N     1 
ATOM   5126 C  CA    . VAL B 2 160 ? 19.09023  -27.39555 -25.24346 1.000 58.46281  ? 160 VAL A CA    1 
ATOM   5127 C  C     . VAL B 2 160 ? 19.23603  -28.22307 -26.51409 1.000 65.84944  ? 160 VAL A C     1 
ATOM   5128 O  O     . VAL B 2 160 ? 19.80503  -29.32188 -26.49624 1.000 65.99888  ? 160 VAL A O     1 
ATOM   5129 C  CB    . VAL B 2 160 ? 17.69402  -27.55760 -24.61531 1.000 65.72307  ? 160 VAL A CB    1 
ATOM   5130 C  CG1   . VAL B 2 160 ? 17.31808  -29.03001 -24.51684 1.000 61.38825  ? 160 VAL A CG1   1 
ATOM   5131 C  CG2   . VAL B 2 160 ? 17.65814  -26.90162 -23.24372 1.000 67.72713  ? 160 VAL A CG2   1 
ATOM   5132 N  N     . ARG B 2 161 ? 18.73672  -27.70528 -27.63963 1.000 61.55964  ? 161 ARG A N     1 
ATOM   5133 C  CA    . ARG B 2 161 ? 18.89816  -28.41017 -28.90620 1.000 64.51471  ? 161 ARG A CA    1 
ATOM   5134 C  C     . ARG B 2 161 ? 20.36545  -28.54488 -29.29133 1.000 73.60061  ? 161 ARG A C     1 
ATOM   5135 O  O     . ARG B 2 161 ? 20.75594  -29.55231 -29.89227 1.000 82.21789  ? 161 ARG A O     1 
ATOM   5136 C  CB    . ARG B 2 161 ? 18.12271  -27.69475 -30.01225 1.000 66.00573  ? 161 ARG A CB    1 
ATOM   5137 C  CG    . ARG B 2 161 ? 16.63615  -27.56314 -29.73546 1.000 64.57726  ? 161 ARG A CG    1 
ATOM   5138 C  CD    . ARG B 2 161 ? 15.90143  -26.97923 -30.92391 1.000 67.34713  ? 161 ARG A CD    1 
ATOM   5139 N  NE    . ARG B 2 161 ? 14.56638  -26.52630 -30.55483 1.000 87.90872  ? 161 ARG A NE    1 
ATOM   5140 C  CZ    . ARG B 2 161 ? 14.24591  -25.26302 -30.31092 1.000 87.88801  ? 161 ARG A CZ    1 
ATOM   5141 N  NH1   . ARG B 2 161 ? 15.13689  -24.29072 -30.42085 1.000 84.67885  ? 161 ARG A NH1   1 
ATOM   5142 N  NH2   . ARG B 2 161 ? 12.99932  -24.96735 -29.95232 1.000 83.32822  ? 161 ARG A NH2   1 
ATOM   5143 N  N     . GLU B 2 162 ? 21.19270  -27.54904 -28.95664 1.000 67.54189  ? 162 GLU A N     1 
ATOM   5144 C  CA    . GLU B 2 162 ? 22.61904  -27.65249 -29.24932 1.000 67.68314  ? 162 GLU A CA    1 
ATOM   5145 C  C     . GLU B 2 162 ? 23.29301  -28.70292 -28.37834 1.000 64.34876  ? 162 GLU A C     1 
ATOM   5146 O  O     . GLU B 2 162 ? 24.27989  -29.31411 -28.80029 1.000 82.77841  ? 162 GLU A O     1 
ATOM   5147 C  CB    . GLU B 2 162 ? 23.30219  -26.29687 -29.06510 1.000 59.39971  ? 162 GLU A CB    1 
ATOM   5148 C  CG    . GLU B 2 162 ? 22.81640  -25.21501 -30.01582 1.000 63.04042  ? 162 GLU A CG    1 
ATOM   5149 C  CD    . GLU B 2 162 ? 23.29893  -25.42176 -31.43634 1.000 78.23743  ? 162 GLU A CD    1 
ATOM   5150 O  OE1   . GLU B 2 162 ? 24.52834  -25.36877 -31.66212 1.000 74.28222  ? 162 GLU A OE1   1 
ATOM   5151 O  OE2   . GLU B 2 162 ? 22.44850  -25.64281 -32.32595 1.000 75.25174  ? 162 GLU A OE2   1 
ATOM   5152 N  N     . ILE B 2 163 ? 22.78388  -28.92255 -27.16517 1.000 74.16597  ? 163 ILE A N     1 
ATOM   5153 C  CA    . ILE B 2 163 ? 23.33287  -29.97027 -26.31041 1.000 65.36995  ? 163 ILE A CA    1 
ATOM   5154 C  C     . ILE B 2 163 ? 22.94629  -31.34534 -26.83988 1.000 72.41003  ? 163 ILE A C     1 
ATOM   5155 O  O     . ILE B 2 163 ? 23.73580  -32.29509 -26.77424 1.000 72.41857  ? 163 ILE A O     1 
ATOM   5156 C  CB    . ILE B 2 163 ? 22.86838  -29.76936 -24.85689 1.000 66.39786  ? 163 ILE A CB    1 
ATOM   5157 C  CG1   . ILE B 2 163 ? 23.38752  -28.43868 -24.31382 1.000 62.66193  ? 163 ILE A CG1   1 
ATOM   5158 C  CG2   . ILE B 2 163 ? 23.32514  -30.92639 -23.98032 1.000 67.44228  ? 163 ILE A CG2   1 
ATOM   5159 C  CD1   . ILE B 2 163 ? 23.10683  -28.23233 -22.84548 1.000 58.18322  ? 163 ILE A CD1   1 
ATOM   5160 N  N     . ARG B 2 164 ? 21.72651  -31.47568 -27.36970 1.000 76.08194  ? 164 ARG A N     1 
ATOM   5161 C  CA    . ARG B 2 164 ? 21.30369  -32.74029 -27.96506 1.000 84.28147  ? 164 ARG A CA    1 
ATOM   5162 C  C     . ARG B 2 164 ? 22.21211  -33.12729 -29.12449 1.000 88.58732  ? 164 ARG A C     1 
ATOM   5163 O  O     . ARG B 2 164 ? 22.65062  -34.27912 -29.22807 1.000 92.90039  ? 164 ARG A O     1 
ATOM   5164 C  CB    . ARG B 2 164 ? 19.85174  -32.64330 -28.43673 1.000 77.34434  ? 164 ARG A CB    1 
ATOM   5165 C  CG    . ARG B 2 164 ? 18.82316  -32.57368 -27.32483 1.000 74.09405  ? 164 ARG A CG    1 
ATOM   5166 C  CD    . ARG B 2 164 ? 17.46523  -32.19359 -27.88988 1.000 80.37325  ? 164 ARG A CD    1 
ATOM   5167 N  NE    . ARG B 2 164 ? 16.42304  -32.17017 -26.87140 1.000 70.09860  ? 164 ARG A NE    1 
ATOM   5168 C  CZ    . ARG B 2 164 ? 15.23157  -31.61316 -27.03755 1.000 69.14382  ? 164 ARG A CZ    1 
ATOM   5169 N  NH1   . ARG B 2 164 ? 14.90545  -31.00264 -28.16557 1.000 67.49769  ? 164 ARG A NH1   1 
ATOM   5170 N  NH2   . ARG B 2 164 ? 14.34727  -31.66496 -26.04573 1.000 65.50575  ? 164 ARG A NH2   1 
ATOM   5171 N  N     . GLN B 2 165 ? 22.50011  -32.17014 -30.01267 1.000 85.97701  ? 165 GLN A N     1 
ATOM   5172 C  CA    . GLN B 2 165 ? 23.40295  -32.42995 -31.12882 1.000 86.80775  ? 165 GLN A CA    1 
ATOM   5173 C  C     . GLN B 2 165 ? 24.76339  -32.91395 -30.64404 1.000 82.01065  ? 165 GLN A C     1 
ATOM   5174 O  O     . GLN B 2 165 ? 25.39067  -33.75907 -31.29370 1.000 84.46355  ? 165 GLN A O     1 
ATOM   5175 C  CB    . GLN B 2 165 ? 23.55199  -31.16640 -31.97901 1.000 73.37758  ? 165 GLN A CB    1 
ATOM   5176 C  CG    . GLN B 2 165 ? 24.46145  -31.31970 -33.18894 1.000 83.89570  ? 165 GLN A CG    1 
ATOM   5177 C  CD    . GLN B 2 165 ? 23.89509  -32.25983 -34.23567 1.000 93.43425  ? 165 GLN A CD    1 
ATOM   5178 O  OE1   . GLN B 2 165 ? 22.67842  -32.40214 -34.37003 1.000 100.95552 ? 165 GLN A OE1   1 
ATOM   5179 N  NE2   . GLN B 2 165 ? 24.77803  -32.90916 -34.98345 1.000 81.17101  ? 165 GLN A NE2   1 
ATOM   5180 N  N     . TYR B 2 166 ? 25.22352  -32.40505 -29.49947 1.000 76.56205  ? 166 TYR A N     1 
ATOM   5181 C  CA    . TYR B 2 166 ? 26.50204  -32.83719 -28.94493 1.000 78.98182  ? 166 TYR A CA    1 
ATOM   5182 C  C     . TYR B 2 166 ? 26.43052  -34.28092 -28.46134 1.000 85.75374  ? 166 TYR A C     1 
ATOM   5183 O  O     . TYR B 2 166 ? 27.33202  -35.08255 -28.73204 1.000 94.54273  ? 166 TYR A O     1 
ATOM   5184 C  CB    . TYR B 2 166 ? 26.91314  -31.90069 -27.80644 1.000 74.12506  ? 166 TYR A CB    1 
ATOM   5185 C  CG    . TYR B 2 166 ? 28.24264  -32.22546 -27.15950 1.000 79.88989  ? 166 TYR A CG    1 
ATOM   5186 C  CD1   . TYR B 2 166 ? 28.32981  -33.15247 -26.12684 1.000 82.13192  ? 166 TYR A CD1   1 
ATOM   5187 C  CD2   . TYR B 2 166 ? 29.40750  -31.58774 -27.56587 1.000 85.20798  ? 166 TYR A CD2   1 
ATOM   5188 C  CE1   . TYR B 2 166 ? 29.54144  -33.44619 -25.52913 1.000 91.46762  ? 166 TYR A CE1   1 
ATOM   5189 C  CE2   . TYR B 2 166 ? 30.62429  -31.87402 -26.97280 1.000 90.87055  ? 166 TYR A CE2   1 
ATOM   5190 C  CZ    . TYR B 2 166 ? 30.68514  -32.80348 -25.95526 1.000 86.75490  ? 166 TYR A CZ    1 
ATOM   5191 O  OH    . TYR B 2 166 ? 31.89290  -33.09255 -25.36290 1.000 85.62698  ? 166 TYR A OH    1 
ATOM   5192 N  N     . ARG B 2 167 ? 25.36612  -34.63012 -27.73507 1.000 83.16620  ? 167 ARG A N     1 
ATOM   5193 C  CA    . ARG B 2 167 ? 25.24484  -35.98757 -27.21442 1.000 86.96669  ? 167 ARG A CA    1 
ATOM   5194 C  C     . ARG B 2 167 ? 24.89271  -36.98349 -28.31044 1.000 89.88522  ? 167 ARG A C     1 
ATOM   5195 O  O     . ARG B 2 167 ? 25.21153  -38.17237 -28.19180 1.000 94.96750  ? 167 ARG A O     1 
ATOM   5196 C  CB    . ARG B 2 167 ? 24.19086  -36.03470 -26.11116 1.000 77.37171  ? 167 ARG A CB    1 
ATOM   5197 C  CG    . ARG B 2 167 ? 24.45274  -35.09311 -24.95823 1.000 67.71670  ? 167 ARG A CG    1 
ATOM   5198 C  CD    . ARG B 2 167 ? 23.24997  -35.03116 -24.04150 1.000 63.84497  ? 167 ARG A CD    1 
ATOM   5199 N  NE    . ARG B 2 167 ? 23.50224  -34.21274 -22.86300 1.000 75.20201  ? 167 ARG A NE    1 
ATOM   5200 C  CZ    . ARG B 2 167 ? 22.58234  -33.89861 -21.96151 1.000 76.81808  ? 167 ARG A CZ    1 
ATOM   5201 N  NH1   . ARG B 2 167 ? 21.32748  -34.29858 -22.08672 1.000 81.00131  ? 167 ARG A NH1   1 
ATOM   5202 N  NH2   . ARG B 2 167 ? 22.92963  -33.16375 -20.90879 1.000 80.58203  ? 167 ARG A NH2   1 
ATOM   5203 N  N     . MET B 2 168 ? 24.24169  -36.52415 -29.37341 1.000 85.33140  ? 168 MET A N     1 
ATOM   5204 C  CA    . MET B 2 168 ? 23.78171  -37.40801 -30.43596 1.000 93.54612  ? 168 MET A CA    1 
ATOM   5205 C  C     . MET B 2 168 ? 24.57099  -37.17617 -31.72116 1.000 82.57543  ? 168 MET A C     1 
ATOM   5206 O  O     . MET B 2 168 ? 24.31175  -37.81108 -32.74272 1.000 92.70919  ? 168 MET A O     1 
ATOM   5207 C  CB    . MET B 2 168 ? 22.28320  -37.20131 -30.68270 1.000 97.15890  ? 168 MET A CB    1 
ATOM   5208 C  CG    . MET B 2 168 ? 21.42599  -37.33332 -29.42566 1.000 95.27282  ? 168 MET A CG    1 
ATOM   5209 S  SD    . MET B 2 168 ? 19.76355  -36.62800 -29.57321 1.000 106.44640 ? 168 MET A SD    1 
ATOM   5210 C  CE    . MET B 2 168 ? 19.07322  -37.62069 -30.88787 1.000 82.31018  ? 168 MET A CE    1 
HETATM 5211 P  PG    . GTP C 3 .   ? 24.83287  -9.34148  -12.85570 1.000 65.91288  ? 201 GTP A PG    1 
HETATM 5212 O  O1G   . GTP C 3 .   ? 25.81393  -8.32686  -12.31639 1.000 72.63498  ? 201 GTP A O1G   1 
HETATM 5213 O  O2G   . GTP C 3 .   ? 24.12144  -9.98354  -11.68854 1.000 63.45782  ? 201 GTP A O2G   1 
HETATM 5214 O  O3G   . GTP C 3 .   ? 25.57930  -10.37504 -13.66621 1.000 56.24860  ? 201 GTP A O3G   1 
HETATM 5215 O  O3B   . GTP C 3 .   ? 23.77059  -8.57556  -13.79703 1.000 69.97941  ? 201 GTP A O3B   1 
HETATM 5216 P  PB    . GTP C 3 .   ? 22.63552  -9.39779  -14.59474 1.000 63.43943  ? 201 GTP A PB    1 
HETATM 5217 O  O1B   . GTP C 3 .   ? 22.05433  -10.45084 -13.68206 1.000 57.77462  ? 201 GTP A O1B   1 
HETATM 5218 O  O2B   . GTP C 3 .   ? 23.18467  -10.02692 -15.85279 1.000 64.20870  ? 201 GTP A O2B   1 
HETATM 5219 O  O3A   . GTP C 3 .   ? 21.51530  -8.29307  -14.95330 1.000 64.06815  ? 201 GTP A O3A   1 
HETATM 5220 P  PA    . GTP C 3 .   ? 20.00985  -8.40689  -14.39671 1.000 66.39026  ? 201 GTP A PA    1 
HETATM 5221 O  O1A   . GTP C 3 .   ? 20.03623  -8.53546  -12.89187 1.000 69.50931  ? 201 GTP A O1A   1 
HETATM 5222 O  O2A   . GTP C 3 .   ? 19.26783  -9.56189  -15.02533 1.000 61.95465  ? 201 GTP A O2A   1 
HETATM 5223 O  "O5'" . GTP C 3 .   ? 19.32099  -7.00713  -14.77281 1.000 62.78745  ? 201 GTP A "O5'" 1 
HETATM 5224 C  "C5'" . GTP C 3 .   ? 20.06937  -5.87322  -15.14121 1.000 68.67158  ? 201 GTP A "C5'" 1 
HETATM 5225 C  "C4'" . GTP C 3 .   ? 19.09967  -4.70386  -15.18288 1.000 64.62319  ? 201 GTP A "C4'" 1 
HETATM 5226 O  "O4'" . GTP C 3 .   ? 18.61449  -4.61682  -16.50229 1.000 70.33594  ? 201 GTP A "O4'" 1 
HETATM 5227 C  "C3'" . GTP C 3 .   ? 17.90714  -4.95976  -14.27961 1.000 73.02785  ? 201 GTP A "C3'" 1 
HETATM 5228 O  "O3'" . GTP C 3 .   ? 17.68505  -3.82254  -13.48324 1.000 73.37085  ? 201 GTP A "O3'" 1 
HETATM 5229 C  "C2'" . GTP C 3 .   ? 16.72428  -5.16994  -15.20092 1.000 66.62715  ? 201 GTP A "C2'" 1 
HETATM 5230 O  "O2'" . GTP C 3 .   ? 15.59530  -4.44980  -14.76119 1.000 79.08123  ? 201 GTP A "O2'" 1 
HETATM 5231 C  "C1'" . GTP C 3 .   ? 17.20500  -4.66256  -16.54705 1.000 69.16177  ? 201 GTP A "C1'" 1 
HETATM 5232 N  N9    . GTP C 3 .   ? 16.82782  -5.60363  -17.60736 1.000 75.16649  ? 201 GTP A N9    1 
HETATM 5233 C  C8    . GTP C 3 .   ? 17.13353  -6.93711  -17.67294 1.000 72.85197  ? 201 GTP A C8    1 
HETATM 5234 N  N7    . GTP C 3 .   ? 16.60963  -7.43679  -18.81532 1.000 70.88456  ? 201 GTP A N7    1 
HETATM 5235 C  C5    . GTP C 3 .   ? 15.98292  -6.43769  -19.47739 1.000 75.77243  ? 201 GTP A C5    1 
HETATM 5236 C  C6    . GTP C 3 .   ? 15.28950  -6.39285  -20.68029 1.000 80.32646  ? 201 GTP A C6    1 
HETATM 5237 O  O6    . GTP C 3 .   ? 15.15781  -7.40956  -21.36157 1.000 77.43472  ? 201 GTP A O6    1 
HETATM 5238 N  N1    . GTP C 3 .   ? 14.74842  -5.19648  -21.10672 1.000 84.65496  ? 201 GTP A N1    1 
HETATM 5239 C  C2    . GTP C 3 .   ? 14.89732  -4.05747  -20.34082 1.000 74.14916  ? 201 GTP A C2    1 
HETATM 5240 N  N2    . GTP C 3 .   ? 14.37610  -2.90503  -20.74739 1.000 82.59404  ? 201 GTP A N2    1 
HETATM 5241 N  N3    . GTP C 3 .   ? 15.58545  -4.11059  -19.14967 1.000 68.09021  ? 201 GTP A N3    1 
HETATM 5242 C  C4    . GTP C 3 .   ? 16.11740  -5.27958  -18.72786 1.000 72.09374  ? 201 GTP A C4    1 
HETATM 5243 MG MG    . MG  D 4 .   ? 22.64082  -11.53839 -12.15813 1.000 61.20175  ? 202 MG  A MG    1 
HETATM 5244 O  O     . HOH E 5 .   ? 4.79398   5.22866   -27.40703 1.000 68.25200  ? 601 HOH B O     1 
HETATM 5245 O  O     . HOH E 5 .   ? 23.91521  -15.18239 -2.48156  1.000 62.46931  ? 602 HOH B O     1 
HETATM 5246 O  O     . HOH E 5 .   ? 13.65347  0.91776   7.68337   1.000 64.00035  ? 603 HOH B O     1 
HETATM 5247 O  O     . HOH F 5 .   ? 26.21467  -23.78443 -30.04117 1.000 60.93513  ? 301 HOH A O     1 
HETATM 5248 O  O     . HOH F 5 .   ? 20.87331  -13.03867 -8.95126  1.000 55.29447  ? 302 HOH A O     1 
HETATM 5249 O  O     . HOH F 5 .   ? 21.33266  -10.20875 -11.00268 1.000 61.25843  ? 303 HOH A O     1 
HETATM 5250 O  O     . HOH F 5 .   ? 15.54704  -40.96579 -15.56150 1.000 64.50721  ? 304 HOH A O     1 
HETATM 5251 O  O     . HOH F 5 .   ? 23.31089  -13.07214 -13.21131 1.000 61.17395  ? 305 HOH A O     1 
HETATM 5252 O  O     . HOH F 5 .   ? 9.59332   -36.91697 -22.84050 1.000 60.18597  ? 306 HOH A 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 7   ? 1.49485 1.21882 1.53948 -0.00199 -0.09124 0.09869  86  SER B N     
2    C  CA    . SER A 7   ? 1.62441 1.33597 1.66862 0.00250  -0.09397 0.11613  86  SER B CA    
3    C  C     . SER A 7   ? 1.55454 1.26228 1.59188 0.01277  -0.09971 0.10858  86  SER B C     
4    O  O     . SER A 7   ? 1.59977 1.31569 1.63355 0.01589  -0.10070 0.09055  86  SER B O     
5    C  CB    . SER A 7   ? 1.56858 1.26326 1.63804 -0.00261 -0.10021 0.12399  86  SER B CB    
6    O  OG    . SER A 7   ? 1.62244 1.30367 1.70578 0.00252  -0.11047 0.11252  86  SER B OG    
7    N  N     . ASN A 8   ? 1.54040 1.23644 1.57683 0.01797  -0.10360 0.12327  87  ASN B N     
8    C  CA    . ASN A 8   ? 1.62272 1.31495 1.65306 0.02818  -0.10991 0.11790  87  ASN B CA    
9    C  C     . ASN A 8   ? 1.74945 1.43145 1.80113 0.03068  -0.11943 0.10176  87  ASN B C     
10   O  O     . ASN A 8   ? 1.69520 1.37855 1.74427 0.03872  -0.12413 0.09124  87  ASN B O     
11   C  CB    . ASN A 8   ? 1.44403 1.12741 1.46527 0.03354  -0.11147 0.13962  87  ASN B CB    
12   C  CG    . ASN A 8   ? 1.56796 1.24789 1.58197 0.04455  -0.11886 0.13494  87  ASN B CG    
13   O  OD1   . ASN A 8   ? 1.46518 1.13154 1.49495 0.04836  -0.12792 0.13265  87  ASN B OD1   
14   N  ND2   . ASN A 8   ? 1.60069 1.29269 1.59204 0.04992  -0.11582 0.13304  87  ASN B ND2   
15   N  N     . ALA A 9   ? 1.72449 1.39671 1.79805 0.02440  -0.12280 0.09898  88  ALA B N     
16   C  CA    . ALA A 9   ? 1.68112 1.34294 1.77531 0.02785  -0.13238 0.08241  88  ALA B CA    
17   C  C     . ALA A 9   ? 1.79560 1.47226 1.88588 0.03115  -0.13111 0.05838  88  ALA B C     
18   O  O     . ALA A 9   ? 1.68643 1.36098 1.78316 0.03911  -0.13722 0.04597  88  ALA B O     
19   C  CB    . ALA A 9   ? 1.57372 1.22294 1.69168 0.02000  -0.13660 0.08240  88  ALA B CB    
20   N  N     . GLU A 10  ? 1.97315 1.66587 2.05349 0.02532  -0.12301 0.05236  89  GLU B N     
21   C  CA    . GLU A 10  ? 1.99547 1.70407 2.07142 0.02789  -0.12077 0.03185  89  GLU B CA    
22   C  C     . GLU A 10  ? 2.00268 1.72170 2.06206 0.03476  -0.11861 0.03217  89  GLU B C     
23   O  O     . GLU A 10  ? 1.96556 1.69449 2.02649 0.03951  -0.11947 0.01642  89  GLU B O     
24   C  CB    . GLU A 10  ? 1.94913 1.67148 2.01940 0.01954  -0.11329 0.02681  89  GLU B CB    
25   C  CG    . GLU A 10  ? 1.89435 1.61042 1.98246 0.01366  -0.11686 0.01827  89  GLU B CG    
26   C  CD    . GLU A 10  ? 1.94206 1.64312 2.04071 0.00715  -0.11895 0.03579  89  GLU B CD    
27   O  OE1   . GLU A 10  ? 1.97143 1.65546 2.08133 0.01030  -0.12570 0.04436  89  GLU B OE1   
28   O  OE2   . GLU A 10  ? 1.89990 1.60676 1.99666 -0.00120 -0.11388 0.04183  89  GLU B OE2   
29   N  N     . VAL A 11  ? 1.73964 1.45731 1.78371 0.03567  -0.11605 0.04970  90  VAL B N     
30   C  CA    . VAL A 11  ? 1.60883 1.33683 1.63599 0.04158  -0.11455 0.04957  90  VAL B CA    
31   C  C     . VAL A 11  ? 1.59770 1.32097 1.63314 0.05097  -0.12297 0.04201  90  VAL B C     
32   O  O     . VAL A 11  ? 1.58140 1.31671 1.61733 0.05456  -0.12318 0.02808  90  VAL B O     
33   C  CB    . VAL A 11  ? 1.54356 1.27001 1.55188 0.04188  -0.11101 0.06942  90  VAL B CB    
34   C  CG1   . VAL A 11  ? 1.35848 1.09366 1.35020 0.04883  -0.11171 0.06783  90  VAL B CG1   
35   C  CG2   . VAL A 11  ? 1.42521 1.15902 1.42622 0.03324  -0.10209 0.07581  90  VAL B CG2   
36   N  N     . ILE A 12  ? 1.58799 1.29421 1.63130 0.05506  -0.13010 0.05196  91  ILE B N     
37   C  CA    . ILE A 12  ? 1.61649 1.31763 1.66777 0.06476  -0.13888 0.04627  91  ILE B CA    
38   C  C     . ILE A 12  ? 1.55636 1.25924 1.62817 0.06673  -0.14241 0.02574  91  ILE B C     
39   O  O     . ILE A 12  ? 1.54414 1.25350 1.62116 0.07409  -0.14626 0.01436  91  ILE B O     
40   C  CB    . ILE A 12  ? 1.59104 1.27287 1.64536 0.06875  -0.14594 0.06372  91  ILE B CB    
41   C  CG1   . ILE A 12  ? 1.55482 1.23723 1.58689 0.06719  -0.14102 0.08440  91  ILE B CG1   
42   C  CG2   . ILE A 12  ? 1.35592 1.03328 1.41677 0.07956  -0.15558 0.05891  91  ILE B CG2   
43   C  CD1   . ILE A 12  ? 1.51509 1.18115 1.54653 0.07194  -0.14720 0.10378  91  ILE B CD1   
44   N  N     . LYS A 13  ? 1.58775 1.28598 1.67181 0.06071  -0.14136 0.02007  92  LYS B N     
45   C  CA    . LYS A 13  ? 1.65593 1.35558 1.75842 0.06391  -0.14515 -0.00054 92  LYS B CA    
46   C  C     . LYS A 13  ? 1.59010 1.31294 1.68671 0.06339  -0.13820 -0.01693 92  LYS B C     
47   O  O     . LYS A 13  ? 1.59121 1.32144 1.69841 0.06993  -0.14065 -0.03317 92  LYS B O     
48   C  CB    . LYS A 13  ? 1.71808 1.40446 1.83584 0.05822  -0.14786 -0.00251 92  LYS B CB    
49   C  CG    . LYS A 13  ? 1.69737 1.35989 1.83290 0.06221  -0.15856 0.00452  92  LYS B CG    
50   C  CD    . LYS A 13  ? 1.61906 1.27009 1.77579 0.05940  -0.16400 -0.00697 92  LYS B CD    
51   C  CE    . LYS A 13  ? 1.53094 1.15757 1.70845 0.06456  -0.17611 -0.00231 92  LYS B CE    
52   N  NZ    . LYS A 13  ? 1.47817 1.09260 1.67825 0.06303  -0.18325 -0.01657 92  LYS B NZ    
53   N  N     . GLU A 14  ? 1.55279 1.28801 1.63348 0.05602  -0.12941 -0.01253 93  GLU B N     
54   C  CA    . GLU A 14  ? 1.59080 1.34808 1.66597 0.05509  -0.12280 -0.02580 93  GLU B CA    
55   C  C     . GLU A 14  ? 1.54376 1.31239 1.61239 0.06090  -0.12277 -0.02615 93  GLU B C     
56   O  O     . GLU A 14  ? 1.47063 1.25747 1.54044 0.06193  -0.11890 -0.03821 93  GLU B O     
57   C  CB    . GLU A 14  ? 1.50346 1.26966 1.56518 0.04546  -0.11426 -0.02091 93  GLU B CB    
58   C  CG    . GLU A 14  ? 1.48866 1.27583 1.54825 0.04342  -0.10796 -0.03551 93  GLU B CG    
59   C  CD    . GLU A 14  ? 1.54457 1.33935 1.59249 0.03418  -0.10062 -0.03087 93  GLU B CD    
60   O  OE1   . GLU A 14  ? 1.54347 1.32668 1.58975 0.02896  -0.10081 -0.01971 93  GLU B OE1   
61   O  OE2   . GLU A 14  ? 1.48588 1.29886 1.52732 0.03212  -0.09466 -0.03769 93  GLU B OE2   
62   N  N     . LEU A 15  ? 1.49129 1.25026 1.55348 0.06474  -0.12727 -0.01291 94  LEU B N     
63   C  CA    . LEU A 15  ? 1.43187 1.19962 1.49162 0.07140  -0.13006 -0.01488 94  LEU B CA    
64   C  C     . LEU A 15  ? 1.55121 1.32151 1.63060 0.07945  -0.13565 -0.02936 94  LEU B C     
65   O  O     . LEU A 15  ? 1.45677 1.24440 1.54034 0.08231  -0.13394 -0.03961 94  LEU B O     
66   C  CB    . LEU A 15  ? 1.44718 1.20289 1.49527 0.07495  -0.13511 0.00179  94  LEU B CB    
67   C  CG    . LEU A 15  ? 1.34189 1.09999 1.36803 0.06959  -0.12934 0.01483  94  LEU B CG    
68   C  CD1   . LEU A 15  ? 1.35915 1.10718 1.37305 0.07546  -0.13507 0.02934  94  LEU B CD1   
69   C  CD2   . LEU A 15  ? 1.31729 1.09483 1.33618 0.06658  -0.12356 0.00706  94  LEU B CD2   
70   N  N     . ASN A 16  ? 1.80039 1.55387 1.89350 0.08331  -0.14243 -0.03014 95  ASN B N     
71   C  CA    . ASN A 16  ? 1.74781 1.50345 1.86106 0.09155  -0.14754 -0.04580 95  ASN B CA    
72   C  C     . ASN A 16  ? 1.71122 1.48342 1.83071 0.08939  -0.14086 -0.06355 95  ASN B C     
73   O  O     . ASN A 16  ? 1.62550 1.41159 1.75651 0.09593  -0.14091 -0.07776 95  ASN B O     
74   C  CB    . ASN A 16  ? 1.68780 1.41971 1.81502 0.09579  -0.15687 -0.04267 95  ASN B CB    
75   C  CG    . ASN A 16  ? 1.69990 1.41963 1.82708 0.10285  -0.16564 -0.03038 95  ASN B CG    
76   O  OD1   . ASN A 16  ? 1.71565 1.43818 1.85512 0.11208  -0.17177 -0.03825 95  ASN B OD1   
77   N  ND2   . ASN A 16  ? 1.78488 1.49209 1.89811 0.09904  -0.16625 -0.01076 95  ASN B ND2   
78   N  N     . LYS A 17  ? 1.51234 1.28453 1.62438 0.08071  -0.13504 -0.06274 96  LYS B N     
79   C  CA    . LYS A 17  ? 1.48949 1.27883 1.60374 0.07850  -0.12843 -0.07854 96  LYS B CA    
80   C  C     . LYS A 17  ? 1.45570 1.27021 1.56226 0.07769  -0.12080 -0.08182 96  LYS B C     
81   O  O     . LYS A 17  ? 1.43049 1.26308 1.54374 0.08054  -0.11670 -0.09648 96  LYS B O     
82   C  CB    . LYS A 17  ? 1.42773 1.21142 1.53454 0.06893  -0.12474 -0.07495 96  LYS B CB    
83   C  CG    . LYS A 17  ? 1.33531 1.13690 1.44051 0.06594  -0.11794 -0.08956 96  LYS B CG    
84   C  CD    . LYS A 17  ? 1.34897 1.14260 1.44901 0.05689  -0.11648 -0.08566 96  LYS B CD    
85   C  CE    . LYS A 17  ? 1.34436 1.15716 1.43933 0.05373  -0.10974 -0.09863 96  LYS B CE    
86   N  NZ    . LYS A 17  ? 1.38387 1.21745 1.46423 0.04998  -0.10064 -0.09368 96  LYS B NZ    
87   N  N     . CYS A 18  ? 1.44815 1.26447 1.54135 0.07425  -0.11910 -0.06829 97  CYS B N     
88   C  CA    . CYS A 18  ? 1.42730 1.26567 1.51514 0.07274  -0.11312 -0.07007 97  CYS B CA    
89   C  C     . CYS A 18  ? 1.42595 1.27441 1.52777 0.08153  -0.11696 -0.07741 97  CYS B C     
90   O  O     . CYS A 18  ? 1.39655 1.26702 1.50439 0.08225  -0.11155 -0.08675 97  CYS B O     
91   C  CB    . CYS A 18  ? 1.43248 1.26800 1.50262 0.06714  -0.11159 -0.05460 97  CYS B CB    
92   S  SG    . CYS A 18  ? 1.35816 1.21773 1.42368 0.06458  -0.10613 -0.05554 97  CYS B SG    
93   N  N     . ARG A 19  ? 1.43134 1.26513 1.53917 0.08832  -0.12618 -0.07258 98  ARG B N     
94   C  CA    . ARG A 19  ? 1.45593 1.29940 1.57846 0.09699  -0.13080 -0.07910 98  ARG B CA    
95   C  C     . ARG A 19  ? 1.46979 1.31956 1.61168 0.10432  -0.13124 -0.09583 98  ARG B C     
96   O  O     . ARG A 19  ? 1.39240 1.26019 1.54762 0.11013  -0.13059 -0.10474 98  ARG B O     
97   C  CB    . ARG A 19  ? 1.45634 1.28239 1.57816 0.10254  -0.14135 -0.06827 98  ARG B CB    
98   C  CG    . ARG A 19  ? 1.59529 1.39543 1.71639 0.10386  -0.14736 -0.06128 98  ARG B CG    
99   C  CD    . ARG A 19  ? 1.67309 1.45781 1.78828 0.10838  -0.15659 -0.04719 98  ARG B CD    
100  N  NE    . ARG A 19  ? 1.55742 1.34245 1.68962 0.11903  -0.16548 -0.05304 98  ARG B NE    
101  C  CZ    . ARG A 19  ? 1.61750 1.38402 1.75990 0.12593  -0.17460 -0.05053 98  ARG B CZ    
102  N  NH1   . ARG A 19  ? 1.69265 1.43845 1.83086 0.12289  -0.17619 -0.04143 98  ARG B NH1   
103  N  NH2   . ARG A 19  ? 1.53443 1.30345 1.69313 0.13601  -0.18263 -0.05662 98  ARG B NH2   
104  N  N     . GLU A 20  ? 1.50210 1.33792 1.64684 0.10450  -0.13264 -0.10064 99  GLU B N     
105  C  CA    . GLU A 20  ? 1.55267 1.39526 1.71410 0.11185  -0.13271 -0.11884 99  GLU B CA    
106  C  C     . GLU A 20  ? 1.53133 1.40140 1.69041 0.10905  -0.12156 -0.12981 99  GLU B C     
107  O  O     . GLU A 20  ? 1.64956 1.53924 1.82159 0.11620  -0.11896 -0.14215 99  GLU B O     
108  C  CB    . GLU A 20  ? 1.64837 1.46796 1.81350 0.11204  -0.13805 -0.12161 99  GLU B CB    
109  C  CG    . GLU A 20  ? 1.80322 1.63033 1.98078 0.11793  -0.13687 -0.14244 99  GLU B CG    
110  C  CD    . GLU A 20  ? 1.92082 1.75258 2.11899 0.13135  -0.14232 -0.15519 99  GLU B CD    
111  O  OE1   . GLU A 20  ? 1.87968 1.70772 2.08379 0.13588  -0.14792 -0.14739 99  GLU B OE1   
112  O  OE2   . GLU A 20  ? 1.99451 1.83413 2.20291 0.13804  -0.14133 -0.17367 99  GLU B OE2   
113  N  N     . GLU A 21  ? 1.37764 1.25061 1.52043 0.09893  -0.11462 -0.12469 100 GLU B N     
114  C  CA    . GLU A 21  ? 1.35260 1.25215 1.49076 0.09542  -0.10388 -0.13185 100 GLU B CA    
115  C  C     . GLU A 21  ? 1.34133 1.26143 1.48037 0.09434  -0.09959 -0.12646 100 GLU B C     
116  O  O     . GLU A 21  ? 1.27102 1.21647 1.41168 0.09349  -0.09098 -0.13277 100 GLU B O     
117  C  CB    . GLU A 21  ? 1.35044 1.24674 1.47114 0.08476  -0.09866 -0.12605 100 GLU B CB    
118  C  CG    . GLU A 21  ? 1.36158 1.24002 1.48295 0.08445  -0.10274 -0.13205 100 GLU B CG    
119  C  CD    . GLU A 21  ? 1.41911 1.29562 1.52458 0.07368  -0.09802 -0.12544 100 GLU B CD    
120  O  OE1   . GLU A 21  ? 1.53044 1.42443 1.62490 0.06783  -0.09000 -0.12083 100 GLU B OE1   
121  O  OE2   . GLU A 21  ? 1.33364 1.19114 1.43909 0.07095  -0.10276 -0.12441 100 GLU B OE2   
122  N  N     . ASN A 22  ? 1.37993 1.28986 1.51827 0.09443  -0.10583 -0.11472 101 ASN B N     
123  C  CA    . ASN A 22  ? 1.26824 1.19453 1.40838 0.09283  -0.10408 -0.10891 101 ASN B CA    
124  C  C     . ASN A 22  ? 1.28829 1.22927 1.41528 0.08264  -0.09467 -0.10372 101 ASN B C     
125  O  O     . ASN A 22  ? 1.15116 1.11467 1.28413 0.08104  -0.08950 -0.10435 101 ASN B O     
126  C  CB    . ASN A 22  ? 1.23891 1.18558 1.40032 0.10151  -0.10375 -0.11980 101 ASN B CB    
127  C  CG    . ASN A 22  ? 1.22354 1.17658 1.39242 0.10261  -0.10852 -0.11260 101 ASN B CG    
128  O  OD1   . ASN A 22  ? 1.25717 1.19353 1.42881 0.10744  -0.11877 -0.10778 101 ASN B OD1   
129  N  ND2   . ASN A 22  ? 1.09375 1.07101 1.26652 0.09810  -0.10172 -0.11148 101 ASN B ND2   
130  N  N     . SER A 23  ? 1.32147 1.24973 1.43190 0.07557  -0.09269 -0.09782 102 SER B N     
131  C  CA    . SER A 23  ? 1.24284 1.18275 1.34031 0.06612  -0.08452 -0.09249 102 SER B CA    
132  C  C     . SER A 23  ? 1.23458 1.17350 1.32536 0.06178  -0.08660 -0.07998 102 SER B C     
133  O  O     . SER A 23  ? 1.21183 1.13308 1.29864 0.06388  -0.09436 -0.07245 102 SER B O     
134  C  CB    . SER A 23  ? 1.29415 1.22051 1.37762 0.06043  -0.08272 -0.09013 102 SER B CB    
135  O  OG    . SER A 23  ? 1.37613 1.31265 1.44695 0.05162  -0.07561 -0.08413 102 SER B OG    
136  N  N     . MET A 24  ? 1.19948 1.15754 1.28890 0.05601  -0.08000 -0.07776 103 MET B N     
137  C  CA    . MET A 24  ? 1.16306 1.12103 1.24698 0.05140  -0.08220 -0.06725 103 MET B CA    
138  C  C     . MET A 24  ? 1.09081 1.03707 1.15477 0.04398  -0.08032 -0.05791 103 MET B C     
139  O  O     . MET A 24  ? 1.08766 1.03926 1.14620 0.03855  -0.07901 -0.05111 103 MET B O     
140  C  CB    . MET A 24  ? 1.11077 1.09473 1.20643 0.04864  -0.07690 -0.06849 103 MET B CB    
141  C  CG    . MET A 24  ? 1.05572 1.05246 1.17313 0.05604  -0.07977 -0.07541 103 MET B CG    
142  S  SD    . MET A 24  ? 1.38306 1.41520 1.51717 0.05268  -0.07040 -0.07739 103 MET B SD    
143  C  CE    . MET A 24  ? 1.16504 1.19607 1.28886 0.04170  -0.07039 -0.06397 103 MET B CE    
144  N  N     . ARG A 25  ? 1.03330 0.96372 1.08783 0.04373  -0.08057 -0.05735 104 ARG B N     
145  C  CA    . ARG A 25  ? 1.02589 0.94701 1.06321 0.03697  -0.07802 -0.04879 104 ARG B CA    
146  C  C     . ARG A 25  ? 1.13203 1.03265 1.16414 0.03864  -0.08129 -0.04684 104 ARG B C     
147  O  O     . ARG A 25  ? 1.16269 1.06190 1.20228 0.04100  -0.08101 -0.05515 104 ARG B O     
148  C  CB    . ARG A 25  ? 1.07398 1.01119 1.10777 0.03031  -0.06912 -0.05126 104 ARG B CB    
149  C  CG    . ARG A 25  ? 1.14760 1.07621 1.16570 0.02373  -0.06631 -0.04395 104 ARG B CG    
150  C  CD    . ARG A 25  ? 1.09923 1.04541 1.11349 0.01716  -0.05855 -0.04434 104 ARG B CD    
151  N  NE    . ARG A 25  ? 1.11873 1.08186 1.14189 0.01897  -0.05397 -0.05523 104 ARG B NE    
152  C  CZ    . ARG A 25  ? 1.19665 1.18020 1.22912 0.01964  -0.05025 -0.05827 104 ARG B CZ    
153  N  NH1   . ARG A 25  ? 1.16114 1.14996 1.19735 0.01779  -0.05142 -0.05142 104 ARG B NH1   
154  N  NH2   . ARG A 25  ? 1.05533 1.05497 1.09417 0.02244  -0.04543 -0.06850 104 ARG B NH2   
155  N  N     . LEU A 26  ? 1.09696 0.98219 1.11696 0.03767  -0.08456 -0.03584 105 LEU B N     
156  C  CA    . LEU A 26  ? 0.99582 0.86203 1.01096 0.03821  -0.08717 -0.03044 105 LEU B CA    
157  C  C     . LEU A 26  ? 1.10982 0.97255 1.10991 0.03129  -0.08258 -0.02115 105 LEU B C     
158  O  O     . LEU A 26  ? 1.12679 0.99222 1.11649 0.02960  -0.08170 -0.01456 105 LEU B O     
159  C  CB    . LEU A 26  ? 1.00739 0.85878 1.02222 0.04502  -0.09538 -0.02415 105 LEU B CB    
160  C  CG    . LEU A 26  ? 1.08956 0.92121 1.10078 0.04572  -0.09826 -0.01600 105 LEU B CG    
161  C  CD1   . LEU A 26  ? 1.23248 1.05914 1.25902 0.04770  -0.10018 -0.02494 105 LEU B CD1   
162  C  CD2   . LEU A 26  ? 1.08489 0.90407 1.09004 0.05191  -0.10538 -0.00637 105 LEU B CD2   
163  N  N     . ASP A 27  ? 1.12634 0.98312 1.12648 0.02760  -0.08028 -0.02114 106 ASP B N     
164  C  CA    . ASP A 27  ? 1.00607 0.86112 0.99472 0.02087  -0.07562 -0.01298 106 ASP B CA    
165  C  C     . ASP A 27  ? 1.05793 0.89506 1.04575 0.02097  -0.07833 -0.00412 106 ASP B C     
166  O  O     . ASP A 27  ? 1.16815 0.99935 1.16542 0.01956  -0.07953 -0.00822 106 ASP B O     
167  C  CB    . ASP A 27  ? 0.99619 0.86384 0.98697 0.01516  -0.07011 -0.02072 106 ASP B CB    
168  C  CG    . ASP A 27  ? 1.15468 1.02222 1.13496 0.00826  -0.06562 -0.01259 106 ASP B CG    
169  O  OD1   . ASP A 27  ? 1.14601 1.00648 1.11652 0.00807  -0.06558 -0.00130 106 ASP B OD1   
170  O  OD2   . ASP A 27  ? 1.11071 0.98603 1.09233 0.00360  -0.06228 -0.01787 106 ASP B OD2   
171  N  N     . LEU A 28  ? 0.99975 0.82864 0.97667 0.02283  -0.07954 0.00814  107 LEU B N     
172  C  CA    . LEU A 28  ? 1.03115 0.84502 1.00594 0.02274  -0.08089 0.01991  107 LEU B CA    
173  C  C     . LEU A 28  ? 1.05143 0.86722 1.01344 0.01774  -0.07497 0.03065  107 LEU B C     
174  O  O     . LEU A 28  ? 1.10391 0.91196 1.05675 0.01979  -0.07489 0.04338  107 LEU B O     
175  C  CB    . LEU A 28  ? 1.10650 0.90954 1.07842 0.03048  -0.08708 0.02671  107 LEU B CB    
176  C  CG    . LEU A 28  ? 1.11290 0.91038 1.09937 0.03642  -0.09413 0.01868  107 LEU B CG    
177  C  CD1   . LEU A 28  ? 1.11014 0.89807 1.09088 0.04419  -0.10051 0.02701  107 LEU B CD1   
178  C  CD2   . LEU A 28  ? 1.18269 0.97033 1.18378 0.03413  -0.09585 0.01631  107 LEU B CD2   
179  N  N     . SER A 29  ? 1.02743 0.85453 0.98861 0.01167  -0.06982 0.02587  108 SER B N     
180  C  CA    . SER A 29  ? 1.10505 0.93593 1.05537 0.00731  -0.06421 0.03474  108 SER B CA    
181  C  C     . SER A 29  ? 1.10788 0.93263 1.06456 0.00201  -0.06233 0.04130  108 SER B C     
182  O  O     . SER A 29  ? 1.15785 0.97876 1.12823 -0.00040 -0.06493 0.03491  108 SER B O     
183  C  CB    . SER A 29  ? 1.01355 0.85942 0.96071 0.00326  -0.06019 0.02768  108 SER B CB    
184  O  OG    . SER A 29  ? 1.04877 0.90065 1.00678 -0.00074 -0.05967 0.01728  108 SER B OG    
185  N  N     . LYS A 30  ? 1.12560 0.94980 1.07306 0.00058  -0.05812 0.05397  109 LYS B N     
186  C  CA    . LYS A 30  ? 1.13626 0.95763 1.09027 -0.00539 -0.05525 0.06233  109 LYS B CA    
187  C  C     . LYS A 30  ? 1.01508 0.82235 0.98247 -0.00529 -0.05979 0.06704  109 LYS B C     
188  O  O     . LYS A 30  ? 1.06993 0.87400 1.05016 -0.01140 -0.05996 0.06900  109 LYS B O     
189  C  CB    . LYS A 30  ? 1.16782 0.99873 1.12865 -0.01262 -0.05315 0.05375  109 LYS B CB    
190  C  CG    . LYS A 30  ? 1.06542 0.90996 1.01498 -0.01328 -0.04917 0.04964  109 LYS B CG    
191  C  CD    . LYS A 30  ? 1.01800 0.87158 0.97243 -0.02060 -0.04650 0.04608  109 LYS B CD    
192  C  CE    . LYS A 30  ? 1.18181 1.04847 1.12980 -0.02128 -0.04477 0.03742  109 LYS B CE    
193  N  NZ    . LYS A 30  ? 1.13844 1.00721 1.09112 -0.01866 -0.04818 0.02487  109 LYS B NZ    
194  N  N     . ARG A 31  ? 1.04599 0.84425 1.01167 0.00153  -0.06430 0.06927  110 ARG B N     
195  C  CA    . ARG A 31  ? 0.92461 0.70812 0.90319 0.00238  -0.06940 0.07499  110 ARG B CA    
196  C  C     . ARG A 31  ? 1.09522 0.87204 1.06601 0.00494  -0.06741 0.09460  110 ARG B C     
197  O  O     . ARG A 31  ? 1.08222 0.84615 1.06118 0.00722  -0.07212 0.10186  110 ARG B O     
198  C  CB    . ARG A 31  ? 0.85915 0.63678 0.84372 0.00870  -0.07667 0.06410  110 ARG B CB    
199  C  CG    . ARG A 31  ? 1.00090 0.78569 0.99492 0.00702  -0.07835 0.04511  110 ARG B CG    
200  C  CD    . ARG A 31  ? 1.20732 0.98834 1.20752 0.01436  -0.08476 0.03511  110 ARG B CD    
201  N  NE    . ARG A 31  ? 1.28408 1.07504 1.29184 0.01392  -0.08511 0.01707  110 ARG B NE    
202  C  CZ    . ARG A 31  ? 1.39274 1.17905 1.41608 0.01330  -0.08913 0.00643  110 ARG B CZ    
203  N  NH1   . ARG A 31  ? 1.45125 1.22151 1.48677 0.01224  -0.09406 0.01185  110 ARG B NH1   
204  N  NH2   . ARG A 31  ? 1.35899 1.15724 1.38611 0.01408  -0.08841 -0.00995 110 ARG B NH2   
205  N  N     . SER A 32  ? 1.02590 0.81163 0.98095 0.00520  -0.06054 0.10349  111 SER B N     
206  C  CA    . SER A 32  ? 1.05679 0.83964 1.00210 0.00823  -0.05692 0.12266  111 SER B CA    
207  C  C     . SER A 32  ? 1.03149 0.80490 0.96903 0.01729  -0.06244 0.12744  111 SER B C     
208  O  O     . SER A 32  ? 1.15394 0.92020 1.09044 0.01939  -0.06209 0.14366  111 SER B O     
209  C  CB    . SER A 32  ? 1.10285 0.88086 1.06426 0.00091  -0.05467 0.13545  111 SER B CB    
210  O  OG    . SER A 32  ? 1.17586 0.96211 1.14670 -0.00753 -0.05134 0.12947  111 SER B OG    
211  N  N     . ILE A 33  ? 1.06057 0.83472 0.99325 0.02270  -0.06769 0.11410  112 ILE B N     
212  C  CA    . ILE A 33  ? 1.04520 0.81076 0.97230 0.03152  -0.07448 0.11662  112 ILE B CA    
213  C  C     . ILE A 33  ? 1.08920 0.85796 0.99271 0.03870  -0.07168 0.12869  112 ILE B C     
214  O  O     . ILE A 33  ? 1.08729 0.86660 0.97653 0.03967  -0.06723 0.12572  112 ILE B O     
215  C  CB    . ILE A 33  ? 1.01768 0.78550 0.94836 0.03494  -0.08071 0.09860  112 ILE B CB    
216  C  CG1   . ILE A 33  ? 1.11880 0.88578 1.07087 0.02888  -0.08253 0.08560  112 ILE B CG1   
217  C  CG2   . ILE A 33  ? 1.14149 0.90054 1.06864 0.04416  -0.08881 0.10090  112 ILE B CG2   
218  C  CD1   . ILE A 33  ? 1.04894 0.82113 1.00613 0.03212  -0.08713 0.06831  112 ILE B CD1   
219  N  N     . HIS A 34  ? 1.18891 0.94846 1.08788 0.04435  -0.07464 0.14234  113 HIS B N     
220  C  CA    . HIS A 34  ? 1.16055 0.92291 1.03525 0.05293  -0.07280 0.15406  113 HIS B CA    
221  C  C     . HIS A 34  ? 1.26132 1.02001 1.12489 0.06309  -0.08197 0.14772  113 HIS B C     
222  O  O     . HIS A 34  ? 1.18991 0.95511 1.03286 0.06987  -0.08208 0.14566  113 HIS B O     
223  C  CB    . HIS A 34  ? 1.03342 0.79018 0.90770 0.05307  -0.06918 0.17639  113 HIS B CB    
224  C  CG    . HIS A 34  ? 1.16835 0.93238 1.04814 0.04489  -0.05890 0.18621  113 HIS B CG    
225  N  ND1   . HIS A 34  ? 1.11888 0.88076 1.02287 0.03402  -0.05778 0.18258  113 HIS B ND1   
226  C  CD2   . HIS A 34  ? 1.12804 0.90230 0.99293 0.04646  -0.04960 0.19925  113 HIS B CD2   
227  C  CE1   . HIS A 34  ? 1.23318 1.00353 1.13813 0.02862  -0.04862 0.19340  113 HIS B CE1   
228  N  NE2   . HIS A 34  ? 1.19198 0.97047 1.07375 0.03607  -0.04297 0.20390  113 HIS B NE2   
229  N  N     . ILE A 35  ? 1.17391 0.92222 1.05154 0.06469  -0.09040 0.14406  114 ILE B N     
230  C  CA    . ILE A 35  ? 1.11811 0.86283 0.98858 0.07424  -0.10020 0.13831  114 ILE B CA    
231  C  C     . ILE A 35  ? 1.11845 0.86085 1.01058 0.07188  -0.10663 0.12133  114 ILE B C     
232  O  O     . ILE A 35  ? 1.08386 0.81738 0.99559 0.06841  -0.10885 0.12193  114 ILE B O     
233  C  CB    . ILE A 35  ? 1.20936 0.94357 1.07255 0.08168  -0.10483 0.15517  114 ILE B CB    
234  C  CG1   . ILE A 35  ? 1.13571 0.87547 0.97322 0.08638  -0.09824 0.17114  114 ILE B CG1   
235  C  CG2   . ILE A 35  ? 1.13969 0.86914 1.00113 0.09084  -0.11677 0.14745  114 ILE B CG2   
236  C  CD1   . ILE A 35  ? 1.15455 0.88596 0.98179 0.09423  -0.10188 0.18980  114 ILE B CD1   
237  N  N     . LEU A 36  ? 1.22763 0.97836 1.11716 0.07395  -0.10963 0.10635  115 LEU B N     
238  C  CA    . LEU A 36  ? 1.12186 0.87365 1.03097 0.07287  -0.11498 0.09034  115 LEU B CA    
239  C  C     . LEU A 36  ? 1.11532 0.85712 1.03011 0.08110  -0.12543 0.09187  115 LEU B C     
240  O  O     . LEU A 36  ? 1.21671 0.95795 1.11665 0.08939  -0.13129 0.09526  115 LEU B O     
241  C  CB    . LEU A 36  ? 1.02925 0.79395 0.93462 0.07262  -0.11504 0.07645  115 LEU B CB    
242  C  CG    . LEU A 36  ? 1.12823 0.89894 1.05387 0.07057  -0.11804 0.05995  115 LEU B CG    
243  C  CD1   . LEU A 36  ? 1.06732 0.84042 1.00784 0.06173  -0.11135 0.05496  115 LEU B CD1   
244  C  CD2   . LEU A 36  ? 0.98078 0.76377 0.90191 0.07121  -0.11926 0.04989  115 LEU B CD2   
245  N  N     . PRO A 37  ? 1.07227 0.80585 1.00803 0.07981  -0.12886 0.08903  116 PRO B N     
246  C  CA    . PRO A 37  ? 1.11532 0.83859 1.05766 0.08819  -0.13935 0.09121  116 PRO B CA    
247  C  C     . PRO A 37  ? 1.19761 0.92863 1.14090 0.09465  -0.14673 0.07815  116 PRO B C     
248  O  O     . PRO A 37  ? 1.27980 1.02339 1.22835 0.09121  -0.14403 0.06423  116 PRO B O     
249  C  CB    . PRO A 37  ? 1.10924 0.82373 1.07694 0.08447  -0.14080 0.08676  116 PRO B CB    
250  C  CG    . PRO A 37  ? 1.19114 0.91562 1.16617 0.07524  -0.13250 0.07564  116 PRO B CG    
251  C  CD    . PRO A 37  ? 1.13928 0.87218 1.09376 0.07123  -0.12412 0.08309  116 PRO B CD    
252  N  N     . SER A 38  ? 1.25826 0.98201 1.19719 0.10405  -0.15647 0.08373  117 SER B N     
253  C  CA    . SER A 38  ? 1.19315 0.92338 1.13422 0.11103  -0.16538 0.07298  117 SER B CA    
254  C  C     . SER A 38  ? 1.16547 0.90035 1.13359 0.11046  -0.16835 0.05688  117 SER B C     
255  O  O     . SER A 38  ? 1.20493 0.94982 1.17857 0.11388  -0.17340 0.04593  117 SER B O     
256  C  CB    . SER A 38  ? 1.18460 0.90511 1.11456 0.12170  -0.17591 0.08395  117 SER B CB    
257  O  OG    . SER A 38  ? 1.32267 1.04161 1.22503 0.12394  -0.17312 0.09798  117 SER B OG    
258  N  N     . SER A 39  ? 1.23051 0.95916 1.21627 0.10656  -0.16557 0.05480  118 SER B N     
259  C  CA    . SER A 39  ? 1.17427 0.90837 1.18495 0.10717  -0.16767 0.03854  118 SER B CA    
260  C  C     . SER A 39  ? 1.08925 0.84251 1.10407 0.10154  -0.16073 0.02406  118 SER B C     
261  O  O     . SER A 39  ? 1.08032 0.84172 1.11462 0.10249  -0.16127 0.01028  118 SER B O     
262  C  CB    . SER A 39  ? 1.19178 0.91403 1.21858 0.10431  -0.16639 0.03889  118 SER B CB    
263  O  OG    . SER A 39  ? 1.15555 0.87594 1.17403 0.09527  -0.15722 0.04575  118 SER B OG    
264  N  N     . ILE A 40  ? 1.12017 0.88136 1.11775 0.09628  -0.15432 0.02705  119 ILE B N     
265  C  CA    . ILE A 40  ? 1.14778 0.92683 1.14958 0.09091  -0.14838 0.01509  119 ILE B CA    
266  C  C     . ILE A 40  ? 1.10174 0.89167 1.10993 0.09608  -0.15518 0.00713  119 ILE B C     
267  O  O     . ILE A 40  ? 1.04284 0.84877 1.05992 0.09222  -0.15122 -0.00301 119 ILE B O     
268  C  CB    . ILE A 40  ? 1.08106 0.86413 1.06367 0.08395  -0.14023 0.02115  119 ILE B CB    
269  C  CG1   . ILE A 40  ? 1.11488 0.91420 1.10420 0.07631  -0.13216 0.01044  119 ILE B CG1   
270  C  CG2   . ILE A 40  ? 0.91730 0.70011 0.88124 0.08857  -0.14516 0.02743  119 ILE B CG2   
271  C  CD1   . ILE A 40  ? 0.98983 0.79181 0.96243 0.06927  -0.12401 0.01655  119 ILE B CD1   
272  N  N     . LYS A 41  ? 1.02308 0.80531 1.02760 0.10463  -0.16562 0.01216  120 LYS B N     
273  C  CA    . LYS A 41  ? 1.03972 0.83189 1.05313 0.10988  -0.17381 0.00452  120 LYS B CA    
274  C  C     . LYS A 41  ? 1.17400 0.97699 1.21497 0.11104  -0.17399 -0.00867 120 LYS B C     
275  O  O     . LYS A 41  ? 0.97301 0.79059 1.02580 0.11215  -0.17694 -0.01691 120 LYS B O     
276  C  CB    . LYS A 41  ? 1.02813 0.80860 1.03228 0.11967  -0.18599 0.01278  120 LYS B CB    
277  C  CG    . LYS A 41  ? 0.99935 0.76708 1.01527 0.12597  -0.19174 0.01593  120 LYS B CG    
278  C  CD    . LYS A 41  ? 0.98585 0.74039 0.98683 0.13495  -0.20249 0.02806  120 LYS B CD    
279  C  CE    . LYS A 41  ? 1.22753 0.99020 1.22930 0.14161  -0.21355 0.02256  120 LYS B CE    
280  N  NZ    . LYS A 41  ? 1.21237 0.96248 1.19925 0.15159  -0.22521 0.03379  120 LYS B NZ    
281  N  N     . GLU A 42  ? 1.13883 0.93554 1.19113 0.11100  -0.17098 -0.01103 121 GLU B N     
282  C  CA    . GLU A 42  ? 1.07120 0.87828 1.14886 0.11364  -0.17080 -0.02452 121 GLU B CA    
283  C  C     . GLU A 42  ? 1.08205 0.90932 1.16661 0.10630  -0.16029 -0.03474 121 GLU B C     
284  O  O     . GLU A 42  ? 1.19359 1.03607 1.29808 0.10887  -0.15965 -0.04614 121 GLU B O     
285  C  CB    . GLU A 42  ? 1.13952 0.93198 1.22643 0.11639  -0.17172 -0.02473 121 GLU B CB    
286  C  CG    . GLU A 42  ? 1.30724 1.08148 1.39404 0.12508  -0.18327 -0.01568 121 GLU B CG    
287  C  CD    . GLU A 42  ? 1.45087 1.23232 1.55566 0.13445  -0.19276 -0.02338 121 GLU B CD    
288  O  OE1   . GLU A 42  ? 1.45062 1.24390 1.57697 0.13651  -0.19074 -0.03716 121 GLU B OE1   
289  O  OE2   . GLU A 42  ? 1.40716 1.18354 1.50447 0.14022  -0.20230 -0.01590 121 GLU B OE2   
290  N  N     . LEU A 43  ? 1.11137 0.94014 1.18019 0.09768  -0.15195 -0.03038 122 LEU B N     
291  C  CA    . LEU A 43  ? 1.06747 0.91396 1.14089 0.09030  -0.14151 -0.03835 122 LEU B CA    
292  C  C     . LEU A 43  ? 1.00549 0.86913 1.08037 0.08767  -0.14112 -0.04015 122 LEU B C     
293  O  O     . LEU A 43  ? 1.09238 0.96243 1.15683 0.08016  -0.13471 -0.03758 122 LEU B O     
294  C  CB    . LEU A 43  ? 1.10659 0.94622 1.16410 0.08238  -0.13348 -0.03254 122 LEU B CB    
295  C  CG    . LEU A 43  ? 1.13741 0.96639 1.19884 0.08146  -0.13074 -0.03436 122 LEU B CG    
296  C  CD1   . LEU A 43  ? 1.09394 0.90417 1.16111 0.08902  -0.13979 -0.03032 122 LEU B CD1   
297  C  CD2   . LEU A 43  ? 1.12738 0.95034 1.17218 0.07319  -0.12399 -0.02623 122 LEU B CD2   
298  N  N     . THR A 44  ? 0.91532 0.78652 1.00516 0.09379  -0.14863 -0.04450 123 THR B N     
299  C  CA    . THR A 44  ? 1.00673 0.89258 1.10086 0.09143  -0.15059 -0.04536 123 THR B CA    
300  C  C     . THR A 44  ? 1.00112 0.90987 1.10755 0.08469  -0.14042 -0.05213 123 THR B C     
301  O  O     . THR A 44  ? 1.01970 0.94081 1.13041 0.08077  -0.14094 -0.05147 123 THR B O     
302  C  CB    . THR A 44  ? 0.99752 0.88595 1.10705 0.09985  -0.16227 -0.04814 123 THR B CB    
303  O  OG1   . THR A 44  ? 1.15634 1.05291 1.28790 0.10516  -0.16131 -0.05718 123 THR B OG1   
304  C  CG2   . THR A 44  ? 0.92209 0.78906 1.01616 0.10648  -0.17318 -0.03970 123 THR B CG2   
305  N  N     . GLN A 45  ? 0.93641 0.85117 1.04871 0.08345  -0.13173 -0.05838 124 GLN B N     
306  C  CA    . GLN A 45  ? 1.00635 0.94398 1.12782 0.07761  -0.12126 -0.06399 124 GLN B CA    
307  C  C     . GLN A 45  ? 1.13374 1.07084 1.23731 0.06804  -0.11324 -0.05843 124 GLN B C     
308  O  O     . GLN A 45  ? 1.14641 1.10200 1.25493 0.06260  -0.10434 -0.06136 124 GLN B O     
309  C  CB    . GLN A 45  ? 1.04810 0.99420 1.18297 0.08195  -0.11588 -0.07481 124 GLN B CB    
310  C  CG    . GLN A 45  ? 1.08715 1.02116 1.20888 0.07958  -0.11059 -0.07584 124 GLN B CG    
311  C  CD    . GLN A 45  ? 1.11883 1.02556 1.23088 0.08341  -0.11853 -0.07024 124 GLN B CD    
312  O  OE1   . GLN A 45  ? 1.20864 1.10590 1.32482 0.08977  -0.12810 -0.06723 124 GLN B OE1   
313  N  NE2   . GLN A 45  ? 1.12079 1.01536 1.22060 0.07945  -0.11481 -0.06807 124 GLN B NE2   
314  N  N     . LEU A 46  ? 1.13515 1.05277 1.21842 0.06624  -0.11598 -0.04999 125 LEU B N     
315  C  CA    . LEU A 46  ? 1.06256 0.97879 1.12940 0.05797  -0.10854 -0.04490 125 LEU B CA    
316  C  C     . LEU A 46  ? 1.01754 0.94504 1.08323 0.05209  -0.10751 -0.04125 125 LEU B C     
317  O  O     . LEU A 46  ? 1.05554 0.98106 1.12329 0.05440  -0.11566 -0.03875 125 LEU B O     
318  C  CB    . LEU A 46  ? 0.94124 0.83485 0.98834 0.05851  -0.11151 -0.03635 125 LEU B CB    
319  C  CG    . LEU A 46  ? 1.03600 0.91665 1.08250 0.06115  -0.11084 -0.03752 125 LEU B CG    
320  C  CD1   . LEU A 46  ? 1.02217 0.88303 1.05004 0.06064  -0.11294 -0.02636 125 LEU B CD1   
321  C  CD2   . LEU A 46  ? 1.03597 0.92690 1.08655 0.05627  -0.10162 -0.04444 125 LEU B CD2   
322  N  N     . THR A 47  ? 1.05512 0.99405 1.11797 0.04457  -0.09823 -0.04103 126 THR B N     
323  C  CA    . THR A 47  ? 1.08676 1.03319 1.14653 0.03795  -0.09691 -0.03592 126 THR B CA    
324  C  C     . THR A 47  ? 1.02194 0.95832 1.06119 0.03260  -0.09298 -0.02934 126 THR B C     
325  O  O     . THR A 47  ? 0.98437 0.92161 1.01831 0.02835  -0.09396 -0.02439 126 THR B O     
326  C  CB    . THR A 47  ? 1.03574 1.00717 1.11171 0.03326  -0.08944 -0.03937 126 THR B CB    
327  O  OG1   . THR A 47  ? 1.10958 1.08791 1.18281 0.03157  -0.07999 -0.04354 126 THR B OG1   
328  C  CG2   . THR A 47  ? 0.94395 0.92821 1.04266 0.03829  -0.09343 -0.04478 126 THR B CG2   
329  N  N     . GLU A 48  ? 0.99757 0.92458 1.02687 0.03279  -0.08909 -0.02931 127 GLU B N     
330  C  CA    . GLU A 48  ? 0.99990 0.91784 1.01132 0.02816  -0.08534 -0.02284 127 GLU B CA    
331  C  C     . GLU A 48  ? 0.96470 0.86417 0.96668 0.03217  -0.08778 -0.02006 127 GLU B C     
332  O  O     . GLU A 48  ? 0.96830 0.86556 0.97807 0.03523  -0.08770 -0.02518 127 GLU B O     
333  C  CB    . GLU A 48  ? 1.01900 0.94994 1.03065 0.02140  -0.07577 -0.02487 127 GLU B CB    
334  C  CG    . GLU A 48  ? 1.05801 1.00866 1.07942 0.01676  -0.07224 -0.02556 127 GLU B CG    
335  C  CD    . GLU A 48  ? 1.17187 1.13833 1.19569 0.01234  -0.06297 -0.02928 127 GLU B CD    
336  O  OE1   . GLU A 48  ? 1.09869 1.05911 1.11179 0.01030  -0.05944 -0.02907 127 GLU B OE1   
337  O  OE2   . GLU A 48  ? 1.21132 1.19713 1.24805 0.01113  -0.05933 -0.03221 127 GLU B OE2   
338  N  N     . LEU A 49  ? 1.00852 0.89512 0.99452 0.03247  -0.09002 -0.01175 128 LEU B N     
339  C  CA    . LEU A 49  ? 0.88664 0.75650 0.86293 0.03562  -0.09164 -0.00603 128 LEU B CA    
340  C  C     . LEU A 49  ? 0.93639 0.80227 0.89732 0.03077  -0.08637 0.00155  128 LEU B C     
341  O  O     . LEU A 49  ? 0.99636 0.86110 0.94627 0.03094  -0.08766 0.00623  128 LEU B O     
342  C  CB    . LEU A 49  ? 0.87545 0.73408 0.84728 0.04350  -0.10072 -0.00224 128 LEU B CB    
343  C  CG    . LEU A 49  ? 0.96835 0.81014 0.92920 0.04717  -0.10247 0.00641  128 LEU B CG    
344  C  CD1   . LEU A 49  ? 0.85271 0.69000 0.82508 0.04696  -0.10098 0.00353  128 LEU B CD1   
345  C  CD2   . LEU A 49  ? 0.93963 0.77249 0.89408 0.05560  -0.11183 0.01034  128 LEU B CD2   
346  N  N     . TYR A 50  ? 1.02660 0.89057 0.98779 0.02684  -0.08104 0.00214  129 TYR B N     
347  C  CA    . TYR A 50  ? 0.88051 0.74273 0.83019 0.02176  -0.07555 0.00897  129 TYR B CA    
348  C  C     . TYR A 50  ? 0.93500 0.78235 0.87795 0.02412  -0.07651 0.01776  129 TYR B C     
349  O  O     . TYR A 50  ? 1.10216 0.94344 1.05373 0.02416  -0.07715 0.01641  129 TYR B O     
350  C  CB    . TYR A 50  ? 0.83369 0.70639 0.78947 0.01494  -0.06921 0.00366  129 TYR B CB    
351  C  CG    . TYR A 50  ? 0.88975 0.77887 0.85264 0.01258  -0.06735 -0.00339 129 TYR B CG    
352  C  CD1   . TYR A 50  ? 0.96777 0.86399 0.92463 0.00923  -0.06552 -0.00004 129 TYR B CD1   
353  C  CD2   . TYR A 50  ? 0.90894 0.80695 0.88541 0.01401  -0.06735 -0.01291 129 TYR B CD2   
354  C  CE1   . TYR A 50  ? 1.03569 0.94723 1.00064 0.00642  -0.06372 -0.00445 129 TYR B CE1   
355  C  CE2   . TYR A 50  ? 1.01899 0.93422 1.00263 0.01180  -0.06461 -0.01770 129 TYR B CE2   
356  C  CZ    . TYR A 50  ? 1.06293 0.98476 1.04114 0.00753  -0.06280 -0.01267 129 TYR B CZ    
357  O  OH    . TYR A 50  ? 1.12046 1.05967 1.10732 0.00466  -0.05999 -0.01547 129 TYR B OH    
358  N  N     . LEU A 51  ? 0.81730 0.65911 0.74539 0.02640  -0.07674 0.02691  130 LEU B N     
359  C  CA    . LEU A 51  ? 0.97474 0.80453 0.89499 0.02896  -0.07667 0.03776  130 LEU B CA    
360  C  C     . LEU A 51  ? 1.00545 0.83697 0.91343 0.02578  -0.07045 0.04612  130 LEU B C     
361  O  O     . LEU A 51  ? 0.95586 0.78082 0.85205 0.02968  -0.06998 0.05646  130 LEU B O     
362  C  CB    . LEU A 51  ? 0.82307 0.64443 0.73563 0.03778  -0.08369 0.04194  130 LEU B CB    
363  C  CG    . LEU A 51  ? 1.09420 0.91327 1.01894 0.04245  -0.09101 0.03477  130 LEU B CG    
364  C  CD1   . LEU A 51  ? 0.97430 0.78670 0.88863 0.05135  -0.09869 0.03896  130 LEU B CD1   
365  C  CD2   . LEU A 51  ? 1.10102 0.91258 1.03887 0.04148  -0.09136 0.03479  130 LEU B CD2   
366  N  N     . TYR A 52  ? 0.93799 0.77930 0.84847 0.01924  -0.06549 0.04220  131 TYR B N     
367  C  CA    . TYR A 52  ? 0.98341 0.82765 0.88338 0.01682  -0.06000 0.04931  131 TYR B CA    
368  C  C     . TYR A 52  ? 1.09225 0.93276 0.99581 0.01273  -0.05549 0.05708  131 TYR B C     
369  O  O     . TYR A 52  ? 1.11145 0.94847 1.02775 0.00973  -0.05650 0.05442  131 TYR B O     
370  C  CB    . TYR A 52  ? 0.97223 0.82821 0.87380 0.01160  -0.05715 0.04321  131 TYR B CB    
371  C  CG    . TYR A 52  ? 1.03926 0.90256 0.95447 0.00528  -0.05541 0.03514  131 TYR B CG    
372  C  CD1   . TYR A 52  ? 1.04671 0.91509 0.97113 0.00597  -0.05850 0.02577  131 TYR B CD1   
373  C  CD2   . TYR A 52  ? 1.01867 0.88513 0.93750 -0.00090 -0.05077 0.03661  131 TYR B CD2   
374  C  CE1   . TYR A 52  ? 1.08441 0.96122 1.01943 0.00144  -0.05636 0.01791  131 TYR B CE1   
375  C  CE2   . TYR A 52  ? 1.00945 0.88310 0.93869 -0.00566 -0.04983 0.02818  131 TYR B CE2   
376  C  CZ    . TYR A 52  ? 1.13212 1.01117 1.06845 -0.00409 -0.05229 0.01875  131 TYR B CZ    
377  O  OH    . TYR A 52  ? 1.02527 0.91307 0.97019 -0.00760 -0.05083 0.00992  131 TYR B OH    
378  N  N     . SER A 53  ? 1.05694 0.89844 0.95012 0.01297  -0.05083 0.06662  132 SER B N     
379  C  CA    . SER A 53  ? 1.05019 0.88999 0.94742 0.00880  -0.04597 0.07618  132 SER B CA    
380  C  C     . SER A 53  ? 1.18180 1.01020 1.08450 0.01106  -0.04867 0.08320  132 SER B C     
381  O  O     . SER A 53  ? 1.28204 1.10642 1.19941 0.00594  -0.04921 0.08314  132 SER B O     
382  C  CB    . SER A 53  ? 1.01068 0.85711 0.92063 -0.00005 -0.04349 0.07036  132 SER B CB    
383  O  OG    . SER A 53  ? 1.18441 1.04125 1.08885 -0.00218 -0.04066 0.06664  132 SER B OG    
384  N  N     . ASN A 54  ? 1.03317 0.85594 0.92389 0.01913  -0.05114 0.08930  133 ASN B N     
385  C  CA    . ASN A 54  ? 0.96477 0.77664 0.85823 0.02224  -0.05365 0.09886  133 ASN B CA    
386  C  C     . ASN A 54  ? 1.00982 0.82179 0.88571 0.02837  -0.04983 0.11327  133 ASN B C     
387  O  O     . ASN A 54  ? 1.20002 1.02051 1.06529 0.02876  -0.04415 0.11608  133 ASN B O     
388  C  CB    . ASN A 54  ? 0.90342 0.70822 0.80106 0.02721  -0.06207 0.09091  133 ASN B CB    
389  C  CG    . ASN A 54  ? 1.05064 0.85469 0.96780 0.02184  -0.06492 0.07908  133 ASN B CG    
390  O  OD1   . ASN A 54  ? 1.06964 0.87113 0.99955 0.01565  -0.06312 0.08085  133 ASN B OD1   
391  N  ND2   . ASN A 54  ? 1.14020 0.94724 1.06037 0.02449  -0.06959 0.06662  133 ASN B ND2   
392  N  N     . LYS A 55  ? 1.02083 0.82380 0.89318 0.03391  -0.05289 0.12282  134 LYS B N     
393  C  CA    . LYS A 55  ? 1.19315 0.99684 1.04799 0.04062  -0.04895 0.13802  134 LYS B CA    
394  C  C     . LYS A 55  ? 1.07815 0.87642 0.91719 0.05162  -0.05599 0.13772  134 LYS B C     
395  O  O     . LYS A 55  ? 1.18476 0.98005 1.01170 0.05804  -0.05509 0.15150  134 LYS B O     
396  C  CB    . LYS A 55  ? 1.18731 0.98656 1.05235 0.03650  -0.04476 0.15481  134 LYS B CB    
397  C  CG    . LYS A 55  ? 1.17652 0.97886 1.06204 0.02491  -0.04049 0.15402  134 LYS B CG    
398  C  CD    . LYS A 55  ? 1.10167 0.91767 0.98050 0.02242  -0.03250 0.15373  134 LYS B CD    
399  C  CE    . LYS A 55  ? 1.27478 1.09708 1.14018 0.02706  -0.02450 0.17139  134 LYS B CE    
400  N  NZ    . LYS A 55  ? 1.30063 1.13660 1.16235 0.02477  -0.01664 0.17119  134 LYS B NZ    
401  N  N     . LEU A 56  ? 1.03226 0.83014 0.87163 0.05392  -0.06315 0.12262  135 LEU B N     
402  C  CA    . LEU A 56  ? 1.06885 0.86165 0.89606 0.06396  -0.07159 0.12061  135 LEU B CA    
403  C  C     . LEU A 56  ? 1.17022 0.96793 0.97171 0.07299  -0.07009 0.12493  135 LEU B C     
404  O  O     . LEU A 56  ? 1.16938 0.97539 0.96423 0.07191  -0.06560 0.12050  135 LEU B O     
405  C  CB    . LEU A 56  ? 0.98444 0.77790 0.82120 0.06334  -0.07921 0.10329  135 LEU B CB    
406  C  CG    . LEU A 56  ? 1.05785 0.84887 0.91899 0.05583  -0.08079 0.09550  135 LEU B CG    
407  C  CD1   . LEU A 56  ? 0.95278 0.74952 0.82167 0.05500  -0.08563 0.07914  135 LEU B CD1   
408  C  CD2   . LEU A 56  ? 1.06859 0.84802 0.93794 0.05878  -0.08601 0.10197  135 LEU B CD2   
409  N  N     . GLN A 57  ? 1.14746 0.93994 0.93397 0.08266  -0.07435 0.13339  136 GLN B N     
410  C  CA    . GLN A 57  ? 1.21314 1.00971 0.97301 0.09358  -0.07511 0.13518  136 GLN B CA    
411  C  C     . GLN A 57  ? 1.24040 1.03260 0.99163 0.10233  -0.08770 0.12463  136 GLN B C     
412  O  O     . GLN A 57  ? 1.24339 1.03892 0.97429 0.11106  -0.09062 0.12058  136 GLN B O     
413  C  CB    . GLN A 57  ? 1.17326 0.97015 0.91777 0.09946  -0.06913 0.15492  136 GLN B CB    
414  C  CG    . GLN A 57  ? 1.19910 1.00117 0.95408 0.09076  -0.05684 0.16739  136 GLN B CG    
415  C  CD    . GLN A 57  ? 1.30962 1.11576 1.04804 0.09712  -0.04940 0.18773  136 GLN B CD    
416  O  OE1   . GLN A 57  ? 1.28215 1.09227 0.99472 0.10905  -0.05029 0.18982  136 GLN B OE1   
417  N  NE2   . GLN A 57  ? 1.33594 1.14166 1.08956 0.08936  -0.04220 0.20294  136 GLN B NE2   
418  N  N     . SER A 58  ? 1.13414 0.91927 0.90117 0.10056  -0.09569 0.11948  137 SER B N     
419  C  CA    . SER A 58  ? 1.23720 1.01939 1.00138 0.10745  -0.10826 0.10827  137 SER B CA    
420  C  C     . SER A 58  ? 1.12377 0.90326 0.91473 0.10054  -0.11298 0.09849  137 SER B C     
421  O  O     . SER A 58  ? 1.13502 0.91196 0.94310 0.09305  -0.10817 0.10236  137 SER B O     
422  C  CB    . SER A 58  ? 1.26919 1.04530 1.01486 0.11942  -0.11515 0.11764  137 SER B CB    
423  O  OG    . SER A 58  ? 1.13700 0.90496 0.89531 0.11773  -0.11644 0.12714  137 SER B OG    
424  N  N     . LEU A 59  ? 1.10275 0.88345 0.89797 0.10338  -0.12266 0.08535  138 LEU B N     
425  C  CA    . LEU A 59  ? 1.16343 0.94356 0.98361 0.09854  -0.12718 0.07614  138 LEU B CA    
426  C  C     . LEU A 59  ? 1.05013 0.82319 0.87093 0.10712  -0.13878 0.07673  138 LEU B C     
427  O  O     . LEU A 59  ? 1.13236 0.90389 0.93547 0.11654  -0.14658 0.07712  138 LEU B O     
428  C  CB    . LEU A 59  ? 1.13679 0.92576 0.96791 0.09377  -0.12900 0.06120  138 LEU B CB    
429  C  CG    . LEU A 59  ? 1.03935 0.83402 0.89403 0.08307  -0.12296 0.05461  138 LEU B CG    
430  C  CD1   . LEU A 59  ? 1.02446 0.81887 0.87833 0.07637  -0.11154 0.06298  138 LEU B CD1   
431  C  CD2   . LEU A 59  ? 0.97504 0.77968 0.83696 0.07869  -0.12371 0.04299  138 LEU B CD2   
432  N  N     . PRO A 60  ? 1.03017 0.79866 0.87062 0.10487  -0.14084 0.07641  139 PRO B N     
433  C  CA    . PRO A 60  ? 1.05396 0.81570 0.89673 0.11341  -0.15247 0.07706  139 PRO B CA    
434  C  C     . PRO A 60  ? 1.05534 0.82314 0.90447 0.11672  -0.16264 0.06291  139 PRO B C     
435  O  O     . PRO A 60  ? 1.06309 0.84006 0.92486 0.11023  -0.16027 0.05165  139 PRO B O     
436  C  CB    . PRO A 60  ? 1.04740 0.80366 0.91352 0.10895  -0.15109 0.07796  139 PRO B CB    
437  C  CG    . PRO A 60  ? 1.05551 0.81942 0.93562 0.09800  -0.14144 0.07035  139 PRO B CG    
438  C  CD    . PRO A 60  ? 1.07375 0.84281 0.93520 0.09518  -0.13338 0.07475  139 PRO B CD    
439  N  N     . ALA A 61  ? 1.00261 0.76564 0.84338 0.12693  -0.17448 0.06434  140 ALA B N     
440  C  CA    . ALA A 61  ? 1.09238 0.86089 0.94118 0.13047  -0.18591 0.05148  140 ALA B CA    
441  C  C     . ALA A 61  ? 1.16405 0.93833 1.04444 0.12505  -0.18691 0.04111  140 ALA B C     
442  O  O     . ALA A 61  ? 1.01740 0.80086 0.91027 0.12338  -0.19169 0.02951  140 ALA B O     
443  C  CB    . ALA A 61  ? 1.01523 0.77710 0.84969 0.14298  -0.19937 0.05550  140 ALA B CB    
444  N  N     . GLU A 62  ? 1.15009 0.91974 1.04441 0.12236  -0.18238 0.04501  141 GLU B N     
445  C  CA    . GLU A 62  ? 1.05596 0.83151 0.97939 0.11904  -0.18318 0.03469  141 GLU B CA    
446  C  C     . GLU A 62  ? 1.07572 0.86477 1.01183 0.10927  -0.17476 0.02442  141 GLU B C     
447  O  O     . GLU A 62  ? 1.06463 0.86301 1.02367 0.10737  -0.17595 0.01423  141 GLU B O     
448  C  CB    . GLU A 62  ? 1.11558 0.88171 1.04961 0.11850  -0.17999 0.04063  141 GLU B CB    
449  C  CG    . GLU A 62  ? 1.16444 0.91896 1.09764 0.12848  -0.19087 0.04789  141 GLU B CG    
450  C  CD    . GLU A 62  ? 1.21494 0.95941 1.11990 0.13410  -0.19249 0.06361  141 GLU B CD    
451  O  OE1   . GLU A 62  ? 1.20943 0.95621 1.09585 0.13052  -0.18463 0.06843  141 GLU B OE1   
452  O  OE2   . GLU A 62  ? 1.21168 0.94669 1.11290 0.14263  -0.20149 0.07154  141 GLU B OE2   
453  N  N     . VAL A 63  ? 1.13436 0.92565 1.05643 0.10346  -0.16611 0.02734  142 VAL B N     
454  C  CA    . VAL A 63  ? 1.01866 0.82275 0.95118 0.09446  -0.15874 0.01888  142 VAL B CA    
455  C  C     . VAL A 63  ? 1.04049 0.85466 0.98215 0.09543  -0.16647 0.00942  142 VAL B C     
456  O  O     . VAL A 63  ? 1.00080 0.82761 0.95925 0.08877  -0.16229 0.00167  142 VAL B O     
457  C  CB    . VAL A 63  ? 0.98321 0.78667 0.89774 0.08922  -0.14930 0.02489  142 VAL B CB    
458  C  CG1   . VAL A 63  ? 0.98226 0.79840 0.90757 0.07975  -0.14159 0.01746  142 VAL B CG1   
459  C  CG2   . VAL A 63  ? 1.07671 0.87074 0.98477 0.08800  -0.14243 0.03536  142 VAL B CG2   
460  N  N     . GLY A 64  ? 1.04754 0.85689 0.97926 0.10368  -0.17814 0.01020  143 GLY B N     
461  C  CA    . GLY A 64  ? 0.97208 0.79003 0.91554 0.10488  -0.18768 0.00119  143 GLY B CA    
462  C  C     . GLY A 64  ? 1.08256 0.90941 1.05468 0.10512  -0.19162 -0.00623 143 GLY B C     
463  O  O     . GLY A 64  ? 1.05725 0.89381 1.04414 0.10474  -0.19870 -0.01349 143 GLY B O     
464  N  N     . CYS A 65  ? 1.00944 0.83344 0.99103 0.10599  -0.18759 -0.00469 144 CYS B N     
465  C  CA    . CYS A 65  ? 0.89409 0.72814 0.90383 0.10667  -0.18962 -0.01270 144 CYS B CA    
466  C  C     . CYS A 65  ? 1.00522 0.85588 1.03262 0.09737  -0.17898 -0.01975 144 CYS B C     
467  O  O     . CYS A 65  ? 1.13728 1.00179 1.18870 0.09735  -0.18072 -0.02741 144 CYS B O     
468  C  CB    . CYS A 65  ? 0.84864 0.67268 0.86264 0.11171  -0.18972 -0.00946 144 CYS B CB    
469  S  SG    . CYS A 65  ? 1.08523 0.89037 1.07983 0.12315  -0.20205 0.00108  144 CYS B SG    
470  N  N     . LEU A 66  ? 0.95593 0.80671 0.97210 0.08983  -0.16798 -0.01685 145 LEU B N     
471  C  CA    . LEU A 66  ? 0.95568 0.82198 0.98554 0.08118  -0.15726 -0.02230 145 LEU B CA    
472  C  C     . LEU A 66  ? 1.02720 0.90648 1.06459 0.07670  -0.15947 -0.02553 145 LEU B C     
473  O  O     . LEU A 66  ? 1.06113 0.94233 1.08893 0.07030  -0.15437 -0.02317 145 LEU B O     
474  C  CB    . LEU A 66  ? 0.91043 0.77147 0.92548 0.07517  -0.14616 -0.01752 145 LEU B CB    
475  C  CG    . LEU A 66  ? 0.91527 0.75922 0.91813 0.07914  -0.14594 -0.01071 145 LEU B CG    
476  C  CD1   . LEU A 66  ? 0.93424 0.77466 0.92428 0.07229  -0.13543 -0.00570 145 LEU B CD1   
477  C  CD2   . LEU A 66  ? 0.84620 0.68922 0.86677 0.08358  -0.14779 -0.01553 145 LEU B CD2   
478  N  N     . VAL A 67  ? 0.99957 0.88795 1.05662 0.08014  -0.16778 -0.03081 146 VAL B N     
479  C  CA    . VAL A 67  ? 1.02311 0.92339 1.09186 0.07611  -0.17221 -0.03349 146 VAL B CA    
480  C  C     . VAL A 67  ? 0.96588 0.88317 1.04623 0.06610  -0.16023 -0.03492 146 VAL B C     
481  O  O     . VAL A 67  ? 1.02284 0.94594 1.10537 0.06020  -0.16093 -0.03384 146 VAL B O     
482  C  CB    . VAL A 67  ? 0.95278 0.86091 1.04415 0.08180  -0.18344 -0.03864 146 VAL B CB    
483  C  CG1   . VAL A 67  ? 1.06843 0.98915 1.17570 0.07682  -0.18895 -0.04096 146 VAL B CG1   
484  C  CG2   . VAL A 67  ? 0.98916 0.88021 1.06704 0.09218  -0.19611 -0.03648 146 VAL B CG2   
485  N  N     . ASN A 68  ? 0.95800 0.88326 1.04574 0.06438  -0.14967 -0.03733 147 ASN B N     
486  C  CA    . ASN A 68  ? 0.98812 0.93149 1.08617 0.05593  -0.13802 -0.03866 147 ASN B CA    
487  C  C     . ASN A 68  ? 0.99563 0.93270 1.07326 0.04953  -0.12930 -0.03378 147 ASN B C     
488  O  O     . ASN A 68  ? 1.04260 0.99349 1.12549 0.04292  -0.11908 -0.03431 147 ASN B O     
489  C  CB    . ASN A 68  ? 1.00309 0.95960 1.11776 0.05818  -0.13097 -0.04504 147 ASN B CB    
490  C  CG    . ASN A 68  ? 0.96242 0.92907 1.10100 0.06433  -0.13844 -0.05020 147 ASN B CG    
491  O  OD1   . ASN A 68  ? 1.02329 0.99891 1.17544 0.06266  -0.14475 -0.04960 147 ASN B OD1   
492  N  ND2   . ASN A 68  ? 1.07440 1.03940 1.21982 0.07163  -0.13852 -0.05546 147 ASN B ND2   
493  N  N     . LEU A 69  ? 0.96192 0.87990 1.01663 0.05170  -0.13287 -0.02876 148 LEU B N     
494  C  CA    . LEU A 69  ? 1.00617 0.91882 1.04280 0.04613  -0.12467 -0.02399 148 LEU B CA    
495  C  C     . LEU A 69  ? 1.06813 0.98991 1.10695 0.03864  -0.12274 -0.02200 148 LEU B C     
496  O  O     . LEU A 69  ? 1.03603 0.95771 1.07959 0.03924  -0.13148 -0.02200 148 LEU B O     
497  C  CB    . LEU A 69  ? 1.01902 0.91119 1.03184 0.05086  -0.12876 -0.01826 148 LEU B CB    
498  C  CG    . LEU A 69  ? 0.97921 0.86117 0.98336 0.05313  -0.12399 -0.01598 148 LEU B CG    
499  C  CD1   . LEU A 69  ? 0.86759 0.73221 0.84842 0.05690  -0.12691 -0.00803 148 LEU B CD1   
500  C  CD2   . LEU A 69  ? 0.93163 0.82172 0.93775 0.04587  -0.11223 -0.01716 148 LEU B CD2   
501  N  N     . MET A 70  ? 0.99527 0.92465 1.03146 0.03163  -0.11201 -0.02038 149 MET B N     
502  C  CA    . MET A 70  ? 0.98321 0.91961 1.01964 0.02414  -0.10929 -0.01690 149 MET B CA    
503  C  C     . MET A 70  ? 0.93681 0.86371 0.95234 0.02110  -0.10399 -0.01187 149 MET B C     
504  O  O     . MET A 70  ? 0.97204 0.89858 0.98367 0.01703  -0.10493 -0.00842 149 MET B O     
505  C  CB    . MET A 70  ? 1.04683 1.00565 1.10208 0.01783  -0.10102 -0.01843 149 MET B CB    
506  C  CG    . MET A 70  ? 1.08208 1.05484 1.16198 0.01900  -0.10578 -0.02177 149 MET B CG    
507  S  SD    . MET A 70  ? 1.11417 1.11564 1.21456 0.01411  -0.09362 -0.02377 149 MET B SD    
508  C  CE    . MET A 70  ? 1.17488 1.18239 1.26758 0.00380  -0.08595 -0.01594 149 MET B CE    
509  N  N     . THR A 71  ? 0.94600 0.86523 0.94978 0.02296  -0.09901 -0.01127 150 THR B N     
510  C  CA    . THR A 71  ? 0.94283 0.85426 0.92871 0.02017  -0.09368 -0.00620 150 THR B CA    
511  C  C     . THR A 71  ? 0.91001 0.80487 0.88153 0.02642  -0.09611 -0.00362 150 THR B C     
512  O  O     . THR A 71  ? 0.92835 0.82084 0.90466 0.02952  -0.09574 -0.00610 150 THR B O     
513  C  CB    . THR A 71  ? 0.93125 0.85398 0.92024 0.01382  -0.08322 -0.00701 150 THR B CB    
514  O  OG1   . THR A 71  ? 1.02846 0.96711 1.02875 0.00781  -0.08042 -0.00697 150 THR B OG1   
515  C  CG2   . THR A 71  ? 0.92623 0.84058 0.89831 0.01140  -0.07845 -0.00188 150 THR B CG2   
516  N  N     . LEU A 72  ? 0.80697 0.69078 0.76150 0.02862  -0.09861 0.00164  151 LEU B N     
517  C  CA    . LEU A 72  ? 0.80527 0.67473 0.74459 0.03437  -0.09988 0.00653  151 LEU B CA    
518  C  C     . LEU A 72  ? 0.99669 0.86280 0.92106 0.03127  -0.09338 0.01272  151 LEU B C     
519  O  O     . LEU A 72  ? 0.85236 0.71624 0.76653 0.03232  -0.09542 0.01482  151 LEU B O     
520  C  CB    . LEU A 72  ? 0.87846 0.73885 0.81055 0.04275  -0.11037 0.00698  151 LEU B CB    
521  C  CG    . LEU A 72  ? 0.88826 0.73505 0.80517 0.04993  -0.11243 0.01316  151 LEU B CG    
522  C  CD1   . LEU A 72  ? 0.88951 0.73416 0.81613 0.05016  -0.11016 0.01316  151 LEU B CD1   
523  C  CD2   . LEU A 72  ? 0.74795 0.58798 0.65726 0.05869  -0.12378 0.01249  151 LEU B CD2   
524  N  N     . ALA A 73  ? 1.00243 0.86833 0.92674 0.02776  -0.08615 0.01505  152 ALA B N     
525  C  CA    . ALA A 73  ? 0.87503 0.73974 0.78856 0.02408  -0.07944 0.02095  152 ALA B CA    
526  C  C     . ALA A 73  ? 0.84301 0.69572 0.74381 0.02909  -0.07940 0.02882  152 ALA B C     
527  O  O     . ALA A 73  ? 0.86844 0.71619 0.77399 0.02955  -0.07862 0.03038  152 ALA B O     
528  C  CB    . ALA A 73  ? 0.86048 0.73373 0.78316 0.01657  -0.07217 0.01858  152 ALA B CB    
529  N  N     . LEU A 74  ? 0.84230 0.69070 0.72737 0.03307  -0.08019 0.03404  153 LEU B N     
530  C  CA    . LEU A 74  ? 0.84834 0.68757 0.71941 0.03869  -0.07943 0.04304  153 LEU B CA    
531  C  C     . LEU A 74  ? 0.92756 0.76875 0.78741 0.03705  -0.07247 0.04966  153 LEU B C     
532  O  O     . LEU A 74  ? 0.96167 0.79817 0.80622 0.04327  -0.07188 0.05688  153 LEU B O     
533  C  CB    . LEU A 74  ? 0.95949 0.79202 0.81960 0.04839  -0.08802 0.04311  153 LEU B CB    
534  C  CG    . LEU A 74  ? 1.04243 0.87296 0.91384 0.05128  -0.09600 0.03724  153 LEU B CG    
535  C  CD1   . LEU A 74  ? 0.82212 0.64893 0.68412 0.05977  -0.10604 0.03447  153 LEU B CD1   
536  C  CD2   . LEU A 74  ? 0.90026 0.72357 0.77529 0.05289  -0.09538 0.04263  153 LEU B CD2   
537  N  N     . SER A 75  ? 0.98018 0.82933 0.84720 0.02929  -0.06707 0.04753  154 SER B N     
538  C  CA    . SER A 75  ? 0.96200 0.81418 0.82040 0.02779  -0.06086 0.05326  154 SER B CA    
539  C  C     . SER A 75  ? 1.08084 0.93024 0.93786 0.02665  -0.05487 0.06283  154 SER B C     
540  O  O     . SER A 75  ? 0.96248 0.80877 0.82972 0.02372  -0.05473 0.06348  154 SER B O     
541  C  CB    . SER A 75  ? 0.88080 0.74246 0.74803 0.01980  -0.05757 0.04882  154 SER B CB    
542  O  OG    . SER A 75  ? 1.05829 0.92404 0.94023 0.01357  -0.05661 0.04411  154 SER B OG    
543  N  N     . GLU A 76  ? 1.10550 0.95631 0.95100 0.02920  -0.05010 0.07035  155 GLU B N     
544  C  CA    . GLU A 76  ? 1.04439 0.89449 0.88915 0.02806  -0.04366 0.08154  155 GLU B CA    
545  C  C     . GLU A 76  ? 0.96965 0.81077 0.81359 0.03221  -0.04633 0.08751  155 GLU B C     
546  O  O     . GLU A 76  ? 0.98955 0.82698 0.84669 0.02738  -0.04631 0.08899  155 GLU B O     
547  C  CB    . GLU A 76  ? 1.02522 0.88084 0.88512 0.01783  -0.03890 0.08120  155 GLU B CB    
548  C  CG    . GLU A 76  ? 1.13742 1.00207 0.99470 0.01511  -0.03386 0.08213  155 GLU B CG    
549  C  CD    . GLU A 76  ? 1.30850 1.17960 1.18017 0.00528  -0.03156 0.07840  155 GLU B CD    
550  O  OE1   . GLU A 76  ? 1.27095 1.13999 1.15381 0.00035  -0.03071 0.08028  155 GLU B OE1   
551  O  OE2   . GLU A 76  ? 1.33474 1.21268 1.20655 0.00274  -0.03127 0.07352  155 GLU B OE2   
552  N  N     . ASN A 77  ? 0.89836 0.73564 0.72608 0.04191  -0.04945 0.09054  156 ASN B N     
553  C  CA    . ASN A 77  ? 0.93608 0.76538 0.75859 0.04767  -0.05178 0.09885  156 ASN B CA    
554  C  C     . ASN A 77  ? 0.97230 0.80328 0.77313 0.05704  -0.04877 0.10791  156 ASN B C     
555  O  O     . ASN A 77  ? 1.19399 1.03251 0.98790 0.05744  -0.04287 0.10967  156 ASN B O     
556  C  CB    . ASN A 77  ? 1.00776 0.83045 0.83342 0.05132  -0.06163 0.09045  156 ASN B CB    
557  C  CG    . ASN A 77  ? 0.90612 0.72696 0.75315 0.04374  -0.06347 0.08424  156 ASN B CG    
558  O  OD1   . ASN A 77  ? 0.98615 0.80094 0.84172 0.04195  -0.06305 0.09034  156 ASN B OD1   
559  N  ND2   . ASN A 77  ? 0.96728 0.79354 0.82336 0.03966  -0.06568 0.07215  156 ASN B ND2   
560  N  N     . SER A 78  ? 1.02904 0.85369 0.81840 0.06548  -0.05293 0.11358  157 SER B N     
561  C  CA    . SER A 78  ? 1.08405 0.91098 0.84981 0.07637  -0.05083 0.12145  157 SER B CA    
562  C  C     . SER A 78  ? 1.18876 1.00937 0.94046 0.08682  -0.06142 0.11580  157 SER B C     
563  O  O     . SER A 78  ? 1.15030 0.96896 0.88457 0.09627  -0.06211 0.12487  157 SER B O     
564  C  CB    . SER A 78  ? 1.06115 0.88907 0.82478 0.07659  -0.04276 0.13989  157 SER B CB    
565  O  OG    . SER A 78  ? 1.14718 0.98203 0.92429 0.06722  -0.03354 0.14496  157 SER B OG    
566  N  N     . LEU A 79  ? 1.19338 1.01162 0.95292 0.08526  -0.06999 0.10120  158 LEU B N     
567  C  CA    . LEU A 79  ? 1.09026 0.90285 0.84015 0.09428  -0.08155 0.09443  158 LEU B CA    
568  C  C     . LEU A 79  ? 1.08907 0.90412 0.81475 0.10541  -0.08394 0.09173  158 LEU B C     
569  O  O     . LEU A 79  ? 1.15793 0.97876 0.88047 0.10441  -0.07976 0.08771  158 LEU B O     
570  C  CB    . LEU A 79  ? 1.01789 0.82941 0.78587 0.08873  -0.08940 0.08005  158 LEU B CB    
571  C  CG    . LEU A 79  ? 0.94966 0.75905 0.74104 0.07987  -0.08907 0.07920  158 LEU B CG    
572  C  CD1   . LEU A 79  ? 0.94467 0.75704 0.75249 0.07490  -0.09485 0.06519  158 LEU B CD1   
573  C  CD2   . LEU A 79  ? 0.98710 0.78830 0.77717 0.08521  -0.09395 0.08611  158 LEU B CD2   
574  N  N     . THR A 80  ? 1.07392 0.88435 0.78211 0.11678  -0.09136 0.09351  159 THR B N     
575  C  CA    . THR A 80  ? 1.12065 0.93225 0.80486 0.12911  -0.09653 0.08800  159 THR B CA    
576  C  C     . THR A 80  ? 1.15813 0.96387 0.84237 0.13412  -0.11212 0.07398  159 THR B C     
577  O  O     . THR A 80  ? 1.17686 0.98268 0.84599 0.14272  -0.11859 0.06509  159 THR B O     
578  C  CB    . THR A 80  ? 1.18855 1.00161 0.84730 0.14059  -0.09260 0.10162  159 THR B CB    
579  O  OG1   . THR A 80  ? 1.27378 1.07994 0.93311 0.14312  -0.09856 0.10821  159 THR B OG1   
580  C  CG2   . THR A 80  ? 0.97314 0.79396 0.63284 0.13587  -0.07687 0.11622  159 THR B CG2   
581  N  N     . SER A 81  ? 1.07096 0.87190 0.77288 0.12928  -0.11869 0.07135  160 SER B N     
582  C  CA    . SER A 81  ? 1.10645 0.90335 0.81373 0.13247  -0.13347 0.05828  160 SER B CA    
583  C  C     . SER A 81  ? 1.10471 0.90040 0.84000 0.12263  -0.13549 0.05568  160 SER B C     
584  O  O     . SER A 81  ? 1.10195 0.89880 0.85019 0.11436  -0.12627 0.06297  160 SER B O     
585  C  CB    . SER A 81  ? 1.29998 1.09205 0.98440 0.14687  -0.14371 0.05956  160 SER B CB    
586  O  OG    . SER A 81  ? 1.29906 1.08767 0.99048 0.14970  -0.15908 0.04619  160 SER B OG    
587  N  N     . LEU A 82  ? 1.12299 0.91687 0.86831 0.12399  -0.14805 0.04466  161 LEU B N     
588  C  CA    . LEU A 82  ? 1.08796 0.88247 0.85980 0.11662  -0.15116 0.04051  161 LEU B CA    
589  C  C     . LEU A 82  ? 1.04161 0.83121 0.81247 0.12511  -0.16521 0.03725  161 LEU B C     
590  O  O     . LEU A 82  ? 1.00833 0.79523 0.76235 0.13485  -0.17526 0.03288  161 LEU B O     
591  C  CB    . LEU A 82  ? 1.00676 0.80777 0.79939 0.10718  -0.15146 0.02965  161 LEU B CB    
592  C  CG    . LEU A 82  ? 1.02089 0.82760 0.81894 0.09743  -0.13819 0.03236  161 LEU B CG    
593  C  CD1   . LEU A 82  ? 1.01671 0.82978 0.83230 0.08966  -0.14000 0.02259  161 LEU B CD1   
594  C  CD2   . LEU A 82  ? 0.96554 0.77313 0.77523 0.09056  -0.12867 0.03979  161 LEU B CD2   
595  N  N     . PRO A 83  ? 1.04709 0.83548 0.83585 0.12228  -0.16688 0.03864  162 PRO B N     
596  C  CA    . PRO A 83  ? 0.82473 0.60851 0.61325 0.13090  -0.18044 0.03667  162 PRO B CA    
597  C  C     . PRO A 83  ? 0.96648 0.75355 0.76495 0.13217  -0.19331 0.02284  162 PRO B C     
598  O  O     . PRO A 83  ? 1.03945 0.83346 0.85973 0.12313  -0.19166 0.01500  162 PRO B O     
599  C  CB    . PRO A 83  ? 0.92804 0.71101 0.73870 0.12585  -0.17772 0.03985  162 PRO B CB    
600  C  CG    . PRO A 83  ? 0.97358 0.75831 0.78845 0.11673  -0.16256 0.04644  162 PRO B CG    
601  C  CD    . PRO A 83  ? 1.02601 0.81690 0.83548 0.11206  -0.15703 0.04174  162 PRO B CD    
602  N  N     . ASP A 84  ? 1.09143 0.87387 0.87418 0.14357  -0.20666 0.02036  163 ASP B N     
603  C  CA    . ASP A 84  ? 1.07083 0.85541 0.86423 0.14542  -0.22130 0.00725  163 ASP B CA    
604  C  C     . ASP A 84  ? 1.11355 0.90328 0.93939 0.13981  -0.22611 0.00204  163 ASP B C     
605  O  O     . ASP A 84  ? 1.20966 1.00369 1.05160 0.13848  -0.23663 -0.00836 163 ASP B O     
606  C  CB    . ASP A 84  ? 1.19785 0.97604 0.96659 0.15990  -0.23570 0.00565  163 ASP B CB    
607  C  CG    . ASP A 84  ? 1.36079 1.13644 1.09907 0.16651  -0.23315 0.00627  163 ASP B CG    
608  O  OD1   . ASP A 84  ? 1.27255 1.05048 1.01472 0.16276  -0.23390 -0.00264 163 ASP B OD1   
609  O  OD2   . ASP A 84  ? 1.35376 1.12565 1.06482 0.17564  -0.23008 0.01615  163 ASP B OD2   
610  N  N     . SER A 85  ? 1.12304 0.91281 0.96007 0.13666  -0.21888 0.00883  164 SER B N     
611  C  CA    . SER A 85  ? 1.01993 0.81595 0.88803 0.13208  -0.22173 0.00369  164 SER B CA    
612  C  C     . SER A 85  ? 1.07191 0.87897 0.96381 0.11952  -0.21252 -0.00199 164 SER B C     
613  O  O     . SER A 85  ? 1.06005 0.87481 0.97822 0.11535  -0.21239 -0.00612 164 SER B O     
614  C  CB    . SER A 85  ? 1.10952 0.90053 0.98072 0.13413  -0.21763 0.01230  164 SER B CB    
615  O  OG    . SER A 85  ? 1.06115 0.85123 0.92937 0.12718  -0.20209 0.01961  164 SER B OG    
616  N  N     . LEU A 86  ? 1.08408 0.89292 0.96746 0.11398  -0.20477 -0.00206 165 LEU B N     
617  C  CA    . LEU A 86  ? 0.89982 0.71934 0.80368 0.10219  -0.19563 -0.00587 165 LEU B CA    
618  C  C     . LEU A 86  ? 1.03623 0.86388 0.95907 0.09883  -0.20455 -0.01524 165 LEU B C     
619  O  O     . LEU A 86  ? 0.99732 0.83528 0.93837 0.08902  -0.19746 -0.01756 165 LEU B O     
620  C  CB    . LEU A 86  ? 0.97665 0.79488 0.86506 0.09732  -0.18342 -0.00099 165 LEU B CB    
621  C  CG    . LEU A 86  ? 0.96842 0.78174 0.84511 0.09683  -0.17174 0.00893  165 LEU B CG    
622  C  CD1   . LEU A 86  ? 0.81262 0.62898 0.68334 0.08936  -0.15932 0.01191  165 LEU B CD1   
623  C  CD2   . LEU A 86  ? 1.06431 0.88031 0.96066 0.09390  -0.16847 0.00935  165 LEU B CD2   
624  N  N     . ASP A 87  ? 1.11391 0.93755 1.03360 0.10656  -0.22021 -0.02020 166 ASP B N     
625  C  CA    . ASP A 87  ? 0.98187 0.81359 0.92518 0.10287  -0.23023 -0.02879 166 ASP B CA    
626  C  C     . ASP A 87  ? 1.03495 0.88014 1.01082 0.09658  -0.22697 -0.03067 166 ASP B C     
627  O  O     . ASP A 87  ? 0.99892 0.85570 0.99870 0.08858  -0.22696 -0.03466 166 ASP B O     
628  C  CB    . ASP A 87  ? 1.06415 0.88907 1.00032 0.11318  -0.24930 -0.03432 166 ASP B CB    
629  C  CG    . ASP A 87  ? 1.18573 0.99724 1.08500 0.12409  -0.25223 -0.03074 166 ASP B CG    
630  O  OD1   . ASP A 87  ? 1.34449 1.15244 1.22516 0.12250  -0.24203 -0.02662 166 ASP B OD1   
631  O  OD2   . ASP A 87  ? 0.99275 0.79833 0.88164 0.13465  -0.26466 -0.03169 166 ASP B OD2   
632  N  N     . ASN A 88  ? 0.95554 0.79984 0.93337 0.10048  -0.22426 -0.02757 167 ASN B N     
633  C  CA    . ASN A 88  ? 0.91002 0.76736 0.91766 0.09657  -0.22109 -0.03026 167 ASN B CA    
634  C  C     . ASN A 88  ? 0.97290 0.84204 0.99333 0.08551  -0.20531 -0.02949 167 ASN B C     
635  O  O     . ASN A 88  ? 1.11673 1.00005 1.16300 0.08172  -0.20171 -0.03267 167 ASN B O     
636  C  CB    . ASN A 88  ? 1.00133 0.85231 1.00563 0.10421  -0.22184 -0.02704 167 ASN B CB    
637  C  CG    . ASN A 88  ? 1.15064 0.99189 1.14434 0.11568  -0.23840 -0.02742 167 ASN B CG    
638  O  OD1   . ASN A 88  ? 0.98315 0.83027 0.99675 0.11930  -0.24884 -0.03224 167 ASN B OD1   
639  N  ND2   . ASN A 88  ? 1.01568 0.84314 0.97782 0.12191  -0.24083 -0.02218 167 ASN B ND2   
640  N  N     . LEU A 89  ? 1.06274 0.92750 1.06572 0.08087  -0.19593 -0.02545 168 LEU B N     
641  C  CA    . LEU A 89  ? 0.92196 0.79800 0.93508 0.07049  -0.18200 -0.02458 168 LEU B CA    
642  C  C     . LEU A 89  ? 0.98094 0.86643 1.00835 0.06355  -0.18504 -0.02741 168 LEU B C     
643  O  O     . LEU A 89  ? 0.93339 0.81680 0.95107 0.05867  -0.18084 -0.02518 168 LEU B O     
644  C  CB    . LEU A 89  ? 0.93499 0.80232 0.92459 0.06876  -0.17117 -0.01849 168 LEU B CB    
645  C  CG    . LEU A 89  ? 0.91257 0.77513 0.89633 0.07066  -0.16313 -0.01472 168 LEU B CG    
646  C  CD1   . LEU A 89  ? 0.93625 0.78720 0.91175 0.08098  -0.17224 -0.01281 168 LEU B CD1   
647  C  CD2   . LEU A 89  ? 0.88341 0.73995 0.84773 0.06700  -0.15262 -0.00858 168 LEU B CD2   
648  N  N     . LYS A 90  ? 0.96856 0.86480 1.02146 0.06315  -0.19295 -0.03194 169 LYS B N     
649  C  CA    . LYS A 90  ? 0.95608 0.86100 1.02684 0.05660  -0.19817 -0.03391 169 LYS B CA    
650  C  C     . LYS A 90  ? 0.92792 0.84916 1.01462 0.04544  -0.18473 -0.03108 169 LYS B C     
651  O  O     . LYS A 90  ? 0.82139 0.75164 0.92644 0.03874  -0.18786 -0.03095 169 LYS B O     
652  C  CB    . LYS A 90  ? 0.89836 0.81047 0.99359 0.05964  -0.21173 -0.03894 169 LYS B CB    
653  C  CG    . LYS A 90  ? 0.79805 0.69462 0.87894 0.06931  -0.22923 -0.04253 169 LYS B CG    
654  C  CD    . LYS A 90  ? 0.88807 0.78271 0.97100 0.07872  -0.23602 -0.04449 169 LYS B CD    
655  C  CE    . LYS A 90  ? 1.05980 0.93918 1.12482 0.08922  -0.25348 -0.04753 169 LYS B CE    
656  N  NZ    . LYS A 90  ? 1.00165 0.88413 1.08382 0.08761  -0.26883 -0.05348 169 LYS B NZ    
657  N  N     . LYS A 91  ? 0.95740 0.88261 1.03780 0.04331  -0.17051 -0.02853 170 LYS B N     
658  C  CA    . LYS A 91  ? 0.95893 0.90005 1.05084 0.03369  -0.15741 -0.02578 170 LYS B CA    
659  C  C     . LYS A 91  ? 1.05941 0.99295 1.12805 0.03080  -0.14679 -0.02156 170 LYS B C     
660  O  O     . LYS A 91  ? 1.12843 1.07387 1.20169 0.02457  -0.13471 -0.01960 170 LYS B O     
661  C  CB    . LYS A 91  ? 1.07017 1.02875 1.18219 0.03361  -0.15011 -0.02838 170 LYS B CB    
662  C  CG    . LYS A 91  ? 1.03993 1.00943 1.17884 0.03613  -0.15964 -0.03221 170 LYS B CG    
663  C  CD    . LYS A 91  ? 1.12815 1.11875 1.28894 0.03576  -0.15059 -0.03483 170 LYS B CD    
664  C  CE    . LYS A 91  ? 1.14716 1.13026 1.29503 0.04280  -0.14543 -0.03805 170 LYS B CE    
665  N  NZ    . LYS A 91  ? 1.16217 1.16542 1.33152 0.04433  -0.13785 -0.04263 170 LYS B NZ    
666  N  N     . LEU A 92  ? 1.01595 0.93110 1.05978 0.03555  -0.15111 -0.02008 171 LEU B N     
667  C  CA    . LEU A 92  ? 0.94668 0.85486 0.96937 0.03335  -0.14157 -0.01572 171 LEU B CA    
668  C  C     . LEU A 92  ? 0.99807 0.91004 1.02197 0.02568  -0.13909 -0.01277 171 LEU B C     
669  O  O     . LEU A 92  ? 0.88757 0.79550 0.91486 0.02586  -0.14894 -0.01387 171 LEU B O     
670  C  CB    . LEU A 92  ? 0.90051 0.78984 0.89732 0.04176  -0.14645 -0.01423 171 LEU B CB    
671  C  CG    . LEU A 92  ? 0.94474 0.82718 0.92086 0.04064  -0.13632 -0.00908 171 LEU B CG    
672  C  CD1   . LEU A 92  ? 0.89828 0.78536 0.87885 0.03915  -0.12694 -0.00860 171 LEU B CD1   
673  C  CD2   . LEU A 92  ? 0.80982 0.67599 0.76137 0.04904  -0.14171 -0.00649 171 LEU B CD2   
674  N  N     . ARG A 93  ? 0.90824 0.82729 0.92962 0.01926  -0.12684 -0.00923 172 ARG B N     
675  C  CA    . ARG A 93  ? 0.90327 0.82774 0.92772 0.01139  -0.12336 -0.00532 172 ARG B CA    
676  C  C     . ARG A 93  ? 0.90037 0.81344 0.90182 0.01166  -0.11948 -0.00172 172 ARG B C     
677  O  O     . ARG A 93  ? 0.87019 0.77690 0.86736 0.01090  -0.12458 -0.00045 172 ARG B O     
678  C  CB    . ARG A 93  ? 0.84982 0.79429 0.89056 0.00355  -0.11254 -0.00336 172 ARG B CB    
679  C  CG    . ARG A 93  ? 1.03994 1.00008 1.10773 0.00144  -0.11560 -0.00521 172 ARG B CG    
680  C  CD    . ARG A 93  ? 1.14037 1.12186 1.22076 -0.00435 -0.10322 -0.00354 172 ARG B CD    
681  N  NE    . ARG A 93  ? 1.36632 1.36534 1.47356 -0.00563 -0.10480 -0.00488 172 ARG B NE    
682  C  CZ    . ARG A 93  ? 1.43678 1.45107 1.56395 -0.01313 -0.10381 0.00032  172 ARG B CZ    
683  N  NH1   . ARG A 93  ? 1.43157 1.44506 1.55484 -0.02006 -0.10160 0.00716  172 ARG B NH1   
684  N  NH2   . ARG A 93  ? 1.36984 1.40110 1.52280 -0.01372 -0.10509 -0.00064 172 ARG B NH2   
685  N  N     . MET A 94  ? 0.67350 0.58405 0.66156 0.01277  -0.11090 -0.00019 173 MET B N     
686  C  CA    . MET A 94  ? 0.82766 0.72924 0.79578 0.01301  -0.10656 0.00378  173 MET B CA    
687  C  C     . MET A 94  ? 0.90665 0.79489 0.85686 0.02115  -0.10795 0.00413  173 MET B C     
688  O  O     . MET A 94  ? 0.75409 0.64226 0.70704 0.02390  -0.10688 0.00264  173 MET B O     
689  C  CB    . MET A 94  ? 0.98055 0.89223 0.94954 0.00564  -0.09471 0.00703  173 MET B CB    
690  C  CG    . MET A 94  ? 1.08609 0.99871 1.05108 0.00658  -0.08754 0.00618  173 MET B CG    
691  S  SD    . MET A 94  ? 1.04160 0.94039 0.98387 0.00980  -0.08390 0.01078  173 MET B SD    
692  C  CE    . MET A 94  ? 1.00420 0.90700 0.94165 0.00359  -0.07959 0.01534  173 MET B CE    
693  N  N     . LEU A 95  ? 0.92188 0.79923 0.85427 0.02538  -0.11040 0.00648  174 LEU B N     
694  C  CA    . LEU A 95  ? 0.86060 0.72627 0.77412 0.03337  -0.11115 0.00887  174 LEU B CA    
695  C  C     . LEU A 95  ? 0.92742 0.79027 0.82579 0.03229  -0.10353 0.01429  174 LEU B C     
696  O  O     . LEU A 95  ? 0.85984 0.71977 0.75068 0.03359  -0.10593 0.01440  174 LEU B O     
697  C  CB    . LEU A 95  ? 0.80906 0.66532 0.71440 0.04233  -0.12323 0.00580  174 LEU B CB    
698  C  CG    . LEU A 95  ? 0.84245 0.68789 0.72731 0.05174  -0.12462 0.00925  174 LEU B CG    
699  C  CD1   . LEU A 95  ? 0.91272 0.75852 0.80309 0.05181  -0.12104 0.01148  174 LEU B CD1   
700  C  CD2   . LEU A 95  ? 0.76594 0.60365 0.64243 0.06102  -0.13773 0.00494  174 LEU B CD2   
701  N  N     . ASP A 96  ? 0.92859 0.79237 0.82405 0.03006  -0.09495 0.01840  175 ASP B N     
702  C  CA    . ASP A 96  ? 0.77680 0.63973 0.66096 0.02829  -0.08714 0.02412  175 ASP B CA    
703  C  C     . ASP A 96  ? 0.86475 0.71803 0.73180 0.03616  -0.08705 0.02941  175 ASP B C     
704  O  O     . ASP A 96  ? 0.85160 0.70196 0.71958 0.03709  -0.08504 0.03224  175 ASP B O     
705  C  CB    . ASP A 96  ? 0.82507 0.69613 0.71870 0.02013  -0.07835 0.02534  175 ASP B CB    
706  C  CG    . ASP A 96  ? 1.05394 0.92590 0.93906 0.01728  -0.07099 0.03097  175 ASP B CG    
707  O  OD1   . ASP A 96  ? 0.92725 0.79461 0.79978 0.02170  -0.07192 0.03392  175 ASP B OD1   
708  O  OD2   . ASP A 96  ? 1.18294 1.06073 1.07426 0.01112  -0.06463 0.03189  175 ASP B OD2   
709  N  N     . LEU A 97  ? 0.91096 0.75955 0.76266 0.04222  -0.08929 0.03097  176 LEU B N     
710  C  CA    . LEU A 97  ? 0.84518 0.68681 0.67838 0.05066  -0.08839 0.03701  176 LEU B CA    
711  C  C     . LEU A 97  ? 0.95833 0.80205 0.78041 0.05091  -0.08062 0.04280  176 LEU B C     
712  O  O     . LEU A 97  ? 0.98591 0.82591 0.79053 0.05931  -0.08006 0.04722  176 LEU B O     
713  C  CB    . LEU A 97  ? 0.77694 0.61171 0.59871 0.06090  -0.09902 0.03297  176 LEU B CB    
714  C  CG    . LEU A 97  ? 0.92125 0.75245 0.74961 0.06393  -0.10731 0.02954  176 LEU B CG    
715  C  CD1   . LEU A 97  ? 0.93979 0.76619 0.76111 0.07205  -0.11970 0.02266  176 LEU B CD1   
716  C  CD2   . LEU A 97  ? 1.06149 0.88777 0.88159 0.06821  -0.10438 0.03757  176 LEU B CD2   
717  N  N     . ARG A 98  ? 0.89792 0.74862 0.72947 0.04246  -0.07457 0.04308  177 ARG B N     
718  C  CA    . ARG A 98  ? 0.98075 0.83428 0.80344 0.04312  -0.06811 0.04793  177 ARG B CA    
719  C  C     . ARG A 98  ? 0.98809 0.84255 0.80695 0.04253  -0.05960 0.05753  177 ARG B C     
720  O  O     . ARG A 98  ? 0.96281 0.81604 0.78982 0.03882  -0.05819 0.05982  177 ARG B O     
721  C  CB    . ARG A 98  ? 0.93593 0.79666 0.77002 0.03466  -0.06549 0.04554  177 ARG B CB    
722  C  CG    . ARG A 98  ? 0.97868 0.84568 0.82754 0.02475  -0.06047 0.04636  177 ARG B CG    
723  C  CD    . ARG A 98  ? 0.77910 0.65327 0.63962 0.01738  -0.06096 0.04241  177 ARG B CD    
724  N  NE    . ARG A 98  ? 0.97064 0.85033 0.84484 0.01051  -0.05957 0.03974  177 ARG B NE    
725  C  CZ    . ARG A 98  ? 0.84160 0.72721 0.72153 0.00420  -0.05332 0.04164  177 ARG B CZ    
726  N  NH1   . ARG A 98  ? 0.86285 0.75044 0.73826 0.00257  -0.04793 0.04688  177 ARG B NH1   
727  N  NH2   . ARG A 98  ? 1.10075 0.99091 0.99169 -0.00008 -0.05288 0.03759  177 ARG B NH2   
728  N  N     . HIS A 99  ? 1.06380 0.92062 0.87138 0.04649  -0.05418 0.06324  178 HIS B N     
729  C  CA    . HIS A 99  ? 1.00362 0.86241 0.80727 0.04684  -0.04591 0.07417  178 HIS B CA    
730  C  C     . HIS A 99  ? 0.91856 0.77058 0.71488 0.05278  -0.04817 0.07909  178 HIS B C     
731  O  O     . HIS A 99  ? 0.97283 0.82302 0.77818 0.04816  -0.04580 0.08439  178 HIS B O     
732  C  CB    . HIS A 99  ? 0.95479 0.81892 0.77512 0.03549  -0.03990 0.07707  178 HIS B CB    
733  C  CG    . HIS A 99  ? 1.04972 0.92176 0.87444 0.03075  -0.03600 0.07598  178 HIS B CG    
734  N  ND1   . HIS A 99  ? 1.05786 0.93365 0.89485 0.02286  -0.03785 0.06937  178 HIS B ND1   
735  C  CD2   . HIS A 99  ? 0.86210 0.73979 0.68073 0.03326  -0.03034 0.08114  178 HIS B CD2   
736  C  CE1   . HIS A 99  ? 0.99040 0.87277 0.82838 0.02051  -0.03415 0.07079  178 HIS B CE1   
737  N  NE2   . HIS A 99  ? 1.00830 0.89189 0.83597 0.02679  -0.02967 0.07746  178 HIS B NE2   
738  N  N     . ASN A 100 ? 0.97177 0.81959 0.75146 0.06361  -0.05366 0.07703  179 ASN B N     
739  C  CA    . ASN A 100 ? 1.02205 0.86406 0.79098 0.07109  -0.05608 0.08290  179 ASN B CA    
740  C  C     . ASN A 100 ? 1.10628 0.95006 0.85190 0.08310  -0.05376 0.08822  179 ASN B C     
741  O  O     . ASN A 100 ? 1.07297 0.92383 0.81378 0.08410  -0.04679 0.09103  179 ASN B O     
742  C  CB    . ASN A 100 ? 1.02159 0.85651 0.79315 0.07361  -0.06750 0.07393  179 ASN B CB    
743  C  CG    . ASN A 100 ? 0.92698 0.75980 0.71832 0.06499  -0.06849 0.07289  179 ASN B CG    
744  O  OD1   . ASN A 100 ? 0.95136 0.77910 0.74317 0.06680  -0.06938 0.07885  179 ASN B OD1   
745  N  ND2   . ASN A 100 ? 0.96767 0.80467 0.77530 0.05614  -0.06845 0.06541  179 ASN B ND2   
746  N  N     . LYS A 101 ? 1.07831 0.91658 0.80896 0.09300  -0.05965 0.08945  180 LYS B N     
747  C  CA    . LYS A 101 ? 1.10901 0.94970 0.81460 0.10615  -0.05783 0.09435  180 LYS B CA    
748  C  C     . LYS A 101 ? 1.13428 0.96805 0.82511 0.11702  -0.07074 0.08439  180 LYS B C     
749  O  O     . LYS A 101 ? 1.31198 1.14263 0.98740 0.12602  -0.07395 0.08953  180 LYS B O     
750  C  CB    . LYS A 101 ? 1.24455 1.08761 0.94407 0.10800  -0.04949 0.11150  180 LYS B CB    
751  C  CG    . LYS A 101 ? 1.27422 1.12542 0.98675 0.09883  -0.03681 0.12224  180 LYS B CG    
752  C  CD    . LYS A 101 ? 1.32509 1.17869 1.03271 0.10085  -0.02913 0.14066  180 LYS B CD    
753  C  CE    . LYS A 101 ? 1.30291 1.16565 1.02485 0.09191  -0.01701 0.15169  180 LYS B CE    
754  N  NZ    . LYS A 101 ? 1.23717 1.09608 0.98610 0.07733  -0.01819 0.14778  180 LYS B NZ    
755  N  N     . LEU A 102 ? 1.09369 0.92506 0.78997 0.11614  -0.07895 0.07024  181 LEU B N     
756  C  CA    . LEU A 102 ? 1.03003 0.85469 0.71597 0.12539  -0.09283 0.05900  181 LEU B CA    
757  C  C     . LEU A 102 ? 1.12372 0.95021 0.78918 0.13712  -0.09450 0.05307  181 LEU B C     
758  O  O     . LEU A 102 ? 1.13954 0.97004 0.81022 0.13394  -0.09017 0.04977  181 LEU B O     
759  C  CB    . LEU A 102 ? 0.94194 0.76270 0.64982 0.11672  -0.10200 0.04731  181 LEU B CB    
760  C  CG    . LEU A 102 ? 0.97778 0.79789 0.70799 0.10544  -0.10097 0.05005  181 LEU B CG    
761  C  CD1   . LEU A 102 ? 0.95049 0.77116 0.70238 0.09640  -0.10655 0.03956  181 LEU B CD1   
762  C  CD2   . LEU A 102 ? 0.98726 0.80155 0.71224 0.11135  -0.10794 0.05252  181 LEU B CD2   
763  N  N     . ARG A 103 ? 1.04766 0.87126 0.68952 0.15134  -0.10125 0.05129  182 ARG B N     
764  C  CA    . ARG A 103 ? 1.13790 0.96223 0.75901 0.16448  -0.10524 0.04262  182 ARG B CA    
765  C  C     . ARG A 103 ? 1.22483 1.04039 0.85084 0.16681  -0.12201 0.02500  182 ARG B C     
766  O  O     . ARG A 103 ? 1.26027 1.07471 0.87514 0.17559  -0.12687 0.01497  182 ARG B O     
767  C  CB    . ARG A 103 ? 1.22335 1.05047 0.81346 0.18036  -0.10393 0.04911  182 ARG B CB    
768  C  CG    . ARG A 103 ? 1.46553 1.29243 1.05435 0.17860  -0.10048 0.06339  182 ARG B CG    
769  C  CD    . ARG A 103 ? 1.40197 1.23832 0.99382 0.17296  -0.08279 0.08153  182 ARG B CD    
770  N  NE    . ARG A 103 ? 1.65042 1.48423 1.24793 0.16845  -0.08067 0.09494  182 ARG B NE    
771  C  CZ    . ARG A 103 ? 1.54097 1.37560 1.11764 0.17883  -0.08049 0.10538  182 ARG B CZ    
772  N  NH1   . ARG A 103 ? 1.56509 1.40430 1.11188 0.19494  -0.08170 0.10378  182 ARG B NH1   
773  N  NH2   . ARG A 103 ? 1.52569 1.35651 1.11138 0.17349  -0.07934 0.11768  182 ARG B NH2   
774  N  N     . GLU A 104 ? 1.21901 1.02861 0.86263 0.15944  -0.13123 0.02098  183 GLU B N     
775  C  CA    . GLU A 104 ? 1.18293 0.98538 0.83819 0.15854  -0.14666 0.00576  183 GLU B CA    
776  C  C     . GLU A 104 ? 1.03878 0.84012 0.72220 0.14482  -0.14924 0.00638  183 GLU B C     
777  O  O     . GLU A 104 ? 1.04646 0.85047 0.73558 0.13935  -0.14181 0.01665  183 GLU B O     
778  C  CB    . GLU A 104 ? 1.28011 1.07608 0.91412 0.17403  -0.16174 -0.00387 183 GLU B CB    
779  C  CG    . GLU A 104 ? 1.35621 1.14829 0.99194 0.17516  -0.17061 -0.00251 183 GLU B CG    
780  C  CD    . GLU A 104 ? 1.44738 1.24297 1.06311 0.18177  -0.16216 0.01177  183 GLU B CD    
781  O  OE1   . GLU A 104 ? 1.46952 1.27192 1.08241 0.17825  -0.14615 0.02426  183 GLU B OE1   
782  O  OE2   . GLU A 104 ? 1.40706 1.19871 1.01084 0.19037  -0.17206 0.01108  183 GLU B OE2   
783  N  N     . ILE A 105 ? 1.13320 0.93102 0.83531 0.13938  -0.15968 -0.00452 184 ILE B N     
784  C  CA    . ILE A 105 ? 1.06226 0.86096 0.79129 0.12756  -0.16256 -0.00470 184 ILE B CA    
785  C  C     . ILE A 105 ? 1.07965 0.87481 0.80322 0.13386  -0.17109 -0.00449 184 ILE B C     
786  O  O     . ILE A 105 ? 1.13436 0.92379 0.84313 0.14544  -0.18402 -0.01219 184 ILE B O     
787  C  CB    . ILE A 105 ? 1.05633 0.85307 0.80682 0.12111  -0.17261 -0.01534 184 ILE B CB    
788  C  CG1   . ILE A 105 ? 1.08300 0.88274 0.83848 0.11531  -0.16451 -0.01452 184 ILE B CG1   
789  C  CG2   . ILE A 105 ? 0.95267 0.75302 0.73093 0.10974  -0.17462 -0.01498 184 ILE B CG2   
790  C  CD1   . ILE A 105 ? 0.97040 0.76769 0.74690 0.10899  -0.17417 -0.02316 184 ILE B CD1   
791  N  N     . PRO A 106 ? 1.04416 0.84207 0.77828 0.12766  -0.16515 0.00366  185 PRO B N     
792  C  CA    . PRO A 106 ? 1.05215 0.84630 0.78184 0.13415  -0.17375 0.00446  185 PRO B CA    
793  C  C     . PRO A 106 ? 1.15526 0.94605 0.89765 0.13556  -0.19101 -0.00803 185 PRO B C     
794  O  O     . PRO A 106 ? 1.15831 0.95174 0.92437 0.12615  -0.19364 -0.01420 185 PRO B O     
795  C  CB    . PRO A 106 ? 0.98612 0.78394 0.73306 0.12441  -0.16429 0.01343  185 PRO B CB    
796  C  CG    . PRO A 106 ? 1.07033 0.87332 0.81903 0.11662  -0.14878 0.02038  185 PRO B CG    
797  C  CD    . PRO A 106 ? 0.98074 0.78488 0.73052 0.11533  -0.15090 0.01220  185 PRO B CD    
798  N  N     . SER A 107 ? 1.05022 0.83577 0.77707 0.14746  -0.20312 -0.01107 186 SER B N     
799  C  CA    . SER A 107 ? 1.12140 0.90343 0.85908 0.15015  -0.22147 -0.02364 186 SER B CA    
800  C  C     . SER A 107 ? 1.09823 0.88499 0.87029 0.13847  -0.22358 -0.02497 186 SER B C     
801  O  O     . SER A 107 ? 1.27573 1.06278 1.06716 0.13508  -0.23516 -0.03462 186 SER B O     
802  C  CB    . SER A 107 ? 1.11411 0.89046 0.82824 0.16536  -0.23403 -0.02570 186 SER B CB    
803  O  OG    . SER A 107 ? 1.20452 0.98171 0.92102 0.16560  -0.23191 -0.01671 186 SER B OG    
804  N  N     . VAL A 108 ? 0.96123 0.75223 0.74243 0.13234  -0.21261 -0.01550 187 VAL B N     
805  C  CA    . VAL A 108 ? 0.99772 0.79476 0.81060 0.12276  -0.21393 -0.01732 187 VAL B CA    
806  C  C     . VAL A 108 ? 0.97476 0.77900 0.81011 0.10983  -0.20720 -0.01979 187 VAL B C     
807  O  O     . VAL A 108 ? 1.00370 0.81425 0.86628 0.10263  -0.21161 -0.02429 187 VAL B O     
808  C  CB    . VAL A 108 ? 0.92721 0.72570 0.74293 0.12128  -0.20518 -0.00775 187 VAL B CB    
809  C  CG1   . VAL A 108 ? 0.99328 0.79439 0.80499 0.11446  -0.18742 0.00124  187 VAL B CG1   
810  C  CG2   . VAL A 108 ? 0.94831 0.75327 0.79489 0.11474  -0.20882 -0.01139 187 VAL B CG2   
811  N  N     . VAL A 109 ? 1.00749 0.81196 0.83249 0.10689  -0.19655 -0.01633 188 VAL B N     
812  C  CA    . VAL A 109 ? 1.00322 0.81461 0.84830 0.09481  -0.19004 -0.01737 188 VAL B CA    
813  C  C     . VAL A 109 ? 1.00343 0.81339 0.86080 0.09395  -0.20325 -0.02699 188 VAL B C     
814  O  O     . VAL A 109 ? 0.96084 0.77805 0.84383 0.08347  -0.20249 -0.02835 188 VAL B O     
815  C  CB    . VAL A 109 ? 1.00130 0.81325 0.83235 0.09246  -0.17604 -0.01090 188 VAL B CB    
816  C  CG1   . VAL A 109 ? 0.79431 0.61409 0.64588 0.07983  -0.16892 -0.01068 188 VAL B CG1   
817  C  CG2   . VAL A 109 ? 0.85545 0.66791 0.67590 0.09342  -0.16462 -0.00104 188 VAL B CG2   
818  N  N     . TYR A 110 ? 1.09619 0.89710 0.93631 0.10500  -0.21600 -0.03368 189 TYR B N     
819  C  CA    . TYR A 110 ? 1.09895 0.89653 0.95196 0.10485  -0.23113 -0.04391 189 TYR B CA    
820  C  C     . TYR A 110 ? 1.12119 0.92331 1.00144 0.10090  -0.24225 -0.04815 189 TYR B C     
821  O  O     . TYR A 110 ? 1.11740 0.91835 1.01540 0.09823  -0.25477 -0.05558 189 TYR B O     
822  C  CB    . TYR A 110 ? 1.05714 0.84357 0.88309 0.11934  -0.24317 -0.05162 189 TYR B CB    
823  C  CG    . TYR A 110 ? 1.07555 0.85847 0.87870 0.12363  -0.23455 -0.04996 189 TYR B CG    
824  C  CD1   . TYR A 110 ? 1.04271 0.82447 0.85629 0.11797  -0.23459 -0.05350 189 TYR B CD1   
825  C  CD2   . TYR A 110 ? 1.06053 0.84189 0.83282 0.13360  -0.22652 -0.04423 189 TYR B CD2   
826  C  CE1   . TYR A 110 ? 1.02938 0.80855 0.82334 0.12262  -0.22698 -0.05239 189 TYR B CE1   
827  C  CE2   . TYR A 110 ? 1.01192 0.79212 0.76484 0.13798  -0.21813 -0.04254 189 TYR B CE2   
828  C  CZ    . TYR A 110 ? 1.11892 0.89801 0.88276 0.13275  -0.21851 -0.04719 189 TYR B CZ    
829  O  OH    . TYR A 110 ? 1.02211 0.80064 0.76780 0.13779  -0.21035 -0.04585 189 TYR B OH    
830  N  N     . ARG A 111 ? 1.08409 0.89143 0.96974 0.10053  -0.23842 -0.04355 190 ARG B N     
831  C  CA    . ARG A 111 ? 0.98021 0.79365 0.89244 0.09765  -0.24806 -0.04719 190 ARG B CA    
832  C  C     . ARG A 111 ? 1.01467 0.84207 0.95551 0.08475  -0.23635 -0.04209 190 ARG B C     
833  O  O     . ARG A 111 ? 1.06101 0.89647 1.02742 0.08148  -0.24251 -0.04458 190 ARG B O     
834  C  CB    . ARG A 111 ? 0.94212 0.75144 0.84107 0.10848  -0.25487 -0.04701 190 ARG B CB    
835  C  CG    . ARG A 111 ? 1.12814 0.92531 0.99737 0.12268  -0.26754 -0.05234 190 ARG B CG    
836  C  CD    . ARG A 111 ? 1.00502 0.79932 0.86733 0.13285  -0.27878 -0.05336 190 ARG B CD    
837  N  NE    . ARG A 111 ? 1.07215 0.86637 0.91984 0.13587  -0.26699 -0.04275 190 ARG B NE    
838  C  CZ    . ARG A 111 ? 1.15433 0.94195 0.96904 0.14463  -0.26141 -0.03672 190 ARG B CZ    
839  N  NH1   . ARG A 111 ? 1.11931 0.90084 0.91004 0.15206  -0.26517 -0.04083 190 ARG B NH1   
840  N  NH2   . ARG A 111 ? 1.04341 0.83092 0.84988 0.14622  -0.25186 -0.02614 190 ARG B NH2   
841  N  N     . LEU A 112 ? 1.05523 0.88673 0.99256 0.07786  -0.21987 -0.03536 191 LEU B N     
842  C  CA    . LEU A 112 ? 0.95196 0.79739 0.91259 0.06672  -0.20782 -0.03086 191 LEU B CA    
843  C  C     . LEU A 112 ? 0.94739 0.80027 0.92975 0.05629  -0.20770 -0.03154 191 LEU B C     
844  O  O     . LEU A 112 ? 0.88385 0.74031 0.86497 0.04936  -0.19634 -0.02684 191 LEU B O     
845  C  CB    . LEU A 112 ? 0.95139 0.79733 0.89686 0.06512  -0.19123 -0.02345 191 LEU B CB    
846  C  CG    . LEU A 112 ? 0.92031 0.75769 0.84321 0.07470  -0.19005 -0.02023 191 LEU B CG    
847  C  CD1   . LEU A 112 ? 0.70801 0.54658 0.62104 0.07100  -0.17388 -0.01262 191 LEU B CD1   
848  C  CD2   . LEU A 112 ? 0.89036 0.73037 0.82630 0.07834  -0.19696 -0.02237 191 LEU B CD2   
849  N  N     . ASP A 113 ? 0.94219 0.79775 0.94628 0.05502  -0.22123 -0.03688 192 ASP B N     
850  C  CA    . ASP A 113 ? 0.81003 0.67073 0.83628 0.04567  -0.22427 -0.03703 192 ASP B CA    
851  C  C     . ASP A 113 ? 0.83454 0.71296 0.88359 0.03347  -0.21032 -0.03009 192 ASP B C     
852  O  O     . ASP A 113 ? 1.13051 1.01434 1.19731 0.02474  -0.21047 -0.02760 192 ASP B O     
853  C  CB    . ASP A 113 ? 1.06316 0.92269 1.10986 0.04708  -0.24323 -0.04409 192 ASP B CB    
854  C  CG    . ASP A 113 ? 1.11969 0.98873 1.18326 0.04891  -0.24696 -0.04556 192 ASP B CG    
855  O  OD1   . ASP A 113 ? 1.08889 0.97375 1.17071 0.04191  -0.23536 -0.04054 192 ASP B OD1   
856  O  OD2   . ASP A 113 ? 1.12704 0.98818 1.18561 0.05798  -0.26200 -0.05219 192 ASP B OD2   
857  N  N     . SER A 114 ? 0.78032 0.66785 0.82938 0.03300  -0.19874 -0.02691 193 SER B N     
858  C  CA    . SER A 114 ? 0.84218 0.74716 0.90860 0.02294  -0.18462 -0.02116 193 SER B CA    
859  C  C     . SER A 114 ? 0.93080 0.83426 0.97945 0.01929  -0.17084 -0.01573 193 SER B C     
860  O  O     . SER A 114 ? 0.92769 0.84533 0.98785 0.01110  -0.15930 -0.01093 193 SER B O     
861  C  CB    . SER A 114 ? 0.76944 0.68550 0.84554 0.02479  -0.17916 -0.02188 193 SER B CB    
862  O  OG    . SER A 114 ? 0.92964 0.83588 0.98114 0.03212  -0.17428 -0.02198 193 SER B OG    
863  N  N     . LEU A 115 ? 0.90677 0.79472 0.92800 0.02549  -0.17176 -0.01624 194 LEU B N     
864  C  CA    . LEU A 115 ? 0.97980 0.86666 0.98471 0.02261  -0.15903 -0.01107 194 LEU B CA    
865  C  C     . LEU A 115 ? 0.92907 0.82166 0.94543 0.01342  -0.15629 -0.00712 194 LEU B C     
866  O  O     . LEU A 115 ? 0.84700 0.73353 0.86976 0.01305  -0.16689 -0.00917 194 LEU B O     
867  C  CB    . LEU A 115 ? 0.80339 0.67390 0.77841 0.03177  -0.16116 -0.01203 194 LEU B CB    
868  C  CG    . LEU A 115 ? 0.91337 0.77864 0.87177 0.03952  -0.15828 -0.01167 194 LEU B CG    
869  C  CD1   . LEU A 115 ? 0.82917 0.68059 0.75874 0.04824  -0.15974 -0.01101 194 LEU B CD1   
870  C  CD2   . LEU A 115 ? 0.79091 0.66542 0.75264 0.03416  -0.14409 -0.00723 194 LEU B CD2   
871  N  N     . THR A 116 ? 0.87851 0.78240 0.89761 0.00622  -0.14273 -0.00150 195 THR B N     
872  C  CA    . THR A 116 ? 0.95655 0.86572 0.98261 -0.00215 -0.13845 0.00405  195 THR B CA    
873  C  C     . THR A 116 ? 0.93262 0.83554 0.93675 -0.00151 -0.13023 0.00736  195 THR B C     
874  O  O     . THR A 116 ? 0.88745 0.79037 0.89351 -0.00638 -0.12920 0.01143  195 THR B O     
875  C  CB    . THR A 116 ? 0.83698 0.76698 0.88482 -0.01138 -0.12952 0.00884  195 THR B CB    
876  O  OG1   . THR A 116 ? 0.85006 0.78715 0.88930 -0.01044 -0.11795 0.00885  195 THR B OG1   
877  C  CG2   . THR A 116 ? 0.87501 0.81371 0.94832 -0.01268 -0.13731 0.00656  195 THR B CG2   
878  N  N     . THR A 117 ? 0.89428 0.79187 0.87925 0.00431  -0.12493 0.00627  196 THR B N     
879  C  CA    . THR A 117 ? 0.80679 0.69998 0.77268 0.00493  -0.11666 0.00980  196 THR B CA    
880  C  C     . THR A 117 ? 0.88527 0.76549 0.82959 0.01493  -0.11885 0.00747  196 THR B C     
881  O  O     . THR A 117 ? 0.79816 0.67782 0.74136 0.01884  -0.11923 0.00551  196 THR B O     
882  C  CB    . THR A 117 ? 0.86420 0.77025 0.83334 -0.00145 -0.10382 0.01356  196 THR B CB    
883  O  OG1   . THR A 117 ? 0.99957 0.91749 0.98327 -0.01031 -0.10050 0.01780  196 THR B OG1   
884  C  CG2   . THR A 117 ? 0.93973 0.84032 0.88936 0.00060  -0.09632 0.01623  196 THR B CG2   
885  N  N     . LEU A 118 ? 0.86090 0.73136 0.78854 0.01948  -0.12019 0.00816  197 LEU B N     
886  C  CA    . LEU A 118 ? 0.85949 0.71901 0.76535 0.02967  -0.12191 0.00717  197 LEU B CA    
887  C  C     . LEU A 118 ? 0.91384 0.77087 0.80378 0.03076  -0.11425 0.01161  197 LEU B C     
888  O  O     . LEU A 118 ? 0.90951 0.76321 0.79692 0.03146  -0.11724 0.01084  197 LEU B O     
889  C  CB    . LEU A 118 ? 0.77840 0.62785 0.67957 0.03810  -0.13585 0.00084  197 LEU B CB    
890  C  CG    . LEU A 118 ? 0.79901 0.63831 0.67555 0.05000  -0.13823 0.00006  197 LEU B CG    
891  C  CD1   . LEU A 118 ? 0.79140 0.63194 0.66532 0.05198  -0.13451 0.00273  197 LEU B CD1   
892  C  CD2   . LEU A 118 ? 0.69693 0.52690 0.56822 0.05860  -0.15317 -0.00767 197 LEU B CD2   
893  N  N     . TYR A 119 ? 0.92384 0.78237 0.80466 0.03107  -0.10496 0.01623  198 TYR B N     
894  C  CA    . TYR A 119 ? 0.84437 0.70231 0.71193 0.03189  -0.09691 0.02134  198 TYR B CA    
895  C  C     . TYR A 119 ? 0.88817 0.73785 0.73535 0.04254  -0.09772 0.02281  198 TYR B C     
896  O  O     . TYR A 119 ? 0.77167 0.61994 0.61537 0.04472  -0.09572 0.02529  198 TYR B O     
897  C  CB    . TYR A 119 ? 0.87304 0.73953 0.74678 0.02390  -0.08606 0.02618  198 TYR B CB    
898  C  CG    . TYR A 119 ? 0.85502 0.73187 0.74655 0.01406  -0.08399 0.02547  198 TYR B CG    
899  C  CD1   . TYR A 119 ? 0.82393 0.70269 0.72280 0.01090  -0.08791 0.02470  198 TYR B CD1   
900  C  CD2   . TYR A 119 ? 0.88217 0.76716 0.78318 0.00837  -0.07826 0.02577  198 TYR B CD2   
901  C  CE1   . TYR A 119 ? 0.80430 0.69397 0.71900 0.00192  -0.08533 0.02592  198 TYR B CE1   
902  C  CE2   . TYR A 119 ? 0.71586 0.61233 0.63123 0.00033  -0.07561 0.02543  198 TYR B CE2   
903  C  CZ    . TYR A 119 ? 0.82784 0.72721 0.74976 -0.00307 -0.07872 0.02634  198 TYR B CZ    
904  O  OH    . TYR A 119 ? 1.00268 0.91486 0.93850 -0.01108 -0.07543 0.02779  198 TYR B OH    
905  N  N     . LEU A 120 ? 0.94271 0.78730 0.77647 0.04962  -0.10063 0.02154  199 LEU B N     
906  C  CA    . LEU A 120 ? 0.90716 0.74624 0.71921 0.06068  -0.10007 0.02371  199 LEU B CA    
907  C  C     . LEU A 120 ? 0.98375 0.82620 0.78580 0.06187  -0.09069 0.02940  199 LEU B C     
908  O  O     . LEU A 120 ? 0.99720 0.83672 0.78086 0.07211  -0.09044 0.03027  199 LEU B O     
909  C  CB    . LEU A 120 ? 0.86095 0.69174 0.66317 0.07097  -0.11264 0.01579  199 LEU B CB    
910  C  CG    . LEU A 120 ? 0.85733 0.68519 0.67100 0.07033  -0.12354 0.00971  199 LEU B CG    
911  C  CD1   . LEU A 120 ? 0.85281 0.67240 0.65914 0.07961  -0.13753 0.00057  199 LEU B CD1   
912  C  CD2   . LEU A 120 ? 0.82917 0.65663 0.63910 0.07253  -0.12164 0.01377  199 LEU B CD2   
913  N  N     . ARG A 121 ? 0.95867 0.80835 0.77254 0.05204  -0.08299 0.03325  200 ARG B N     
914  C  CA    . ARG A 121 ? 0.93259 0.78680 0.74088 0.05209  -0.07480 0.03834  200 ARG B CA    
915  C  C     . ARG A 121 ? 0.89705 0.75269 0.69241 0.05699  -0.06680 0.04633  200 ARG B C     
916  O  O     . ARG A 121 ? 0.86371 0.71821 0.65990 0.05587  -0.06528 0.04985  200 ARG B O     
917  C  CB    . ARG A 121 ? 0.95258 0.81477 0.77724 0.03997  -0.06922 0.04089  200 ARG B CB    
918  C  CG    . ARG A 121 ? 1.06507 0.93243 0.88796 0.03899  -0.06297 0.04487  200 ARG B CG    
919  C  CD    . ARG A 121 ? 1.13250 1.00844 0.96984 0.02720  -0.05718 0.04830  200 ARG B CD    
920  N  NE    . ARG A 121 ? 1.08135 0.95880 0.93184 0.02061  -0.06238 0.04419  200 ARG B NE    
921  C  CZ    . ARG A 121 ? 1.03910 0.92174 0.89747 0.01493  -0.06139 0.04561  200 ARG B CZ    
922  N  NH1   . ARG A 121 ? 1.19441 1.08131 1.04972 0.01480  -0.05577 0.05010  200 ARG B NH1   
923  N  NH2   . ARG A 121 ? 1.13328 1.01768 1.00378 0.00919  -0.06614 0.04328  200 ARG B NH2   
924  N  N     . PHE A 122 ? 0.96647 0.82497 0.75089 0.06270  -0.06171 0.04970  201 PHE B N     
925  C  CA    . PHE A 122 ? 0.95095 0.81331 0.72436 0.06718  -0.05277 0.05918  201 PHE B CA    
926  C  C     . PHE A 122 ? 0.99672 0.85344 0.75722 0.07518  -0.05591 0.06094  201 PHE B C     
927  O  O     . PHE A 122 ? 0.93637 0.79270 0.70104 0.07141  -0.05282 0.06726  201 PHE B O     
928  C  CB    . PHE A 122 ? 0.90931 0.77855 0.69645 0.05619  -0.04378 0.06714  201 PHE B CB    
929  C  CG    . PHE A 122 ? 1.00858 0.88537 0.80382 0.05077  -0.03887 0.06828  201 PHE B CG    
930  C  CD1   . PHE A 122 ? 0.98440 0.86737 0.77180 0.05624  -0.03212 0.07371  201 PHE B CD1   
931  C  CD2   . PHE A 122 ? 0.97197 0.85089 0.78272 0.04064  -0.04082 0.06445  201 PHE B CD2   
932  C  CE1   . PHE A 122 ? 0.97311 0.86329 0.76900 0.05160  -0.02826 0.07481  201 PHE B CE1   
933  C  CE2   . PHE A 122 ? 0.98571 0.87162 0.80337 0.03596  -0.03703 0.06607  201 PHE B CE2   
934  C  CZ    . PHE A 122 ? 1.03123 0.92231 0.84196 0.04139  -0.03114 0.07106  201 PHE B CZ    
935  N  N     . ASN A 123 ? 1.01236 0.86417 0.75697 0.08685  -0.06302 0.05483  202 ASN B N     
936  C  CA    . ASN A 123 ? 1.01303 0.86049 0.74057 0.09712  -0.06624 0.05677  202 ASN B CA    
937  C  C     . ASN A 123 ? 0.97978 0.82843 0.68498 0.11144  -0.06651 0.05463  202 ASN B C     
938  O  O     . ASN A 123 ? 1.12859 0.98122 0.83356 0.11290  -0.06378 0.05190  202 ASN B O     
939  C  CB    . ASN A 123 ? 1.08575 0.92469 0.81777 0.09721  -0.07868 0.04840  202 ASN B CB    
940  C  CG    . ASN A 123 ? 1.00235 0.84090 0.75124 0.08694  -0.07722 0.05233  202 ASN B CG    
941  O  OD1   . ASN A 123 ? 0.94486 0.78186 0.68874 0.08915  -0.07501 0.05969  202 ASN B OD1   
942  N  ND2   . ASN A 123 ? 0.91320 0.75334 0.68215 0.07620  -0.07863 0.04751  202 ASN B ND2   
943  N  N     . ARG A 124 ? 1.04393 0.88952 0.72972 0.12287  -0.07007 0.05564  203 ARG B N     
944  C  CA    . ARG A 124 ? 1.14072 0.98800 0.80187 0.13866  -0.07095 0.05263  203 ARG B CA    
945  C  C     . ARG A 124 ? 1.11021 0.94751 0.76184 0.14777  -0.08699 0.03819  203 ARG B C     
946  O  O     . ARG A 124 ? 1.19728 1.03344 0.82521 0.16213  -0.09101 0.03604  203 ARG B O     
947  C  CB    . ARG A 124 ? 1.13255 0.98624 0.77551 0.14647  -0.06182 0.06613  203 ARG B CB    
948  C  CG    . ARG A 124 ? 1.26720 1.13089 0.92140 0.13740  -0.04657 0.08130  203 ARG B CG    
949  C  CD    . ARG A 124 ? 1.40810 1.26851 1.07559 0.12732  -0.04501 0.09078  203 ARG B CD    
950  N  NE    . ARG A 124 ? 1.37687 1.24194 1.03110 0.13316  -0.03742 0.10595  203 ARG B NE    
951  C  CZ    . ARG A 124 ? 1.43776 1.31111 1.10044 0.12695  -0.02500 0.12091  203 ARG B CZ    
952  N  NH1   . ARG A 124 ? 1.32842 1.20625 1.01200 0.11500  -0.01914 0.12193  203 ARG B NH1   
953  N  NH2   . ARG A 124 ? 1.51101 1.38850 1.16151 0.13277  -0.01876 0.13574  203 ARG B NH2   
954  N  N     . ILE A 125 ? 1.11985 0.95050 0.79040 0.13950  -0.09661 0.02839  204 ILE B N     
955  C  CA    . ILE A 125 ? 1.21642 1.03731 0.88340 0.14601  -0.11314 0.01490  204 ILE B CA    
956  C  C     . ILE A 125 ? 1.24229 1.06085 0.89540 0.15795  -0.11879 0.00421  204 ILE B C     
957  O  O     . ILE A 125 ? 1.23039 1.05232 0.89021 0.15520  -0.11357 0.00348  204 ILE B O     
958  C  CB    . ILE A 125 ? 1.18634 1.00275 0.88093 0.13252  -0.12063 0.00948  204 ILE B CB    
959  C  CG1   . ILE A 125 ? 0.98623 0.80526 0.69369 0.12237  -0.11520 0.01862  204 ILE B CG1   
960  C  CG2   . ILE A 125 ? 1.17402 0.98085 0.86858 0.13838  -0.13851 -0.00418 204 ILE B CG2   
961  C  CD1   . ILE A 125 ? 1.04594 0.86371 0.78024 0.10955  -0.12034 0.01429  204 ILE B CD1   
962  N  N     . THR A 126 ? 1.26030 1.07283 0.89384 0.17200  -0.13031 -0.00478 205 THR B N     
963  C  CA    . THR A 126 ? 1.29648 1.10551 0.91466 0.18567  -0.13776 -0.01724 205 THR B CA    
964  C  C     . THR A 126 ? 1.21612 1.01250 0.84155 0.18794  -0.15793 -0.03371 205 THR B C     
965  O  O     . THR A 126 ? 1.20463 0.99588 0.82395 0.19691  -0.16601 -0.04588 205 THR B O     
966  C  CB    . THR A 126 ? 1.22934 1.04350 0.81333 0.20380  -0.13409 -0.01507 205 THR B CB    
967  O  OG1   . THR A 126 ? 1.41470 1.22402 0.98745 0.20927  -0.14352 -0.01616 205 THR B OG1   
968  C  CG2   . THR A 126 ? 1.27030 1.09806 0.84879 0.20160  -0.11396 0.00253  205 THR B CG2   
969  N  N     . THR A 127 ? 1.26296 1.05432 0.90275 0.18029  -0.16671 -0.03469 206 THR B N     
970  C  CA    . THR A 127 ? 1.23621 1.01646 0.88316 0.18306  -0.18679 -0.04957 206 THR B CA    
971  C  C     . THR A 127 ? 1.23743 1.01594 0.91797 0.16578  -0.19082 -0.04826 206 THR B C     
972  O  O     . THR A 127 ? 1.26826 1.05215 0.95785 0.15684  -0.18317 -0.03800 206 THR B O     
973  C  CB    . THR A 127 ? 1.33259 1.10933 0.95645 0.19684  -0.19704 -0.05414 206 THR B CB    
974  O  OG1   . THR A 127 ? 1.50919 1.29014 1.09979 0.21354  -0.19140 -0.05379 206 THR B OG1   
975  C  CG2   . THR A 127 ? 1.30476 1.06983 0.93634 0.20061  -0.21949 -0.07100 206 THR B CG2   
976  N  N     . VAL A 128 ? 1.11477 0.88615 0.81420 0.16151  -0.20285 -0.05848 207 VAL B N     
977  C  CA    . VAL A 128 ? 1.01359 0.78358 0.74460 0.14723  -0.20975 -0.05898 207 VAL B CA    
978  C  C     . VAL A 128 ? 1.19752 0.95760 0.92947 0.15459  -0.23102 -0.07264 207 VAL B C     
979  O  O     . VAL A 128 ? 1.30820 1.05938 1.04181 0.15992  -0.24381 -0.08456 207 VAL B O     
980  C  CB    . VAL A 128 ? 1.14656 0.91734 0.90223 0.13479  -0.20669 -0.05757 207 VAL B CB    
981  C  CG1   . VAL A 128 ? 1.00329 0.77458 0.79129 0.12076  -0.21364 -0.05734 207 VAL B CG1   
982  C  CG2   . VAL A 128 ? 1.16883 0.94975 0.92256 0.12827  -0.18669 -0.04471 207 VAL B CG2   
983  N  N     . GLU A 129 ? 1.16795 0.92910 0.89964 0.15524  -0.23576 -0.07135 208 GLU B N     
984  C  CA    . GLU A 129 ? 1.10780 0.86046 0.83841 0.16338  -0.25647 -0.08406 208 GLU B CA    
985  C  C     . GLU A 129 ? 1.13343 0.88152 0.89873 0.15251  -0.26974 -0.09110 208 GLU B C     
986  O  O     . GLU A 129 ? 1.16059 0.91436 0.95223 0.13725  -0.26175 -0.08368 208 GLU B O     
987  C  CB    . GLU A 129 ? 1.08554 0.84148 0.80989 0.16590  -0.25778 -0.07944 208 GLU B CB    
988  C  CG    . GLU A 129 ? 1.18671 0.94626 0.87648 0.17776  -0.24718 -0.07190 208 GLU B CG    
989  C  CD    . GLU A 129 ? 1.39274 1.14603 1.05033 0.19701  -0.25731 -0.08272 208 GLU B CD    
990  O  OE1   . GLU A 129 ? 1.41028 1.15466 1.07266 0.20185  -0.27555 -0.09786 208 GLU B OE1   
991  O  OE2   . GLU A 129 ? 1.42514 1.18289 1.05295 0.20754  -0.24717 -0.07606 208 GLU B OE2   
992  N  N     . LYS A 130 ? 1.19819 0.93632 0.96340 0.16078  -0.29074 -0.10542 209 LYS B N     
993  C  CA    . LYS A 130 ? 1.08997 0.82322 0.88987 0.15094  -0.30564 -0.11215 209 LYS B CA    
994  C  C     . LYS A 130 ? 1.08967 0.83181 0.91845 0.13729  -0.30411 -0.10441 209 LYS B C     
995  O  O     . LYS A 130 ? 1.18281 0.92596 1.04545 0.12483  -0.30978 -0.10441 209 LYS B O     
996  C  CB    . LYS A 130 ? 1.10425 0.82462 0.89753 0.16358  -0.32999 -0.12991 209 LYS B CB    
997  C  CG    . LYS A 130 ? 1.30582 1.01633 1.07753 0.17641  -0.33461 -0.14063 209 LYS B CG    
998  C  CD    . LYS A 130 ? 1.18315 0.87962 0.95713 0.18608  -0.36131 -0.15985 209 LYS B CD    
999  C  CE    . LYS A 130 ? 1.52678 1.21268 1.28688 0.19681  -0.36653 -0.17143 209 LYS B CE    
1000 N  NZ    . LYS A 130 ? 1.50602 1.19321 1.28847 0.18357  -0.35518 -0.16310 209 LYS B NZ    
1001 N  N     . ASP A 131 ? 1.08150 0.83060 0.89852 0.13961  -0.29650 -0.09740 210 ASP B N     
1002 C  CA    . ASP A 131 ? 1.15034 0.90898 0.99336 0.12803  -0.29350 -0.09018 210 ASP B CA    
1003 C  C     . ASP A 131 ? 1.08033 0.84941 0.94468 0.11207  -0.27599 -0.07834 210 ASP B C     
1004 O  O     . ASP A 131 ? 1.13400 0.91259 1.02154 0.10213  -0.27230 -0.07263 210 ASP B O     
1005 C  CB    . ASP A 131 ? 1.29850 1.06062 1.12164 0.13569  -0.28927 -0.08533 210 ASP B CB    
1006 C  CG    . ASP A 131 ? 1.34738 1.10142 1.15483 0.15000  -0.30868 -0.09641 210 ASP B CG    
1007 O  OD1   . ASP A 131 ? 1.30488 1.05695 1.13535 0.14739  -0.32558 -0.10444 210 ASP B OD1   
1008 O  OD2   . ASP A 131 ? 1.49125 1.24173 1.26357 0.16399  -0.30717 -0.09677 210 ASP B OD2   
1009 N  N     . ILE A 132 ? 1.08679 0.85515 0.94356 0.11008  -0.26534 -0.07483 211 ILE B N     
1010 C  CA    . ILE A 132 ? 1.06665 0.84481 0.94290 0.09536  -0.25013 -0.06423 211 ILE B CA    
1011 C  C     . ILE A 132 ? 1.14023 0.92204 1.05420 0.08269  -0.25803 -0.06484 211 ILE B C     
1012 O  O     . ILE A 132 ? 1.07574 0.86922 1.00974 0.07002  -0.24668 -0.05560 211 ILE B O     
1013 C  CB    . ILE A 132 ? 1.01966 0.79509 0.88132 0.09693  -0.24054 -0.06188 211 ILE B CB    
1014 C  CG1   . ILE A 132 ? 0.91637 0.70313 0.79135 0.08341  -0.22270 -0.04964 211 ILE B CG1   
1015 C  CG2   . ILE A 132 ? 0.99121 0.75566 0.85965 0.09962  -0.25499 -0.07182 211 ILE B CG2   
1016 C  CD1   . ILE A 132 ? 0.75530 0.55081 0.61934 0.08247  -0.20760 -0.04062 211 ILE B CD1   
1017 N  N     . LYS A 133 ? 1.07467 0.84740 0.99930 0.08607  -0.27768 -0.07548 212 LYS B N     
1018 C  CA    . LYS A 133 ? 1.09460 0.87114 1.05774 0.07397  -0.28660 -0.07534 212 LYS B CA    
1019 C  C     . LYS A 133 ? 1.04576 0.83617 1.02933 0.06639  -0.28272 -0.06952 212 LYS B C     
1020 O  O     . LYS A 133 ? 1.01596 0.81591 1.03247 0.05360  -0.28209 -0.06436 212 LYS B O     
1021 C  CB    . LYS A 133 ? 1.15824 0.92127 1.12807 0.08051  -0.31055 -0.08906 212 LYS B CB    
1022 C  CG    . LYS A 133 ? 1.18316 0.94157 1.13755 0.09305  -0.32351 -0.09840 212 LYS B CG    
1023 C  CD    . LYS A 133 ? 1.18863 0.93332 1.15003 0.09966  -0.34863 -0.11334 212 LYS B CD    
1024 C  CE    . LYS A 133 ? 1.31340 1.05396 1.25682 0.11311  -0.36209 -0.12277 212 LYS B CE    
1025 N  NZ    . LYS A 133 ? 1.35581 1.08207 1.30306 0.12109  -0.38793 -0.13921 212 LYS B NZ    
1026 N  N     . ASN A 134 ? 1.02054 0.81288 0.98593 0.07431  -0.27997 -0.06976 213 ASN B N     
1027 C  CA    . ASN A 134 ? 1.01909 0.82436 1.00319 0.06851  -0.27612 -0.06493 213 ASN B CA    
1028 C  C     . ASN A 134 ? 1.00457 0.82413 0.99943 0.05689  -0.25580 -0.05308 213 ASN B C     
1029 O  O     . ASN A 134 ? 1.03303 0.86580 1.05280 0.04900  -0.25264 -0.04914 213 ASN B O     
1030 C  CB    . ASN A 134 ? 1.02741 0.82966 0.98789 0.08059  -0.27824 -0.06740 213 ASN B CB    
1031 C  CG    . ASN A 134 ? 1.26871 1.05878 1.21904 0.09270  -0.29971 -0.07963 213 ASN B CG    
1032 O  OD1   . ASN A 134 ? 1.31918 1.10728 1.29320 0.08967  -0.31563 -0.08653 213 ASN B OD1   
1033 N  ND2   . ASN A 134 ? 1.38891 1.17124 1.30424 0.10657  -0.30055 -0.08208 213 ASN B ND2   
1034 N  N     . LEU A 135 ? 1.13255 0.95065 1.10952 0.05620  -0.24233 -0.04784 214 LEU B N     
1035 C  CA    . LEU A 135 ? 1.10918 0.94029 1.09420 0.04578  -0.22384 -0.03747 214 LEU B CA    
1036 C  C     . LEU A 135 ? 1.09426 0.93046 1.10248 0.03411  -0.22238 -0.03330 214 LEU B C     
1037 O  O     . LEU A 135 ? 1.04962 0.88787 1.05156 0.02969  -0.21084 -0.02724 214 LEU B O     
1038 C  CB    . LEU A 135 ? 1.00661 0.83447 0.96159 0.05085  -0.21033 -0.03327 214 LEU B CB    
1039 C  CG    . LEU A 135 ? 0.91802 0.73898 0.84671 0.06335  -0.21197 -0.03579 214 LEU B CG    
1040 C  CD1   . LEU A 135 ? 0.72323 0.54288 0.62655 0.06653  -0.19750 -0.02960 214 LEU B CD1   
1041 C  CD2   . LEU A 135 ? 0.79599 0.62429 0.73686 0.06260  -0.21274 -0.03506 214 LEU B CD2   
1042 N  N     . SER A 136 ? 1.10738 0.94612 1.14409 0.02881  -0.23457 -0.03577 215 SER B N     
1043 C  CA    . SER A 136 ? 1.08617 0.92810 1.14704 0.01801  -0.23599 -0.03120 215 SER B CA    
1044 C  C     . SER A 136 ? 1.04102 0.90226 1.12045 0.00544  -0.22006 -0.01965 215 SER B C     
1045 O  O     . SER A 136 ? 1.16511 1.03032 1.26105 -0.00384 -0.21802 -0.01313 215 SER B O     
1046 C  CB    . SER A 136 ? 1.02981 0.86791 1.11722 0.01628  -0.25542 -0.03715 215 SER B CB    
1047 O  OG    . SER A 136 ? 1.27256 1.12249 1.37816 0.01447  -0.25763 -0.03734 215 SER B OG    
1048 N  N     . LYS A 137 ? 0.83842 0.71170 0.91557 0.00538  -0.20924 -0.01704 216 LYS B N     
1049 C  CA    . LYS A 137 ? 0.87851 0.77052 0.96848 -0.00464 -0.19324 -0.00746 216 LYS B CA    
1050 C  C     . LYS A 137 ? 0.97167 0.86286 1.03859 -0.00487 -0.17862 -0.00258 216 LYS B C     
1051 O  O     . LYS A 137 ? 0.81182 0.71793 0.88440 -0.01178 -0.16494 0.00438  216 LYS B O     
1052 C  CB    . LYS A 137 ? 0.81067 0.71618 0.90989 -0.00393 -0.18868 -0.00814 216 LYS B CB    
1053 C  CG    . LYS A 137 ? 1.09621 1.00663 1.22332 -0.00505 -0.20209 -0.01174 216 LYS B CG    
1054 C  CD    . LYS A 137 ? 1.10352 1.02608 1.23774 -0.00222 -0.19821 -0.01352 216 LYS B CD    
1055 C  CE    . LYS A 137 ? 0.98061 0.90564 1.13962 -0.00106 -0.21384 -0.01855 216 LYS B CE    
1056 N  NZ    . LYS A 137 ? 1.12849 1.06211 1.29097 0.00437  -0.21209 -0.02175 216 LYS B NZ    
1057 N  N     . LEU A 138 ? 0.90026 0.77541 0.94182 0.00289  -0.18142 -0.00632 217 LEU B N     
1058 C  CA    . LEU A 138 ? 0.87262 0.74723 0.89347 0.00303  -0.16828 -0.00174 217 LEU B CA    
1059 C  C     . LEU A 138 ? 0.95301 0.83329 0.98555 -0.00660 -0.16331 0.00594  217 LEU B C     
1060 O  O     . LEU A 138 ? 1.07356 0.94812 1.11961 -0.00932 -0.17335 0.00577  217 LEU B O     
1061 C  CB    . LEU A 138 ? 0.81731 0.67507 0.80963 0.01440  -0.17257 -0.00725 217 LEU B CB    
1062 C  CG    . LEU A 138 ? 0.84864 0.70178 0.82058 0.02431  -0.17179 -0.01118 217 LEU B CG    
1063 C  CD1   . LEU A 138 ? 0.83503 0.67355 0.77974 0.03545  -0.17586 -0.01543 217 LEU B CD1   
1064 C  CD2   . LEU A 138 ? 0.86130 0.72475 0.82844 0.02092  -0.15628 -0.00530 217 LEU B CD2   
1065 N  N     . SER A 139 ? 0.90703 0.79829 0.93483 -0.01167 -0.14847 0.01275  218 SER B N     
1066 C  CA    . SER A 139 ? 0.93731 0.83340 0.97000 -0.01939 -0.14248 0.02075  218 SER B CA    
1067 C  C     . SER A 139 ? 0.83231 0.72155 0.84045 -0.01530 -0.13534 0.02172  218 SER B C     
1068 O  O     . SER A 139 ? 0.85030 0.73974 0.85979 -0.01964 -0.13291 0.02728  218 SER B O     
1069 C  CB    . SER A 139 ? 0.75980 0.67695 0.80868 -0.02923 -0.13129 0.02862  218 SER B CB    
1070 O  OG    . SER A 139 ? 0.91219 0.83645 0.94829 -0.02681 -0.12050 0.02726  218 SER B OG    
1071 N  N     . MET A 140 ? 0.82852 0.71216 0.81572 -0.00716 -0.13218 0.01725  219 MET B N     
1072 C  CA    . MET A 140 ? 0.85115 0.72978 0.81630 -0.00303 -0.12490 0.01865  219 MET B CA    
1073 C  C     . MET A 140 ? 0.88413 0.74968 0.82930 0.00886  -0.13022 0.01195  219 MET B C     
1074 O  O     . MET A 140 ? 0.82200 0.68826 0.76230 0.01257  -0.12927 0.00953  219 MET B O     
1075 C  CB    . MET A 140 ? 0.86769 0.75863 0.82931 -0.00771 -0.11100 0.02346  219 MET B CB    
1076 C  CG    . MET A 140 ? 0.97409 0.86037 0.91425 -0.00297 -0.10381 0.02450  219 MET B CG    
1077 S  SD    . MET A 140 ? 1.11571 1.00137 1.05159 -0.00582 -0.10035 0.03003  219 MET B SD    
1078 C  CE    . MET A 140 ? 0.93058 0.81427 0.84473 -0.00047 -0.09099 0.03127  219 MET B CE    
1079 N  N     . LEU A 141 ? 0.83408 0.68815 0.76758 0.01539  -0.13587 0.00910  220 LEU B N     
1080 C  CA    . LEU A 141 ? 0.91391 0.75700 0.82514 0.02780  -0.13974 0.00350  220 LEU B CA    
1081 C  C     . LEU A 141 ? 0.89545 0.73724 0.78905 0.03130  -0.13105 0.00698  220 LEU B C     
1082 O  O     . LEU A 141 ? 0.92067 0.75878 0.81500 0.03152  -0.13329 0.00698  220 LEU B O     
1083 C  CB    . LEU A 141 ? 0.92061 0.75170 0.83290 0.03480  -0.15572 -0.00509 220 LEU B CB    
1084 C  CG    . LEU A 141 ? 1.01033 0.83102 0.89806 0.04908  -0.16106 -0.01178 220 LEU B CG    
1085 C  CD1   . LEU A 141 ? 0.92903 0.75327 0.80888 0.05181  -0.15694 -0.01045 220 LEU B CD1   
1086 C  CD2   . LEU A 141 ? 0.81970 0.62889 0.71042 0.05569  -0.17866 -0.02189 220 LEU B CD2   
1087 N  N     . SER A 142 ? 0.92879 0.77375 0.80841 0.03392  -0.12150 0.01031  221 SER B N     
1088 C  CA    . SER A 142 ? 0.89786 0.74397 0.76288 0.03656  -0.11209 0.01482  221 SER B CA    
1089 C  C     . SER A 142 ? 0.88707 0.72679 0.72986 0.04873  -0.11232 0.01294  221 SER B C     
1090 O  O     . SER A 142 ? 0.87798 0.71942 0.71509 0.04996  -0.10810 0.01551  221 SER B O     
1091 C  CB    . SER A 142 ? 0.90381 0.76097 0.77427 0.02757  -0.09977 0.02210  221 SER B CB    
1092 O  OG    . SER A 142 ? 1.03871 0.89735 0.89634 0.03026  -0.09125 0.02665  221 SER B OG    
1093 N  N     . ILE A 143 ? 0.86088 0.69350 0.69107 0.05819  -0.11726 0.00870  222 ILE B N     
1094 C  CA    . ILE A 143 ? 0.93728 0.76614 0.74396 0.07075  -0.11588 0.00797  222 ILE B CA    
1095 C  C     . ILE A 143 ? 0.92799 0.76087 0.72507 0.07352  -0.10651 0.01257  222 ILE B C     
1096 O  O     . ILE A 143 ? 0.96668 0.79617 0.74618 0.08540  -0.10769 0.00958  222 ILE B O     
1097 C  CB    . ILE A 143 ? 0.92134 0.73970 0.71843 0.08216  -0.12998 -0.00230 222 ILE B CB    
1098 C  CG1   . ILE A 143 ? 1.03456 0.84721 0.84216 0.08149  -0.13925 -0.00897 222 ILE B CG1   
1099 C  CG2   . ILE A 143 ? 0.95228 0.76804 0.75595 0.08116  -0.13820 -0.00562 222 ILE B CG2   
1100 C  CD1   . ILE A 143 ? 1.15660 0.95793 0.95909 0.09142  -0.15559 -0.02075 222 ILE B CD1   
1101 N  N     . ARG A 144 ? 0.97854 0.81966 0.78718 0.06308  -0.09729 0.01956  223 ARG B N     
1102 C  CA    . ARG A 144 ? 0.96047 0.80701 0.76375 0.06426  -0.08840 0.02458  223 ARG B CA    
1103 C  C     . ARG A 144 ? 0.94243 0.79268 0.72878 0.07127  -0.07953 0.03028  223 ARG B C     
1104 O  O     . ARG A 144 ? 0.97563 0.82669 0.75987 0.06986  -0.07684 0.03388  223 ARG B O     
1105 C  CB    . ARG A 144 ? 0.96032 0.81543 0.78024 0.05100  -0.08152 0.03080  223 ARG B CB    
1106 C  CG    . ARG A 144 ? 1.04415 0.90512 0.86293 0.05095  -0.07437 0.03543  223 ARG B CG    
1107 C  CD    . ARG A 144 ? 1.01334 0.88403 0.84525 0.03844  -0.06670 0.04231  223 ARG B CD    
1108 N  NE    . ARG A 144 ? 0.93484 0.81044 0.77116 0.03642  -0.06355 0.04550  223 ARG B NE    
1109 C  CZ    . ARG A 144 ? 0.99226 0.86694 0.83980 0.03172  -0.06868 0.04441  223 ARG B CZ    
1110 N  NH1   . ARG A 144 ? 1.06800 0.93778 0.92467 0.02799  -0.07681 0.04061  223 ARG B NH1   
1111 N  NH2   . ARG A 144 ? 1.14494 1.02419 0.99585 0.03063  -0.06576 0.04804  223 ARG B NH2   
1112 N  N     . GLU A 145 ? 0.88654 0.73945 0.66179 0.07914  -0.07501 0.03160  224 GLU B N     
1113 C  CA    . GLU A 145 ? 0.97778 0.83686 0.73834 0.08573  -0.06506 0.03895  224 GLU B CA    
1114 C  C     . GLU A 145 ? 1.00375 0.85764 0.74731 0.09569  -0.06895 0.03721  224 GLU B C     
1115 O  O     . GLU A 145 ? 0.91794 0.77323 0.66046 0.09296  -0.06498 0.04366  224 GLU B O     
1116 C  CB    . GLU A 145 ? 1.03678 0.90464 0.80826 0.07451  -0.05428 0.04943  224 GLU B CB    
1117 C  CG    . GLU A 145 ? 1.06296 0.93783 0.84802 0.06627  -0.04956 0.05224  224 GLU B CG    
1118 C  CD    . GLU A 145 ? 1.13496 1.01786 0.91269 0.07273  -0.04124 0.05738  224 GLU B CD    
1119 O  OE1   . GLU A 145 ? 1.08567 0.96998 0.84751 0.08322  -0.03772 0.05977  224 GLU B OE1   
1120 O  OE2   . GLU A 145 ? 1.22937 1.11822 1.01732 0.06763  -0.03807 0.05948  224 GLU B OE2   
1121 N  N     . ASN A 146 ? 0.95370 0.80107 0.68393 0.10787  -0.07770 0.02798  225 ASN B N     
1122 C  CA    . ASN A 146 ? 0.92127 0.76390 0.63203 0.11972  -0.08286 0.02500  225 ASN B CA    
1123 C  C     . ASN A 146 ? 1.10055 0.94293 0.79117 0.13576  -0.08472 0.01877  225 ASN B C     
1124 O  O     . ASN A 146 ? 1.19716 1.04445 0.88943 0.13737  -0.07969 0.01887  225 ASN B O     
1125 C  CB    . ASN A 146 ? 1.10291 0.93553 0.82091 0.11733  -0.09664 0.01648  225 ASN B CB    
1126 C  CG    . ASN A 146 ? 1.07234 0.90657 0.80481 0.10539  -0.09386 0.02287  225 ASN B CG    
1127 O  OD1   . ASN A 146 ? 1.01528 0.84927 0.73896 0.10854  -0.09236 0.02760  225 ASN B OD1   
1128 N  ND2   . ASN A 146 ? 1.02703 0.86312 0.78153 0.09223  -0.09335 0.02304  225 ASN B ND2   
1129 N  N     . LYS A 147 ? 1.14910 0.98611 0.82027 0.14847  -0.09244 0.01276  226 LYS B N     
1130 C  CA    . LYS A 147 ? 1.28084 1.11765 0.92923 0.16609  -0.09530 0.00513  226 LYS B CA    
1131 C  C     . LYS A 147 ? 1.25846 1.08185 0.90371 0.17333  -0.11391 -0.01142 226 LYS B C     
1132 O  O     . LYS A 147 ? 1.23570 1.05609 0.85796 0.18885  -0.12053 -0.01882 226 LYS B O     
1133 C  CB    . LYS A 147 ? 1.25104 1.09568 0.87462 0.17730  -0.08690 0.01362  226 LYS B CB    
1134 C  CG    . LYS A 147 ? 1.18551 1.04385 0.81302 0.17099  -0.06880 0.03059  226 LYS B CG    
1135 C  CD    . LYS A 147 ? 1.35212 1.21785 0.95696 0.18107  -0.06118 0.04095  226 LYS B CD    
1136 C  CE    . LYS A 147 ? 1.46394 1.33209 1.04018 0.20167  -0.06396 0.03287  226 LYS B CE    
1137 N  NZ    . LYS A 147 ? 1.17946 1.05425 0.73126 0.21238  -0.05844 0.04278  226 LYS B NZ    
1138 N  N     . ILE A 148 ? 1.21398 1.02969 0.88283 0.16214  -0.12287 -0.01715 227 ILE B N     
1139 C  CA    . ILE A 148 ? 1.24977 1.05240 0.92177 0.16630  -0.14157 -0.03194 227 ILE B CA    
1140 C  C     . ILE A 148 ? 1.19276 0.99035 0.86004 0.17648  -0.14793 -0.04331 227 ILE B C     
1141 O  O     . ILE A 148 ? 1.22844 1.02887 0.90874 0.17066  -0.14233 -0.04061 227 ILE B O     
1142 C  CB    . ILE A 148 ? 1.24088 1.03901 0.94243 0.14942  -0.14782 -0.03153 227 ILE B CB    
1143 C  CG1   . ILE A 148 ? 1.19343 0.99557 0.89829 0.14195  -0.14341 -0.02281 227 ILE B CG1   
1144 C  CG2   . ILE A 148 ? 1.12033 0.90541 0.83025 0.15230  -0.16739 -0.04610 227 ILE B CG2   
1145 C  CD1   . ILE A 148 ? 1.09158 0.89447 0.82524 0.12472  -0.14403 -0.01934 227 ILE B CD1   
1146 N  N     . LYS A 149 ? 1.27398 1.06383 0.92251 0.19235  -0.16041 -0.05660 228 LYS B N     
1147 C  CA    . LYS A 149 ? 1.19279 0.97640 0.83506 0.20450  -0.16831 -0.06981 228 LYS B CA    
1148 C  C     . LYS A 149 ? 1.19190 0.95921 0.85095 0.20268  -0.18927 -0.08440 228 LYS B C     
1149 O  O     . LYS A 149 ? 1.18962 0.94945 0.85028 0.21005  -0.19733 -0.09544 228 LYS B O     
1150 C  CB    . LYS A 149 ? 1.14179 0.92914 0.74882 0.22629  -0.16740 -0.07601 228 LYS B CB    
1151 C  CG    . LYS A 149 ? 1.43069 1.23504 1.02321 0.23059  -0.14651 -0.06295 228 LYS B CG    
1152 C  CD    . LYS A 149 ? 1.55940 1.36833 1.11948 0.25371  -0.14596 -0.07130 228 LYS B CD    
1153 C  CE    . LYS A 149 ? 1.64414 1.46925 1.19878 0.25761  -0.12711 -0.06158 228 LYS B CE    
1154 N  NZ    . LYS A 149 ? 1.42143 1.24367 1.00031 0.24965  -0.12710 -0.06397 228 LYS B NZ    
1155 N  N     . GLN A 150 ? 1.20780 0.96961 0.88113 0.19311  -0.19853 -0.08459 229 GLN B N     
1156 C  CA    . GLN A 150 ? 1.23416 0.98147 0.92684 0.19016  -0.21869 -0.09714 229 GLN B CA    
1157 C  C     . GLN A 150 ? 1.13420 0.88184 0.85135 0.17335  -0.22154 -0.09041 229 GLN B C     
1158 O  O     . GLN A 150 ? 1.17227 0.92713 0.88230 0.17095  -0.21461 -0.08246 229 GLN B O     
1159 C  CB    . GLN A 150 ? 1.18398 0.92097 0.85572 0.20860  -0.23602 -0.11470 229 GLN B CB    
1160 C  CG    . GLN A 150 ? 1.32553 1.04614 1.01847 0.20686  -0.25844 -0.12925 229 GLN B CG    
1161 C  CD    . GLN A 150 ? 1.60191 1.31267 1.27696 0.22248  -0.27744 -0.14608 229 GLN B CD    
1162 O  OE1   . GLN A 150 ? 1.63343 1.34989 1.28609 0.22993  -0.27498 -0.14424 229 GLN B OE1   
1163 N  NE2   . GLN A 150 ? 1.53726 1.23270 1.22244 0.22772  -0.29737 -0.16259 229 GLN B NE2   
1164 N  N     . LEU A 151 ? 1.13661 0.87686 0.88341 0.16205  -0.23169 -0.09321 230 LEU B N     
1165 C  CA    . LEU A 151 ? 1.10167 0.84199 0.87417 0.14755  -0.23732 -0.08932 230 LEU B CA    
1166 C  C     . LEU A 151 ? 1.27927 1.00621 1.05967 0.15255  -0.26047 -0.10418 230 LEU B C     
1167 O  O     . LEU A 151 ? 1.37239 1.08767 1.15499 0.15946  -0.27331 -0.11593 230 LEU B O     
1168 C  CB    . LEU A 151 ? 1.13310 0.87726 0.93622 0.12966  -0.23135 -0.07946 230 LEU B CB    
1169 C  CG    . LEU A 151 ? 1.21133 0.96943 1.01290 0.12125  -0.20985 -0.06421 230 LEU B CG    
1170 C  CD1   . LEU A 151 ? 1.05589 0.81719 0.88735 0.10450  -0.20690 -0.05593 230 LEU B CD1   
1171 C  CD2   . LEU A 151 ? 1.07483 0.84251 0.86756 0.11886  -0.20017 -0.05642 230 LEU B CD2   
1172 N  N     . PRO A 152 ? 1.27599 1.00395 1.06200 0.14953  -0.26713 -0.10454 231 PRO B N     
1173 C  CA    . PRO A 152 ? 1.15586 0.87177 0.95279 0.15318  -0.29031 -0.11852 231 PRO B CA    
1174 C  C     . PRO A 152 ? 1.21333 0.92414 1.04911 0.13855  -0.29937 -0.11806 231 PRO B C     
1175 O  O     . PRO A 152 ? 1.26920 0.98813 1.12468 0.12384  -0.28712 -0.10515 231 PRO B O     
1176 C  CB    . PRO A 152 ? 1.25146 0.97321 1.04626 0.15198  -0.29158 -0.11557 231 PRO B CB    
1177 C  CG    . PRO A 152 ? 1.09470 0.83084 0.89532 0.13961  -0.27031 -0.09820 231 PRO B CG    
1178 C  CD    . PRO A 152 ? 1.16380 0.90374 0.94783 0.14289  -0.25460 -0.09254 231 PRO B CD    
1179 N  N     . ALA A 153 ? 1.20608 0.90332 1.05300 0.14297  -0.32184 -0.13226 232 ALA B N     
1180 C  CA    . ALA A 153 ? 1.18714 0.87883 1.07370 0.12898  -0.33271 -0.13144 232 ALA B CA    
1181 C  C     . ALA A 153 ? 1.24451 0.94798 1.15898 0.11215  -0.32840 -0.11959 232 ALA B C     
1182 O  O     . ALA A 153 ? 1.21616 0.92171 1.16383 0.09711  -0.32893 -0.11195 232 ALA B O     
1183 C  CB    . ALA A 153 ? 1.24064 0.91448 1.13369 0.13798  -0.35939 -0.15015 232 ALA B CB    
1184 N  N     . GLU A 154 ? 1.21709 0.92911 1.11890 0.11474  -0.32366 -0.11731 233 GLU B N     
1185 C  CA    . GLU A 154 ? 1.19157 0.91635 1.11761 0.10062  -0.31821 -0.10670 233 GLU B CA    
1186 C  C     . GLU A 154 ? 1.24261 0.98122 1.17936 0.08663  -0.29663 -0.08985 233 GLU B C     
1187 O  O     . GLU A 154 ? 1.17049 0.92118 1.12809 0.07475  -0.29060 -0.08083 233 GLU B O     
1188 C  CB    . GLU A 154 ? 1.13976 0.86956 1.04617 0.10868  -0.31741 -0.10828 233 GLU B CB    
1189 C  CG    . GLU A 154 ? 1.15454 0.87441 1.06060 0.11831  -0.34073 -0.12310 233 GLU B CG    
1190 C  CD    . GLU A 154 ? 1.36252 1.06713 1.24313 0.13528  -0.35375 -0.13854 233 GLU B CD    
1191 O  OE1   . GLU A 154 ? 1.24959 0.95319 1.10600 0.14233  -0.34232 -0.13725 233 GLU B OE1   
1192 O  OE2   . GLU A 154 ? 1.32924 1.02337 1.21480 0.14195  -0.37593 -0.15258 233 GLU B OE2   
1193 N  N     . ILE A 155 ? 1.19571 0.93346 1.11921 0.08827  -0.28547 -0.08599 234 ILE B N     
1194 C  CA    . ILE A 155 ? 1.03915 0.78931 0.97304 0.07531  -0.26686 -0.07095 234 ILE B CA    
1195 C  C     . ILE A 155 ? 1.19027 0.94317 1.16258 0.05965  -0.27146 -0.06470 234 ILE B C     
1196 O  O     . ILE A 155 ? 1.11338 0.87999 1.09940 0.04709  -0.25756 -0.05171 234 ILE B O     
1197 C  CB    . ILE A 155 ? 1.26017 1.00797 1.17271 0.08152  -0.25639 -0.06932 234 ILE B CB    
1198 C  CG1   . ILE A 155 ? 1.13409 0.89635 1.03496 0.07687  -0.23426 -0.05660 234 ILE B CG1   
1199 C  CG2   . ILE A 155 ? 1.20850 0.94935 1.14086 0.07562  -0.26193 -0.06861 234 ILE B CG2   
1200 C  CD1   . ILE A 155 ? 1.11075 0.87746 0.98915 0.08464  -0.22889 -0.05710 234 ILE B CD1   
1201 N  N     . GLY A 156 ? 1.23396 0.97437 1.22435 0.06027  -0.29105 -0.07350 235 GLY B N     
1202 C  CA    . GLY A 156 ? 1.18758 0.92896 1.21667 0.04597  -0.29815 -0.06757 235 GLY B CA    
1203 C  C     . GLY A 156 ? 1.10945 0.86339 1.16472 0.03518  -0.29917 -0.06187 235 GLY B C     
1204 O  O     . GLY A 156 ? 1.13963 0.89901 1.22851 0.02160  -0.30130 -0.05345 235 GLY B O     
1205 N  N     . GLU A 157 ? 1.00889 0.76844 1.05053 0.04097  -0.29745 -0.06546 236 GLU B N     
1206 C  CA    . GLU A 157 ? 1.04005 0.81289 1.10603 0.03204  -0.29775 -0.06061 236 GLU B CA    
1207 C  C     . GLU A 157 ? 1.19316 0.98530 1.25796 0.02399  -0.27560 -0.04729 236 GLU B C     
1208 O  O     . GLU A 157 ? 1.31202 1.11733 1.39511 0.01757  -0.27342 -0.04315 236 GLU B O     
1209 C  CB    . GLU A 157 ? 1.04553 0.81299 1.10099 0.04312  -0.31117 -0.07276 236 GLU B CB    
1210 C  CG    . GLU A 157 ? 1.18586 0.93467 1.24432 0.05133  -0.33543 -0.08769 236 GLU B CG    
1211 C  CD    . GLU A 157 ? 1.22133 0.96554 1.26867 0.06266  -0.34971 -0.09979 236 GLU B CD    
1212 O  OE1   . GLU A 157 ? 1.28726 1.04409 1.33886 0.06007  -0.34397 -0.09513 236 GLU B OE1   
1213 O  OE2   . GLU A 157 ? 1.20190 0.92988 1.23581 0.07482  -0.36716 -0.11439 236 GLU B OE2   
1214 N  N     . LEU A 158 ? 1.21343 1.00787 1.25825 0.02452  -0.25976 -0.04112 237 LEU B N     
1215 C  CA    . LEU A 158 ? 1.10001 0.91203 1.14527 0.01621  -0.23958 -0.02894 237 LEU B CA    
1216 C  C     . LEU A 158 ? 1.14959 0.97047 1.22052 0.00209  -0.23385 -0.01736 237 LEU B C     
1217 O  O     . LEU A 158 ? 1.22072 1.04605 1.28313 -0.00137 -0.22082 -0.00960 237 LEU B O     
1218 C  CB    . LEU A 158 ? 1.09171 0.90233 1.10273 0.02412  -0.22612 -0.02821 237 LEU B CB    
1219 C  CG    . LEU A 158 ? 1.13499 0.93606 1.11699 0.03917  -0.23105 -0.03800 237 LEU B CG    
1220 C  CD1   . LEU A 158 ? 1.14227 0.94477 1.09500 0.04471  -0.21569 -0.03413 237 LEU B CD1   
1221 C  CD2   . LEU A 158 ? 1.04696 0.85385 1.03516 0.04017  -0.23490 -0.04030 237 LEU B CD2   
1222 N  N     . CYS A 159 ? 1.17809 1.00219 1.28188 -0.00619 -0.24429 -0.01562 238 CYS B N     
1223 C  CA    . CYS A 159 ? 1.14323 0.97386 1.27481 -0.01936 -0.24258 -0.00425 238 CYS B CA    
1224 C  C     . CYS A 159 ? 1.00217 0.85448 1.13881 -0.02937 -0.22260 0.00963  238 CYS B C     
1225 O  O     . CYS A 159 ? 1.04701 0.90736 1.20519 -0.04045 -0.21932 0.02101  238 CYS B O     
1226 C  CB    . CYS A 159 ? 1.18180 1.01212 1.34948 -0.02590 -0.25883 -0.00510 238 CYS B CB    
1227 S  SG    . CYS A 159 ? 1.34013 1.18670 1.52359 -0.02753 -0.25924 -0.00659 238 CYS B SG    
1228 N  N     . ASN A 160 ? 0.92867 0.79045 1.04637 -0.02560 -0.20975 0.00913  239 ASN B N     
1229 C  CA    . ASN A 160 ? 0.98786 0.86942 1.10721 -0.03345 -0.19131 0.02010  239 ASN B CA    
1230 C  C     . ASN A 160 ? 0.92388 0.80305 1.01439 -0.02963 -0.17877 0.02191  239 ASN B C     
1231 O  O     . ASN A 160 ? 0.88071 0.77495 0.96801 -0.03448 -0.16381 0.02910  239 ASN B O     
1232 C  CB    . ASN A 160 ? 1.04868 0.94449 1.17254 -0.03303 -0.18590 0.01854  239 ASN B CB    
1233 C  CG    . ASN A 160 ? 1.09764 1.00101 1.25478 -0.03862 -0.19607 0.01903  239 ASN B CG    
1234 O  OD1   . ASN A 160 ? 1.04868 0.96966 1.23082 -0.04926 -0.19006 0.02928  239 ASN B OD1   
1235 N  ND2   . ASN A 160 ? 0.91361 0.80482 1.07151 -0.03126 -0.21159 0.00828  239 ASN B ND2   
1236 N  N     . LEU A 161 ? 0.88261 0.74408 0.95278 -0.02077 -0.18472 0.01523  240 LEU B N     
1237 C  CA    . LEU A 161 ? 0.92794 0.78774 0.97180 -0.01653 -0.17324 0.01675  240 LEU B CA    
1238 C  C     . LEU A 161 ? 0.98074 0.84823 1.03237 -0.02569 -0.16490 0.02803  240 LEU B C     
1239 O  O     . LEU A 161 ? 0.91910 0.78159 0.98748 -0.03040 -0.17281 0.03168  240 LEU B O     
1240 C  CB    . LEU A 161 ? 0.81830 0.65909 0.84020 -0.00416 -0.18170 0.00711  240 LEU B CB    
1241 C  CG    . LEU A 161 ? 0.82189 0.65658 0.82251 0.00744  -0.18408 -0.00225 240 LEU B CG    
1242 C  CD1   . LEU A 161 ? 0.80944 0.62862 0.78603 0.01977  -0.18934 -0.00988 240 LEU B CD1   
1243 C  CD2   . LEU A 161 ? 0.86771 0.71452 0.85683 0.00637  -0.16879 0.00223  240 LEU B CD2   
1244 N  N     . ILE A 162 ? 0.86179 0.74099 0.90162 -0.02807 -0.14971 0.03362  241 ILE B N     
1245 C  CA    . ILE A 162 ? 0.91633 0.80210 0.95689 -0.03460 -0.14136 0.04348  241 ILE B CA    
1246 C  C     . ILE A 162 ? 0.86909 0.74523 0.88527 -0.02712 -0.13795 0.04089  241 ILE B C     
1247 O  O     . ILE A 162 ? 0.83984 0.71233 0.85712 -0.02894 -0.13855 0.04568  241 ILE B O     
1248 C  CB    . ILE A 162 ? 0.82714 0.73424 0.87252 -0.04260 -0.12733 0.05141  241 ILE B CB    
1249 C  CG1   . ILE A 162 ? 0.75843 0.67772 0.83001 -0.04986 -0.12981 0.05496  241 ILE B CG1   
1250 C  CG2   . ILE A 162 ? 0.73063 0.64506 0.77432 -0.04866 -0.11911 0.06155  241 ILE B CG2   
1251 C  CD1   . ILE A 162 ? 0.74152 0.68345 0.81794 -0.05660 -0.11600 0.06201  241 ILE B CD1   
1252 N  N     . THR A 163 ? 0.76952 0.64196 0.76483 -0.01859 -0.13448 0.03401  242 THR B N     
1253 C  CA    . THR A 163 ? 0.82848 0.69366 0.80120 -0.01089 -0.13046 0.03186  242 THR B CA    
1254 C  C     . THR A 163 ? 0.84873 0.70038 0.80590 0.00138  -0.13822 0.02144  242 THR B C     
1255 O  O     . THR A 163 ? 0.87968 0.73235 0.83349 0.00433  -0.13893 0.01727  242 THR B O     
1256 C  CB    . THR A 163 ? 0.83130 0.70811 0.79233 -0.01309 -0.11589 0.03624  242 THR B CB    
1257 O  OG1   . THR A 163 ? 0.88373 0.77226 0.85459 -0.02268 -0.10910 0.04549  242 THR B OG1   
1258 C  CG2   . THR A 163 ? 0.76442 0.63417 0.70306 -0.00419 -0.11218 0.03354  242 THR B CG2   
1259 N  N     . LEU A 164 ? 0.88215 0.72166 0.82951 0.00917  -0.14417 0.01720  243 LEU B N     
1260 C  CA    . LEU A 164 ? 0.86816 0.69627 0.79566 0.02261  -0.14980 0.00766  243 LEU B CA    
1261 C  C     . LEU A 164 ? 0.89809 0.72660 0.80556 0.02867  -0.14038 0.00959  243 LEU B C     
1262 O  O     . LEU A 164 ? 0.92126 0.74510 0.82847 0.03078  -0.14230 0.00981  243 LEU B O     
1263 C  CB    . LEU A 164 ? 0.73135 0.54503 0.66495 0.02840  -0.16655 -0.00108 243 LEU B CB    
1264 C  CG    . LEU A 164 ? 0.91427 0.71682 0.82570 0.04363  -0.17360 -0.01216 243 LEU B CG    
1265 C  CD1   . LEU A 164 ? 1.02860 0.83492 0.93286 0.04598  -0.17236 -0.01412 243 LEU B CD1   
1266 C  CD2   . LEU A 164 ? 0.85838 0.64612 0.77676 0.04948  -0.19150 -0.02223 243 LEU B CD2   
1267 N  N     . ASP A 165 ? 0.94699 0.78133 0.83952 0.03133  -0.13046 0.01143  244 ASP B N     
1268 C  CA    . ASP A 165 ? 0.87132 0.70867 0.74726 0.03589  -0.12020 0.01485  244 ASP B CA    
1269 C  C     . ASP A 165 ? 0.94984 0.77942 0.80406 0.05016  -0.12303 0.00826  244 ASP B C     
1270 O  O     . ASP A 165 ? 0.97502 0.80550 0.81980 0.05351  -0.12098 0.00770  244 ASP B O     
1271 C  CB    . ASP A 165 ? 0.96576 0.81540 0.84209 0.02827  -0.10727 0.02248  244 ASP B CB    
1272 C  CG    . ASP A 165 ? 1.07750 0.93149 0.94066 0.03135  -0.09689 0.02707  244 ASP B CG    
1273 O  OD1   . ASP A 165 ? 0.92573 0.77518 0.78115 0.03855  -0.09854 0.02530  244 ASP B OD1   
1274 O  OD2   . ASP A 165 ? 1.17991 1.04211 1.04168 0.02676  -0.08742 0.03218  244 ASP B OD2   
1275 N  N     . VAL A 166 ? 0.96405 0.78629 0.81011 0.05918  -0.12791 0.00337  245 VAL B N     
1276 C  CA    . VAL A 166 ? 1.03529 0.85208 0.85843 0.07423  -0.12956 -0.00278 245 VAL B CA    
1277 C  C     . VAL A 166 ? 1.03421 0.85596 0.84549 0.07979  -0.11975 0.00096  245 VAL B C     
1278 O  O     . VAL A 166 ? 0.98157 0.79932 0.77571 0.09328  -0.12170 -0.00476 245 VAL B O     
1279 C  CB    . VAL A 166 ? 1.00267 0.80599 0.82445 0.08334  -0.14608 -0.01500 245 VAL B CB    
1280 C  CG1   . VAL A 166 ? 1.10214 0.90198 0.93891 0.07706  -0.15608 -0.01806 245 VAL B CG1   
1281 C  CG2   . VAL A 166 ? 1.07679 0.87410 0.90851 0.08363  -0.15211 -0.01796 245 VAL B CG2   
1282 N  N     . ALA A 167 ? 1.01695 0.84849 0.83730 0.06996  -0.10926 0.01032  246 ALA B N     
1283 C  CA    . ALA A 167 ? 0.94084 0.77861 0.75389 0.07390  -0.10016 0.01462  246 ALA B CA    
1284 C  C     . ALA A 167 ? 1.00877 0.85163 0.80179 0.08293  -0.09141 0.01701  246 ALA B C     
1285 O  O     . ALA A 167 ? 0.96757 0.81121 0.75491 0.08237  -0.08959 0.01870  246 ALA B O     
1286 C  CB    . ALA A 167 ? 0.90271 0.75056 0.73026 0.06074  -0.09166 0.02421  246 ALA B CB    
1287 N  N     . HIS A 168 ? 0.99846 0.84541 0.78173 0.09154  -0.08589 0.01786  247 HIS B N     
1288 C  CA    . HIS A 168 ? 0.90940 0.76354 0.67445 0.10072  -0.07624 0.02192  247 HIS B CA    
1289 C  C     . HIS A 168 ? 1.00216 0.84943 0.74926 0.11194  -0.08243 0.01543  247 HIS B C     
1290 O  O     . HIS A 168 ? 0.99920 0.84961 0.73835 0.11183  -0.07753 0.02071  247 HIS B O     
1291 C  CB    . HIS A 168 ? 0.92218 0.78729 0.69310 0.09026  -0.06393 0.03394  247 HIS B CB    
1292 C  CG    . HIS A 168 ? 1.02487 0.89881 0.80900 0.08225  -0.05697 0.04038  247 HIS B CG    
1293 N  ND1   . HIS A 168 ? 1.05051 0.92442 0.85265 0.06954  -0.05963 0.04169  247 HIS B ND1   
1294 C  CD2   . HIS A 168 ? 1.06453 0.94861 0.84661 0.08555  -0.04771 0.04611  247 HIS B CD2   
1295 C  CE1   . HIS A 168 ? 1.01514 0.89794 0.82467 0.06548  -0.05301 0.04760  247 HIS B CE1   
1296 N  NE2   . HIS A 168 ? 0.93144 0.82047 0.73014 0.07482  -0.04589 0.05021  247 HIS B NE2   
1297 N  N     . ASN A 169 ? 1.01274 0.84990 0.75398 0.12196  -0.09437 0.00358  248 ASN B N     
1298 C  CA    . ASN A 169 ? 1.08356 0.91434 0.80480 0.13556  -0.10164 -0.00452 248 ASN B CA    
1299 C  C     . ASN A 169 ? 1.15159 0.98047 0.85720 0.15229  -0.10473 -0.01353 248 ASN B C     
1300 O  O     . ASN A 169 ? 1.18677 1.02344 0.89318 0.15449  -0.09629 -0.00990 248 ASN B O     
1301 C  CB    . ASN A 169 ? 1.10553 0.92419 0.83573 0.13175  -0.11675 -0.01289 248 ASN B CB    
1302 C  CG    . ASN A 169 ? 1.06641 0.88779 0.80418 0.12084  -0.11379 -0.00572 248 ASN B CG    
1303 O  OD1   . ASN A 169 ? 1.02158 0.84416 0.74457 0.12654  -0.11193 -0.00370 248 ASN B OD1   
1304 N  ND2   . ASN A 169 ? 1.09203 0.91470 0.85271 0.10568  -0.11350 -0.00176 248 ASN B ND2   
1305 N  N     . GLN A 170 ? 1.23242 1.05136 0.92411 0.16473  -0.11725 -0.02598 249 GLN B N     
1306 C  CA    . GLN A 170 ? 1.22666 1.04297 0.90133 0.18275  -0.12176 -0.03710 249 GLN B CA    
1307 C  C     . GLN A 170 ? 1.20273 1.00194 0.88228 0.18746  -0.14200 -0.05352 249 GLN B C     
1308 O  O     . GLN A 170 ? 1.30879 1.10216 0.96889 0.20422  -0.15091 -0.06619 249 GLN B O     
1309 C  CB    . GLN A 170 ? 1.24172 1.06616 0.88645 0.19815  -0.11483 -0.03580 249 GLN B CB    
1310 C  CG    . GLN A 170 ? 1.32178 1.16398 0.96220 0.19623  -0.09475 -0.02003 249 GLN B CG    
1311 C  CD    . GLN A 170 ? 1.42790 1.27660 1.05802 0.19372  -0.08693 -0.00860 249 GLN B CD    
1312 O  OE1   . GLN A 170 ? 1.51357 1.36020 1.12188 0.20568  -0.09137 -0.01266 249 GLN B OE1   
1313 N  NE2   . GLN A 170 ? 1.30807 1.16424 0.95395 0.17843  -0.07599 0.00563  249 GLN B NE2   
1314 N  N     . LEU A 171 ? 1.14096 0.93235 0.84705 0.17287  -0.14984 -0.05343 250 LEU B N     
1315 C  CA    . LEU A 171 ? 1.20590 0.98085 0.92205 0.17511  -0.16962 -0.06751 250 LEU B CA    
1316 C  C     . LEU A 171 ? 1.24738 1.01612 0.96128 0.18686  -0.17543 -0.07791 250 LEU B C     
1317 O  O     . LEU A 171 ? 1.33223 1.10676 1.05548 0.18295  -0.16683 -0.07149 250 LEU B O     
1318 C  CB    . LEU A 171 ? 1.15306 0.92379 0.90028 0.15570  -0.17456 -0.06209 250 LEU B CB    
1319 C  CG    . LEU A 171 ? 1.16404 0.93836 0.91777 0.14447  -0.17295 -0.05518 250 LEU B CG    
1320 C  CD1   . LEU A 171 ? 1.11189 0.88374 0.89683 0.12677  -0.17757 -0.05049 250 LEU B CD1   
1321 C  CD2   . LEU A 171 ? 1.17389 0.94051 0.91295 0.15510  -0.18531 -0.06592 250 LEU B CD2   
1322 N  N     . GLU A 172 ? 1.26787 1.02470 0.96948 0.20191  -0.19080 -0.09466 251 GLU B N     
1323 C  CA    . GLU A 172 ? 1.28870 1.03600 0.99133 0.21336  -0.20032 -0.10751 251 GLU B CA    
1324 C  C     . GLU A 172 ? 1.28667 1.01585 1.01641 0.20555  -0.21984 -0.11573 251 GLU B C     
1325 O  O     . GLU A 172 ? 1.25103 0.97208 0.99184 0.20885  -0.22631 -0.12171 251 GLU B O     
1326 C  CB    . GLU A 172 ? 1.32139 1.06691 0.99224 0.23727  -0.20559 -0.12268 251 GLU B CB    
1327 C  CG    . GLU A 172 ? 1.45646 1.21960 1.10374 0.24917  -0.18681 -0.11667 251 GLU B CG    
1328 C  CD    . GLU A 172 ? 1.68301 1.44474 1.29997 0.27441  -0.19274 -0.13318 251 GLU B CD    
1329 O  OE1   . GLU A 172 ? 1.69067 1.44137 1.29651 0.28248  -0.20833 -0.14626 251 GLU B OE1   
1330 O  OE2   . GLU A 172 ? 1.68561 1.45799 1.28998 0.28669  -0.18208 -0.13347 251 GLU B OE2   
1331 N  N     . HIS A 173 ? 1.30458 1.02766 1.04680 0.19529  -0.22940 -0.11553 252 HIS B N     
1332 C  CA    . HIS A 173 ? 1.31836 1.02587 1.08963 0.18604  -0.24747 -0.12107 252 HIS B CA    
1333 C  C     . HIS A 173 ? 1.25061 0.96251 1.04212 0.16678  -0.24572 -0.10933 252 HIS B C     
1334 O  O     . HIS A 173 ? 1.32990 1.05082 1.10879 0.16568  -0.23834 -0.10435 252 HIS B O     
1335 C  CB    . HIS A 173 ? 1.33818 1.02872 1.10207 0.20077  -0.26974 -0.14204 252 HIS B CB    
1336 C  CG    . HIS A 173 ? 1.36633 1.05193 1.10995 0.22155  -0.27315 -0.15618 252 HIS B CG    
1337 N  ND1   . HIS A 173 ? 1.42500 1.09879 1.18475 0.22388  -0.28233 -0.16305 252 HIS B ND1   
1338 C  CD2   . HIS A 173 ? 1.39390 1.08557 1.10249 0.24163  -0.26842 -0.16461 252 HIS B CD2   
1339 C  CE1   . HIS A 173 ? 1.41427 1.08692 1.14997 0.24501  -0.28325 -0.17633 252 HIS B CE1   
1340 N  NE2   . HIS A 173 ? 1.51577 1.20002 1.21966 0.25619  -0.27444 -0.17734 252 HIS B NE2   
1341 N  N     . LEU A 174 ? 1.26832 0.97430 1.09185 0.15196  -0.25244 -0.10449 253 LEU B N     
1342 C  CA    . LEU A 174 ? 1.27165 0.98166 1.11754 0.13434  -0.25278 -0.09484 253 LEU B CA    
1343 C  C     . LEU A 174 ? 1.34389 1.03902 1.20450 0.13506  -0.27522 -0.10704 253 LEU B C     
1344 O  O     . LEU A 174 ? 1.42625 1.10676 1.30115 0.13767  -0.29025 -0.11572 253 LEU B O     
1345 C  CB    . LEU A 174 ? 1.27348 0.98901 1.14578 0.11708  -0.24514 -0.08004 253 LEU B CB    
1346 C  CG    . LEU A 174 ? 1.18796 0.92022 1.06821 0.10121  -0.22905 -0.06331 253 LEU B CG    
1347 C  CD1   . LEU A 174 ? 1.21287 0.94775 1.12075 0.08571  -0.22659 -0.05137 253 LEU B CD1   
1348 C  CD2   . LEU A 174 ? 1.31248 1.04685 1.19787 0.09611  -0.23372 -0.06403 253 LEU B CD2   
1349 N  N     . PRO A 175 ? 1.36133 1.05891 1.22023 0.13329  -0.27926 -0.10854 254 PRO B N     
1350 C  CA    . PRO A 175 ? 1.23714 0.92131 1.11317 0.13313  -0.30169 -0.12000 254 PRO B CA    
1351 C  C     . PRO A 175 ? 1.28842 0.96766 1.20447 0.11647  -0.30934 -0.11328 254 PRO B C     
1352 O  O     . PRO A 175 ? 1.27308 0.96446 1.20648 0.10045  -0.29679 -0.09701 254 PRO B O     
1353 C  CB    . PRO A 175 ? 1.17153 0.86436 1.04158 0.13072  -0.29956 -0.11752 254 PRO B CB    
1354 C  CG    . PRO A 175 ? 1.29863 1.00923 1.15797 0.12425  -0.27552 -0.10156 254 PRO B CG    
1355 C  CD    . PRO A 175 ? 1.24547 0.95734 1.08634 0.13274  -0.26485 -0.10080 254 PRO B CD    
1356 N  N     . LYS A 176 ? 1.28950 0.95084 1.22022 0.12075  -0.33053 -0.12596 255 LYS B N     
1357 C  CA    . LYS A 176 ? 1.25606 0.91075 1.22604 0.10586  -0.33951 -0.11936 255 LYS B CA    
1358 C  C     . LYS A 176 ? 1.26576 0.93031 1.26380 0.08798  -0.33893 -0.10768 255 LYS B C     
1359 O  O     . LYS A 176 ? 1.23757 0.90368 1.26750 0.07256  -0.33921 -0.09576 255 LYS B O     
1360 C  CB    . LYS A 176 ? 1.20600 0.83792 1.18682 0.11486  -0.36501 -0.13705 255 LYS B CB    
1361 C  CG    . LYS A 176 ? 1.17717 0.80065 1.14634 0.12669  -0.38234 -0.15495 255 LYS B CG    
1362 C  CD    . LYS A 176 ? 1.41460 1.01486 1.38743 0.13948  -0.40684 -0.17532 255 LYS B CD    
1363 C  CE    . LYS A 176 ? 1.23388 0.82604 1.19142 0.15305  -0.42483 -0.19461 255 LYS B CE    
1364 N  NZ    . LYS A 176 ? 1.32285 0.91810 1.30842 0.13920  -0.43423 -0.19012 255 LYS B NZ    
1365 N  N     . GLU A 177 ? 1.17078 0.84295 1.15796 0.09004  -0.33776 -0.11017 256 GLU B N     
1366 C  CA    . GLU A 177 ? 1.24678 0.93027 1.25990 0.07447  -0.33633 -0.09978 256 GLU B CA    
1367 C  C     . GLU A 177 ? 1.26887 0.97168 1.28786 0.06043  -0.31342 -0.07989 256 GLU B C     
1368 O  O     . GLU A 177 ? 1.25357 0.96813 1.29465 0.04733  -0.31013 -0.07025 256 GLU B O     
1369 C  CB    . GLU A 177 ? 1.21820 0.90466 1.21620 0.08206  -0.34111 -0.10822 256 GLU B CB    
1370 C  CG    . GLU A 177 ? 1.15160 0.82073 1.15233 0.09251  -0.36713 -0.12725 256 GLU B CG    
1371 C  CD    . GLU A 177 ? 1.30354 0.95865 1.27234 0.11258  -0.37401 -0.14344 256 GLU B CD    
1372 O  OE1   . GLU A 177 ? 1.33938 1.00085 1.27982 0.11974  -0.35696 -0.13966 256 GLU B OE1   
1373 O  OE2   . GLU A 177 ? 1.34283 0.98119 1.31548 0.12152  -0.39666 -0.16025 256 GLU B OE2   
1374 N  N     . ILE A 178 ? 1.15395 0.86104 1.15449 0.06323  -0.29805 -0.07405 257 ILE B N     
1375 C  CA    . ILE A 178 ? 1.16451 0.88934 1.16945 0.05069  -0.27744 -0.05639 257 ILE B CA    
1376 C  C     . ILE A 178 ? 1.20702 0.93497 1.24862 0.03387  -0.27948 -0.04402 257 ILE B C     
1377 O  O     . ILE A 178 ? 1.20505 0.94979 1.25755 0.02129  -0.26605 -0.02996 257 ILE B O     
1378 C  CB    . ILE A 178 ? 1.22172 0.94917 1.20043 0.05817  -0.26301 -0.05401 257 ILE B CB    
1379 C  CG1   . ILE A 178 ? 1.01556 0.76159 0.99620 0.04623  -0.24229 -0.03720 257 ILE B CG1   
1380 C  CG2   . ILE A 178 ? 1.17175 0.88518 1.15627 0.06253  -0.27196 -0.05826 257 ILE B CG2   
1381 C  CD1   . ILE A 178 ? 1.10273 0.86248 1.07687 0.04278  -0.23243 -0.03330 257 ILE B CD1   
1382 N  N     . GLY A 179 ? 1.19596 0.90825 1.25743 0.03357  -0.29645 -0.04884 258 GLY B N     
1383 C  CA    . GLY A 179 ? 1.23491 0.94913 1.33357 0.01757  -0.30026 -0.03619 258 GLY B CA    
1384 C  C     . GLY A 179 ? 1.30499 1.02992 1.43057 0.00526  -0.30312 -0.02987 258 GLY B C     
1385 O  O     . GLY A 179 ? 1.21038 0.93991 1.36826 -0.00891 -0.30479 -0.01724 258 GLY B O     
1386 N  N     . ASN A 180 ? 1.28928 1.01926 1.40344 0.01033  -0.30352 -0.03741 259 ASN B N     
1387 C  CA    . ASN A 180 ? 1.18266 0.92492 1.32247 -0.00052 -0.30529 -0.03165 259 ASN B CA    
1388 C  C     . ASN A 180 ? 1.20822 0.97395 1.34248 -0.00811 -0.28332 -0.01873 259 ASN B C     
1389 O  O     . ASN A 180 ? 1.24630 1.02567 1.40363 -0.01803 -0.28191 -0.01184 259 ASN B O     
1390 C  CB    . ASN A 180 ? 1.28868 1.02256 1.42369 0.00919  -0.32120 -0.04776 259 ASN B CB    
1391 C  CG    . ASN A 180 ? 1.33593 1.04641 1.47892 0.01679  -0.34546 -0.06241 259 ASN B CG    
1392 O  OD1   . ASN A 180 ? 1.33649 1.03558 1.48514 0.01657  -0.34976 -0.06160 259 ASN B OD1   
1393 N  ND2   . ASN A 180 ? 1.37526 1.07804 1.51826 0.02430  -0.36218 -0.07659 259 ASN B ND2   
1394 N  N     . CYS A 181 ? 1.13349 0.90457 1.23905 -0.00342 -0.26672 -0.01577 260 CYS B N     
1395 C  CA    . CYS A 181 ? 1.08326 0.87537 1.18324 -0.01043 -0.24621 -0.00409 260 CYS B CA    
1396 C  C     . CYS A 181 ? 1.09724 0.89914 1.21441 -0.02322 -0.23680 0.01197  260 CYS B C     
1397 O  O     . CYS A 181 ? 1.15561 0.96224 1.25641 -0.02297 -0.22362 0.01793  260 CYS B O     
1398 C  CB    . CYS A 181 ? 0.99721 0.78987 1.05976 0.00060  -0.23428 -0.00874 260 CYS B CB    
1399 S  SG    . CYS A 181 ? 1.04469 0.82278 1.08129 0.01839  -0.24623 -0.02709 260 CYS B SG    
1400 N  N     . THR A 182 ? 1.19599 1.00135 1.34777 -0.03463 -0.24440 0.01956  261 THR B N     
1401 C  CA    . THR A 182 ? 1.10169 0.91372 1.27236 -0.04641 -0.23898 0.03536  261 THR B CA    
1402 C  C     . THR A 182 ? 0.93208 0.76618 1.09338 -0.05278 -0.21729 0.04791  261 THR B C     
1403 O  O     . THR A 182 ? 1.11422 0.95180 1.27428 -0.05736 -0.20966 0.05835  261 THR B O     
1404 C  CB    . THR A 182 ? 1.09201 0.90631 1.30351 -0.05810 -0.25037 0.04270  261 THR B CB    
1405 O  OG1   . THR A 182 ? 0.93249 0.76447 1.15561 -0.06302 -0.24558 0.04482  261 THR B OG1   
1406 C  CG2   . THR A 182 ? 1.08189 0.87214 1.30400 -0.05184 -0.27386 0.02946  261 THR B CG2   
1407 N  N     . GLN A 183 ? 0.95725 0.80593 1.11159 -0.05251 -0.20789 0.04649  262 GLN B N     
1408 C  CA    . GLN A 183 ? 0.93084 0.80054 1.07715 -0.05802 -0.18840 0.05671  262 GLN B CA    
1409 C  C     . GLN A 183 ? 0.93347 0.80013 1.04749 -0.05076 -0.17789 0.05434  262 GLN B C     
1410 O  O     . GLN A 183 ? 0.92353 0.80618 1.02861 -0.05429 -0.16260 0.06107  262 GLN B O     
1411 C  CB    . GLN A 183 ? 0.98554 0.87032 1.13428 -0.05856 -0.18248 0.05425  262 GLN B CB    
1412 C  CG    . GLN A 183 ? 1.02847 0.92465 1.21234 -0.06813 -0.18792 0.06044  262 GLN B CG    
1413 C  CD    . GLN A 183 ? 1.24156 1.15607 1.42748 -0.06852 -0.17924 0.05919  262 GLN B CD    
1414 O  OE1   . GLN A 183 ? 1.26578 1.18844 1.42986 -0.06485 -0.16595 0.05786  262 GLN B OE1   
1415 N  NE2   . GLN A 183 ? 1.07009 0.99100 1.28380 -0.07279 -0.18737 0.05931  262 GLN B NE2   
1416 N  N     . ILE A 184 ? 0.94348 0.79110 1.04060 -0.04052 -0.18570 0.04482  263 ILE B N     
1417 C  CA    . ILE A 184 ? 0.89391 0.73982 0.96202 -0.03328 -0.17573 0.04273  263 ILE B CA    
1418 C  C     . ILE A 184 ? 0.98614 0.83838 1.05764 -0.04027 -0.16798 0.05513  263 ILE B C     
1419 O  O     . ILE A 184 ? 1.00789 0.85190 1.09480 -0.04361 -0.17652 0.05966  263 ILE B O     
1420 C  CB    . ILE A 184 ? 0.85558 0.68135 0.90547 -0.01954 -0.18598 0.02931  263 ILE B CB    
1421 C  CG1   . ILE A 184 ? 0.87720 0.70023 0.91328 -0.01081 -0.18876 0.01803  263 ILE B CG1   
1422 C  CG2   . ILE A 184 ? 0.88062 0.70446 0.90818 -0.01384 -0.17718 0.03025  263 ILE B CG2   
1423 C  CD1   . ILE A 184 ? 0.91310 0.71994 0.92534 0.00412  -0.19562 0.00554  263 ILE B CD1   
1424 N  N     . THR A 185 ? 0.96368 0.83024 1.02137 -0.04240 -0.15253 0.06065  264 THR B N     
1425 C  CA    . THR A 185 ? 0.89568 0.76826 0.95071 -0.04692 -0.14475 0.07096  264 THR B CA    
1426 C  C     . THR A 185 ? 0.88332 0.75087 0.91235 -0.03807 -0.13890 0.06609  264 THR B C     
1427 O  O     . THR A 185 ? 0.86694 0.73504 0.89363 -0.03949 -0.13592 0.07260  264 THR B O     
1428 C  CB    . THR A 185 ? 0.88223 0.77747 0.94359 -0.05713 -0.13180 0.08225  264 THR B CB    
1429 O  OG1   . THR A 185 ? 0.89783 0.80157 0.94058 -0.05337 -0.12124 0.07694  264 THR B OG1   
1430 C  CG2   . THR A 185 ? 0.86604 0.76993 0.95367 -0.06557 -0.13566 0.08759  264 THR B CG2   
1431 N  N     . ASN A 186 ? 0.90804 0.77131 0.91867 -0.02904 -0.13736 0.05569  265 ASN B N     
1432 C  CA    . ASN A 186 ? 0.92318 0.78391 0.91022 -0.02084 -0.13065 0.05199  265 ASN B CA    
1433 C  C     . ASN A 186 ? 0.89045 0.73610 0.86392 -0.00814 -0.13873 0.03947  265 ASN B C     
1434 O  O     . ASN A 186 ? 0.81923 0.66462 0.78729 -0.00469 -0.13962 0.03336  265 ASN B O     
1435 C  CB    . ASN A 186 ? 0.84765 0.72314 0.82395 -0.02359 -0.11684 0.05464  265 ASN B CB    
1436 C  CG    . ASN A 186 ? 0.91969 0.79352 0.87457 -0.01615 -0.10992 0.05200  265 ASN B CG    
1437 O  OD1   . ASN A 186 ? 0.96166 0.82914 0.91155 -0.01181 -0.11170 0.05234  265 ASN B OD1   
1438 N  ND2   . ASN A 186 ? 0.89432 0.77413 0.83798 -0.01455 -0.10213 0.04969  265 ASN B ND2   
1439 N  N     . LEU A 187 ? 0.95863 0.79228 0.92612 -0.00049 -0.14474 0.03556  266 LEU B N     
1440 C  CA    . LEU A 187 ? 0.92116 0.74139 0.87303 0.01327  -0.15209 0.02332  266 LEU B CA    
1441 C  C     . LEU A 187 ? 1.02582 0.84699 0.95787 0.02131  -0.14378 0.02302  266 LEU B C     
1442 O  O     . LEU A 187 ? 1.02441 0.84302 0.95978 0.02185  -0.14456 0.02598  266 LEU B O     
1443 C  CB    . LEU A 187 ? 0.97007 0.77442 0.93453 0.01681  -0.16893 0.01672  266 LEU B CB    
1444 C  CG    . LEU A 187 ? 0.91242 0.70235 0.86088 0.03213  -0.17890 0.00219  266 LEU B CG    
1445 C  CD1   . LEU A 187 ? 0.89958 0.69030 0.84157 0.03498  -0.18124 -0.00402 266 LEU B CD1   
1446 C  CD2   . LEU A 187 ? 0.91203 0.68558 0.87453 0.03535  -0.19590 -0.00434 266 LEU B CD2   
1447 N  N     . ASP A 188 ? 0.95291 0.77820 0.86589 0.02746  -0.13597 0.02020  267 ASP B N     
1448 C  CA    . ASP A 188 ? 0.93851 0.76774 0.83414 0.03418  -0.12636 0.02149  267 ASP B CA    
1449 C  C     . ASP A 188 ? 0.98978 0.80929 0.86685 0.04969  -0.13135 0.01105  267 ASP B C     
1450 O  O     . ASP A 188 ? 0.94231 0.76092 0.80836 0.05448  -0.13155 0.00675  267 ASP B O     
1451 C  CB    . ASP A 188 ? 0.95137 0.79414 0.84090 0.02856  -0.11274 0.02813  267 ASP B CB    
1452 C  CG    . ASP A 188 ? 1.05565 0.90560 0.93567 0.03074  -0.10235 0.03305  267 ASP B CG    
1453 O  OD1   . ASP A 188 ? 0.99283 0.83748 0.86412 0.04070  -0.10423 0.02935  267 ASP B OD1   
1454 O  OD2   . ASP A 188 ? 1.15038 1.01179 1.03235 0.02282  -0.09263 0.04015  267 ASP B OD2   
1455 N  N     . LEU A 189 ? 1.10214 0.91491 0.97530 0.05821  -0.13543 0.00700  268 LEU B N     
1456 C  CA    . LEU A 189 ? 1.03240 0.83698 0.88680 0.07460  -0.14018 -0.00371 268 LEU B CA    
1457 C  C     . LEU A 189 ? 1.01655 0.82801 0.85690 0.08269  -0.12979 -0.00141 268 LEU B C     
1458 O  O     . LEU A 189 ? 1.15500 0.96088 0.98135 0.09721  -0.13337 -0.00998 268 LEU B O     
1459 C  CB    . LEU A 189 ? 0.95285 0.74154 0.81554 0.08039  -0.15715 -0.01398 268 LEU B CB    
1460 C  CG    . LEU A 189 ? 0.95890 0.74108 0.84412 0.06990  -0.16872 -0.01408 268 LEU B CG    
1461 C  CD1   . LEU A 189 ? 0.94852 0.71459 0.84513 0.07488  -0.18526 -0.02272 268 LEU B CD1   
1462 C  CD2   . LEU A 189 ? 0.88761 0.66947 0.76756 0.07060  -0.17194 -0.01854 268 LEU B CD2   
1463 N  N     . GLN A 190 ? 1.00697 0.83124 0.85116 0.07406  -0.11725 0.00959  269 GLN B N     
1464 C  CA    . GLN A 190 ? 0.98327 0.81533 0.81912 0.08019  -0.10792 0.01288  269 GLN B CA    
1465 C  C     . GLN A 190 ? 0.99561 0.83298 0.80970 0.09112  -0.10001 0.01122  269 GLN B C     
1466 O  O     . GLN A 190 ? 1.06835 0.90557 0.87451 0.09099  -0.09923 0.01056  269 GLN B O     
1467 C  CB    . GLN A 190 ? 0.96763 0.81221 0.81469 0.06738  -0.09789 0.02491  269 GLN B CB    
1468 C  CG    . GLN A 190 ? 0.95921 0.81392 0.80282 0.05976  -0.08787 0.03137  269 GLN B CG    
1469 C  CD    . GLN A 190 ? 1.02610 0.89255 0.88069 0.04762  -0.07973 0.04148  269 GLN B CD    
1470 O  OE1   . GLN A 190 ? 1.09891 0.97409 0.95074 0.04925  -0.07171 0.04616  269 GLN B OE1   
1471 N  NE2   . GLN A 190 ? 0.95838 0.82615 0.82574 0.03572  -0.08193 0.04480  269 GLN B NE2   
1472 N  N     . HIS A 191 ? 1.04119 0.88407 0.84637 0.10093  -0.09398 0.01130  270 HIS B N     
1473 C  CA    . HIS A 191 ? 1.07371 0.92455 0.85891 0.11185  -0.08461 0.01199  270 HIS B CA    
1474 C  C     . HIS A 191 ? 1.10503 0.94688 0.87304 0.12354  -0.09223 0.00201  270 HIS B C     
1475 O  O     . HIS A 191 ? 1.04630 0.89227 0.80200 0.12519  -0.08693 0.00503  270 HIS B O     
1476 C  CB    . HIS A 191 ? 0.90391 0.76768 0.69042 0.10191  -0.07149 0.02408  270 HIS B CB    
1477 C  CG    . HIS A 191 ? 1.05116 0.92627 0.84964 0.09447  -0.06287 0.03310  270 HIS B CG    
1478 N  ND1   . HIS A 191 ? 1.00686 0.89261 0.79979 0.10235  -0.05394 0.03656  270 HIS B ND1   
1479 C  CD2   . HIS A 191 ? 1.08065 0.95904 0.89637 0.08034  -0.06218 0.03928  270 HIS B CD2   
1480 C  CE1   . HIS A 191 ? 1.06632 0.96073 0.87357 0.09301  -0.04886 0.04425  270 HIS B CE1   
1481 N  NE2   . HIS A 191 ? 1.08340 0.97332 0.90351 0.07982  -0.05387 0.04588  270 HIS B NE2   
1482 N  N     . ASN A 192 ? 1.08015 0.90907 0.84784 0.13197  -0.10573 -0.01009 271 ASN B N     
1483 C  CA    . ASN A 192 ? 1.11761 0.93769 0.86739 0.14578  -0.11473 -0.02183 271 ASN B CA    
1484 C  C     . ASN A 192 ? 1.09204 0.90970 0.82898 0.16376  -0.11789 -0.03205 271 ASN B C     
1485 O  O     . ASN A 192 ? 1.30351 1.13203 1.03819 0.16794  -0.10736 -0.02720 271 ASN B O     
1486 C  CB    . ASN A 192 ? 1.11171 0.91699 0.87329 0.14019  -0.13088 -0.02949 271 ASN B CB    
1487 C  CG    . ASN A 192 ? 1.09539 0.90320 0.86019 0.12941  -0.12878 -0.02339 271 ASN B CG    
1488 O  OD1   . ASN A 192 ? 1.08854 0.89367 0.83859 0.13650  -0.13222 -0.02796 271 ASN B OD1   
1489 N  ND2   . ASN A 192 ? 1.10954 0.92292 0.89323 0.11292  -0.12339 -0.01329 271 ASN B ND2   
1490 N  N     . GLU A 193 ? 1.14506 0.94889 0.87436 0.17488  -0.13287 -0.04684 272 GLU B N     
1491 C  CA    . GLU A 193 ? 1.19313 0.99283 0.90925 0.19381  -0.13822 -0.05964 272 GLU B CA    
1492 C  C     . GLU A 193 ? 1.20208 0.98163 0.92933 0.19639  -0.15909 -0.07428 272 GLU B C     
1493 O  O     . GLU A 193 ? 1.22675 0.99751 0.93891 0.21325  -0.16977 -0.08977 272 GLU B O     
1494 C  CB    . GLU A 193 ? 1.25028 1.05679 0.93533 0.21108  -0.13335 -0.06420 272 GLU B CB    
1495 C  CG    . GLU A 193 ? 1.20257 1.02960 0.87730 0.21053  -0.11257 -0.04932 272 GLU B CG    
1496 C  CD    . GLU A 193 ? 1.42183 1.25589 1.06672 0.22531  -0.10775 -0.05085 272 GLU B CD    
1497 O  OE1   . GLU A 193 ? 1.48680 1.30955 1.11853 0.23446  -0.12098 -0.06322 272 GLU B OE1   
1498 O  OE2   . GLU A 193 ? 1.55871 1.41004 1.19381 0.22770  -0.09103 -0.03911 272 GLU B OE2   
1499 N  N     . LEU A 194 ? 1.08828 0.86060 0.84248 0.17973  -0.16545 -0.06940 273 LEU B N     
1500 C  CA    . LEU A 194 ? 1.19815 0.95127 0.96783 0.17912  -0.18568 -0.08083 273 LEU B CA    
1501 C  C     . LEU A 194 ? 1.31995 1.06414 1.09070 0.19236  -0.19380 -0.09207 273 LEU B C     
1502 O  O     . LEU A 194 ? 1.25349 1.00417 1.03220 0.19058  -0.18566 -0.08522 273 LEU B O     
1503 C  CB    . LEU A 194 ? 1.06616 0.81691 0.86559 0.15767  -0.18802 -0.06993 273 LEU B CB    
1504 C  CG    . LEU A 194 ? 1.16507 0.92316 0.96726 0.14432  -0.18224 -0.06051 273 LEU B CG    
1505 C  CD1   . LEU A 194 ? 1.14573 0.90442 0.97671 0.12441  -0.18270 -0.04930 273 LEU B CD1   
1506 C  CD2   . LEU A 194 ? 1.16603 0.91459 0.95929 0.15090  -0.19505 -0.07198 273 LEU B CD2   
1507 N  N     . LEU A 195 ? 1.23453 0.96358 0.99765 0.20618  -0.21070 -0.11004 274 LEU B N     
1508 C  CA    . LEU A 195 ? 1.25388 0.97140 1.01948 0.21977  -0.22149 -0.12342 274 LEU B CA    
1509 C  C     . LEU A 195 ? 1.26587 0.96528 1.06381 0.20875  -0.23838 -0.12509 274 LEU B C     
1510 O  O     . LEU A 195 ? 1.25195 0.94361 1.06068 0.21399  -0.24408 -0.12956 274 LEU B O     
1511 C  CB    . LEU A 195 ? 1.21628 0.92651 0.95571 0.24236  -0.23196 -0.14372 274 LEU B CB    
1512 C  CG    . LEU A 195 ? 1.20164 0.92990 0.90686 0.25547  -0.21612 -0.14224 274 LEU B CG    
1513 C  CD1   . LEU A 195 ? 1.31171 1.03192 0.99088 0.27695  -0.22876 -0.16252 274 LEU B CD1   
1514 C  CD2   . LEU A 195 ? 1.26994 1.01461 0.96867 0.26189  -0.19850 -0.13494 274 LEU B CD2   
1515 N  N     . ASP A 196 ? 1.24597 0.93911 1.06075 0.19367  -0.24634 -0.12082 275 ASP B N     
1516 C  CA    . ASP A 196 ? 1.29223 0.97022 1.14025 0.18093  -0.26131 -0.11925 275 ASP B CA    
1517 C  C     . ASP A 196 ? 1.31245 0.99597 1.17680 0.16045  -0.25850 -0.10577 275 ASP B C     
1518 O  O     . ASP A 196 ? 1.38917 1.08624 1.23884 0.15741  -0.24635 -0.09951 275 ASP B O     
1519 C  CB    . ASP A 196 ? 1.34762 1.00303 1.19965 0.19307  -0.28558 -0.13992 275 ASP B CB    
1520 C  CG    . ASP A 196 ? 1.45284 1.10497 1.28747 0.20061  -0.29399 -0.15192 275 ASP B CG    
1521 O  OD1   . ASP A 196 ? 1.43800 1.09083 1.28550 0.18654  -0.29688 -0.14533 275 ASP B OD1   
1522 O  OD2   . ASP A 196 ? 1.55711 1.20673 1.36492 0.22127  -0.29785 -0.16805 275 ASP B OD2   
1523 N  N     . LEU A 197 ? 1.22731 0.90053 1.12316 0.14666  -0.26988 -0.10096 276 LEU B N     
1524 C  CA    . LEU A 197 ? 1.18702 0.86534 1.10205 0.12764  -0.26888 -0.08893 276 LEU B CA    
1525 C  C     . LEU A 197 ? 1.21717 0.87729 1.15531 0.12431  -0.29153 -0.09768 276 LEU B C     
1526 O  O     . LEU A 197 ? 1.35261 0.99598 1.30487 0.12897  -0.30660 -0.10562 276 LEU B O     
1527 C  CB    . LEU A 197 ? 1.15495 0.84409 1.08937 0.11035  -0.25689 -0.06892 276 LEU B CB    
1528 C  CG    . LEU A 197 ? 1.22285 0.93296 1.14015 0.10759  -0.23398 -0.05688 276 LEU B CG    
1529 C  CD1   . LEU A 197 ? 1.16980 0.88658 1.10368 0.09628  -0.22611 -0.04170 276 LEU B CD1   
1530 C  CD2   . LEU A 197 ? 1.16723 0.88952 1.08023 0.09827  -0.22542 -0.05024 276 LEU B CD2   
1531 N  N     . PRO A 198 ? 1.17695 0.83970 1.12114 0.11641  -0.29505 -0.09656 277 PRO B N     
1532 C  CA    . PRO A 198 ? 1.20715 0.85390 1.17661 0.11207  -0.31701 -0.10408 277 PRO B CA    
1533 C  C     . PRO A 198 ? 1.20735 0.84976 1.21396 0.09548  -0.32174 -0.09097 277 PRO B C     
1534 O  O     . PRO A 198 ? 1.23257 0.88931 1.24772 0.08205  -0.30641 -0.07267 277 PRO B O     
1535 C  CB    . PRO A 198 ? 1.28394 0.94023 1.25164 0.10556  -0.31482 -0.10177 277 PRO B CB    
1536 C  CG    . PRO A 198 ? 1.19495 0.87279 1.14960 0.09846  -0.29046 -0.08614 277 PRO B CG    
1537 C  CD    . PRO A 198 ? 1.22403 0.90452 1.15444 0.11087  -0.27969 -0.08816 277 PRO B CD    
1538 N  N     . ASP A 199 ? 1.22591 0.84806 1.25484 0.09680  -0.34392 -0.10050 278 ASP B N     
1539 C  CA    . ASP A 199 ? 1.20319 0.81939 1.27005 0.08113  -0.35071 -0.08754 278 ASP B CA    
1540 C  C     . ASP A 199 ? 1.26315 0.89254 1.35397 0.06091  -0.34585 -0.07103 278 ASP B C     
1541 O  O     . ASP A 199 ? 1.23894 0.87275 1.35561 0.04570  -0.34231 -0.05361 278 ASP B O     
1542 C  CB    . ASP A 199 ? 1.28836 0.87839 1.37533 0.08743  -0.37736 -0.10243 278 ASP B CB    
1543 C  CG    . ASP A 199 ? 1.40245 0.97928 1.46954 0.10738  -0.38252 -0.11825 278 ASP B CG    
1544 O  OD1   . ASP A 199 ? 1.28318 0.87243 1.32427 0.11463  -0.36447 -0.11501 278 ASP B OD1   
1545 O  OD2   . ASP A 199 ? 1.49957 1.05395 1.57805 0.11611  -0.40495 -0.13430 278 ASP B OD2   
1546 N  N     . THR A 200 ? 1.18130 0.81808 1.26385 0.06094  -0.34527 -0.07567 279 THR B N     
1547 C  CA    . THR A 200 ? 1.26344 0.91459 1.36810 0.04322  -0.34005 -0.06120 279 THR B CA    
1548 C  C     . THR A 200 ? 1.32910 1.00325 1.42705 0.03273  -0.31530 -0.04208 279 THR B C     
1549 O  O     . THR A 200 ? 1.27646 0.96504 1.39117 0.01857  -0.30873 -0.02953 279 THR B O     
1550 C  CB    . THR A 200 ? 1.36158 1.01483 1.45724 0.04787  -0.34592 -0.07227 279 THR B CB    
1551 O  OG1   . THR A 200 ? 1.35532 1.01270 1.41015 0.06357  -0.33633 -0.08223 279 THR B OG1   
1552 C  CG2   . THR A 200 ? 1.28389 0.91613 1.39774 0.05272  -0.37300 -0.08809 279 THR B CG2   
1553 N  N     . ILE A 201 ? 1.29511 0.97365 1.36995 0.03957  -0.30190 -0.03998 280 ILE B N     
1554 C  CA    . ILE A 201 ? 1.18605 0.88553 1.25457 0.03010  -0.27984 -0.02298 280 ILE B CA    
1555 C  C     . ILE A 201 ? 1.25826 0.96334 1.35840 0.01262  -0.27841 -0.00440 280 ILE B C     
1556 O  O     . ILE A 201 ? 1.28272 1.00704 1.38381 0.00175  -0.26227 0.01050  280 ILE B O     
1557 C  CB    . ILE A 201 ? 1.24354 0.94527 1.28368 0.04157  -0.26814 -0.02533 280 ILE B CB    
1558 C  CG1   . ILE A 201 ? 1.21981 0.94381 1.24681 0.03455  -0.24565 -0.01202 280 ILE B CG1   
1559 C  CG2   . ILE A 201 ? 1.19673 0.88692 1.24937 0.04270  -0.27478 -0.02287 280 ILE B CG2   
1560 C  CD1   . ILE A 201 ? 1.13394 0.86227 1.13499 0.04495  -0.23368 -0.01351 280 ILE B CD1   
1561 N  N     . GLY A 202 ? 1.22981 0.91854 1.35623 0.00984  -0.29541 -0.00478 281 GLY B N     
1562 C  CA    . GLY A 202 ? 1.25824 0.95181 1.41706 -0.00706 -0.29551 0.01419  281 GLY B CA    
1563 C  C     . GLY A 202 ? 1.28107 0.98696 1.46318 -0.02131 -0.29524 0.02346  281 GLY B C     
1564 O  O     . GLY A 202 ? 1.17044 0.88548 1.37788 -0.03617 -0.29182 0.04178  281 GLY B O     
1565 N  N     . ASN A 203 ? 1.15473 0.86205 1.32926 -0.01682 -0.29867 0.01186  282 ASN B N     
1566 C  CA    . ASN A 203 ? 1.20901 0.93060 1.40550 -0.02965 -0.29708 0.02050  282 ASN B CA    
1567 C  C     . ASN A 203 ? 1.18296 0.93063 1.36804 -0.03719 -0.27380 0.03410  282 ASN B C     
1568 O  O     . ASN A 203 ? 1.22093 0.98455 1.42850 -0.05088 -0.26837 0.04807  282 ASN B O     
1569 C  CB    . ASN A 203 ? 1.30490 1.01970 1.49752 -0.02188 -0.30917 0.00351  282 ASN B CB    
1570 C  CG    . ASN A 203 ? 1.40930 1.09807 1.61257 -0.01354 -0.33383 -0.01213 282 ASN B CG    
1571 O  OD1   . ASN A 203 ? 1.51155 1.18726 1.73437 -0.01671 -0.34370 -0.00829 282 ASN B OD1   
1572 N  ND2   . ASN A 203 ? 1.38178 1.06242 1.57227 -0.00238 -0.34472 -0.03019 282 ASN B ND2   
1573 N  N     . LEU A 204 ? 1.11354 0.86645 1.26486 -0.02827 -0.26009 0.03015  283 LEU B N     
1574 C  CA    . LEU A 204 ? 1.09625 0.87227 1.23586 -0.03450 -0.23910 0.04139  283 LEU B CA    
1575 C  C     . LEU A 204 ? 1.09952 0.88551 1.25367 -0.04630 -0.23095 0.06026  283 LEU B C     
1576 O  O     . LEU A 204 ? 1.15600 0.94503 1.29293 -0.04353 -0.22102 0.06423  283 LEU B O     
1577 C  CB    . LEU A 204 ? 1.15142 0.92888 1.25376 -0.02219 -0.22808 0.03270  283 LEU B CB    
1578 C  CG    . LEU A 204 ? 0.91526 0.68045 0.99828 -0.00770 -0.23673 0.01402  283 LEU B CG    
1579 C  CD1   . LEU A 204 ? 0.96941 0.73956 1.01788 0.00249  -0.22320 0.00963  283 LEU B CD1   
1580 C  CD2   . LEU A 204 ? 1.07435 0.84460 1.16824 -0.01106 -0.24158 0.01055  283 LEU B CD2   
1581 N  N     . SER A 205 ? 1.16117 0.95300 1.34766 -0.05944 -0.23535 0.07263  284 SER B N     
1582 C  CA    . SER A 205 ? 1.07381 0.87497 1.27557 -0.07077 -0.22895 0.09208  284 SER B CA    
1583 C  C     . SER A 205 ? 1.07327 0.89921 1.25965 -0.07573 -0.20762 0.10288  284 SER B C     
1584 O  O     . SER A 205 ? 1.17223 1.00549 1.35944 -0.08121 -0.20027 0.11656  284 SER B O     
1585 C  CB    . SER A 205 ? 1.00933 0.81216 1.25089 -0.08383 -0.23862 0.10388  284 SER B CB    
1586 O  OG    . SER A 205 ? 1.17681 0.99593 1.42787 -0.08940 -0.23410 0.10483  284 SER B OG    
1587 N  N     . SER A 206 ? 1.02890 0.86742 1.20154 -0.07358 -0.19840 0.09678  285 SER B N     
1588 C  CA    . SER A 206 ? 1.05340 0.91371 1.20954 -0.07657 -0.17927 0.10392  285 SER B CA    
1589 C  C     . SER A 206 ? 1.01820 0.87450 1.14123 -0.06591 -0.17172 0.09529  285 SER B C     
1590 O  O     . SER A 206 ? 0.94064 0.81306 1.04870 -0.06748 -0.15693 0.09958  285 SER B O     
1591 C  CB    . SER A 206 ? 0.91290 0.78920 1.07252 -0.07951 -0.17298 0.10192  285 SER B CB    
1592 O  OG    . SER A 206 ? 1.13873 1.02799 1.32889 -0.09173 -0.17373 0.11513  285 SER B OG    
1593 N  N     . LEU A 207 ? 0.89388 0.72988 1.00593 -0.05493 -0.18159 0.08320  286 LEU B N     
1594 C  CA    . LEU A 207 ? 0.97985 0.81313 1.06248 -0.04464 -0.17429 0.07596  286 LEU B CA    
1595 C  C     . LEU A 207 ? 1.02553 0.86762 1.10430 -0.04909 -0.16482 0.08826  286 LEU B C     
1596 O  O     . LEU A 207 ? 1.13484 0.96942 1.22699 -0.05183 -0.17166 0.09533  286 LEU B O     
1597 C  CB    . LEU A 207 ? 1.00403 0.81502 1.07817 -0.03173 -0.18727 0.06165  286 LEU B CB    
1598 C  CG    . LEU A 207 ? 1.00971 0.81816 1.05424 -0.01970 -0.18020 0.05357  286 LEU B CG    
1599 C  CD1   . LEU A 207 ? 0.87827 0.69488 0.90382 -0.01540 -0.17159 0.04677  286 LEU B CD1   
1600 C  CD2   . LEU A 207 ? 0.93777 0.72548 0.97718 -0.00717 -0.19334 0.04139  286 LEU B CD2   
1601 N  N     . SER A 208 ? 0.82850 0.68615 0.88977 -0.04973 -0.14995 0.09075  287 SER B N     
1602 C  CA    . SER A 208 ? 0.92049 0.78798 0.97555 -0.05323 -0.14081 0.10121  287 SER B CA    
1603 C  C     . SER A 208 ? 0.95593 0.82106 0.98643 -0.04360 -0.13476 0.09414  287 SER B C     
1604 O  O     . SER A 208 ? 1.03861 0.90675 1.06553 -0.04420 -0.13125 0.10092  287 SER B O     
1605 C  CB    . SER A 208 ? 0.96352 0.85400 1.02111 -0.06339 -0.12838 0.11187  287 SER B CB    
1606 O  OG    . SER A 208 ? 0.87314 0.77173 0.91561 -0.06023 -0.11995 0.10376  287 SER B OG    
1607 N  N     . ARG A 209 ? 0.90209 0.76278 0.91660 -0.03489 -0.13349 0.08174  288 ARG B N     
1608 C  CA    . ARG A 209 ? 0.82531 0.68515 0.81788 -0.02587 -0.12710 0.07593  288 ARG B CA    
1609 C  C     . ARG A 209 ? 0.93783 0.78173 0.92072 -0.01338 -0.13523 0.06220  288 ARG B C     
1610 O  O     . ARG A 209 ? 0.92137 0.76226 0.90337 -0.01138 -0.13861 0.05517  288 ARG B O     
1611 C  CB    . ARG A 209 ? 0.82402 0.69941 0.80404 -0.02857 -0.11381 0.07691  288 ARG B CB    
1612 C  CG    . ARG A 209 ? 0.87839 0.75509 0.83869 -0.02106 -0.10635 0.07307  288 ARG B CG    
1613 C  CD    . ARG A 209 ? 0.89796 0.78936 0.84994 -0.02536 -0.09463 0.07483  288 ARG B CD    
1614 N  NE    . ARG A 209 ? 0.89278 0.78610 0.82900 -0.01943 -0.08769 0.07249  288 ARG B NE    
1615 C  CZ    . ARG A 209 ? 1.06926 0.95722 0.99271 -0.01112 -0.08634 0.06491  288 ARG B CZ    
1616 N  NH1   . ARG A 209 ? 0.92335 0.80313 0.84590 -0.00702 -0.09192 0.05797  288 ARG B NH1   
1617 N  NH2   . ARG A 209 ? 1.09401 0.98555 1.00589 -0.00684 -0.07942 0.06500  288 ARG B NH2   
1618 N  N     . LEU A 210 ? 0.86094 0.69542 0.83636 -0.00433 -0.13856 0.05820  289 LEU B N     
1619 C  CA    . LEU A 210 ? 0.94467 0.76431 0.90977 0.00912  -0.14686 0.04477  289 LEU B CA    
1620 C  C     . LEU A 210 ? 0.95858 0.78056 0.90375 0.01921  -0.13903 0.04158  289 LEU B C     
1621 O  O     . LEU A 210 ? 1.00348 0.82567 0.95063 0.02056  -0.13807 0.04569  289 LEU B O     
1622 C  CB    . LEU A 210 ? 0.93089 0.73396 0.91155 0.01162  -0.16258 0.04128  289 LEU B CB    
1623 C  CG    . LEU A 210 ? 0.88970 0.67653 0.85946 0.02697  -0.17298 0.02574  289 LEU B CG    
1624 C  CD1   . LEU A 210 ? 1.01363 0.79894 0.97420 0.03088  -0.17521 0.01661  289 LEU B CD1   
1625 C  CD2   . LEU A 210 ? 0.95083 0.72062 0.93905 0.02845  -0.18951 0.02248  289 LEU B CD2   
1626 N  N     . GLY A 211 ? 0.85103 0.67532 0.77821 0.02632  -0.13357 0.03504  290 GLY B N     
1627 C  CA    . GLY A 211 ? 0.86668 0.69479 0.77584 0.03594  -0.12543 0.03288  290 GLY B CA    
1628 C  C     . GLY A 211 ? 1.02282 0.83830 0.92093 0.05155  -0.13336 0.02093  290 GLY B C     
1629 O  O     . GLY A 211 ? 1.03821 0.84759 0.92667 0.05841  -0.13789 0.01224  290 GLY B O     
1630 N  N     . LEU A 212 ? 1.11071 0.92254 1.00966 0.05808  -0.13546 0.01995  291 LEU B N     
1631 C  CA    . LEU A 212 ? 1.03430 0.83465 0.92281 0.07431  -0.14325 0.00754  291 LEU B CA    
1632 C  C     . LEU A 212 ? 0.97094 0.77953 0.84423 0.08506  -0.13329 0.00711  291 LEU B C     
1633 O  O     . LEU A 212 ? 1.00488 0.80649 0.86702 0.10028  -0.13797 -0.00351 291 LEU B O     
1634 C  CB    . LEU A 212 ? 0.98123 0.76656 0.88688 0.07526  -0.15817 0.00382  291 LEU B CB    
1635 C  CG    . LEU A 212 ? 0.99253 0.76821 0.91671 0.06574  -0.17033 0.00376  291 LEU B CG    
1636 C  CD1   . LEU A 212 ? 0.99971 0.75972 0.94186 0.06740  -0.18525 0.00078  291 LEU B CD1   
1637 C  CD2   . LEU A 212 ? 1.04562 0.81554 0.95926 0.07169  -0.17595 -0.00704 291 LEU B CD2   
1638 N  N     . ARG A 213 ? 1.04611 0.86997 0.91911 0.07809  -0.12002 0.01789  292 ARG B N     
1639 C  CA    . ARG A 213 ? 0.96463 0.79747 0.82851 0.08705  -0.11118 0.01899  292 ARG B CA    
1640 C  C     . ARG A 213 ? 1.02676 0.86403 0.86888 0.09908  -0.10446 0.01339  292 ARG B C     
1641 O  O     . ARG A 213 ? 1.09797 0.93524 0.93199 0.09704  -0.10306 0.01243  292 ARG B O     
1642 C  CB    . ARG A 213 ? 1.01619 0.86428 0.88765 0.07563  -0.10011 0.03204  292 ARG B CB    
1643 C  CG    . ARG A 213 ? 0.99555 0.85481 0.86187 0.06668  -0.08978 0.03835  292 ARG B CG    
1644 C  CD    . ARG A 213 ? 0.97850 0.85311 0.84912 0.06022  -0.07908 0.04849  292 ARG B CD    
1645 N  NE    . ARG A 213 ? 1.04138 0.92404 0.91691 0.04628  -0.07377 0.05579  292 ARG B NE    
1646 C  CZ    . ARG A 213 ? 1.16533 1.05738 1.03393 0.04380  -0.06422 0.05891  292 ARG B CZ    
1647 N  NH1   . ARG A 213 ? 1.24963 1.14525 1.10619 0.05348  -0.05803 0.05716  292 ARG B NH1   
1648 N  NH2   . ARG A 213 ? 1.21028 1.10861 1.08457 0.03160  -0.06085 0.06415  292 ARG B NH2   
1649 N  N     . TYR A 214 ? 1.05346 0.89515 0.88650 0.11225  -0.10032 0.01015  293 TYR B N     
1650 C  CA    . TYR A 214 ? 1.08679 0.93491 0.89850 0.12561  -0.09290 0.00601  293 TYR B CA    
1651 C  C     . TYR A 214 ? 1.11890 0.95383 0.91743 0.13559  -0.10329 -0.00663 293 TYR B C     
1652 O  O     . TYR A 214 ? 1.03506 0.87150 0.82208 0.13517  -0.10059 -0.00638 293 TYR B O     
1653 C  CB    . TYR A 214 ? 0.94834 0.81174 0.75544 0.11761  -0.07846 0.01720  293 TYR B CB    
1654 C  CG    . TYR A 214 ? 1.13101 1.00962 0.94549 0.11450  -0.06746 0.02688  293 TYR B CG    
1655 C  CD1   . TYR A 214 ? 1.15395 1.03658 0.98600 0.09976  -0.06653 0.03555  293 TYR B CD1   
1656 C  CD2   . TYR A 214 ? 1.14812 1.03806 0.95234 0.12687  -0.05837 0.02728  293 TYR B CD2   
1657 C  CE1   . TYR A 214 ? 1.27619 1.17275 1.11561 0.09714  -0.05786 0.04381  293 TYR B CE1   
1658 C  CE2   . TYR A 214 ? 1.23378 1.13849 1.04714 0.12395  -0.04895 0.03616  293 TYR B CE2   
1659 C  CZ    . TYR A 214 ? 1.30031 1.20772 1.13144 0.10899  -0.04933 0.04406  293 TYR B CZ    
1660 O  OH    . TYR A 214 ? 1.24532 1.16752 1.08603 0.10620  -0.04118 0.05240  293 TYR B OH    
1661 N  N     . ASN A 215 ? 1.11307 0.93439 0.91411 0.14504  -0.11632 -0.01812 294 ASN B N     
1662 C  CA    . ASN A 215 ? 1.10446 0.91277 0.89227 0.15759  -0.12803 -0.03267 294 ASN B CA    
1663 C  C     . ASN A 215 ? 1.10439 0.90888 0.88274 0.17686  -0.13241 -0.04466 294 ASN B C     
1664 O  O     . ASN A 215 ? 1.22544 1.04269 0.99994 0.18308  -0.12145 -0.04056 294 ASN B O     
1665 C  CB    . ASN A 215 ? 1.15131 0.94297 0.95553 0.14835  -0.14405 -0.03706 294 ASN B CB    
1666 C  CG    . ASN A 215 ? 1.14039 0.93548 0.94829 0.13412  -0.14105 -0.02940 294 ASN B CG    
1667 O  OD1   . ASN A 215 ? 1.09360 0.89519 0.88481 0.13755  -0.13431 -0.02873 294 ASN B OD1   
1668 N  ND2   . ASN A 215 ? 1.09594 0.88722 0.92607 0.11849  -0.14594 -0.02316 294 ASN B ND2   
1669 N  N     . ARG A 216 ? 1.12296 0.91033 0.89839 0.18681  -0.14882 -0.06004 295 ARG B N     
1670 C  CA    . ARG A 216 ? 1.18387 0.96477 0.95151 0.20607  -0.15589 -0.07426 295 ARG B CA    
1671 C  C     . ARG A 216 ? 1.23259 0.99128 1.01922 0.20505  -0.17646 -0.08455 295 ARG B C     
1672 O  O     . ARG A 216 ? 1.22034 0.96655 0.99897 0.22136  -0.18916 -0.10161 295 ARG B O     
1673 C  CB    . ARG A 216 ? 1.20841 0.99190 0.94596 0.22524  -0.15515 -0.08593 295 ARG B CB    
1674 C  CG    . ARG A 216 ? 1.24830 1.05331 0.96774 0.22600  -0.13526 -0.07431 295 ARG B CG    
1675 C  CD    . ARG A 216 ? 1.37650 1.18320 1.06591 0.24313  -0.13580 -0.08411 295 ARG B CD    
1676 N  NE    . ARG A 216 ? 1.48151 1.30607 1.15720 0.23965  -0.11871 -0.07038 295 ARG B NE    
1677 C  CZ    . ARG A 216 ? 1.49496 1.33859 1.15664 0.24901  -0.10247 -0.06385 295 ARG B CZ    
1678 N  NH1   . ARG A 216 ? 1.59520 1.44427 1.25320 0.26355  -0.10009 -0.07038 295 ARG B NH1   
1679 N  NH2   . ARG A 216 ? 1.51620 1.37414 1.16875 0.24373  -0.08837 -0.05009 295 ARG B NH2   
1680 N  N     . LEU A 217 ? 1.12879 0.88264 0.94094 0.18614  -0.18016 -0.07418 296 LEU B N     
1681 C  CA    . LEU A 217 ? 1.22696 0.96007 1.06077 0.18227  -0.19958 -0.08084 296 LEU B CA    
1682 C  C     . LEU A 217 ? 1.30861 1.03365 1.14992 0.19370  -0.20647 -0.08824 296 LEU B C     
1683 O  O     . LEU A 217 ? 1.27831 1.01544 1.12113 0.19459  -0.19502 -0.08025 296 LEU B O     
1684 C  CB    . LEU A 217 ? 1.17823 0.91192 1.03722 0.15914  -0.19918 -0.06511 296 LEU B CB    
1685 C  CG    . LEU A 217 ? 1.20148 0.94133 1.05819 0.14669  -0.19463 -0.05837 296 LEU B CG    
1686 C  CD1   . LEU A 217 ? 1.21129 0.95384 1.09297 0.12539  -0.19327 -0.04298 296 LEU B CD1   
1687 C  CD2   . LEU A 217 ? 1.22782 0.95338 1.07912 0.15344  -0.20990 -0.07282 296 LEU B CD2   
1688 N  N     . SER A 218 ? 1.28865 0.99271 1.13608 0.20262  -0.22624 -0.10401 297 SER B N     
1689 C  CA    . SER A 218 ? 1.28238 0.97488 1.14003 0.21364  -0.23613 -0.11271 297 SER B CA    
1690 C  C     . SER A 218 ? 1.25434 0.92964 1.14556 0.19982  -0.25105 -0.10736 297 SER B C     
1691 O  O     . SER A 218 ? 1.28927 0.95509 1.19350 0.20603  -0.25865 -0.11088 297 SER B O     
1692 C  CB    . SER A 218 ? 1.26618 0.94655 1.10560 0.23719  -0.24872 -0.13668 297 SER B CB    
1693 O  OG    . SER A 218 ? 1.40194 1.09945 1.20915 0.25069  -0.23452 -0.14052 297 SER B OG    
1694 N  N     . ALA A 219 ? 1.20968 0.88140 1.11596 0.18159  -0.25521 -0.09832 298 ALA B N     
1695 C  CA    . ALA A 219 ? 1.14471 0.80224 1.08398 0.16700  -0.26826 -0.09054 298 ALA B CA    
1696 C  C     . ALA A 219 ? 1.29398 0.95877 1.24431 0.14585  -0.26375 -0.07575 298 ALA B C     
1697 O  O     . ALA A 219 ? 1.40028 1.07577 1.33357 0.14457  -0.25522 -0.07589 298 ALA B O     
1698 C  CB    . ALA A 219 ? 1.08607 0.71721 1.03733 0.17640  -0.29292 -0.10842 298 ALA B CB    
1699 N  N     . ILE A 220 ? 1.26119 0.92053 1.24046 0.12981  -0.26952 -0.06265 299 ILE B N     
1700 C  CA    . ILE A 220 ? 1.12069 0.78677 1.11490 0.10949  -0.26655 -0.04809 299 ILE B CA    
1701 C  C     . ILE A 220 ? 1.24666 0.89233 1.26693 0.10400  -0.28792 -0.05269 299 ILE B C     
1702 O  O     . ILE A 220 ? 1.25433 0.88373 1.29394 0.10601  -0.30152 -0.05455 299 ILE B O     
1703 C  CB    . ILE A 220 ? 1.16433 0.84480 1.17093 0.09400  -0.25380 -0.02626 299 ILE B CB    
1704 C  CG1   . ILE A 220 ? 1.16774 0.86903 1.15051 0.09827  -0.23326 -0.02171 299 ILE B CG1   
1705 C  CG2   . ILE A 220 ? 0.99651 0.68333 1.02053 0.07403  -0.25231 -0.01207 299 ILE B CG2   
1706 C  CD1   . ILE A 220 ? 1.02690 0.74105 0.98813 0.09849  -0.22206 -0.02416 299 ILE B CD1   
1707 N  N     . PRO A 221 ? 1.21677 0.86227 1.24008 0.09726  -0.29224 -0.05461 300 PRO B N     
1708 C  CA    . PRO A 221 ? 1.27804 0.90510 1.32960 0.09092  -0.31311 -0.05817 300 PRO B CA    
1709 C  C     . PRO A 221 ? 1.21511 0.84145 1.29964 0.07309  -0.31502 -0.03850 300 PRO B C     
1710 O  O     . PRO A 221 ? 1.19426 0.83911 1.28086 0.05976  -0.29913 -0.01998 300 PRO B O     
1711 C  CB    . PRO A 221 ? 1.25674 0.89092 1.30368 0.08521  -0.31206 -0.06004 300 PRO B CB    
1712 C  CG    . PRO A 221 ? 1.21745 0.86631 1.22784 0.09624  -0.29600 -0.06564 300 PRO B CG    
1713 C  CD    . PRO A 221 ? 1.21954 0.88088 1.22121 0.09640  -0.27946 -0.05475 300 PRO B CD    
1714 N  N     . ARG A 222 ? 1.28645 0.89102 1.39694 0.07330  -0.33522 -0.04262 301 ARG B N     
1715 C  CA    . ARG A 222 ? 1.32105 0.92356 1.46512 0.05628  -0.33877 -0.02281 301 ARG B CA    
1716 C  C     . ARG A 222 ? 1.27667 0.89290 1.43710 0.03675  -0.33331 -0.00703 301 ARG B C     
1717 O  O     . ARG A 222 ? 1.26516 0.89092 1.44430 0.02129  -0.32676 0.01426  301 ARG B O     
1718 C  CB    . ARG A 222 ? 1.34299 0.91750 1.51457 0.05986  -0.36370 -0.03093 301 ARG B CB    
1719 C  CG    . ARG A 222 ? 1.49716 1.06802 1.69995 0.04621  -0.36666 -0.01009 301 ARG B CG    
1720 C  CD    . ARG A 222 ? 1.60783 1.15662 1.84984 0.03819  -0.39024 -0.00938 301 ARG B CD    
1721 N  NE    . ARG A 222 ? 1.74884 1.27090 2.00143 0.05117  -0.40958 -0.02278 301 ARG B NE    
1722 C  CZ    . ARG A 222 ? 1.83839 1.33691 2.09861 0.06169  -0.43176 -0.04439 301 ARG B CZ    
1723 N  NH1   . ARG A 222 ? 1.65230 1.15035 1.91132 0.06061  -0.43827 -0.05488 301 ARG B NH1   
1724 N  NH2   . ARG A 222 ? 1.79951 1.27418 2.06933 0.07402  -0.44865 -0.05630 301 ARG B NH2   
1725 N  N     . SER A 223 ? 1.35823 0.97685 1.51140 0.03780  -0.33556 -0.01689 302 SER B N     
1726 C  CA    . SER A 223 ? 1.35983 0.99256 1.52856 0.02077  -0.33044 -0.00367 302 SER B CA    
1727 C  C     . SER A 223 ? 1.29596 0.95571 1.45000 0.01194  -0.30586 0.01266  302 SER B C     
1728 O  O     . SER A 223 ? 1.27705 0.95094 1.44581 -0.00308 -0.29965 0.02650  302 SER B O     
1729 C  CB    . SER A 223 ? 1.27641 0.90529 1.43834 0.02630  -0.33900 -0.01988 302 SER B CB    
1730 O  OG    . SER A 223 ? 1.32728 0.96198 1.45086 0.04158  -0.32944 -0.03354 302 SER B OG    
1731 N  N     . LEU A 224 ? 1.26821 0.93599 1.39475 0.02105  -0.29210 0.01112  303 LEU B N     
1732 C  CA    . LEU A 224 ? 1.24977 0.94195 1.36402 0.01262  -0.27029 0.02612  303 LEU B CA    
1733 C  C     . LEU A 224 ? 1.21513 0.91498 1.35310 -0.00326 -0.26662 0.04828  303 LEU B C     
1734 O  O     . LEU A 224 ? 1.27923 1.00013 1.41301 -0.01338 -0.25069 0.06211  303 LEU B O     
1735 C  CB    . LEU A 224 ? 1.08070 0.77882 1.16409 0.02564  -0.25811 0.02001  303 LEU B CB    
1736 C  CG    . LEU A 224 ? 1.11112 0.83361 1.17714 0.01956  -0.23641 0.03065  303 LEU B CG    
1737 C  CD1   . LEU A 224 ? 1.13728 0.86906 1.19603 0.01612  -0.23160 0.02730  303 LEU B CD1   
1738 C  CD2   . LEU A 224 ? 1.10269 0.83029 1.14235 0.03213  -0.22590 0.02516  303 LEU B CD2   
1739 N  N     . ALA A 225 ? 1.25449 0.93767 1.41730 -0.00534 -0.28147 0.05199  304 ALA B N     
1740 C  CA    . ALA A 225 ? 1.27089 0.96077 1.45835 -0.02092 -0.27943 0.07471  304 ALA B CA    
1741 C  C     . ALA A 225 ? 1.18485 0.88819 1.39140 -0.03712 -0.27637 0.08739  304 ALA B C     
1742 O  O     . ALA A 225 ? 1.19703 0.91384 1.41801 -0.05068 -0.26902 0.10826  304 ALA B O     
1743 C  CB    . ALA A 225 ? 1.17605 0.84256 1.38897 -0.01951 -0.29835 0.07550  304 ALA B CB    
1744 N  N     . LYS A 226 ? 1.15178 0.85291 1.35869 -0.03552 -0.28178 0.07549  305 LYS B N     
1745 C  CA    . LYS A 226 ? 1.17731 0.89324 1.40218 -0.04976 -0.27812 0.08629  305 LYS B CA    
1746 C  C     . LYS A 226 ? 1.26104 1.00364 1.46463 -0.05371 -0.25619 0.09284  305 LYS B C     
1747 O  O     . LYS A 226 ? 1.18139 0.94111 1.39945 -0.06650 -0.24931 0.10588  305 LYS B O     
1748 C  CB    . LYS A 226 ? 1.19921 0.90300 1.43351 -0.04612 -0.29317 0.07059  305 LYS B CB    
1749 C  CG    . LYS A 226 ? 1.15007 0.82650 1.40852 -0.04272 -0.31724 0.06255  305 LYS B CG    
1750 C  CD    . LYS A 226 ? 1.17584 0.84198 1.44353 -0.03953 -0.33255 0.04675  305 LYS B CD    
1751 C  CE    . LYS A 226 ? 1.27302 0.91074 1.56578 -0.03588 -0.35818 0.03727  305 LYS B CE    
1752 N  NZ    . LYS A 226 ? 1.24191 0.86981 1.54550 -0.03330 -0.37474 0.02175  305 LYS B NZ    
1753 N  N     . CYS A 227 ? 1.16890 0.91575 1.33977 -0.04287 -0.24531 0.08404  306 CYS B N     
1754 C  CA    . CYS A 227 ? 1.10855 0.87886 1.25909 -0.04588 -0.22542 0.08922  306 CYS B CA    
1755 C  C     . CYS A 227 ? 1.04325 0.82764 1.19391 -0.05374 -0.21365 0.10733  306 CYS B C     
1756 O  O     . CYS A 227 ? 1.07853 0.87037 1.20644 -0.04851 -0.20246 0.10668  306 CYS B O     
1757 C  CB    . CYS A 227 ? 1.18116 0.94966 1.29885 -0.03136 -0.21977 0.07255  306 CYS B CB    
1758 S  SG    . CYS A 227 ? 1.12347 0.87525 1.23607 -0.01974 -0.23417 0.05059  306 CYS B SG    
1759 N  N     . SER A 228 ? 1.10516 0.89369 1.28301 -0.06666 -0.21681 0.12432  307 SER B N     
1760 C  CA    . SER A 228 ? 1.07455 0.87566 1.25612 -0.07492 -0.20817 0.14361  307 SER B CA    
1761 C  C     . SER A 228 ? 1.00771 0.83566 1.17244 -0.08018 -0.18869 0.15129  307 SER B C     
1762 O  O     . SER A 228 ? 1.04230 0.88345 1.20905 -0.08744 -0.18103 0.16773  307 SER B O     
1763 C  CB    . SER A 228 ? 1.12769 0.92653 1.34427 -0.08755 -0.21720 0.16080  307 SER B CB    
1764 O  OG    . SER A 228 ? 1.17730 0.98629 1.41054 -0.09638 -0.21677 0.16411  307 SER B OG    
1765 N  N     . ALA A 229 ? 0.92068 0.75677 1.06922 -0.07648 -0.18121 0.14008  308 ALA B N     
1766 C  CA    . ALA A 229 ? 0.96590 0.82516 1.09675 -0.07951 -0.16373 0.14429  308 ALA B CA    
1767 C  C     . ALA A 229 ? 0.95347 0.81233 1.05498 -0.06916 -0.15618 0.13452  308 ALA B C     
1768 O  O     . ALA A 229 ? 0.91603 0.79242 1.00227 -0.07102 -0.14262 0.13719  308 ALA B O     
1769 C  CB    . ALA A 229 ? 0.90969 0.77933 1.04278 -0.08230 -0.15972 0.13915  308 ALA B CB    
1770 N  N     . LEU A 230 ? 0.86385 0.70373 0.95815 -0.05816 -0.16481 0.12322  309 LEU B N     
1771 C  CA    . LEU A 230 ? 0.99906 0.83926 1.06777 -0.04806 -0.15771 0.11470  309 LEU B CA    
1772 C  C     . LEU A 230 ? 0.98650 0.84002 1.04953 -0.05230 -0.14834 0.12717  309 LEU B C     
1773 O  O     . LEU A 230 ? 0.99721 0.84745 1.07351 -0.05622 -0.15346 0.13820  309 LEU B O     
1774 C  CB    . LEU A 230 ? 0.87093 0.68961 0.93593 -0.03531 -0.16917 0.10205  309 LEU B CB    
1775 C  CG    . LEU A 230 ? 0.96435 0.77204 1.01991 -0.02545 -0.17481 0.08459  309 LEU B CG    
1776 C  CD1   . LEU A 230 ? 0.99495 0.78267 1.04665 -0.01213 -0.18624 0.07262  309 LEU B CD1   
1777 C  CD2   . LEU A 230 ? 0.98867 0.80895 1.02052 -0.02172 -0.16138 0.07900  309 LEU B CD2   
1778 N  N     . GLU A 231 ? 0.97670 0.84484 1.02051 -0.05140 -0.13540 0.12540  310 GLU B N     
1779 C  CA    . GLU A 231 ? 1.04296 0.92421 1.07885 -0.05422 -0.12689 0.13490  310 GLU B CA    
1780 C  C     . GLU A 231 ? 0.98606 0.86140 1.00709 -0.04365 -0.12596 0.12757  310 GLU B C     
1781 O  O     . GLU A 231 ? 1.05483 0.93861 1.07173 -0.04498 -0.12150 0.13515  310 GLU B O     
1782 C  CB    . GLU A 231 ? 1.07016 0.97239 1.09610 -0.06037 -0.11381 0.13787  310 GLU B CB    
1783 C  CG    . GLU A 231 ? 1.12490 1.03685 1.16482 -0.07010 -0.11265 0.14494  310 GLU B CG    
1784 C  CD    . GLU A 231 ? 1.26148 1.19432 1.29070 -0.07455 -0.09985 0.14620  310 GLU B CD    
1785 O  OE1   . GLU A 231 ? 1.22994 1.17119 1.24382 -0.07275 -0.09257 0.14589  310 GLU B OE1   
1786 O  OE2   . GLU A 231 ? 1.24601 1.18699 1.28314 -0.07952 -0.09757 0.14696  310 GLU B OE2   
1787 N  N     . GLU A 232 ? 0.93987 0.80215 0.95296 -0.03291 -0.13005 0.11341  311 GLU B N     
1788 C  CA    . GLU A 232 ? 0.90282 0.76173 0.90188 -0.02207 -0.12789 0.10640  311 GLU B CA    
1789 C  C     . GLU A 232 ? 0.89551 0.73621 0.89220 -0.01013 -0.13714 0.09252  311 GLU B C     
1790 O  O     . GLU A 232 ? 1.10092 0.93705 1.09498 -0.00844 -0.13930 0.08432  311 GLU B O     
1791 C  CB    . GLU A 232 ? 0.88927 0.76263 0.87040 -0.02141 -0.11483 0.10365  311 GLU B CB    
1792 C  CG    . GLU A 232 ? 1.08491 0.95646 1.05254 -0.01017 -0.11161 0.09650  311 GLU B CG    
1793 C  CD    . GLU A 232 ? 1.25813 1.14333 1.21120 -0.01067 -0.09948 0.09486  311 GLU B CD    
1794 O  OE1   . GLU A 232 ? 1.31576 1.21227 1.26899 -0.01985 -0.09372 0.09955  311 GLU B OE1   
1795 O  OE2   . GLU A 232 ? 1.16121 1.04611 1.10348 -0.00167 -0.09579 0.08897  311 GLU B OE2   
1796 N  N     . LEU A 233 ? 0.90996 0.74080 0.90728 -0.00120 -0.14293 0.08945  312 LEU B N     
1797 C  CA    . LEU A 233 ? 0.89278 0.70725 0.88524 0.01248  -0.15152 0.07493  312 LEU B CA    
1798 C  C     . LEU A 233 ? 0.97468 0.79439 0.95010 0.02372  -0.14382 0.06954  312 LEU B C     
1799 O  O     . LEU A 233 ? 1.06515 0.88511 1.04428 0.02707  -0.14457 0.07335  312 LEU B O     
1800 C  CB    . LEU A 233 ? 0.94984 0.74663 0.96090 0.01433  -0.16691 0.07482  312 LEU B CB    
1801 C  CG    . LEU A 233 ? 0.97317 0.75112 0.98104 0.02847  -0.17860 0.05809  312 LEU B CG    
1802 C  CD1   . LEU A 233 ? 0.99385 0.76832 0.99801 0.02789  -0.18143 0.04965  312 LEU B CD1   
1803 C  CD2   . LEU A 233 ? 0.79098 0.55096 0.81956 0.02992  -0.19445 0.05860  312 LEU B CD2   
1804 N  N     . ASN A 234 ? 1.03980 0.86447 0.99776 0.02943  -0.13637 0.06160  313 ASN B N     
1805 C  CA    . ASN A 234 ? 0.96629 0.79889 0.90848 0.03913  -0.12718 0.05794  313 ASN B CA    
1806 C  C     . ASN A 234 ? 1.03932 0.86106 0.96914 0.05453  -0.13179 0.04327  313 ASN B C     
1807 O  O     . ASN A 234 ? 0.97999 0.80138 0.89898 0.05646  -0.12991 0.03729  313 ASN B O     
1808 C  CB    . ASN A 234 ? 0.86059 0.71022 0.79304 0.03217  -0.11344 0.06328  313 ASN B CB    
1809 C  CG    . ASN A 234 ? 0.87776 0.73690 0.79698 0.04069  -0.10365 0.06141  313 ASN B CG    
1810 O  OD1   . ASN A 234 ? 1.00043 0.85557 0.91733 0.05210  -0.10594 0.05667  313 ASN B OD1   
1811 N  ND2   . ASN A 234 ? 0.87946 0.75172 0.79129 0.03527  -0.09276 0.06527  313 ASN B ND2   
1812 N  N     . LEU A 235 ? 1.02234 0.83571 0.95324 0.06620  -0.13799 0.03733  314 LEU B N     
1813 C  CA    . LEU A 235 ? 0.98467 0.78789 0.90312 0.08291  -0.14332 0.02234  314 LEU B CA    
1814 C  C     . LEU A 235 ? 1.01950 0.83426 0.92267 0.09483  -0.13238 0.01996  314 LEU B C     
1815 O  O     . LEU A 235 ? 1.09979 0.90833 0.99703 0.11020  -0.13666 0.00986  314 LEU B O     
1816 C  CB    . LEU A 235 ? 0.94920 0.73329 0.88061 0.08930  -0.15980 0.01507  314 LEU B CB    
1817 C  CG    . LEU A 235 ? 1.10484 0.87841 1.05861 0.07608  -0.17116 0.02144  314 LEU B CG    
1818 C  CD1   . LEU A 235 ? 0.86252 0.61712 0.83099 0.08319  -0.18727 0.01535  314 LEU B CD1   
1819 C  CD2   . LEU A 235 ? 1.00279 0.77240 0.95539 0.07063  -0.17482 0.01761  314 LEU B CD2   
1820 N  N     . GLU A 236 ? 0.97593 0.80815 0.87356 0.08807  -0.11830 0.02912  315 GLU B N     
1821 C  CA    . GLU A 236 ? 1.05748 0.90320 0.94525 0.09697  -0.10717 0.02988  315 GLU B CA    
1822 C  C     . GLU A 236 ? 1.10195 0.94680 0.96999 0.11251  -0.10467 0.01882  315 GLU B C     
1823 O  O     . GLU A 236 ? 1.12947 0.97053 0.98749 0.11206  -0.10537 0.01475  315 GLU B O     
1824 C  CB    . GLU A 236 ? 1.09318 0.95672 0.98098 0.08515  -0.09400 0.04182  315 GLU B CB    
1825 C  CG    . GLU A 236 ? 1.09977 0.97894 0.98167 0.09226  -0.08244 0.04466  315 GLU B CG    
1826 C  CD    . GLU A 236 ? 1.15040 1.04559 1.03288 0.08055  -0.07084 0.05512  315 GLU B CD    
1827 O  OE1   . GLU A 236 ? 1.29579 1.19014 1.18291 0.06729  -0.07183 0.05980  315 GLU B OE1   
1828 O  OE2   . GLU A 236 ? 1.17009 1.07913 1.04925 0.08485  -0.06092 0.05844  315 GLU B OE2   
1829 N  N     . ASN A 237 ? 1.12950 0.97876 0.99193 0.12695  -0.10179 0.01416  316 ASN B N     
1830 C  CA    . ASN A 237 ? 1.08163 0.93511 0.92372 0.14336  -0.09652 0.00545  316 ASN B CA    
1831 C  C     . ASN A 237 ? 1.05166 0.88730 0.88427 0.15315  -0.10941 -0.00917 316 ASN B C     
1832 O  O     . ASN A 237 ? 1.07906 0.91282 0.89917 0.15290  -0.10898 -0.01201 316 ASN B O     
1833 C  CB    . ASN A 237 ? 1.03302 0.90249 0.86400 0.13836  -0.08179 0.01367  316 ASN B CB    
1834 C  CG    . ASN A 237 ? 1.17058 1.05206 0.98431 0.15438  -0.07175 0.01053  316 ASN B CG    
1835 O  OD1   . ASN A 237 ? 1.27421 1.17194 1.09125 0.15588  -0.06090 0.01779  316 ASN B OD1   
1836 N  ND2   . ASN A 237 ? 1.18002 1.05466 0.97547 0.16665  -0.07534 0.00006  316 ASN B ND2   
1837 N  N     . ASN A 238 ? 1.03332 0.85549 0.87293 0.16228  -0.12182 -0.01876 317 ASN B N     
1838 C  CA    . ASN A 238 ? 1.10907 0.91257 0.94240 0.17261  -0.13674 -0.03442 317 ASN B CA    
1839 C  C     . ASN A 238 ? 1.23380 1.03106 1.06557 0.19128  -0.14342 -0.04676 317 ASN B C     
1840 O  O     . ASN A 238 ? 1.22377 1.03462 1.05416 0.19838  -0.13354 -0.04347 317 ASN B O     
1841 C  CB    . ASN A 238 ? 1.14854 0.93593 1.00032 0.15804  -0.15036 -0.03278 317 ASN B CB    
1842 C  CG    . ASN A 238 ? 1.19247 0.98357 1.04013 0.14556  -0.14630 -0.02694 317 ASN B CG    
1843 O  OD1   . ASN A 238 ? 1.24595 1.02978 1.08173 0.15132  -0.15212 -0.03635 317 ASN B OD1   
1844 N  ND2   . ASN A 238 ? 0.99523 0.79784 0.85246 0.12914  -0.13678 -0.01200 317 ASN B ND2   
1845 N  N     . ASN A 239 ? 1.20606 0.98292 1.03910 0.19961  -0.16073 -0.06151 318 ASN B N     
1846 C  CA    A ASN A 239 ? 1.29981 1.06678 1.13181 0.21856  -0.17044 -0.07646 318 ASN B CA    
1847 C  CA    B ASN A 239 ? 1.28753 1.05460 1.11965 0.21849  -0.17037 -0.07635 318 ASN B CA    
1848 C  C     . ASN A 239 ? 1.25427 0.99806 1.11062 0.21300  -0.19013 -0.08050 318 ASN B C     
1849 O  O     . ASN A 239 ? 1.31472 1.04014 1.17037 0.22524  -0.20630 -0.09726 318 ASN B O     
1850 C  CB    A ASN A 239 ? 1.29597 1.06051 1.10147 0.23846  -0.17325 -0.09377 318 ASN B CB    
1851 C  CB    B ASN A 239 ? 1.30887 1.07371 1.11447 0.23868  -0.17302 -0.09370 318 ASN B CB    
1852 C  CG    A ASN A 239 ? 1.26139 1.02450 1.05927 0.26153  -0.17660 -0.10852 318 ASN B CG    
1853 C  CG    B ASN A 239 ? 1.24491 1.03331 1.02690 0.24423  -0.15319 -0.08780 318 ASN B CG    
1854 O  OD1   A ASN A 239 ? 1.28206 1.03454 1.09837 0.26372  -0.18611 -0.11175 318 ASN B OD1   
1855 O  OD1   B ASN A 239 ? 1.30746 1.11446 1.09187 0.24207  -0.13800 -0.07620 318 ASN B OD1   
1856 N  ND2   A ASN A 239 ? 1.28810 1.06244 1.05849 0.27949  -0.16873 -0.11736 318 ASN B ND2   
1857 N  ND2   B ASN A 239 ? 1.19734 0.98513 0.95734 0.25129  -0.15379 -0.09519 318 ASN B ND2   
1858 N  N     . ILE A 240 ? 1.18483 0.92935 1.06347 0.19421  -0.18935 -0.06471 319 ILE B N     
1859 C  CA    . ILE A 240 ? 1.26525 0.98979 1.16980 0.18548  -0.20650 -0.06378 319 ILE B CA    
1860 C  C     . ILE A 240 ? 1.26838 0.99154 1.18783 0.19013  -0.20861 -0.06089 319 ILE B C     
1861 O  O     . ILE A 240 ? 1.22009 0.96171 1.13710 0.18949  -0.19420 -0.05103 319 ILE B O     
1862 C  CB    . ILE A 240 ? 1.17925 0.90640 1.09845 0.16164  -0.20444 -0.04719 319 ILE B CB    
1863 C  CG1   . ILE A 240 ? 1.22071 0.95056 1.12521 0.15807  -0.20170 -0.05025 319 ILE B CG1   
1864 C  CG2   . ILE A 240 ? 1.19949 0.90729 1.14664 0.15205  -0.22167 -0.04423 319 ILE B CG2   
1865 C  CD1   . ILE A 240 ? 1.25895 0.99409 1.17597 0.13623  -0.19797 -0.03500 319 ILE B CD1   
1866 N  N     . SER A 241 ? 1.26984 0.97077 1.20611 0.19497  -0.22738 -0.06955 320 SER B N     
1867 C  CA    . SER A 241 ? 1.25248 0.94872 1.20525 0.20011  -0.23224 -0.06761 320 SER B CA    
1868 C  C     . SER A 241 ? 1.34483 1.02486 1.32811 0.18478  -0.24599 -0.05679 320 SER B C     
1869 O  O     . SER A 241 ? 1.32662 1.00863 1.32500 0.18219  -0.24557 -0.04682 320 SER B O     
1870 C  CB    . SER A 241 ? 1.11948 0.80374 1.06445 0.22503  -0.24249 -0.08972 320 SER B CB    
1871 O  OG    . SER A 241 ? 1.17769 0.83671 1.12943 0.22833  -0.26299 -0.10392 320 SER B OG    
1872 N  N     . THR A 242 ? 1.33982 1.00463 1.33345 0.17470  -0.25827 -0.05772 321 THR B N     
1873 C  CA    . THR A 242 ? 1.33055 0.98101 1.35449 0.15912  -0.27098 -0.04565 321 THR B CA    
1874 C  C     . THR A 242 ? 1.30454 0.95849 1.33318 0.13982  -0.26901 -0.03505 321 THR B C     
1875 O  O     . THR A 242 ? 1.45821 1.12051 1.46787 0.14052  -0.26181 -0.04061 321 THR B O     
1876 C  CB    . THR A 242 ? 1.29970 0.92123 1.34086 0.16913  -0.29472 -0.06035 321 THR B CB    
1877 O  OG1   . THR A 242 ? 1.40161 1.01199 1.43232 0.17620  -0.30424 -0.07799 321 THR B OG1   
1878 C  CG2   . THR A 242 ? 1.29289 0.91040 1.33087 0.18952  -0.29754 -0.07194 321 THR B CG2   
1879 N  N     . LEU A 243 ? 1.30862 0.95670 1.36343 0.12280  -0.27547 -0.01905 322 LEU B N     
1880 C  CA    . LEU A 243 ? 1.25436 0.90421 1.31915 0.10460  -0.27600 -0.00879 322 LEU B CA    
1881 C  C     . LEU A 243 ? 1.29661 0.92184 1.38981 0.09988  -0.29797 -0.01080 322 LEU B C     
1882 O  O     . LEU A 243 ? 1.41811 1.02856 1.53020 0.10291  -0.30979 -0.00940 322 LEU B O     
1883 C  CB    . LEU A 243 ? 1.10170 0.77117 1.17246 0.08634  -0.26173 0.01506  322 LEU B CB    
1884 C  CG    . LEU A 243 ? 1.12569 0.82029 1.17152 0.08736  -0.24030 0.01888  322 LEU B CG    
1885 C  CD1   . LEU A 243 ? 1.06822 0.78014 1.12145 0.06975  -0.22904 0.04099  322 LEU B CD1   
1886 C  CD2   . LEU A 243 ? 1.04251 0.74350 1.06734 0.09043  -0.23378 0.00849  322 LEU B CD2   
1887 N  N     . PRO A 244 ? 1.24712 0.86727 1.34569 0.09243  -0.30445 -0.01382 323 PRO B N     
1888 C  CA    . PRO A 244 ? 1.29949 0.89584 1.42722 0.08798  -0.32661 -0.01666 323 PRO B CA    
1889 C  C     . PRO A 244 ? 1.41923 1.01350 1.57783 0.07120  -0.33007 0.00604  323 PRO B C     
1890 O  O     . PRO A 244 ? 1.48216 1.09539 1.63890 0.06055  -0.31480 0.02500  323 PRO B O     
1891 C  CB    . PRO A 244 ? 1.32488 0.92381 1.45060 0.08079  -0.32803 -0.02059 323 PRO B CB    
1892 C  CG    . PRO A 244 ? 1.31984 0.94605 1.42306 0.07449  -0.30482 -0.01088 323 PRO B CG    
1893 C  CD    . PRO A 244 ? 1.25218 0.88798 1.33189 0.08795  -0.29252 -0.01488 323 PRO B CD    
1894 N  N     . GLU A 245 ? 1.56401 1.13447 1.75179 0.06905  -0.35136 0.00397  324 GLU B N     
1895 C  CA    . GLU A 245 ? 1.58393 1.14902 1.80365 0.05450  -0.35743 0.02552  324 GLU B CA    
1896 C  C     . GLU A 245 ? 1.56292 1.14759 1.79199 0.03253  -0.34570 0.04855  324 GLU B C     
1897 O  O     . GLU A 245 ? 1.51794 1.10643 1.74840 0.02575  -0.34600 0.04594  324 GLU B O     
1898 C  CB    . GLU A 245 ? 1.60649 1.14089 1.85756 0.05614  -0.38395 0.01781  324 GLU B CB    
1899 C  CG    . GLU A 245 ? 1.65526 1.18023 1.91223 0.05456  -0.39569 0.00461  324 GLU B CG    
1900 C  CD    . GLU A 245 ? 1.73172 1.22827 2.02714 0.05055  -0.42199 0.00259  324 GLU B CD    
1901 O  OE1   . GLU A 245 ? 1.66980 1.14870 1.98178 0.05570  -0.43380 0.00340  324 GLU B OE1   
1902 O  OE2   . GLU A 245 ? 1.80516 1.29693 2.11586 0.04209  -0.43139 0.00043  324 GLU B OE2   
1903 N  N     . SER A 246 ? 1.61082 1.20886 1.84570 0.02224  -0.33537 0.07079  325 SER B N     
1904 C  CA    . SER A 246 ? 1.62552 1.24260 1.87114 0.00172  -0.32471 0.09464  325 SER B CA    
1905 C  C     . SER A 246 ? 1.58446 1.22402 1.80584 -0.00146 -0.30757 0.09154  325 SER B C     
1906 O  O     . SER A 246 ? 1.45227 1.10230 1.68441 -0.01570 -0.30394 0.10235  325 SER B O     
1907 C  CB    . SER A 246 ? 1.54392 1.14680 1.82725 -0.01154 -0.34101 0.10480  325 SER B CB    
1908 O  OG    . SER A 246 ? 1.60772 1.19203 1.91585 -0.01150 -0.35521 0.11302  325 SER B OG    
1909 N  N     . LEU A 247 ? 1.39063 1.03817 1.58020 0.01203  -0.29689 0.07715  326 LEU B N     
1910 C  CA    . LEU A 247 ? 1.21378 0.88245 1.37988 0.00948  -0.28015 0.07513  326 LEU B CA    
1911 C  C     . LEU A 247 ? 1.27481 0.96851 1.43318 -0.00139 -0.26152 0.09459  326 LEU B C     
1912 O  O     . LEU A 247 ? 1.22728 0.93674 1.38854 -0.01464 -0.25280 0.10595  326 LEU B O     
1913 C  CB    . LEU A 247 ? 1.27416 0.94169 1.41024 0.02790  -0.27626 0.05317  326 LEU B CB    
1914 C  CG    . LEU A 247 ? 1.23609 0.92662 1.34583 0.02636  -0.25690 0.05308  326 LEU B CG    
1915 C  CD1   . LEU A 247 ? 1.20227 0.89716 1.31761 0.01645  -0.25726 0.05367  326 LEU B CD1   
1916 C  CD2   . LEU A 247 ? 1.24285 0.93379 1.32377 0.04459  -0.25180 0.03495  326 LEU B CD2   
1917 N  N     . LEU A 248 ? 1.32675 1.02480 1.47566 0.00464  -0.25575 0.09806  327 LEU B N     
1918 C  CA    . LEU A 248 ? 1.20615 0.92803 1.34507 -0.00392 -0.23882 0.11419  327 LEU B CA    
1919 C  C     . LEU A 248 ? 1.26496 0.99320 1.42642 -0.02127 -0.23957 0.13733  327 LEU B C     
1920 O  O     . LEU A 248 ? 1.30001 1.04992 1.45477 -0.03186 -0.22594 0.14976  327 LEU B O     
1921 C  CB    . LEU A 248 ? 1.18047 0.90436 1.30807 0.00659  -0.23495 0.11285  327 LEU B CB    
1922 C  CG    . LEU A 248 ? 1.23659 0.95935 1.34029 0.02391  -0.23090 0.09242  327 LEU B CG    
1923 C  CD1   . LEU A 248 ? 1.17849 0.90603 1.27511 0.03289  -0.22655 0.09370  327 LEU B CD1   
1924 C  CD2   . LEU A 248 ? 1.21730 0.95743 1.29916 0.02177  -0.21619 0.08801  327 LEU B CD2   
1925 N  N     . SER A 249 ? 1.31219 1.02212 1.50073 -0.02412 -0.25549 0.14364  328 SER B N     
1926 C  CA    . SER A 249 ? 1.20938 0.92573 1.42098 -0.04085 -0.25635 0.16755  328 SER B CA    
1927 C  C     . SER A 249 ? 1.17379 0.89877 1.39424 -0.05268 -0.25374 0.17145  328 SER B C     
1928 O  O     . SER A 249 ? 1.13669 0.87806 1.36695 -0.06694 -0.24658 0.19156  328 SER B O     
1929 C  CB    . SER A 249 ? 1.29196 0.98495 1.53269 -0.04090 -0.27510 0.17381  328 SER B CB    
1930 O  OG    . SER A 249 ? 1.52096 1.19055 1.77479 -0.03474 -0.29159 0.15710  328 SER B OG    
1931 N  N     . SER A 250 ? 1.22429 0.93977 1.44103 -0.04647 -0.25924 0.15263  329 SER B N     
1932 C  CA    . SER A 250 ? 1.21801 0.94154 1.44450 -0.05677 -0.25769 0.15506  329 SER B CA    
1933 C  C     . SER A 250 ? 1.19498 0.94553 1.39840 -0.06086 -0.23755 0.15761  329 SER B C     
1934 O  O     . SER A 250 ? 1.14785 0.91348 1.36142 -0.07326 -0.23157 0.16920  329 SER B O     
1935 C  CB    . SER A 250 ? 1.21241 0.91646 1.44224 -0.04802 -0.27163 0.13346  329 SER B CB    
1936 O  OG    . SER A 250 ? 1.25798 0.93566 1.50991 -0.04359 -0.29171 0.12928  329 SER B OG    
1937 N  N     . LEU A 251 ? 1.15766 0.91497 1.33156 -0.05051 -0.22713 0.14703  330 LEU B N     
1938 C  CA    . LEU A 251 ? 1.06277 0.84379 1.21465 -0.05339 -0.20900 0.14799  330 LEU B CA    
1939 C  C     . LEU A 251 ? 1.11407 0.91444 1.26705 -0.06382 -0.19830 0.16899  330 LEU B C     
1940 O  O     . LEU A 251 ? 1.17220 0.98028 1.30906 -0.05975 -0.19061 0.17101  330 LEU B O     
1941 C  CB    . LEU A 251 ? 1.07139 0.85204 1.19439 -0.03920 -0.20269 0.13073  330 LEU B CB    
1942 C  CG    . LEU A 251 ? 1.12494 0.88562 1.24363 -0.02604 -0.21406 0.10964  330 LEU B CG    
1943 C  CD1   . LEU A 251 ? 1.09858 0.86298 1.18790 -0.01262 -0.20524 0.09570  330 LEU B CD1   
1944 C  CD2   . LEU A 251 ? 1.06159 0.82005 1.18948 -0.03065 -0.21907 0.10430  330 LEU B CD2   
1945 N  N     . VAL A 252 ? 1.11790 0.92750 1.29054 -0.07742 -0.19787 0.18513  331 VAL B N     
1946 C  CA    . VAL A 252 ? 1.10258 0.92898 1.28033 -0.08776 -0.19048 0.20738  331 VAL B CA    
1947 C  C     . VAL A 252 ? 1.11119 0.96325 1.26449 -0.08956 -0.17231 0.20924  331 VAL B C     
1948 O  O     . VAL A 252 ? 1.14418 1.01305 1.29587 -0.09665 -0.16463 0.22585  331 VAL B O     
1949 C  CB    . VAL A 252 ? 1.08943 0.91913 1.29693 -0.10153 -0.19528 0.22486  331 VAL B CB    
1950 C  CG1   . VAL A 252 ? 1.00986 0.81258 1.24437 -0.10036 -0.21495 0.22395  331 VAL B CG1   
1951 C  CG2   . VAL A 252 ? 1.01115 0.85364 1.21969 -0.10666 -0.18883 0.22050  331 VAL B CG2   
1952 N  N     . LYS A 253 ? 1.15594 1.01101 1.29009 -0.08295 -0.16591 0.19232  332 LYS B N     
1953 C  CA    . LYS A 253 ? 1.21743 1.09461 1.32936 -0.08399 -0.14996 0.19182  332 LYS B CA    
1954 C  C     . LYS A 253 ? 1.14475 1.01871 1.23258 -0.07227 -0.14578 0.17719  332 LYS B C     
1955 O  O     . LYS A 253 ? 1.18641 1.07414 1.25608 -0.07127 -0.13447 0.17157  332 LYS B O     
1956 C  CB    . LYS A 253 ? 1.09770 0.98597 1.21029 -0.08870 -0.14390 0.18779  332 LYS B CB    
1957 C  CG    . LYS A 253 ? 0.98098 0.88325 1.11362 -0.10169 -0.14193 0.20540  332 LYS B CG    
1958 C  CD    . LYS A 253 ? 1.34033 1.26171 1.46660 -0.10537 -0.13074 0.20225  332 LYS B CD    
1959 C  CE    . LYS A 253 ? 1.40557 1.34249 1.50434 -0.10170 -0.11732 0.19744  332 LYS B CE    
1960 N  NZ    . LYS A 253 ? 1.18797 1.14144 1.27996 -0.10364 -0.10724 0.19198  332 LYS B NZ    
1961 N  N     . LEU A 254 ? 1.08894 0.94556 1.17740 -0.06327 -0.15466 0.17127  333 LEU B N     
1962 C  CA    . LEU A 254 ? 1.17942 1.03337 1.24723 -0.05146 -0.15083 0.15756  333 LEU B CA    
1963 C  C     . LEU A 254 ? 1.08128 0.95199 1.13634 -0.05301 -0.14078 0.16561  333 LEU B C     
1964 O  O     . LEU A 254 ? 1.06323 0.93550 1.12649 -0.05636 -0.14373 0.17854  333 LEU B O     
1965 C  CB    . LEU A 254 ? 1.05929 0.89094 1.13288 -0.04052 -0.16347 0.14863  333 LEU B CB    
1966 C  CG    . LEU A 254 ? 1.03959 0.86508 1.09437 -0.02643 -0.16160 0.13047  333 LEU B CG    
1967 C  CD1   . LEU A 254 ? 0.97788 0.79991 1.02683 -0.02421 -0.16157 0.11795  333 LEU B CD1   
1968 C  CD2   . LEU A 254 ? 0.97895 0.78559 1.03938 -0.01507 -0.17319 0.12362  333 LEU B CD2   
1969 N  N     . ASN A 255 ? 1.05496 0.93776 1.09073 -0.05051 -0.12977 0.15809  334 ASN B N     
1970 C  CA    . ASN A 255 ? 1.11384 1.01222 1.13727 -0.05132 -0.12107 0.16332  334 ASN B CA    
1971 C  C     . ASN A 255 ? 1.02307 0.91505 1.03824 -0.04016 -0.12217 0.15540  334 ASN B C     
1972 O  O     . ASN A 255 ? 1.02180 0.92079 1.03553 -0.04011 -0.12093 0.16268  334 ASN B O     
1973 C  CB    . ASN A 255 ? 1.09932 1.01466 1.10848 -0.05512 -0.10911 0.15983  334 ASN B CB    
1974 C  CG    . ASN A 255 ? 1.30132 1.22761 1.31774 -0.06573 -0.10609 0.16843  334 ASN B CG    
1975 O  OD1   . ASN A 255 ? 1.27135 1.20009 1.30093 -0.07258 -0.10976 0.18226  334 ASN B OD1   
1976 N  ND2   . ASN A 255 ? 1.29985 1.23353 1.30850 -0.06691 -0.09918 0.16089  334 ASN B ND2   
1977 N  N     . SER A 256 ? 0.99757 0.87778 1.00707 -0.03029 -0.12424 0.14087  335 SER B N     
1978 C  CA    . SER A 256 ? 1.00632 0.88250 1.00798 -0.01875 -0.12407 0.13314  335 SER B CA    
1979 C  C     . SER A 256 ? 1.02283 0.87982 1.02639 -0.00780 -0.13271 0.12032  335 SER B C     
1980 O  O     . SER A 256 ? 0.96123 0.81113 0.96510 -0.00812 -0.13541 0.11356  335 SER B O     
1981 C  CB    . SER A 256 ? 1.00597 0.89611 0.99052 -0.01676 -0.11210 0.12782  335 SER B CB    
1982 O  OG    . SER A 256 ? 1.13169 1.01837 1.10754 -0.01364 -0.10914 0.11693  335 SER B OG    
1983 N  N     . LEU A 257 ? 0.91506 0.76424 0.91995 0.00252  -0.13748 0.11654  336 LEU B N     
1984 C  CA    . LEU A 257 ? 0.92397 0.75646 0.92744 0.01581  -0.14512 0.10245  336 LEU B CA    
1985 C  C     . LEU A 257 ? 0.99174 0.83109 0.98045 0.02750  -0.13741 0.09458  336 LEU B C     
1986 O  O     . LEU A 257 ? 0.97224 0.82187 0.96133 0.02774  -0.13296 0.10108  336 LEU B O     
1987 C  CB    . LEU A 257 ? 0.86604 0.68139 0.88730 0.01905  -0.15946 0.10428  336 LEU B CB    
1988 C  CG    . LEU A 257 ? 0.91926 0.71627 0.93933 0.03429  -0.16908 0.08804  336 LEU B CG    
1989 C  CD1   . LEU A 257 ? 1.02781 0.81633 1.04440 0.03436  -0.17283 0.07805  336 LEU B CD1   
1990 C  CD2   . LEU A 257 ? 0.93747 0.71773 0.97674 0.03751  -0.18356 0.09041  336 LEU B CD2   
1991 N  N     . THR A 258 ? 0.94524 0.78005 0.92145 0.03716  -0.13582 0.08133  337 THR B N     
1992 C  CA    . THR A 258 ? 0.97924 0.82234 0.94108 0.04836  -0.12717 0.07461  337 THR B CA    
1993 C  C     . THR A 258 ? 1.02987 0.85857 0.98601 0.06429  -0.13425 0.05970  337 THR B C     
1994 O  O     . THR A 258 ? 1.07564 0.89902 1.02198 0.06773  -0.13492 0.05080  337 THR B O     
1995 C  CB    . THR A 258 ? 0.94009 0.79753 0.88829 0.04342  -0.11448 0.07528  337 THR B CB    
1996 O  OG1   . THR A 258 ? 1.00202 0.87066 0.95580 0.02859  -0.11011 0.08723  337 THR B OG1   
1997 C  CG2   . THR A 258 ? 0.87919 0.74843 0.81664 0.05240  -0.10454 0.07274  337 THR B CG2   
1998 N  N     . LEU A 259 ? 0.99184 0.81445 0.95390 0.07467  -0.14006 0.05657  338 LEU B N     
1999 C  CA    . LEU A 259 ? 0.99839 0.80850 0.95434 0.09203  -0.14688 0.04126  338 LEU B CA    
2000 C  C     . LEU A 259 ? 1.02643 0.84981 0.96826 0.10514  -0.13593 0.03628  338 LEU B C     
2001 O  O     . LEU A 259 ? 1.06592 0.88288 1.00501 0.12116  -0.14042 0.02564  338 LEU B O     
2002 C  CB    . LEU A 259 ? 0.98094 0.77372 0.95437 0.09641  -0.16206 0.03947  338 LEU B CB    
2003 C  CG    . LEU A 259 ? 0.95732 0.73880 0.94976 0.08205  -0.17273 0.04852  338 LEU B CG    
2004 C  CD1   . LEU A 259 ? 1.16045 0.92807 1.17216 0.08540  -0.18576 0.05090  338 LEU B CD1   
2005 C  CD2   . LEU A 259 ? 1.01332 0.78183 1.00444 0.08092  -0.18054 0.03974  338 LEU B CD2   
2006 N  N     . ALA A 260 ? 1.03028 0.87254 0.96405 0.09880  -0.12173 0.04379  339 ALA B N     
2007 C  CA    . ALA A 260 ? 0.99295 0.85073 0.91744 0.10887  -0.11035 0.04252  339 ALA B CA    
2008 C  C     . ALA A 260 ? 1.11727 0.97319 1.02345 0.12378  -0.10759 0.02960  339 ALA B C     
2009 O  O     . ALA A 260 ? 1.11316 0.96091 1.01032 0.12259  -0.11043 0.02405  339 ALA B O     
2010 C  CB    . ALA A 260 ? 1.04022 0.91751 0.96313 0.09678  -0.09723 0.05424  339 ALA B CB    
2011 N  N     . ARG A 261 ? 1.11342 0.97837 1.01411 0.13839  -0.10182 0.02522  340 ARG B N     
2012 C  CA    . ARG A 261 ? 0.99933 0.86628 0.88106 0.15492  -0.09752 0.01381  340 ARG B CA    
2013 C  C     . ARG A 261 ? 1.12585 0.97091 1.00230 0.16403  -0.11206 -0.00089 340 ARG B C     
2014 O  O     . ARG A 261 ? 1.20845 1.04723 1.07346 0.16271  -0.11394 -0.00565 340 ARG B O     
2015 C  CB    . ARG A 261 ? 1.04526 0.92572 0.91288 0.14957  -0.08433 0.01902  340 ARG B CB    
2016 C  CG    . ARG A 261 ? 1.05537 0.95630 0.92966 0.13940  -0.07124 0.03301  340 ARG B CG    
2017 C  CD    . ARG A 261 ? 1.17676 1.08856 1.03816 0.13501  -0.05959 0.03743  340 ARG B CD    
2018 N  NE    . ARG A 261 ? 1.44435 1.37358 1.31455 0.12334  -0.04908 0.05042  340 ARG B NE    
2019 C  CZ    . ARG A 261 ? 1.58460 1.53207 1.45591 0.12871  -0.03804 0.05537  340 ARG B CZ    
2020 N  NH1   . ARG A 261 ? 1.40888 1.36152 1.27188 0.14616  -0.03440 0.04903  340 ARG B NH1   
2021 N  NH2   . ARG A 261 ? 1.61255 1.57419 1.49415 0.11658  -0.03064 0.06674  340 ARG B NH2   
2022 N  N     . ASN A 262 ? 1.17289 1.00607 1.05913 0.17358  -0.12328 -0.00830 341 ASN B N     
2023 C  CA    . ASN A 262 ? 1.16864 0.97946 1.05321 0.18304  -0.13940 -0.02344 341 ASN B CA    
2024 C  C     . ASN A 262 ? 1.25081 1.05700 1.13756 0.20226  -0.14524 -0.03473 341 ASN B C     
2025 O  O     . ASN A 262 ? 1.30427 1.12753 1.18807 0.21079  -0.13417 -0.03236 341 ASN B O     
2026 C  CB    . ASN A 262 ? 1.15882 0.95246 1.06190 0.16707  -0.15276 -0.01849 341 ASN B CB    
2027 C  CG    . ASN A 262 ? 1.12820 0.92112 1.02491 0.15460  -0.15114 -0.01531 341 ASN B CG    
2028 O  OD1   . ASN A 262 ? 1.20211 0.98157 1.09221 0.15944  -0.16059 -0.02652 341 ASN B OD1   
2029 N  ND2   . ASN A 262 ? 1.09783 0.90528 0.99700 0.13899  -0.13983 -0.00067 341 ASN B ND2   
2030 N  N     . CYS A 263 ? 1.25507 1.03830 1.14845 0.20932  -0.16310 -0.04731 342 CYS B N     
2031 C  CA    . CYS A 263 ? 1.30672 1.08179 1.20367 0.22837  -0.17155 -0.06029 342 CYS B CA    
2032 C  C     . CYS A 263 ? 1.23178 0.99038 1.15621 0.22147  -0.18595 -0.05581 342 CYS B C     
2033 O  O     . CYS A 263 ? 1.24608 0.98743 1.17773 0.23479  -0.20032 -0.06899 342 CYS B O     
2034 C  CB    . CYS A 263 ? 1.25223 1.01323 1.13260 0.24633  -0.18183 -0.08169 342 CYS B CB    
2035 S  SG    . CYS A 263 ? 1.40124 1.18216 1.24710 0.25764  -0.16522 -0.08684 342 CYS B SG    
2036 N  N     . PHE A 264 ? 1.17872 0.94235 1.11847 0.20110  -0.18263 -0.03721 343 PHE B N     
2037 C  CA    . PHE A 264 ? 1.29925 1.04968 1.26495 0.19310  -0.19487 -0.02938 343 PHE B CA    
2038 C  C     . PHE A 264 ? 1.29915 1.05606 1.27218 0.20584  -0.19326 -0.03022 343 PHE B C     
2039 O  O     . PHE A 264 ? 1.20631 0.98500 1.17813 0.20272  -0.17908 -0.01928 343 PHE B O     
2040 C  CB    . PHE A 264 ? 1.27534 1.03369 1.25187 0.16926  -0.18953 -0.00870 343 PHE B CB    
2041 C  CG    . PHE A 264 ? 1.20797 0.95447 1.18743 0.15557  -0.19662 -0.00680 343 PHE B CG    
2042 C  CD1   . PHE A 264 ? 1.14611 0.90187 1.10825 0.15073  -0.18716 -0.00763 343 PHE B CD1   
2043 C  CD2   . PHE A 264 ? 1.12216 0.84893 1.12345 0.14726  -0.21275 -0.00316 343 PHE B CD2   
2044 C  CE1   . PHE A 264 ? 1.16379 0.90998 1.13013 0.13857  -0.19363 -0.00595 343 PHE B CE1   
2045 C  CE2   . PHE A 264 ? 1.21408 0.93197 1.22039 0.13446  -0.21883 -0.00065 343 PHE B CE2   
2046 C  CZ    . PHE A 264 ? 1.21504 0.94303 1.20379 0.13038  -0.20921 -0.00249 343 PHE B CZ    
2047 N  N     . GLN A 265 ? 1.28976 1.02779 1.27152 0.22059  -0.20839 -0.04373 344 GLN B N     
2048 C  CA    . GLN A 265 ? 1.33800 1.07880 1.33157 0.23223  -0.20997 -0.04433 344 GLN B CA    
2049 C  C     . GLN A 265 ? 1.33301 1.05938 1.35463 0.22063  -0.22298 -0.03197 344 GLN B C     
2050 O  O     . GLN A 265 ? 1.35415 1.08515 1.38811 0.22632  -0.22330 -0.02762 344 GLN B O     
2051 C  CB    . GLN A 265 ? 1.35228 1.08244 1.33817 0.25821  -0.21826 -0.06771 344 GLN B CB    
2052 C  CG    . GLN A 265 ? 1.46797 1.21580 1.42487 0.27281  -0.20401 -0.07917 344 GLN B CG    
2053 C  CD    . GLN A 265 ? 1.46205 1.20462 1.41076 0.30054  -0.20983 -0.10130 344 GLN B CD    
2054 O  OE1   . GLN A 265 ? 1.39708 1.12296 1.36307 0.30948  -0.22438 -0.10858 344 GLN B OE1   
2055 N  NE2   . GLN A 265 ? 1.41809 1.17519 1.34017 0.31484  -0.19853 -0.11199 344 GLN B NE2   
2056 N  N     . LEU A 266 ? 1.38063 1.09073 1.41317 0.20466  -0.23346 -0.02537 345 LEU B N     
2057 C  CA    . LEU A 266 ? 1.25068 0.94860 1.30952 0.19131  -0.24474 -0.01038 345 LEU B CA    
2058 C  C     . LEU A 266 ? 1.18512 0.88796 1.24634 0.16740  -0.24034 0.00676  345 LEU B C     
2059 O  O     . LEU A 266 ? 1.24099 0.94974 1.28641 0.16250  -0.23321 0.00354  345 LEU B O     
2060 C  CB    . LEU A 266 ? 1.14212 0.80881 1.21902 0.19913  -0.26767 -0.02174 345 LEU B CB    
2061 C  CG    . LEU A 266 ? 1.20152 0.85945 1.29032 0.21724  -0.27671 -0.03021 345 LEU B CG    
2062 C  CD1   . LEU A 266 ? 1.19591 0.82057 1.30321 0.22349  -0.30081 -0.04216 345 LEU B CD1   
2063 C  CD2   . LEU A 266 ? 1.36745 1.03645 1.47202 0.20824  -0.27253 -0.00971 345 LEU B CD2   
2064 N  N     . TYR A 267 ? 1.25154 0.95261 1.33250 0.15316  -0.24460 0.02529  346 TYR B N     
2065 C  CA    . TYR A 267 ? 1.22447 0.92941 1.30994 0.13116  -0.24189 0.04177  346 TYR B CA    
2066 C  C     . TYR A 267 ? 1.18327 0.86599 1.27738 0.12689  -0.25608 0.03525  346 TYR B C     
2067 O  O     . TYR A 267 ? 1.23748 0.89721 1.34446 0.13686  -0.27286 0.02417  346 TYR B O     
2068 C  CB    . TYR A 267 ? 1.29546 1.00370 1.39969 0.11847  -0.24406 0.06331  346 TYR B CB    
2069 C  CG    . TYR A 267 ? 1.21755 0.95351 1.31112 0.10910  -0.22668 0.07735  346 TYR B CG    
2070 C  CD1   . TYR A 267 ? 1.23666 0.99013 1.31777 0.12024  -0.21521 0.07216  346 TYR B CD1   
2071 C  CD2   . TYR A 267 ? 1.22020 0.96544 1.31704 0.08939  -0.22210 0.09562  346 TYR B CD2   
2072 C  CE1   . TYR A 267 ? 1.23160 1.00959 1.30493 0.11137  -0.20082 0.08435  346 TYR B CE1   
2073 C  CE2   . TYR A 267 ? 1.21585 0.98560 1.30273 0.08147  -0.20761 0.10685  346 TYR B CE2   
2074 C  CZ    . TYR A 267 ? 1.20462 0.98989 1.28039 0.09221  -0.19763 0.10096  346 TYR B CZ    
2075 O  OH    . TYR A 267 ? 1.19911 1.00796 1.26685 0.08407  -0.18463 0.11148  346 TYR B OH    
2076 N  N     . PRO A 268 ? 1.34649 1.03558 1.43484 0.11256  -0.25031 0.04122  347 PRO B N     
2077 C  CA    . PRO A 268 ? 1.37717 1.04688 1.47547 0.10787  -0.26380 0.03537  347 PRO B CA    
2078 C  C     . PRO A 268 ? 1.31061 0.96262 1.43954 0.09793  -0.27966 0.04794  347 PRO B C     
2079 O  O     . PRO A 268 ? 1.30679 0.96771 1.44655 0.08580  -0.27579 0.06814  347 PRO B O     
2080 C  CB    . PRO A 268 ? 1.21714 0.90293 1.30342 0.09353  -0.25119 0.04255  347 PRO B CB    
2081 C  CG    . PRO A 268 ? 1.25593 0.96577 1.33560 0.08492  -0.23492 0.05887  347 PRO B CG    
2082 C  CD    . PRO A 268 ? 1.27844 0.99272 1.35215 0.10041  -0.23186 0.05285  347 PRO B CD    
2083 N  N     . VAL A 269 ? 1.34127 0.96789 1.48444 0.10339  -0.29827 0.03593  348 VAL B N     
2084 C  CA    . VAL A 269 ? 1.33984 0.94678 1.51511 0.09485  -0.31537 0.04719  348 VAL B CA    
2085 C  C     . VAL A 269 ? 1.37000 0.98379 1.55796 0.07190  -0.31263 0.06744  348 VAL B C     
2086 O  O     . VAL A 269 ? 1.52652 1.15267 1.70128 0.06478  -0.30302 0.06655  348 VAL B O     
2087 C  CB    . VAL A 269 ? 1.35158 0.92854 1.53995 0.10735  -0.33729 0.02731  348 VAL B CB    
2088 C  CG1   . VAL A 269 ? 1.38630 0.95865 1.56052 0.13162  -0.33897 0.00653  348 VAL B CG1   
2089 C  CG2   . VAL A 269 ? 1.39373 0.96588 1.57600 0.10454  -0.34086 0.01574  348 VAL B CG2   
2090 N  N     . GLY A 270 ? 1.43592 1.04214 1.65041 0.06059  -0.32115 0.08651  349 GLY B N     
2091 C  CA    . GLY A 270 ? 1.44012 1.05464 1.66868 0.03906  -0.31817 0.10826  349 GLY B CA    
2092 C  C     . GLY A 270 ? 1.49314 1.11477 1.73617 0.02842  -0.31625 0.13371  349 GLY B C     
2093 O  O     . GLY A 270 ? 1.42839 1.04977 1.69214 0.01203  -0.31987 0.15341  349 GLY B O     
2094 N  N     . GLY A 271 ? 1.46511 1.09427 1.69760 0.03782  -0.31046 0.13412  350 GLY B N     
2095 C  CA    . GLY A 271 ? 1.61439 1.25032 1.85851 0.02996  -0.30946 0.15706  350 GLY B CA    
2096 C  C     . GLY A 271 ? 1.57386 1.24056 1.80035 0.01821  -0.28971 0.17292  350 GLY B C     
2097 O  O     . GLY A 271 ? 1.48688 1.17028 1.68983 0.01890  -0.27557 0.16399  350 GLY B O     
2098 N  N     . PRO A 272 ? 1.64062 1.31512 1.87817 0.00758  -0.28902 0.19685  351 PRO B N     
2099 C  CA    . PRO A 272 ? 1.57531 1.27932 1.79585 -0.00329 -0.27134 0.21186  351 PRO B CA    
2100 C  C     . PRO A 272 ? 1.61140 1.32712 1.83029 -0.01855 -0.26365 0.21965  351 PRO B C     
2101 O  O     . PRO A 272 ? 1.51177 1.25207 1.71173 -0.02497 -0.24785 0.22527  351 PRO B O     
2102 C  CB    . PRO A 272 ? 1.47003 1.17593 1.70488 -0.00890 -0.27597 0.23507  351 PRO B CB    
2103 C  CG    . PRO A 272 ? 1.43292 1.11108 1.68860 0.00277  -0.29446 0.22851  351 PRO B CG    
2104 C  CD    . PRO A 272 ? 1.45687 1.11394 1.72098 0.00713  -0.30448 0.21023  351 PRO B CD    
2105 N  N     . SER A 273 ? 1.52500 1.22430 1.76409 -0.02427 -0.27468 0.21970  352 SER B N     
2106 C  CA    . SER A 273 ? 1.38523 1.09610 1.62721 -0.03917 -0.26828 0.22882  352 SER B CA    
2107 C  C     . SER A 273 ? 1.34922 1.06948 1.56905 -0.03563 -0.25776 0.21008  352 SER B C     
2108 O  O     . SER A 273 ? 1.45873 1.18932 1.68010 -0.04671 -0.25201 0.21535  352 SER B O     
2109 C  CB    . SER A 273 ? 1.39797 1.08794 1.67269 -0.04667 -0.28481 0.23557  352 SER B CB    
2110 O  OG    . SER A 273 ? 1.49042 1.15492 1.77156 -0.03414 -0.29899 0.21274  352 SER B OG    
2111 N  N     . GLN A 274 ? 1.29011 1.00784 1.49022 -0.02044 -0.25495 0.18924  353 GLN B N     
2112 C  CA    . GLN A 274 ? 1.22465 0.95028 1.40337 -0.01610 -0.24549 0.17193  353 GLN B CA    
2113 C  C     . GLN A 274 ? 1.22639 0.97797 1.37884 -0.01655 -0.22668 0.17338  353 GLN B C     
2114 O  O     . GLN A 274 ? 1.19179 0.95173 1.32607 -0.01388 -0.21757 0.16112  353 GLN B O     
2115 C  CB    . GLN A 274 ? 1.31894 1.02529 1.49224 0.00148  -0.25455 0.14728  353 GLN B CB    
2116 C  CG    . GLN A 274 ? 1.30360 1.00984 1.46575 0.01607  -0.25293 0.13992  353 GLN B CG    
2117 C  CD    . GLN A 274 ? 1.29506 0.98260 1.45277 0.03441  -0.26243 0.11585  353 GLN B CD    
2118 O  OE1   . GLN A 274 ? 1.35127 1.03092 1.50472 0.03748  -0.26603 0.10177  353 GLN B OE1   
2119 N  NE2   . GLN A 274 ? 1.32871 1.00982 1.48712 0.04741  -0.26677 0.11076  353 GLN B NE2   
2120 N  N     . PHE A 275 ? 1.27707 1.04112 1.42772 -0.01981 -0.22151 0.18804  354 PHE B N     
2121 C  CA    . PHE A 275 ? 1.26801 1.05640 1.39598 -0.02086 -0.20523 0.18989  354 PHE B CA    
2122 C  C     . PHE A 275 ? 1.23244 1.04007 1.36199 -0.03596 -0.19783 0.21150  354 PHE B C     
2123 O  O     . PHE A 275 ? 1.18134 1.00791 1.29603 -0.03718 -0.18747 0.21656  354 PHE B O     
2124 C  CB    . PHE A 275 ? 1.18853 0.97783 1.30875 -0.00865 -0.20464 0.18480  354 PHE B CB    
2125 C  CG    . PHE A 275 ? 1.15584 0.93034 1.27113 0.00783  -0.20956 0.16313  354 PHE B CG    
2126 C  CD1   . PHE A 275 ? 1.19787 0.97815 1.29413 0.01348  -0.20074 0.14733  354 PHE B CD1   
2127 C  CD2   . PHE A 275 ? 1.19244 0.94775 1.32169 0.01836  -0.22301 0.15869  354 PHE B CD2   
2128 C  CE1   . PHE A 275 ? 1.19759 0.96616 1.28736 0.02939  -0.20458 0.12808  354 PHE B CE1   
2129 C  CE2   . PHE A 275 ? 1.22339 0.96662 1.34650 0.03486  -0.22713 0.13792  354 PHE B CE2   
2130 C  CZ    . PHE A 275 ? 1.18590 0.93652 1.28847 0.04043  -0.21754 0.12289  354 PHE B CZ    
2131 N  N     . SER A 276 ? 1.16603 0.97009 1.31345 -0.04729 -0.20300 0.22427  355 SER B N     
2132 C  CA    . SER A 276 ? 1.13125 0.95385 1.28154 -0.06101 -0.19660 0.24648  355 SER B CA    
2133 C  C     . SER A 276 ? 1.12656 0.97144 1.26027 -0.06818 -0.18171 0.24561  355 SER B C     
2134 O  O     . SER A 276 ? 1.18862 1.05089 1.32315 -0.07912 -0.17541 0.26283  355 SER B O     
2135 C  CB    . SER A 276 ? 1.27471 1.08568 1.45339 -0.07047 -0.20787 0.26249  355 SER B CB    
2136 O  OG    . SER A 276 ? 1.45531 1.24479 1.65105 -0.06412 -0.22264 0.26435  355 SER B OG    
2137 N  N     . THR A 277 ? 1.10741 0.95269 1.22603 -0.06188 -0.17598 0.22643  356 THR B N     
2138 C  CA    . THR A 277 ? 1.15909 1.02343 1.26353 -0.06790 -0.16295 0.22424  356 THR B CA    
2139 C  C     . THR A 277 ? 1.10546 0.97974 1.18527 -0.06038 -0.15250 0.20984  356 THR B C     
2140 O  O     . THR A 277 ? 1.11687 1.00884 1.18406 -0.06547 -0.14133 0.20973  356 THR B O     
2141 C  CB    . THR A 277 ? 1.17607 1.03225 1.29061 -0.07095 -0.16626 0.21721  356 THR B CB    
2142 O  OG1   . THR A 277 ? 1.14293 0.97829 1.25756 -0.05941 -0.17480 0.19852  356 THR B OG1   
2143 C  CG2   . THR A 277 ? 1.13066 0.98261 1.27136 -0.08170 -0.17420 0.23438  356 THR B CG2   
2144 N  N     . ILE A 278 ? 1.15013 1.01439 1.22371 -0.04848 -0.15561 0.19805  357 ILE B N     
2145 C  CA    . ILE A 278 ? 1.05945 0.93271 1.11216 -0.04155 -0.14583 0.18488  357 ILE B CA    
2146 C  C     . ILE A 278 ? 1.04933 0.94095 1.09202 -0.04384 -0.13840 0.19347  357 ILE B C     
2147 O  O     . ILE A 278 ? 1.16191 1.05314 1.21215 -0.04406 -0.14355 0.20446  357 ILE B O     
2148 C  CB    . ILE A 278 ? 1.01154 0.86862 1.06176 -0.02720 -0.15130 0.16874  357 ILE B CB    
2149 C  CG1   . ILE A 278 ? 1.00279 0.84987 1.06406 -0.02113 -0.16064 0.17358  357 ILE B CG1   
2150 C  CG2   . ILE A 278 ? 1.08316 0.92360 1.13944 -0.02418 -0.15835 0.15762  357 ILE B CG2   
2151 C  CD1   . ILE A 278 ? 1.07198 0.90735 1.12868 -0.00555 -0.16413 0.15758  357 ILE B CD1   
2152 N  N     . TYR A 279 ? 1.02457 0.93199 1.05083 -0.04552 -0.12710 0.18837  358 TYR B N     
2153 C  CA    . TYR A 279 ? 0.96423 0.88821 0.97947 -0.04583 -0.12058 0.19206  358 TYR B CA    
2154 C  C     . TYR A 279 ? 0.99171 0.91307 0.99974 -0.03472 -0.11904 0.18018  358 TYR B C     
2155 O  O     . TYR A 279 ? 1.07477 1.00753 1.07791 -0.03364 -0.11617 0.18338  358 TYR B O     
2156 C  CB    . TYR A 279 ? 1.02565 0.96820 1.02820 -0.05339 -0.10991 0.19230  358 TYR B CB    
2157 C  CG    . TYR A 279 ? 1.16193 1.11287 1.16986 -0.06420 -0.10906 0.20519  358 TYR B CG    
2158 C  CD1   . TYR A 279 ? 1.19797 1.14295 1.21323 -0.06794 -0.10977 0.20344  358 TYR B CD1   
2159 C  CD2   . TYR A 279 ? 1.22735 1.19369 1.23301 -0.07035 -0.10737 0.21943  358 TYR B CD2   
2160 C  CE1   . TYR A 279 ? 1.28362 1.23860 1.30539 -0.07777 -0.10801 0.21612  358 TYR B CE1   
2161 C  CE2   . TYR A 279 ? 1.27438 1.25079 1.28422 -0.07968 -0.10540 0.23222  358 TYR B CE2   
2162 C  CZ    . TYR A 279 ? 1.36332 1.33449 1.38194 -0.08350 -0.10529 0.23080  358 TYR B CZ    
2163 O  OH    . TYR A 279 ? 1.56192 1.54533 1.58630 -0.09277 -0.10243 0.24445  358 TYR B OH    
2164 N  N     . SER A 280 ? 0.99868 0.90646 1.00615 -0.02628 -0.12092 0.16691  359 SER B N     
2165 C  CA    . SER A 280 ? 0.95602 0.86300 0.95600 -0.01514 -0.11796 0.15566  359 SER B CA    
2166 C  C     . SER A 280 ? 0.99626 0.88346 1.00242 -0.00424 -0.12628 0.14601  359 SER B C     
2167 O  O     . SER A 280 ? 0.92750 0.80154 0.94082 -0.00584 -0.13294 0.14434  359 SER B O     
2168 C  CB    . SER A 280 ? 0.83617 0.75305 0.82149 -0.01559 -0.10723 0.14690  359 SER B CB    
2169 O  OG    . SER A 280 ? 1.11783 1.03309 1.09714 -0.00450 -0.10427 0.13665  359 SER B OG    
2170 N  N     . LEU A 281 ? 1.07442 0.96039 1.07839 0.00727  -0.12614 0.13930  360 LEU B N     
2171 C  CA    . LEU A 281 ? 0.96731 0.83594 0.97502 0.02011  -0.13374 0.12826  360 LEU B CA    
2172 C  C     . LEU A 281 ? 0.91795 0.79378 0.91573 0.03200  -0.12670 0.11897  360 LEU B C     
2173 O  O     . LEU A 281 ? 1.04562 0.93147 1.04612 0.03445  -0.12448 0.12374  360 LEU B O     
2174 C  CB    . LEU A 281 ? 0.89941 0.75517 0.92415 0.02225  -0.14629 0.13457  360 LEU B CB    
2175 C  CG    . LEU A 281 ? 0.96619 0.80260 0.99620 0.03657  -0.15603 0.12200  360 LEU B CG    
2176 C  CD1   . LEU A 281 ? 0.99593 0.81917 1.02332 0.03712  -0.15994 0.11187  360 LEU B CD1   
2177 C  CD2   . LEU A 281 ? 1.08570 0.90936 1.13463 0.03788  -0.16898 0.12953  360 LEU B CD2   
2178 N  N     . ASN A 282 ? 0.96183 0.83370 0.94868 0.03937  -0.12318 0.10653  361 ASN B N     
2179 C  CA    . ASN A 282 ? 0.85224 0.73207 0.82900 0.05092  -0.11532 0.09831  361 ASN B CA    
2180 C  C     . ASN A 282 ? 1.00181 0.86624 0.97744 0.06645  -0.12230 0.08529  361 ASN B C     
2181 O  O     . ASN A 282 ? 1.02827 0.88005 0.99970 0.06821  -0.12701 0.07732  361 ASN B O     
2182 C  CB    . ASN A 282 ? 0.91525 0.80611 0.87787 0.04679  -0.10385 0.09578  361 ASN B CB    
2183 C  CG    . ASN A 282 ? 1.06759 0.97097 1.02211 0.05595  -0.09403 0.09168  361 ASN B CG    
2184 O  OD1   . ASN A 282 ? 1.06611 0.96965 1.02408 0.06742  -0.09546 0.08850  361 ASN B OD1   
2185 N  ND2   . ASN A 282 ? 1.11345 1.02782 1.05837 0.05109  -0.08397 0.09206  361 ASN B ND2   
2186 N  N     . MET A 283 ? 0.97323 0.83923 0.95278 0.07831  -0.12341 0.08249  362 MET B N     
2187 C  CA    . MET A 283 ? 0.97787 0.83074 0.95564 0.09527  -0.12992 0.06884  362 MET B CA    
2188 C  C     . MET A 283 ? 1.05425 0.92105 1.02273 0.10888  -0.11981 0.06274  362 MET B C     
2189 O  O     . MET A 283 ? 1.03490 0.89584 1.00463 0.12457  -0.12422 0.05346  362 MET B O     
2190 C  CB    . MET A 283 ? 0.93570 0.77326 0.93080 0.09900  -0.14413 0.07000  362 MET B CB    
2191 C  CG    . MET A 283 ? 1.08584 0.90797 1.09254 0.08703  -0.15535 0.07602  362 MET B CG    
2192 S  SD    . MET A 283 ? 1.33458 1.13663 1.36341 0.09268  -0.17307 0.07737  362 MET B SD    
2193 C  CE    . MET A 283 ? 1.24395 1.02975 1.28512 0.07749  -0.18409 0.08430  362 MET B CE    
2194 N  N     . GLU A 284 ? 1.00068 0.88627 0.96076 0.10342  -0.10637 0.06782  363 GLU B N     
2195 C  CA    . GLU A 284 ? 1.02636 0.92842 0.98152 0.11428  -0.09587 0.06554  363 GLU B CA    
2196 C  C     . GLU A 284 ? 1.08809 0.98607 1.02827 0.13016  -0.09344 0.05182  363 GLU B C     
2197 O  O     . GLU A 284 ? 1.13976 1.02598 1.06982 0.12980  -0.09681 0.04516  363 GLU B O     
2198 C  CB    . GLU A 284 ? 1.01923 0.94149 0.97143 0.10320  -0.08310 0.07509  363 GLU B CB    
2199 C  CG    . GLU A 284 ? 1.25323 1.17552 1.19178 0.09648  -0.07709 0.07355  363 GLU B CG    
2200 C  CD    . GLU A 284 ? 1.40816 1.34940 1.34574 0.08651  -0.06543 0.08222  363 GLU B CD    
2201 O  OE1   . GLU A 284 ? 1.14870 1.10459 1.09495 0.08713  -0.06098 0.08800  363 GLU B OE1   
2202 O  OE2   . GLU A 284 ? 1.53442 1.47562 1.46379 0.07821  -0.06144 0.08294  363 GLU B OE2   
2203 N  N     . HIS A 285 ? 1.12127 1.03027 1.06017 0.14479  -0.08762 0.04770  364 HIS B N     
2204 C  CA    . HIS A 285 ? 1.13383 1.04291 1.05731 0.16251  -0.08392 0.03501  364 HIS B CA    
2205 C  C     . HIS A 285 ? 1.11277 0.99769 1.03376 0.17246  -0.09879 0.02124  364 HIS B C     
2206 O  O     . HIS A 285 ? 1.20744 1.08146 1.11567 0.17368  -0.10207 0.01352  364 HIS B O     
2207 C  CB    . HIS A 285 ? 1.17445 1.09303 1.08123 0.15859  -0.07233 0.03643  364 HIS B CB    
2208 C  CG    . HIS A 285 ? 1.30651 1.24789 1.21715 0.14969  -0.05855 0.04897  364 HIS B CG    
2209 N  ND1   . HIS A 285 ? 1.36819 1.32927 1.27961 0.15975  -0.04763 0.05076  364 HIS B ND1   
2210 C  CD2   . HIS A 285 ? 1.29538 1.24318 1.21063 0.13185  -0.05451 0.05996  364 HIS B CD2   
2211 C  CE1   . HIS A 285 ? 1.36676 1.34466 1.28441 0.14768  -0.03808 0.06270  364 HIS B CE1   
2212 N  NE2   . HIS A 285 ? 1.34865 1.31829 1.26800 0.13102  -0.04237 0.06776  364 HIS B NE2   
2213 N  N     . ASN A 286 ? 1.14903 1.02549 1.08398 0.17970  -0.10868 0.01826  365 ASN B N     
2214 C  CA    . ASN A 286 ? 1.18516 1.03862 1.12087 0.19159  -0.12394 0.00398  365 ASN B CA    
2215 C  C     . ASN A 286 ? 1.18320 1.03784 1.12689 0.20933  -0.12725 -0.00311 365 ASN B C     
2216 O  O     . ASN A 286 ? 1.17916 1.05500 1.12088 0.21699  -0.11492 -0.00063 365 ASN B O     
2217 C  CB    . ASN A 286 ? 1.23876 1.07178 1.18893 0.17721  -0.13851 0.00878  365 ASN B CB    
2218 C  CG    . ASN A 286 ? 1.15024 0.97592 1.09085 0.16618  -0.13944 0.00848  365 ASN B CG    
2219 O  OD1   . ASN A 286 ? 1.11436 0.92398 1.04800 0.17356  -0.14859 -0.00431 365 ASN B OD1   
2220 N  ND2   . ASN A 286 ? 1.22730 1.06487 1.16800 0.14896  -0.13060 0.02189  365 ASN B ND2   
2221 N  N     . ARG A 287 ? 1.22721 1.05946 1.18152 0.21610  -0.14408 -0.01185 366 ARG B N     
2222 C  CA    . ARG A 287 ? 1.23212 1.06244 1.19531 0.23419  -0.14942 -0.02036 366 ARG B CA    
2223 C  C     . ARG A 287 ? 1.17672 0.98716 1.16377 0.22840  -0.16634 -0.01606 366 ARG B C     
2224 O  O     . ARG A 287 ? 1.20779 1.00201 1.20275 0.24302  -0.17925 -0.02819 366 ARG B O     
2225 C  CB    . ARG A 287 ? 1.29750 1.11972 1.24483 0.25684  -0.15337 -0.04181 366 ARG B CB    
2226 C  CG    . ARG A 287 ? 1.28071 1.12410 1.20362 0.26558  -0.13625 -0.04570 366 ARG B CG    
2227 C  CD    . ARG A 287 ? 1.41825 1.26005 1.32829 0.29244  -0.13845 -0.06580 366 ARG B CD    
2228 N  NE    . ARG A 287 ? 1.62752 1.47519 1.55255 0.30520  -0.13960 -0.06790 366 ARG B NE    
2229 C  CZ    . ARG A 287 ? 1.69141 1.52911 1.61557 0.32756  -0.14890 -0.08610 366 ARG B CZ    
2230 N  NH1   . ARG A 287 ? 1.58085 1.40144 1.48940 0.34002  -0.15885 -0.10466 366 ARG B NH1   
2231 N  NH2   . ARG A 287 ? 1.53488 1.37982 1.47459 0.33819  -0.14900 -0.08639 366 ARG B NH2   
2232 N  N     . ILE A 288 ? 1.22005 1.03163 1.21891 0.20741  -0.16668 0.00145  367 ILE B N     
2233 C  CA    . ILE A 288 ? 1.26479 1.05895 1.28636 0.19991  -0.18194 0.00898  367 ILE B CA    
2234 C  C     . ILE A 288 ? 1.31815 1.12107 1.35384 0.20882  -0.18193 0.01274  367 ILE B C     
2235 O  O     . ILE A 288 ? 1.38043 1.20695 1.41575 0.20484  -0.16904 0.02303  367 ILE B O     
2236 C  CB    . ILE A 288 ? 1.25903 1.05472 1.28653 0.17546  -0.18090 0.02716  367 ILE B CB    
2237 C  CG1   . ILE A 288 ? 1.27167 1.05999 1.28618 0.16758  -0.18058 0.02281  367 ILE B CG1   
2238 C  CG2   . ILE A 288 ? 1.26027 1.03931 1.31118 0.16773  -0.19611 0.03706  367 ILE B CG2   
2239 C  CD1   . ILE A 288 ? 1.19647 0.99054 1.21372 0.14484  -0.17656 0.03942  367 ILE B CD1   
2240 N  N     . ASN A 289 ? 1.29450 1.07804 1.34415 0.22100  -0.19728 0.00419  368 ASN B N     
2241 C  CA    . ASN A 289 ? 1.24143 1.03134 1.30540 0.23251  -0.19894 0.00531  368 ASN B CA    
2242 C  C     . ASN A 289 ? 1.34386 1.12743 1.43062 0.21901  -0.20828 0.02317  368 ASN B C     
2243 O  O     . ASN A 289 ? 1.34466 1.13722 1.44393 0.22557  -0.20829 0.02782  368 ASN B O     
2244 C  CB    . ASN A 289 ? 1.32368 1.09685 1.38995 0.25635  -0.21043 -0.01565 368 ASN B CB    
2245 C  CG    . ASN A 289 ? 1.39216 1.13156 1.47143 0.25404  -0.23188 -0.02085 368 ASN B CG    
2246 O  OD1   . ASN A 289 ? 1.39647 1.12549 1.47528 0.23722  -0.23587 -0.01398 368 ASN B OD1   
2247 N  ND2   . ASN A 289 ? 1.41385 1.13612 1.50640 0.27109  -0.24613 -0.03303 368 ASN B ND2   
2248 N  N     . LYS A 290 ? 1.28574 1.05535 1.37843 0.20082  -0.21602 0.03383  369 LYS B N     
2249 C  CA    . LYS A 290 ? 1.25478 1.01922 1.36769 0.18772  -0.22455 0.05244  369 LYS B CA    
2250 C  C     . LYS A 290 ? 1.30159 1.06131 1.41367 0.16542  -0.22540 0.06586  369 LYS B C     
2251 O  O     . LYS A 290 ? 1.28888 1.03561 1.39426 0.16283  -0.22894 0.05788  369 LYS B O     
2252 C  CB    . LYS A 290 ? 1.21844 0.95746 1.35265 0.19848  -0.24409 0.04737  369 LYS B CB    
2253 C  CG    . LYS A 290 ? 1.21794 0.92908 1.35326 0.20387  -0.25798 0.03225  369 LYS B CG    
2254 C  CD    . LYS A 290 ? 1.33431 1.01939 1.49344 0.21402  -0.27844 0.02785  369 LYS B CD    
2255 C  CE    . LYS A 290 ? 1.53595 1.19256 1.69736 0.22032  -0.29375 0.01081  369 LYS B CE    
2256 N  NZ    . LYS A 290 ? 1.45834 1.11958 1.59737 0.23905  -0.28741 -0.01337 369 LYS B NZ    
2257 N  N     . ILE A 291 ? 1.27832 1.04981 1.39709 0.15007  -0.22219 0.08595  370 ILE B N     
2258 C  CA    . ILE A 291 ? 1.25331 1.02122 1.37450 0.12928  -0.22400 0.10107  370 ILE B CA    
2259 C  C     . ILE A 291 ? 1.16925 0.91438 1.31403 0.12599  -0.24217 0.11007  370 ILE B C     
2260 O  O     . ILE A 291 ? 1.18107 0.92573 1.33981 0.13088  -0.24823 0.11711  370 ILE B O     
2261 C  CB    . ILE A 291 ? 1.16883 0.96231 1.28302 0.11498  -0.21104 0.11757  370 ILE B CB    
2262 C  CG1   . ILE A 291 ? 1.06548 0.88000 1.15877 0.11773  -0.19389 0.10903  370 ILE B CG1   
2263 C  CG2   . ILE A 291 ? 1.07021 0.86102 1.18696 0.09484  -0.21295 0.13318  370 ILE B CG2   
2264 C  CD1   . ILE A 291 ? 1.00998 0.84918 1.09718 0.10496  -0.18211 0.12293  370 ILE B CD1   
2265 N  N     . PRO A 292 ? 1.17054 0.89664 1.32207 0.11783  -0.25168 0.11075  371 PRO B N     
2266 C  CA    . PRO A 292 ? 1.20238 0.90457 1.37908 0.11558  -0.27022 0.11871  371 PRO B CA    
2267 C  C     . PRO A 292 ? 1.24213 0.95295 1.43022 0.10130  -0.27076 0.14418  371 PRO B C     
2268 O  O     . PRO A 292 ? 1.30466 1.03556 1.48186 0.08718  -0.25884 0.15722  371 PRO B O     
2269 C  CB    . PRO A 292 ? 1.28138 0.96655 1.46112 0.10719  -0.27724 0.11503  371 PRO B CB    
2270 C  CG    . PRO A 292 ? 1.27722 0.97249 1.43270 0.11262  -0.26521 0.09802  371 PRO B CG    
2271 C  CD    . PRO A 292 ? 1.26662 0.99119 1.40481 0.11155  -0.24691 0.10320  371 PRO B CD    
2272 N  N     . PHE A 293 ? 1.26189 0.95708 1.47183 0.10592  -0.28533 0.15083  372 PHE B N     
2273 C  CA    . PHE A 293 ? 1.23167 0.93182 1.45427 0.09310  -0.28860 0.17621  372 PHE B CA    
2274 C  C     . PHE A 293 ? 1.30247 0.99778 1.53081 0.07350  -0.29077 0.19190  372 PHE B C     
2275 O  O     . PHE A 293 ? 1.42306 1.09571 1.66490 0.07219  -0.30250 0.18750  372 PHE B O     
2276 C  CB    . PHE A 293 ? 1.19629 0.87713 1.44305 0.10323  -0.30564 0.17921  372 PHE B CB    
2277 C  CG    . PHE A 293 ? 1.37132 1.05596 1.63177 0.09125  -0.31047 0.20632  372 PHE B CG    
2278 C  CD1   . PHE A 293 ? 1.24602 0.95110 1.50172 0.09358  -0.30415 0.21528  372 PHE B CD1   
2279 C  CD2   . PHE A 293 ? 1.31053 0.97885 1.58936 0.07787  -0.32178 0.22344  372 PHE B CD2   
2280 C  CE1   . PHE A 293 ? 1.17343 0.88244 1.44003 0.08336  -0.30920 0.24033  372 PHE B CE1   
2281 C  CE2   . PHE A 293 ? 1.29677 0.96965 1.58699 0.06727  -0.32587 0.24975  372 PHE B CE2   
2282 C  CZ    . PHE A 293 ? 1.17849 0.87158 1.46146 0.07036  -0.31974 0.25797  372 PHE B CZ    
2283 N  N     . GLY A 294 ? 1.26693 0.98434 1.48559 0.05858  -0.27965 0.20985  373 GLY B N     
2284 C  CA    . GLY A 294 ? 1.20740 0.92410 1.43150 0.04021  -0.28017 0.22651  373 GLY B CA    
2285 C  C     . GLY A 294 ? 1.26727 0.98584 1.47907 0.03479  -0.27261 0.21542  373 GLY B C     
2286 O  O     . GLY A 294 ? 1.31477 1.02919 1.53507 0.02120  -0.27505 0.22640  373 GLY B O     
2287 N  N     . ILE A 295 ? 1.26472 0.99039 1.45734 0.04513  -0.26330 0.19465  374 ILE B N     
2288 C  CA    . ILE A 295 ? 1.29956 1.02713 1.47966 0.04080  -0.25635 0.18388  374 ILE B CA    
2289 C  C     . ILE A 295 ? 1.23728 0.98782 1.40500 0.02419  -0.24265 0.19807  374 ILE B C     
2290 O  O     . ILE A 295 ? 1.24665 0.99771 1.41021 0.01624  -0.23906 0.19563  374 ILE B O     
2291 C  CB    . ILE A 295 ? 1.28714 1.01787 1.44882 0.05658  -0.24934 0.15974  374 ILE B CB    
2292 C  CG1   . ILE A 295 ? 1.32184 1.04570 1.47552 0.05532  -0.24814 0.14622  374 ILE B CG1   
2293 C  CG2   . ILE A 295 ? 1.22165 0.97998 1.36359 0.05675  -0.23259 0.16149  374 ILE B CG2   
2294 C  CD1   . ILE A 295 ? 1.26288 0.95913 1.43743 0.05517  -0.26585 0.14280  374 ILE B CD1   
2295 N  N     . PHE A 296 ? 1.19880 0.96853 1.36092 0.01921  -0.23558 0.21248  375 PHE B N     
2296 C  CA    . PHE A 296 ? 1.23463 1.02711 1.38405 0.00474  -0.22310 0.22536  375 PHE B CA    
2297 C  C     . PHE A 296 ? 1.26120 1.05676 1.42359 -0.00795 -0.22792 0.25075  375 PHE B C     
2298 O  O     . PHE A 296 ? 1.21817 1.03536 1.36921 -0.01768 -0.21824 0.26329  375 PHE B O     
2299 C  CB    . PHE A 296 ? 1.10760 0.92297 1.23676 0.00872  -0.20988 0.22055  375 PHE B CB    
2300 C  CG    . PHE A 296 ? 1.22410 1.04018 1.33916 0.01978  -0.20284 0.19833  375 PHE B CG    
2301 C  CD1   . PHE A 296 ? 1.21140 1.01920 1.32180 0.01909  -0.20148 0.18665  375 PHE B CD1   
2302 C  CD2   . PHE A 296 ? 1.15684 0.98281 1.26397 0.03096  -0.19764 0.18997  375 PHE B CD2   
2303 C  CE1   . PHE A 296 ? 1.14520 0.95426 1.24142 0.02959  -0.19497 0.16753  375 PHE B CE1   
2304 C  CE2   . PHE A 296 ? 1.14745 0.97559 1.24172 0.04110  -0.19037 0.17139  375 PHE B CE2   
2305 C  CZ    . PHE A 296 ? 1.16397 0.98343 1.25186 0.04054  -0.18902 0.16040  375 PHE B CZ    
2306 N  N     . SER A 297 ? 1.11943 0.89382 1.30544 -0.00776 -0.24304 0.25873  376 SER B N     
2307 C  CA    . SER A 297 ? 1.21326 0.98982 1.41321 -0.02000 -0.24805 0.28487  376 SER B CA    
2308 C  C     . SER A 297 ? 1.34862 1.13448 1.54812 -0.03589 -0.24180 0.29640  376 SER B C     
2309 O  O     . SER A 297 ? 1.31102 1.10586 1.51701 -0.04721 -0.24184 0.31969  376 SER B O     
2310 C  CB    . SER A 297 ? 1.22394 0.97327 1.45197 -0.01578 -0.26678 0.29029  376 SER B CB    
2311 O  OG    . SER A 297 ? 1.27782 1.00571 1.51920 -0.01512 -0.27522 0.27904  376 SER B OG    
2312 N  N     . ARG A 298 ? 1.29305 1.07796 1.48524 -0.03656 -0.23637 0.28125  377 ARG B N     
2313 C  CA    . ARG A 298 ? 1.27680 1.07307 1.46774 -0.05054 -0.22904 0.29007  377 ARG B CA    
2314 C  C     . ARG A 298 ? 1.27974 1.09687 1.44440 -0.05118 -0.21268 0.27826  377 ARG B C     
2315 O  O     . ARG A 298 ? 1.26516 1.09298 1.42709 -0.06136 -0.20552 0.28273  377 ARG B O     
2316 C  CB    . ARG A 298 ? 1.38718 1.16168 1.59913 -0.05300 -0.23977 0.28528  377 ARG B CB    
2317 C  CG    . ARG A 298 ? 1.32503 1.07610 1.56671 -0.05328 -0.25765 0.29673  377 ARG B CG    
2318 C  CD    . ARG A 298 ? 1.49537 1.22710 1.75923 -0.05794 -0.26822 0.29306  377 ARG B CD    
2319 N  NE    . ARG A 298 ? 1.58809 1.29475 1.88269 -0.05786 -0.28692 0.30250  377 ARG B NE    
2320 C  CZ    . ARG A 298 ? 1.61485 1.30275 1.93573 -0.06368 -0.29940 0.30424  377 ARG B CZ    
2321 N  NH1   . ARG A 298 ? 1.52054 1.21258 1.84112 -0.07010 -0.29524 0.29760  377 ARG B NH1   
2322 N  NH2   . ARG A 298 ? 1.48416 1.14832 1.83381 -0.06310 -0.31722 0.31295  377 ARG B NH2   
2323 N  N     . ALA A 299 ? 1.12955 0.95306 1.27635 -0.04063 -0.20669 0.26378  378 ALA B N     
2324 C  CA    . ALA A 299 ? 1.20000 1.04180 1.32324 -0.04073 -0.19200 0.25236  378 ALA B CA    
2325 C  C     . ALA A 299 ? 1.17482 1.04171 1.28449 -0.04731 -0.18241 0.26565  378 ALA B C     
2326 O  O     . ALA A 299 ? 1.22622 1.10286 1.32409 -0.04102 -0.17828 0.26109  378 ALA B O     
2327 C  CB    . ALA A 299 ? 1.28057 1.11632 1.39334 -0.02618 -0.19060 0.23035  378 ALA B CB    
2328 N  N     . LYS A 300 ? 1.04279 0.92129 1.15449 -0.06000 -0.17893 0.28221  379 LYS B N     
2329 C  CA    . LYS A 300 ? 1.20225 1.10433 1.30148 -0.06628 -0.17146 0.29639  379 LYS B CA    
2330 C  C     . LYS A 300 ? 1.14701 1.06967 1.22339 -0.06825 -0.15734 0.28667  379 LYS B C     
2331 O  O     . LYS A 300 ? 1.16330 1.10559 1.22633 -0.07103 -0.15144 0.29376  379 LYS B O     
2332 C  CB    . LYS A 300 ? 1.28454 1.19169 1.39577 -0.07824 -0.17385 0.32026  379 LYS B CB    
2333 C  CG    . LYS A 300 ? 1.27203 1.16138 1.40581 -0.07718 -0.18822 0.33428  379 LYS B CG    
2334 C  CD    . LYS A 300 ? 1.49336 1.38335 1.64423 -0.08955 -0.19127 0.35668  379 LYS B CD    
2335 C  CE    . LYS A 300 ? 1.51148 1.37999 1.68805 -0.08845 -0.20711 0.36984  379 LYS B CE    
2336 N  NZ    . LYS A 300 ? 1.53698 1.40314 1.73484 -0.10090 -0.21098 0.39094  379 LYS B NZ    
2337 N  N     . VAL A 301 ? 1.13087 1.04915 1.20261 -0.06650 -0.15266 0.27042  380 VAL B N     
2338 C  CA    . VAL A 301 ? 1.18039 1.11529 1.23201 -0.06723 -0.14027 0.25953  380 VAL B CA    
2339 C  C     . VAL A 301 ? 1.16435 1.09385 1.20691 -0.05633 -0.13821 0.24010  380 VAL B C     
2340 O  O     . VAL A 301 ? 1.07609 1.01811 1.10304 -0.05622 -0.12865 0.23077  380 VAL B O     
2341 C  CB    . VAL A 301 ? 1.12096 1.05912 1.17275 -0.07444 -0.13474 0.25747  380 VAL B CB    
2342 C  CG1   . VAL A 301 ? 1.10957 1.06474 1.16256 -0.08566 -0.13093 0.27657  380 VAL B CG1   
2343 C  CG2   . VAL A 301 ? 1.07119 0.98675 1.14026 -0.07226 -0.14357 0.25182  380 VAL B CG2   
2344 N  N     . LEU A 302 ? 1.17069 1.08237 1.22307 -0.04687 -0.14682 0.23389  381 LEU B N     
2345 C  CA    . LEU A 302 ? 1.07873 0.98664 1.12317 -0.03552 -0.14440 0.21661  381 LEU B CA    
2346 C  C     . LEU A 302 ? 1.08807 1.01329 1.12202 -0.03377 -0.13897 0.21829  381 LEU B C     
2347 O  O     . LEU A 302 ? 1.08791 1.01440 1.12837 -0.03196 -0.14469 0.22777  381 LEU B O     
2348 C  CB    . LEU A 302 ? 0.96167 0.84779 1.01968 -0.02504 -0.15545 0.21051  381 LEU B CB    
2349 C  CG    . LEU A 302 ? 1.00036 0.88219 1.05128 -0.01158 -0.15326 0.19284  381 LEU B CG    
2350 C  CD1   . LEU A 302 ? 1.06278 0.94511 1.10168 -0.01079 -0.14566 0.17899  381 LEU B CD1   
2351 C  CD2   . LEU A 302 ? 1.10908 0.97002 1.17406 -0.00064 -0.16528 0.18770  381 LEU B CD2   
2352 N  N     . SER A 303 ? 0.95915 0.89754 0.97809 -0.03449 -0.12870 0.20937  382 SER B N     
2353 C  CA    . SER A 303 ? 0.92457 0.88002 0.93460 -0.03381 -0.12384 0.20996  382 SER B CA    
2354 C  C     . SER A 303 ? 0.99140 0.94672 0.99739 -0.02396 -0.11991 0.19584  382 SER B C     
2355 O  O     . SER A 303 ? 0.95642 0.92394 0.95999 -0.02189 -0.11799 0.19657  382 SER B O     
2356 C  CB    . SER A 303 ? 0.94334 0.91691 0.94025 -0.04336 -0.11544 0.21248  382 SER B CB    
2357 O  OG    . SER A 303 ? 1.01924 0.99400 1.00696 -0.04239 -0.10753 0.19885  382 SER B OG    
2358 N  N     . LYS A 304 ? 0.90301 0.84597 0.90849 -0.01780 -0.11875 0.18360  383 LYS B N     
2359 C  CA    . LYS A 304 ? 0.89882 0.84275 0.89967 -0.00806 -0.11388 0.17107  383 LYS B CA    
2360 C  C     . LYS A 304 ? 0.90338 0.82911 0.91180 0.00346  -0.12037 0.16335  383 LYS B C     
2361 O  O     . LYS A 304 ? 0.88855 0.79972 0.89970 0.00328  -0.12481 0.16018  383 LYS B O     
2362 C  CB    . LYS A 304 ? 0.97458 0.92413 0.96292 -0.01084 -0.10424 0.16204  383 LYS B CB    
2363 C  CG    . LYS A 304 ? 1.01060 0.97808 0.99083 -0.02047 -0.09778 0.16648  383 LYS B CG    
2364 C  CD    . LYS A 304 ? 1.03487 1.00619 1.00465 -0.02153 -0.08899 0.15657  383 LYS B CD    
2365 C  CE    . LYS A 304 ? 1.19754 1.18568 1.16007 -0.03022 -0.08365 0.15926  383 LYS B CE    
2366 N  NZ    . LYS A 304 ? 1.35577 1.34660 1.30992 -0.03099 -0.07584 0.14980  383 LYS B NZ    
2367 N  N     . LEU A 305 ? 0.94178 0.86894 0.95411 0.01390  -0.12127 0.15976  384 LEU B N     
2368 C  CA    . LEU A 305 ? 0.87657 0.78854 0.89424 0.02728  -0.12659 0.15010  384 LEU B CA    
2369 C  C     . LEU A 305 ? 0.98279 0.90401 0.99386 0.03761  -0.11826 0.14009  384 LEU B C     
2370 O  O     . LEU A 305 ? 1.00232 0.94004 1.01371 0.03687  -0.11307 0.14401  384 LEU B O     
2371 C  CB    . LEU A 305 ? 0.84248 0.74537 0.87548 0.03190  -0.13796 0.15682  384 LEU B CB    
2372 C  CG    . LEU A 305 ? 0.90189 0.78825 0.94149 0.04717  -0.14493 0.14566  384 LEU B CG    
2373 C  CD1   . LEU A 305 ? 0.92862 0.79797 0.96495 0.04828  -0.14831 0.13625  384 LEU B CD1   
2374 C  CD2   . LEU A 305 ? 0.95286 0.82961 1.00941 0.05062  -0.15712 0.15354  384 LEU B CD2   
2375 N  N     . ASN A 306 ? 0.89500 0.80638 0.90046 0.04724  -0.11717 0.12757  385 ASN B N     
2376 C  CA    . ASN A 306 ? 0.83602 0.75627 0.83437 0.05801  -0.10850 0.11846  385 ASN B CA    
2377 C  C     . ASN A 306 ? 0.97365 0.88023 0.97491 0.07430  -0.11456 0.10782  385 ASN B C     
2378 O  O     . ASN A 306 ? 1.03529 0.92675 1.03147 0.07829  -0.11868 0.09908  385 ASN B O     
2379 C  CB    . ASN A 306 ? 0.83932 0.76430 0.82332 0.05400  -0.09893 0.11325  385 ASN B CB    
2380 C  CG    . ASN A 306 ? 0.96128 0.89949 0.93882 0.06253  -0.08833 0.10781  385 ASN B CG    
2381 O  OD1   . ASN A 306 ? 0.96465 0.90626 0.94710 0.07438  -0.08821 0.10483  385 ASN B OD1   
2382 N  ND2   . ASN A 306 ? 1.02271 0.96897 0.99018 0.05669  -0.07923 0.10700  385 ASN B ND2   
2383 N  N     . MET A 307 ? 0.98494 0.89717 0.99463 0.08427  -0.11563 0.10783  386 MET B N     
2384 C  CA    . MET A 307 ? 0.93329 0.83498 0.94572 0.10182  -0.12075 0.09659  386 MET B CA    
2385 C  C     . MET A 307 ? 0.94233 0.86024 0.94843 0.11415  -0.10945 0.08984  386 MET B C     
2386 O  O     . MET A 307 ? 0.97015 0.88715 0.98141 0.12949  -0.11179 0.08312  386 MET B O     
2387 C  CB    . MET A 307 ? 0.91862 0.81172 0.94840 0.10547  -0.13276 0.10155  386 MET B CB    
2388 C  CG    . MET A 307 ? 1.01356 0.88873 1.05141 0.09513  -0.14484 0.10843  386 MET B CG    
2389 S  SD    . MET A 307 ? 1.05198 0.90286 1.08462 0.10025  -0.15267 0.09480  386 MET B SD    
2390 C  CE    . MET A 307 ? 1.13404 0.97629 1.16972 0.12420  -0.15801 0.07893  386 MET B CE    
2391 N  N     . LYS A 308 ? 0.95263 0.88576 0.94846 0.10782  -0.09714 0.09186  387 LYS B N     
2392 C  CA    . LYS A 308 ? 0.94515 0.89649 0.93694 0.11729  -0.08517 0.08865  387 LYS B CA    
2393 C  C     . LYS A 308 ? 0.98662 0.93053 0.96866 0.13517  -0.08446 0.07462  387 LYS B C     
2394 O  O     . LYS A 308 ? 1.04612 0.97279 1.01888 0.13680  -0.09007 0.06676  387 LYS B O     
2395 C  CB    . LYS A 308 ? 0.89241 0.85779 0.87551 0.10582  -0.07360 0.09366  387 LYS B CB    
2396 C  CG    . LYS A 308 ? 0.90264 0.88999 0.88602 0.11176  -0.06080 0.09475  387 LYS B CG    
2397 C  CD    . LYS A 308 ? 1.06727 1.06111 1.03816 0.10507  -0.05048 0.09529  387 LYS B CD    
2398 C  CE    . LYS A 308 ? 0.92416 0.94176 0.90141 0.10260  -0.03895 0.10230  387 LYS B CE    
2399 N  NZ    . LYS A 308 ? 0.98355 1.00931 0.97225 0.08753  -0.04134 0.11218  387 LYS B NZ    
2400 N  N     . ASP A 309 ? 0.97822 0.93619 0.96264 0.14916  -0.07777 0.07126  388 ASP B N     
2401 C  CA    . ASP A 309 ? 1.03773 0.99321 1.01070 0.16794  -0.07501 0.05782  388 ASP B CA    
2402 C  C     . ASP A 309 ? 1.07089 1.00093 1.04387 0.17732  -0.09002 0.04638  388 ASP B C     
2403 O  O     . ASP A 309 ? 1.06666 0.98158 1.02711 0.17789  -0.09418 0.03839  388 ASP B O     
2404 C  CB    . ASP A 309 ? 0.97734 0.93794 0.93152 0.16589  -0.06450 0.05562  388 ASP B CB    
2405 C  CG    . ASP A 309 ? 0.95994 0.92599 0.90084 0.18581  -0.05789 0.04436  388 ASP B CG    
2406 O  OD1   . ASP A 309 ? 1.25612 1.24055 1.20291 0.19617  -0.04991 0.04547  388 ASP B OD1   
2407 O  OD2   . ASP A 309 ? 1.15439 1.10752 1.07903 0.19153  -0.06066 0.03450  388 ASP B OD2   
2408 N  N     . ASN A 310 ? 1.07481 0.99958 1.06298 0.18489  -0.09902 0.04532  389 ASN B N     
2409 C  CA    . ASN A 310 ? 1.18537 1.08479 1.17726 0.19401  -0.11487 0.03460  389 ASN B CA    
2410 C  C     . ASN A 310 ? 1.20844 1.11036 1.21106 0.21275  -0.11836 0.02772  389 ASN B C     
2411 O  O     . ASN A 310 ? 1.19091 1.11468 1.19235 0.22266  -0.10653 0.02726  389 ASN B O     
2412 C  CB    . ASN A 310 ? 1.14939 1.03157 1.15327 0.17726  -0.12753 0.04389  389 ASN B CB    
2413 C  CG    . ASN A 310 ? 1.12983 1.00063 1.12259 0.16523  -0.12908 0.04345  389 ASN B CG    
2414 O  OD1   . ASN A 310 ? 1.10616 0.95782 1.09388 0.17152  -0.13819 0.03201  389 ASN B OD1   
2415 N  ND2   . ASN A 310 ? 1.03717 0.91961 1.02717 0.14808  -0.12107 0.05544  389 ASN B ND2   
2416 N  N     . GLN A 311 ? 1.17734 1.05690 1.19183 0.21792  -0.13487 0.02246  390 GLN B N     
2417 C  CA    . GLN A 311 ? 1.26338 1.14133 1.28926 0.23690  -0.14074 0.01414  390 GLN B CA    
2418 C  C     . GLN A 311 ? 1.19193 1.06347 1.24147 0.23014  -0.15174 0.02550  390 GLN B C     
2419 O  O     . GLN A 311 ? 1.22392 1.08400 1.28606 0.24403  -0.16271 0.01818  390 GLN B O     
2420 C  CB    . GLN A 311 ? 1.31201 1.16748 1.33104 0.25411  -0.15216 -0.00575 390 GLN B CB    
2421 C  CG    . GLN A 311 ? 1.35938 1.22143 1.35338 0.26404  -0.14227 -0.01820 390 GLN B CG    
2422 C  CD    . GLN A 311 ? 1.43720 1.32473 1.42425 0.28196  -0.12770 -0.02348 390 GLN B CD    
2423 O  OE1   . GLN A 311 ? 1.50198 1.38872 1.49646 0.30062  -0.13224 -0.03350 390 GLN B OE1   
2424 N  NE2   . GLN A 311 ? 1.37381 1.28466 1.34782 0.27655  -0.11006 -0.01633 390 GLN B NE2   
2425 N  N     . LEU A 312 ? 1.14256 1.02149 1.19803 0.20987  -0.14935 0.04305  391 LEU B N     
2426 C  CA    . LEU A 312 ? 1.06927 0.94255 1.14525 0.20233  -0.15998 0.05563  391 LEU B CA    
2427 C  C     . LEU A 312 ? 1.21854 1.10984 1.30722 0.21401  -0.15635 0.05734  391 LEU B C     
2428 O  O     . LEU A 312 ? 1.24377 1.16123 1.32901 0.21274  -0.14210 0.06200  391 LEU B O     
2429 C  CB    . LEU A 312 ? 0.95165 0.83130 1.02732 0.17871  -0.15700 0.07321  391 LEU B CB    
2430 C  CG    . LEU A 312 ? 1.04602 0.91022 1.11165 0.16551  -0.16018 0.07366  391 LEU B CG    
2431 C  CD1   . LEU A 312 ? 0.84334 0.71853 0.90783 0.14404  -0.15515 0.09048  391 LEU B CD1   
2432 C  CD2   . LEU A 312 ? 1.06414 0.89916 1.14084 0.16779  -0.17816 0.06994  391 LEU B CD2   
2433 N  N     . THR A 313 ? 1.15159 1.02885 1.25664 0.22548  -0.16974 0.05361  392 THR B N     
2434 C  CA    . THR A 313 ? 1.12288 1.01561 1.24346 0.23646  -0.16863 0.05608  392 THR B CA    
2435 C  C     . THR A 313 ? 1.06631 0.95640 1.20579 0.22467  -0.17858 0.07341  392 THR B C     
2436 O  O     . THR A 313 ? 1.21976 1.12782 1.37176 0.22880  -0.17591 0.07966  392 THR B O     
2437 C  CB    . THR A 313 ? 1.03683 0.91815 1.16312 0.26127  -0.17621 0.03822  392 THR B CB    
2438 O  OG1   . THR A 313 ? 1.19098 1.03920 1.32466 0.26138  -0.19500 0.03393  392 THR B OG1   
2439 C  CG2   . THR A 313 ? 1.11487 1.00517 1.22111 0.27564  -0.16425 0.02153  392 THR B CG2   
2440 N  N     . SER A 314 ? 1.04801 0.91735 1.19013 0.21035  -0.18987 0.08186  393 SER B N     
2441 C  CA    . SER A 314 ? 1.09252 0.95949 1.25013 0.19807  -0.19909 0.10013  393 SER B CA    
2442 C  C     . SER A 314 ? 1.07509 0.93015 1.22599 0.17751  -0.20244 0.11082  393 SER B C     
2443 O  O     . SER A 314 ? 1.04702 0.89308 1.18431 0.17431  -0.19964 0.10285  393 SER B O     
2444 C  CB    . SER A 314 ? 1.02459 0.87261 1.20323 0.21066  -0.21596 0.09829  393 SER B CB    
2445 O  OG    . SER A 314 ? 1.13328 0.95209 1.31227 0.21596  -0.22761 0.08709  393 SER B OG    
2446 N  N     . LEU A 315 ? 1.09903 0.95527 1.25957 0.16408  -0.20841 0.12920  394 LEU B N     
2447 C  CA    . LEU A 315 ? 1.04950 0.89777 1.20483 0.14456  -0.21084 0.14139  394 LEU B CA    
2448 C  C     . LEU A 315 ? 1.09146 0.91405 1.26397 0.14213  -0.22876 0.14961  394 LEU B C     
2449 O  O     . LEU A 315 ? 1.23928 1.05501 1.42896 0.15212  -0.23911 0.15153  394 LEU B O     
2450 C  CB    . LEU A 315 ? 0.96837 0.83996 1.11853 0.12911  -0.20271 0.15760  394 LEU B CB    
2451 C  CG    . LEU A 315 ? 1.03061 0.92713 1.16577 0.12870  -0.18558 0.15143  394 LEU B CG    
2452 C  CD1   . LEU A 315 ? 1.08229 1.00049 1.21512 0.11477  -0.18028 0.16634  394 LEU B CD1   
2453 C  CD2   . LEU A 315 ? 0.99963 0.89070 1.11746 0.12477  -0.17794 0.14153  394 LEU B CD2   
2454 N  N     . PRO A 316 ? 1.07686 0.88492 1.24687 0.12915  -0.23304 0.15497  395 PRO B N     
2455 C  CA    . PRO A 316 ? 1.11056 0.89507 1.29916 0.12476  -0.24993 0.16565  395 PRO B CA    
2456 C  C     . PRO A 316 ? 1.08898 0.88263 1.28814 0.11675  -0.25420 0.18722  395 PRO B C     
2457 O  O     . PRO A 316 ? 1.19821 1.01613 1.38751 0.10930  -0.24392 0.19594  395 PRO B O     
2458 C  CB    . PRO A 316 ? 1.15477 0.93005 1.33638 0.10972  -0.24936 0.16910  395 PRO B CB    
2459 C  CG    . PRO A 316 ? 1.15023 0.94923 1.30942 0.10225  -0.23157 0.16687  395 PRO B CG    
2460 C  CD    . PRO A 316 ? 1.14711 0.95971 1.29892 0.11812  -0.22285 0.15182  395 PRO B CD    
2461 N  N     . LEU A 317 ? 1.14668 0.91990 1.36666 0.11870  -0.27058 0.19581  396 LEU B N     
2462 C  CA    . LEU A 317 ? 1.25098 1.03130 1.48210 0.11339  -0.27648 0.21649  396 LEU B CA    
2463 C  C     . LEU A 317 ? 1.29342 1.08544 1.51571 0.09234  -0.27165 0.23722  396 LEU B C     
2464 O  O     . LEU A 317 ? 1.32884 1.13917 1.54890 0.08682  -0.26923 0.25176  396 LEU B O     
2465 C  CB    . LEU A 317 ? 1.24651 1.00026 1.50317 0.12070  -0.29593 0.22128  396 LEU B CB    
2466 C  CG    . LEU A 317 ? 1.28798 1.03012 1.55521 0.14351  -0.30239 0.20085  396 LEU B CG    
2467 C  CD1   . LEU A 317 ? 1.16637 0.88347 1.46072 0.14994  -0.32261 0.20822  396 LEU B CD1   
2468 C  CD2   . LEU A 317 ? 1.24449 1.01332 1.50393 0.15420  -0.29094 0.19373  396 LEU B CD2   
2469 N  N     . ASP A 318 ? 1.17330 0.95615 1.39043 0.08102  -0.27036 0.23852  397 ASP B N     
2470 C  CA    . ASP A 318 ? 1.21406 1.00963 1.42156 0.06191  -0.26430 0.25664  397 ASP B CA    
2471 C  C     . ASP A 318 ? 1.30020 1.11883 1.48337 0.05630  -0.24667 0.24876  397 ASP B C     
2472 O  O     . ASP A 318 ? 1.22424 1.05086 1.39736 0.04167  -0.24045 0.25798  397 ASP B O     
2473 C  CB    . ASP A 318 ? 1.19387 0.96889 1.41178 0.05175  -0.27246 0.26455  397 ASP B CB    
2474 C  CG    . ASP A 318 ? 1.19023 0.95380 1.40232 0.05461  -0.26938 0.24482  397 ASP B CG    
2475 O  OD1   . ASP A 318 ? 1.26446 1.02984 1.46806 0.06801  -0.26432 0.22403  397 ASP B OD1   
2476 O  OD2   . ASP A 318 ? 1.16405 0.91760 1.38047 0.04358  -0.27211 0.25073  397 ASP B OD2   
2477 N  N     . PHE A 319 ? 1.21433 1.04410 1.38892 0.06783  -0.23849 0.23223  398 PHE B N     
2478 C  CA    . PHE A 319 ? 1.24158 1.09286 1.39510 0.06278  -0.22238 0.22537  398 PHE B CA    
2479 C  C     . PHE A 319 ? 1.21857 1.09258 1.36348 0.05039  -0.21683 0.24160  398 PHE B C     
2480 O  O     . PHE A 319 ? 1.28803 1.17686 1.41631 0.04136  -0.20542 0.24020  398 PHE B O     
2481 C  CB    . PHE A 319 ? 1.22900 1.08826 1.37842 0.07821  -0.21550 0.20687  398 PHE B CB    
2482 C  CG    . PHE A 319 ? 1.14745 1.03461 1.28657 0.07595  -0.20408 0.20857  398 PHE B CG    
2483 C  CD1   . PHE A 319 ? 1.23069 1.13218 1.35203 0.06902  -0.19053 0.20276  398 PHE B CD1   
2484 C  CD2   . PHE A 319 ? 1.23900 1.13759 1.38779 0.08107  -0.20774 0.21556  398 PHE B CD2   
2485 C  CE1   . PHE A 319 ? 1.23666 1.16260 1.35080 0.06658  -0.18125 0.20402  398 PHE B CE1   
2486 C  CE2   . PHE A 319 ? 1.28698 1.21113 1.42846 0.07865  -0.19844 0.21674  398 PHE B CE2   
2487 C  CZ    . PHE A 319 ? 1.16814 1.10559 1.29265 0.07119  -0.18535 0.21088  398 PHE B CZ    
2488 N  N     . GLY A 320 ? 1.18072 1.05730 1.33641 0.05015  -0.22543 0.25670  399 GLY B N     
2489 C  CA    . GLY A 320 ? 1.19620 1.09354 1.34329 0.03910  -0.22221 0.27265  399 GLY B CA    
2490 C  C     . GLY A 320 ? 1.12382 1.02099 1.26464 0.02325  -0.22186 0.28804  399 GLY B C     
2491 O  O     . GLY A 320 ? 1.08823 1.00473 1.21743 0.01397  -0.21730 0.29915  399 GLY B O     
2492 N  N     . THR A 321 ? 0.97494 0.85176 1.12360 0.02021  -0.22672 0.28880  400 THR B N     
2493 C  CA    . THR A 321 ? 1.13413 1.01176 1.27905 0.00521  -0.22554 0.30367  400 THR B CA    
2494 C  C     . THR A 321 ? 1.05676 0.94296 1.18454 -0.00181 -0.21257 0.29336  400 THR B C     
2495 O  O     . THR A 321 ? 1.06383 0.95418 1.18712 -0.01411 -0.20958 0.30441  400 THR B O     
2496 C  CB    . THR A 321 ? 1.19648 1.04828 1.36213 0.00408  -0.23828 0.31177  400 THR B CB    
2497 O  OG1   . THR A 321 ? 1.16097 0.99444 1.33143 0.01158  -0.23946 0.29219  400 THR B OG1   
2498 C  CG2   . THR A 321 ? 1.08518 0.92674 1.26939 0.01130  -0.25219 0.32257  400 THR B CG2   
2499 N  N     . TRP A 322 ? 1.06981 0.95949 1.18849 0.00590  -0.20467 0.27326  401 TRP B N     
2500 C  CA    . TRP A 322 ? 0.92299 0.82121 1.02527 0.00008  -0.19248 0.26317  401 TRP B CA    
2501 C  C     . TRP A 322 ? 1.09702 1.02038 1.18312 -0.00963 -0.18360 0.27137  401 TRP B C     
2502 O  O     . TRP A 322 ? 1.10340 1.04139 1.17734 -0.00748 -0.17476 0.26100  401 TRP B O     
2503 C  CB    . TRP A 322 ? 0.97330 0.86976 1.07026 0.01158  -0.18661 0.24133  401 TRP B CB    
2504 C  CG    . TRP A 322 ? 1.02845 0.90128 1.13856 0.02323  -0.19521 0.23031  401 TRP B CG    
2505 C  CD1   . TRP A 322 ? 1.06473 0.91611 1.19145 0.02301  -0.20770 0.23651  401 TRP B CD1   
2506 C  CD2   . TRP A 322 ? 1.11112 0.97978 1.21890 0.03729  -0.19232 0.21089  401 TRP B CD2   
2507 N  NE1   . TRP A 322 ? 1.01085 0.84396 1.14529 0.03651  -0.21365 0.22055  401 TRP B NE1   
2508 C  CE2   . TRP A 322 ? 1.05170 0.89582 1.17358 0.04588  -0.20388 0.20472  401 TRP B CE2   
2509 C  CE3   . TRP A 322 ? 1.02065 0.90440 1.11625 0.04353  -0.18114 0.19860  401 TRP B CE3   
2510 C  CZ2   . TRP A 322 ? 1.00941 0.84458 1.13116 0.06144  -0.20430 0.18572  401 TRP B CZ2   
2511 C  CZ3   . TRP A 322 ? 1.03288 0.90868 1.12912 0.05832  -0.18064 0.18164  401 TRP B CZ3   
2512 C  CH2   . TRP A 322 ? 0.95298 0.80510 1.06101 0.06763  -0.19200 0.17483  401 TRP B CH2   
2513 N  N     . THR A 323 ? 1.06002 0.98877 1.14616 -0.02018 -0.18612 0.29007  402 THR B N     
2514 C  CA    . THR A 323 ? 0.96105 0.91382 1.03192 -0.02787 -0.17998 0.29898  402 THR B CA    
2515 C  C     . THR A 323 ? 1.03769 1.00272 1.09134 -0.03531 -0.16771 0.29123  402 THR B C     
2516 O  O     . THR A 323 ? 1.07638 1.06146 1.11545 -0.03879 -0.16154 0.29126  402 THR B O     
2517 C  CB    . THR A 323 ? 0.87889 0.83432 0.95459 -0.03553 -0.18675 0.32262  402 THR B CB    
2518 O  OG1   . THR A 323 ? 0.93991 0.88338 1.02324 -0.04274 -0.18795 0.32977  402 THR B OG1   
2519 C  CG2   . THR A 323 ? 0.86941 0.81493 0.96139 -0.02783 -0.19927 0.33102  402 THR B CG2   
2520 N  N     . SER A 324 ? 0.99047 0.94377 1.04608 -0.03746 -0.16489 0.28414  403 SER B N     
2521 C  CA    . SER A 324 ? 1.00121 0.96479 1.04212 -0.04377 -0.15377 0.27629  403 SER B CA    
2522 C  C     . SER A 324 ? 1.00201 0.96680 1.03488 -0.03686 -0.14673 0.25598  403 SER B C     
2523 O  O     . SER A 324 ? 1.06120 1.03277 1.08266 -0.04100 -0.13790 0.24789  403 SER B O     
2524 C  CB    . SER A 324 ? 1.14518 1.09701 1.19316 -0.04987 -0.15431 0.27928  403 SER B CB    
2525 O  OG    . SER A 324 ? 1.26404 1.19300 1.32587 -0.04239 -0.16114 0.27006  403 SER B OG    
2526 N  N     . MET A 325 ? 1.08084 1.04004 1.11998 -0.02625 -0.15021 0.24828  404 MET B N     
2527 C  CA    . MET A 325 ? 0.95637 0.91722 0.98942 -0.01908 -0.14328 0.23068  404 MET B CA    
2528 C  C     . MET A 325 ? 0.87178 0.85438 0.89259 -0.02222 -0.13588 0.22886  404 MET B C     
2529 O  O     . MET A 325 ? 0.97513 0.96883 0.99729 -0.02235 -0.13940 0.23697  404 MET B O     
2530 C  CB    . MET A 325 ? 1.00146 0.95106 1.04629 -0.00595 -0.14911 0.22392  404 MET B CB    
2531 C  CG    . MET A 325 ? 1.01778 0.96364 1.05834 0.00278  -0.14268 0.20603  404 MET B CG    
2532 S  SD    . MET A 325 ? 1.29542 1.21860 1.33825 0.00507  -0.14519 0.19692  404 MET B SD    
2533 C  CE    . MET A 325 ? 0.89650 0.79978 0.95934 0.01061  -0.16060 0.20465  404 MET B CE    
2534 N  N     . VAL A 326 ? 0.96215 0.95026 0.97191 -0.02460 -0.12657 0.21806  405 VAL B N     
2535 C  CA    . VAL A 326 ? 0.93565 0.94247 0.93514 -0.02767 -0.11996 0.21426  405 VAL B CA    
2536 C  C     . VAL A 326 ? 0.90221 0.91046 0.90347 -0.01940 -0.11537 0.20163  405 VAL B C     
2537 O  O     . VAL A 326 ? 0.83817 0.85948 0.84089 -0.01777 -0.11485 0.20144  405 VAL B O     
2538 C  CB    . VAL A 326 ? 0.87094 0.88464 0.85741 -0.03693 -0.11288 0.21233  405 VAL B CB    
2539 C  CG1   . VAL A 326 ? 0.85535 0.88574 0.83244 -0.03930 -0.10687 0.20583  405 VAL B CG1   
2540 C  CG2   . VAL A 326 ? 0.97667 0.99403 0.96113 -0.04502 -0.11626 0.22663  405 VAL B CG2   
2541 N  N     . GLU A 327 ? 0.90147 0.89728 0.90302 -0.01402 -0.11210 0.19146  406 GLU B N     
2542 C  CA    . GLU A 327 ? 0.81090 0.80806 0.81359 -0.00534 -0.10685 0.18041  406 GLU B CA    
2543 C  C     . GLU A 327 ? 0.97771 0.95895 0.98932 0.00612  -0.11165 0.17614  406 GLU B C     
2544 O  O     . GLU A 327 ? 1.00813 0.97360 1.02021 0.00654  -0.11520 0.17462  406 GLU B O     
2545 C  CB    . GLU A 327 ? 0.81148 0.81008 0.80336 -0.00831 -0.09762 0.17090  406 GLU B CB    
2546 C  CG    . GLU A 327 ? 0.90211 0.91481 0.88515 -0.01897 -0.09344 0.17314  406 GLU B CG    
2547 C  CD    . GLU A 327 ? 1.10516 1.11812 1.07927 -0.02118 -0.08501 0.16362  406 GLU B CD    
2548 O  OE1   . GLU A 327 ? 1.11933 1.12541 1.09393 -0.01385 -0.08133 0.15578  406 GLU B OE1   
2549 O  OE2   . GLU A 327 ? 1.14651 1.16678 1.11276 -0.02964 -0.08223 0.16398  406 GLU B OE2   
2550 N  N     . LEU A 328 ? 0.99495 0.98078 1.01453 0.01570  -0.11223 0.17379  407 LEU B N     
2551 C  CA    . LEU A 328 ? 0.90750 0.87994 0.93561 0.02862  -0.11692 0.16836  407 LEU B CA    
2552 C  C     . LEU A 328 ? 0.91926 0.90017 0.94727 0.03885  -0.10910 0.15867  407 LEU B C     
2553 O  O     . LEU A 328 ? 0.92094 0.91898 0.95286 0.03862  -0.10541 0.16123  407 LEU B O     
2554 C  CB    . LEU A 328 ? 0.92623 0.89539 0.96782 0.03187  -0.12760 0.17764  407 LEU B CB    
2555 C  CG    . LEU A 328 ? 0.90071 0.85520 0.95296 0.04628  -0.13413 0.17154  407 LEU B CG    
2556 C  CD1   . LEU A 328 ? 0.81068 0.74466 0.85954 0.04837  -0.13690 0.16403  407 LEU B CD1   
2557 C  CD2   . LEU A 328 ? 0.81213 0.76294 0.87863 0.04812  -0.14553 0.18234  407 LEU B CD2   
2558 N  N     . ASN A 329 ? 0.94652 0.91631 0.97038 0.04786  -0.10674 0.14794  408 ASN B N     
2559 C  CA    . ASN A 329 ? 0.85721 0.83513 0.87919 0.05858  -0.09821 0.13901  408 ASN B CA    
2560 C  C     . ASN A 329 ? 0.91173 0.87789 0.93998 0.07454  -0.10358 0.13170  408 ASN B C     
2561 O  O     . ASN A 329 ? 0.96974 0.91791 0.99365 0.07882  -0.10817 0.12482  408 ASN B O     
2562 C  CB    . ASN A 329 ? 0.73574 0.71333 0.74358 0.05577  -0.08919 0.13204  408 ASN B CB    
2563 C  CG    . ASN A 329 ? 0.82917 0.81968 0.83483 0.06439  -0.07863 0.12627  408 ASN B CG    
2564 O  OD1   . ASN A 329 ? 0.83108 0.82899 0.84558 0.07494  -0.07799 0.12531  408 ASN B OD1   
2565 N  ND2   . ASN A 329 ? 0.82907 0.82302 0.82378 0.06009  -0.07011 0.12309  408 ASN B ND2   
2566 N  N     . LEU A 330 ? 0.88097 0.85756 0.92013 0.08377  -0.10352 0.13247  409 LEU B N     
2567 C  CA    . LEU A 330 ? 0.84346 0.81167 0.88918 0.10092  -0.10784 0.12433  409 LEU B CA    
2568 C  C     . LEU A 330 ? 0.89607 0.88109 0.94105 0.11276  -0.09666 0.11771  409 LEU B C     
2569 O  O     . LEU A 330 ? 0.96140 0.94988 1.01621 0.12668  -0.09832 0.11411  409 LEU B O     
2570 C  CB    . LEU A 330 ? 0.77525 0.73941 0.83735 0.10352  -0.11938 0.13145  409 LEU B CB    
2571 C  CG    . LEU A 330 ? 0.82889 0.77461 0.89418 0.09434  -0.13158 0.13888  409 LEU B CG    
2572 C  CD1   . LEU A 330 ? 0.89510 0.84133 0.97662 0.09527  -0.14165 0.14909  409 LEU B CD1   
2573 C  CD2   . LEU A 330 ? 0.91126 0.83319 0.97386 0.10143  -0.13825 0.12891  409 LEU B CD2   
2574 N  N     . ALA A 331 ? 0.89677 0.89290 0.93100 0.10758  -0.08508 0.11659  410 ALA B N     
2575 C  CA    . ALA A 331 ? 0.90929 0.92391 0.94377 0.11696  -0.07320 0.11308  410 ALA B CA    
2576 C  C     . ALA A 331 ? 0.93067 0.93702 0.95733 0.13477  -0.07145 0.10033  410 ALA B C     
2577 O  O     . ALA A 331 ? 0.97887 0.96482 0.99599 0.13729  -0.07781 0.09298  410 ALA B O     
2578 C  CB    . ALA A 331 ? 0.76648 0.79361 0.79257 0.10574  -0.06213 0.11648  410 ALA B CB    
2579 N  N     . THR A 332 ? 0.96875 0.99232 1.00009 0.14758  -0.06292 0.09765  411 THR B N     
2580 C  CA    . THR A 332 ? 0.88199 0.90330 0.90459 0.16656  -0.05895 0.08536  411 THR B CA    
2581 C  C     . THR A 332 ? 0.92263 0.92054 0.94665 0.17745  -0.07304 0.07591  411 THR B C     
2582 O  O     . THR A 332 ? 0.91641 0.89515 0.92766 0.18071  -0.07814 0.06680  411 THR B O     
2583 C  CB    . THR A 332 ? 0.78618 0.80621 0.78883 0.16487  -0.05006 0.08107  411 THR B CB    
2584 O  OG1   . THR A 332 ? 0.86527 0.90443 0.86934 0.15262  -0.03892 0.09105  411 THR B OG1   
2585 C  CG2   . THR A 332 ? 0.85070 0.87467 0.84299 0.18539  -0.04353 0.06967  411 THR B CG2   
2586 N  N     . ASN A 333 ? 0.97329 0.97298 1.01479 0.18291  -0.08014 0.07846  412 ASN B N     
2587 C  CA    . ASN A 333 ? 1.01575 0.99470 1.06302 0.19511  -0.09395 0.06983  412 ASN B CA    
2588 C  C     . ASN A 333 ? 0.98933 0.98254 1.05173 0.21122  -0.09270 0.06772  412 ASN B C     
2589 O  O     . ASN A 333 ? 1.08452 1.10305 1.14890 0.21618  -0.07949 0.06969  412 ASN B O     
2590 C  CB    . ASN A 333 ? 1.03546 0.99478 1.09065 0.18107  -0.10847 0.07774  412 ASN B CB    
2591 C  CG    . ASN A 333 ? 1.04470 0.98554 1.08583 0.17059  -0.11198 0.07551  412 ASN B CG    
2592 O  OD1   . ASN A 333 ? 1.04304 0.96406 1.07847 0.17924  -0.11956 0.06413  412 ASN B OD1   
2593 N  ND2   . ASN A 333 ? 0.86113 0.80855 0.89750 0.15227  -0.10712 0.08580  412 ASN B ND2   
2594 N  N     . GLN A 334 ? 1.03333 1.01068 1.10817 0.21965  -0.10666 0.06410  413 GLN B N     
2595 C  CA    . GLN A 334 ? 1.07283 1.06156 1.16397 0.23590  -0.10750 0.06145  413 GLN B CA    
2596 C  C     . GLN A 334 ? 1.00302 0.98608 1.11457 0.22864  -0.12022 0.07265  413 GLN B C     
2597 O  O     . GLN A 334 ? 1.04544 1.02203 1.17142 0.24218  -0.12955 0.06835  413 GLN B O     
2598 C  CB    . GLN A 334 ? 1.12388 1.09951 1.21070 0.25899  -0.11236 0.04311  413 GLN B CB    
2599 C  CG    . GLN A 334 ? 1.09780 1.07753 1.16181 0.26780  -0.10117 0.03130  413 GLN B CG    
2600 C  CD    . GLN A 334 ? 1.33065 1.28333 1.37907 0.26136  -0.10971 0.02475  413 GLN B CD    
2601 O  OE1   . GLN A 334 ? 1.46641 1.39302 1.52029 0.26478  -0.12590 0.01824  413 GLN B OE1   
2602 N  NE2   . GLN A 334 ? 1.18978 1.14843 1.22040 0.25182  -0.09941 0.02683  413 GLN B NE2   
2603 N  N     . LEU A 335 ? 1.01012 0.99572 1.12276 0.20775  -0.12106 0.08716  414 LEU B N     
2604 C  CA    . LEU A 335 ? 0.95405 0.93559 1.08362 0.19973  -0.13288 0.09956  414 LEU B CA    
2605 C  C     . LEU A 335 ? 1.05051 1.05683 1.19738 0.20671  -0.12888 0.10452  414 LEU B C     
2606 O  O     . LEU A 335 ? 1.03643 1.06777 1.18270 0.20150  -0.11633 0.10931  414 LEU B O     
2607 C  CB    . LEU A 335 ? 0.93473 0.91508 1.05807 0.17652  -0.13362 0.11296  414 LEU B CB    
2608 C  CG    . LEU A 335 ? 1.08410 1.04019 1.19432 0.16769  -0.13931 0.11068  414 LEU B CG    
2609 C  CD1   . LEU A 335 ? 1.12280 1.08311 1.22687 0.14585  -0.13769 0.12391  414 LEU B CD1   
2610 C  CD2   . LEU A 335 ? 1.04806 0.97771 1.16866 0.17409  -0.15612 0.10841  414 LEU B CD2   
2611 N  N     . THR A 336 ? 1.13814 1.13731 1.30213 0.21843  -0.14017 0.10356  415 THR B N     
2612 C  CA    . THR A 336 ? 1.00953 1.03108 1.19278 0.22638  -0.13842 0.10805  415 THR B CA    
2613 C  C     . THR A 336 ? 1.03431 1.05830 1.23098 0.21297  -0.14823 0.12468  415 THR B C     
2614 O  O     . THR A 336 ? 1.01758 1.06233 1.23069 0.21663  -0.14714 0.13035  415 THR B O     
2615 C  CB    . THR A 336 ? 0.99146 1.00598 1.18647 0.25021  -0.14455 0.09569  415 THR B CB    
2616 O  OG1   . THR A 336 ? 1.14101 1.12544 1.34246 0.25058  -0.16287 0.09624  415 THR B OG1   
2617 C  CG2   . THR A 336 ? 1.15789 1.17177 1.33751 0.26522  -0.13480 0.07838  415 THR B CG2   
2618 N  N     . LYS A 337 ? 0.98913 0.99381 1.17932 0.19791  -0.15764 0.13291  416 LYS B N     
2619 C  CA    . LYS A 337 ? 0.93917 0.94488 1.13985 0.18613  -0.16787 0.14913  416 LYS B CA    
2620 C  C     . LYS A 337 ? 0.99962 0.99118 1.18590 0.16679  -0.17126 0.15766  416 LYS B C     
2621 O  O     . LYS A 337 ? 1.02284 0.99309 1.19887 0.16618  -0.17359 0.15133  416 LYS B O     
2622 C  CB    . LYS A 337 ? 0.95124 0.94248 1.17103 0.19824  -0.18344 0.15048  416 LYS B CB    
2623 C  CG    . LYS A 337 ? 1.11421 1.08270 1.33591 0.18679  -0.19862 0.16290  416 LYS B CG    
2624 C  CD    . LYS A 337 ? 1.21365 1.15236 1.44304 0.19903  -0.21146 0.15498  416 LYS B CD    
2625 C  CE    . LYS A 337 ? 1.24524 1.17067 1.45914 0.20390  -0.20551 0.13864  416 LYS B CE    
2626 N  NZ    . LYS A 337 ? 1.19905 1.09446 1.42127 0.21611  -0.21949 0.12928  416 LYS B NZ    
2627 N  N     . ILE A 338 ? 1.09865 1.10330 1.28440 0.15160  -0.17152 0.17146  417 ILE B N     
2628 C  CA    . ILE A 338 ? 1.01049 1.00496 1.18432 0.13355  -0.17542 0.18172  417 ILE B CA    
2629 C  C     . ILE A 338 ? 0.97918 0.96410 1.16524 0.13080  -0.19087 0.19575  417 ILE B C     
2630 O  O     . ILE A 338 ? 0.97387 0.97472 1.17103 0.13134  -0.19428 0.20403  417 ILE B O     
2631 C  CB    . ILE A 338 ? 1.02254 1.03815 1.18509 0.11874  -0.16530 0.18687  417 ILE B CB    
2632 C  CG1   . ILE A 338 ? 1.00452 1.02814 1.15568 0.12104  -0.15033 0.17443  417 ILE B CG1   
2633 C  CG2   . ILE A 338 ? 1.03329 1.04024 1.18397 0.10147  -0.16966 0.19769  417 ILE B CG2   
2634 C  CD1   . ILE A 338 ? 0.93667 0.93868 1.07443 0.12208  -0.14904 0.16539  417 ILE B CD1   
2635 N  N     . PRO A 339 ? 0.98650 0.94646 1.17210 0.12779  -0.20081 0.19954  418 PRO B N     
2636 C  CA    . PRO A 339 ? 0.88414 0.83384 1.08318 0.12627  -0.21599 0.21411  418 PRO B CA    
2637 C  C     . PRO A 339 ? 1.04517 1.01063 1.23890 0.11087  -0.21692 0.23122  418 PRO B C     
2638 O  O     . PRO A 339 ? 0.99057 0.96847 1.16825 0.09859  -0.20747 0.23226  418 PRO B O     
2639 C  CB    . PRO A 339 ? 1.00415 0.92458 1.20207 0.12347  -0.22410 0.21438  418 PRO B CB    
2640 C  CG    . PRO A 339 ? 1.14270 1.05653 1.33099 0.13058  -0.21532 0.19541  418 PRO B CG    
2641 C  CD    . PRO A 339 ? 1.09584 1.03542 1.27076 0.12662  -0.19934 0.19058  418 PRO B CD    
2642 N  N     . GLU A 340 ? 1.09910 1.06376 1.30649 0.11244  -0.22923 0.24448  419 GLU B N     
2643 C  CA    . GLU A 340 ? 1.06929 1.04746 1.27110 0.09907  -0.23246 0.26176  419 GLU B CA    
2644 C  C     . GLU A 340 ? 1.09970 1.06718 1.28722 0.08358  -0.23317 0.27206  419 GLU B C     
2645 O  O     . GLU A 340 ? 1.04056 1.02243 1.21636 0.07117  -0.23144 0.28302  419 GLU B O     
2646 C  CB    . GLU A 340 ? 0.99119 0.96883 1.21101 0.10530  -0.24671 0.27442  419 GLU B CB    
2647 C  CG    . GLU A 340 ? 1.13288 1.12780 1.36762 0.11871  -0.24607 0.26742  419 GLU B CG    
2648 C  CD    . GLU A 340 ? 1.12679 1.15138 1.35442 0.11119  -0.23880 0.26957  419 GLU B CD    
2649 O  OE1   . GLU A 340 ? 1.04951 1.08046 1.26023 0.09606  -0.23626 0.27761  419 GLU B OE1   
2650 O  OE2   . GLU A 340 ? 1.04910 1.09110 1.28895 0.12068  -0.23584 0.26285  419 GLU B OE2   
2651 N  N     . ASP A 341 ? 1.12652 1.06999 1.31524 0.08442  -0.23585 0.26839  420 ASP B N     
2652 C  CA    . ASP A 341 ? 1.10306 1.03662 1.28095 0.07008  -0.23605 0.27801  420 ASP B CA    
2653 C  C     . ASP A 341 ? 1.07819 1.02532 1.23492 0.05944  -0.22179 0.27169  420 ASP B C     
2654 O  O     . ASP A 341 ? 1.12596 1.06869 1.27269 0.04723  -0.22031 0.27928  420 ASP B O     
2655 C  CB    . ASP A 341 ? 1.23181 1.13626 1.41939 0.07453  -0.24308 0.27356  420 ASP B CB    
2656 C  CG    . ASP A 341 ? 1.49235 1.38055 1.70261 0.08623  -0.25815 0.27800  420 ASP B CG    
2657 O  OD1   . ASP A 341 ? 1.39649 1.28866 1.61626 0.10106  -0.25872 0.26688  420 ASP B OD1   
2658 O  OD2   . ASP A 341 ? 1.68848 1.56037 1.90808 0.08077  -0.26939 0.29301  420 ASP B OD2   
2659 N  N     . VAL A 342 ? 1.08345 1.04721 1.23445 0.06377  -0.21134 0.25860  421 VAL B N     
2660 C  CA    . VAL A 342 ? 0.95150 0.92844 1.08389 0.05401  -0.19849 0.25279  421 VAL B CA    
2661 C  C     . VAL A 342 ? 0.94946 0.94261 1.07055 0.04040  -0.19828 0.26648  421 VAL B C     
2662 O  O     . VAL A 342 ? 0.98972 0.99082 1.09482 0.03060  -0.18943 0.26382  421 VAL B O     
2663 C  CB    . VAL A 342 ? 1.01858 1.01042 1.15084 0.06218  -0.18840 0.23776  421 VAL B CB    
2664 C  CG1   . VAL A 342 ? 1.00251 1.01639 1.14154 0.06337  -0.19017 0.24337  421 VAL B CG1   
2665 C  CG2   . VAL A 342 ? 0.98783 0.98568 1.10289 0.05451  -0.17542 0.22865  421 VAL B CG2   
2666 N  N     . SER A 343 ? 0.98526 0.98346 1.11377 0.04019  -0.20831 0.28089  422 SER B N     
2667 C  CA    . SER A 343 ? 1.01242 1.02702 1.12871 0.02864  -0.20912 0.29392  422 SER B CA    
2668 C  C     . SER A 343 ? 0.98240 0.98936 1.08677 0.01670  -0.20848 0.30418  422 SER B C     
2669 O  O     . SER A 343 ? 1.02514 1.04715 1.11495 0.00686  -0.20631 0.31233  422 SER B O     
2670 C  CB    . SER A 343 ? 0.93025 0.95117 1.05762 0.03254  -0.22117 0.30756  422 SER B CB    
2671 O  OG    . SER A 343 ? 1.08585 1.08597 1.22773 0.03753  -0.23198 0.31677  422 SER B OG    
2672 N  N     . GLY A 344 ? 0.92733 0.91233 1.03801 0.01760  -0.21048 0.30370  423 GLY B N     
2673 C  CA    . GLY A 344 ? 0.98221 0.96074 1.08476 0.00617  -0.20958 0.31401  423 GLY B CA    
2674 C  C     . GLY A 344 ? 1.02580 1.00924 1.11216 -0.00114 -0.19701 0.30330  423 GLY B C     
2675 O  O     . GLY A 344 ? 1.00779 0.99211 1.08531 -0.01158 -0.19458 0.31223  423 GLY B O     
2676 N  N     . LEU A 345 ? 1.05282 1.04020 1.13575 0.00429  -0.18880 0.28509  424 LEU B N     
2677 C  CA    . LEU A 345 ? 0.91918 0.91061 0.98754 -0.00169 -0.17713 0.27410  424 LEU B CA    
2678 C  C     . LEU A 345 ? 0.93433 0.94913 0.98686 -0.00975 -0.17107 0.27589  424 LEU B C     
2679 O  O     . LEU A 345 ? 0.93635 0.96232 0.98302 -0.00850 -0.16369 0.26383  424 LEU B O     
2680 C  CB    . LEU A 345 ? 0.96008 0.94562 1.03156 0.00788  -0.17128 0.25524  424 LEU B CB    
2681 C  CG    . LEU A 345 ? 0.98502 0.95046 1.07268 0.01995  -0.17840 0.25017  424 LEU B CG    
2682 C  CD1   . LEU A 345 ? 0.98562 0.94972 1.07209 0.02958  -0.17066 0.23136  424 LEU B CD1   
2683 C  CD2   . LEU A 345 ? 1.09433 1.03890 1.18724 0.01619  -0.18472 0.25624  424 LEU B CD2   
2684 N  N     . VAL A 346 ? 0.95324 0.97546 0.99909 -0.01800 -0.17472 0.29159  425 VAL B N     
2685 C  CA    . VAL A 346 ? 1.01196 1.05658 1.04257 -0.02437 -0.17145 0.29390  425 VAL B CA    
2686 C  C     . VAL A 346 ? 1.04646 1.09761 1.06132 -0.03137 -0.16028 0.28382  425 VAL B C     
2687 O  O     . VAL A 346 ? 1.23131 1.30002 1.23406 -0.03511 -0.15675 0.28016  425 VAL B O     
2688 C  CB    . VAL A 346 ? 0.94639 0.99809 0.97269 -0.02992 -0.17872 0.31423  425 VAL B CB    
2689 C  CG1   . VAL A 346 ? 0.84377 0.89171 0.88533 -0.02250 -0.19044 0.32381  425 VAL B CG1   
2690 C  CG2   . VAL A 346 ? 0.91535 0.95616 0.94070 -0.03671 -0.17786 0.32475  425 VAL B CG2   
2691 N  N     . SER A 347 ? 1.01887 1.05609 1.03430 -0.03292 -0.15545 0.27869  426 SER B N     
2692 C  CA    . SER A 347 ? 1.03770 1.07977 1.03984 -0.03867 -0.14516 0.26861  426 SER B CA    
2693 C  C     . SER A 347 ? 0.90781 0.94608 0.91173 -0.03298 -0.13872 0.25049  426 SER B C     
2694 O  O     . SER A 347 ? 1.00648 1.04504 1.00160 -0.03658 -0.13062 0.24128  426 SER B O     
2695 C  CB    . SER A 347 ? 1.04973 1.08097 1.05142 -0.04444 -0.14349 0.27429  426 SER B CB    
2696 O  OG    . SER A 347 ? 1.01859 1.05693 1.01699 -0.05089 -0.14745 0.29239  426 SER B OG    
2697 N  N     . LEU A 348 ? 0.97397 1.00969 0.98927 -0.02391 -0.14189 0.24586  427 LEU B N     
2698 C  CA    . LEU A 348 ? 0.90697 0.94026 0.92473 -0.01759 -0.13534 0.23042  427 LEU B CA    
2699 C  C     . LEU A 348 ? 0.89249 0.94394 0.90214 -0.02117 -0.12923 0.22366  427 LEU B C     
2700 O  O     . LEU A 348 ? 0.85558 0.92135 0.86566 -0.02261 -0.13327 0.22873  427 LEU B O     
2701 C  CB    . LEU A 348 ? 0.88982 0.91650 0.92325 -0.00588 -0.14039 0.22845  427 LEU B CB    
2702 C  CG    . LEU A 348 ? 0.92454 0.94434 0.96170 0.00300  -0.13417 0.21397  427 LEU B CG    
2703 C  CD1   . LEU A 348 ? 0.81845 0.81895 0.85340 0.00376  -0.13335 0.20946  427 LEU B CD1   
2704 C  CD2   . LEU A 348 ? 0.76456 0.78426 0.81674 0.01507  -0.13853 0.21244  427 LEU B CD2   
2705 N  N     . GLU A 349 ? 0.90475 0.95512 0.90779 -0.02261 -0.12037 0.21225  428 GLU B N     
2706 C  CA    . GLU A 349 ? 0.89949 0.96464 0.89690 -0.02616 -0.11480 0.20500  428 GLU B CA    
2707 C  C     . GLU A 349 ? 0.85744 0.92275 0.86230 -0.01941 -0.10895 0.19455  428 GLU B C     
2708 O  O     . GLU A 349 ? 0.83385 0.91277 0.84116 -0.02070 -0.10686 0.19106  428 GLU B O     
2709 C  CB    . GLU A 349 ? 0.89123 0.95792 0.87404 -0.03472 -0.10903 0.20137  428 GLU B CB    
2710 C  CG    . GLU A 349 ? 0.99651 1.06862 0.97013 -0.04186 -0.11304 0.21186  428 GLU B CG    
2711 C  CD    . GLU A 349 ? 1.00907 1.08545 0.96867 -0.04925 -0.10678 0.20722  428 GLU B CD    
2712 O  OE1   . GLU A 349 ? 1.00356 1.07924 0.96082 -0.04938 -0.10024 0.19569  428 GLU B OE1   
2713 O  OE2   . GLU A 349 ? 1.03832 1.11936 0.98961 -0.05460 -0.10827 0.21562  428 GLU B OE2   
2714 N  N     . VAL A 350 ? 0.73884 0.79003 0.74766 -0.01212 -0.10653 0.18972  429 VAL B N     
2715 C  CA    . VAL A 350 ? 0.87169 0.92373 0.88640 -0.00435 -0.10022 0.18076  429 VAL B CA    
2716 C  C     . VAL A 350 ? 0.85774 0.89891 0.88264 0.00734  -0.10402 0.18054  429 VAL B C     
2717 O  O     . VAL A 350 ? 0.90167 0.92659 0.92488 0.00936  -0.10755 0.18095  429 VAL B O     
2718 C  CB    . VAL A 350 ? 0.75935 0.80565 0.76420 -0.00642 -0.09143 0.17173  429 VAL B CB    
2719 C  CG1   . VAL A 350 ? 0.85937 0.90600 0.86960 0.00294  -0.08488 0.16421  429 VAL B CG1   
2720 C  CG2   . VAL A 350 ? 0.73147 0.78879 0.72810 -0.01675 -0.08792 0.17046  429 VAL B CG2   
2721 N  N     . LEU A 351 ? 0.87511 0.92549 0.91175 0.01526  -0.10369 0.17948  430 LEU B N     
2722 C  CA    . LEU A 351 ? 0.89856 0.94081 0.94585 0.02819  -0.10713 0.17787  430 LEU B CA    
2723 C  C     . LEU A 351 ? 0.85698 0.90741 0.90899 0.03717  -0.09820 0.16954  430 LEU B C     
2724 O  O     . LEU A 351 ? 0.85530 0.92349 0.91580 0.03697  -0.09534 0.17106  430 LEU B O     
2725 C  CB    . LEU A 351 ? 0.81586 0.86304 0.87539 0.03056  -0.11698 0.18713  430 LEU B CB    
2726 C  CG    . LEU A 351 ? 0.93780 0.97572 1.00997 0.04456  -0.12220 0.18555  430 LEU B CG    
2727 C  CD1   . LEU A 351 ? 0.81909 0.83390 0.88641 0.04779  -0.12533 0.18187  430 LEU B CD1   
2728 C  CD2   . LEU A 351 ? 0.82185 0.86465 0.90620 0.04575  -0.13281 0.19608  430 LEU B CD2   
2729 N  N     . ILE A 352 ? 0.86356 0.90192 0.91042 0.04506  -0.09399 0.16118  431 ILE B N     
2730 C  CA    . ILE A 352 ? 0.87089 0.91673 0.91961 0.05467  -0.08448 0.15365  431 ILE B CA    
2731 C  C     . ILE A 352 ? 0.86280 0.90204 0.92009 0.07053  -0.08813 0.14962  431 ILE B C     
2732 O  O     . ILE A 352 ? 0.91231 0.93247 0.96519 0.07572  -0.09353 0.14533  431 ILE B O     
2733 C  CB    . ILE A 352 ? 0.84154 0.88022 0.87552 0.05279  -0.07643 0.14640  431 ILE B CB    
2734 C  CG1   . ILE A 352 ? 0.81736 0.85882 0.84268 0.03733  -0.07487 0.14971  431 ILE B CG1   
2735 C  CG2   . ILE A 352 ? 0.88266 0.93291 0.91808 0.06135  -0.06547 0.14119  431 ILE B CG2   
2736 C  CD1   . ILE A 352 ? 0.88867 0.95015 0.92064 0.03041  -0.07102 0.15375  431 ILE B CD1   
2737 N  N     . LEU A 353 ? 0.82436 0.87957 0.89510 0.07854  -0.08563 0.15051  432 LEU B N     
2738 C  CA    . LEU A 353 ? 0.84755 0.89946 0.92803 0.09508  -0.08867 0.14605  432 LEU B CA    
2739 C  C     . LEU A 353 ? 0.89284 0.96162 0.97767 0.10610  -0.07695 0.14068  432 LEU B C     
2740 O  O     . LEU A 353 ? 0.90094 0.97703 0.99851 0.11924  -0.07763 0.13894  432 LEU B O     
2741 C  CB    . LEU A 353 ? 0.81028 0.86549 0.90654 0.09611  -0.09933 0.15403  432 LEU B CB    
2742 C  CG    . LEU A 353 ? 0.80543 0.84489 0.89922 0.08693  -0.11148 0.16150  432 LEU B CG    
2743 C  CD1   . LEU A 353 ? 0.93755 0.98451 1.04694 0.08773  -0.12091 0.17089  432 LEU B CD1   
2744 C  CD2   . LEU A 353 ? 0.79187 0.80633 0.88068 0.09353  -0.11753 0.15552  432 LEU B CD2   
2745 N  N     . SER A 354 ? 0.95096 1.02676 1.02603 0.10121  -0.06597 0.13862  433 SER B N     
2746 C  CA    . SER A 354 ? 0.87451 0.96875 0.95407 0.11010  -0.05362 0.13606  433 SER B CA    
2747 C  C     . SER A 354 ? 0.98433 1.07072 1.05768 0.12848  -0.05088 0.12568  433 SER B C     
2748 O  O     . SER A 354 ? 0.91775 0.98251 0.97840 0.13163  -0.05640 0.11880  433 SER B O     
2749 C  CB    . SER A 354 ? 0.64150 0.74346 0.71240 0.09934  -0.04343 0.13777  433 SER B CB    
2750 O  OG    . SER A 354 ? 0.89734 0.98031 0.95092 0.09108  -0.04632 0.13493  433 SER B OG    
2751 N  N     . ASN A 355 ? 0.96050 1.06569 1.04376 0.14110  -0.04259 0.12437  434 ASN B N     
2752 C  CA    . ASN A 355 ? 0.82091 0.92373 0.89844 0.16090  -0.03841 0.11388  434 ASN B CA    
2753 C  C     . ASN A 355 ? 0.88746 0.97031 0.96755 0.17145  -0.05202 0.10711  434 ASN B C     
2754 O  O     . ASN A 355 ? 0.87348 0.93555 0.93990 0.17797  -0.05673 0.09755  434 ASN B O     
2755 C  CB    . ASN A 355 ? 0.84884 0.94403 0.90451 0.16204  -0.03051 0.10751  434 ASN B CB    
2756 C  CG    . ASN A 355 ? 1.01217 1.12884 1.06753 0.15575  -0.01581 0.11404  434 ASN B CG    
2757 O  OD1   . ASN A 355 ? 1.07301 1.20919 1.13291 0.16706  -0.00466 0.11393  434 ASN B OD1   
2758 N  ND2   . ASN A 355 ? 0.91610 1.02970 0.96702 0.13785  -0.01573 0.12008  434 ASN B ND2   
2759 N  N     . ASN A 356 ? 0.86664 0.95602 0.96593 0.17318  -0.05909 0.11231  435 ASN B N     
2760 C  CA    . ASN A 356 ? 0.91459 0.98777 1.02123 0.18471  -0.07201 0.10713  435 ASN B CA    
2761 C  C     . ASN A 356 ? 0.97993 1.07332 1.10723 0.19777  -0.07021 0.10824  435 ASN B C     
2762 O  O     . ASN A 356 ? 1.03431 1.15406 1.16906 0.19881  -0.05806 0.11208  435 ASN B O     
2763 C  CB    . ASN A 356 ? 0.89185 0.94649 1.00092 0.17075  -0.08655 0.11454  435 ASN B CB    
2764 C  CG    . ASN A 356 ? 0.93494 0.96551 1.02603 0.16330  -0.09080 0.11051  435 ASN B CG    
2765 O  OD1   . ASN A 356 ? 1.00517 1.01440 1.09300 0.17220  -0.09945 0.10221  435 ASN B OD1   
2766 N  ND2   . ASN A 356 ? 0.90314 0.93693 0.98384 0.14706  -0.08541 0.11601  435 ASN B ND2   
2767 N  N     . LEU A 357 ? 0.90838 0.98958 1.04680 0.20775  -0.08271 0.10535  436 LEU B N     
2768 C  CA    . LEU A 357 ? 0.94825 1.04629 1.10765 0.22191  -0.08298 0.10537  436 LEU B CA    
2769 C  C     . LEU A 357 ? 0.94998 1.04990 1.12776 0.21255  -0.09458 0.11753  436 LEU B C     
2770 O  O     . LEU A 357 ? 1.02167 1.11927 1.21549 0.22403  -0.10368 0.11655  436 LEU B O     
2771 C  CB    . LEU A 357 ? 1.03422 1.11842 1.19383 0.24432  -0.08843 0.09107  436 LEU B CB    
2772 C  CG    . LEU A 357 ? 0.95999 1.04833 1.10444 0.26084  -0.07681 0.07705  436 LEU B CG    
2773 C  CD1   . LEU A 357 ? 0.99449 1.10851 1.13142 0.25418  -0.05830 0.08223  436 LEU B CD1   
2774 C  CD2   . LEU A 357 ? 0.94658 1.00383 1.07150 0.26293  -0.08481 0.06590  436 LEU B CD2   
2775 N  N     . LEU A 358 ? 0.97002 1.07438 1.14536 0.19233  -0.09482 0.12885  437 LEU B N     
2776 C  CA    . LEU A 358 ? 1.00516 1.11128 1.19448 0.18269  -0.10631 0.14075  437 LEU B CA    
2777 C  C     . LEU A 358 ? 0.96482 1.10052 1.17611 0.18751  -0.10207 0.14581  437 LEU B C     
2778 O  O     . LEU A 358 ? 0.94703 1.10518 1.16025 0.18173  -0.09020 0.14859  437 LEU B O     
2779 C  CB    . LEU A 358 ? 0.96290 1.06490 1.14040 0.16059  -0.10789 0.14977  437 LEU B CB    
2780 C  CG    . LEU A 358 ? 0.93060 1.00437 1.08960 0.15375  -0.11375 0.14728  437 LEU B CG    
2781 C  CD1   . LEU A 358 ? 0.88887 0.96287 1.03818 0.13285  -0.11477 0.15677  437 LEU B CD1   
2782 C  CD2   . LEU A 358 ? 0.89767 0.94922 1.06369 0.16159  -0.12880 0.14688  437 LEU B CD2   
2783 N  N     . LYS A 359 ? 0.91139 1.04701 1.14088 0.19799  -0.11228 0.14736  438 LYS B N     
2784 C  CA    . LYS A 359 ? 0.95099 1.11419 1.20420 0.20178  -0.11098 0.15341  438 LYS B CA    
2785 C  C     . LYS A 359 ? 0.94588 1.11527 1.20561 0.18446  -0.11990 0.16710  438 LYS B C     
2786 O  O     . LYS A 359 ? 0.94795 1.14328 1.22114 0.17930  -0.11521 0.17296  438 LYS B O     
2787 C  CB    . LYS A 359 ? 1.09724 1.25850 1.36819 0.22226  -0.11833 0.14836  438 LYS B CB    
2788 C  CG    . LYS A 359 ? 1.07668 1.26103 1.35868 0.24072  -0.10515 0.13989  438 LYS B CG    
2789 C  CD    . LYS A 359 ? 1.17340 1.34089 1.44099 0.25735  -0.10150 0.12451  438 LYS B CD    
2790 C  CE    . LYS A 359 ? 1.23295 1.42327 1.51339 0.27950  -0.09074 0.11585  438 LYS B CE    
2791 N  NZ    . LYS A 359 ? 0.90931 1.10770 1.21659 0.29161  -0.10037 0.11782  438 LYS B NZ    
2792 N  N     . LYS A 360 ? 1.00271 1.14941 1.25356 0.17566  -0.13298 0.17248  439 LYS B N     
2793 C  CA    . LYS A 360 ? 1.03041 1.18165 1.28330 0.15979  -0.14203 0.18529  439 LYS B CA    
2794 C  C     . LYS A 360 ? 0.94889 1.07437 1.18157 0.14766  -0.14925 0.18889  439 LYS B C     
2795 O  O     . LYS A 360 ? 0.92713 1.03089 1.14809 0.15210  -0.14891 0.18181  439 LYS B O     
2796 C  CB    . LYS A 360 ? 0.96010 1.11906 1.23565 0.16709  -0.15432 0.19240  439 LYS B CB    
2797 C  CG    . LYS A 360 ? 0.95494 1.09477 1.23830 0.18397  -0.16325 0.18774  439 LYS B CG    
2798 C  CD    . LYS A 360 ? 0.94388 1.09795 1.25383 0.19541  -0.17148 0.19206  439 LYS B CD    
2799 C  CE    . LYS A 360 ? 1.10659 1.24896 1.42059 0.18863  -0.18933 0.20526  439 LYS B CE    
2800 N  NZ    . LYS A 360 ? 1.06471 1.21892 1.40530 0.20135  -0.19857 0.20911  439 LYS B NZ    
2801 N  N     . LEU A 361 ? 0.97883 1.10797 1.20779 0.13246  -0.15593 0.19989  440 LEU B N     
2802 C  CA    . LEU A 361 ? 1.00763 1.11693 1.21762 0.11968  -0.16126 0.20486  440 LEU B CA    
2803 C  C     . LEU A 361 ? 0.89416 0.99622 1.10984 0.11659  -0.17711 0.21762  440 LEU B C     
2804 O  O     . LEU A 361 ? 1.05264 1.17057 1.28345 0.11868  -0.18329 0.22416  440 LEU B O     
2805 C  CB    . LEU A 361 ? 0.91792 1.03733 1.11288 0.10313  -0.15360 0.20628  440 LEU B CB    
2806 C  CG    . LEU A 361 ? 0.85475 0.97936 1.04199 0.10401  -0.13815 0.19557  440 LEU B CG    
2807 C  CD1   . LEU A 361 ? 0.83734 0.97285 1.01362 0.08786  -0.13253 0.19776  440 LEU B CD1   
2808 C  CD2   . LEU A 361 ? 0.91479 1.01549 1.08852 0.10911  -0.13574 0.18760  440 LEU B CD2   
2809 N  N     . PRO A 362 ? 0.89694 0.97591 1.10161 0.11154  -0.18414 0.22224  441 PRO B N     
2810 C  CA    . PRO A 362 ? 0.88142 0.95252 1.09178 0.10912  -0.19922 0.23617  441 PRO B CA    
2811 C  C     . PRO A 362 ? 0.98249 1.07051 1.18645 0.09528  -0.20229 0.24749  441 PRO B C     
2812 O  O     . PRO A 362 ? 0.94215 1.04129 1.13289 0.08454  -0.19375 0.24482  441 PRO B O     
2813 C  CB    . PRO A 362 ? 0.96372 1.00724 1.16291 0.10521  -0.20322 0.23795  441 PRO B CB    
2814 C  CG    . PRO A 362 ? 0.93106 0.97367 1.11271 0.09862  -0.19006 0.22800  441 PRO B CG    
2815 C  CD    . PRO A 362 ? 0.90613 0.96542 1.09405 0.10796  -0.17893 0.21570  441 PRO B CD    
2816 N  N     . HIS A 363 ? 0.88271 0.97235 1.09630 0.09629  -0.21549 0.26004  442 HIS B N     
2817 C  CA    . HIS A 363 ? 0.97772 1.08298 1.18385 0.08433  -0.22037 0.27108  442 HIS B CA    
2818 C  C     . HIS A 363 ? 0.93615 1.03035 1.12020 0.07048  -0.22120 0.27908  442 HIS B C     
2819 O  O     . HIS A 363 ? 0.98600 1.09392 1.15763 0.05941  -0.22156 0.28455  442 HIS B O     
2820 C  CB    . HIS A 363 ? 0.96227 1.07413 1.18506 0.09046  -0.23464 0.28254  442 HIS B CB    
2821 C  CG    . HIS A 363 ? 1.14069 1.22961 1.37116 0.09736  -0.24589 0.29087  442 HIS B CG    
2822 N  ND1   . HIS A 363 ? 1.18035 1.25183 1.39754 0.08856  -0.25108 0.30199  442 HIS B ND1   
2823 C  CD2   . HIS A 363 ? 1.10901 1.18973 1.36069 0.11230  -0.25340 0.29008  442 HIS B CD2   
2824 C  CE1   . HIS A 363 ? 1.08504 1.13749 1.31577 0.09705  -0.26175 0.30826  442 HIS B CE1   
2825 N  NE2   . HIS A 363 ? 1.14079 1.19772 1.39215 0.11188  -0.26371 0.30054  442 HIS B NE2   
2826 N  N     . GLY A 364 ? 0.91672 0.98731 1.09620 0.07112  -0.22155 0.27935  443 GLY B N     
2827 C  CA    . GLY A 364 ? 0.94800 1.00953 1.10797 0.05812  -0.22011 0.28592  443 GLY B CA    
2828 C  C     . GLY A 364 ? 0.93400 1.00266 1.07678 0.04927  -0.20669 0.27562  443 GLY B C     
2829 O  O     . GLY A 364 ? 1.02024 1.08463 1.14640 0.03826  -0.20459 0.28047  443 GLY B O     
2830 N  N     . LEU A 365 ? 1.00791 1.08789 1.15514 0.05396  -0.19744 0.26220  444 LEU B N     
2831 C  CA    . LEU A 365 ? 0.95960 1.04602 1.09209 0.04587  -0.18509 0.25272  444 LEU B CA    
2832 C  C     . LEU A 365 ? 0.94688 1.04927 1.06615 0.03318  -0.18590 0.25860  444 LEU B C     
2833 O  O     . LEU A 365 ? 0.96076 1.06314 1.06366 0.02393  -0.17858 0.25465  444 LEU B O     
2834 C  CB    . LEU A 365 ? 0.89897 0.99638 1.04142 0.05370  -0.17569 0.23968  444 LEU B CB    
2835 C  CG    . LEU A 365 ? 0.88266 0.98541 1.01278 0.04701  -0.16260 0.22950  444 LEU B CG    
2836 C  CD1   . LEU A 365 ? 0.69571 0.77813 0.81612 0.04873  -0.15662 0.22249  444 LEU B CD1   
2837 C  CD2   . LEU A 365 ? 0.97175 1.09287 1.11469 0.05255  -0.15520 0.22172  444 LEU B CD2   
2838 N  N     . GLY A 366 ? 0.90884 1.02497 1.03468 0.03322  -0.19529 0.26738  445 GLY B N     
2839 C  CA    . GLY A 366 ? 0.87523 1.00711 0.98783 0.02250  -0.19769 0.27208  445 GLY B CA    
2840 C  C     . GLY A 366 ? 0.88729 1.01139 0.98002 0.01309  -0.19969 0.28155  445 GLY B C     
2841 O  O     . GLY A 366 ? 0.95341 1.09038 1.03143 0.00439  -0.20017 0.28353  445 GLY B O     
2842 N  N     . ASN A 367 ? 0.84935 0.95351 0.94206 0.01483  -0.20106 0.28729  446 ASN B N     
2843 C  CA    . ASN A 367 ? 0.99587 1.09308 1.07247 0.00592  -0.20228 0.29800  446 ASN B CA    
2844 C  C     . ASN A 367 ? 1.03906 1.13095 1.10108 -0.00116 -0.19060 0.28884  446 ASN B C     
2845 O  O     . ASN A 367 ? 1.06909 1.15782 1.11750 -0.00910 -0.18982 0.29672  446 ASN B O     
2846 C  CB    . ASN A 367 ? 0.97717 1.05514 1.06389 0.01027  -0.21052 0.31012  446 ASN B CB    
2847 C  CG    . ASN A 367 ? 0.98109 1.05731 1.05476 0.00117  -0.21460 0.32701  446 ASN B CG    
2848 O  OD1   . ASN A 367 ? 0.88447 0.97757 0.94500 -0.00478 -0.21693 0.33444  446 ASN B OD1   
2849 N  ND2   . ASN A 367 ? 0.83157 0.88803 0.90907 0.00023  -0.21560 0.33321  446 ASN B ND2   
2850 N  N     . LEU A 368 ? 1.02524 1.11695 1.09022 0.00171  -0.18138 0.27322  447 LEU B N     
2851 C  CA    . LEU A 368 ? 0.90565 0.99335 0.95719 -0.00460 -0.17054 0.26387  447 LEU B CA    
2852 C  C     . LEU A 368 ? 0.91244 1.01855 0.94927 -0.01342 -0.16766 0.26161  447 LEU B C     
2853 O  O     . LEU A 368 ? 0.95627 1.07221 0.99371 -0.01390 -0.16203 0.25041  447 LEU B O     
2854 C  CB    . LEU A 368 ? 0.75946 0.84048 0.81904 0.00233  -0.16232 0.24926  447 LEU B CB    
2855 C  CG    . LEU A 368 ? 0.75647 0.81993 0.83043 0.01317  -0.16559 0.24845  447 LEU B CG    
2856 C  CD1   . LEU A 368 ? 0.71529 0.77271 0.79120 0.01926  -0.15589 0.23344  447 LEU B CD1   
2857 C  CD2   . LEU A 368 ? 0.84967 0.89553 0.92124 0.01029  -0.17128 0.25839  447 LEU B CD2   
2858 N  N     . ARG A 369 ? 1.04721 1.15808 1.07088 -0.02031 -0.17193 0.27280  448 ARG B N     
2859 C  CA    . ARG A 369 ? 0.97332 1.10187 0.98116 -0.02773 -0.17104 0.27101  448 ARG B CA    
2860 C  C     . ARG A 369 ? 1.08198 1.21021 1.07880 -0.03308 -0.15998 0.25793  448 ARG B C     
2861 O  O     . ARG A 369 ? 1.12820 1.27009 1.11764 -0.03694 -0.15839 0.25023  448 ARG B O     
2862 C  CB    . ARG A 369 ? 1.06719 1.20048 1.06163 -0.03275 -0.17697 0.28663  448 ARG B CB    
2863 C  CG    . ARG A 369 ? 1.21508 1.33133 1.21023 -0.03389 -0.17608 0.29698  448 ARG B CG    
2864 C  CD    . ARG A 369 ? 1.39572 1.51854 1.37881 -0.03903 -0.18129 0.31497  448 ARG B CD    
2865 N  NE    . ARG A 369 ? 1.59369 1.72987 1.55519 -0.04659 -0.17498 0.31229  448 ARG B NE    
2866 C  CZ    . ARG A 369 ? 1.65328 1.78408 1.60673 -0.05177 -0.16620 0.31011  448 ARG B CZ    
2867 N  NH1   . ARG A 369 ? 1.61270 1.72460 1.57758 -0.05091 -0.16307 0.31005  448 ARG B NH1   
2868 N  NH2   . ARG A 369 ? 1.70846 1.85351 1.64236 -0.05744 -0.16096 0.30719  448 ARG B NH2   
2869 N  N     . LYS A 370 ? 1.06741 1.17990 1.06378 -0.03322 -0.15323 0.25497  449 LYS B N     
2870 C  CA    . LYS A 370 ? 0.99613 1.10712 0.98222 -0.03800 -0.14319 0.24357  449 LYS B CA    
2871 C  C     . LYS A 370 ? 0.91015 1.01633 0.90599 -0.03334 -0.13657 0.22993  449 LYS B C     
2872 O  O     . LYS A 370 ? 0.85742 0.96115 0.84614 -0.03660 -0.12840 0.22038  449 LYS B O     
2873 C  CB    . LYS A 370 ? 1.06042 1.15851 1.03990 -0.04148 -0.13968 0.24843  449 LYS B CB    
2874 C  CG    . LYS A 370 ? 1.02801 1.13352 0.99519 -0.04765 -0.14313 0.26204  449 LYS B CG    
2875 C  CD    . LYS A 370 ? 1.20757 1.33088 1.15757 -0.05337 -0.14022 0.25690  449 LYS B CD    
2876 C  CE    . LYS A 370 ? 1.28746 1.41790 1.22245 -0.05927 -0.14004 0.26869  449 LYS B CE    
2877 N  NZ    . LYS A 370 ? 1.20122 1.34990 1.11808 -0.06331 -0.13799 0.26254  449 LYS B NZ    
2878 N  N     . LEU A 371 ? 0.96181 1.06748 0.97371 -0.02545 -0.13966 0.22931  450 LEU B N     
2879 C  CA    . LEU A 371 ? 0.93637 1.03821 0.95766 -0.01986 -0.13257 0.21806  450 LEU B CA    
2880 C  C     . LEU A 371 ? 0.91658 1.03166 0.93508 -0.02450 -0.12728 0.20882  450 LEU B C     
2881 O  O     . LEU A 371 ? 0.92894 1.05916 0.95015 -0.02687 -0.13225 0.21018  450 LEU B O     
2882 C  CB    . LEU A 371 ? 0.88475 0.98663 0.92436 -0.00970 -0.13703 0.22004  450 LEU B CB    
2883 C  CG    . LEU A 371 ? 0.90075 0.99662 0.94949 -0.00154 -0.12931 0.21005  450 LEU B CG    
2884 C  CD1   . LEU A 371 ? 0.80694 0.88273 0.84990 0.00084  -0.12617 0.20737  450 LEU B CD1   
2885 C  CD2   . LEU A 371 ? 0.74086 0.84180 0.80827 0.00897  -0.13320 0.21140  450 LEU B CD2   
2886 N  N     . ARG A 372 ? 0.90928 1.01807 0.92325 -0.02573 -0.11802 0.19945  451 ARG B N     
2887 C  CA    . ARG A 372 ? 0.80053 0.91906 0.81290 -0.03049 -0.11283 0.19078  451 ARG B CA    
2888 C  C     . ARG A 372 ? 0.82243 0.94183 0.84780 -0.02484 -0.10609 0.18417  451 ARG B C     
2889 O  O     . ARG A 372 ? 0.85839 0.98927 0.88966 -0.02796 -0.10415 0.17976  451 ARG B O     
2890 C  CB    . ARG A 372 ? 0.84068 0.95327 0.83687 -0.03732 -0.10731 0.18571  451 ARG B CB    
2891 C  CG    . ARG A 372 ? 1.10879 1.23142 1.10157 -0.04361 -0.10462 0.17759  451 ARG B CG    
2892 C  CD    . ARG A 372 ? 1.17797 1.29392 1.15587 -0.04896 -0.09898 0.17191  451 ARG B CD    
2893 N  NE    . ARG A 372 ? 1.12872 1.23147 1.10780 -0.04557 -0.09091 0.16705  451 ARG B NE    
2894 C  CZ    . ARG A 372 ? 1.13613 1.22572 1.11002 -0.04340 -0.08909 0.16926  451 ARG B CZ    
2895 N  NH1   . ARG A 372 ? 1.09096 1.17846 1.05935 -0.04493 -0.09400 0.17732  451 ARG B NH1   
2896 N  NH2   . ARG A 372 ? 1.01289 1.09144 0.98761 -0.03968 -0.08258 0.16370  451 ARG B NH2   
2897 N  N     . GLU A 373 ? 0.79301 0.90123 0.82340 -0.01643 -0.10277 0.18356  452 GLU B N     
2898 C  CA    . GLU A 373 ? 0.80093 0.91068 0.84103 -0.01004 -0.09488 0.17757  452 GLU B CA    
2899 C  C     . GLU A 373 ? 0.89504 0.99885 0.94516 0.00183  -0.09641 0.17953  452 GLU B C     
2900 O  O     . GLU A 373 ? 0.87695 0.96515 0.92128 0.00552  -0.09831 0.18011  452 GLU B O     
2901 C  CB    . GLU A 373 ? 0.88017 0.98012 0.90938 -0.01210 -0.08596 0.17023  452 GLU B CB    
2902 C  CG    . GLU A 373 ? 1.00887 1.10960 1.04529 -0.00473 -0.07708 0.16516  452 GLU B CG    
2903 C  CD    . GLU A 373 ? 1.17304 1.26410 1.19764 -0.00696 -0.06920 0.15873  452 GLU B CD    
2904 O  OE1   . GLU A 373 ? 1.08885 1.17339 1.10116 -0.01451 -0.07063 0.15761  452 GLU B OE1   
2905 O  OE2   . GLU A 373 ? 1.18206 1.27296 1.20957 -0.00070 -0.06146 0.15513  452 GLU B OE2   
2906 N  N     . LEU A 374 ? 0.86946 0.98592 0.93582 0.00801  -0.09589 0.18015  453 LEU B N     
2907 C  CA    . LEU A 374 ? 0.82091 0.93442 0.89869 0.02073  -0.09749 0.18110  453 LEU B CA    
2908 C  C     . LEU A 374 ? 0.83895 0.96096 0.92610 0.02837  -0.08734 0.17562  453 LEU B C     
2909 O  O     . LEU A 374 ? 0.91962 1.05951 1.01892 0.02614  -0.08471 0.17676  453 LEU B O     
2910 C  CB    . LEU A 374 ? 0.77236 0.89553 0.86283 0.02248  -0.10771 0.18890  453 LEU B CB    
2911 C  CG    . LEU A 374 ? 0.80454 0.92653 0.90973 0.03633  -0.11057 0.18992  453 LEU B CG    
2912 C  CD1   . LEU A 374 ? 0.79157 0.89142 0.88915 0.04324  -0.11175 0.18730  453 LEU B CD1   
2913 C  CD2   . LEU A 374 ? 0.67697 0.80788 0.79351 0.03654  -0.12202 0.19869  453 LEU B CD2   
2914 N  N     . ASP A 375 ? 0.83348 0.94349 0.91541 0.03747  -0.08189 0.16999  454 ASP B N     
2915 C  CA    . ASP A 375 ? 0.79623 0.91403 0.88394 0.04626  -0.07121 0.16510  454 ASP B CA    
2916 C  C     . ASP A 375 ? 0.84728 0.96367 0.94480 0.06195  -0.07298 0.16355  454 ASP B C     
2917 O  O     . ASP A 375 ? 0.87515 0.97357 0.96592 0.06805  -0.07818 0.16078  454 ASP B O     
2918 C  CB    . ASP A 375 ? 0.86012 0.96639 0.93159 0.04537  -0.06304 0.15862  454 ASP B CB    
2919 C  CG    . ASP A 375 ? 0.97604 1.09373 1.05175 0.05186  -0.05077 0.15557  454 ASP B CG    
2920 O  OD1   . ASP A 375 ? 0.94779 1.07774 1.03721 0.06231  -0.04797 0.15630  454 ASP B OD1   
2921 O  OD2   . ASP A 375 ? 0.98496 1.10002 1.05055 0.04678  -0.04369 0.15298  454 ASP B OD2   
2922 N  N     . LEU A 376 ? 0.76103 0.89658 0.87580 0.06865  -0.06897 0.16510  455 LEU B N     
2923 C  CA    . LEU A 376 ? 0.85627 0.99403 0.98241 0.08493  -0.06975 0.16294  455 LEU B CA    
2924 C  C     . LEU A 376 ? 0.85151 1.00625 0.98540 0.09435  -0.05655 0.15983  455 LEU B C     
2925 O  O     . LEU A 376 ? 0.87921 1.04765 1.02963 0.10566  -0.05538 0.16039  455 LEU B O     
2926 C  CB    . LEU A 376 ? 0.82888 0.97553 0.97227 0.08565  -0.08021 0.16982  455 LEU B CB    
2927 C  CG    . LEU A 376 ? 0.78529 0.91584 0.92244 0.07948  -0.09381 0.17458  455 LEU B CG    
2928 C  CD1   . LEU A 376 ? 0.69802 0.84337 0.84756 0.07214  -0.10200 0.18337  455 LEU B CD1   
2929 C  CD2   . LEU A 376 ? 0.73220 0.84618 0.87130 0.09270  -0.10059 0.17179  455 LEU B CD2   
2930 N  N     . GLU A 377 ? 0.81493 0.96974 0.93743 0.09016  -0.04634 0.15717  456 GLU B N     
2931 C  CA    . GLU A 377 ? 0.80939 0.98224 0.93872 0.09731  -0.03273 0.15659  456 GLU B CA    
2932 C  C     . GLU A 377 ? 0.89952 1.06947 1.02611 0.11695  -0.02858 0.14937  456 GLU B C     
2933 O  O     . GLU A 377 ? 0.89091 1.03936 1.00242 0.12299  -0.03343 0.14222  456 GLU B O     
2934 C  CB    . GLU A 377 ? 0.96316 1.13378 1.07922 0.08801  -0.02395 0.15614  456 GLU B CB    
2935 C  CG    . GLU A 377 ? 1.09414 1.28334 1.21612 0.09399  -0.00913 0.15766  456 GLU B CG    
2936 C  CD    . GLU A 377 ? 1.04646 1.23221 1.15655 0.08372  -0.00187 0.15859  456 GLU B CD    
2937 O  OE1   . GLU A 377 ? 0.89246 1.07072 0.99905 0.06879  -0.00789 0.16031  456 GLU B OE1   
2938 O  OE2   . GLU A 377 ? 1.15469 1.34543 1.25850 0.09120  0.00972  0.15758  456 GLU B OE2   
2939 N  N     . GLU A 378 ? 0.81611 1.00864 0.95838 0.12727  -0.01986 0.15099  457 GLU B N     
2940 C  CA    . GLU A 378 ? 0.90931 1.10401 1.04942 0.14765  -0.01386 0.14357  457 GLU B CA    
2941 C  C     . GLU A 378 ? 0.82382 1.00222 0.96512 0.15846  -0.02658 0.13761  457 GLU B C     
2942 O  O     . GLU A 378 ? 0.78764 0.94693 0.91385 0.16864  -0.02929 0.12810  457 GLU B O     
2943 C  CB    . GLU A 378 ? 0.91953 1.10452 1.03662 0.15210  -0.00476 0.13699  457 GLU B CB    
2944 C  CG    . GLU A 378 ? 1.07625 1.27980 1.19419 0.14576  0.00970  0.14332  457 GLU B CG    
2945 C  CD    . GLU A 378 ? 1.16256 1.36856 1.26492 0.16000  0.02196  0.13755  457 GLU B CD    
2946 O  OE1   . GLU A 378 ? 1.06800 1.28564 1.17537 0.17796  0.02694  0.13347  457 GLU B OE1   
2947 O  OE2   . GLU A 378 ? 1.17975 1.37641 1.26434 0.15396  0.02639  0.13683  457 GLU B OE2   
2948 N  N     . ASN A 379 ? 0.93066 1.11663 1.09126 0.15612  -0.03531 0.14350  458 ASN B N     
2949 C  CA    . ASN A 379 ? 0.87219 1.04709 1.03961 0.16819  -0.04674 0.13950  458 ASN B CA    
2950 C  C     . ASN A 379 ? 0.90497 1.10484 1.09643 0.18102  -0.04307 0.14129  458 ASN B C     
2951 O  O     . ASN A 379 ? 0.95991 1.18449 1.15979 0.18328  -0.02970 0.14392  458 ASN B O     
2952 C  CB    . ASN A 379 ? 0.87076 1.03002 1.03917 0.15542  -0.06235 0.14546  458 ASN B CB    
2953 C  CG    . ASN A 379 ? 0.89770 1.02815 1.04428 0.14913  -0.06844 0.14138  458 ASN B CG    
2954 O  OD1   . ASN A 379 ? 0.87287 0.98326 1.01601 0.15770  -0.07742 0.13596  458 ASN B OD1   
2955 N  ND2   . ASN A 379 ? 0.77329 0.90159 0.90666 0.13418  -0.06402 0.14390  458 ASN B ND2   
2956 N  N     . LYS A 380 ? 0.86002 1.05431 1.06399 0.18952  -0.05476 0.14058  459 LYS B N     
2957 C  CA    . LYS A 380 ? 0.94883 1.16631 1.17787 0.20197  -0.05324 0.14239  459 LYS B CA    
2958 C  C     . LYS A 380 ? 0.98454 1.20726 1.23185 0.19195  -0.06578 0.15266  459 LYS B C     
2959 O  O     . LYS A 380 ? 1.01598 1.24333 1.28128 0.20272  -0.07341 0.15312  459 LYS B O     
2960 C  CB    . LYS A 380 ? 1.05105 1.25935 1.28079 0.22485  -0.05592 0.13104  459 LYS B CB    
2961 C  CG    . LYS A 380 ? 0.86718 1.06866 1.07609 0.23645  -0.04530 0.11932  459 LYS B CG    
2962 C  CD    . LYS A 380 ? 0.91838 1.14936 1.12920 0.23793  -0.02603 0.12206  459 LYS B CD    
2963 C  CE    . LYS A 380 ? 0.97527 1.19868 1.16131 0.24726  -0.01577 0.11190  459 LYS B CE    
2964 N  NZ    . LYS A 380 ? 1.11520 1.32997 1.29682 0.27140  -0.01825 0.09759  459 LYS B NZ    
2965 N  N     . LEU A 381 ? 0.89723 1.11935 1.13956 0.17178  -0.06847 0.16062  460 LEU B N     
2966 C  CA    . LEU A 381 ? 0.92104 1.14534 1.17525 0.16105  -0.08177 0.17001  460 LEU B CA    
2967 C  C     . LEU A 381 ? 0.97803 1.23300 1.26110 0.16515  -0.07990 0.17557  460 LEU B C     
2968 O  O     . LEU A 381 ? 0.90152 1.17888 1.19341 0.15902  -0.06951 0.17891  460 LEU B O     
2969 C  CB    . LEU A 381 ? 0.88768 1.10637 1.12810 0.13978  -0.08361 0.17545  460 LEU B CB    
2970 C  CG    . LEU A 381 ? 0.93544 1.12420 1.15215 0.13238  -0.09124 0.17378  460 LEU B CG    
2971 C  CD1   . LEU A 381 ? 0.85227 1.04137 1.05983 0.11229  -0.09383 0.18001  460 LEU B CD1   
2972 C  CD2   . LEU A 381 ? 0.94331 1.11552 1.16400 0.13935  -0.10595 0.17533  460 LEU B CD2   
2973 N  N     . GLU A 382 ? 0.91755 1.17354 1.21702 0.17524  -0.09055 0.17711  461 GLU B N     
2974 C  CA    . GLU A 382 ? 0.92146 1.20600 1.25031 0.17865  -0.09151 0.18309  461 GLU B CA    
2975 C  C     . GLU A 382 ? 0.90094 1.19099 1.23687 0.16201  -0.10341 0.19334  461 GLU B C     
2976 O  O     . GLU A 382 ? 0.84604 1.16257 1.20512 0.15949  -0.10275 0.19886  461 GLU B O     
2977 C  CB    . GLU A 382 ? 0.87276 1.15698 1.21760 0.19874  -0.09793 0.17957  461 GLU B CB    
2978 C  CG    . GLU A 382 ? 1.07142 1.35016 1.40933 0.21798  -0.08789 0.16759  461 GLU B CG    
2979 C  CD    . GLU A 382 ? 1.15475 1.42785 1.50666 0.23789  -0.09690 0.16266  461 GLU B CD    
2980 O  OE1   . GLU A 382 ? 1.01701 1.29751 1.38918 0.23789  -0.10848 0.16983  461 GLU B OE1   
2981 O  OE2   . GLU A 382 ? 1.17513 1.43591 1.51774 0.25399  -0.09318 0.15115  461 GLU B OE2   
2982 N  N     . SER A 383 ? 0.92664 1.19347 1.24352 0.15090  -0.11430 0.19599  462 SER B N     
2983 C  CA    . SER A 383 ? 0.86526 1.13652 1.18565 0.13669  -0.12665 0.20519  462 SER B CA    
2984 C  C     . SER A 383 ? 0.93687 1.18427 1.22941 0.12279  -0.13171 0.20644  462 SER B C     
2985 O  O     . SER A 383 ? 0.94758 1.17126 1.22264 0.12657  -0.13121 0.20192  462 SER B O     
2986 C  CB    . SER A 383 ? 0.83549 1.10893 1.17369 0.14518  -0.14131 0.21071  462 SER B CB    
2987 O  OG    . SER A 383 ? 0.83603 1.08281 1.16361 0.15387  -0.14874 0.20863  462 SER B OG    
2988 N  N     . LEU A 384 ? 0.95865 1.21341 1.24801 0.10703  -0.13677 0.21217  463 LEU B N     
2989 C  CA    . LEU A 384 ? 0.96305 1.19794 1.22755 0.09453  -0.14308 0.21459  463 LEU B CA    
2990 C  C     . LEU A 384 ? 0.91426 1.14200 1.17995 0.09448  -0.15984 0.22326  463 LEU B C     
2991 O  O     . LEU A 384 ? 0.89584 1.14030 1.18066 0.09689  -0.16793 0.22864  463 LEU B O     
2992 C  CB    . LEU A 384 ? 0.80408 1.04897 1.06126 0.07805  -0.14022 0.21520  463 LEU B CB    
2993 C  CG    . LEU A 384 ? 0.87675 1.11756 1.12063 0.07285  -0.12588 0.20821  463 LEU B CG    
2994 C  CD1   . LEU A 384 ? 0.84222 1.09216 1.08145 0.05664  -0.12638 0.20923  463 LEU B CD1   
2995 C  CD2   . LEU A 384 ? 0.94342 1.15716 1.16330 0.07408  -0.12403 0.20443  463 LEU B CD2   
2996 N  N     . PRO A 385 ? 0.99825 1.20203 1.24495 0.09184  -0.16551 0.22559  464 PRO B N     
2997 C  CA    . PRO A 385 ? 0.92318 1.12072 1.16916 0.08978  -0.18124 0.23619  464 PRO B CA    
2998 C  C     . PRO A 385 ? 0.89289 1.10475 1.13349 0.07579  -0.18720 0.24218  464 PRO B C     
2999 O  O     . PRO A 385 ? 0.89122 1.10527 1.11753 0.06441  -0.18067 0.23850  464 PRO B O     
3000 C  CB    . PRO A 385 ? 0.85445 1.02395 1.08042 0.08791  -0.18298 0.23717  464 PRO B CB    
3001 C  CG    . PRO A 385 ? 0.88781 1.05253 1.09837 0.08237  -0.16919 0.22784  464 PRO B CG    
3002 C  CD    . PRO A 385 ? 0.79220 0.97434 1.01799 0.09008  -0.15810 0.21964  464 PRO B CD    
3003 N  N     . ASN A 386 ? 0.90542 1.12706 1.15771 0.07739  -0.20041 0.25092  465 ASN B N     
3004 C  CA    . ASN A 386 ? 0.97791 1.21410 1.22513 0.06558  -0.20812 0.25604  465 ASN B CA    
3005 C  C     . ASN A 386 ? 0.87297 1.09598 1.09107 0.05325  -0.20960 0.25916  465 ASN B C     
3006 O  O     . ASN A 386 ? 0.84095 1.07512 1.04971 0.04252  -0.21236 0.25942  465 ASN B O     
3007 C  CB    . ASN A 386 ? 0.99460 1.24088 1.25727 0.07078  -0.22362 0.26584  465 ASN B CB    
3008 C  CG    . ASN A 386 ? 1.01470 1.27931 1.30854 0.08205  -0.22259 0.26285  465 ASN B CG    
3009 O  OD1   . ASN A 386 ? 1.05151 1.33813 1.35865 0.07813  -0.22056 0.25968  465 ASN B OD1   
3010 N  ND2   . ASN A 386 ? 1.10524 1.36124 1.41227 0.09634  -0.22427 0.26378  465 ASN B ND2   
3011 N  N     . GLU A 387 ? 0.96929 1.16946 1.17373 0.05480  -0.20789 0.26098  466 GLU B N     
3012 C  CA    . GLU A 387 ? 0.92175 1.11017 1.10057 0.04407  -0.20962 0.26592  466 GLU B CA    
3013 C  C     . GLU A 387 ? 0.88049 1.06769 1.04284 0.03455  -0.19747 0.25644  466 GLU B C     
3014 O  O     . GLU A 387 ? 0.98479 1.16374 1.12587 0.02575  -0.19751 0.25942  466 GLU B O     
3015 C  CB    . GLU A 387 ? 0.95757 1.12216 1.13159 0.04890  -0.21303 0.27240  466 GLU B CB    
3016 C  CG    . GLU A 387 ? 0.92830 1.09128 1.11269 0.05487  -0.22791 0.28565  466 GLU B CG    
3017 C  CD    . GLU A 387 ? 0.95895 1.12941 1.17059 0.06867  -0.23113 0.28304  466 GLU B CD    
3018 O  OE1   . GLU A 387 ? 1.05271 1.22223 1.27426 0.07617  -0.22111 0.27164  466 GLU B OE1   
3019 O  OE2   . GLU A 387 ? 0.92220 1.10043 1.14516 0.07255  -0.24362 0.29259  466 GLU B OE2   
3020 N  N     . ILE A 388 ? 0.87764 1.07346 1.04962 0.03616  -0.18701 0.24590  467 ILE B N     
3021 C  CA    . ILE A 388 ? 0.91223 1.10726 1.06961 0.02684  -0.17654 0.23764  467 ILE B CA    
3022 C  C     . ILE A 388 ? 0.89510 1.10291 1.04212 0.01514  -0.18188 0.23879  467 ILE B C     
3023 O  O     . ILE A 388 ? 0.93496 1.13938 1.06540 0.00640  -0.17595 0.23353  467 ILE B O     
3024 C  CB    . ILE A 388 ? 0.92503 1.12779 1.09610 0.03101  -0.16434 0.22783  467 ILE B CB    
3025 C  CG1   . ILE A 388 ? 0.91154 1.13562 1.10903 0.03681  -0.16788 0.22902  467 ILE B CG1   
3026 C  CG2   . ILE A 388 ? 0.82773 1.01340 0.99720 0.04020  -0.15581 0.22316  467 ILE B CG2   
3027 C  CD1   . ILE A 388 ? 0.96957 1.21335 1.17220 0.02693  -0.17152 0.22822  467 ILE B CD1   
3028 N  N     . ALA A 389 ? 0.85071 1.07323 1.00710 0.01542  -0.19365 0.24488  468 ALA B N     
3029 C  CA    . ALA A 389 ? 0.90319 1.13844 1.04924 0.00548  -0.20053 0.24493  468 ALA B CA    
3030 C  C     . ALA A 389 ? 0.87198 1.09677 0.98983 -0.00153 -0.20280 0.24944  468 ALA B C     
3031 O  O     . ALA A 389 ? 0.99304 1.22527 1.09667 -0.01016 -0.20442 0.24575  468 ALA B O     
3032 C  CB    . ALA A 389 ? 0.91604 1.16821 1.07735 0.00857  -0.21435 0.25139  468 ALA B CB    
3033 N  N     . TYR A 390 ? 0.73080 0.93901 0.84122 0.00217  -0.20304 0.25721  469 TYR B N     
3034 C  CA    . TYR A 390 ? 0.93755 1.13765 1.02388 -0.00402 -0.20543 0.26440  469 TYR B CA    
3035 C  C     . TYR A 390 ? 0.98927 1.17523 1.06086 -0.00873 -0.19329 0.25793  469 TYR B C     
3036 O  O     . TYR A 390 ? 1.03320 1.21086 1.08713 -0.01311 -0.19341 0.26437  469 TYR B O     
3037 C  CB    . TYR A 390 ? 0.92657 1.11746 1.01548 0.00166  -0.21434 0.27900  469 TYR B CB    
3038 C  CG    . TYR A 390 ? 0.84836 1.05116 0.95647 0.00874  -0.22581 0.28476  469 TYR B CG    
3039 C  CD1   . TYR A 390 ? 0.75220 0.97456 0.85855 0.00524  -0.23494 0.28605  469 TYR B CD1   
3040 C  CD2   . TYR A 390 ? 0.82208 1.01681 0.95063 0.01952  -0.22815 0.28803  469 TYR B CD2   
3041 C  CE1   . TYR A 390 ? 0.73960 0.97366 0.86473 0.01177  -0.24606 0.29127  469 TYR B CE1   
3042 C  CE2   . TYR A 390 ? 0.80082 1.00718 0.94833 0.02659  -0.23871 0.29315  469 TYR B CE2   
3043 C  CZ    . TYR A 390 ? 0.74173 0.96801 0.88781 0.02242  -0.24763 0.29517  469 TYR B CZ    
3044 O  OH    . TYR A 390 ? 0.74930 0.98793 0.91537 0.02950  -0.25883 0.30032  469 TYR B OH    
3045 N  N     . LEU A 391 ? 0.94678 1.13083 1.02581 -0.00787 -0.18280 0.24612  470 LEU B N     
3046 C  CA    . LEU A 391 ? 0.94917 1.12157 1.01456 -0.01252 -0.17160 0.23875  470 LEU B CA    
3047 C  C     . LEU A 391 ? 0.96870 1.15191 1.02099 -0.02200 -0.16975 0.23162  470 LEU B C     
3048 O  O     . LEU A 391 ? 0.89589 1.08342 0.95338 -0.02416 -0.16303 0.22126  470 LEU B O     
3049 C  CB    . LEU A 391 ? 0.87634 1.04135 0.95470 -0.00619 -0.16165 0.23025  470 LEU B CB    
3050 C  CG    . LEU A 391 ? 0.81097 0.96450 0.90248 0.00484  -0.16318 0.23427  470 LEU B CG    
3051 C  CD1   . LEU A 391 ? 0.74605 0.89482 0.84686 0.01146  -0.15236 0.22426  470 LEU B CD1   
3052 C  CD2   . LEU A 391 ? 0.79057 0.92646 0.87064 0.00414  -0.16643 0.24217  470 LEU B CD2   
3053 N  N     . LYS A 392 ? 0.93274 1.12038 0.96768 -0.02734 -0.17614 0.23772  471 LYS B N     
3054 C  CA    . LYS A 392 ? 1.02867 1.22835 1.05069 -0.03498 -0.17725 0.23075  471 LYS B CA    
3055 C  C     . LYS A 392 ? 1.07086 1.26329 1.08403 -0.03984 -0.16578 0.21955  471 LYS B C     
3056 O  O     . LYS A 392 ? 1.06234 1.26326 1.07402 -0.04457 -0.16504 0.20968  471 LYS B O     
3057 C  CB    . LYS A 392 ? 1.12236 1.32785 1.12440 -0.03830 -0.18512 0.23996  471 LYS B CB    
3058 C  CG    . LYS A 392 ? 1.21290 1.42389 1.22177 -0.03335 -0.19701 0.25335  471 LYS B CG    
3059 C  CD    . LYS A 392 ? 1.29823 1.52474 1.32392 -0.03103 -0.20543 0.24948  471 LYS B CD    
3060 C  CE    . LYS A 392 ? 1.18665 1.41715 1.22266 -0.02468 -0.21705 0.26275  471 LYS B CE    
3061 N  NZ    . LYS A 392 ? 1.09917 1.33207 1.11468 -0.02653 -0.22468 0.27573  471 LYS B NZ    
3062 N  N     . ASP A 393 ? 1.07258 1.24897 1.08101 -0.03866 -0.15770 0.22067  472 ASP B N     
3063 C  CA    . ASP A 393 ? 0.95714 1.12576 0.95600 -0.04291 -0.14736 0.21121  472 ASP B CA    
3064 C  C     . ASP A 393 ? 0.93560 1.09811 0.94889 -0.03955 -0.13885 0.20274  472 ASP B C     
3065 O  O     . ASP A 393 ? 0.92846 1.08286 0.93509 -0.04209 -0.13018 0.19550  472 ASP B O     
3066 C  CB    . ASP A 393 ? 1.01216 1.16772 0.99746 -0.04408 -0.14370 0.21723  472 ASP B CB    
3067 C  CG    . ASP A 393 ? 1.00549 1.16910 0.97182 -0.04928 -0.14824 0.22365  472 ASP B CG    
3068 O  OD1   . ASP A 393 ? 1.28520 1.45829 1.25100 -0.04815 -0.15769 0.23268  472 ASP B OD1   
3069 O  OD2   . ASP A 393 ? 1.16416 1.32546 1.11589 -0.05397 -0.14223 0.21996  472 ASP B OD2   
3070 N  N     . LEU A 394 ? 1.06094 1.22808 1.09366 -0.03348 -0.14084 0.20391  473 LEU B N     
3071 C  CA    . LEU A 394 ? 0.93364 1.09676 0.97945 -0.02917 -0.13188 0.19732  473 LEU B CA    
3072 C  C     . LEU A 394 ? 0.92561 1.09744 0.97435 -0.03507 -0.12773 0.18810  473 LEU B C     
3073 O  O     . LEU A 394 ? 0.97267 1.15850 1.02635 -0.03913 -0.13451 0.18703  473 LEU B O     
3074 C  CB    . LEU A 394 ? 0.89935 1.06753 0.96586 -0.02023 -0.13481 0.20151  473 LEU B CB    
3075 C  CG    . LEU A 394 ? 0.81429 0.97733 0.89248 -0.01290 -0.12491 0.19657  473 LEU B CG    
3076 C  CD1   . LEU A 394 ? 0.80259 0.94608 0.87133 -0.00807 -0.12094 0.19687  473 LEU B CD1   
3077 C  CD2   . LEU A 394 ? 0.78074 0.95537 0.88155 -0.00467 -0.12751 0.19937  473 LEU B CD2   
3078 N  N     . GLN A 395 ? 0.95230 1.11532 0.99861 -0.03551 -0.11741 0.18149  474 GLN B N     
3079 C  CA    . GLN A 395 ? 0.94705 1.11581 0.99804 -0.04082 -0.11277 0.17353  474 GLN B CA    
3080 C  C     . GLN A 395 ? 0.86681 1.03633 0.93403 -0.03581 -0.10394 0.17161  474 GLN B C     
3081 O  O     . GLN A 395 ? 0.94966 1.12922 1.02967 -0.03938 -0.10240 0.16845  474 GLN B O     
3082 C  CB    . GLN A 395 ? 0.99372 1.15280 1.02619 -0.04687 -0.10812 0.16729  474 GLN B CB    
3083 C  CG    . GLN A 395 ? 0.95991 1.11999 0.97443 -0.05167 -0.11488 0.16876  474 GLN B CG    
3084 C  CD    . GLN A 395 ? 1.02270 1.17450 1.02067 -0.05657 -0.10939 0.16216  474 GLN B CD    
3085 O  OE1   . GLN A 395 ? 1.10502 1.25216 1.10597 -0.05799 -0.10241 0.15523  474 GLN B OE1   
3086 N  NE2   . GLN A 395 ? 1.14945 1.30016 1.13043 -0.05893 -0.11233 0.16502  474 GLN B NE2   
3087 N  N     . LYS A 396 ? 0.79042 0.95005 0.85775 -0.02747 -0.09834 0.17352  475 LYS B N     
3088 C  CA    . LYS A 396 ? 0.84970 1.01056 0.92924 -0.02112 -0.08889 0.17174  475 LYS B CA    
3089 C  C     . LYS A 396 ? 0.91568 1.07763 1.00583 -0.00994 -0.09028 0.17641  475 LYS B C     
3090 O  O     . LYS A 396 ? 0.87303 1.02226 0.95414 -0.00514 -0.09294 0.17829  475 LYS B O     
3091 C  CB    . LYS A 396 ? 0.84324 0.98932 0.90930 -0.02062 -0.07951 0.16661  475 LYS B CB    
3092 C  CG    . LYS A 396 ? 0.91184 1.06053 0.98749 -0.01477 -0.06884 0.16479  475 LYS B CG    
3093 C  CD    . LYS A 396 ? 1.08589 1.21797 1.14600 -0.01152 -0.06150 0.16043  475 LYS B CD    
3094 C  CE    . LYS A 396 ? 1.09875 1.23436 1.16511 -0.00655 -0.05041 0.15892  475 LYS B CE    
3095 N  NZ    . LYS A 396 ? 1.15297 1.29519 1.22396 -0.01582 -0.04685 0.15781  475 LYS B NZ    
3096 N  N     . LEU A 397 ? 0.87389 1.05117 0.98466 -0.00572 -0.08880 0.17832  476 LEU B N     
3097 C  CA    . LEU A 397 ? 0.78149 0.96202 0.90487 0.00632  -0.08917 0.18165  476 LEU B CA    
3098 C  C     . LEU A 397 ? 0.89231 1.08125 1.02831 0.01298  -0.07744 0.17965  476 LEU B C     
3099 O  O     . LEU A 397 ? 0.89032 1.09550 1.04172 0.00868  -0.07453 0.18076  476 LEU B O     
3100 C  CB    . LEU A 397 ? 0.87835 1.07317 1.01677 0.00637  -0.09999 0.18744  476 LEU B CB    
3101 C  CG    . LEU A 397 ? 0.79313 0.99242 0.94678 0.01921  -0.10214 0.19110  476 LEU B CG    
3102 C  CD1   . LEU A 397 ? 0.78798 0.96710 0.92862 0.02671  -0.10400 0.19106  476 LEU B CD1   
3103 C  CD2   . LEU A 397 ? 0.60963 0.82366 0.77778 0.01780  -0.11390 0.19705  476 LEU B CD2   
3104 N  N     . VAL A 398 ? 0.84200 1.02037 0.97175 0.02350  -0.07098 0.17689  477 VAL B N     
3105 C  CA    . VAL A 398 ? 0.87645 1.06230 1.01394 0.03161  -0.05873 0.17498  477 VAL B CA    
3106 C  C     . VAL A 398 ? 0.91911 1.11119 1.06962 0.04626  -0.05914 0.17616  477 VAL B C     
3107 O  O     . VAL A 398 ? 0.82552 1.00262 0.96693 0.05515  -0.06213 0.17335  477 VAL B O     
3108 C  CB    . VAL A 398 ? 0.74212 0.91168 0.86008 0.03334  -0.05054 0.16933  477 VAL B CB    
3109 C  CG1   . VAL A 398 ? 0.86034 1.03870 0.98446 0.04375  -0.03795 0.16809  477 VAL B CG1   
3110 C  CG2   . VAL A 398 ? 0.91916 1.08388 1.02650 0.01954  -0.04986 0.16794  477 VAL B CG2   
3111 N  N     . LEU A 399 ? 0.89934 1.11369 1.07270 0.04900  -0.05648 0.18006  478 LEU B N     
3112 C  CA    . LEU A 399 ? 0.92926 1.15339 1.11824 0.06356  -0.05622 0.18109  478 LEU B CA    
3113 C  C     . LEU A 399 ? 0.85787 1.09864 1.05832 0.07230  -0.04177 0.18082  478 LEU B C     
3114 O  O     . LEU A 399 ? 0.77416 1.03214 0.99445 0.08235  -0.03994 0.18311  478 LEU B O     
3115 C  CB    . LEU A 399 ? 0.97173 1.21031 1.18045 0.06085  -0.06711 0.18704  478 LEU B CB    
3116 C  CG    . LEU A 399 ? 0.84905 1.07426 1.04744 0.05414  -0.08184 0.18913  478 LEU B CG    
3117 C  CD1   . LEU A 399 ? 0.67166 0.91457 0.88897 0.04916  -0.09190 0.19519  478 LEU B CD1   
3118 C  CD2   . LEU A 399 ? 0.88524 1.09292 1.07563 0.06553  -0.08692 0.18748  478 LEU B CD2   
3119 N  N     . THR A 400 ? 0.87375 1.11062 1.06225 0.06911  -0.03127 0.17863  479 THR B N     
3120 C  CA    . THR A 400 ? 0.88106 1.13551 1.07958 0.07597  -0.01664 0.18040  479 THR B CA    
3121 C  C     . THR A 400 ? 0.93693 1.19158 1.13312 0.09573  -0.01110 0.17578  479 THR B C     
3122 O  O     . THR A 400 ? 0.89233 1.12574 1.06983 0.10283  -0.01528 0.16876  479 THR B O     
3123 C  CB    . THR A 400 ? 0.89965 1.14696 1.08317 0.06826  -0.00780 0.17955  479 THR B CB    
3124 O  OG1   . THR A 400 ? 0.91976 1.16566 1.10551 0.05071  -0.01401 0.18230  479 THR B OG1   
3125 C  CG2   . THR A 400 ? 0.99532 1.26293 1.19022 0.07413  0.00772  0.18393  479 THR B CG2   
3126 N  N     . ASN A 401 ? 0.89622 1.17578 1.11284 0.10482  -0.00202 0.17957  480 ASN B N     
3127 C  CA    . ASN A 401 ? 0.91195 1.19709 1.12859 0.12519  0.00525  0.17491  480 ASN B CA    
3128 C  C     . ASN A 401 ? 0.90986 1.18573 1.12992 0.13537  -0.00704 0.17040  480 ASN B C     
3129 O  O     . ASN A 401 ? 0.84448 1.09814 1.04602 0.14387  -0.01150 0.16214  480 ASN B O     
3130 C  CB    . ASN A 401 ? 0.86840 1.13824 1.05827 0.13221  0.01369  0.16788  480 ASN B CB    
3131 C  CG    . ASN A 401 ? 0.95827 1.24200 1.14926 0.15261  0.02574  0.16430  480 ASN B CG    
3132 O  OD1   . ASN A 401 ? 1.02870 1.32738 1.23746 0.16444  0.02536  0.16426  480 ASN B OD1   
3133 N  ND2   . ASN A 401 ? 1.04259 1.32209 1.21401 0.15761  0.03642  0.16105  480 ASN B ND2   
3134 N  N     . ASN A 402 ? 0.93799 1.23052 1.18291 0.13467  -0.01320 0.17598  481 ASN B N     
3135 C  CA    . ASN A 402 ? 0.92897 1.21516 1.18105 0.14471  -0.02515 0.17336  481 ASN B CA    
3136 C  C     . ASN A 402 ? 0.92593 1.24211 1.20960 0.15227  -0.02280 0.17865  481 ASN B C     
3137 O  O     . ASN A 402 ? 0.98648 1.32757 1.28444 0.15276  -0.00989 0.18314  481 ASN B O     
3138 C  CB    . ASN A 402 ? 0.92501 1.19168 1.16954 0.13137  -0.04166 0.17547  481 ASN B CB    
3139 C  CG    . ASN A 402 ? 0.88918 1.12507 1.10488 0.12900  -0.04538 0.16914  481 ASN B CG    
3140 O  OD1   . ASN A 402 ? 0.82158 1.04071 1.02949 0.14072  -0.05046 0.16299  481 ASN B OD1   
3141 N  ND2   . ASN A 402 ? 0.88179 1.11007 1.08312 0.11383  -0.04354 0.17044  481 ASN B ND2   
3142 N  N     . GLN A 403 ? 0.93001 1.24444 1.22596 0.15810  -0.03542 0.17896  482 GLN B N     
3143 C  CA    . GLN A 403 ? 1.03882 1.38048 1.36582 0.16684  -0.03517 0.18329  482 GLN B CA    
3144 C  C     . GLN A 403 ? 0.95622 1.30546 1.30082 0.15375  -0.04886 0.19153  482 GLN B C     
3145 O  O     . GLN A 403 ? 1.02237 1.38680 1.39068 0.16156  -0.05477 0.19439  482 GLN B O     
3146 C  CB    . GLN A 403 ? 1.10214 1.43804 1.43191 0.18844  -0.03845 0.17597  482 GLN B CB    
3147 C  CG    . GLN A 403 ? 1.01234 1.33083 1.31795 0.20150  -0.03078 0.16503  482 GLN B CG    
3148 C  CD    . GLN A 403 ? 1.11786 1.46084 1.42946 0.21499  -0.01207 0.16277  482 GLN B CD    
3149 O  OE1   . GLN A 403 ? 1.37138 1.72200 1.69038 0.23535  -0.00893 0.15636  482 GLN B OE1   
3150 N  NE2   . GLN A 403 ? 1.05985 1.41563 1.36835 0.20422  0.00054  0.16826  482 GLN B NE2   
3151 N  N     . LEU A 404 ? 0.88504 1.22451 1.21827 0.13478  -0.05442 0.19489  483 LEU B N     
3152 C  CA    . LEU A 404 ? 0.92006 1.26404 1.26507 0.12281  -0.06905 0.20137  483 LEU B CA    
3153 C  C     . LEU A 404 ? 0.82570 1.20288 1.20308 0.11924  -0.06578 0.20811  483 LEU B C     
3154 O  O     . LEU A 404 ? 0.92740 1.31814 1.31055 0.11207  -0.05442 0.21032  483 LEU B O     
3155 C  CB    . LEU A 404 ? 0.82913 1.15487 1.15177 0.10460  -0.07489 0.20181  483 LEU B CB    
3156 C  CG    . LEU A 404 ? 0.86474 1.15835 1.15673 0.10506  -0.07905 0.19656  483 LEU B CG    
3157 C  CD1   . LEU A 404 ? 0.89071 1.17203 1.16441 0.08682  -0.08399 0.19777  483 LEU B CD1   
3158 C  CD2   . LEU A 404 ? 0.90636 1.18807 1.19973 0.11464  -0.09209 0.19698  483 LEU B CD2   
3159 N  N     . THR A 405 ? 0.71770 1.10798 1.11771 0.12400  -0.07635 0.21199  484 THR B N     
3160 C  CA    . THR A 405 ? 0.90206 1.32394 1.33555 0.11954  -0.07633 0.21876  484 THR B CA    
3161 C  C     . THR A 405 ? 0.91591 1.33832 1.35325 0.10271  -0.09205 0.22330  484 THR B C     
3162 O  O     . THR A 405 ? 0.77969 1.22411 1.23960 0.09315  -0.09165 0.22791  484 THR B O     
3163 C  CB    . THR A 405 ? 0.76155 1.20259 1.22215 0.13686  -0.07741 0.22006  484 THR B CB    
3164 O  OG1   . THR A 405 ? 0.81440 1.24080 1.27126 0.14075  -0.09489 0.22013  484 THR B OG1   
3165 C  CG2   . THR A 405 ? 0.84915 1.29094 1.30513 0.15540  -0.06204 0.21413  484 THR B CG2   
3166 N  N     . THR A 406 ? 0.89175 1.29111 1.30812 0.09911  -0.10611 0.22225  485 THR B N     
3167 C  CA    . THR A 406 ? 0.85464 1.25319 1.26933 0.08430  -0.12141 0.22575  485 THR B CA    
3168 C  C     . THR A 406 ? 0.92287 1.29135 1.30149 0.07678  -0.12703 0.22291  485 THR B C     
3169 O  O     . THR A 406 ? 0.94126 1.28902 1.30121 0.08523  -0.12487 0.21983  485 THR B O     
3170 C  CB    . THR A 406 ? 0.84423 1.25412 1.27887 0.08961  -0.13704 0.23080  485 THR B CB    
3171 O  OG1   . THR A 406 ? 0.86738 1.25995 1.29171 0.10320  -0.14154 0.22989  485 THR B OG1   
3172 C  CG2   . THR A 406 ? 0.77254 1.21541 1.24643 0.09547  -0.13278 0.23425  485 THR B CG2   
3173 N  N     . LEU A 407 ? 0.97661 1.34352 1.34662 0.06105  -0.13450 0.22365  486 LEU B N     
3174 C  CA    . LEU A 407 ? 0.89703 1.23975 1.23528 0.05315  -0.14176 0.22223  486 LEU B CA    
3175 C  C     . LEU A 407 ? 0.81528 1.15823 1.15347 0.05170  -0.16015 0.22756  486 LEU B C     
3176 O  O     . LEU A 407 ? 0.97363 1.33707 1.33405 0.04950  -0.16870 0.23091  486 LEU B O     
3177 C  CB    . LEU A 407 ? 0.92322 1.26354 1.24922 0.03760  -0.13849 0.21880  486 LEU B CB    
3178 C  CG    . LEU A 407 ? 0.85177 1.18964 1.17406 0.03674  -0.12113 0.21446  486 LEU B CG    
3179 C  CD1   . LEU A 407 ? 0.81413 1.15515 1.13409 0.02108  -0.12097 0.21225  486 LEU B CD1   
3180 C  CD2   . LEU A 407 ? 0.68881 1.00126 0.98323 0.04229  -0.11467 0.21054  486 LEU B CD2   
3181 N  N     . PRO A 408 ? 0.94567 1.26708 1.26038 0.05295  -0.16694 0.22923  487 PRO B N     
3182 C  CA    . PRO A 408 ? 0.96459 1.28633 1.27643 0.05072  -0.18443 0.23585  487 PRO B CA    
3183 C  C     . PRO A 408 ? 0.93996 1.27141 1.24684 0.03617  -0.19205 0.23527  487 PRO B C     
3184 O  O     . PRO A 408 ? 0.98694 1.31216 1.27814 0.02627  -0.18569 0.22995  487 PRO B O     
3185 C  CB    . PRO A 408 ? 0.83518 1.13017 1.12003 0.05263  -0.18677 0.23793  487 PRO B CB    
3186 C  CG    . PRO A 408 ? 0.93920 1.22210 1.22175 0.06129  -0.17253 0.23222  487 PRO B CG    
3187 C  CD    . PRO A 408 ? 0.89474 1.19128 1.18619 0.05700  -0.15941 0.22602  487 PRO B CD    
3188 N  N     . ARG A 409 ? 0.85120 1.19809 1.17207 0.03555  -0.20655 0.24016  488 ARG B N     
3189 C  CA    . ARG A 409 ? 0.90573 1.26395 1.22467 0.02297  -0.21558 0.23824  488 ARG B CA    
3190 C  C     . ARG A 409 ? 1.00209 1.34329 1.28550 0.01392  -0.21907 0.23691  488 ARG B C     
3191 O  O     . ARG A 409 ? 1.00748 1.35279 1.28321 0.00299  -0.22106 0.23142  488 ARG B O     
3192 C  CB    . ARG A 409 ? 0.86308 1.23993 1.20173 0.02535  -0.23224 0.24391  488 ARG B CB    
3193 C  CG    . ARG A 409 ? 0.93163 1.32665 1.30694 0.03578  -0.22952 0.24619  488 ARG B CG    
3194 C  CD    . ARG A 409 ? 0.84499 1.26103 1.24220 0.03623  -0.24668 0.25082  488 ARG B CD    
3195 N  NE    . ARG A 409 ? 0.96593 1.39877 1.37523 0.02438  -0.25095 0.24602  488 ARG B NE    
3196 C  CZ    . ARG A 409 ? 1.15653 1.60995 1.58743 0.02242  -0.26589 0.24795  488 ARG B CZ    
3197 N  NH1   . ARG A 409 ? 1.13383 1.59460 1.57614 0.03158  -0.27806 0.25516  488 ARG B NH1   
3198 N  NH2   . ARG A 409 ? 1.13661 1.60312 1.57900 0.01107  -0.26957 0.24239  488 ARG B NH2   
3199 N  N     . GLY A 410 ? 1.01631 1.33872 1.27901 0.01845  -0.21982 0.24177  489 GLY B N     
3200 C  CA    . GLY A 410 ? 0.96210 1.26911 1.19181 0.01070  -0.22109 0.24160  489 GLY B CA    
3201 C  C     . GLY A 410 ? 1.04084 1.33684 1.25599 0.00413  -0.20707 0.23306  489 GLY B C     
3202 O  O     . GLY A 410 ? 1.19331 1.47829 1.38201 -0.00264 -0.20737 0.23201  489 GLY B O     
3203 N  N     . ILE A 411 ? 0.94536 1.24505 1.17706 0.00624  -0.19468 0.22746  490 ILE B N     
3204 C  CA    . ILE A 411 ? 0.98311 1.27285 1.20229 0.00032  -0.18158 0.21983  490 ILE B CA    
3205 C  C     . ILE A 411 ? 1.02688 1.32006 1.23348 -0.01231 -0.18604 0.21438  490 ILE B C     
3206 O  O     . ILE A 411 ? 1.03891 1.31998 1.22687 -0.01801 -0.17844 0.20895  490 ILE B O     
3207 C  CB    . ILE A 411 ? 1.00060 1.29866 1.24273 0.00468  -0.16872 0.21628  490 ILE B CB    
3208 C  CG1   . ILE A 411 ? 0.85946 1.14371 1.08672 0.00134  -0.15437 0.20997  490 ILE B CG1   
3209 C  CG2   . ILE A 411 ? 0.99753 1.31866 1.26542 -0.00049 -0.17282 0.21511  490 ILE B CG2   
3210 C  CD1   . ILE A 411 ? 0.77940 1.04482 0.99355 0.01030  -0.14673 0.21041  490 ILE B CD1   
3211 N  N     . GLY A 412 ? 0.99993 1.30929 1.21631 -0.01627 -0.19907 0.21505  491 GLY B N     
3212 C  CA    . GLY A 412 ? 1.03120 1.34407 1.23554 -0.02711 -0.20547 0.20853  491 GLY B CA    
3213 C  C     . GLY A 412 ? 0.97785 1.27898 1.14852 -0.03028 -0.21046 0.20940  491 GLY B C     
3214 O  O     . GLY A 412 ? 0.99925 1.30097 1.15568 -0.03841 -0.21359 0.20227  491 GLY B O     
3215 N  N     . HIS A 413 ? 1.02192 1.31292 1.18055 -0.02392 -0.21136 0.21809  492 HIS B N     
3216 C  CA    . HIS A 413 ? 1.01042 1.29083 1.13805 -0.02679 -0.21428 0.22113  492 HIS B CA    
3217 C  C     . HIS A 413 ? 0.99723 1.26082 1.10680 -0.03020 -0.20088 0.21597  492 HIS B C     
3218 O  O     . HIS A 413 ? 1.03449 1.28960 1.11925 -0.03277 -0.20138 0.21861  492 HIS B O     
3219 C  CB    . HIS A 413 ? 0.88964 1.16500 1.01389 -0.01931 -0.22066 0.23404  492 HIS B CB    
3220 C  CG    . HIS A 413 ? 1.03677 1.32801 1.17115 -0.01672 -0.23640 0.24035  492 HIS B CG    
3221 N  ND1   . HIS A 413 ? 1.03575 1.32509 1.17477 -0.00894 -0.24381 0.25246  492 HIS B ND1   
3222 C  CD2   . HIS A 413 ? 1.08891 1.39784 1.23026 -0.02072 -0.24714 0.23607  492 HIS B CD2   
3223 C  CE1   . HIS A 413 ? 0.94705 1.25285 1.09481 -0.00806 -0.25810 0.25586  492 HIS B CE1   
3224 N  NE2   . HIS A 413 ? 1.18933 1.50749 1.33860 -0.01516 -0.26059 0.24573  492 HIS B NE2   
3225 N  N     . LEU A 414 ? 0.91432 1.17398 1.03593 -0.03012 -0.18895 0.20940  493 LEU B N     
3226 C  CA    . LEU A 414 ? 0.85818 1.10228 0.96413 -0.03302 -0.17658 0.20404  493 LEU B CA    
3227 C  C     . LEU A 414 ? 0.92952 1.17717 1.02593 -0.04249 -0.17658 0.19409  493 LEU B C     
3228 O  O     . LEU A 414 ? 0.89284 1.13986 0.99800 -0.04569 -0.16873 0.18664  493 LEU B O     
3229 C  CB    . LEU A 414 ? 1.00258 1.24087 1.12412 -0.02744 -0.16423 0.20218  493 LEU B CB    
3230 C  CG    . LEU A 414 ? 0.87128 1.10521 1.00309 -0.01660 -0.16419 0.20985  493 LEU B CG    
3231 C  CD1   . LEU A 414 ? 0.88603 1.11645 1.03151 -0.01035 -0.15154 0.20620  493 LEU B CD1   
3232 C  CD2   . LEU A 414 ? 0.67218 0.89020 0.78371 -0.01494 -0.16632 0.21599  493 LEU B CD2   
3233 N  N     . THR A 415 ? 0.98561 1.23694 1.06310 -0.04650 -0.18583 0.19430  494 THR B N     
3234 C  CA    . THR A 415 ? 1.01017 1.26681 1.07852 -0.05431 -0.18918 0.18389  494 THR B CA    
3235 C  C     . THR A 415 ? 0.97344 1.21724 1.03007 -0.05838 -0.17728 0.17581  494 THR B C     
3236 O  O     . THR A 415 ? 1.09849 1.34522 1.15271 -0.06440 -0.17875 0.16559  494 THR B O     
3237 C  CB    . THR A 415 ? 1.11260 1.37578 1.15894 -0.05582 -0.20074 0.18619  494 THR B CB    
3238 O  OG1   . THR A 415 ? 1.35721 1.62913 1.39967 -0.06187 -0.20751 0.17467  494 THR B OG1   
3239 C  CG2   . THR A 415 ? 1.05936 1.31045 1.07904 -0.05565 -0.19447 0.19055  494 THR B CG2   
3240 N  N     . ASN A 416 ? 1.04614 1.27553 1.09635 -0.05504 -0.16652 0.17961  495 ASN B N     
3241 C  CA    . ASN A 416 ? 0.99724 1.21421 1.03725 -0.05817 -0.15536 0.17255  495 ASN B CA    
3242 C  C     . ASN A 416 ? 1.01201 1.22266 1.06924 -0.05527 -0.14443 0.17118  495 ASN B C     
3243 O  O     . ASN A 416 ? 0.91145 1.11056 0.96098 -0.05660 -0.13472 0.16661  495 ASN B O     
3244 C  CB    . ASN A 416 ? 0.89162 1.09700 0.90857 -0.05724 -0.15165 0.17716  495 ASN B CB    
3245 C  CG    . ASN A 416 ? 1.03978 1.25238 1.03603 -0.06050 -0.15997 0.17806  495 ASN B CG    
3246 O  OD1   . ASN A 416 ? 1.07810 1.30024 1.07088 -0.06471 -0.16592 0.16991  495 ASN B OD1   
3247 N  ND2   . ASN A 416 ? 1.03203 1.24033 1.01457 -0.05830 -0.16063 0.18810  495 ASN B ND2   
3248 N  N     . LEU A 417 ? 1.04114 1.26012 1.12120 -0.05083 -0.14562 0.17520  496 LEU B N     
3249 C  CA    . LEU A 417 ? 1.04405 1.25941 1.13955 -0.04674 -0.13455 0.17480  496 LEU B CA    
3250 C  C     . LEU A 417 ? 0.99484 1.21294 1.09882 -0.05321 -0.12970 0.16698  496 LEU B C     
3251 O  O     . LEU A 417 ? 1.10415 1.33428 1.21966 -0.05864 -0.13716 0.16378  496 LEU B O     
3252 C  CB    . LEU A 417 ? 0.95903 1.18537 1.07759 -0.03959 -0.13704 0.18129  496 LEU B CB    
3253 C  CG    . LEU A 417 ? 0.91162 1.13556 1.04421 -0.03238 -0.12518 0.18226  496 LEU B CG    
3254 C  CD1   . LEU A 417 ? 0.94363 1.14939 1.05983 -0.02624 -0.11860 0.18343  496 LEU B CD1   
3255 C  CD2   . LEU A 417 ? 0.85524 1.09419 1.01288 -0.02556 -0.12834 0.18774  496 LEU B CD2   
3256 N  N     . THR A 418 ? 1.01232 1.21870 1.11119 -0.05264 -0.11799 0.16403  497 THR B N     
3257 C  CA    . THR A 418 ? 1.12687 1.33372 1.23416 -0.05827 -0.11235 0.15813  497 THR B CA    
3258 C  C     . THR A 418 ? 1.05967 1.26794 1.18373 -0.05340 -0.10103 0.16127  497 THR B C     
3259 O  O     . THR A 418 ? 0.95262 1.16641 1.09160 -0.05803 -0.09762 0.15945  497 THR B O     
3260 C  CB    . THR A 418 ? 1.10215 1.29469 1.18767 -0.06270 -0.10838 0.15130  497 THR B CB    
3261 O  OG1   . THR A 418 ? 0.95697 1.13592 1.03115 -0.05684 -0.09883 0.15337  497 THR B OG1   
3262 C  CG2   . THR A 418 ? 1.06722 1.25970 1.13375 -0.06637 -0.11798 0.14846  497 THR B CG2   
3263 N  N     . HIS A 419 ? 1.05054 1.25423 1.17275 -0.04397 -0.09537 0.16599  498 HIS B N     
3264 C  CA    . HIS A 419 ? 0.99744 1.20311 1.13210 -0.03733 -0.08392 0.16857  498 HIS B CA    
3265 C  C     . HIS A 419 ? 0.99735 1.21156 1.14457 -0.02741 -0.08536 0.17453  498 HIS B C     
3266 O  O     . HIS A 419 ? 0.98156 1.18759 1.11743 -0.02199 -0.08957 0.17619  498 HIS B O     
3267 C  CB    . HIS A 419 ? 0.95653 1.14470 1.07256 -0.03391 -0.07420 0.16565  498 HIS B CB    
3268 C  CG    . HIS A 419 ? 1.03340 1.22383 1.15861 -0.02651 -0.06214 0.16770  498 HIS B CG    
3269 N  ND1   . HIS A 419 ? 1.12586 1.31471 1.25251 -0.02994 -0.05336 0.16619  498 HIS B ND1   
3270 C  CD2   . HIS A 419 ? 1.04545 1.24019 1.17821 -0.01516 -0.05739 0.17121  498 HIS B CD2   
3271 C  CE1   . HIS A 419 ? 1.10447 1.29758 1.23802 -0.02110 -0.04321 0.16942  498 HIS B CE1   
3272 N  NE2   . HIS A 419 ? 1.00486 1.20183 1.14202 -0.01168 -0.04534 0.17175  498 HIS B NE2   
3273 N  N     . LEU A 420 ? 0.89745 1.12829 1.06940 -0.02493 -0.08194 0.17812  499 LEU B N     
3274 C  CA    . LEU A 420 ? 0.86156 1.10294 1.04871 -0.01449 -0.08244 0.18330  499 LEU B CA    
3275 C  C     . LEU A 420 ? 0.93220 1.18300 1.13476 -0.00787 -0.06903 0.18558  499 LEU B C     
3276 O  O     . LEU A 420 ? 0.80817 1.07425 1.03118 -0.01300 -0.06599 0.18805  499 LEU B O     
3277 C  CB    . LEU A 420 ? 0.82909 1.08724 1.03454 -0.01791 -0.09460 0.18656  499 LEU B CB    
3278 C  CG    . LEU A 420 ? 0.88263 1.15192 1.10440 -0.00705 -0.09753 0.19195  499 LEU B CG    
3279 C  CD1   . LEU A 420 ? 0.81094 1.06370 1.01410 0.00159  -0.09976 0.19228  499 LEU B CD1   
3280 C  CD2   . LEU A 420 ? 0.62731 0.91319 0.86659 -0.01162 -0.11087 0.19488  499 LEU B CD2   
3281 N  N     . GLY A 421 ? 0.89834 1.14045 1.09138 0.00362  -0.06127 0.18490  500 GLY B N     
3282 C  CA    . GLY A 421 ? 0.88708 1.13850 1.09081 0.01198  -0.04778 0.18683  500 GLY B CA    
3283 C  C     . GLY A 421 ? 0.77349 1.03925 0.99494 0.02473  -0.04698 0.19032  500 GLY B C     
3284 O  O     . GLY A 421 ? 0.79002 1.04577 1.00157 0.03593  -0.04790 0.18801  500 GLY B O     
3285 N  N     . LEU A 422 ? 0.85481 1.14420 1.10419 0.02331  -0.04568 0.19573  501 LEU B N     
3286 C  CA    . LEU A 422 ? 0.97502 1.28187 1.24540 0.03520  -0.04495 0.19939  501 LEU B CA    
3287 C  C     . LEU A 422 ? 0.91002 1.23437 1.19529 0.04319  -0.02891 0.20289  501 LEU B C     
3288 O  O     . LEU A 422 ? 0.89615 1.24360 1.20788 0.04884  -0.02668 0.20791  501 LEU B O     
3289 C  CB    . LEU A 422 ? 0.97621 1.29955 1.26972 0.02854  -0.05713 0.20358  501 LEU B CB    
3290 C  CG    . LEU A 422 ? 0.88820 1.19801 1.16754 0.02158  -0.07339 0.20137  501 LEU B CG    
3291 C  CD1   . LEU A 422 ? 0.86597 1.19383 1.16798 0.01363  -0.08504 0.20499  501 LEU B CD1   
3292 C  CD2   . LEU A 422 ? 0.89433 1.19143 1.16155 0.03332  -0.07841 0.20024  501 LEU B CD2   
3293 N  N     . GLY A 423 ? 0.95720 1.27196 1.22582 0.04410  -0.01749 0.20083  502 GLY B N     
3294 C  CA    . GLY A 423 ? 0.93097 1.26281 1.21087 0.05150  -0.00146 0.20523  502 GLY B CA    
3295 C  C     . GLY A 423 ? 0.92706 1.26289 1.20449 0.07129  0.00516  0.20265  502 GLY B C     
3296 O  O     . GLY A 423 ? 0.82434 1.14231 1.08454 0.07944  -0.00141 0.19583  502 GLY B O     
3297 N  N     . GLU A 424 ? 0.91751 1.27797 1.21380 0.07919  0.01834  0.20841  503 GLU B N     
3298 C  CA    . GLU A 424 ? 0.92767 1.29611 1.22273 0.09965  0.02718  0.20561  503 GLU B CA    
3299 C  C     . GLU A 424 ? 0.96492 1.33116 1.26646 0.10922  0.01536  0.20136  503 GLU B C     
3300 O  O     . GLU A 424 ? 0.88216 1.23453 1.16769 0.12340  0.01410  0.19349  503 GLU B O     
3301 C  CB    . GLU A 424 ? 0.90911 1.25771 1.17194 0.10809  0.03471  0.19839  503 GLU B CB    
3302 C  CG    . GLU A 424 ? 1.03676 1.39205 1.29517 0.10286  0.04894  0.20400  503 GLU B CG    
3303 C  CD    . GLU A 424 ? 1.17159 1.49986 1.39581 0.10272  0.05003  0.19685  503 GLU B CD    
3304 O  OE1   . GLU A 424 ? 1.25218 1.56013 1.45643 0.11166  0.04334  0.18697  503 GLU B OE1   
3305 O  OE2   . GLU A 424 ? 1.14571 1.47282 1.36449 0.09343  0.05689  0.20139  503 GLU B OE2   
3306 N  N     . ASN A 425 ? 0.91126 1.29097 1.23738 0.10142  0.00575  0.20664  504 ASN B N     
3307 C  CA    . ASN A 425 ? 0.91876 1.30051 1.25636 0.10952  -0.00596 0.20501  504 ASN B CA    
3308 C  C     . ASN A 425 ? 0.99141 1.40751 1.36625 0.11346  -0.00212 0.21257  504 ASN B C     
3309 O  O     . ASN A 425 ? 0.99768 1.43552 1.38936 0.10937  0.00973  0.21948  504 ASN B O     
3310 C  CB    . ASN A 425 ? 0.86267 1.22672 1.19276 0.09642  -0.02413 0.20419  504 ASN B CB    
3311 C  CG    . ASN A 425 ? 0.92966 1.26173 1.22839 0.09949  -0.03076 0.19649  504 ASN B CG    
3312 O  OD1   . ASN A 425 ? 0.95194 1.27520 1.24897 0.10964  -0.03910 0.19352  504 ASN B OD1   
3313 N  ND2   . ASN A 425 ? 0.90518 1.21967 1.18052 0.09069  -0.02743 0.19361  504 ASN B ND2   
3314 N  N     . LEU A 426 ? 0.75557 1.17690 1.14480 0.12142  -0.01252 0.21200  505 LEU B N     
3315 C  CA    . LEU A 426 ? 0.88750 1.34201 1.31433 0.12526  -0.01073 0.21903  505 LEU B CA    
3316 C  C     . LEU A 426 ? 0.97327 1.43669 1.41930 0.10660  -0.02253 0.22554  505 LEU B C     
3317 O  O     . LEU A 426 ? 0.97819 1.46279 1.44587 0.09728  -0.01583 0.23268  505 LEU B O     
3318 C  CB    . LEU A 426 ? 0.86595 1.32295 1.30126 0.14348  -0.01679 0.21522  505 LEU B CB    
3319 C  CG    . LEU A 426 ? 0.79707 1.24163 1.21144 0.16286  -0.00778 0.20629  505 LEU B CG    
3320 C  CD1   . LEU A 426 ? 0.89565 1.34365 1.32233 0.18135  -0.01449 0.20223  505 LEU B CD1   
3321 C  CD2   . LEU A 426 ? 0.65705 1.12072 1.07314 0.16939  0.01348  0.20807  505 LEU B CD2   
3322 N  N     . LEU A 427 ? 0.92754 1.37487 1.36584 0.10116  -0.04060 0.22327  506 LEU B N     
3323 C  CA    . LEU A 427 ? 0.90433 1.35397 1.35201 0.08355  -0.05444 0.22691  506 LEU B CA    
3324 C  C     . LEU A 427 ? 0.88675 1.36996 1.37509 0.07894  -0.05421 0.23474  506 LEU B C     
3325 O  O     . LEU A 427 ? 0.84412 1.34127 1.34566 0.07059  -0.04414 0.23924  506 LEU B O     
3326 C  CB    . LEU A 427 ? 0.86833 1.29995 1.29325 0.06766  -0.05330 0.22484  506 LEU B CB    
3327 C  CG    . LEU A 427 ? 0.74438 1.14279 1.13250 0.06489  -0.06169 0.21826  506 LEU B CG    
3328 C  CD1   . LEU A 427 ? 0.64132 1.02884 1.01627 0.04681  -0.06503 0.21717  506 LEU B CD1   
3329 C  CD2   . LEU A 427 ? 0.85332 1.24514 1.24062 0.06881  -0.07839 0.21803  506 LEU B CD2   
3330 N  N     . THR A 428 ? 0.91562 1.41179 1.42531 0.08376  -0.06611 0.23702  507 THR B N     
3331 C  CA    . THR A 428 ? 0.89957 1.42753 1.44979 0.07821  -0.06869 0.24431  507 THR B CA    
3332 C  C     . THR A 428 ? 0.90601 1.43148 1.45938 0.05787  -0.08205 0.24540  507 THR B C     
3333 O  O     . THR A 428 ? 0.84008 1.38819 1.42368 0.04855  -0.08063 0.25096  507 THR B O     
3334 C  CB    . THR A 428 ? 0.73454 1.27781 1.30758 0.09089  -0.07783 0.24611  507 THR B CB    
3335 O  OG1   . THR A 428 ? 0.85564 1.37755 1.40995 0.08911  -0.09673 0.24284  507 THR B OG1   
3336 C  CG2   . THR A 428 ? 0.61239 1.16060 1.18561 0.11225  -0.06431 0.24396  507 THR B CG2   
3337 N  N     . HIS A 429 ? 0.85744 1.35644 1.38090 0.05100  -0.09505 0.24013  508 HIS B N     
3338 C  CA    . HIS A 429 ? 0.92420 1.41969 1.44691 0.03323  -0.10868 0.23927  508 HIS B CA    
3339 C  C     . HIS A 429 ? 0.98928 1.45282 1.47065 0.02878  -0.11686 0.23290  508 HIS B C     
3340 O  O     . HIS A 429 ? 0.95934 1.40543 1.41801 0.03924  -0.11577 0.23048  508 HIS B O     
3341 C  CB    . HIS A 429 ? 0.87722 1.39301 1.42927 0.03089  -0.12537 0.24279  508 HIS B CB    
3342 C  CG    . HIS A 429 ? 0.90835 1.41584 1.45004 0.04095  -0.13842 0.24206  508 HIS B CG    
3343 N  ND1   . HIS A 429 ? 0.86172 1.36542 1.39906 0.05824  -0.13170 0.24221  508 HIS B ND1   
3344 C  CD2   . HIS A 429 ? 0.94575 1.44792 1.48080 0.03646  -0.15824 0.24155  508 HIS B CD2   
3345 C  CE1   . HIS A 429 ? 0.95799 1.45344 1.48798 0.06338  -0.14699 0.24253  508 HIS B CE1   
3346 N  NE2   . HIS A 429 ? 0.98602 1.48103 1.51379 0.05040  -0.16290 0.24276  508 HIS B NE2   
3347 N  N     . LEU A 430 ? 0.93185 1.38843 1.40496 0.01310  -0.12537 0.23011  509 LEU B N     
3348 C  CA    . LEU A 430 ? 0.94805 1.37924 1.38567 0.00696  -0.13518 0.22460  509 LEU B CA    
3349 C  C     . LEU A 430 ? 1.01056 1.44642 1.45149 0.00379  -0.15583 0.22517  509 LEU B C     
3350 O  O     . LEU A 430 ? 0.88409 1.34193 1.35528 0.00006  -0.16407 0.22790  509 LEU B O     
3351 C  CB    . LEU A 430 ? 0.85941 1.28039 1.28450 -0.00717 -0.13195 0.22008  509 LEU B CB    
3352 C  CG    . LEU A 430 ? 0.81954 1.23553 1.24021 -0.00618 -0.11253 0.22003  509 LEU B CG    
3353 C  CD1   . LEU A 430 ? 0.87311 1.27597 1.27931 -0.02026 -0.11267 0.21511  509 LEU B CD1   
3354 C  CD2   . LEU A 430 ? 0.97244 1.37146 1.36817 0.00687  -0.10299 0.21852  509 LEU B CD2   
3355 N  N     . PRO A 431 ? 0.99179 1.40827 1.40277 0.00527  -0.16483 0.22332  510 PRO B N     
3356 C  CA    . PRO A 431 ? 0.83235 1.25339 1.24327 0.00261  -0.18463 0.22471  510 PRO B CA    
3357 C  C     . PRO A 431 ? 0.90900 1.33492 1.32102 -0.01225 -0.19483 0.22010  510 PRO B C     
3358 O  O     . PRO A 431 ? 0.96857 1.38500 1.36875 -0.02114 -0.18826 0.21479  510 PRO B O     
3359 C  CB    . PRO A 431 ? 0.98067 1.37766 1.35581 0.00690  -0.18846 0.22474  510 PRO B CB    
3360 C  CG    . PRO A 431 ? 1.00004 1.38323 1.36502 0.01547  -0.17160 0.22396  510 PRO B CG    
3361 C  CD    . PRO A 431 ? 0.99808 1.38887 1.37552 0.01032  -0.15748 0.22096  510 PRO B CD    
3362 N  N     . GLU A 432 ? 0.99044 1.43120 1.41735 -0.01434 -0.21205 0.22166  511 GLU B N     
3363 C  CA    . GLU A 432 ? 1.01724 1.46217 1.44381 -0.02731 -0.22510 0.21586  511 GLU B CA    
3364 C  C     . GLU A 432 ? 1.11098 1.53444 1.49567 -0.03231 -0.23055 0.21035  511 GLU B C     
3365 O  O     . GLU A 432 ? 1.03518 1.45695 1.41309 -0.04298 -0.23698 0.20294  511 GLU B O     
3366 C  CB    . GLU A 432 ? 0.99526 1.46142 1.44663 -0.02695 -0.24351 0.21862  511 GLU B CB    
3367 C  CG    . GLU A 432 ? 0.92850 1.41963 1.42550 -0.02297 -0.23901 0.22410  511 GLU B CG    
3368 C  CD    . GLU A 432 ? 1.25741 1.76747 1.77621 -0.01808 -0.25628 0.22864  511 GLU B CD    
3369 O  OE1   . GLU A 432 ? 1.31048 1.81189 1.80652 -0.01360 -0.26836 0.23003  511 GLU B OE1   
3370 O  OE2   . GLU A 432 ? 1.39565 1.92993 1.95516 -0.01872 -0.25787 0.23159  511 GLU B OE2   
3371 N  N     . GLU A 433 ? 1.11305 1.52043 1.47072 -0.02467 -0.22811 0.21376  512 GLU B N     
3372 C  CA    . GLU A 433 ? 1.01712 1.40520 1.33540 -0.02861 -0.23115 0.21022  512 GLU B CA    
3373 C  C     . GLU A 433 ? 1.03904 1.41062 1.34010 -0.03359 -0.21605 0.20423  512 GLU B C     
3374 O  O     . GLU A 433 ? 1.06230 1.41712 1.33104 -0.03568 -0.21548 0.20177  512 GLU B O     
3375 C  CB    . GLU A 433 ? 0.95423 1.33147 1.25340 -0.01912 -0.23394 0.21780  512 GLU B CB    
3376 C  CG    . GLU A 433 ? 0.99682 1.38660 1.30305 -0.01528 -0.25207 0.22389  512 GLU B CG    
3377 C  CD    . GLU A 433 ? 1.06276 1.47139 1.40725 -0.00773 -0.25359 0.22885  512 GLU B CD    
3378 O  OE1   . GLU A 433 ? 1.00631 1.41647 1.36838 -0.00307 -0.23895 0.22904  512 GLU B OE1   
3379 O  OE2   . GLU A 433 ? 1.07610 1.49904 1.43291 -0.00595 -0.26944 0.23261  512 GLU B OE2   
3380 N  N     . ILE A 434 ? 0.92522 1.30206 1.24758 -0.03537 -0.20377 0.20263  513 ILE B N     
3381 C  CA    . ILE A 434 ? 0.95647 1.31848 1.26416 -0.04021 -0.19017 0.19733  513 ILE B CA    
3382 C  C     . ILE A 434 ? 0.95476 1.31250 1.24975 -0.05209 -0.19779 0.18844  513 ILE B C     
3383 O  O     . ILE A 434 ? 1.04119 1.38356 1.31661 -0.05615 -0.18940 0.18323  513 ILE B O     
3384 C  CB    . ILE A 434 ? 1.01243 1.38360 1.34764 -0.03877 -0.17557 0.19951  513 ILE B CB    
3385 C  CG1   . ILE A 434 ? 0.92111 1.27446 1.23759 -0.03902 -0.15924 0.19667  513 ILE B CG1   
3386 C  CG2   . ILE A 434 ? 1.02227 1.41101 1.38739 -0.04837 -0.18134 0.19749  513 ILE B CG2   
3387 C  CD1   . ILE A 434 ? 0.88511 1.22600 1.18573 -0.02727 -0.14995 0.20011  513 ILE B CD1   
3388 N  N     . GLY A 435 ? 1.07209 1.44300 1.37762 -0.05713 -0.21429 0.18583  514 GLY B N     
3389 C  CA    . GLY A 435 ? 1.02215 1.39068 1.31909 -0.06761 -0.22312 0.17572  514 GLY B CA    
3390 C  C     . GLY A 435 ? 1.05154 1.40571 1.30853 -0.06857 -0.22840 0.17070  514 GLY B C     
3391 O  O     . GLY A 435 ? 1.18108 1.53019 1.42667 -0.07613 -0.23266 0.16078  514 GLY B O     
3392 N  N     . THR A 436 ? 1.02315 1.37113 1.25968 -0.06094 -0.22835 0.17748  515 THR B N     
3393 C  CA    . THR A 436 ? 1.07118 1.40689 1.27006 -0.06145 -0.23155 0.17506  515 THR B CA    
3394 C  C     . THR A 436 ? 1.15741 1.47382 1.33570 -0.06150 -0.21559 0.17343  515 THR B C     
3395 O  O     . THR A 436 ? 1.19567 1.50196 1.34360 -0.06204 -0.21607 0.17196  515 THR B O     
3396 C  CB    . THR A 436 ? 1.13820 1.47642 1.32581 -0.05399 -0.23985 0.18486  515 THR B CB    
3397 O  OG1   . THR A 436 ? 1.20771 1.54345 1.40905 -0.04567 -0.23080 0.19419  515 THR B OG1   
3398 C  CG2   . THR A 436 ? 1.01544 1.37217 1.21611 -0.05461 -0.25858 0.18494  515 THR B CG2   
3399 N  N     . LEU A 437 ? 1.13294 1.44517 1.32703 -0.06069 -0.20153 0.17407  516 LEU B N     
3400 C  CA    . LEU A 437 ? 1.08376 1.37824 1.26035 -0.06105 -0.18697 0.17155  516 LEU B CA    
3401 C  C     . LEU A 437 ? 1.16664 1.45715 1.33664 -0.07031 -0.18769 0.16042  516 LEU B C     
3402 O  O     . LEU A 437 ? 1.16446 1.45608 1.35266 -0.07466 -0.18177 0.15687  516 LEU B O     
3403 C  CB    . LEU A 437 ? 0.99007 1.28287 1.18483 -0.05586 -0.17257 0.17616  516 LEU B CB    
3404 C  CG    . LEU A 437 ? 1.00989 1.30579 1.21284 -0.04527 -0.17142 0.18565  516 LEU B CG    
3405 C  CD1   . LEU A 437 ? 0.91492 1.20967 1.13327 -0.03945 -0.15632 0.18811  516 LEU B CD1   
3406 C  CD2   . LEU A 437 ? 0.91703 1.19932 1.09231 -0.04095 -0.17351 0.18944  516 LEU B CD2   
3407 N  N     . GLU A 438 ? 1.20078 1.48688 1.34426 -0.07296 -0.19521 0.15519  517 GLU B N     
3408 C  CA    . GLU A 438 ? 1.20409 1.48741 1.34023 -0.08072 -0.19878 0.14297  517 GLU B CA    
3409 C  C     . GLU A 438 ? 1.23798 1.50671 1.37046 -0.08308 -0.18414 0.13905  517 GLU B C     
3410 O  O     . GLU A 438 ? 1.23833 1.50695 1.38590 -0.08903 -0.18319 0.13242  517 GLU B O     
3411 C  CB    . GLU A 438 ? 1.23500 1.51730 1.34001 -0.08095 -0.20797 0.13870  517 GLU B CB    
3412 C  CG    . GLU A 438 ? 1.33253 1.62744 1.43500 -0.07695 -0.22123 0.14534  517 GLU B CG    
3413 C  CD    . GLU A 438 ? 1.32418 1.61598 1.39174 -0.07466 -0.22462 0.14690  517 GLU B CD    
3414 O  OE1   . GLU A 438 ? 1.24560 1.52561 1.29240 -0.07584 -0.21553 0.14327  517 GLU B OE1   
3415 O  OE2   . GLU A 438 ? 1.23522 1.53724 1.29663 -0.07156 -0.23623 0.15250  517 GLU B OE2   
3416 N  N     . ASN A 439 ? 1.17332 1.42938 1.28701 -0.07853 -0.17331 0.14349  518 ASN B N     
3417 C  CA    . ASN A 439 ? 1.27358 1.51496 1.37883 -0.08015 -0.16053 0.13944  518 ASN B CA    
3418 C  C     . ASN A 439 ? 1.20182 1.44057 1.32628 -0.07711 -0.14793 0.14504  518 ASN B C     
3419 O  O     . ASN A 439 ? 1.20157 1.42741 1.31699 -0.07640 -0.13654 0.14384  518 ASN B O     
3420 C  CB    . ASN A 439 ? 1.24173 1.47115 1.31657 -0.07719 -0.15605 0.14067  518 ASN B CB    
3421 C  CG    . ASN A 439 ? 1.27004 1.50390 1.32346 -0.07927 -0.16691 0.13619  518 ASN B CG    
3422 O  OD1   . ASN A 439 ? 1.32079 1.55995 1.37488 -0.08425 -0.17493 0.12640  518 ASN B OD1   
3423 N  ND2   . ASN A 439 ? 1.19757 1.42960 1.23208 -0.07518 -0.16753 0.14348  518 ASN B ND2   
3424 N  N     . LEU A 440 ? 1.10597 1.35766 1.25633 -0.07477 -0.14964 0.15108  519 LEU B N     
3425 C  CA    . LEU A 440 ? 1.11823 1.37035 1.28683 -0.07101 -0.13706 0.15647  519 LEU B CA    
3426 C  C     . LEU A 440 ? 1.15207 1.40088 1.33075 -0.07779 -0.13084 0.15154  519 LEU B C     
3427 O  O     . LEU A 440 ? 1.19683 1.45155 1.38699 -0.08556 -0.13928 0.14598  519 LEU B O     
3428 C  CB    . LEU A 440 ? 1.07937 1.34921 1.27568 -0.06715 -0.14069 0.16368  519 LEU B CB    
3429 C  CG    . LEU A 440 ? 1.03339 1.30796 1.25018 -0.06196 -0.12737 0.16985  519 LEU B CG    
3430 C  CD1   . LEU A 440 ? 0.86752 1.12851 1.06614 -0.05278 -0.11645 0.17271  519 LEU B CD1   
3431 C  CD2   . LEU A 440 ? 1.00732 1.30246 1.25399 -0.05865 -0.13191 0.17631  519 LEU B CD2   
3432 N  N     . GLU A 441 ? 1.07978 1.31855 1.25430 -0.07464 -0.11682 0.15356  520 GLU B N     
3433 C  CA    . GLU A 441 ? 0.99788 1.23151 1.17964 -0.08057 -0.11020 0.15023  520 GLU B CA    
3434 C  C     . GLU A 441 ? 1.01723 1.25537 1.21666 -0.07625 -0.09677 0.15810  520 GLU B C     
3435 O  O     . GLU A 441 ? 1.02020 1.26194 1.23783 -0.08174 -0.09293 0.15914  520 GLU B O     
3436 C  CB    . GLU A 441 ? 1.07407 1.28911 1.22808 -0.08202 -0.10655 0.14331  520 GLU B CB    
3437 C  CG    . GLU A 441 ? 1.18033 1.39235 1.31557 -0.08598 -0.11835 0.13513  520 GLU B CG    
3438 C  CD    . GLU A 441 ? 1.16773 1.36327 1.27621 -0.08621 -0.11358 0.12913  520 GLU B CD    
3439 O  OE1   . GLU A 441 ? 1.08173 1.26722 1.18731 -0.08405 -0.10213 0.13071  520 GLU B OE1   
3440 O  OE2   . GLU A 441 ? 1.07983 1.27357 1.17015 -0.08813 -0.12126 0.12298  520 GLU B OE2   
3441 N  N     . GLU A 442 ? 1.05098 1.28911 1.24536 -0.06613 -0.08970 0.16379  521 GLU B N     
3442 C  CA    . GLU A 442 ? 0.96309 1.20640 1.17040 -0.05972 -0.07624 0.17066  521 GLU B CA    
3443 C  C     . GLU A 442 ? 0.91261 1.16987 1.13334 -0.05075 -0.07684 0.17700  521 GLU B C     
3444 O  O     . GLU A 442 ? 0.93025 1.18185 1.13636 -0.04438 -0.08099 0.17657  521 GLU B O     
3445 C  CB    . GLU A 442 ? 1.00401 1.22994 1.18793 -0.05418 -0.06523 0.16910  521 GLU B CB    
3446 C  CG    . GLU A 442 ? 1.08892 1.30070 1.25968 -0.06202 -0.06420 0.16289  521 GLU B CG    
3447 C  CD    . GLU A 442 ? 1.07451 1.26908 1.22131 -0.05635 -0.05519 0.16087  521 GLU B CD    
3448 O  OE1   . GLU A 442 ? 1.11462 1.30961 1.25978 -0.04657 -0.04682 0.16504  521 GLU B OE1   
3449 O  OE2   . GLU A 442 ? 1.19124 1.37222 1.32116 -0.06120 -0.05696 0.15447  521 GLU B OE2   
3450 N  N     . LEU A 443 ? 0.96629 1.24208 1.21619 -0.05021 -0.07279 0.18338  522 LEU B N     
3451 C  CA    . LEU A 443 ? 0.95227 1.24418 1.21927 -0.04111 -0.07264 0.18946  522 LEU B CA    
3452 C  C     . LEU A 443 ? 0.92220 1.22557 1.20579 -0.03479 -0.05718 0.19631  522 LEU B C     
3453 O  O     . LEU A 443 ? 0.81541 1.13402 1.12508 -0.04073 -0.05422 0.20128  522 LEU B O     
3454 C  CB    . LEU A 443 ? 0.93513 1.24401 1.22543 -0.04697 -0.08614 0.19073  522 LEU B CB    
3455 C  CG    . LEU A 443 ? 0.91482 1.24250 1.22657 -0.03797 -0.08746 0.19712  522 LEU B CG    
3456 C  CD1   . LEU A 443 ? 0.79597 1.11317 1.08700 -0.02688 -0.08938 0.19632  522 LEU B CD1   
3457 C  CD2   . LEU A 443 ? 0.86082 1.20529 1.19657 -0.04514 -0.10199 0.19790  522 LEU B CD2   
3458 N  N     . TYR A 444 ? 0.88865 1.18523 1.15755 -0.02256 -0.04758 0.19672  523 TYR B N     
3459 C  CA    . TYR A 444 ? 0.93021 1.23759 1.20960 -0.01407 -0.03201 0.20252  523 TYR B CA    
3460 C  C     . TYR A 444 ? 0.92252 1.24974 1.22262 -0.00343 -0.03143 0.20733  523 TYR B C     
3461 O  O     . TYR A 444 ? 0.87127 1.19214 1.16007 0.00667  -0.03510 0.20449  523 TYR B O     
3462 C  CB    . TYR A 444 ? 0.83487 1.12362 1.08558 -0.00583 -0.02250 0.19870  523 TYR B CB    
3463 C  CG    . TYR A 444 ? 0.88546 1.15642 1.11804 -0.01533 -0.02155 0.19463  523 TYR B CG    
3464 C  CD1   . TYR A 444 ? 1.03341 1.28538 1.24414 -0.02089 -0.03157 0.18727  523 TYR B CD1   
3465 C  CD2   . TYR A 444 ? 0.77912 1.05314 1.01711 -0.01844 -0.01049 0.19883  523 TYR B CD2   
3466 C  CE1   . TYR A 444 ? 1.03993 1.27657 1.23514 -0.02877 -0.03068 0.18300  523 TYR B CE1   
3467 C  CE2   . TYR A 444 ? 0.88928 1.14655 1.11175 -0.02659 -0.01027 0.19505  523 TYR B CE2   
3468 C  CZ    . TYR A 444 ? 1.02020 1.25890 1.22155 -0.03149 -0.02044 0.18653  523 TYR B CZ    
3469 O  OH    . TYR A 444 ? 1.04198 1.26489 1.22880 -0.03880 -0.02023 0.18218  523 TYR B OH    
3470 N  N     . LEU A 445 ? 0.96460 1.31602 1.29667 -0.00568 -0.02705 0.21494  524 LEU B N     
3471 C  CA    . LEU A 445 ? 0.98224 1.35623 1.33849 0.00425  -0.02568 0.22010  524 LEU B CA    
3472 C  C     . LEU A 445 ? 0.98843 1.38023 1.35840 0.01345  -0.00756 0.22725  524 LEU B C     
3473 O  O     . LEU A 445 ? 0.91986 1.33493 1.31469 0.02131  -0.00436 0.23259  524 LEU B O     
3474 C  CB    . LEU A 445 ? 0.82242 1.21435 1.20913 -0.00555 -0.03787 0.22354  524 LEU B CB    
3475 C  CG    . LEU A 445 ? 0.95521 1.33470 1.33070 -0.01329 -0.05682 0.21716  524 LEU B CG    
3476 C  CD1   . LEU A 445 ? 0.93735 1.33652 1.34480 -0.02272 -0.06853 0.22032  524 LEU B CD1   
3477 C  CD2   . LEU A 445 ? 0.95995 1.32992 1.31805 -0.00161 -0.06256 0.21385  524 LEU B CD2   
3478 N  N     . ASN A 446 ? 1.02633 1.40886 1.38048 0.01331  0.00445  0.22774  525 ASN B N     
3479 C  CA    . ASN A 446 ? 0.99470 1.39582 1.36100 0.02101  0.02233  0.23594  525 ASN B CA    
3480 C  C     . ASN A 446 ? 1.03391 1.44385 1.39708 0.04085  0.02945  0.23450  525 ASN B C     
3481 O  O     . ASN A 446 ? 1.02720 1.42020 1.36925 0.04934  0.02264  0.22584  525 ASN B O     
3482 C  CB    . ASN A 446 ? 1.07219 1.45815 1.41630 0.01838  0.03243  0.23591  525 ASN B CB    
3483 C  CG    . ASN A 446 ? 1.00918 1.36832 1.31457 0.02713  0.03156  0.22550  525 ASN B CG    
3484 O  OD1   . ASN A 446 ? 0.99483 1.35489 1.28771 0.04245  0.04132  0.22393  525 ASN B OD1   
3485 N  ND2   . ASN A 446 ? 0.87307 1.20880 1.15987 0.01768  0.01964  0.21805  525 ASN B ND2   
3486 N  N     . ASP A 447 ? 1.02671 1.46408 1.41252 0.04835  0.04323  0.24336  526 ASP B N     
3487 C  CA    . ASP A 447 ? 0.94871 1.39876 1.33427 0.06872  0.05233  0.24220  526 ASP B CA    
3488 C  C     . ASP A 447 ? 0.98721 1.44015 1.38330 0.07502  0.03925  0.23757  526 ASP B C     
3489 O  O     . ASP A 447 ? 1.04099 1.47927 1.41746 0.08773  0.03534  0.22887  526 ASP B O     
3490 C  CB    . ASP A 447 ? 0.97890 1.40806 1.32698 0.08096  0.05973  0.23419  526 ASP B CB    
3491 C  CG    . ASP A 447 ? 1.07267 1.50376 1.41194 0.07826  0.07469  0.24029  526 ASP B CG    
3492 O  OD1   . ASP A 447 ? 1.02490 1.47313 1.38825 0.06658  0.07967  0.25150  526 ASP B OD1   
3493 O  OD2   . ASP A 447 ? 1.22717 1.64244 1.53617 0.08777  0.08082  0.23418  526 ASP B OD2   
3494 N  N     . ASN A 448 ? 1.04489 1.51695 1.47382 0.06580  0.03170  0.24386  527 ASN B N     
3495 C  CA    . ASN A 448 ? 1.04245 1.52310 1.48787 0.07151  0.01970  0.24198  527 ASN B CA    
3496 C  C     . ASN A 448 ? 1.05479 1.57328 1.54240 0.07390  0.02676  0.25235  527 ASN B C     
3497 O  O     . ASN A 448 ? 1.07723 1.60952 1.59249 0.05969  0.01991  0.25873  527 ASN B O     
3498 C  CB    . ASN A 448 ? 1.04362 1.50814 1.48543 0.05719  -0.00057 0.23818  527 ASN B CB    
3499 C  CG    . ASN A 448 ? 0.93686 1.36764 1.34034 0.05934  -0.00889 0.22810  527 ASN B CG    
3500 O  OD1   . ASN A 448 ? 0.89165 1.31516 1.28815 0.07003  -0.01615 0.22356  527 ASN B OD1   
3501 N  ND2   . ASN A 448 ? 0.98950 1.39973 1.36954 0.04915  -0.00807 0.22506  527 ASN B ND2   
3502 N  N     . PRO A 449 ? 1.03489 1.57174 1.52938 0.09211  0.04025  0.25392  528 PRO B N     
3503 C  CA    . PRO A 449 ? 1.07337 1.64952 1.60894 0.09499  0.05014  0.26512  528 PRO B CA    
3504 C  C     . PRO A 449 ? 1.07188 1.66478 1.63996 0.09333  0.03608  0.26700  528 PRO B C     
3505 O  O     . PRO A 449 ? 0.99931 1.62563 1.60600 0.09245  0.04205  0.27703  528 PRO B O     
3506 C  CB    . PRO A 449 ? 1.13603 1.72384 1.66310 0.11781  0.06743  0.26342  528 PRO B CB    
3507 C  CG    . PRO A 449 ? 0.95971 1.51357 1.44079 0.12291  0.06867  0.25293  528 PRO B CG    
3508 C  CD    . PRO A 449 ? 0.99466 1.51789 1.45939 0.11091  0.04821  0.24546  528 PRO B CD    
3509 N  N     . ASN A 450 ? 1.12598 1.69808 1.68086 0.09290  0.01773  0.25862  529 ASN B N     
3510 C  CA    . ASN A 450 ? 1.09914 1.68573 1.68247 0.09193  0.00286  0.26030  529 ASN B CA    
3511 C  C     . ASN A 450 ? 1.01725 1.59628 1.60749 0.07096  -0.01461 0.26131  529 ASN B C     
3512 O  O     . ASN A 450 ? 0.94831 1.54019 1.56296 0.06826  -0.02842 0.26313  529 ASN B O     
3513 C  CB    . ASN A 450 ? 1.08192 1.65331 1.64899 0.10742  -0.00673 0.25155  529 ASN B CB    
3514 C  CG    . ASN A 450 ? 1.09711 1.67477 1.65724 0.12985  0.00854  0.24819  529 ASN B CG    
3515 O  OD1   . ASN A 450 ? 0.90634 1.51077 1.48454 0.13637  0.02582  0.25432  529 ASN B OD1   
3516 N  ND2   . ASN A 450 ? 1.08852 1.64179 1.62267 0.14207  0.00202  0.23846  529 ASN B ND2   
3517 N  N     . LEU A 451 ? 1.01691 1.57585 1.58630 0.05683  -0.01487 0.25959  530 LEU B N     
3518 C  CA    . LEU A 451 ? 1.02995 1.57951 1.60199 0.03783  -0.03169 0.25843  530 LEU B CA    
3519 C  C     . LEU A 451 ? 1.00495 1.58165 1.61754 0.02545  -0.02906 0.26822  530 LEU B C     
3520 O  O     . LEU A 451 ? 1.05438 1.63018 1.66779 0.01591  -0.01967 0.27235  530 LEU B O     
3521 C  CB    . LEU A 451 ? 0.99653 1.51309 1.52962 0.02914  -0.03322 0.25156  530 LEU B CB    
3522 C  CG    . LEU A 451 ? 0.96584 1.46803 1.49291 0.01233  -0.05188 0.24722  530 LEU B CG    
3523 C  CD1   . LEU A 451 ? 0.92493 1.41962 1.44386 0.01674  -0.06933 0.24231  530 LEU B CD1   
3524 C  CD2   . LEU A 451 ? 0.96431 1.43826 1.45719 0.00409  -0.04964 0.24150  530 LEU B CD2   
3525 N  N     . HIS A 452 ? 0.98052 1.58166 1.62884 0.02545  -0.03812 0.27247  531 HIS B N     
3526 C  CA    . HIS A 452 ? 1.06594 1.69435 1.75801 0.01318  -0.03847 0.28191  531 HIS B CA    
3527 C  C     . HIS A 452 ? 1.02535 1.64540 1.72416 -0.00476 -0.06004 0.27813  531 HIS B C     
3528 O  O     . HIS A 452 ? 1.02790 1.66901 1.76520 -0.01612 -0.06433 0.28473  531 HIS B O     
3529 C  CB    . HIS A 452 ? 0.94314 1.60734 1.67540 0.02400  -0.03493 0.28937  531 HIS B CB    
3530 C  CG    . HIS A 452 ? 1.00497 1.68367 1.73662 0.04176  -0.01238 0.29376  531 HIS B CG    
3531 N  ND1   . HIS A 452 ? 0.92321 1.62637 1.67835 0.04061  0.00671  0.30514  531 HIS B ND1   
3532 C  CD2   . HIS A 452 ? 1.04257 1.71507 1.75281 0.06162  -0.00617 0.28810  531 HIS B CD2   
3533 C  CE1   . HIS A 452 ? 0.99045 1.70298 1.73677 0.05970  0.02424  0.30588  531 HIS B CE1   
3534 N  NE2   . HIS A 452 ? 1.03314 1.72670 1.75258 0.07284  0.01633  0.29482  531 HIS B NE2   
3535 N  N     . SER A 453 ? 1.06244 1.65313 1.72550 -0.00734 -0.07385 0.26769  532 SER B N     
3536 C  CA    . SER A 453 ? 1.08476 1.66749 1.75005 -0.02239 -0.09497 0.26255  532 SER B CA    
3537 C  C     . SER A 453 ? 1.00945 1.55664 1.62754 -0.02641 -0.10088 0.25229  532 SER B C     
3538 O  O     . SER A 453 ? 1.03615 1.56525 1.62129 -0.01612 -0.09242 0.24889  532 SER B O     
3539 C  CB    . SER A 453 ? 1.12104 1.71767 1.80476 -0.01864 -0.11271 0.26189  532 SER B CB    
3540 O  OG    . SER A 453 ? 1.13106 1.71715 1.80908 -0.03151 -0.13394 0.25522  532 SER B OG    
3541 N  N     . LEU A 454 ? 1.08202 1.62004 1.69829 -0.04130 -0.11597 0.24699  533 LEU B N     
3542 C  CA    . LEU A 454 ? 1.02459 1.53205 1.59918 -0.04614 -0.12384 0.23692  533 LEU B CA    
3543 C  C     . LEU A 454 ? 1.00950 1.51590 1.58346 -0.05231 -0.14744 0.23079  533 LEU B C     
3544 O  O     . LEU A 454 ? 1.22550 1.74945 1.83219 -0.06111 -0.15853 0.23215  533 LEU B O     
3545 C  CB    . LEU A 454 ? 1.03051 1.52494 1.59788 -0.05809 -0.11724 0.23497  533 LEU B CB    
3546 C  CG    . LEU A 454 ? 1.07769 1.54498 1.60273 -0.05402 -0.10611 0.23029  533 LEU B CG    
3547 C  CD1   . LEU A 454 ? 0.97302 1.44336 1.49020 -0.03779 -0.08950 0.23509  533 LEU B CD1   
3548 C  CD2   . LEU A 454 ? 1.05165 1.51053 1.57731 -0.06521 -0.09868 0.23043  533 LEU B CD2   
3549 N  N     . PRO A 455 ? 1.03791 1.52495 1.57593 -0.04771 -0.15582 0.22450  534 PRO B N     
3550 C  CA    . PRO A 455 ? 1.06377 1.55132 1.59844 -0.05189 -0.17812 0.21958  534 PRO B CA    
3551 C  C     . PRO A 455 ? 1.12952 1.61218 1.66548 -0.06738 -0.18968 0.21220  534 PRO B C     
3552 O  O     . PRO A 455 ? 1.19198 1.65745 1.70939 -0.07371 -0.18296 0.20750  534 PRO B O     
3553 C  CB    . PRO A 455 ? 1.11038 1.57562 1.60222 -0.04391 -0.18030 0.21596  534 PRO B CB    
3554 C  CG    . PRO A 455 ? 1.05906 1.50606 1.52764 -0.04141 -0.16184 0.21504  534 PRO B CG    
3555 C  CD    . PRO A 455 ? 1.07217 1.53619 1.57115 -0.03883 -0.14558 0.22206  534 PRO B CD    
3556 N  N     . PHE A 456 ? 1.26322 1.76122 1.82222 -0.07297 -0.20810 0.21061  535 PHE B N     
3557 C  CA    . PHE A 456 ? 1.33653 1.83134 1.90061 -0.08712 -0.22153 0.20228  535 PHE B CA    
3558 C  C     . PHE A 456 ? 1.33666 1.80716 1.85541 -0.08933 -0.23019 0.19136  535 PHE B C     
3559 O  O     . PHE A 456 ? 1.39879 1.85891 1.91126 -0.09956 -0.23504 0.18286  535 PHE B O     
3560 C  CB    . PHE A 456 ? 1.44696 1.96476 2.04694 -0.09150 -0.24059 0.20258  535 PHE B CB    
3561 C  CG    . PHE A 456 ? 1.51728 2.06174 2.16692 -0.09130 -0.23267 0.21337  535 PHE B CG    
3562 C  CD1   . PHE A 456 ? 1.50619 2.05272 2.17043 -0.09330 -0.21242 0.22008  535 PHE B CD1   
3563 C  CD2   . PHE A 456 ? 1.52466 2.09339 2.20663 -0.08879 -0.24527 0.21748  535 PHE B CD2   
3564 C  CE1   . PHE A 456 ? 1.49432 2.06773 2.20446 -0.09287 -0.20393 0.23121  535 PHE B CE1   
3565 C  CE2   . PHE A 456 ? 1.53249 2.12798 2.26193 -0.08842 -0.23730 0.22793  535 PHE B CE2   
3566 C  CZ    . PHE A 456 ? 1.53499 2.13337 2.27849 -0.09049 -0.21611 0.23507  535 PHE B CZ    
3567 N  N     . GLU A 457 ? 1.27222 1.73374 1.76010 -0.07971 -0.23208 0.19175  536 GLU B N     
3568 C  CA    . GLU A 457 ? 1.28189 1.72270 1.72651 -0.08101 -0.23910 0.18311  536 GLU B CA    
3569 C  C     . GLU A 457 ? 1.24740 1.66618 1.66466 -0.08189 -0.22279 0.18027  536 GLU B C     
3570 O  O     . GLU A 457 ? 1.20897 1.61080 1.59068 -0.08303 -0.22652 0.17329  536 GLU B O     
3571 C  CB    . GLU A 457 ? 1.18377 1.62294 1.60663 -0.07078 -0.24607 0.18680  536 GLU B CB    
3572 C  CG    . GLU A 457 ? 1.23795 1.69719 1.69045 -0.06229 -0.24790 0.19648  536 GLU B CG    
3573 C  CD    . GLU A 457 ? 1.22588 1.70644 1.70863 -0.06720 -0.26704 0.19519  536 GLU B CD    
3574 O  OE1   . GLU A 457 ? 1.33915 1.81664 1.80994 -0.07464 -0.28289 0.18635  536 GLU B OE1   
3575 O  OE2   . GLU A 457 ? 1.23260 1.73367 1.75144 -0.06313 -0.26648 0.20256  536 GLU B OE2   
3576 N  N     . LEU A 458 ? 1.14499 1.56469 1.57763 -0.08098 -0.20489 0.18579  537 LEU B N     
3577 C  CA    . LEU A 458 ? 1.25484 1.65419 1.66271 -0.08152 -0.18980 0.18335  537 LEU B CA    
3578 C  C     . LEU A 458 ? 1.23462 1.62289 1.63506 -0.09329 -0.19525 0.17332  537 LEU B C     
3579 O  O     . LEU A 458 ? 1.14193 1.51069 1.51368 -0.09389 -0.18765 0.16864  537 LEU B O     
3580 C  CB    . LEU A 458 ? 1.22631 1.63184 1.65384 -0.07738 -0.17022 0.19204  537 LEU B CB    
3581 C  CG    . LEU A 458 ? 0.99320 1.37939 1.39602 -0.07503 -0.15293 0.19144  537 LEU B CG    
3582 C  CD1   . LEU A 458 ? 1.00682 1.37721 1.37403 -0.06521 -0.15040 0.19042  537 LEU B CD1   
3583 C  CD2   . LEU A 458 ? 0.97513 1.37214 1.40150 -0.07152 -0.13526 0.20035  537 LEU B CD2   
3584 N  N     . ALA A 459 ? 1.26191 1.66194 1.68841 -0.10235 -0.20906 0.16937  538 ALA B N     
3585 C  CA    . ALA A 459 ? 1.14926 1.53852 1.57187 -0.11319 -0.21579 0.15870  538 ALA B CA    
3586 C  C     . ALA A 459 ? 1.15884 1.53257 1.54083 -0.11286 -0.22612 0.14725  538 ALA B C     
3587 O  O     . ALA A 459 ? 1.25261 1.61253 1.62170 -0.11917 -0.22758 0.13757  538 ALA B O     
3588 C  CB    . ALA A 459 ? 1.28039 1.68623 1.74290 -0.12259 -0.23032 0.15670  538 ALA B CB    
3589 N  N     . LEU A 460 ? 1.17304 1.54926 1.53507 -0.10534 -0.23307 0.14862  539 LEU B N     
3590 C  CA    . LEU A 460 ? 1.17573 1.53969 1.49828 -0.10429 -0.24164 0.13973  539 LEU B CA    
3591 C  C     . LEU A 460 ? 1.18550 1.52893 1.47506 -0.10141 -0.22652 0.13881  539 LEU B C     
3592 O  O     . LEU A 460 ? 1.27704 1.60990 1.53476 -0.10172 -0.23144 0.13082  539 LEU B O     
3593 C  CB    . LEU A 460 ? 1.20274 1.57590 1.51457 -0.09689 -0.25246 0.14425  539 LEU B CB    
3594 C  CG    . LEU A 460 ? 1.17660 1.56874 1.51215 -0.09978 -0.27263 0.14186  539 LEU B CG    
3595 C  CD1   . LEU A 460 ? 1.06168 1.46659 1.40248 -0.09091 -0.27728 0.15241  539 LEU B CD1   
3596 C  CD2   . LEU A 460 ? 1.01778 1.40622 1.33087 -0.10412 -0.28978 0.12820  539 LEU B CD2   
3597 N  N     . CYS A 461 ? 1.13690 1.47553 1.43317 -0.09825 -0.20854 0.14658  540 CYS B N     
3598 C  CA    . CYS A 461 ? 1.21049 1.52973 1.47891 -0.09605 -0.19441 0.14533  540 CYS B CA    
3599 C  C     . CYS A 461 ? 1.16759 1.47740 1.43828 -0.10494 -0.19300 0.13634  540 CYS B C     
3600 O  O     . CYS A 461 ? 1.19306 1.50431 1.48728 -0.10849 -0.18417 0.13984  540 CYS B O     
3601 C  CB    . CYS A 461 ? 1.18239 1.50055 1.45729 -0.08863 -0.17718 0.15594  540 CYS B CB    
3602 S  SG    . CYS A 461 ? 1.20510 1.53373 1.48229 -0.07720 -0.17912 0.16625  540 CYS B SG    
3603 N  N     . SER A 462 ? 1.19183 1.49227 1.43796 -0.10812 -0.20166 0.12501  541 SER B N     
3604 C  CA    . SER A 462 ? 1.26188 1.55374 1.51198 -0.11639 -0.20392 0.11454  541 SER B CA    
3605 C  C     . SER A 462 ? 1.31020 1.58650 1.55241 -0.11624 -0.18652 0.11640  541 SER B C     
3606 O  O     . SER A 462 ? 1.41879 1.69184 1.68070 -0.12251 -0.18313 0.11510  541 SER B O     
3607 C  CB    . SER A 462 ? 1.36960 1.65651 1.59338 -0.11795 -0.21758 0.10090  541 SER B CB    
3608 O  OG    . SER A 462 ? 1.43863 1.71539 1.62548 -0.11185 -0.21083 0.10113  541 SER B OG    
3609 N  N     . LYS A 463 ? 1.22011 1.48652 1.43465 -0.10930 -0.17603 0.11985  542 LYS B N     
3610 C  CA    . LYS A 463 ? 1.21211 1.46280 1.41485 -0.10859 -0.16115 0.12014  542 LYS B CA    
3611 C  C     . LYS A 463 ? 1.15827 1.41156 1.37885 -0.10503 -0.14631 0.13189  542 LYS B C     
3612 O  O     . LYS A 463 ? 1.17599 1.41691 1.38509 -0.10274 -0.13342 0.13346  542 LYS B O     
3613 C  CB    . LYS A 463 ? 1.21389 1.45278 1.37954 -0.10312 -0.15736 0.11793  542 LYS B CB    
3614 C  CG    . LYS A 463 ? 1.20289 1.44379 1.34806 -0.10404 -0.17119 0.10910  542 LYS B CG    
3615 C  CD    . LYS A 463 ? 1.26193 1.49149 1.37245 -0.09971 -0.16551 0.10778  542 LYS B CD    
3616 C  CE    . LYS A 463 ? 1.27025 1.50668 1.36011 -0.09807 -0.17764 0.10438  542 LYS B CE    
3617 N  NZ    . LYS A 463 ? 1.22757 1.47108 1.32297 -0.10330 -0.19249 0.09251  542 LYS B NZ    
3618 N  N     . LEU A 464 ? 1.14467 1.41464 1.39273 -0.10395 -0.14785 0.13989  543 LEU B N     
3619 C  CA    . LEU A 464 ? 1.15603 1.43163 1.42078 -0.09903 -0.13340 0.15110  543 LEU B CA    
3620 C  C     . LEU A 464 ? 1.14605 1.41970 1.43028 -0.10572 -0.12600 0.15251  543 LEU B C     
3621 O  O     . LEU A 464 ? 1.31807 1.60378 1.63331 -0.11260 -0.13160 0.15433  543 LEU B O     
3622 C  CB    . LEU A 464 ? 1.11641 1.41248 1.40604 -0.09547 -0.13770 0.15890  543 LEU B CB    
3623 C  CG    . LEU A 464 ? 1.05692 1.36252 1.36485 -0.08870 -0.12289 0.17027  543 LEU B CG    
3624 C  CD1   . LEU A 464 ? 1.02796 1.31998 1.30855 -0.07880 -0.11049 0.17215  543 LEU B CD1   
3625 C  CD2   . LEU A 464 ? 0.96027 1.28743 1.29389 -0.08494 -0.12867 0.17687  543 LEU B CD2   
3626 N  N     . SER A 465 ? 1.10745 1.36596 1.37472 -0.10384 -0.11374 0.15243  544 SER B N     
3627 C  CA    . SER A 465 ? 1.11301 1.36737 1.39522 -0.10969 -0.10615 0.15472  544 SER B CA    
3628 C  C     . SER A 465 ? 1.12955 1.39048 1.42289 -0.10362 -0.08933 0.16711  544 SER B C     
3629 O  O     . SER A 465 ? 1.23877 1.51070 1.56155 -0.10812 -0.08512 0.17482  544 SER B O     
3630 C  CB    . SER A 465 ? 1.20252 1.43554 1.45880 -0.11204 -0.10488 0.14562  544 SER B CB    
3631 O  OG    . SER A 465 ? 1.26549 1.48768 1.49227 -0.10335 -0.09576 0.14600  544 SER B OG    
3632 N  N     . ILE A 466 ? 1.06571 1.32063 1.33642 -0.09325 -0.07981 0.16926  545 ILE B N     
3633 C  CA    . ILE A 466 ? 1.08130 1.34108 1.35669 -0.08542 -0.06367 0.17909  545 ILE B CA    
3634 C  C     . ILE A 466 ? 1.03693 1.31548 1.32740 -0.07764 -0.06282 0.18587  545 ILE B C     
3635 O  O     . ILE A 466 ? 1.00005 1.27860 1.27969 -0.07329 -0.07094 0.18238  545 ILE B O     
3636 C  CB    . ILE A 466 ? 0.97024 1.21146 1.21263 -0.07798 -0.05470 0.17607  545 ILE B CB    
3637 C  CG1   . ILE A 466 ? 0.97672 1.20091 1.20749 -0.08519 -0.05448 0.17026  545 ILE B CG1   
3638 C  CG2   . ILE A 466 ? 0.94737 1.19458 1.19166 -0.06764 -0.03931 0.18483  545 ILE B CG2   
3639 C  CD1   . ILE A 466 ? 1.12527 1.33184 1.32597 -0.07848 -0.04606 0.16742  545 ILE B CD1   
3640 N  N     . MET A 467 ? 0.87812 1.17339 1.19420 -0.07558 -0.05289 0.19617  546 MET B N     
3641 C  CA    . MET A 467 ? 0.84142 1.15645 1.17437 -0.06702 -0.05042 0.20291  546 MET B CA    
3642 C  C     . MET A 467 ? 0.95355 1.28310 1.30507 -0.06246 -0.03389 0.21419  546 MET B C     
3643 O  O     . MET A 467 ? 1.14389 1.47678 1.51201 -0.07079 -0.02951 0.21939  546 MET B O     
3644 C  CB    . MET A 467 ? 0.91474 1.24565 1.27380 -0.07364 -0.06503 0.20276  546 MET B CB    
3645 C  CG    . MET A 467 ? 0.93292 1.28645 1.31406 -0.06514 -0.06311 0.21019  546 MET B CG    
3646 S  SD    . MET A 467 ? 1.21899 1.58922 1.62714 -0.07243 -0.08296 0.20862  546 MET B SD    
3647 C  CE    . MET A 467 ? 1.17363 1.54699 1.60853 -0.08922 -0.08737 0.20918  546 MET B CE    
3648 N  N     . SER A 468 ? 0.95314 1.29128 1.30161 -0.04882 -0.02487 0.21807  547 SER B N     
3649 C  CA    . SER A 468 ? 1.07311 1.42800 1.43671 -0.04162 -0.00817 0.22864  547 SER B CA    
3650 C  C     . SER A 468 ? 0.94405 1.32453 1.33399 -0.03438 -0.00799 0.23444  547 SER B C     
3651 O  O     . SER A 468 ? 0.95527 1.33406 1.33679 -0.02690 -0.01545 0.22935  547 SER B O     
3652 C  CB    . SER A 468 ? 1.00213 1.34351 1.33489 -0.02934 0.00429  0.22664  547 SER B CB    
3653 O  OG    . SER A 468 ? 0.97138 1.30737 1.28715 -0.01745 0.00085  0.22062  547 SER B OG    
3654 N  N     . ILE A 469 ? 1.00825 1.41287 1.43137 -0.03663 0.00042  0.24580  548 ILE B N     
3655 C  CA    . ILE A 469 ? 1.00540 1.43760 1.45836 -0.03031 0.00112  0.25216  548 ILE B CA    
3656 C  C     . ILE A 469 ? 0.95764 1.41210 1.42699 -0.02200 0.02093  0.26426  548 ILE B C     
3657 O  O     . ILE A 469 ? 1.03514 1.51761 1.53700 -0.01881 0.02429  0.27244  548 ILE B O     
3658 C  CB    . ILE A 469 ? 1.03813 1.48381 1.52521 -0.04393 -0.01338 0.25414  548 ILE B CB    
3659 C  CG1   . ILE A 469 ? 1.06451 1.51484 1.57423 -0.05832 -0.01017 0.26172  548 ILE B CG1   
3660 C  CG2   . ILE A 469 ? 0.94939 1.37636 1.41867 -0.04969 -0.03314 0.24197  548 ILE B CG2   
3661 C  CD1   . ILE A 469 ? 1.05991 1.54335 1.61487 -0.05995 -0.00209 0.27620  548 ILE B CD1   
3662 N  N     . GLU A 470 ? 0.98675 1.43040 1.43406 -0.01803 0.03427  0.26585  549 GLU B N     
3663 C  CA    . GLU A 470 ? 1.07594 1.54128 1.53514 -0.00925 0.05401  0.27780  549 GLU B CA    
3664 C  C     . GLU A 470 ? 1.04736 1.52793 1.50548 0.00978  0.06057  0.27659  549 GLU B C     
3665 O  O     . GLU A 470 ? 1.15351 1.61730 1.58528 0.01946  0.05447  0.26526  549 GLU B O     
3666 C  CB    . GLU A 470 ? 1.02330 1.47199 1.45411 -0.00737 0.06569  0.27862  549 GLU B CB    
3667 C  CG    . GLU A 470 ? 1.04641 1.46364 1.43344 -0.00124 0.06035  0.26439  549 GLU B CG    
3668 C  CD    . GLU A 470 ? 1.09535 1.48693 1.46993 -0.01644 0.04719  0.25722  549 GLU B CD    
3669 O  OE1   . GLU A 470 ? 1.17640 1.57339 1.57620 -0.03093 0.03806  0.26017  549 GLU B OE1   
3670 O  OE2   . GLU A 470 ? 1.16415 1.53065 1.50450 -0.01357 0.04571  0.24823  549 GLU B OE2   
3671 N  N     . ASN A 471 ? 1.07403 1.58717 1.56285 0.01507  0.07287  0.28869  550 ASN B N     
3672 C  CA    . ASN A 471 ? 0.92512 1.45858 1.42067 0.03341  0.07980  0.28867  550 ASN B CA    
3673 C  C     . ASN A 471 ? 0.86720 1.40268 1.37582 0.03379  0.06284  0.28189  550 ASN B C     
3674 O  O     . ASN A 471 ? 0.85146 1.38776 1.35067 0.04955  0.06232  0.27543  550 ASN B O     
3675 C  CB    . ASN A 471 ? 0.99281 1.51203 1.44950 0.05172  0.08934  0.28062  550 ASN B CB    
3676 C  CG    . ASN A 471 ? 1.09918 1.61880 1.54181 0.05349  0.10656  0.28782  550 ASN B CG    
3677 O  OD1   . ASN A 471 ? 1.06804 1.61362 1.53616 0.05075  0.11950  0.30239  550 ASN B OD1   
3678 N  ND2   . ASN A 471 ? 1.11432 1.60562 1.51700 0.05789  0.10655  0.27842  550 ASN B ND2   
3679 N  N     . CYS A 472 ? 1.01818 1.55402 1.54843 0.01691  0.04812  0.28308  551 CYS B N     
3680 C  CA    . CYS A 472 ? 1.03232 1.57540 1.58079 0.01601  0.03195  0.27925  551 CYS B CA    
3681 C  C     . CYS A 472 ? 1.03089 1.60762 1.62915 0.00839  0.03246  0.29132  551 CYS B C     
3682 O  O     . CYS A 472 ? 1.13309 1.71333 1.74964 -0.00728 0.03219  0.29830  551 CYS B O     
3683 C  CB    . CYS A 472 ? 1.07207 1.58759 1.60263 0.00344  0.01174  0.26898  551 CYS B CB    
3684 S  SG    . CYS A 472 ? 1.18969 1.66790 1.66670 0.01223  0.00783  0.25498  551 CYS B SG    
3685 N  N     . PRO A 473 ? 0.94852 1.55029 1.57140 0.01885  0.03268  0.29418  552 PRO B N     
3686 C  CA    . PRO A 473 ? 0.87154 1.50817 1.54522 0.01193  0.03378  0.30651  552 PRO B CA    
3687 C  C     . PRO A 473 ? 1.02165 1.65381 1.71567 -0.00856 0.01437  0.30578  552 PRO B C     
3688 O  O     . PRO A 473 ? 0.97751 1.61851 1.69569 -0.02275 0.01708  0.31480  552 PRO B O     
3689 C  CB    . PRO A 473 ? 0.93243 1.58983 1.62140 0.02833  0.03296  0.30545  552 PRO B CB    
3690 C  CG    . PRO A 473 ? 0.95001 1.58936 1.59828 0.04683  0.04076  0.29636  552 PRO B CG    
3691 C  CD    . PRO A 473 ? 0.97703 1.57713 1.58426 0.03824  0.03260  0.28669  552 PRO B CD    
3692 N  N     . LEU A 474 ? 1.08501 1.70303 1.76899 -0.01000 -0.00566 0.29511  553 LEU B N     
3693 C  CA    . LEU A 474 ? 1.08642 1.70052 1.78712 -0.02743 -0.02632 0.29217  553 LEU B CA    
3694 C  C     . LEU A 474 ? 1.11904 1.76802 1.87529 -0.03543 -0.02716 0.30401  553 LEU B C     
3695 O  O     . LEU A 474 ? 1.15333 1.80364 1.93126 -0.05248 -0.03412 0.30733  553 LEU B O     
3696 C  CB    . LEU A 474 ? 1.04444 1.63053 1.72198 -0.04171 -0.03026 0.28719  553 LEU B CB    
3697 C  CG    . LEU A 474 ? 1.05684 1.60790 1.68144 -0.03634 -0.03180 0.27514  553 LEU B CG    
3698 C  CD1   . LEU A 474 ? 1.02982 1.55864 1.63652 -0.04862 -0.03010 0.27291  553 LEU B CD1   
3699 C  CD2   . LEU A 474 ? 1.10337 1.64129 1.71272 -0.03594 -0.05228 0.26429  553 LEU B CD2   
3700 N  N     . SER A 475 ? 0.95212 1.62982 1.73309 -0.02267 -0.02038 0.31024  554 SER B N     
3701 C  CA    . SER A 475 ? 0.95623 1.67100 1.79264 -0.02855 -0.01849 0.32304  554 SER B CA    
3702 C  C     . SER A 475 ? 1.06192 1.78161 1.92516 -0.04083 -0.04332 0.31930  554 SER B C     
3703 O  O     . SER A 475 ? 1.04502 1.78836 1.95416 -0.05253 -0.04614 0.32867  554 SER B O     
3704 C  CB    . SER A 475 ? 0.96546 1.71078 1.81986 -0.00970 -0.00339 0.33008  554 SER B CB    
3705 O  OG    . SER A 475 ? 1.11126 1.85326 1.95597 0.00237  -0.01564 0.32089  554 SER B OG    
3706 N  N     . HIS A 476 ? 1.09415 1.79285 1.93057 -0.03839 -0.06165 0.30633  555 HIS B N     
3707 C  CA    . HIS A 476 ? 0.98752 1.68940 1.84455 -0.04948 -0.08648 0.30167  555 HIS B CA    
3708 C  C     . HIS A 476 ? 1.04921 1.73528 1.90759 -0.06964 -0.09751 0.29822  555 HIS B C     
3709 O  O     . HIS A 476 ? 1.08383 1.77996 1.97264 -0.08143 -0.11559 0.29729  555 HIS B O     
3710 C  CB    . HIS A 476 ? 0.93509 1.61861 1.75978 -0.04066 -0.10224 0.28987  555 HIS B CB    
3711 C  CG    . HIS A 476 ? 0.97371 1.67218 1.80145 -0.02110 -0.09551 0.29231  555 HIS B CG    
3712 N  ND1   . HIS A 476 ? 0.95362 1.68122 1.80990 -0.01116 -0.07642 0.30302  555 HIS B ND1   
3713 C  CD2   . HIS A 476 ? 0.96264 1.65103 1.76903 -0.00919 -0.10553 0.28552  555 HIS B CD2   
3714 C  CE1   . HIS A 476 ? 0.93253 1.66679 1.78478 0.00662  -0.07533 0.30132  555 HIS B CE1   
3715 N  NE2   . HIS A 476 ? 0.95118 1.66122 1.77403 0.00781  -0.09319 0.29114  555 HIS B NE2   
3716 N  N     . LEU A 477 ? 1.09912 1.76058 1.92590 -0.07333 -0.08790 0.29566  556 LEU B N     
3717 C  CA    . LEU A 477 ? 1.18954 1.83516 2.01729 -0.09106 -0.09483 0.29307  556 LEU B CA    
3718 C  C     . LEU A 477 ? 1.29803 1.96479 2.16582 -0.09923 -0.08012 0.30846  556 LEU B C     
3719 O  O     . LEU A 477 ? 1.14084 1.82695 2.01844 -0.08901 -0.05910 0.32001  556 LEU B O     
3720 C  CB    . LEU A 477 ? 1.15154 1.76084 1.92588 -0.08984 -0.09092 0.28342  556 LEU B CB    
3721 C  CG    . LEU A 477 ? 1.21485 1.80249 1.94597 -0.08058 -0.10160 0.27033  556 LEU B CG    
3722 C  CD1   . LEU A 477 ? 1.17015 1.72391 1.85318 -0.08099 -0.09703 0.26193  556 LEU B CD1   
3723 C  CD2   . LEU A 477 ? 1.24638 1.83462 1.98667 -0.08783 -0.12744 0.26205  556 LEU B CD2   
3724 N  N     . PRO A 478 ? 1.34646 2.01069 2.23872 -0.11727 -0.09090 0.30922  557 PRO B N     
3725 C  CA    . PRO A 478 ? 1.31768 2.00300 2.25264 -0.12639 -0.07813 0.32580  557 PRO B CA    
3726 C  C     . PRO A 478 ? 1.32656 2.00184 2.23654 -0.12135 -0.05412 0.33310  557 PRO B C     
3727 O  O     . PRO A 478 ? 1.35073 1.99447 2.21311 -0.11850 -0.05322 0.32275  557 PRO B O     
3728 C  CB    . PRO A 478 ? 1.30101 1.97553 2.25752 -0.14671 -0.09855 0.32083  557 PRO B CB    
3729 C  CG    . PRO A 478 ? 1.26155 1.92384 2.20144 -0.14641 -0.12350 0.30367  557 PRO B CG    
3730 C  CD    . PRO A 478 ? 1.26037 1.90523 2.14665 -0.12976 -0.11666 0.29527  557 PRO B CD    
3731 N  N     . PRO A 479 ? 1.32461 2.02720 2.26537 -0.11970 -0.03402 0.35134  558 PRO B N     
3732 C  CA    . PRO A 479 ? 1.28927 1.98386 2.20582 -0.11442 -0.01095 0.35928  558 PRO B CA    
3733 C  C     . PRO A 479 ? 1.35432 2.02171 2.26032 -0.12945 -0.01504 0.35768  558 PRO B C     
3734 O  O     . PRO A 479 ? 1.40793 2.05498 2.27583 -0.12422 -0.00278 0.35637  558 PRO B O     
3735 C  CB    . PRO A 479 ? 1.13445 1.86966 2.09480 -0.11142 0.00892  0.38072  558 PRO B CB    
3736 C  CG    . PRO A 479 ? 1.12590 1.88925 2.12191 -0.10821 -0.00115 0.38089  558 PRO B CG    
3737 C  CD    . PRO A 479 ? 1.22402 1.96790 2.22104 -0.12064 -0.03037 0.36585  558 PRO B CD    
3738 N  N     . GLN A 480 ? 1.49012 2.15616 2.42946 -0.14764 -0.03280 0.35714  559 GLN B N     
3739 C  CA    . GLN A 480 ? 1.49068 2.12981 2.42221 -0.16179 -0.03836 0.35455  559 GLN B CA    
3740 C  C     . GLN A 480 ? 1.47923 2.08009 2.35863 -0.15989 -0.05193 0.33291  559 GLN B C     
3741 O  O     . GLN A 480 ? 1.40681 1.98194 2.26041 -0.16371 -0.04861 0.32979  559 GLN B O     
3742 C  CB    . GLN A 480 ? 1.52437 2.17322 2.50946 -0.18139 -0.05470 0.35940  559 GLN B CB    
3743 C  CG    . GLN A 480 ? 1.52553 2.18243 2.52983 -0.18455 -0.07874 0.34783  559 GLN B CG    
3744 C  CD    . GLN A 480 ? 1.59410 2.22650 2.60098 -0.20003 -0.10472 0.33303  559 GLN B CD    
3745 O  OE1   . GLN A 480 ? 1.61783 2.22110 2.59898 -0.20528 -0.10581 0.32659  559 GLN B OE1   
3746 N  NE2   . GLN A 480 ? 1.54511 2.18960 2.58319 -0.20677 -0.12634 0.32692  559 GLN B NE2   
3747 N  N     . ILE A 481 ? 1.49587 2.09331 2.35974 -0.15385 -0.06700 0.31864  560 ILE B N     
3748 C  CA    . ILE A 481 ? 1.44929 2.01311 2.26399 -0.15156 -0.07920 0.29926  560 ILE B CA    
3749 C  C     . ILE A 481 ? 1.47664 2.02627 2.24311 -0.13619 -0.06162 0.29751  560 ILE B C     
3750 O  O     . ILE A 481 ? 1.40476 1.92531 2.13372 -0.13689 -0.06194 0.28842  560 ILE B O     
3751 C  CB    . ILE A 481 ? 1.39257 1.95878 2.20652 -0.15000 -0.10086 0.28640  560 ILE B CB    
3752 C  CG1   . ILE A 481 ? 1.41602 1.99398 2.27664 -0.16582 -0.12054 0.28621  560 ILE B CG1   
3753 C  CG2   . ILE A 481 ? 1.46715 2.00112 2.22890 -0.14655 -0.11162 0.26799  560 ILE B CG2   
3754 C  CD1   . ILE A 481 ? 1.40650 1.96091 2.26687 -0.18088 -0.13126 0.27928  560 ILE B CD1   
3755 N  N     . VAL A 482 ? 1.41358 1.98367 2.18117 -0.12170 -0.04648 0.30560  561 VAL B N     
3756 C  CA    . VAL A 482 ? 1.41215 1.96937 2.13564 -0.10622 -0.03087 0.30311  561 VAL B CA    
3757 C  C     . VAL A 482 ? 1.44790 2.00071 2.16472 -0.10692 -0.01144 0.31360  561 VAL B C     
3758 O  O     . VAL A 482 ? 1.40189 1.93539 2.07728 -0.09770 -0.00193 0.30876  561 VAL B O     
3759 C  CB    . VAL A 482 ? 1.18513 1.76499 1.91212 -0.08931 -0.02214 0.30684  561 VAL B CB    
3760 C  CG1   . VAL A 482 ? 1.19738 1.78106 1.93099 -0.08856 -0.04227 0.29738  561 VAL B CG1   
3761 C  CG2   . VAL A 482 ? 1.21626 1.83169 1.98589 -0.08784 -0.00581 0.32538  561 VAL B CG2   
3762 N  N     . ALA A 483 ? 1.31292 1.88321 2.07024 -0.11783 -0.00577 0.32848  562 ALA B N     
3763 C  CA    . ALA A 483 ? 1.32659 1.89349 2.07857 -0.11889 0.01247  0.34036  562 ALA B CA    
3764 C  C     . ALA A 483 ? 1.37465 1.90590 2.09868 -0.12800 0.00459  0.33071  562 ALA B C     
3765 O  O     . ALA A 483 ? 1.35597 1.87466 2.05486 -0.12385 0.01844  0.33454  562 ALA B O     
3766 C  CB    . ALA A 483 ? 1.31844 1.91464 2.12420 -0.12895 0.02027  0.36079  562 ALA B CB    
3767 N  N     . GLY A 484 ? 1.36820 1.88355 2.09580 -0.13960 -0.01763 0.31784  563 GLY B N     
3768 C  CA    . GLY A 484 ? 1.35014 1.83273 2.05329 -0.14791 -0.02640 0.30726  563 GLY B CA    
3769 C  C     . GLY A 484 ? 1.43644 1.89409 2.08390 -0.13600 -0.02161 0.29535  563 GLY B C     
3770 O  O     . GLY A 484 ? 1.46989 1.91979 2.09695 -0.13043 -0.00567 0.30128  563 GLY B O     
3771 N  N     . GLY A 485 ? 1.47665 1.92217 2.09972 -0.13205 -0.03558 0.27913  564 GLY B N     
3772 C  CA    . GLY A 485 ? 1.52463 1.94694 2.09757 -0.12168 -0.03284 0.26775  564 GLY B CA    
3773 C  C     . GLY A 485 ? 1.55851 1.97099 2.11214 -0.11974 -0.05039 0.25196  564 GLY B C     
3774 O  O     . GLY A 485 ? 1.43637 1.86501 2.01265 -0.12139 -0.06156 0.25113  564 GLY B O     
3775 N  N     . PRO A 486 ? 1.70489 2.09146 2.21636 -0.11604 -0.05310 0.23981  565 PRO B N     
3776 C  CA    . PRO A 486 ? 1.64994 2.02727 2.14075 -0.11415 -0.06918 0.22594  565 PRO B CA    
3777 C  C     . PRO A 486 ? 1.65013 2.02712 2.15992 -0.12711 -0.08955 0.21820  565 PRO B C     
3778 O  O     . PRO A 486 ? 1.62107 2.00933 2.14068 -0.12663 -0.10233 0.21460  565 PRO B O     
3779 C  CB    . PRO A 486 ? 1.60635 1.95639 2.05148 -0.10925 -0.06560 0.21668  565 PRO B CB    
3780 C  CG    . PRO A 486 ? 1.64256 1.99149 2.08247 -0.10383 -0.04578 0.22641  565 PRO B CG    
3781 C  CD    . PRO A 486 ? 1.65221 2.01841 2.13303 -0.11261 -0.04127 0.23902  565 PRO B CD    
3782 N  N     . SER A 487 ? 1.61628 1.98044 2.13203 -0.13830 -0.09364 0.21524  566 SER B N     
3783 C  CA    . SER A 487 ? 1.60501 1.96593 2.13604 -0.15000 -0.11438 0.20521  566 SER B CA    
3784 C  C     . SER A 487 ? 1.56757 1.95423 2.14613 -0.15632 -0.12210 0.21282  566 SER B C     
3785 O  O     . SER A 487 ? 1.62147 2.01055 2.21135 -0.16255 -0.14165 0.20354  566 SER B O     
3786 C  CB    . SER A 487 ? 1.53145 1.87298 2.06214 -0.15992 -0.11632 0.20102  566 SER B CB    
3787 O  OG    . SER A 487 ? 1.52679 1.86338 2.07007 -0.17017 -0.13743 0.18899  566 SER B OG    
3788 N  N     . PHE A 488 ? 1.49518 1.90234 2.10208 -0.15449 -0.10724 0.22954  567 PHE B N     
3789 C  CA    . PHE A 488 ? 1.45577 1.88998 2.11116 -0.16042 -0.11335 0.23824  567 PHE B CA    
3790 C  C     . PHE A 488 ? 1.48677 1.93455 2.14082 -0.15319 -0.12377 0.23333  567 PHE B C     
3791 O  O     . PHE A 488 ? 1.46982 1.92752 2.14899 -0.16039 -0.14191 0.22886  567 PHE B O     
3792 C  CB    . PHE A 488 ? 1.41314 1.86832 2.09641 -0.15835 -0.09266 0.25824  567 PHE B CB    
3793 C  CG    . PHE A 488 ? 1.35643 1.81572 2.07874 -0.17283 -0.09269 0.26799  567 PHE B CG    
3794 C  CD1   . PHE A 488 ? 1.21016 1.64972 1.91968 -0.17721 -0.08476 0.27001  567 PHE B CD1   
3795 C  CD2   . PHE A 488 ? 1.31594 1.79874 2.08950 -0.18227 -0.10133 0.27567  567 PHE B CD2   
3796 C  CE1   . PHE A 488 ? 1.28699 1.72926 2.03391 -0.19081 -0.08537 0.28011  567 PHE B CE1   
3797 C  CE2   . PHE A 488 ? 1.13937 1.62550 1.95169 -0.19640 -0.10200 0.28569  567 PHE B CE2   
3798 C  CZ    . PHE A 488 ? 1.22928 1.69465 2.02819 -0.20071 -0.09399 0.28822  567 PHE B CZ    
3799 N  N     . ILE A 489 ? 1.53906 1.98701 2.16458 -0.13873 -0.11338 0.23402  568 ILE B N     
3800 C  CA    . ILE A 489 ? 1.57835 2.03642 2.19951 -0.13101 -0.12354 0.22958  568 ILE B CA    
3801 C  C     . ILE A 489 ? 1.62840 2.06638 2.21779 -0.13288 -0.14204 0.21289  568 ILE B C     
3802 O  O     . ILE A 489 ? 1.57926 2.02577 2.17173 -0.13107 -0.15689 0.20811  568 ILE B O     
3803 C  CB    . ILE A 489 ? 1.55403 2.01767 2.15675 -0.11461 -0.10692 0.23578  568 ILE B CB    
3804 C  CG1   . ILE A 489 ? 1.46875 1.95050 2.09648 -0.11180 -0.08615 0.25158  568 ILE B CG1   
3805 C  CG2   . ILE A 489 ? 1.62430 2.10315 2.23320 -0.10668 -0.11663 0.23466  568 ILE B CG2   
3806 C  CD1   . ILE A 489 ? 1.35541 1.84428 1.96724 -0.09458 -0.06992 0.25670  568 ILE B CD1   
3807 N  N     . ILE A 490 ? 1.63192 2.04444 2.19095 -0.13614 -0.14146 0.20423  569 ILE B N     
3808 C  CA    . ILE A 490 ? 1.67218 2.06701 2.20088 -0.13793 -0.15801 0.18841  569 ILE B CA    
3809 C  C     . ILE A 490 ? 1.66812 2.07067 2.22347 -0.14875 -0.17981 0.18128  569 ILE B C     
3810 O  O     . ILE A 490 ? 1.66170 2.06645 2.20684 -0.14696 -0.19592 0.17281  569 ILE B O     
3811 C  CB    . ILE A 490 ? 1.71625 2.08438 2.21228 -0.13970 -0.15211 0.18107  569 ILE B CB    
3812 C  CG1   . ILE A 490 ? 1.77200 2.12957 2.23142 -0.12733 -0.13669 0.18332  569 ILE B CG1   
3813 C  CG2   . ILE A 490 ? 1.71382 2.06715 2.19093 -0.14547 -0.17088 0.16450  569 ILE B CG2   
3814 C  CD1   . ILE A 490 ? 1.66418 1.99768 2.09476 -0.12834 -0.12864 0.17812  569 ILE B CD1   
3815 N  N     . GLN A 491 ? 1.61690 2.02374 2.20740 -0.16009 -0.18125 0.18492  570 GLN B N     
3816 C  CA    . GLN A 491 ? 1.61748 2.03147 2.23732 -0.17086 -0.20306 0.17774  570 GLN B CA    
3817 C  C     . GLN A 491 ? 1.53747 1.97985 2.19241 -0.16955 -0.20952 0.18557  570 GLN B C     
3818 O  O     . GLN A 491 ? 1.44864 1.89744 2.11502 -0.17371 -0.23066 0.17688  570 GLN B O     
3819 C  CB    . GLN A 491 ? 1.61532 2.02406 2.26504 -0.18390 -0.20329 0.17995  570 GLN B CB    
3820 C  CG    . GLN A 491 ? 1.65538 2.04366 2.29358 -0.19201 -0.22181 0.16196  570 GLN B CG    
3821 C  CD    . GLN A 491 ? 1.65992 2.02317 2.24505 -0.18533 -0.21696 0.15096  570 GLN B CD    
3822 O  OE1   . GLN A 491 ? 1.61922 1.97362 2.18560 -0.18013 -0.19768 0.15816  570 GLN B OE1   
3823 N  NE2   . GLN A 491 ? 1.63911 1.99198 2.19982 -0.18507 -0.23454 0.13346  570 GLN B NE2   
3824 N  N     . PHE A 492 ? 1.50800 1.96820 2.17990 -0.16307 -0.19198 0.20134  571 PHE B N     
3825 C  CA    . PHE A 492 ? 1.51945 2.00874 2.22859 -0.16139 -0.19671 0.20976  571 PHE B CA    
3826 C  C     . PHE A 492 ? 1.56066 2.05267 2.24777 -0.15221 -0.20933 0.20225  571 PHE B C     
3827 O  O     . PHE A 492 ? 1.54107 2.05074 2.25462 -0.15456 -0.22541 0.20133  571 PHE B O     
3828 C  CB    . PHE A 492 ? 1.54960 2.05733 2.27793 -0.15456 -0.17324 0.22768  571 PHE B CB    
3829 C  CG    . PHE A 492 ? 1.59571 2.13463 2.36016 -0.15028 -0.17559 0.23670  571 PHE B CG    
3830 C  CD1   . PHE A 492 ? 1.54854 2.10678 2.36135 -0.16130 -0.18981 0.23932  571 PHE B CD1   
3831 C  CD2   . PHE A 492 ? 1.57824 2.12718 2.33005 -0.13503 -0.16407 0.24232  571 PHE B CD2   
3832 C  CE1   . PHE A 492 ? 1.44588 2.03414 2.29374 -0.15717 -0.19208 0.24778  571 PHE B CE1   
3833 C  CE2   . PHE A 492 ? 1.52363 2.10177 2.30967 -0.13024 -0.16622 0.25030  571 PHE B CE2   
3834 C  CZ    . PHE A 492 ? 1.40285 2.00136 2.23705 -0.14132 -0.17994 0.25330  571 PHE B CZ    
3835 N  N     . LEU A 493 ? 1.67874 2.15364 2.31863 -0.14190 -0.20285 0.19749  572 LEU B N     
3836 C  CA    . LEU A 493 ? 1.75622 2.23269 2.37411 -0.13310 -0.21423 0.19218  572 LEU B CA    
3837 C  C     . LEU A 493 ? 1.76777 2.23518 2.37256 -0.13964 -0.23822 0.17709  572 LEU B C     
3838 O  O     . LEU A 493 ? 1.69482 2.17091 2.29622 -0.13552 -0.25307 0.17387  572 LEU B O     
3839 C  CB    . LEU A 493 ? 1.63581 2.09628 2.20935 -0.12083 -0.20035 0.19256  572 LEU B CB    
3840 C  CG    . LEU A 493 ? 1.58929 2.05896 2.17043 -0.11102 -0.17805 0.20565  572 LEU B CG    
3841 C  CD1   . LEU A 493 ? 1.61119 2.06260 2.14779 -0.09933 -0.16813 0.20372  572 LEU B CD1   
3842 C  CD2   . LEU A 493 ? 1.49675 1.99516 2.11450 -0.10594 -0.18007 0.21492  572 LEU B CD2   
3843 N  N     . LYS A 494 ? 1.57501 2.02535 2.17191 -0.14907 -0.24267 0.16751  573 LYS B N     
3844 C  CA    . LYS A 494 ? 1.51227 1.95465 2.09684 -0.15461 -0.26570 0.15159  573 LYS B CA    
3845 C  C     . LYS A 494 ? 1.60177 2.06444 2.22978 -0.16217 -0.28525 0.15040  573 LYS B C     
3846 O  O     . LYS A 494 ? 1.56154 2.02551 2.18019 -0.16247 -0.30633 0.13924  573 LYS B O     
3847 C  CB    . LYS A 494 ? 1.31392 1.73340 1.88267 -0.16218 -0.26543 0.14106  573 LYS B CB    
3848 C  CG    . LYS A 494 ? 1.31826 1.71645 1.84122 -0.15516 -0.24961 0.13952  573 LYS B CG    
3849 C  CD    . LYS A 494 ? 1.36965 1.74647 1.87993 -0.16255 -0.25123 0.12827  573 LYS B CD    
3850 C  CE    . LYS A 494 ? 1.26437 1.62094 1.73032 -0.15565 -0.23623 0.12650  573 LYS B CE    
3851 N  NZ    . LYS A 494 ? 1.25264 1.58892 1.70758 -0.16218 -0.23771 0.11548  573 LYS B NZ    
3852 N  N     . MET A 495 ? 1.60557 2.08510 2.28134 -0.16815 -0.27881 0.16207  574 MET B N     
3853 C  CA    . MET A 495 ? 1.52597 2.02550 2.24830 -0.17661 -0.29740 0.16167  574 MET B CA    
3854 C  C     . MET A 495 ? 1.53521 2.05434 2.26178 -0.16834 -0.30785 0.16408  574 MET B C     
3855 O  O     . MET A 495 ? 1.62191 2.14423 2.34769 -0.17032 -0.33131 0.15313  574 MET B O     
3856 C  CB    . MET A 495 ? 1.47752 1.99243 2.25101 -0.18456 -0.28533 0.17644  574 MET B CB    
3857 C  CG    . MET A 495 ? 1.53585 2.03228 2.30383 -0.19053 -0.27008 0.17860  574 MET B CG    
3858 S  SD    . MET A 495 ? 1.69681 2.16496 2.44595 -0.20072 -0.28888 0.15768  574 MET B SD    
3859 C  CE    . MET A 495 ? 1.39941 1.85006 2.14682 -0.20541 -0.26624 0.16585  574 MET B CE    
3860 N  N     . GLN A 496 ? 1.50934 2.04167 2.23989 -0.15830 -0.29121 0.17799  575 GLN B N     
3861 C  CA    . GLN A 496 ? 1.60604 2.15753 2.34359 -0.14938 -0.29958 0.18203  575 GLN B CA    
3862 C  C     . GLN A 496 ? 1.60379 2.13893 2.28705 -0.13868 -0.30264 0.17503  575 GLN B C     
3863 O  O     . GLN A 496 ? 1.58828 2.11845 2.24840 -0.12783 -0.28619 0.18196  575 GLN B O     
3864 C  CB    . GLN A 496 ? 1.58664 2.15980 2.35407 -0.14254 -0.28062 0.19932  575 GLN B CB    
3865 C  CG    . GLN A 496 ? 1.63205 2.22331 2.45367 -0.15301 -0.27451 0.20905  575 GLN B CG    
3866 C  CD    . GLN A 496 ? 1.74328 2.35226 2.60782 -0.16328 -0.29851 0.20535  575 GLN B CD    
3867 O  OE1   . GLN A 496 ? 1.78294 2.40076 2.64615 -0.15902 -0.31659 0.20023  575 GLN B OE1   
3868 N  NE2   . GLN A 496 ? 1.69082 2.30481 2.59447 -0.17699 -0.29956 0.20825  575 GLN B NE2   
3869 N  N     . GLY A 497 ? 1.52427 2.05139 2.18746 -0.14165 -0.32435 0.16122  576 GLY B N     
3870 C  CA    . GLY A 497 ? 1.34984 1.86313 1.96245 -0.13260 -0.32894 0.15517  576 GLY B CA    
3871 C  C     . GLY A 497 ? 1.16154 1.66686 1.75319 -0.13716 -0.35256 0.13879  576 GLY B C     
3872 O  O     . GLY A 497 ? 1.16116 1.64668 1.72590 -0.14128 -0.35219 0.12796  576 GLY B O     
3873 N  N     . MET B 1   ? 0.89294 0.72479 1.03447 -0.09287 -0.11873 -0.01889 1   MET A N     
3874 C  CA    . MET B 1   ? 0.97797 0.82556 1.10588 -0.09175 -0.12054 -0.03367 1   MET A CA    
3875 C  C     . MET B 1   ? 0.98305 0.83894 1.08550 -0.08247 -0.11494 -0.04477 1   MET A C     
3876 O  O     . MET B 1   ? 0.81040 0.66125 0.90533 -0.07736 -0.10882 -0.03954 1   MET A O     
3877 C  CB    . MET B 1   ? 0.79521 0.65840 0.91953 -0.09745 -0.11446 -0.02074 1   MET A CB    
3878 C  CG    . MET B 1   ? 0.82509 0.69699 0.93084 -0.09442 -0.10052 -0.00547 1   MET A CG    
3879 S  SD    . MET B 1   ? 1.04080 0.93214 1.14093 -0.09922 -0.09425 0.00608  1   MET A SD    
3880 C  CE    . MET B 1   ? 0.98006 0.86519 1.11139 -0.10887 -0.09768 0.02164  1   MET A CE    
3881 N  N     . THR B 2   ? 0.98255 0.85215 1.07236 -0.08041 -0.11721 -0.05944 2   THR A N     
3882 C  CA    . THR B 2   ? 0.86763 0.74757 0.93517 -0.07210 -0.11208 -0.07018 2   THR A CA    
3883 C  C     . THR B 2   ? 0.87769 0.76920 0.92761 -0.07127 -0.09932 -0.05548 2   THR A C     
3884 O  O     . THR B 2   ? 0.97674 0.87540 1.02590 -0.07650 -0.09541 -0.04270 2   THR A O     
3885 C  CB    . THR B 2   ? 0.85905 0.75186 0.91775 -0.07016 -0.11802 -0.08865 2   THR A CB    
3886 O  OG1   . THR B 2   ? 0.90067 0.78170 0.97685 -0.07088 -0.13147 -0.10333 2   THR A OG1   
3887 C  CG2   . THR B 2   ? 0.89704 0.80146 0.93485 -0.06126 -0.11258 -0.09982 2   THR A CG2   
3888 N  N     . GLU B 3   ? 0.85884 0.75216 0.89587 -0.06439 -0.09339 -0.05778 3   GLU A N     
3889 C  CA    . GLU B 3   ? 0.85509 0.75823 0.87594 -0.06280 -0.08268 -0.04612 3   GLU A CA    
3890 C  C     . GLU B 3   ? 0.85181 0.77032 0.85526 -0.05735 -0.07931 -0.05713 3   GLU A C     
3891 O  O     . GLU B 3   ? 0.95444 0.87392 0.95761 -0.05252 -0.08357 -0.07328 3   GLU A O     
3892 C  CB    . GLU B 3   ? 0.86318 0.75444 0.88605 -0.06004 -0.07827 -0.03521 3   GLU A CB    
3893 C  CG    . GLU B 3   ? 0.98457 0.86161 1.02401 -0.06488 -0.08037 -0.02209 3   GLU A CG    
3894 C  CD    . GLU B 3   ? 1.12837 0.99555 1.16627 -0.06138 -0.07558 -0.01015 3   GLU A CD    
3895 O  OE1   . GLU B 3   ? 1.18941 1.06223 1.21256 -0.05609 -0.07004 -0.01023 3   GLU A OE1   
3896 O  OE2   . GLU B 3   ? 1.22214 1.07627 1.27404 -0.06396 -0.07775 -0.00024 3   GLU A OE2   
3897 N  N     . TYR B 4   ? 0.86606 0.79704 0.85567 -0.05787 -0.07157 -0.04798 4   TYR A N     
3898 C  CA    . TYR B 4   ? 0.82552 0.77237 0.79942 -0.05362 -0.06697 -0.05421 4   TYR A CA    
3899 C  C     . TYR B 4   ? 0.77983 0.72849 0.74571 -0.05217 -0.05872 -0.04163 4   TYR A C     
3900 O  O     . TYR B 4   ? 0.79481 0.74532 0.75755 -0.05572 -0.05517 -0.02873 4   TYR A O     
3901 C  CB    . TYR B 4   ? 0.72348 0.68617 0.68875 -0.05645 -0.06789 -0.05702 4   TYR A CB    
3902 C  CG    . TYR B 4   ? 0.92786 0.89033 0.89931 -0.05715 -0.07726 -0.07147 4   TYR A CG    
3903 C  CD1   . TYR B 4   ? 0.94361 0.91325 0.90915 -0.05124 -0.08012 -0.08891 4   TYR A CD1   
3904 C  CD2   . TYR B 4   ? 0.88545 0.84138 0.86918 -0.06334 -0.08358 -0.06812 4   TYR A CD2   
3905 C  CE1   . TYR B 4   ? 0.94833 0.91728 0.91865 -0.05095 -0.08988 -0.10388 4   TYR A CE1   
3906 C  CE2   . TYR B 4   ? 0.84844 0.80341 0.83915 -0.06411 -0.09374 -0.08223 4   TYR A CE2   
3907 C  CZ    . TYR B 4   ? 0.86295 0.82381 0.84618 -0.05764 -0.09728 -0.10070 4   TYR A CZ    
3908 O  OH    . TYR B 4   ? 0.93948 0.89889 0.92881 -0.05749 -0.10850 -0.11641 4   TYR A OH    
3909 N  N     . LYS B 5   ? 0.84068 0.78897 0.80412 -0.04657 -0.05627 -0.04601 5   LYS A N     
3910 C  CA    . LYS B 5   ? 0.78361 0.73306 0.74076 -0.04474 -0.04999 -0.03589 5   LYS A CA    
3911 C  C     . LYS B 5   ? 0.80931 0.77716 0.75439 -0.04497 -0.04506 -0.03501 5   LYS A C     
3912 O  O     . LYS B 5   ? 0.85959 0.83899 0.80081 -0.04159 -0.04393 -0.04467 5   LYS A O     
3913 C  CB    . LYS B 5   ? 0.84847 0.79033 0.81023 -0.03884 -0.05039 -0.04072 5   LYS A CB    
3914 C  CG    . LYS B 5   ? 0.94588 0.86814 0.91919 -0.03838 -0.05472 -0.03761 5   LYS A CG    
3915 C  CD    . LYS B 5   ? 1.12425 1.04018 1.10240 -0.03172 -0.05615 -0.04412 5   LYS A CD    
3916 C  CE    . LYS B 5   ? 1.16819 1.06498 1.15502 -0.03093 -0.05910 -0.03586 5   LYS A CE    
3917 N  NZ    . LYS B 5   ? 1.11174 0.99652 1.11064 -0.03471 -0.06495 -0.03624 5   LYS A NZ    
3918 N  N     . LEU B 6   ? 0.77501 0.74609 0.71471 -0.04858 -0.04197 -0.02297 6   LEU A N     
3919 C  CA    . LEU B 6   ? 0.77828 0.76534 0.70803 -0.04970 -0.03798 -0.01964 6   LEU A CA    
3920 C  C     . LEU B 6   ? 0.88387 0.86970 0.81078 -0.04845 -0.03377 -0.00995 6   LEU A C     
3921 O  O     . LEU B 6   ? 0.89616 0.86970 0.82554 -0.04820 -0.03384 -0.00223 6   LEU A O     
3922 C  CB    . LEU B 6   ? 0.78322 0.77553 0.70998 -0.05463 -0.03912 -0.01419 6   LEU A CB    
3923 C  CG    . LEU B 6   ? 0.82619 0.81801 0.75766 -0.05671 -0.04501 -0.02278 6   LEU A CG    
3924 C  CD1   . LEU B 6   ? 0.71031 0.70861 0.63954 -0.06146 -0.04623 -0.01610 6   LEU A CD1   
3925 C  CD2   . LEU B 6   ? 0.77850 0.78038 0.70606 -0.05331 -0.04682 -0.03763 6   LEU A CD2   
3926 N  N     . VAL B 7   ? 0.77372 0.77283 0.69572 -0.04750 -0.03035 -0.01027 7   VAL A N     
3927 C  CA    . VAL B 7   ? 0.81224 0.81139 0.73324 -0.04678 -0.02750 -0.00196 7   VAL A CA    
3928 C  C     . VAL B 7   ? 0.76818 0.78125 0.68305 -0.05009 -0.02487 0.00476  7   VAL A C     
3929 O  O     . VAL B 7   ? 0.77200 0.79994 0.68296 -0.05080 -0.02341 0.00046  7   VAL A O     
3930 C  CB    . VAL B 7   ? 0.84852 0.84979 0.77404 -0.04243 -0.02636 -0.00778 7   VAL A CB    
3931 C  CG1   . VAL B 7   ? 0.72480 0.72632 0.65108 -0.04225 -0.02475 0.00060  7   VAL A CG1   
3932 C  CG2   . VAL B 7   ? 0.74909 0.73566 0.68117 -0.03878 -0.02973 -0.01383 7   VAL A CG2   
3933 N  N     . VAL B 8   ? 0.68735 0.69565 0.60107 -0.05158 -0.02455 0.01527  8   VAL A N     
3934 C  CA    . VAL B 8   ? 0.72915 0.74794 0.63874 -0.05477 -0.02299 0.02331  8   VAL A CA    
3935 C  C     . VAL B 8   ? 0.81815 0.83933 0.73109 -0.05403 -0.02149 0.02780  8   VAL A C     
3936 O  O     . VAL B 8   ? 0.80598 0.81521 0.72164 -0.05228 -0.02322 0.03156  8   VAL A O     
3937 C  CB    . VAL B 8   ? 0.68846 0.70032 0.59601 -0.05672 -0.02463 0.03149  8   VAL A CB    
3938 C  CG1   . VAL B 8   ? 0.81760 0.84091 0.72139 -0.05995 -0.02388 0.03897  8   VAL A CG1   
3939 C  CG2   . VAL B 8   ? 0.69065 0.69791 0.59883 -0.05752 -0.02669 0.02753  8   VAL A CG2   
3940 N  N     . VAL B 9   ? 0.79273 0.83009 0.70583 -0.05522 -0.01849 0.02763  9   VAL A N     
3941 C  CA    . VAL B 9   ? 0.87206 0.91420 0.79137 -0.05552 -0.01710 0.03261  9   VAL A CA    
3942 C  C     . VAL B 9   ? 0.86477 0.91886 0.78246 -0.05995 -0.01554 0.04293  9   VAL A C     
3943 O  O     . VAL B 9   ? 0.84329 0.90694 0.75386 -0.06199 -0.01440 0.04421  9   VAL A O     
3944 C  CB    . VAL B 9   ? 0.72159 0.77399 0.64611 -0.05278 -0.01418 0.02484  9   VAL A CB    
3945 C  CG1   . VAL B 9   ? 0.76733 0.80690 0.69411 -0.04816 -0.01656 0.01494  9   VAL A CG1   
3946 C  CG2   . VAL B 9   ? 0.72885 0.80143 0.64795 -0.05345 -0.00990 0.02148  9   VAL A CG2   
3947 N  N     . GLY B 10  ? 0.87763 0.93062 0.80270 -0.06140 -0.01632 0.05050  10  GLY A N     
3948 C  CA    . GLY B 10  ? 0.77726 0.83949 0.70385 -0.06590 -0.01567 0.06201  10  GLY A CA    
3949 C  C     . GLY B 10  ? 0.80869 0.85927 0.74419 -0.06672 -0.02001 0.06901  10  GLY A C     
3950 O  O     . GLY B 10  ? 0.83265 0.86716 0.76982 -0.06331 -0.02386 0.06502  10  GLY A O     
3951 N  N     . ALA B 11  ? 0.83846 0.89735 0.77978 -0.07112 -0.01989 0.07986  11  ALA A N     
3952 C  CA    . ALA B 11  ? 0.73249 0.78066 0.68440 -0.07234 -0.02525 0.08651  11  ALA A CA    
3953 C  C     . ALA B 11  ? 0.86435 0.89315 0.81100 -0.06942 -0.03082 0.08595  11  ALA A C     
3954 O  O     . ALA B 11  ? 0.84728 0.87362 0.78361 -0.06796 -0.02992 0.08363  11  ALA A O     
3955 C  CB    . ALA B 11  ? 0.74206 0.80240 0.70181 -0.07827 -0.02447 0.09975  11  ALA A CB    
3956 N  N     . GLY B 12  ? 0.82752 0.84319 0.78208 -0.06818 -0.03687 0.08770  12  GLY A N     
3957 C  CA    . GLY B 12  ? 0.66854 0.66676 0.61788 -0.06401 -0.04198 0.08649  12  GLY A CA    
3958 C  C     . GLY B 12  ? 0.70937 0.70838 0.65717 -0.06641 -0.04336 0.09521  12  GLY A C     
3959 O  O     . GLY B 12  ? 0.81852 0.82443 0.77464 -0.07127 -0.04440 0.10446  12  GLY A O     
3960 N  N     . GLY B 13  ? 0.80497 0.79733 0.74316 -0.06297 -0.04340 0.09299  13  GLY A N     
3961 C  CA    . GLY B 13  ? 0.80343 0.79538 0.74029 -0.06393 -0.04535 0.10030  13  GLY A CA    
3962 C  C     . GLY B 13  ? 0.81236 0.81979 0.74399 -0.06811 -0.04099 0.10471  13  GLY A C     
3963 O  O     . GLY B 13  ? 0.86909 0.87762 0.80048 -0.06925 -0.04305 0.11194  13  GLY A O     
3964 N  N     . VAL B 14  ? 0.83389 0.85321 0.76111 -0.06978 -0.03570 0.10003  14  VAL A N     
3965 C  CA    . VAL B 14  ? 0.82452 0.85938 0.74532 -0.07303 -0.03235 0.10295  14  VAL A CA    
3966 C  C     . VAL B 14  ? 0.82614 0.85822 0.73894 -0.07079 -0.03256 0.09875  14  VAL A C     
3967 O  O     . VAL B 14  ? 0.87450 0.91663 0.78260 -0.07298 -0.03229 0.10253  14  VAL A O     
3968 C  CB    . VAL B 14  ? 0.84292 0.89268 0.76180 -0.07472 -0.02701 0.09834  14  VAL A CB    
3969 C  CG1   . VAL B 14  ? 0.82219 0.87788 0.75138 -0.07749 -0.02611 0.10404  14  VAL A CG1   
3970 C  CG2   . VAL B 14  ? 0.73943 0.78297 0.65512 -0.07085 -0.02556 0.08576  14  VAL A CG2   
3971 N  N     . GLY B 15  ? 0.81780 0.83739 0.72950 -0.06655 -0.03319 0.09171  15  GLY A N     
3972 C  CA    . GLY B 15  ? 0.82159 0.83899 0.72871 -0.06486 -0.03324 0.08910  15  GLY A CA    
3973 C  C     . GLY B 15  ? 0.82888 0.84528 0.73314 -0.06361 -0.03077 0.07953  15  GLY A C     
3974 O  O     . GLY B 15  ? 0.84498 0.86330 0.74705 -0.06387 -0.03069 0.07733  15  GLY A O     
3975 N  N     . LYS B 16  ? 0.73790 0.75091 0.64380 -0.06228 -0.02942 0.07403  16  LYS A N     
3976 C  CA    . LYS B 16  ? 0.65120 0.66211 0.55575 -0.06088 -0.02775 0.06506  16  LYS A CA    
3977 C  C     . LYS B 16  ? 0.73095 0.73036 0.63522 -0.05786 -0.02844 0.06423  16  LYS A C     
3978 O  O     . LYS B 16  ? 0.74189 0.74177 0.64605 -0.05843 -0.02785 0.05984  16  LYS A O     
3979 C  CB    . LYS B 16  ? 0.77162 0.77999 0.67926 -0.05917 -0.02684 0.06019  16  LYS A CB    
3980 C  CG    . LYS B 16  ? 0.67165 0.69394 0.58121 -0.06195 -0.02486 0.06094  16  LYS A CG    
3981 C  CD    . LYS B 16  ? 0.78890 0.80936 0.70346 -0.05974 -0.02402 0.05535  16  LYS A CD    
3982 C  CE    . LYS B 16  ? 0.76397 0.77000 0.68272 -0.05684 -0.02743 0.05750  16  LYS A CE    
3983 N  NZ    . LYS B 16  ? 0.77283 0.77969 0.69597 -0.05908 -0.02972 0.06630  16  LYS A NZ    
3984 N  N     . SER B 17  ? 0.77938 0.76880 0.68411 -0.05437 -0.02981 0.06841  17  SER A N     
3985 C  CA    . SER B 17  ? 0.76691 0.74758 0.67070 -0.05071 -0.02933 0.06884  17  SER A CA    
3986 C  C     . SER B 17  ? 0.86076 0.84696 0.76528 -0.05226 -0.02928 0.07328  17  SER A C     
3987 O  O     . SER B 17  ? 0.75691 0.74189 0.66299 -0.05181 -0.02792 0.07286  17  SER A O     
3988 C  CB    . SER B 17  ? 0.84576 0.81509 0.74808 -0.04503 -0.03089 0.07069  17  SER A CB    
3989 O  OG    . SER B 17  ? 0.86205 0.82634 0.76471 -0.04345 -0.03188 0.06642  17  SER A OG    
3990 N  N     . ALA B 18  ? 0.85583 0.84845 0.76062 -0.05425 -0.03105 0.07830  18  ALA A N     
3991 C  CA    . ALA B 18  ? 0.76063 0.75939 0.66690 -0.05548 -0.03178 0.08264  18  ALA A CA    
3992 C  C     . ALA B 18  ? 0.82609 0.83449 0.73282 -0.06000 -0.03161 0.07892  18  ALA A C     
3993 O  O     . ALA B 18  ? 0.86971 0.88076 0.77982 -0.06062 -0.03196 0.07995  18  ALA A O     
3994 C  CB    . ALA B 18  ? 0.78855 0.79123 0.69534 -0.05633 -0.03455 0.08942  18  ALA A CB    
3995 N  N     . LEU B 19  ? 0.76907 0.78339 0.67315 -0.06282 -0.03138 0.07411  19  LEU A N     
3996 C  CA    . LEU B 19  ? 0.76018 0.78290 0.66377 -0.06605 -0.03218 0.06829  19  LEU A CA    
3997 C  C     . LEU B 19  ? 0.81983 0.83496 0.72795 -0.06527 -0.03165 0.06273  19  LEU A C     
3998 O  O     . LEU B 19  ? 0.82004 0.83843 0.73215 -0.06748 -0.03354 0.06097  19  LEU A O     
3999 C  CB    . LEU B 19  ? 0.65491 0.68632 0.55383 -0.06768 -0.03144 0.06356  19  LEU A CB    
4000 C  CG    . LEU B 19  ? 0.75492 0.79754 0.64965 -0.06964 -0.03171 0.07010  19  LEU A CG    
4001 C  CD1   . LEU B 19  ? 0.72542 0.77672 0.61663 -0.07024 -0.02920 0.06593  19  LEU A CD1   
4002 C  CD2   . LEU B 19  ? 0.83826 0.89122 0.73034 -0.07197 -0.03470 0.07271  19  LEU A CD2   
4003 N  N     . THR B 20  ? 0.70652 0.71145 0.61511 -0.06232 -0.02969 0.06045  20  THR A N     
4004 C  CA    . THR B 20  ? 0.72498 0.72190 0.63832 -0.06155 -0.02923 0.05671  20  THR A CA    
4005 C  C     . THR B 20  ? 0.78885 0.78281 0.70717 -0.06089 -0.02853 0.06310  20  THR A C     
4006 O  O     . THR B 20  ? 0.85538 0.85037 0.78060 -0.06349 -0.02961 0.06190  20  THR A O     
4007 C  CB    . THR B 20  ? 0.70014 0.68694 0.61212 -0.05779 -0.02766 0.05443  20  THR A CB    
4008 O  OG1   . THR B 20  ? 0.76515 0.75672 0.67478 -0.05840 -0.02792 0.04826  20  THR A OG1   
4009 C  CG2   . THR B 20  ? 0.70650 0.68428 0.62358 -0.05684 -0.02734 0.05244  20  THR A CG2   
4010 N  N     . ILE B 21  ? 0.70751 0.69836 0.62347 -0.05720 -0.02695 0.06979  21  ILE A N     
4011 C  CA    . ILE B 21  ? 0.80457 0.79433 0.72497 -0.05521 -0.02515 0.07606  21  ILE A CA    
4012 C  C     . ILE B 21  ? 0.80586 0.80628 0.73208 -0.05912 -0.02719 0.07841  21  ILE A C     
4013 O  O     . ILE B 21  ? 0.79122 0.79355 0.72567 -0.06003 -0.02628 0.08152  21  ILE A O     
4014 C  CB    . ILE B 21  ? 0.75182 0.73623 0.66714 -0.04896 -0.02360 0.08085  21  ILE A CB    
4015 C  CG1   . ILE B 21  ? 0.71498 0.68863 0.62512 -0.04476 -0.02251 0.07813  21  ILE A CG1   
4016 C  CG2   . ILE B 21  ? 0.76742 0.75365 0.68677 -0.04578 -0.02102 0.08727  21  ILE A CG2   
4017 C  CD1   . ILE B 21  ? 1.05828 1.02562 0.96254 -0.03795 -0.02250 0.08072  21  ILE A CD1   
4018 N  N     . GLN B 22  ? 0.82210 0.83045 0.74496 -0.06161 -0.03014 0.07761  22  GLN A N     
4019 C  CA    . GLN B 22  ? 0.84510 0.86416 0.77265 -0.06523 -0.03329 0.07917  22  GLN A CA    
4020 C  C     . GLN B 22  ? 0.82797 0.84947 0.76218 -0.06959 -0.03560 0.07320  22  GLN A C     
4021 O  O     . GLN B 22  ? 0.90277 0.92904 0.84640 -0.07179 -0.03730 0.07552  22  GLN A O     
4022 C  CB    . GLN B 22  ? 0.76191 0.78916 0.68275 -0.06689 -0.03617 0.07969  22  GLN A CB    
4023 C  CG    . GLN B 22  ? 0.94072 0.97967 0.86458 -0.07010 -0.04044 0.08134  22  GLN A CG    
4024 C  CD    . GLN B 22  ? 0.90821 0.94873 0.83953 -0.06797 -0.04050 0.08901  22  GLN A CD    
4025 O  OE1   . GLN B 22  ? 0.97248 1.01690 0.91328 -0.06962 -0.04162 0.08933  22  GLN A OE1   
4026 N  NE2   . GLN B 22  ? 0.72310 0.76092 0.65162 -0.06412 -0.03965 0.09508  22  GLN A NE2   
4027 N  N     . LEU B 23  ? 0.85647 0.87472 0.78741 -0.07070 -0.03621 0.06516  23  LEU A N     
4028 C  CA    . LEU B 23  ? 0.79459 0.81305 0.73268 -0.07428 -0.03957 0.05801  23  LEU A CA    
4029 C  C     . LEU B 23  ? 0.82572 0.83523 0.77454 -0.07415 -0.03750 0.06105  23  LEU A C     
4030 O  O     . LEU B 23  ? 0.92085 0.93185 0.88131 -0.07790 -0.04061 0.06007  23  LEU A O     
4031 C  CB    . LEU B 23  ? 0.84495 0.86250 0.77662 -0.07421 -0.04075 0.04786  23  LEU A CB    
4032 C  CG    . LEU B 23  ? 0.79482 0.80912 0.73415 -0.07662 -0.04484 0.03847  23  LEU A CG    
4033 C  CD1   . LEU B 23  ? 0.83586 0.86087 0.77668 -0.08008 -0.05122 0.03308  23  LEU A CD1   
4034 C  CD2   . LEU B 23  ? 0.91624 0.92557 0.85067 -0.07420 -0.04405 0.02965  23  LEU A CD2   
4035 N  N     . ILE B 24  ? 0.85719 0.85783 0.80275 -0.06988 -0.03263 0.06527  24  ILE A N     
4036 C  CA    . ILE B 24  ? 0.84008 0.83221 0.79367 -0.06916 -0.03007 0.06883  24  ILE A CA    
4037 C  C     . ILE B 24  ? 0.82205 0.81780 0.78268 -0.06808 -0.02666 0.07927  24  ILE A C     
4038 O  O     . ILE B 24  ? 0.86566 0.86002 0.83821 -0.07019 -0.02569 0.08338  24  ILE A O     
4039 C  CB    . ILE B 24  ? 0.83004 0.81153 0.77552 -0.06434 -0.02702 0.06786  24  ILE A CB    
4040 C  CG1   . ILE B 24  ? 0.81153 0.78642 0.76009 -0.06603 -0.02983 0.05939  24  ILE A CG1   
4041 C  CG2   . ILE B 24  ? 0.80940 0.78510 0.75548 -0.05995 -0.02202 0.07686  24  ILE A CG2   
4042 C  CD1   . ILE B 24  ? 0.94405 0.92581 0.89084 -0.06910 -0.03447 0.04922  24  ILE A CD1   
4043 N  N     . GLN B 25  ? 0.84165 0.84265 0.79652 -0.06475 -0.02489 0.08396  25  GLN A N     
4044 C  CA    . GLN B 25  ? 0.92808 0.93343 0.88867 -0.06191 -0.02093 0.09322  25  GLN A CA    
4045 C  C     . GLN B 25  ? 0.89508 0.91199 0.85945 -0.06308 -0.02337 0.09585  25  GLN A C     
4046 O  O     . GLN B 25  ? 0.92014 0.94223 0.88988 -0.05991 -0.02005 0.10315  25  GLN A O     
4047 C  CB    . GLN B 25  ? 0.84476 0.84347 0.79495 -0.05390 -0.01596 0.09697  25  GLN A CB    
4048 C  CG    . GLN B 25  ? 0.73372 0.72258 0.68214 -0.05152 -0.01263 0.09788  25  GLN A CG    
4049 C  CD    . GLN B 25  ? 0.86505 0.84641 0.80003 -0.04341 -0.01002 0.09840  25  GLN A CD    
4050 O  OE1   . GLN B 25  ? 0.91950 0.90255 0.84804 -0.03937 -0.01052 0.09847  25  GLN A OE1   
4051 N  NE2   . GLN B 25  ? 0.83497 0.80738 0.76618 -0.04081 -0.00817 0.09855  25  GLN A NE2   
4052 N  N     . ASN B 26  ? 0.87843 0.90029 0.83974 -0.06682 -0.02891 0.09040  26  ASN A N     
4053 C  CA    . ASN B 26  ? 0.90448 0.93786 0.87025 -0.06868 -0.03268 0.09284  26  ASN A CA    
4054 C  C     . ASN B 26  ? 0.84083 0.87609 0.80292 -0.06272 -0.03018 0.09955  26  ASN A C     
4055 O  O     . ASN B 26  ? 0.88220 0.92555 0.85324 -0.06170 -0.03010 0.10512  26  ASN A O     
4056 C  CB    . ASN B 26  ? 0.82983 0.87044 0.81258 -0.07320 -0.03463 0.09497  26  ASN A CB    
4057 C  CG    . ASN B 26  ? 0.97580 1.01385 0.96376 -0.07917 -0.03926 0.08703  26  ASN A CG    
4058 O  OD1   . ASN B 26  ? 1.13843 1.18185 1.12465 -0.08275 -0.04586 0.08035  26  ASN A OD1   
4059 N  ND2   . ASN B 26  ? 0.92803 0.95776 0.92217 -0.07975 -0.03625 0.08758  26  ASN A ND2   
4060 N  N     . HIS B 27  ? 0.89068 0.91836 0.84083 -0.05854 -0.02874 0.09861  27  HIS A N     
4061 C  CA    . HIS B 27  ? 0.90415 0.93153 0.85067 -0.05268 -0.02810 0.10339  27  HIS A CA    
4062 C  C     . HIS B 27  ? 0.84216 0.86178 0.77720 -0.05110 -0.02935 0.10062  27  HIS A C     
4063 O  O     . HIS B 27  ? 0.88583 0.89908 0.81569 -0.05236 -0.02847 0.09576  27  HIS A O     
4064 C  CB    . HIS B 27  ? 0.82802 0.85289 0.77758 -0.04582 -0.02249 0.10800  27  HIS A CB    
4065 C  CG    . HIS B 27  ? 0.97677 0.99030 0.91824 -0.04178 -0.01864 0.10579  27  HIS A CG    
4066 N  ND1   . HIS B 27  ? 1.05556 1.06030 0.98675 -0.03623 -0.01912 0.10404  27  HIS A ND1   
4067 C  CD2   . HIS B 27  ? 0.95826 0.96760 0.90106 -0.04242 -0.01505 0.10534  27  HIS A CD2   
4068 C  CE1   . HIS B 27  ? 1.04496 1.04118 0.97054 -0.03330 -0.01612 0.10206  27  HIS A CE1   
4069 N  NE2   . HIS B 27  ? 1.01223 1.01101 0.94428 -0.03686 -0.01335 0.10327  27  HIS A NE2   
4070 N  N     . PHE B 28  ? 0.78903 0.80934 0.72192 -0.04835 -0.03181 0.10416  28  PHE A N     
4071 C  CA    . PHE B 28  ? 0.89573 0.91018 0.82101 -0.04793 -0.03400 0.10326  28  PHE A CA    
4072 C  C     . PHE B 28  ? 1.05165 1.05479 0.97355 -0.04047 -0.03239 0.10330  28  PHE A C     
4073 O  O     . PHE B 28  ? 0.94954 0.95194 0.87412 -0.03450 -0.03208 0.10645  28  PHE A O     
4074 C  CB    . PHE B 28  ? 0.85457 0.87577 0.78065 -0.04993 -0.03876 0.10802  28  PHE A CB    
4075 C  CG    . PHE B 28  ? 0.93057 0.94568 0.85218 -0.04921 -0.04112 0.10975  28  PHE A CG    
4076 C  CD1   . PHE B 28  ? 0.97146 0.98515 0.88797 -0.05285 -0.04059 0.10641  28  PHE A CD1   
4077 C  CD2   . PHE B 28  ? 0.96657 0.97771 0.89088 -0.04490 -0.04424 0.11486  28  PHE A CD2   
4078 C  CE1   . PHE B 28  ? 0.94918 0.95843 0.86439 -0.05296 -0.04280 0.10913  28  PHE A CE1   
4079 C  CE2   . PHE B 28  ? 0.94253 0.94736 0.86548 -0.04502 -0.04733 0.11715  28  PHE A CE2   
4080 C  CZ    . PHE B 28  ? 0.93421 0.93855 0.85312 -0.04946 -0.04646 0.11478  28  PHE A CZ    
4081 N  N     . VAL B 29  ? 1.04086 1.03574 0.95704 -0.04020 -0.03182 0.09914  29  VAL A N     
4082 C  CA    . VAL B 29  ? 1.07279 1.05641 0.98483 -0.03314 -0.03201 0.09792  29  VAL A CA    
4083 C  C     . VAL B 29  ? 1.08125 1.06183 0.99394 -0.03283 -0.03726 0.10030  29  VAL A C     
4084 O  O     . VAL B 29  ? 0.96539 0.94842 0.87815 -0.03856 -0.03945 0.10082  29  VAL A O     
4085 C  CB    . VAL B 29  ? 0.99183 0.96796 0.89879 -0.03287 -0.03030 0.09267  29  VAL A CB    
4086 C  CG1   . VAL B 29  ? 0.99530 0.97202 0.90251 -0.03162 -0.02542 0.09201  29  VAL A CG1   
4087 C  CG2   . VAL B 29  ? 1.04833 1.02787 0.95519 -0.04000 -0.03168 0.09008  29  VAL A CG2   
4088 N  N     . ASP B 30  ? 1.15950 1.13528 1.07350 -0.02591 -0.03930 0.10211  30  ASP A N     
4089 C  CA    . ASP B 30  ? 1.00511 0.97650 0.92222 -0.02541 -0.04537 0.10509  30  ASP A CA    
4090 C  C     . ASP B 30  ? 0.99928 0.95807 0.91401 -0.02245 -0.04876 0.10114  30  ASP A C     
4091 O  O     . ASP B 30  ? 1.01790 0.97431 0.93653 -0.02643 -0.05337 0.10366  30  ASP A O     
4092 C  CB    . ASP B 30  ? 1.04309 1.01472 0.96450 -0.01883 -0.04727 0.10812  30  ASP A CB    
4093 C  CG    . ASP B 30  ? 1.29613 1.26654 1.22361 -0.02067 -0.05399 0.11369  30  ASP A CG    
4094 O  OD1   . ASP B 30  ? 1.29128 1.25270 1.21975 -0.02141 -0.05860 0.11348  30  ASP A OD1   
4095 O  OD2   . ASP B 30  ? 1.48894 1.46756 1.42135 -0.02164 -0.05509 0.11893  30  ASP A OD2   
4096 N  N     . GLU B 31  ? 1.09329 1.04463 1.00222 -0.01563 -0.04682 0.09556  31  GLU A N     
4097 C  CA    . GLU B 31  ? 1.16461 1.10382 1.07112 -0.01207 -0.05115 0.09075  31  GLU A CA    
4098 C  C     . GLU B 31  ? 0.98478 0.92527 0.89164 -0.01952 -0.05073 0.08939  31  GLU A C     
4099 O  O     . GLU B 31  ? 0.99868 0.94805 0.90474 -0.02535 -0.04601 0.09007  31  GLU A O     
4100 C  CB    . GLU B 31  ? 1.16100 1.09340 1.05902 -0.00204 -0.04909 0.08518  31  GLU A CB    
4101 C  CG    . GLU B 31  ? 1.22782 1.16191 1.12459 0.00663  -0.04737 0.08599  31  GLU A CG    
4102 C  CD    . GLU B 31  ? 1.38543 1.31661 1.27201 0.01629  -0.04317 0.08178  31  GLU A CD    
4103 O  OE1   . GLU B 31  ? 1.24859 1.17272 1.12862 0.01764  -0.04419 0.07735  31  GLU A OE1   
4104 O  OE2   . GLU B 31  ? 1.45992 1.39693 1.34520 0.02276  -0.03869 0.08348  31  GLU A OE2   
4105 N  N     . TYR B 32  ? 0.94870 0.88034 0.85781 -0.01887 -0.05623 0.08688  32  TYR A N     
4106 C  CA    . TYR B 32  ? 0.98678 0.91970 0.89763 -0.02456 -0.05609 0.08507  32  TYR A CA    
4107 C  C     . TYR B 32  ? 0.93650 0.85946 0.84160 -0.01818 -0.05749 0.07781  32  TYR A C     
4108 O  O     . TYR B 32  ? 0.92475 0.83684 0.83017 -0.01227 -0.06391 0.07453  32  TYR A O     
4109 C  CB    . TYR B 32  ? 0.91014 0.84331 0.83115 -0.03040 -0.06141 0.08951  32  TYR A CB    
4110 C  CG    . TYR B 32  ? 0.98771 0.92374 0.91224 -0.03553 -0.06097 0.08772  32  TYR A CG    
4111 C  CD1   . TYR B 32  ? 0.95955 0.90468 0.87993 -0.03897 -0.05453 0.08556  32  TYR A CD1   
4112 C  CD2   . TYR B 32  ? 0.98854 0.91840 0.92220 -0.03675 -0.06744 0.08794  32  TYR A CD2   
4113 C  CE1   . TYR B 32  ? 0.95323 0.90196 0.87754 -0.04267 -0.05390 0.08336  32  TYR A CE1   
4114 C  CE2   . TYR B 32  ? 0.87422 0.80855 0.81297 -0.04124 -0.06670 0.08663  32  TYR A CE2   
4115 C  CZ    . TYR B 32  ? 0.94619 0.89037 0.87980 -0.04380 -0.05958 0.08421  32  TYR A CZ    
4116 O  OH    . TYR B 32  ? 0.90722 0.85678 0.84657 -0.04731 -0.05865 0.08237  32  TYR A OH    
4117 N  N     . ASP B 33  ? 0.90790 0.83413 0.80796 -0.01910 -0.05235 0.07511  33  ASP A N     
4118 C  CA    . ASP B 33  ? 0.85652 0.77453 0.75076 -0.01364 -0.05353 0.06913  33  ASP A CA    
4119 C  C     . ASP B 33  ? 0.92393 0.84643 0.82216 -0.01986 -0.05219 0.06746  33  ASP A C     
4120 O  O     . ASP B 33  ? 0.84432 0.77428 0.74142 -0.02365 -0.04648 0.06798  33  ASP A O     
4121 C  CB    . ASP B 33  ? 0.85205 0.76906 0.73636 -0.00716 -0.04841 0.06831  33  ASP A CB    
4122 C  CG    . ASP B 33  ? 0.99608 0.90348 0.87202 0.00076  -0.05073 0.06306  33  ASP A CG    
4123 O  OD1   . ASP B 33  ? 0.94805 0.84829 0.82616 0.00215  -0.05764 0.05896  33  ASP A OD1   
4124 O  OD2   . ASP B 33  ? 1.11729 1.02475 0.98501 0.00554  -0.04592 0.06361  33  ASP A OD2   
4125 N  N     . PRO B 34  ? 0.83064 0.74930 0.73486 -0.02092 -0.05761 0.06513  34  PRO A N     
4126 C  CA    . PRO B 34  ? 0.90593 0.83110 0.81573 -0.02652 -0.05592 0.06366  34  PRO A CA    
4127 C  C     . PRO B 34  ? 0.83140 0.75517 0.73440 -0.02360 -0.05217 0.05937  34  PRO A C     
4128 O  O     . PRO B 34  ? 0.88153 0.79627 0.77635 -0.01626 -0.05344 0.05676  34  PRO A O     
4129 C  CB    . PRO B 34  ? 0.79121 0.71056 0.70939 -0.02615 -0.06355 0.06173  34  PRO A CB    
4130 C  CG    . PRO B 34  ? 0.80389 0.71663 0.72430 -0.02399 -0.06908 0.06433  34  PRO A CG    
4131 C  CD    . PRO B 34  ? 0.76666 0.67572 0.67511 -0.01740 -0.06607 0.06380  34  PRO A CD    
4132 N  N     . THR B 35  ? 0.74823 0.68115 0.65456 -0.02899 -0.04776 0.05878  35  THR A N     
4133 C  CA    . THR B 35  ? 0.75634 0.68821 0.65846 -0.02729 -0.04430 0.05531  35  THR A CA    
4134 C  C     . THR B 35  ? 0.81302 0.74244 0.71923 -0.02596 -0.04710 0.05038  35  THR A C     
4135 O  O     . THR B 35  ? 0.80418 0.74004 0.71935 -0.02989 -0.04856 0.04977  35  THR A O     
4136 C  CB    . THR B 35  ? 0.69169 0.63419 0.59548 -0.03308 -0.03886 0.05596  35  THR A CB    
4137 O  OG1   . THR B 35  ? 0.80027 0.74552 0.70129 -0.03417 -0.03693 0.06064  35  THR A OG1   
4138 C  CG2   . THR B 35  ? 0.78970 0.72944 0.69148 -0.03153 -0.03641 0.05224  35  THR A CG2   
4139 N  N     . ILE B 36  ? 0.81388 0.73476 0.71413 -0.02023 -0.04783 0.04768  36  ILE A N     
4140 C  CA    . ILE B 36  ? 0.80120 0.72049 0.70544 -0.01880 -0.04989 0.04291  36  ILE A CA    
4141 C  C     . ILE B 36  ? 0.82859 0.75365 0.73499 -0.02204 -0.04473 0.04120  36  ILE A C     
4142 O  O     . ILE B 36  ? 0.92429 0.85839 0.83870 -0.02602 -0.04345 0.03816  36  ILE A O     
4143 C  CB    . ILE B 36  ? 0.77912 0.68601 0.67539 -0.01043 -0.05425 0.04124  36  ILE A CB    
4144 C  CG1   . ILE B 36  ? 0.75818 0.65912 0.65330 -0.00670 -0.06113 0.04057  36  ILE A CG1   
4145 C  CG2   . ILE B 36  ? 0.69706 0.60238 0.59757 -0.00875 -0.05618 0.03684  36  ILE A CG2   
4146 C  CD1   . ILE B 36  ? 0.92116 0.81059 0.80609 0.00267  -0.06632 0.03808  36  ILE A CD1   
4147 N  N     . GLU B 37  ? 0.83740 0.75780 0.73741 -0.02017 -0.04185 0.04315  37  GLU A N     
4148 C  CA    . GLU B 37  ? 0.79808 0.72279 0.70116 -0.02380 -0.03788 0.04175  37  GLU A CA    
4149 C  C     . GLU B 37  ? 0.84365 0.76454 0.74127 -0.02298 -0.03492 0.04692  37  GLU A C     
4150 O  O     . GLU B 37  ? 0.85463 0.76790 0.74508 -0.01756 -0.03546 0.05068  37  GLU A O     
4151 C  CB    . GLU B 37  ? 0.80962 0.73075 0.71696 -0.02168 -0.03931 0.03656  37  GLU A CB    
4152 C  CG    . GLU B 37  ? 0.97969 0.88835 0.88120 -0.01516 -0.04152 0.03864  37  GLU A CG    
4153 C  CD    . GLU B 37  ? 1.02475 0.92906 0.92460 -0.01548 -0.03837 0.04246  37  GLU A CD    
4154 O  OE1   . GLU B 37  ? 1.11561 1.02471 1.02200 -0.02036 -0.03624 0.04006  37  GLU A OE1   
4155 O  OE2   . GLU B 37  ? 1.18011 1.07673 1.07246 -0.01073 -0.03822 0.04802  37  GLU A OE2   
4156 N  N     . ASP B 38  ? 0.76820 0.69552 0.66957 -0.02813 -0.03188 0.04704  38  ASP A N     
4157 C  CA    . ASP B 38  ? 0.87720 0.80277 0.77727 -0.02861 -0.02904 0.05221  38  ASP A CA    
4158 C  C     . ASP B 38  ? 0.92266 0.85152 0.83023 -0.03350 -0.02823 0.04870  38  ASP A C     
4159 O  O     . ASP B 38  ? 0.87897 0.81631 0.79008 -0.03754 -0.02861 0.04350  38  ASP A O     
4160 C  CB    . ASP B 38  ? 0.79119 0.72229 0.68858 -0.02980 -0.02744 0.05720  38  ASP A CB    
4161 C  CG    . ASP B 38  ? 0.87200 0.79753 0.76173 -0.02343 -0.02867 0.06039  38  ASP A CG    
4162 O  OD1   . ASP B 38  ? 0.89311 0.81129 0.77729 -0.01775 -0.02804 0.06303  38  ASP A OD1   
4163 O  OD2   . ASP B 38  ? 0.80821 0.73664 0.69744 -0.02377 -0.03064 0.06026  38  ASP A OD2   
4164 N  N     . SER B 39  ? 0.85336 0.77565 0.76348 -0.03284 -0.02743 0.05161  39  SER A N     
4165 C  CA    . SER B 39  ? 0.82571 0.74827 0.74479 -0.03706 -0.02818 0.04781  39  SER A CA    
4166 C  C     . SER B 39  ? 0.86091 0.78479 0.78422 -0.04029 -0.02611 0.05455  39  SER A C     
4167 O  O     . SER B 39  ? 0.80072 0.72186 0.72051 -0.03747 -0.02337 0.06321  39  SER A O     
4168 C  CB    . SER B 39  ? 0.84791 0.76022 0.77066 -0.03405 -0.03042 0.04529  39  SER A CB    
4169 O  OG    . SER B 39  ? 0.97754 0.88123 0.89677 -0.03008 -0.02915 0.05409  39  SER A OG    
4170 N  N     . TYR B 40  ? 0.86975 0.79881 0.80097 -0.04582 -0.02758 0.05028  40  TYR A N     
4171 C  CA    . TYR B 40  ? 0.75996 0.69191 0.69836 -0.04995 -0.02664 0.05591  40  TYR A CA    
4172 C  C     . TYR B 40  ? 0.83709 0.76634 0.78753 -0.05436 -0.03059 0.04998  40  TYR A C     
4173 O  O     . TYR B 40  ? 0.87210 0.80197 0.82328 -0.05467 -0.03387 0.03937  40  TYR A O     
4174 C  CB    . TYR B 40  ? 0.81501 0.75874 0.75076 -0.05262 -0.02580 0.05696  40  TYR A CB    
4175 C  CG    . TYR B 40  ? 0.87524 0.82098 0.80062 -0.04830 -0.02324 0.06147  40  TYR A CG    
4176 C  CD1   . TYR B 40  ? 0.84551 0.79002 0.76842 -0.04495 -0.01982 0.07055  40  TYR A CD1   
4177 C  CD2   . TYR B 40  ? 0.84160 0.79087 0.76060 -0.04734 -0.02444 0.05662  40  TYR A CD2   
4178 C  CE1   . TYR B 40  ? 0.62063 0.56582 0.53444 -0.04018 -0.01865 0.07308  40  TYR A CE1   
4179 C  CE2   . TYR B 40  ? 0.78443 0.73400 0.69618 -0.04373 -0.02350 0.06042  40  TYR A CE2   
4180 C  CZ    . TYR B 40  ? 0.73989 0.68664 0.64880 -0.03988 -0.02111 0.06785  40  TYR A CZ    
4181 O  OH    . TYR B 40  ? 0.88137 0.82728 0.78335 -0.03546 -0.02127 0.07008  40  TYR A OH    
4182 N  N     . ARG B 41  ? 0.87318 0.79986 0.83403 -0.05752 -0.03042 0.05682  41  ARG A N     
4183 C  CA    . ARG B 41  ? 0.87357 0.79737 0.84882 -0.06265 -0.03545 0.05176  41  ARG A CA    
4184 C  C     . ARG B 41  ? 0.77976 0.71186 0.76375 -0.06812 -0.03551 0.05695  41  ARG A C     
4185 O  O     . ARG B 41  ? 0.92393 0.85668 0.91196 -0.06840 -0.03136 0.06911  41  ARG A O     
4186 C  CB    . ARG B 41  ? 0.79162 0.70186 0.77602 -0.06183 -0.03668 0.05589  41  ARG A CB    
4187 C  CG    . ARG B 41  ? 1.03284 0.93484 1.00875 -0.05551 -0.03662 0.05258  41  ARG A CG    
4188 C  CD    . ARG B 41  ? 1.03054 0.91851 1.01681 -0.05482 -0.03946 0.05541  41  ARG A CD    
4189 N  NE    . ARG B 41  ? 1.07971 0.96266 1.07678 -0.05685 -0.04642 0.04277  41  ARG A NE    
4190 C  CZ    . ARG B 41  ? 1.15038 1.02835 1.16424 -0.06218 -0.05126 0.04212  41  ARG A CZ    
4191 N  NH1   . ARG B 41  ? 1.20743 1.08559 1.23100 -0.06686 -0.04941 0.05475  41  ARG A NH1   
4192 N  NH2   . ARG B 41  ? 1.02831 0.90137 1.05045 -0.06258 -0.05838 0.02825  41  ARG A NH2   
4193 N  N     . LYS B 42  ? 0.75027 0.68988 0.73700 -0.07196 -0.04017 0.04780  42  LYS A N     
4194 C  CA    . LYS B 42  ? 0.79188 0.74136 0.78598 -0.07688 -0.04138 0.05123  42  LYS A CA    
4195 C  C     . LYS B 42  ? 0.84500 0.79401 0.85197 -0.08208 -0.04970 0.04131  42  LYS A C     
4196 O  O     . LYS B 42  ? 0.82502 0.77572 0.82612 -0.08110 -0.05400 0.02821  42  LYS A O     
4197 C  CB    . LYS B 42  ? 0.79099 0.75264 0.77208 -0.07543 -0.03938 0.05050  42  LYS A CB    
4198 C  CG    . LYS B 42  ? 0.80500 0.77795 0.79270 -0.08015 -0.04249 0.05121  42  LYS A CG    
4199 C  CD    . LYS B 42  ? 0.80168 0.77851 0.79664 -0.08078 -0.03798 0.06473  42  LYS A CD    
4200 C  CE    . LYS B 42  ? 0.92819 0.91764 0.92940 -0.08478 -0.04136 0.06537  42  LYS A CE    
4201 N  NZ    . LYS B 42  ? 0.93475 0.93020 0.94347 -0.08446 -0.03631 0.07839  42  LYS A NZ    
4202 N  N     . GLN B 43  ? 0.82427 0.77177 0.84922 -0.08734 -0.05214 0.04737  43  GLN A N     
4203 C  CA    . GLN B 43  ? 0.78113 0.72760 0.82071 -0.09268 -0.06163 0.03776  43  GLN A CA    
4204 C  C     . GLN B 43  ? 0.79127 0.75212 0.82845 -0.09533 -0.06514 0.03345  43  GLN A C     
4205 O  O     . GLN B 43  ? 0.94663 0.91719 0.98159 -0.09570 -0.06054 0.04321  43  GLN A O     
4206 C  CB    . GLN B 43  ? 0.70397 0.64311 0.76693 -0.09814 -0.06373 0.04690  43  GLN A CB    
4207 C  CG    . GLN B 43  ? 0.78687 0.72293 0.86796 -0.10402 -0.07529 0.03642  43  GLN A CG    
4208 C  CD    . GLN B 43  ? 0.94692 0.87686 1.05458 -0.11069 -0.07758 0.04754  43  GLN A CD    
4209 O  OE1   . GLN B 43  ? 0.87398 0.79363 0.98760 -0.11001 -0.07357 0.05749  43  GLN A OE1   
4210 N  NE2   . GLN B 43  ? 0.94618 0.88311 1.07074 -0.11730 -0.08429 0.04670  43  GLN A NE2   
4211 N  N     . VAL B 44  ? 0.82933 0.79178 0.86660 -0.09644 -0.07370 0.01842  44  VAL A N     
4212 C  CA    . VAL B 44  ? 0.76081 0.73728 0.79319 -0.09813 -0.07806 0.01313  44  VAL A CA    
4213 C  C     . VAL B 44  ? 0.79079 0.76552 0.83100 -0.10041 -0.08983 -0.00296 44  VAL A C     
4214 O  O     . VAL B 44  ? 0.78884 0.75144 0.83531 -0.09948 -0.09383 -0.01138 44  VAL A O     
4215 C  CB    . VAL B 44  ? 0.75466 0.74059 0.76349 -0.09291 -0.07269 0.01147  44  VAL A CB    
4216 C  CG1   . VAL B 44  ? 0.74645 0.73137 0.74393 -0.08897 -0.07573 -0.00398 44  VAL A CG1   
4217 C  CG2   . VAL B 44  ? 1.11996 1.12085 1.12457 -0.09469 -0.07412 0.01454  44  VAL A CG2   
4218 N  N     . VAL B 45  ? 0.79862 0.78502 0.83881 -0.10290 -0.09626 -0.00786 45  VAL A N     
4219 C  CA    . VAL B 45  ? 0.87986 0.86608 0.92550 -0.10426 -0.10870 -0.02467 45  VAL A CA    
4220 C  C     . VAL B 45  ? 0.77864 0.77881 0.80130 -0.09970 -0.10995 -0.03489 45  VAL A C     
4221 O  O     . VAL B 45  ? 0.85960 0.87304 0.87474 -0.10045 -0.10847 -0.02854 45  VAL A O     
4222 C  CB    . VAL B 45  ? 0.77241 0.75998 0.84170 -0.11175 -0.11768 -0.02217 45  VAL A CB    
4223 C  CG1   . VAL B 45  ? 0.85718 0.85829 0.92671 -0.11415 -0.11287 -0.00779 45  VAL A CG1   
4224 C  CG2   . VAL B 45  ? 0.73859 0.72872 0.80924 -0.11212 -0.13173 -0.04118 45  VAL A CG2   
4225 N  N     . ILE B 46  ? 0.78722 0.78505 0.79904 -0.09457 -0.11243 -0.05008 46  ILE A N     
4226 C  CA    . ILE B 46  ? 0.81484 0.82689 0.80370 -0.08931 -0.11234 -0.05969 46  ILE A CA    
4227 C  C     . ILE B 46  ? 0.79790 0.81051 0.78838 -0.08784 -0.12510 -0.07987 46  ILE A C     
4228 O  O     . ILE B 46  ? 0.83972 0.83955 0.83944 -0.08620 -0.12986 -0.09096 46  ILE A O     
4229 C  CB    . ILE B 46  ? 0.84669 0.85878 0.81933 -0.08308 -0.10239 -0.05974 46  ILE A CB    
4230 C  CG1   . ILE B 46  ? 0.89952 0.90923 0.87147 -0.08418 -0.09133 -0.04106 46  ILE A CG1   
4231 C  CG2   . ILE B 46  ? 0.79274 0.82177 0.74280 -0.07796 -0.10148 -0.06800 46  ILE A CG2   
4232 C  CD1   . ILE B 46  ? 0.86715 0.87361 0.82863 -0.07891 -0.08283 -0.04050 46  ILE A CD1   
4233 N  N     . ASP B 47  ? 0.76881 0.79583 0.75036 -0.08791 -0.13138 -0.08495 47  ASP A N     
4234 C  CA    . ASP B 47  ? 0.76555 0.79538 0.74532 -0.08545 -0.14455 -0.10543 47  ASP A CA    
4235 C  C     . ASP B 47  ? 0.86656 0.87938 0.87332 -0.08993 -0.15596 -0.11313 47  ASP A C     
4236 O  O     . ASP B 47  ? 0.97799 0.98531 0.98622 -0.08626 -0.16573 -0.13240 47  ASP A O     
4237 C  CB    . ASP B 47  ? 0.86657 0.90194 0.82523 -0.07631 -0.14186 -0.12011 47  ASP A CB    
4238 C  CG    . ASP B 47  ? 0.92211 0.97585 0.85557 -0.07244 -0.13153 -0.11231 47  ASP A CG    
4239 O  OD1   . ASP B 47  ? 1.11973 1.18618 1.04635 -0.07476 -0.13313 -0.10528 47  ASP A OD1   
4240 O  OD2   . ASP B 47  ? 0.94660 1.00215 0.86859 -0.06725 -0.12215 -0.11257 47  ASP A OD2   
4241 N  N     . GLY B 48  ? 0.87545 0.88001 0.90454 -0.09763 -0.15478 -0.09787 48  GLY A N     
4242 C  CA    . GLY B 48  ? 0.84219 0.83136 0.90039 -0.10347 -0.16510 -0.10117 48  GLY A CA    
4243 C  C     . GLY B 48  ? 0.86837 0.83894 0.93960 -0.10373 -0.16018 -0.09657 48  GLY A C     
4244 O  O     . GLY B 48  ? 0.87764 0.83480 0.97587 -0.10978 -0.16716 -0.09432 48  GLY A O     
4245 N  N     . GLU B 49  ? 0.89469 0.86426 0.94887 -0.09759 -0.14888 -0.09434 49  GLU A N     
4246 C  CA    . GLU B 49  ? 0.90682 0.85912 0.97108 -0.09661 -0.14476 -0.09086 49  GLU A CA    
4247 C  C     . GLU B 49  ? 0.94187 0.89262 1.00994 -0.10009 -0.13237 -0.06752 49  GLU A C     
4248 O  O     . GLU B 49  ? 0.90083 0.86265 0.95049 -0.09744 -0.12190 -0.05872 49  GLU A O     
4249 C  CB    . GLU B 49  ? 0.81358 0.76579 0.85867 -0.08723 -0.14059 -0.10320 49  GLU A CB    
4250 C  CG    . GLU B 49  ? 0.81917 0.75391 0.87394 -0.08547 -0.13660 -0.09935 49  GLU A CG    
4251 C  CD    . GLU B 49  ? 0.96756 0.90528 1.00324 -0.07619 -0.12998 -0.10791 49  GLU A CD    
4252 O  OE1   . GLU B 49  ? 0.96710 0.92185 0.98088 -0.07241 -0.12331 -0.10848 49  GLU A OE1   
4253 O  OE2   . GLU B 49  ? 0.86957 0.79300 0.91349 -0.07274 -0.13160 -0.11342 49  GLU A OE2   
4254 N  N     . THR B 50  ? 0.87447 0.81167 0.96651 -0.10569 -0.13381 -0.05750 50  THR A N     
4255 C  CA    . THR B 50  ? 0.84762 0.78168 0.94222 -0.10721 -0.12185 -0.03669 50  THR A CA    
4256 C  C     . THR B 50  ? 0.83605 0.76096 0.91888 -0.10039 -0.11527 -0.03846 50  THR A C     
4257 O  O     . THR B 50  ? 1.02106 0.93096 1.11506 -0.09931 -0.12076 -0.04551 50  THR A O     
4258 C  CB    . THR B 50  ? 0.76224 0.68661 0.88634 -0.11520 -0.12512 -0.02435 50  THR A CB    
4259 O  OG1   . THR B 50  ? 0.93159 0.86603 1.06839 -0.12161 -0.13177 -0.02311 50  THR A OG1   
4260 C  CG2   . THR B 50  ? 0.69130 0.61442 0.81507 -0.11541 -0.11197 -0.00288 50  THR A CG2   
4261 N  N     . CYS B 51  ? 0.85674 0.79033 0.91840 -0.09573 -0.10436 -0.03228 51  CYS A N     
4262 C  CA    . CYS B 51  ? 0.83243 0.75970 0.88239 -0.08908 -0.09832 -0.03417 51  CYS A CA    
4263 C  C     . CYS B 51  ? 0.76816 0.69779 0.80949 -0.08805 -0.08644 -0.01643 51  CYS A C     
4264 O  O     . CYS B 51  ? 0.86642 0.80508 0.90662 -0.09112 -0.08228 -0.00501 51  CYS A O     
4265 C  CB    . CYS B 51  ? 0.87260 0.80959 0.90304 -0.08258 -0.09877 -0.05023 51  CYS A CB    
4266 S  SG    . CYS B 51  ? 0.91177 0.87106 0.92185 -0.08243 -0.09382 -0.04715 51  CYS A SG    
4267 N  N     . LEU B 52  ? 0.76151 0.68294 0.79687 -0.08301 -0.08165 -0.01502 52  LEU A N     
4268 C  CA    . LEU B 52  ? 0.79134 0.71279 0.81797 -0.08074 -0.07167 -0.00019 52  LEU A CA    
4269 C  C     . LEU B 52  ? 0.85245 0.78202 0.85872 -0.07470 -0.06665 -0.00568 52  LEU A C     
4270 O  O     . LEU B 52  ? 0.87701 0.80343 0.87979 -0.07026 -0.06866 -0.01717 52  LEU A O     
4271 C  CB    . LEU B 52  ? 0.81940 0.72474 0.85652 -0.07986 -0.07088 0.00747  52  LEU A CB    
4272 C  CG    . LEU B 52  ? 0.99949 0.90335 1.03698 -0.08048 -0.06303 0.02680  52  LEU A CG    
4273 C  CD1   . LEU B 52  ? 1.10690 0.99549 1.16095 -0.08208 -0.06503 0.03484  52  LEU A CD1   
4274 C  CD2   . LEU B 52  ? 0.94888 0.85619 0.96666 -0.07403 -0.05530 0.03032  52  LEU A CD2   
4275 N  N     . LEU B 53  ? 0.76517 0.70559 0.75967 -0.07451 -0.06045 0.00253  53  LEU A N     
4276 C  CA    . LEU B 53  ? 0.74077 0.68937 0.71828 -0.06986 -0.05569 -0.00024 53  LEU A CA    
4277 C  C     . LEU B 53  ? 0.84071 0.78196 0.81356 -0.06596 -0.04968 0.00896  53  LEU A C     
4278 O  O     . LEU B 53  ? 0.83515 0.77358 0.80951 -0.06682 -0.04601 0.02162  53  LEU A O     
4279 C  CB    . LEU B 53  ? 0.72569 0.68914 0.69381 -0.07167 -0.05352 0.00348  53  LEU A CB    
4280 C  CG    . LEU B 53  ? 0.71522 0.68852 0.68457 -0.07485 -0.05972 -0.00526 53  LEU A CG    
4281 C  CD1   . LEU B 53  ? 0.69551 0.68349 0.65328 -0.07546 -0.05697 -0.00033 53  LEU A CD1   
4282 C  CD2   . LEU B 53  ? 0.90205 0.87617 0.86879 -0.07183 -0.06429 -0.02180 53  LEU A CD2   
4283 N  N     . ASP B 54  ? 0.76499 0.70413 0.73217 -0.06114 -0.04889 0.00224  54  ASP A N     
4284 C  CA    . ASP B 54  ? 0.79739 0.73013 0.75949 -0.05681 -0.04457 0.00908  54  ASP A CA    
4285 C  C     . ASP B 54  ? 0.75353 0.69743 0.70296 -0.05442 -0.04076 0.00811  54  ASP A C     
4286 O  O     . ASP B 54  ? 0.82801 0.77666 0.77456 -0.05169 -0.04114 -0.00110 54  ASP A O     
4287 C  CB    . ASP B 54  ? 0.75711 0.67786 0.72584 -0.05322 -0.04753 0.00324  54  ASP A CB    
4288 C  CG    . ASP B 54  ? 0.99229 0.90275 0.95944 -0.04974 -0.04477 0.01344  54  ASP A CG    
4289 O  OD1   . ASP B 54  ? 0.98152 0.89602 0.93827 -0.04671 -0.04093 0.01734  54  ASP A OD1   
4290 O  OD2   . ASP B 54  ? 1.20904 1.10734 1.18555 -0.05002 -0.04693 0.01792  54  ASP A OD2   
4291 N  N     . ILE B 55  ? 0.75572 0.70414 0.69888 -0.05531 -0.03716 0.01791  55  ILE A N     
4292 C  CA    . ILE B 55  ? 0.76553 0.72445 0.69895 -0.05436 -0.03437 0.01878  55  ILE A CA    
4293 C  C     . ILE B 55  ? 0.78966 0.74245 0.71883 -0.04992 -0.03206 0.02337  55  ILE A C     
4294 O  O     . ILE B 55  ? 0.73568 0.67977 0.66454 -0.04813 -0.03096 0.03127  55  ILE A O     
4295 C  CB    . ILE B 55  ? 0.76133 0.72835 0.69163 -0.05766 -0.03322 0.02592  55  ILE A CB    
4296 C  CG1   . ILE B 55  ? 0.75459 0.72834 0.68930 -0.06192 -0.03680 0.02057  55  ILE A CG1   
4297 C  CG2   . ILE B 55  ? 0.74827 0.72455 0.67007 -0.05690 -0.03093 0.02831  55  ILE A CG2   
4298 C  CD1   . ILE B 55  ? 0.85709 0.84127 0.78844 -0.06486 -0.03652 0.02619  55  ILE A CD1   
4299 N  N     . LEU B 56  ? 0.79801 0.75633 0.72414 -0.04786 -0.03146 0.01845  56  LEU A N     
4300 C  CA    . LEU B 56  ? 0.74310 0.69718 0.66639 -0.04398 -0.03053 0.02171  56  LEU A CA    
4301 C  C     . LEU B 56  ? 0.78375 0.74755 0.70196 -0.04539 -0.02881 0.02598  56  LEU A C     
4302 O  O     . LEU B 56  ? 0.73542 0.71151 0.65313 -0.04737 -0.02787 0.02230  56  LEU A O     
4303 C  CB    . LEU B 56  ? 0.75950 0.71235 0.68680 -0.04059 -0.03174 0.01350  56  LEU A CB    
4304 C  CG    . LEU B 56  ? 0.95193 0.89410 0.87964 -0.03566 -0.03304 0.01588  56  LEU A CG    
4305 C  CD1   . LEU B 56  ? 1.01370 0.95616 0.94757 -0.03236 -0.03465 0.00684  56  LEU A CD1   
4306 C  CD2   . LEU B 56  ? 0.84038 0.78442 0.76310 -0.03462 -0.03243 0.02189  56  LEU A CD2   
4307 N  N     . ASP B 57  ? 0.75253 0.71103 0.66711 -0.04398 -0.02853 0.03390  57  ASP A N     
4308 C  CA    . ASP B 57  ? 0.73983 0.70464 0.65125 -0.04511 -0.02807 0.03884  57  ASP A CA    
4309 C  C     . ASP B 57  ? 0.76124 0.72253 0.67346 -0.04186 -0.02954 0.03852  57  ASP A C     
4310 O  O     . ASP B 57  ? 0.93122 0.88156 0.84133 -0.03752 -0.03122 0.04052  57  ASP A O     
4311 C  CB    . ASP B 57  ? 0.72087 0.68193 0.62893 -0.04481 -0.02773 0.04647  57  ASP A CB    
4312 C  CG    . ASP B 57  ? 0.85583 0.82385 0.76212 -0.04669 -0.02798 0.05138  57  ASP A CG    
4313 O  OD1   . ASP B 57  ? 0.87470 0.85260 0.78230 -0.04971 -0.02782 0.05000  57  ASP A OD1   
4314 O  OD2   . ASP B 57  ? 0.89962 0.86358 0.80350 -0.04478 -0.02827 0.05704  57  ASP A OD2   
4315 N  N     . THR B 58  ? 0.82443 0.79590 0.73998 -0.04376 -0.02907 0.03621  58  THR A N     
4316 C  CA    . THR B 58  ? 0.84976 0.81966 0.76953 -0.04139 -0.03094 0.03524  58  THR A CA    
4317 C  C     . THR B 58  ? 0.81447 0.78575 0.73504 -0.04275 -0.03266 0.04185  58  THR A C     
4318 O  O     . THR B 58  ? 0.85947 0.83252 0.77679 -0.04501 -0.03225 0.04726  58  THR A O     
4319 C  CB    . THR B 58  ? 0.67209 0.65338 0.59789 -0.04222 -0.02913 0.02892  58  THR A CB    
4320 O  OG1   . THR B 58  ? 0.76196 0.75875 0.68805 -0.04673 -0.02625 0.03146  58  THR A OG1   
4321 C  CG2   . THR B 58  ? 0.86516 0.84441 0.79099 -0.04065 -0.02839 0.02128  58  THR A CG2   
4322 N  N     . ALA B 59  ? 0.90297 0.87315 0.82952 -0.04131 -0.03538 0.04127  59  ALA A N     
4323 C  CA    . ALA B 59  ? 0.71380 0.68285 0.64405 -0.04237 -0.03880 0.04676  59  ALA A CA    
4324 C  C     . ALA B 59  ? 0.74268 0.72752 0.68048 -0.04817 -0.03645 0.05057  59  ALA A C     
4325 O  O     . ALA B 59  ? 0.91015 0.90712 0.85196 -0.04973 -0.03276 0.04726  59  ALA A O     
4326 C  CB    . ALA B 59  ? 0.76039 0.71983 0.69481 -0.03795 -0.04431 0.04417  59  ALA A CB    
4327 N  N     . GLY B 60  ? 0.75467 0.73967 0.69461 -0.05090 -0.03860 0.05792  60  GLY A N     
4328 C  CA    . GLY B 60  ? 0.83488 0.83423 0.78308 -0.05664 -0.03684 0.06423  60  GLY A CA    
4329 C  C     . GLY B 60  ? 0.76301 0.75973 0.72416 -0.05760 -0.04197 0.06737  60  GLY A C     
4330 O  O     . GLY B 60  ? 0.89920 0.90921 0.87123 -0.06141 -0.03989 0.07019  60  GLY A O     
4331 N  N     . ARG B 61  ? 0.83317 0.81348 0.79381 -0.05393 -0.04888 0.06680  61  ARG A N     
4332 C  CA    . ARG B 61  ? 0.77927 0.75432 0.75275 -0.05404 -0.05590 0.06778  61  ARG A CA    
4333 C  C     . ARG B 61  ? 0.88699 0.86384 0.86619 -0.05154 -0.05639 0.06087  61  ARG A C     
4334 O  O     . ARG B 61  ? 0.86919 0.84120 0.83919 -0.04664 -0.05472 0.05390  61  ARG A O     
4335 C  CB    . ARG B 61  ? 0.75076 0.70707 0.71970 -0.04888 -0.06387 0.06637  61  ARG A CB    
4336 C  CG    . ARG B 61  ? 0.68260 0.63619 0.64753 -0.05029 -0.06432 0.07274  61  ARG A CG    
4337 C  CD    . ARG B 61  ? 0.79245 0.72806 0.75222 -0.04341 -0.07200 0.06951  61  ARG A CD    
4338 N  NE    . ARG B 61  ? 0.81660 0.74392 0.78824 -0.04245 -0.08146 0.06763  61  ARG A NE    
4339 C  CZ    . ARG B 61  ? 0.89670 0.82063 0.88089 -0.04575 -0.08805 0.07295  61  ARG A CZ    
4340 N  NH1   . ARG B 61  ? 0.83465 0.76271 0.82048 -0.04991 -0.08603 0.08121  61  ARG A NH1   
4341 N  NH2   . ARG B 61  ? 0.79650 0.71228 0.79287 -0.04486 -0.09773 0.07007  61  ARG A NH2   
4342 N  N     . GLU B 62  ? 0.82098 0.80502 0.81705 -0.05504 -0.05901 0.06349  62  GLU A N     
4343 C  CA    . GLU B 62  ? 0.80797 0.79750 0.81209 -0.05311 -0.05876 0.05755  62  GLU A CA    
4344 C  C     . GLU B 62  ? 0.83300 0.80506 0.83265 -0.04567 -0.06660 0.04971  62  GLU A C     
4345 O  O     . GLU B 62  ? 0.93960 0.91111 0.93546 -0.04128 -0.06509 0.04299  62  GLU A O     
4346 C  CB    . GLU B 62  ? 0.90242 0.90571 0.92810 -0.05903 -0.05956 0.06342  62  GLU A CB    
4347 C  CG    . GLU B 62  ? 1.13854 1.15819 1.17292 -0.05879 -0.05397 0.05956  62  GLU A CG    
4348 C  CD    . GLU B 62  ? 1.38810 1.42211 1.41190 -0.05926 -0.04315 0.05846  62  GLU A CD    
4349 O  OE1   . GLU B 62  ? 1.22833 1.26702 1.24454 -0.06295 -0.03910 0.06473  62  GLU A OE1   
4350 O  OE2   . GLU B 62  ? 1.37498 1.41523 1.39825 -0.05547 -0.03948 0.05077  62  GLU A OE2   
4351 N  N     . GLU B 63  ? 0.74421 0.70172 0.74375 -0.04353 -0.07545 0.05027  63  GLU A N     
4352 C  CA    . GLU B 63  ? 0.84879 0.79045 0.84200 -0.03550 -0.08342 0.04278  63  GLU A CA    
4353 C  C     . GLU B 63  ? 0.85029 0.78428 0.82329 -0.02931 -0.07926 0.03875  63  GLU A C     
4354 O  O     . GLU B 63  ? 0.93162 0.85768 0.89881 -0.02286 -0.08251 0.03300  63  GLU A O     
4355 C  CB    . GLU B 63  ? 0.78803 0.71582 0.78327 -0.03351 -0.09393 0.04312  63  GLU A CB    
4356 C  CG    . GLU B 63  ? 0.89761 0.83131 0.90763 -0.04141 -0.09519 0.05148  63  GLU A CG    
4357 C  CD    . GLU B 63  ? 0.86850 0.80175 0.86771 -0.04300 -0.09001 0.05694  63  GLU A CD    
4358 O  OE1   . GLU B 63  ? 0.80947 0.72935 0.79425 -0.03655 -0.09278 0.05359  63  GLU A OE1   
4359 O  OE2   . GLU B 63  ? 0.96107 0.90837 0.96600 -0.05022 -0.08308 0.06469  63  GLU A OE2   
4360 N  N     . TYR B 64  ? 0.89246 0.82889 0.85557 -0.03127 -0.07253 0.04245  64  TYR A N     
4361 C  CA    . TYR B 64  ? 0.79104 0.72300 0.73858 -0.02709 -0.06755 0.04006  64  TYR A CA    
4362 C  C     . TYR B 64  ? 1.02042 0.96251 0.97007 -0.02881 -0.06102 0.03730  64  TYR A C     
4363 O  O     . TYR B 64  ? 0.95977 0.89652 0.90007 -0.02492 -0.05870 0.03436  64  TYR A O     
4364 C  CB    . TYR B 64  ? 0.70974 0.64170 0.64847 -0.02886 -0.06341 0.04491  64  TYR A CB    
4365 C  CG    . TYR B 64  ? 0.80136 0.72182 0.73520 -0.02506 -0.06929 0.04641  64  TYR A CG    
4366 C  CD1   . TYR B 64  ? 0.75021 0.66897 0.69496 -0.02735 -0.07597 0.04857  64  TYR A CD1   
4367 C  CD2   . TYR B 64  ? 0.81800 0.72992 0.73739 -0.01902 -0.06811 0.04582  64  TYR A CD2   
4368 C  CE1   . TYR B 64  ? 0.77594 0.68322 0.71661 -0.02297 -0.08221 0.04851  64  TYR A CE1   
4369 C  CE2   . TYR B 64  ? 0.77815 0.68067 0.69254 -0.01423 -0.07311 0.04610  64  TYR A CE2   
4370 C  CZ    . TYR B 64  ? 0.84844 0.74795 0.77313 -0.01587 -0.08055 0.04669  64  TYR A CZ    
4371 O  OH    . TYR B 64  ? 0.93403 0.82310 0.85406 -0.01016 -0.08642 0.04557  64  TYR A OH    
4372 N  N     . SER B 65  ? 0.96787 0.92468 0.93024 -0.03418 -0.05814 0.03831  65  SER A N     
4373 C  CA    . SER B 65  ? 0.92068 0.88963 0.88465 -0.03576 -0.05117 0.03523  65  SER A CA    
4374 C  C     . SER B 65  ? 1.00092 0.96912 0.97084 -0.03139 -0.05314 0.02848  65  SER A C     
4375 O  O     . SER B 65  ? 1.09149 1.07180 1.06704 -0.03230 -0.04829 0.02500  65  SER A O     
4376 C  CB    . SER B 65  ? 1.12984 1.11748 1.10320 -0.04259 -0.04613 0.03980  65  SER A CB    
4377 O  OG    . SER B 65  ? 1.27591 1.27125 1.24068 -0.04488 -0.03941 0.04028  65  SER A OG    
4378 N  N     . ALA B 66  ? 1.03519 0.99002 1.00381 -0.02599 -0.06048 0.02617  66  ALA A N     
4379 C  CA    . ALA B 66  ? 1.06384 1.01604 1.03593 -0.02087 -0.06278 0.02004  66  ALA A CA    
4380 C  C     . ALA B 66  ? 1.13619 1.08455 1.09828 -0.01844 -0.05803 0.01721  66  ALA A C     
4381 O  O     . ALA B 66  ? 1.12271 1.06411 1.07265 -0.01853 -0.05588 0.02009  66  ALA A O     
4382 C  CB    . ALA B 66  ? 0.96379 0.90159 0.93350 -0.01485 -0.07234 0.01854  66  ALA A CB    
4383 N  N     . MET B 67  ? 1.04756 1.00104 1.01666 -0.01636 -0.05663 0.01158  67  MET A N     
4384 C  CA    . MET B 67  ? 1.09271 1.04314 1.05658 -0.01440 -0.05303 0.00779  67  MET A CA    
4385 C  C     . MET B 67  ? 1.14008 1.10128 1.10156 -0.01953 -0.04581 0.00774  67  MET A C     
4386 O  O     . MET B 67  ? 1.18927 1.14564 1.14490 -0.01894 -0.04372 0.00563  67  MET A O     
4387 C  CB    . MET B 67  ? 1.05342 0.98613 1.00449 -0.01025 -0.05578 0.01031  67  MET A CB    
4388 C  CG    . MET B 67  ? 1.11598 1.03782 1.06766 -0.00333 -0.06197 0.00815  67  MET A CG    
4389 S  SD    . MET B 67  ? 1.36777 1.27223 1.30364 0.00080  -0.06262 0.01330  67  MET A SD    
4390 C  CE    . MET B 67  ? 1.11929 1.02763 1.05652 -0.00384 -0.05560 0.01198  67  MET A CE    
4391 N  N     . ARG B 68  ? 1.16485 1.14067 1.13111 -0.02464 -0.04245 0.01042  68  ARG A N     
4392 C  CA    . ARG B 68  ? 1.12335 1.11030 1.08566 -0.02883 -0.03615 0.01030  68  ARG A CA    
4393 C  C     . ARG B 68  ? 1.12923 1.12569 1.09618 -0.02667 -0.03273 0.00147  68  ARG A C     
4394 O  O     . ARG B 68  ? 1.18679 1.18643 1.14790 -0.02784 -0.02952 -0.00170 68  ARG A O     
4395 C  CB    . ARG B 68  ? 1.20281 1.20347 1.16859 -0.03454 -0.03350 0.01689  68  ARG A CB    
4396 C  CG    . ARG B 68  ? 1.25511 1.26687 1.21419 -0.03866 -0.02782 0.01821  68  ARG A CG    
4397 C  CD    . ARG B 68  ? 1.16717 1.18741 1.12734 -0.04425 -0.02662 0.02770  68  ARG A CD    
4398 N  NE    . ARG B 68  ? 1.16304 1.19754 1.13635 -0.04626 -0.02528 0.03048  68  ARG A NE    
4399 C  CZ    . ARG B 68  ? 1.18936 1.23084 1.16833 -0.05133 -0.02527 0.03990  68  ARG A CZ    
4400 N  NH1   . ARG B 68  ? 0.98090 1.01579 0.95297 -0.05428 -0.02692 0.04676  68  ARG A NH1   
4401 N  NH2   . ARG B 68  ? 1.24728 1.30296 1.24071 -0.05348 -0.02372 0.04298  68  ARG A NH2   
4402 N  N     . ASP B 69  ? 1.16080 1.16179 1.13877 -0.02297 -0.03404 -0.00334 69  ASP A N     
4403 C  CA    . ASP B 69  ? 1.06234 1.07246 1.04553 -0.01949 -0.03110 -0.01300 69  ASP A CA    
4404 C  C     . ASP B 69  ? 0.94150 0.93615 0.91904 -0.01590 -0.03367 -0.01865 69  ASP A C     
4405 O  O     . ASP B 69  ? 1.02702 1.02670 1.00318 -0.01510 -0.03108 -0.02587 69  ASP A O     
4406 C  CB    . ASP B 69  ? 1.06810 1.08577 1.06599 -0.01559 -0.03255 -0.01660 69  ASP A CB    
4407 C  CG    . ASP B 69  ? 1.13914 1.18079 1.14639 -0.01878 -0.02683 -0.01437 69  ASP A CG    
4408 O  OD1   . ASP B 69  ? 1.19744 1.24863 1.19849 -0.02408 -0.02219 -0.00907 69  ASP A OD1   
4409 O  OD2   . ASP B 69  ? 1.22137 1.27318 1.24288 -0.01593 -0.02689 -0.01719 69  ASP A OD2   
4410 N  N     . GLN B 70  ? 0.88015 0.85607 0.85465 -0.01352 -0.03912 -0.01531 70  GLN A N     
4411 C  CA    . GLN B 70  ? 0.92857 0.88949 0.89996 -0.01049 -0.04173 -0.01859 70  GLN A CA    
4412 C  C     . GLN B 70  ? 0.96879 0.92721 0.93130 -0.01488 -0.03927 -0.01662 70  GLN A C     
4413 O  O     . GLN B 70  ? 0.99699 0.95176 0.96065 -0.01401 -0.03964 -0.02267 70  GLN A O     
4414 C  CB    . GLN B 70  ? 1.00760 0.95091 0.97656 -0.00679 -0.04753 -0.01345 70  GLN A CB    
4415 C  CG    . GLN B 70  ? 0.93714 0.86429 0.90342 -0.00429 -0.05011 -0.01362 70  GLN A CG    
4416 C  CD    . GLN B 70  ? 1.02104 0.94789 0.99760 -0.00002 -0.05176 -0.02343 70  GLN A CD    
4417 O  OE1   . GLN B 70  ? 1.00917 0.94735 0.99479 0.00271  -0.05135 -0.03019 70  GLN A OE1   
4418 N  NE2   . GLN B 70  ? 1.09682 1.01089 1.07342 0.00073  -0.05382 -0.02408 70  GLN A NE2   
4419 N  N     . TYR B 71  ? 1.06177 1.02184 1.01672 -0.01947 -0.03752 -0.00853 71  TYR A N     
4420 C  CA    . TYR B 71  ? 0.95361 0.91341 0.90145 -0.02376 -0.03536 -0.00632 71  TYR A CA    
4421 C  C     . TYR B 71  ? 0.97291 0.94748 0.92218 -0.02551 -0.03205 -0.01404 71  TYR A C     
4422 O  O     . TYR B 71  ? 0.92322 0.89470 0.87106 -0.02639 -0.03265 -0.01833 71  TYR A O     
4423 C  CB    . TYR B 71  ? 0.92626 0.88694 0.86710 -0.02753 -0.03425 0.00331  71  TYR A CB    
4424 C  CG    . TYR B 71  ? 1.11980 1.06619 1.05683 -0.02467 -0.03769 0.00983  71  TYR A CG    
4425 C  CD1   . TYR B 71  ? 1.10325 1.03543 1.03909 -0.02094 -0.04027 0.01016  71  TYR A CD1   
4426 C  CD2   . TYR B 71  ? 1.02459 0.97169 0.95915 -0.02525 -0.03877 0.01565  71  TYR A CD2   
4427 C  CE1   . TYR B 71  ? 1.06861 0.98925 0.99873 -0.01732 -0.04308 0.01620  71  TYR A CE1   
4428 C  CE2   . TYR B 71  ? 0.98185 0.91630 0.91125 -0.02134 -0.04246 0.02004  71  TYR A CE2   
4429 C  CZ    . TYR B 71  ? 1.13008 1.05211 1.05619 -0.01710 -0.04423 0.02033  71  TYR A CZ    
4430 O  OH    . TYR B 71  ? 1.15770 1.06860 1.07648 -0.01227 -0.04754 0.02487  71  TYR A OH    
4431 N  N     . MET B 72  ? 0.88139 0.87275 0.83387 -0.02581 -0.02878 -0.01590 72  MET A N     
4432 C  CA    . MET B 72  ? 0.79515 0.80290 0.74725 -0.02607 -0.02509 -0.02362 72  MET A CA    
4433 C  C     . MET B 72  ? 0.93271 0.93769 0.89061 -0.02051 -0.02698 -0.03615 72  MET A C     
4434 O  O     . MET B 72  ? 0.98948 1.00145 0.94489 -0.01989 -0.02610 -0.04461 72  MET A O     
4435 C  CB    . MET B 72  ? 0.87681 0.90462 0.83215 -0.02719 -0.02036 -0.02114 72  MET A CB    
4436 C  CG    . MET B 72  ? 1.03391 1.06584 0.98486 -0.03301 -0.01885 -0.00909 72  MET A CG    
4437 S  SD    . MET B 72  ? 1.07567 1.13129 1.03418 -0.03494 -0.01350 -0.00451 72  MET A SD    
4438 C  CE    . MET B 72  ? 1.08092 1.13693 1.03367 -0.04208 -0.01338 0.00965  72  MET A CE    
4439 N  N     . ARG B 73  ? 0.92381 0.91824 0.88945 -0.01592 -0.03039 -0.03799 73  ARG A N     
4440 C  CA    . ARG B 73  ? 0.95722 0.94908 0.93039 -0.00984 -0.03268 -0.05007 73  ARG A CA    
4441 C  C     . ARG B 73  ? 0.99293 0.96984 0.96449 -0.01016 -0.03687 -0.05420 73  ARG A C     
4442 O  O     . ARG B 73  ? 0.99656 0.97464 0.97242 -0.00636 -0.03853 -0.06626 73  ARG A O     
4443 C  CB    . ARG B 73  ? 0.95229 0.93609 0.93469 -0.00483 -0.03610 -0.04968 73  ARG A CB    
4444 C  CG    . ARG B 73  ? 0.95696 0.94129 0.94953 0.00248  -0.03816 -0.06234 73  ARG A CG    
4445 C  CD    . ARG B 73  ? 0.89026 0.87130 0.89286 0.00744  -0.04116 -0.06132 73  ARG A CD    
4446 N  NE    . ARG B 73  ? 0.92620 0.92623 0.93321 0.00652  -0.03683 -0.05837 73  ARG A NE    
4447 C  CZ    . ARG B 73  ? 1.02654 1.02500 1.03285 0.00326  -0.03782 -0.04800 73  ARG A CZ    
4448 N  NH1   . ARG B 73  ? 1.01856 0.99838 1.01776 0.00159  -0.04240 -0.04003 73  ARG A NH1   
4449 N  NH2   . ARG B 73  ? 1.04829 1.06477 1.06183 0.00195  -0.03432 -0.04561 73  ARG A NH2   
4450 N  N     . THR B 74  ? 0.95388 0.91737 0.92035 -0.01447 -0.03875 -0.04458 74  THR A N     
4451 C  CA    . THR B 74  ? 0.95440 0.90354 0.92219 -0.01575 -0.04287 -0.04618 74  THR A CA    
4452 C  C     . THR B 74  ? 1.08307 1.03949 1.04506 -0.02074 -0.04173 -0.04792 74  THR A C     
4453 O  O     . THR B 74  ? 1.12413 1.07174 1.08991 -0.02169 -0.04585 -0.05259 74  THR A O     
4454 C  CB    . THR B 74  ? 0.97306 0.90487 0.93961 -0.01719 -0.04514 -0.03402 74  THR A CB    
4455 O  OG1   . THR B 74  ? 0.90401 0.84081 0.86165 -0.02122 -0.04166 -0.02352 74  THR A OG1   
4456 C  CG2   . THR B 74  ? 1.01062 0.93323 0.98264 -0.01145 -0.04801 -0.03314 74  THR A CG2   
4457 N  N     . GLY B 75  ? 0.98226 0.95415 0.93625 -0.02402 -0.03704 -0.04400 75  GLY A N     
4458 C  CA    . GLY B 75  ? 0.87888 0.85780 0.82662 -0.02858 -0.03659 -0.04451 75  GLY A CA    
4459 C  C     . GLY B 75  ? 0.85894 0.84764 0.80703 -0.02579 -0.03783 -0.05932 75  GLY A C     
4460 O  O     . GLY B 75  ? 0.95661 0.95357 0.90760 -0.02029 -0.03644 -0.06850 75  GLY A O     
4461 N  N     . GLU B 76  ? 0.85573 0.84408 0.80108 -0.02913 -0.04082 -0.06219 76  GLU A N     
4462 C  CA    . GLU B 76  ? 0.75874 0.75692 0.70205 -0.02634 -0.04305 -0.07709 76  GLU A CA    
4463 C  C     . GLU B 76  ? 0.72980 0.74826 0.66071 -0.02868 -0.03929 -0.07592 76  GLU A C     
4464 O  O     . GLU B 76  ? 0.91444 0.94753 0.84011 -0.02452 -0.03858 -0.08763 76  GLU A O     
4465 C  CB    . GLU B 76  ? 0.79605 0.77912 0.74673 -0.02790 -0.05119 -0.08346 76  GLU A CB    
4466 C  CG    . GLU B 76  ? 0.80522 0.76687 0.76886 -0.02652 -0.05543 -0.08199 76  GLU A CG    
4467 C  CD    . GLU B 76  ? 1.11352 1.06087 1.08726 -0.02858 -0.06396 -0.08809 76  GLU A CD    
4468 O  OE1   . GLU B 76  ? 1.16665 1.11870 1.14091 -0.02577 -0.06857 -0.10350 76  GLU A OE1   
4469 O  OE2   . GLU B 76  ? 1.03863 0.97061 1.02012 -0.03288 -0.06622 -0.07741 76  GLU A OE2   
4470 N  N     . GLY B 77  ? 0.75205 0.77191 0.67787 -0.03458 -0.03705 -0.06215 77  GLY A N     
4471 C  CA    . GLY B 77  ? 0.80397 0.84247 0.71843 -0.03700 -0.03355 -0.05839 77  GLY A CA    
4472 C  C     . GLY B 77  ? 0.76512 0.80527 0.67735 -0.04093 -0.02890 -0.04209 77  GLY A C     
4473 O  O     . GLY B 77  ? 0.80439 0.82964 0.72199 -0.04274 -0.02980 -0.03376 77  GLY A O     
4474 N  N     . PHE B 78  ? 0.71444 0.77306 0.61861 -0.04189 -0.02417 -0.03748 78  PHE A N     
4475 C  CA    . PHE B 78  ? 0.75382 0.81498 0.65772 -0.04507 -0.02017 -0.02302 78  PHE A CA    
4476 C  C     . PHE B 78  ? 0.74853 0.82128 0.64355 -0.04937 -0.01918 -0.01457 78  PHE A C     
4477 O  O     . PHE B 78  ? 0.88671 0.97628 0.77359 -0.04842 -0.01778 -0.01901 78  PHE A O     
4478 C  CB    . PHE B 78  ? 0.74897 0.82120 0.65638 -0.04207 -0.01496 -0.02306 78  PHE A CB    
4479 C  CG    . PHE B 78  ? 0.80416 0.86467 0.72130 -0.03761 -0.01643 -0.02987 78  PHE A CG    
4480 C  CD1   . PHE B 78  ? 0.74971 0.81186 0.66911 -0.03214 -0.01771 -0.04448 78  PHE A CD1   
4481 C  CD2   . PHE B 78  ? 0.80414 0.85145 0.72795 -0.03826 -0.01735 -0.02215 78  PHE A CD2   
4482 C  CE1   . PHE B 78  ? 0.85500 0.90571 0.78418 -0.02773 -0.01971 -0.05021 78  PHE A CE1   
4483 C  CE2   . PHE B 78  ? 0.73460 0.77121 0.66677 -0.03384 -0.01938 -0.02777 78  PHE A CE2   
4484 C  CZ    . PHE B 78  ? 0.87002 0.90820 0.80540 -0.02875 -0.02050 -0.04129 78  PHE A CZ    
4485 N  N     . LEU B 79  ? 0.67893 0.74289 0.57505 -0.05335 -0.02015 -0.00262 79  LEU A N     
4486 C  CA    . LEU B 79  ? 0.79587 0.86934 0.68559 -0.05728 -0.01937 0.00780  79  LEU A CA    
4487 C  C     . LEU B 79  ? 0.83922 0.91895 0.73135 -0.05839 -0.01512 0.01809  79  LEU A C     
4488 O  O     . LEU B 79  ? 0.91052 0.97795 0.80880 -0.05910 -0.01587 0.02475  79  LEU A O     
4489 C  CB    . LEU B 79  ? 0.72919 0.78999 0.62028 -0.06029 -0.02326 0.01429  79  LEU A CB    
4490 C  CG    . LEU B 79  ? 0.68982 0.74977 0.57887 -0.06136 -0.02796 0.00810  79  LEU A CG    
4491 C  CD1   . LEU B 79  ? 0.72569 0.77795 0.61701 -0.06456 -0.03034 0.01770  79  LEU A CD1   
4492 C  CD2   . LEU B 79  ? 0.83754 0.91609 0.71688 -0.06110 -0.02812 0.00323  79  LEU A CD2   
4493 N  N     . CYS B 80  ? 0.78047 0.87982 0.66816 -0.05838 -0.01092 0.01948  80  CYS A N     
4494 C  CA    . CYS B 80  ? 0.79192 0.89949 0.68397 -0.06054 -0.00704 0.03083  80  CYS A CA    
4495 C  C     . CYS B 80  ? 0.75630 0.86581 0.64459 -0.06511 -0.00843 0.04400  80  CYS A C     
4496 O  O     . CYS B 80  ? 0.85021 0.97339 0.72919 -0.06612 -0.00783 0.04582  80  CYS A O     
4497 C  CB    . CYS B 80  ? 0.82174 0.95123 0.71219 -0.05836 -0.00099 0.02773  80  CYS A CB    
4498 S  SG    . CYS B 80  ? 0.90066 1.02790 0.79750 -0.05186 0.00025  0.01160  80  CYS A SG    
4499 N  N     . VAL B 81  ? 0.69728 0.79291 0.59245 -0.06716 -0.01092 0.05267  81  VAL A N     
4500 C  CA    . VAL B 81  ? 0.79933 0.89181 0.69262 -0.07046 -0.01375 0.06373  81  VAL A CA    
4501 C  C     . VAL B 81  ? 0.92171 1.01910 0.82179 -0.07360 -0.01246 0.07666  81  VAL A C     
4502 O  O     . VAL B 81  ? 1.00322 1.09593 0.91285 -0.07326 -0.01187 0.07733  81  VAL A O     
4503 C  CB    . VAL B 81  ? 0.84291 0.91487 0.73884 -0.06945 -0.01832 0.06293  81  VAL A CB    
4504 C  CG1   . VAL B 81  ? 0.85317 0.92383 0.74672 -0.07179 -0.02130 0.07242  81  VAL A CG1   
4505 C  CG2   . VAL B 81  ? 0.70257 0.76813 0.59607 -0.06682 -0.01953 0.05085  81  VAL A CG2   
4506 N  N     . PHE B 82  ? 0.89166 0.99821 0.78789 -0.07679 -0.01278 0.08728  82  PHE A N     
4507 C  CA    . PHE B 82  ? 0.85377 0.96178 0.75811 -0.08052 -0.01329 0.10161  82  PHE A CA    
4508 C  C     . PHE B 82  ? 0.90098 1.00422 0.80219 -0.08229 -0.01779 0.11048  82  PHE A C     
4509 O  O     . PHE B 82  ? 0.86064 0.96611 0.75236 -0.08126 -0.01921 0.10674  82  PHE A O     
4510 C  CB    . PHE B 82  ? 0.89409 1.02456 0.79911 -0.08297 -0.00740 0.10861  82  PHE A CB    
4511 C  CG    . PHE B 82  ? 0.92473 1.07348 0.81619 -0.08343 -0.00512 0.11149  82  PHE A CG    
4512 C  CD1   . PHE B 82  ? 1.02418 1.18407 0.90423 -0.07970 -0.00219 0.09901  82  PHE A CD1   
4513 C  CD2   . PHE B 82  ? 1.00036 1.15481 0.89039 -0.08710 -0.00675 0.12637  82  PHE A CD2   
4514 C  CE1   . PHE B 82  ? 1.02757 1.20457 0.89362 -0.07931 -0.00105 0.10054  82  PHE A CE1   
4515 C  CE2   . PHE B 82  ? 0.97718 1.14897 0.85333 -0.08699 -0.00528 0.12930  82  PHE A CE2   
4516 C  CZ    . PHE B 82  ? 0.90990 1.09334 0.77336 -0.08295 -0.00248 0.11601  82  PHE A CZ    
4517 N  N     . ALA B 83  ? 0.98320 1.07959 0.89385 -0.08480 -0.02082 0.12197  83  ALA A N     
4518 C  CA    . ALA B 83  ? 0.99998 1.09180 0.90993 -0.08611 -0.02552 0.13157  83  ALA A CA    
4519 C  C     . ALA B 83  ? 1.00245 1.11172 0.91150 -0.09042 -0.02370 0.14564  83  ALA A C     
4520 O  O     . ALA B 83  ? 1.05412 1.17151 0.97118 -0.09346 -0.02070 0.15283  83  ALA A O     
4521 C  CB    . ALA B 83  ? 0.96075 1.03256 0.88177 -0.08519 -0.03117 0.13483  83  ALA A CB    
4522 N  N     . ILE B 84  ? 1.03348 1.14931 0.93346 -0.09073 -0.02562 0.15034  84  ILE A N     
4523 C  CA    . ILE B 84  ? 1.06401 1.19794 0.96041 -0.09428 -0.02382 0.16438  84  ILE A CA    
4524 C  C     . ILE B 84  ? 1.09164 1.21938 1.00179 -0.09819 -0.02740 0.18092  84  ILE A C     
4525 O  O     . ILE B 84  ? 1.13163 1.27417 1.04176 -0.10192 -0.02551 0.19531  84  ILE A O     
4526 C  CB    . ILE B 84  ? 1.04041 1.18281 0.92293 -0.09308 -0.02624 0.16481  84  ILE A CB    
4527 C  CG1   . ILE B 84  ? 1.03202 1.15798 0.91951 -0.09214 -0.03376 0.16828  84  ILE A CG1   
4528 C  CG2   . ILE B 84  ? 0.92042 1.06843 0.79088 -0.08951 -0.02410 0.14798  84  ILE A CG2   
4529 C  CD1   . ILE B 84  ? 1.19326 1.32809 1.07003 -0.09144 -0.03725 0.17107  84  ILE A CD1   
4530 N  N     . ASN B 85  ? 1.10012 1.20642 1.02203 -0.09711 -0.03289 0.17941  85  ASN A N     
4531 C  CA    . ASN B 85  ? 1.07302 1.17035 1.01047 -0.10038 -0.03780 0.19299  85  ASN A CA    
4532 C  C     . ASN B 85  ? 1.04847 1.13908 1.00037 -0.10190 -0.03729 0.19109  85  ASN A C     
4533 O  O     . ASN B 85  ? 1.13417 1.21029 1.10090 -0.10317 -0.04359 0.19697  85  ASN A O     
4534 C  CB    . ASN B 85  ? 1.11018 1.18827 1.05106 -0.09716 -0.04595 0.19293  85  ASN A CB    
4535 C  CG    . ASN B 85  ? 1.12569 1.18560 1.06776 -0.09178 -0.04794 0.17776  85  ASN A CG    
4536 O  OD1   . ASN B 85  ? 1.18650 1.24884 1.12205 -0.08981 -0.04335 0.16560  85  ASN A OD1   
4537 N  ND2   . ASN B 85  ? 1.11267 1.15443 1.06289 -0.08883 -0.05496 0.17857  85  ASN A ND2   
4538 N  N     . ASN B 86  ? 1.06595 1.16671 1.01458 -0.10143 -0.03068 0.18239  86  ASN A N     
4539 C  CA    . ASN B 86  ? 1.07750 1.17359 1.03991 -0.10242 -0.03021 0.17925  86  ASN A CA    
4540 C  C     . ASN B 86  ? 1.06593 1.18585 1.02658 -0.10462 -0.02109 0.18040  86  ASN A C     
4541 O  O     . ASN B 86  ? 1.06224 1.18840 1.01264 -0.10087 -0.01623 0.16728  86  ASN A O     
4542 C  CB    . ASN B 86  ? 1.10177 1.17990 1.06221 -0.09670 -0.03286 0.16260  86  ASN A CB    
4543 C  CG    . ASN B 86  ? 1.02195 1.09497 0.99602 -0.09707 -0.03352 0.15859  86  ASN A CG    
4544 O  OD1   . ASN B 86  ? 1.01207 1.09306 1.00029 -0.10210 -0.03299 0.16873  86  ASN A OD1   
4545 N  ND2   . ASN B 86  ? 0.91014 0.97025 0.88091 -0.09182 -0.03499 0.14447  86  ASN A ND2   
4546 N  N     . SER B 87  ? 1.11034 1.24387 1.08190 -0.11045 -0.01880 0.19644  87  SER A N     
4547 C  CA    . SER B 87  ? 1.13558 1.29525 1.10550 -0.11211 -0.00901 0.19932  87  SER A CA    
4548 C  C     . SER B 87  ? 1.13558 1.29493 1.11500 -0.11041 -0.00629 0.18823  87  SER A C     
4549 O  O     . SER B 87  ? 1.10479 1.28329 1.07828 -0.10846 0.00200  0.18269  87  SER A O     
4550 C  CB    . SER B 87  ? 1.18677 1.36171 1.16825 -0.11917 -0.00689 0.22148  87  SER A CB    
4551 O  OG    . SER B 87  ? 1.13931 1.31680 1.11041 -0.12021 -0.00911 0.23224  87  SER A OG    
4552 N  N     . LYS B 88  ? 1.11102 1.24922 1.10482 -0.11038 -0.01359 0.18431  88  LYS A N     
4553 C  CA    . LYS B 88  ? 1.11917 1.25586 1.12191 -0.10823 -0.01230 0.17341  88  LYS A CA    
4554 C  C     . LYS B 88  ? 1.15976 1.29407 1.14565 -0.10114 -0.00943 0.15478  88  LYS A C     
4555 O  O     . LYS B 88  ? 1.11501 1.26025 1.10217 -0.09883 -0.00400 0.14672  88  LYS A O     
4556 C  CB    . LYS B 88  ? 1.10678 1.22005 1.12636 -0.10888 -0.02232 0.17239  88  LYS A CB    
4557 C  CG    . LYS B 88  ? 1.19238 1.30259 1.22167 -0.10633 -0.02267 0.16126  88  LYS A CG    
4558 C  CD    . LYS B 88  ? 1.22709 1.34560 1.28178 -0.11254 -0.02366 0.17222  88  LYS A CD    
4559 C  CE    . LYS B 88  ? 1.43528 1.53475 1.50521 -0.11641 -0.03484 0.18115  88  LYS A CE    
4560 N  NZ    . LYS B 88  ? 1.42156 1.52769 1.51959 -0.12325 -0.03732 0.19199  88  LYS A NZ    
4561 N  N     . SER B 89  ? 1.15932 1.27976 1.13091 -0.09762 -0.01320 0.14815  89  SER A N     
4562 C  CA    . SER B 89  ? 1.12220 1.23901 1.07990 -0.09163 -0.01134 0.13164  89  SER A CA    
4563 C  C     . SER B 89  ? 1.02339 1.16314 0.96883 -0.09040 -0.00319 0.12830  89  SER A C     
4564 O  O     . SER B 89  ? 1.06299 1.20531 1.00353 -0.08598 -0.00018 0.11487  89  SER A O     
4565 C  CB    . SER B 89  ? 0.97881 1.07743 0.92648 -0.08885 -0.01701 0.12731  89  SER A CB    
4566 O  OG    . SER B 89  ? 0.91446 1.02054 0.85398 -0.09109 -0.01698 0.13624  89  SER A OG    
4567 N  N     . PHE B 90  ? 1.06136 1.21779 1.00139 -0.09365 -0.00003 0.14004  90  PHE A N     
4568 C  CA    . PHE B 90  ? 1.07869 1.25866 1.00539 -0.09153 0.00753  0.13654  90  PHE A CA    
4569 C  C     . PHE B 90  ? 1.00484 1.20425 0.94067 -0.09160 0.01523  0.13730  90  PHE A C     
4570 O  O     . PHE B 90  ? 1.08730 1.30151 1.01386 -0.08697 0.02108  0.12674  90  PHE A O     
4571 C  CB    . PHE B 90  ? 1.08131 1.27425 0.99796 -0.09435 0.00832  0.14962  90  PHE A CB    
4572 C  CG    . PHE B 90  ? 1.13280 1.35169 1.03370 -0.09149 0.01572  0.14654  90  PHE A CG    
4573 C  CD1   . PHE B 90  ? 1.04058 1.25926 0.92612 -0.08572 0.01540  0.12938  90  PHE A CD1   
4574 C  CD2   . PHE B 90  ? 1.04114 1.28498 0.94280 -0.09430 0.02271  0.16094  90  PHE A CD2   
4575 C  CE1   . PHE B 90  ? 1.05961 1.30177 0.92976 -0.08201 0.02117  0.12473  90  PHE A CE1   
4576 C  CE2   . PHE B 90  ? 1.02550 1.29459 0.91052 -0.09039 0.02973  0.15748  90  PHE A CE2   
4577 C  CZ    . PHE B 90  ? 1.02177 1.28967 0.89043 -0.08384 0.02858  0.13842  90  PHE A CZ    
4578 N  N     . ALA B 91  ? 1.01048 1.21049 0.96562 -0.09652 0.01497  0.14923  91  ALA A N     
4579 C  CA    . ALA B 91  ? 1.04277 1.26126 1.01019 -0.09668 0.02205  0.14998  91  ALA A CA    
4580 C  C     . ALA B 91  ? 1.02926 1.23779 1.00014 -0.09112 0.02103  0.13204  91  ALA A C     
4581 O  O     . ALA B 91  ? 1.05187 1.27803 1.02400 -0.08761 0.02805  0.12538  91  ALA A O     
4582 C  CB    . ALA B 91  ? 0.98451 1.20440 0.97509 -0.10408 0.02050  0.16746  91  ALA A CB    
4583 N  N     . ASP B 92  ? 1.17228 1.35342 1.14437 -0.08962 0.01247  0.12426  92  ASP A N     
4584 C  CA    . ASP B 92  ? 1.18565 1.35508 1.16035 -0.08425 0.01047  0.10850  92  ASP A CA    
4585 C  C     . ASP B 92  ? 1.13325 1.30641 1.09113 -0.07784 0.01367  0.09314  92  ASP A C     
4586 O  O     . ASP B 92  ? 1.19129 1.35820 1.15173 -0.07299 0.01307  0.08031  92  ASP A O     
4587 C  CB    . ASP B 92  ? 1.17507 1.31516 1.15321 -0.08391 0.00067  0.10567  92  ASP A CB    
4588 C  CG    . ASP B 92  ? 1.28209 1.41527 1.27845 -0.08923 -0.00458 0.11787  92  ASP A CG    
4589 O  OD1   . ASP B 92  ? 1.21204 1.36297 1.22120 -0.09401 -0.00056 0.12927  92  ASP A OD1   
4590 O  OD2   . ASP B 92  ? 1.33999 1.45024 1.33834 -0.08843 -0.01292 0.11606  92  ASP A OD2   
4591 N  N     . ILE B 93  ? 1.04699 1.22952 0.98861 -0.07758 0.01607  0.09400  93  ILE A N     
4592 C  CA    . ILE B 93  ? 0.93540 1.11924 0.86179 -0.07168 0.01713  0.07854  93  ILE A CA    
4593 C  C     . ILE B 93  ? 1.05713 1.25741 0.98638 -0.06652 0.02351  0.06829  93  ILE A C     
4594 O  O     . ILE B 93  ? 1.07551 1.26727 1.00192 -0.06097 0.02181  0.05281  93  ILE A O     
4595 C  CB    . ILE B 93  ? 0.91979 1.11438 0.82922 -0.07246 0.01818  0.08219  93  ILE A CB    
4596 C  CG1   . ILE B 93  ? 0.99315 1.16872 0.89991 -0.07598 0.01084  0.08893  93  ILE A CG1   
4597 C  CG2   . ILE B 93  ? 0.85774 1.05771 0.75295 -0.06620 0.01924  0.06551  93  ILE A CG2   
4598 C  CD1   . ILE B 93  ? 1.03891 1.19100 0.94349 -0.07300 0.00467  0.07681  93  ILE A CD1   
4599 N  N     . ASN B 94  ? 0.96957 1.19398 0.90575 -0.06808 0.03097  0.07718  94  ASN A N     
4600 C  CA    . ASN B 94  ? 0.98630 1.22882 0.92614 -0.06231 0.03779  0.06743  94  ASN A CA    
4601 C  C     . ASN B 94  ? 0.96395 1.19228 0.92018 -0.06017 0.03438  0.05984  94  ASN A C     
4602 O  O     . ASN B 94  ? 1.01500 1.24829 0.97204 -0.05341 0.03671  0.04595  94  ASN A O     
4603 C  CB    . ASN B 94  ? 0.87153 1.14518 0.81686 -0.06461 0.04744  0.08057  94  ASN A CB    
4604 C  CG    . ASN B 94  ? 1.04262 1.33836 0.99111 -0.05751 0.05558  0.07012  94  ASN A CG    
4605 O  OD1   . ASN B 94  ? 1.11719 1.42735 1.04947 -0.05098 0.05990  0.05963  94  ASN A OD1   
4606 N  ND2   . ASN B 94  ? 1.01246 1.31093 0.98232 -0.05813 0.05706  0.07199  94  ASN A ND2   
4607 N  N     . LEU B 95  ? 0.98120 1.19171 0.95033 -0.06516 0.02819  0.06814  95  LEU A N     
4608 C  CA    . LEU B 95  ? 0.90724 1.10320 0.89035 -0.06269 0.02362  0.06090  95  LEU A CA    
4609 C  C     . LEU B 95  ? 0.92581 1.10030 0.89873 -0.05705 0.01809  0.04547  95  LEU A C     
4610 O  O     . LEU B 95  ? 0.93448 1.10607 0.91302 -0.05152 0.01757  0.03411  95  LEU A O     
4611 C  CB    . LEU B 95  ? 0.95848 1.13981 0.95600 -0.06874 0.01707  0.07253  95  LEU A CB    
4612 C  CG    . LEU B 95  ? 1.03191 1.23165 1.04674 -0.07507 0.02084  0.08836  95  LEU A CG    
4613 C  CD1   . LEU B 95  ? 0.92114 1.10197 0.95207 -0.07972 0.01176  0.09563  95  LEU A CD1   
4614 C  CD2   . LEU B 95  ? 0.87053 1.09515 0.89704 -0.07206 0.02890  0.08523  95  LEU A CD2   
4615 N  N     . TYR B 96  ? 1.00806 1.16784 0.96735 -0.05841 0.01384  0.04559  96  TYR A N     
4616 C  CA    . TYR B 96  ? 0.93873 1.07830 0.89020 -0.05405 0.00863  0.03312  96  TYR A CA    
4617 C  C     . TYR B 96  ? 0.91208 1.06179 0.85591 -0.04790 0.01208  0.01883  96  TYR A C     
4618 O  O     . TYR B 96  ? 0.88256 1.01999 0.82825 -0.04295 0.00890  0.00709  96  TYR A O     
4619 C  CB    . TYR B 96  ? 0.76064 0.88515 0.70139 -0.05724 0.00392  0.03776  96  TYR A CB    
4620 C  CG    . TYR B 96  ? 0.84886 0.95635 0.79679 -0.06073 -0.00163 0.04715  96  TYR A CG    
4621 C  CD1   . TYR B 96  ? 0.92694 1.01315 0.87788 -0.05787 -0.00731 0.04198  96  TYR A CD1   
4622 C  CD2   . TYR B 96  ? 0.88436 0.99702 0.83591 -0.06633 -0.00160 0.06106  96  TYR A CD2   
4623 C  CE1   . TYR B 96  ? 0.91932 0.99051 0.87517 -0.05972 -0.01277 0.04901  96  TYR A CE1   
4624 C  CE2   . TYR B 96  ? 0.88231 0.97852 0.84079 -0.06861 -0.00770 0.06797  96  TYR A CE2   
4625 C  CZ    . TYR B 96  ? 0.91459 0.99043 0.87446 -0.06490 -0.01324 0.06119  96  TYR A CZ    
4626 O  OH    . TYR B 96  ? 0.94690 1.00686 0.91197 -0.06589 -0.01968 0.06658  96  TYR A OH    
4627 N  N     . ARG B 97  ? 0.90285 1.07481 0.83796 -0.04762 0.01810  0.01947  97  ARG A N     
4628 C  CA    . ARG B 97  ? 0.92010 1.10231 0.84712 -0.04072 0.02070  0.00423  97  ARG A CA    
4629 C  C     . ARG B 97  ? 0.98830 1.17925 0.92753 -0.03490 0.02414  -0.00414 97  ARG A C     
4630 O  O     . ARG B 97  ? 1.04796 1.23246 0.98644 -0.02834 0.02192  -0.01939 97  ARG A O     
4631 C  CB    . ARG B 97  ? 0.91403 1.12032 0.82749 -0.04078 0.02645  0.00694  97  ARG A CB    
4632 C  CG    . ARG B 97  ? 1.01057 1.22835 0.91421 -0.03252 0.02847  -0.01053 97  ARG A CG    
4633 C  CD    . ARG B 97  ? 1.08640 1.32572 0.97279 -0.03194 0.03246  -0.00876 97  ARG A CD    
4634 N  NE    . ARG B 97  ? 1.20601 1.45066 1.08096 -0.02371 0.03132  -0.02794 97  ARG A NE    
4635 C  CZ    . ARG B 97  ? 1.35745 1.62431 1.23001 -0.01580 0.03786  -0.03780 97  ARG A CZ    
4636 N  NH1   . ARG B 97  ? 1.27613 1.56420 1.15766 -0.01539 0.04705  -0.02932 97  ARG A NH1   
4637 N  NH2   . ARG B 97  ? 1.39127 1.65959 1.25321 -0.00787 0.03489  -0.05688 97  ARG A NH2   
4638 N  N     . GLU B 98  ? 0.96181 1.16745 0.91412 -0.03722 0.02909  0.00583  98  GLU A N     
4639 C  CA    . GLU B 98  ? 0.96403 1.18004 0.93026 -0.03166 0.03248  -0.00137 98  GLU A CA    
4640 C  C     . GLU B 98  ? 0.87764 1.06834 0.85416 -0.02962 0.02456  -0.00762 98  GLU A C     
4641 O  O     . GLU B 98  ? 0.93015 1.12081 0.91254 -0.02246 0.02428  -0.02024 98  GLU A O     
4642 C  CB    . GLU B 98  ? 0.98494 1.22400 0.96511 -0.03566 0.03948  0.01255  98  GLU A CB    
4643 C  CG    . GLU B 98  ? 0.96751 1.23687 0.93798 -0.03576 0.04917  0.01822  98  GLU A CG    
4644 C  CD    . GLU B 98  ? 1.19840 1.48581 1.16094 -0.02565 0.05492  0.00185  98  GLU A CD    
4645 O  OE1   . GLU B 98  ? 1.19452 1.48287 1.16908 -0.01943 0.05527  -0.00871 98  GLU A OE1   
4646 O  OE2   . GLU B 98  ? 1.19607 1.49653 1.14029 -0.02331 0.05843  -0.00110 98  GLU A OE2   
4647 N  N     . GLN B 99  ? 0.91313 1.08231 0.89137 -0.03510 0.01787  0.00088  99  GLN A N     
4648 C  CA    . GLN B 99  ? 0.96358 1.10840 0.94824 -0.03263 0.01012  -0.00446 99  GLN A CA    
4649 C  C     . GLN B 99  ? 0.98863 1.11836 0.96306 -0.02752 0.00632  -0.01780 99  GLN A C     
4650 O  O     . GLN B 99  ? 0.98132 1.09954 0.96219 -0.02225 0.00245  -0.02661 99  GLN A O     
4651 C  CB    . GLN B 99  ? 0.90225 1.02866 0.88824 -0.03864 0.00405  0.00699  99  GLN A CB    
4652 C  CG    . GLN B 99  ? 1.06881 1.17288 1.06142 -0.03575 -0.00364 0.00337  99  GLN A CG    
4653 C  CD    . GLN B 99  ? 1.15655 1.24319 1.14838 -0.04028 -0.00973 0.01319  99  GLN A CD    
4654 O  OE1   . GLN B 99  ? 1.07050 1.15993 1.05749 -0.04572 -0.00866 0.02251  99  GLN A OE1   
4655 N  NE2   . GLN B 99  ? 1.18918 1.25782 1.18535 -0.03732 -0.01653 0.01087  99  GLN A NE2   
4656 N  N     . ILE B 100 ? 0.87044 1.00005 0.83021 -0.02910 0.00673  -0.01910 100 ILE A N     
4657 C  CA    . ILE B 100 ? 0.97671 1.09307 0.92895 -0.02498 0.00257  -0.03166 100 ILE A CA    
4658 C  C     . ILE B 100 ? 0.94908 1.07833 0.90389 -0.01699 0.00544  -0.04650 100 ILE A C     
4659 O  O     . ILE B 100 ? 0.97212 1.08755 0.93120 -0.01174 0.00079  -0.05745 100 ILE A O     
4660 C  CB    . ILE B 100 ? 1.00105 1.11597 0.93872 -0.02892 0.00162  -0.02935 100 ILE A CB    
4661 C  CG1   . ILE B 100 ? 0.94606 1.04368 0.88219 -0.03512 -0.00255 -0.01717 100 ILE A CG1   
4662 C  CG2   . ILE B 100 ? 0.93356 1.03972 0.86552 -0.02464 -0.00244 -0.04366 100 ILE A CG2   
4663 C  CD1   . ILE B 100 ? 0.89821 0.99804 0.82220 -0.03952 -0.00290 -0.01227 100 ILE A CD1   
4664 N  N     . LYS B 101 ? 0.97179 1.12808 0.92429 -0.01545 0.01315  -0.04683 101 LYS A N     
4665 C  CA    . LYS B 101 ? 0.97912 1.15030 0.93266 -0.00656 0.01655  -0.06202 101 LYS A CA    
4666 C  C     . LYS B 101 ? 1.06605 1.23413 1.03663 -0.00112 0.01566  -0.06744 101 LYS A C     
4667 O  O     . LYS B 101 ? 1.10832 1.27635 1.08163 0.00725  0.01442  -0.08276 101 LYS A O     
4668 C  CB    . LYS B 101 ? 0.93391 1.13766 0.88128 -0.00572 0.02630  -0.05902 101 LYS A CB    
4669 C  CG    . LYS B 101 ? 1.07865 1.28805 1.00705 -0.00842 0.02664  -0.05768 101 LYS A CG    
4670 C  CD    . LYS B 101 ? 1.25373 1.49512 1.17609 -0.00942 0.03659  -0.04861 101 LYS A CD    
4671 C  CE    . LYS B 101 ? 1.29358 1.56062 1.21958 -0.00008 0.04443  -0.05910 101 LYS A CE    
4672 N  NZ    . LYS B 101 ? 1.10211 1.40239 1.02408 -0.00141 0.05542  -0.04734 101 LYS A NZ    
4673 N  N     . ARG B 102 ? 0.96115 1.12604 0.94397 -0.00531 0.01529  -0.05577 102 ARG A N     
4674 C  CA    . ARG B 102 ? 1.03187 1.19505 1.03163 -0.00005 0.01373  -0.06053 102 ARG A CA    
4675 C  C     . ARG B 102 ? 1.07578 1.20821 1.07817 0.00168  0.00387  -0.06491 102 ARG A C     
4676 O  O     . ARG B 102 ? 1.24979 1.37775 1.26165 0.00900  0.00113  -0.07520 102 ARG A O     
4677 C  CB    . ARG B 102 ? 1.13219 1.30765 1.14615 -0.00475 0.01693  -0.04704 102 ARG A CB    
4678 C  CG    . ARG B 102 ? 1.20598 1.36297 1.21993 -0.01307 0.01123  -0.03331 102 ARG A CG    
4679 C  CD    . ARG B 102 ? 1.16993 1.33579 1.20214 -0.01639 0.01174  -0.02311 102 ARG A CD    
4680 N  NE    . ARG B 102 ? 1.33389 1.48197 1.36564 -0.02349 0.00549  -0.01142 102 ARG A NE    
4681 C  CZ    . ARG B 102 ? 1.34949 1.47386 1.38385 -0.02249 -0.00337 -0.01220 102 ARG A CZ    
4682 N  NH1   . ARG B 102 ? 1.28688 1.40140 1.32542 -0.01539 -0.00740 -0.02264 102 ARG A NH1   
4683 N  NH2   . ARG B 102 ? 1.31564 1.42597 1.34799 -0.02815 -0.00854 -0.00229 102 ARG A NH2   
4684 N  N     . VAL B 103 ? 1.01983 1.13160 1.01426 -0.00440 -0.00137 -0.05689 103 VAL A N     
4685 C  CA    . VAL B 103 ? 1.04255 1.12678 1.03860 -0.00260 -0.00985 -0.05945 103 VAL A CA    
4686 C  C     . VAL B 103 ? 0.96323 1.03748 0.95356 0.00193  -0.01301 -0.07235 103 VAL A C     
4687 O  O     . VAL B 103 ? 0.94654 1.00402 0.94310 0.00662  -0.01890 -0.07861 103 VAL A O     
4688 C  CB    . VAL B 103 ? 0.97316 1.04015 0.96292 -0.00962 -0.01380 -0.04664 103 VAL A CB    
4689 C  CG1   . VAL B 103 ? 1.02823 1.10278 1.02586 -0.01352 -0.01259 -0.03539 103 VAL A CG1   
4690 C  CG2   . VAL B 103 ? 1.07830 1.14559 1.05380 -0.01476 -0.01219 -0.04344 103 VAL A CG2   
4691 N  N     . LYS B 104 ? 0.92818 1.01199 0.90738 0.00070  -0.01005 -0.07642 104 LYS A N     
4692 C  CA    . LYS B 104 ? 1.06985 1.14634 1.04538 0.00539  -0.01380 -0.09059 104 LYS A CA    
4693 C  C     . LYS B 104 ? 1.12167 1.21439 1.10310 0.01475  -0.01088 -0.10563 104 LYS A C     
4694 O  O     . LYS B 104 ? 1.24003 1.32378 1.22238 0.02047  -0.01570 -0.11960 104 LYS A O     
4695 C  CB    . LYS B 104 ? 1.08563 1.16538 1.04672 0.00071  -0.01329 -0.08994 104 LYS A CB    
4696 C  CG    . LYS B 104 ? 0.95172 1.01604 0.90722 -0.00774 -0.01619 -0.07622 104 LYS A CG    
4697 C  CD    . LYS B 104 ? 0.90964 0.94682 0.86961 -0.00775 -0.02399 -0.07719 104 LYS A CD    
4698 C  CE    . LYS B 104 ? 0.80607 0.83645 0.76401 -0.00567 -0.02883 -0.08963 104 LYS A CE    
4699 N  NZ    . LYS B 104 ? 0.90230 0.90676 0.86706 -0.00629 -0.03619 -0.08869 104 LYS A NZ    
4700 N  N     . ASP B 105 ? 0.98153 1.09797 0.96821 0.01660  -0.00333 -0.10300 105 ASP A N     
4701 C  CA    . ASP B 105 ? 1.03970 1.17563 1.03290 0.02628  0.00102  -0.11646 105 ASP A CA    
4702 C  C     . ASP B 105 ? 1.17164 1.31656 1.15235 0.03110  0.00187  -0.13068 105 ASP A C     
4703 O  O     . ASP B 105 ? 1.17852 1.32164 1.16290 0.04032  -0.00110 -0.14762 105 ASP A O     
4704 C  CB    . ASP B 105 ? 1.19086 1.31225 1.19947 0.03339  -0.00490 -0.12467 105 ASP A CB    
4705 C  CG    . ASP B 105 ? 1.28123 1.42579 1.30076 0.04316  0.00071  -0.13517 105 ASP A CG    
4706 O  OD1   . ASP B 105 ? 1.33068 1.49820 1.35609 0.04156  0.00859  -0.12677 105 ASP A OD1   
4707 O  OD2   . ASP B 105 ? 1.29547 1.43547 1.31909 0.05254  -0.00293 -0.15167 105 ASP A OD2   
4708 N  N     . SER B 106 ? 1.14087 1.29500 1.10671 0.02513  0.00508  -0.12405 106 SER A N     
4709 C  CA    . SER B 106 ? 1.10948 1.27239 1.06112 0.02901  0.00493  -0.13655 106 SER A CA    
4710 C  C     . SER B 106 ? 1.08559 1.27418 1.02392 0.02479  0.01349  -0.12659 106 SER A C     
4711 O  O     . SER B 106 ? 1.03439 1.22417 0.97309 0.01603  0.01637  -0.10859 106 SER A O     
4712 C  CB    . SER B 106 ? 1.08797 1.22399 1.03426 0.02548  -0.00539 -0.14056 106 SER A CB    
4713 O  OG    . SER B 106 ? 1.23339 1.37851 1.16592 0.02868  -0.00663 -0.15250 106 SER A OG    
4714 N  N     . ASP B 107 ? 1.12812 1.33711 1.05445 0.03161  0.01706  -0.13858 107 ASP A N     
4715 C  CA    . ASP B 107 ? 1.15508 1.38972 1.06656 0.02857  0.02499  -0.12944 107 ASP A CA    
4716 C  C     . ASP B 107 ? 1.15968 1.38318 1.05600 0.02207  0.01895  -0.12616 107 ASP A C     
4717 O  O     . ASP B 107 ? 1.19536 1.42611 1.08502 0.01405  0.02246  -0.10944 107 ASP A O     
4718 C  CB    . ASP B 107 ? 1.23562 1.50067 1.13903 0.03984  0.03242  -0.14311 107 ASP A CB    
4719 C  CG    . ASP B 107 ? 1.50738 1.80332 1.39741 0.03709  0.04279  -0.13027 107 ASP A CG    
4720 O  OD1   . ASP B 107 ? 1.44277 1.73727 1.33464 0.02640  0.04491  -0.10966 107 ASP A OD1   
4721 O  OD2   . ASP B 107 ? 1.62081 1.94245 1.49829 0.04602  0.04856  -0.14067 107 ASP A OD2   
4722 N  N     . ASP B 108 ? 1.14543 1.35138 1.03778 0.02528  0.00937  -0.14152 108 ASP A N     
4723 C  CA    . ASP B 108 ? 1.21522 1.40893 1.09656 0.01890  0.00230  -0.13896 108 ASP A CA    
4724 C  C     . ASP B 108 ? 1.08971 1.25102 0.98299 0.01161  -0.00582 -0.13215 108 ASP A C     
4725 O  O     . ASP B 108 ? 1.01882 1.16080 0.92309 0.01516  -0.01241 -0.14268 108 ASP A O     
4726 C  CB    . ASP B 108 ? 1.22751 1.42420 1.09716 0.02639  -0.00383 -0.15961 108 ASP A CB    
4727 C  CG    . ASP B 108 ? 1.26915 1.44241 1.15082 0.03186  -0.01364 -0.17733 108 ASP A CG    
4728 O  OD1   . ASP B 108 ? 1.27060 1.44122 1.16562 0.03719  -0.01157 -0.18181 108 ASP A OD1   
4729 O  OD2   . ASP B 108 ? 1.07066 1.22784 0.94989 0.03057  -0.02397 -0.18613 108 ASP A OD2   
4730 N  N     . VAL B 109 ? 1.06262 1.21880 0.95413 0.00193  -0.00500 -0.11391 109 VAL A N     
4731 C  CA    . VAL B 109 ? 1.03276 1.16117 0.93298 -0.00487 -0.01159 -0.10580 109 VAL A CA    
4732 C  C     . VAL B 109 ? 0.94985 1.07555 0.83983 -0.01201 -0.01485 -0.09787 109 VAL A C     
4733 O  O     . VAL B 109 ? 0.99640 1.13917 0.87692 -0.01531 -0.00949 -0.08722 109 VAL A O     
4734 C  CB    . VAL B 109 ? 0.91318 1.03680 0.82414 -0.00858 -0.00754 -0.09114 109 VAL A CB    
4735 C  CG1   . VAL B 109 ? 0.93609 1.03281 0.85328 -0.01451 -0.01384 -0.08283 109 VAL A CG1   
4736 C  CG2   . VAL B 109 ? 1.07847 1.20634 1.00073 -0.00119 -0.00487 -0.09926 109 VAL A CG2   
4737 N  N     . PRO B 110 ? 0.91735 1.02294 0.80999 -0.01454 -0.02366 -0.10217 110 PRO A N     
4738 C  CA    . PRO B 110 ? 0.84339 0.94739 0.72813 -0.02111 -0.02714 -0.09480 110 PRO A CA    
4739 C  C     . PRO B 110 ? 0.88981 0.99562 0.77344 -0.02814 -0.02227 -0.07451 110 PRO A C     
4740 O  O     . PRO B 110 ? 0.90591 0.99721 0.79914 -0.03097 -0.02188 -0.06547 110 PRO A O     
4741 C  CB    . PRO B 110 ? 0.89763 0.97673 0.79232 -0.02327 -0.03661 -0.09994 110 PRO A CB    
4742 C  CG    . PRO B 110 ? 0.94005 1.01317 0.84256 -0.01563 -0.03960 -0.11661 110 PRO A CG    
4743 C  CD    . PRO B 110 ? 0.87028 0.95474 0.77465 -0.01135 -0.03114 -0.11391 110 PRO A CD    
4744 N  N     . MET B 111 ? 0.80925 0.93276 0.68091 -0.03045 -0.01905 -0.06743 111 MET A N     
4745 C  CA    . MET B 111 ? 0.85263 0.98084 0.72378 -0.03605 -0.01399 -0.04879 111 MET A CA    
4746 C  C     . MET B 111 ? 0.83606 0.97510 0.69508 -0.03980 -0.01505 -0.04174 111 MET A C     
4747 O  O     . MET B 111 ? 0.90986 1.06273 0.75752 -0.03653 -0.01636 -0.05075 111 MET A O     
4748 C  CB    . MET B 111 ? 0.89058 1.03578 0.76354 -0.03348 -0.00539 -0.04474 111 MET A CB    
4749 C  CG    . MET B 111 ? 0.88446 1.02920 0.76291 -0.03917 -0.00156 -0.02644 111 MET A CG    
4750 S  SD    . MET B 111 ? 1.09772 1.26230 0.98313 -0.03631 0.00759  -0.02305 111 MET A SD    
4751 C  CE    . MET B 111 ? 0.89643 1.04949 0.79219 -0.02893 0.00525  -0.04032 111 MET A CE    
4752 N  N     . VAL B 112 ? 0.77088 0.90352 0.63210 -0.04600 -0.01502 -0.02601 112 VAL A N     
4753 C  CA    . VAL B 112 ? 0.85497 0.99602 0.70667 -0.04987 -0.01655 -0.01702 112 VAL A CA    
4754 C  C     . VAL B 112 ? 0.80716 0.95116 0.66154 -0.05438 -0.01200 0.00139  112 VAL A C     
4755 O  O     . VAL B 112 ? 0.90958 1.03784 0.77435 -0.05676 -0.01239 0.00805  112 VAL A O     
4756 C  CB    . VAL B 112 ? 0.86982 0.99524 0.72394 -0.05294 -0.02468 -0.01865 112 VAL A CB    
4757 C  CG1   . VAL B 112 ? 0.81673 0.94894 0.66416 -0.05731 -0.02612 -0.00618 112 VAL A CG1   
4758 C  CG2   . VAL B 112 ? 0.87861 1.00334 0.73000 -0.04921 -0.03074 -0.03651 112 VAL A CG2   
4759 N  N     . LEU B 113 ? 0.82415 0.98812 0.66921 -0.05526 -0.00820 0.00966  113 LEU A N     
4760 C  CA    . LEU B 113 ? 0.93475 1.10144 0.78332 -0.06009 -0.00515 0.02802  113 LEU A CA    
4761 C  C     . LEU B 113 ? 0.89260 1.05003 0.73957 -0.06430 -0.01089 0.03668  113 LEU A C     
4762 O  O     . LEU B 113 ? 0.87384 1.03716 0.71106 -0.06390 -0.01487 0.03303  113 LEU A O     
4763 C  CB    . LEU B 113 ? 0.86769 1.06043 0.70830 -0.05952 0.00162  0.03519  113 LEU A CB    
4764 C  CG    . LEU B 113 ? 0.90804 1.10530 0.75390 -0.06498 0.00457  0.05540  113 LEU A CG    
4765 C  CD1   . LEU B 113 ? 0.72325 0.90798 0.58593 -0.06677 0.00614  0.05965  113 LEU A CD1   
4766 C  CD2   . LEU B 113 ? 0.99099 1.21634 0.82775 -0.06440 0.01144  0.06322  113 LEU A CD2   
4767 N  N     . VAL B 114 ? 0.75308 0.89639 0.60995 -0.06775 -0.01183 0.04746  114 VAL A N     
4768 C  CA    . VAL B 114 ? 0.76666 0.89932 0.62455 -0.07076 -0.01710 0.05499  114 VAL A CA    
4769 C  C     . VAL B 114 ? 0.94863 1.08337 0.81025 -0.07431 -0.01578 0.07204  114 VAL A C     
4770 O  O     . VAL B 114 ? 0.97250 1.10204 0.84335 -0.07509 -0.01325 0.07700  114 VAL A O     
4771 C  CB    . VAL B 114 ? 0.87156 0.98201 0.73850 -0.07027 -0.02065 0.04995  114 VAL A CB    
4772 C  CG1   . VAL B 114 ? 0.80719 0.90851 0.67664 -0.07271 -0.02487 0.05902  114 VAL A CG1   
4773 C  CG2   . VAL B 114 ? 0.76289 0.87002 0.62826 -0.06759 -0.02321 0.03447  114 VAL A CG2   
4774 N  N     . GLY B 115 ? 0.94569 1.08741 0.80124 -0.07639 -0.01843 0.08089  115 GLY A N     
4775 C  CA    . GLY B 115 ? 0.83327 0.97392 0.69386 -0.07976 -0.01897 0.09741  115 GLY A CA    
4776 C  C     . GLY B 115 ? 0.89394 1.01882 0.75935 -0.08044 -0.02493 0.10120  115 GLY A C     
4777 O  O     . GLY B 115 ? 0.99324 1.12178 0.85268 -0.08050 -0.02891 0.10139  115 GLY A O     
4778 N  N     . ASN B 116 ? 0.94434 1.05254 0.82058 -0.08038 -0.02581 0.10382  116 ASN A N     
4779 C  CA    . ASN B 116 ? 0.93815 1.03121 0.81923 -0.07947 -0.03050 0.10539  116 ASN A CA    
4780 C  C     . ASN B 116 ? 1.03950 1.13122 0.92477 -0.08126 -0.03356 0.11985  116 ASN A C     
4781 O  O     . ASN B 116 ? 1.02869 1.12924 0.91481 -0.08389 -0.03216 0.12971  116 ASN A O     
4782 C  CB    . ASN B 116 ? 0.84082 0.91649 0.72946 -0.07695 -0.03012 0.09904  116 ASN A CB    
4783 C  CG    . ASN B 116 ? 0.87822 0.94109 0.76977 -0.07478 -0.03348 0.09762  116 ASN A CG    
4784 O  OD1   . ASN B 116 ? 0.93524 1.00254 0.82368 -0.07510 -0.03567 0.09630  116 ASN A OD1   
4785 N  ND2   . ASN B 116 ? 0.86277 0.91077 0.76057 -0.07222 -0.03404 0.09793  116 ASN A ND2   
4786 N  N     . LYS B 117 ? 1.04937 1.13019 0.93838 -0.07960 -0.03781 0.12141  117 LYS A N     
4787 C  CA    . LYS B 117 ? 0.98413 1.06020 0.87886 -0.07995 -0.04192 0.13351  117 LYS A CA    
4788 C  C     . LYS B 117 ? 1.01337 1.10480 0.90223 -0.08267 -0.04368 0.14339  117 LYS A C     
4789 O  O     . LYS B 117 ? 1.13685 1.22981 1.02984 -0.08473 -0.04530 0.15601  117 LYS A O     
4790 C  CB    . LYS B 117 ? 0.92221 0.98866 0.82628 -0.08039 -0.04200 0.13907  117 LYS A CB    
4791 C  CG    . LYS B 117 ? 0.98460 1.03417 0.89388 -0.07653 -0.04206 0.13056  117 LYS A CG    
4792 C  CD    . LYS B 117 ? 1.08392 1.12434 1.00279 -0.07692 -0.04367 0.13502  117 LYS A CD    
4793 C  CE    . LYS B 117 ? 0.83975 0.86319 0.76188 -0.07194 -0.04489 0.12651  117 LYS A CE    
4794 N  NZ    . LYS B 117 ? 1.05214 1.06603 0.98424 -0.07206 -0.04822 0.12980  117 LYS A NZ    
4795 N  N     . CYS B 118 ? 1.04261 1.14523 0.92213 -0.08259 -0.04410 0.13786  118 CYS A N     
4796 C  CA    . CYS B 118 ? 1.14068 1.25824 1.01261 -0.08420 -0.04680 0.14636  118 CYS A CA    
4797 C  C     . CYS B 118 ? 1.14716 1.25928 1.02431 -0.08311 -0.05316 0.15388  118 CYS A C     
4798 O  O     . CYS B 118 ? 1.15266 1.27512 1.02547 -0.08433 -0.05640 0.16409  118 CYS A O     
4799 C  CB    . CYS B 118 ? 1.14120 1.27265 1.00088 -0.08376 -0.04631 0.13606  118 CYS A CB    
4800 S  SG    . CYS B 118 ? 1.22891 1.37352 1.08001 -0.08421 -0.03893 0.13008  118 CYS A SG    
4801 N  N     . ASP B 119 ? 1.10081 1.19796 0.98700 -0.08031 -0.05487 0.14945  119 ASP A N     
4802 C  CA    . ASP B 119 ? 1.10861 1.20034 1.00179 -0.07822 -0.06041 0.15652  119 ASP A CA    
4803 C  C     . ASP B 119 ? 1.21931 1.30525 1.11927 -0.07868 -0.06285 0.16994  119 ASP A C     
4804 O  O     . ASP B 119 ? 1.15365 1.23828 1.05830 -0.07723 -0.06828 0.17825  119 ASP A O     
4805 C  CB    . ASP B 119 ? 1.19416 1.27270 1.09530 -0.07426 -0.06029 0.14850  119 ASP A CB    
4806 C  CG    . ASP B 119 ? 1.08523 1.15018 0.99046 -0.07269 -0.05641 0.14389  119 ASP A CG    
4807 O  OD1   . ASP B 119 ? 1.03753 1.10476 0.93804 -0.07455 -0.05214 0.13756  119 ASP A OD1   
4808 O  OD2   . ASP B 119 ? 1.14708 1.19935 1.06014 -0.06901 -0.05812 0.14615  119 ASP A OD2   
4809 N  N     . LEU B 120 ? 1.19148 1.27372 1.09376 -0.08068 -0.05961 0.17224  120 LEU A N     
4810 C  CA    . LEU B 120 ? 1.29139 1.36660 1.20303 -0.08179 -0.06278 0.18490  120 LEU A CA    
4811 C  C     . LEU B 120 ? 1.39542 1.48472 1.30303 -0.08526 -0.06514 0.19948  120 LEU A C     
4812 O  O     . LEU B 120 ? 1.33261 1.43906 1.22837 -0.08768 -0.06178 0.19948  120 LEU A O     
4813 C  CB    . LEU B 120 ? 1.27630 1.34603 1.19298 -0.08386 -0.05911 0.18384  120 LEU A CB    
4814 C  CG    . LEU B 120 ? 1.13576 1.18954 1.05708 -0.07984 -0.05807 0.17143  120 LEU A CG    
4815 C  CD1   . LEU B 120 ? 0.99951 1.04866 0.92705 -0.08203 -0.05588 0.17135  120 LEU A CD1   
4816 C  CD2   . LEU B 120 ? 1.07342 1.11181 1.00269 -0.07461 -0.06375 0.17170  120 LEU A CD2   
4817 N  N     . PRO B 121 ? 1.55521 1.63774 1.47206 -0.08500 -0.07120 0.21204  121 PRO A N     
4818 C  CA    . PRO B 121 ? 1.40674 1.50270 1.31945 -0.08801 -0.07400 0.22752  121 PRO A CA    
4819 C  C     . PRO B 121 ? 1.38799 1.49550 1.29852 -0.09363 -0.06935 0.23791  121 PRO A C     
4820 O  O     . PRO B 121 ? 1.55149 1.67800 1.45004 -0.09583 -0.06743 0.24490  121 PRO A O     
4821 C  CB    . PRO B 121 ? 1.54651 1.62844 1.47286 -0.08560 -0.08226 0.23729  121 PRO A CB    
4822 C  CG    . PRO B 121 ? 1.56329 1.62535 1.50182 -0.08313 -0.08258 0.22988  121 PRO A CG    
4823 C  CD    . PRO B 121 ? 1.46384 1.52624 1.39483 -0.08121 -0.07633 0.21240  121 PRO A CD    
4824 N  N     . THR B 122 ? 1.34387 1.44162 1.26585 -0.09575 -0.06755 0.23925  122 THR A N     
4825 C  CA    . THR B 122 ? 1.34740 1.45639 1.27158 -0.10150 -0.06297 0.25072  122 THR A CA    
4826 C  C     . THR B 122 ? 1.30502 1.41665 1.22726 -0.10204 -0.05542 0.23811  122 THR A C     
4827 O  O     . THR B 122 ? 1.34269 1.43819 1.27181 -0.09935 -0.05626 0.22618  122 THR A O     
4828 C  CB    . THR B 122 ? 1.38660 1.48274 1.33012 -0.10456 -0.06858 0.26559  122 THR A CB    
4829 O  OG1   . THR B 122 ? 1.39282 1.46745 1.34881 -0.10184 -0.07153 0.25485  122 THR A OG1   
4830 C  CG2   . THR B 122 ? 1.43581 1.52789 1.38256 -0.10334 -0.07687 0.27808  122 THR A CG2   
4831 N  N     . ARG B 123 ? 1.26514 1.39771 1.17775 -0.10485 -0.04815 0.24091  123 ARG A N     
4832 C  CA    . ARG B 123 ? 1.22637 1.36450 1.13715 -0.10502 -0.04067 0.22970  123 ARG A CA    
4833 C  C     . ARG B 123 ? 1.17833 1.32854 1.09782 -0.11052 -0.03572 0.24346  123 ARG A C     
4834 O  O     . ARG B 123 ? 1.40536 1.56360 1.32860 -0.11445 -0.03697 0.26223  123 ARG A O     
4835 C  CB    . ARG B 123 ? 1.27924 1.43308 1.17055 -0.10200 -0.03577 0.21703  123 ARG A CB    
4836 C  CG    . ARG B 123 ? 1.25715 1.43370 1.13403 -0.10303 -0.03409 0.22749  123 ARG A CG    
4837 C  CD    . ARG B 123 ? 1.30817 1.50216 1.16746 -0.10007 -0.02815 0.21390  123 ARG A CD    
4838 N  NE    . ARG B 123 ? 1.26007 1.44491 1.11286 -0.09582 -0.03189 0.19616  123 ARG A NE    
4839 C  CZ    . ARG B 123 ? 1.30465 1.49656 1.14686 -0.09273 -0.02856 0.17975  123 ARG A CZ    
4840 N  NH1   . ARG B 123 ? 1.18925 1.39749 1.02518 -0.09237 -0.02104 0.17706  123 ARG A NH1   
4841 N  NH2   . ARG B 123 ? 1.37753 1.56019 1.21673 -0.08978 -0.03301 0.16583  123 ARG A NH2   
4842 N  N     . THR B 124 ? 1.17194 1.32391 1.09591 -0.11083 -0.03012 0.23471  124 THR A N     
4843 C  CA    . THR B 124 ? 1.11531 1.28067 1.04970 -0.11593 -0.02443 0.24620  124 THR A CA    
4844 C  C     . THR B 124 ? 1.14619 1.33400 1.06889 -0.11446 -0.01421 0.23817  124 THR A C     
4845 O  O     . THR B 124 ? 1.05380 1.25684 0.98469 -0.11817 -0.00792 0.24744  124 THR A O     
4846 C  CB    . THR B 124 ? 1.18266 1.32940 1.13918 -0.11801 -0.02819 0.24516  124 THR A CB    
4847 O  OG1   . THR B 124 ? 1.28444 1.42377 1.23831 -0.11372 -0.02612 0.22534  124 THR A OG1   
4848 C  CG2   . THR B 124 ? 1.20345 1.32596 1.17089 -0.11764 -0.03904 0.24938  124 THR A CG2   
4849 N  N     . VAL B 125 ? 1.16079 1.35125 1.06620 -0.10901 -0.01262 0.22116  125 VAL A N     
4850 C  CA    . VAL B 125 ? 1.16920 1.37943 1.06270 -0.10616 -0.00402 0.21079  125 VAL A CA    
4851 C  C     . VAL B 125 ? 1.14806 1.37726 1.01991 -0.10374 -0.00248 0.21207  125 VAL A C     
4852 O  O     . VAL B 125 ? 1.12952 1.35025 0.99283 -0.10175 -0.00902 0.20855  125 VAL A O     
4853 C  CB    . VAL B 125 ? 1.15486 1.35185 1.04711 -0.10143 -0.00437 0.18859  125 VAL A CB    
4854 C  CG1   . VAL B 125 ? 1.02756 1.24428 0.90976 -0.09798 0.00397  0.17761  125 VAL A CG1   
4855 C  CG2   . VAL B 125 ? 1.06449 1.24122 0.97641 -0.10303 -0.00750 0.18720  125 VAL A CG2   
4856 N  N     . ASP B 126 ? 1.18152 1.43736 1.04461 -0.10347 0.00600  0.21693  126 ASP A N     
4857 C  CA    . ASP B 126 ? 1.28708 1.56371 1.12760 -0.10036 0.00761  0.21817  126 ASP A CA    
4858 C  C     . ASP B 126 ? 1.17431 1.45210 0.99926 -0.09357 0.00763  0.19406  126 ASP A C     
4859 O  O     . ASP B 126 ? 1.25570 1.53800 1.08200 -0.09076 0.01334  0.18139  126 ASP A O     
4860 C  CB    . ASP B 126 ? 1.25915 1.56549 1.09571 -0.10196 0.01729  0.23349  126 ASP A CB    
4861 C  CG    . ASP B 126 ? 1.27371 1.60174 1.08670 -0.09914 0.01788  0.23993  126 ASP A CG    
4862 O  OD1   . ASP B 126 ? 1.34742 1.66707 1.14810 -0.09617 0.01000  0.23166  126 ASP A OD1   
4863 O  OD2   . ASP B 126 ? 1.18800 1.54254 0.99502 -0.09978 0.02620  0.25377  126 ASP A OD2   
4864 N  N     . THR B 127 ? 1.10418 1.37760 0.91606 -0.09097 0.00055  0.18782  127 THR A N     
4865 C  CA    . THR B 127 ? 1.19638 1.47090 0.99452 -0.08501 -0.00097 0.16557  127 THR A CA    
4866 C  C     . THR B 127 ? 1.15996 1.46172 0.94212 -0.08031 0.00709  0.15952  127 THR A C     
4867 O  O     . THR B 127 ? 1.10618 1.40825 0.88338 -0.07531 0.00841  0.13969  127 THR A O     
4868 C  CB    . THR B 127 ? 1.35683 1.62573 1.14491 -0.08375 -0.01043 0.16293  127 THR A CB    
4869 O  OG1   . THR B 127 ? 1.34964 1.59324 1.15321 -0.08670 -0.01719 0.16543  127 THR A OG1   
4870 C  CG2   . THR B 127 ? 1.09700 1.36844 0.87176 -0.07807 -0.01313 0.14051  127 THR A CG2   
4871 N  N     . LYS B 128 ? 1.18489 1.51000 0.95929 -0.08141 0.01264  0.17662  128 LYS A N     
4872 C  CA    . LYS B 128 ? 1.19992 1.55384 0.95900 -0.07614 0.02180  0.17217  128 LYS A CA    
4873 C  C     . LYS B 128 ? 1.15999 1.51527 0.93210 -0.07518 0.03002  0.16414  128 LYS A C     
4874 O  O     . LYS B 128 ? 1.24763 1.61749 1.00904 -0.06841 0.03516  0.14863  128 LYS A O     
4875 C  CB    . LYS B 128 ? 1.39396 1.77300 1.14475 -0.07825 0.02725  0.19585  128 LYS A CB    
4876 C  CG    . LYS B 128 ? 1.38880 1.76972 1.12472 -0.07829 0.01906  0.20461  128 LYS A CG    
4877 C  CD    . LYS B 128 ? 1.48734 1.89420 1.21495 -0.08023 0.02511  0.22970  128 LYS A CD    
4878 C  CE    . LYS B 128 ? 1.44099 1.85074 1.15253 -0.07950 0.01633  0.23844  128 LYS A CE    
4879 N  NZ    . LYS B 128 ? 1.41785 1.85305 1.12078 -0.08132 0.02215  0.26472  128 LYS A NZ    
4880 N  N     . GLN B 129 ? 1.07367 1.41384 0.86932 -0.08133 0.03065  0.17379  129 GLN A N     
4881 C  CA    . GLN B 129 ? 1.19613 1.53686 1.00606 -0.08059 0.03734  0.16657  129 GLN A CA    
4882 C  C     . GLN B 129 ? 1.14579 1.46879 0.95549 -0.07553 0.03317  0.14127  129 GLN A C     
4883 O  O     . GLN B 129 ? 1.15728 1.48971 0.96642 -0.07045 0.03892  0.12802  129 GLN A O     
4884 C  CB    . GLN B 129 ? 1.32261 1.64977 1.15826 -0.08840 0.03691  0.18235  129 GLN A CB    
4885 C  CG    . GLN B 129 ? 1.18087 1.52516 1.02217 -0.09435 0.04143  0.20884  129 GLN A CG    
4886 C  CD    . GLN B 129 ? 1.34101 1.66919 1.21018 -0.10204 0.03910  0.22222  129 GLN A CD    
4887 O  OE1   . GLN B 129 ? 1.31293 1.61892 1.19029 -0.10607 0.03011  0.22898  129 GLN A OE1   
4888 N  NE2   . GLN B 129 ? 1.24608 1.58552 1.13079 -0.10365 0.04664  0.22527  129 GLN A NE2   
4889 N  N     . ALA B 130 ? 1.16730 1.46509 0.97848 -0.07669 0.02328  0.13493  130 ALA A N     
4890 C  CA    . ALA B 130 ? 1.05622 1.33557 0.86962 -0.07287 0.01900  0.11346  130 ALA A CA    
4891 C  C     . ALA B 130 ? 1.13558 1.42748 0.93022 -0.06545 0.01901  0.09512  130 ALA A C     
4892 O  O     . ALA B 130 ? 1.10545 1.39474 0.90205 -0.06069 0.02057  0.07808  130 ALA A O     
4893 C  CB    . ALA B 130 ? 1.02852 1.28064 0.84841 -0.07598 0.00927  0.11332  130 ALA A CB    
4894 N  N     . HIS B 131 ? 1.17319 1.47801 0.94986 -0.06394 0.01627  0.09774  131 HIS A N     
4895 C  CA    . HIS B 131 ? 1.07923 1.39849 0.83674 -0.05619 0.01574  0.08011  131 HIS A CA    
4896 C  C     . HIS B 131 ? 1.08316 1.42609 0.83644 -0.05069 0.02653  0.07555  131 HIS A C     
4897 O  O     . HIS B 131 ? 1.15477 1.49932 0.90353 -0.04374 0.02675  0.05503  131 HIS A O     
4898 C  CB    . HIS B 131 ? 1.04737 1.38003 0.78552 -0.05540 0.01128  0.08643  131 HIS A CB    
4899 C  CG    . HIS B 131 ? 1.24552 1.55828 0.98368 -0.05717 -0.00080 0.08063  131 HIS A CG    
4900 N  ND1   . HIS B 131 ? 1.25474 1.55328 1.00251 -0.06365 -0.00580 0.09603  131 HIS A ND1   
4901 C  CD2   . HIS B 131 ? 1.16708 1.47253 0.89839 -0.05323 -0.00907 0.06121  131 HIS A CD2   
4902 C  CE1   . HIS B 131 ? 1.06609 1.35090 0.81289 -0.06349 -0.01578 0.08676  131 HIS A CE1   
4903 N  NE2   . HIS B 131 ? 1.06605 1.35454 0.80359 -0.05774 -0.01816 0.06605  131 HIS A NE2   
4904 N  N     . GLU B 132 ? 1.05298 1.41461 0.80931 -0.05363 0.03549  0.09485  132 GLU A N     
4905 C  CA    . GLU B 132 ? 1.09764 1.48522 0.85162 -0.04850 0.04709  0.09287  132 GLU A CA    
4906 C  C     . GLU B 132 ? 1.03468 1.41000 0.80741 -0.04726 0.04955  0.08098  132 GLU A C     
4907 O  O     . GLU B 132 ? 1.04519 1.43320 0.81323 -0.03933 0.05447  0.06520  132 GLU A O     
4908 C  CB    . GLU B 132 ? 1.18438 1.59341 0.94184 -0.05358 0.05588  0.11932  132 GLU A CB    
4909 C  CG    . GLU B 132 ? 1.40690 1.85134 1.15594 -0.04748 0.06891  0.12052  132 GLU A CG    
4910 C  CD    . GLU B 132 ? 1.63969 2.10495 1.39516 -0.05381 0.07759  0.14948  132 GLU A CD    
4911 O  OE1   . GLU B 132 ? 1.60500 2.05321 1.38007 -0.06341 0.07418  0.16637  132 GLU A OE1   
4912 O  OE2   . GLU B 132 ? 1.66957 2.16841 1.41078 -0.04896 0.08762  0.15552  132 GLU A OE2   
4913 N  N     . LEU B 133 ? 1.01257 1.36323 0.80618 -0.05426 0.04567  0.08775  133 LEU A N     
4914 C  CA    . LEU B 133 ? 1.08263 1.42094 0.89417 -0.05321 0.04712  0.07784  133 LEU A CA    
4915 C  C     . LEU B 133 ? 1.13909 1.46240 0.94549 -0.04667 0.04096  0.05281  133 LEU A C     
4916 O  O     . LEU B 133 ? 1.08886 1.41787 0.89835 -0.04039 0.04486  0.03869  133 LEU A O     
4917 C  CB    . LEU B 133 ? 1.03334 1.34788 0.86590 -0.06151 0.04289  0.09020  133 LEU A CB    
4918 C  CG    . LEU B 133 ? 0.92595 1.22507 0.77700 -0.06069 0.04266  0.08090  133 LEU A CG    
4919 C  CD1   . LEU B 133 ? 0.90157 1.22473 0.75929 -0.05713 0.05302  0.08025  133 LEU A CD1   
4920 C  CD2   . LEU B 133 ? 0.88736 1.16421 0.75651 -0.06822 0.03764  0.09328  133 LEU A CD2   
4921 N  N     . ALA B 134 ? 1.14613 1.45021 0.94642 -0.04811 0.03102  0.04746  134 ALA A N     
4922 C  CA    . ALA B 134 ? 1.01396 1.30293 0.81137 -0.04292 0.02422  0.02516  134 ALA A CA    
4923 C  C     . ALA B 134 ? 1.14421 1.45408 0.92423 -0.03369 0.02646  0.00892  134 ALA A C     
4924 O  O     . ALA B 134 ? 1.10525 1.40832 0.88707 -0.02757 0.02415  -0.01070 134 ALA A O     
4925 C  CB    . ALA B 134 ? 0.88582 1.15372 0.68117 -0.04688 0.01360  0.02495  134 ALA A CB    
4926 N  N     . LYS B 135 ? 1.12790 1.46317 0.89074 -0.03199 0.03057  0.01665  135 LYS A N     
4927 C  CA    . LYS B 135 ? 1.06503 1.42264 0.80889 -0.02193 0.03298  0.00088  135 LYS A CA    
4928 C  C     . LYS B 135 ? 1.02537 1.39769 0.77578 -0.01543 0.04278  -0.00692 135 LYS A C     
4929 O  O     . LYS B 135 ? 1.07744 1.45329 0.82150 -0.00612 0.04156  -0.02873 135 LYS A O     
4930 C  CB    . LYS B 135 ? 0.95294 1.33669 0.67625 -0.02136 0.03628  0.01362  135 LYS A CB    
4931 C  CG    . LYS B 135 ? 1.05326 1.46254 0.75343 -0.00988 0.03870  -0.00246 135 LYS A CG    
4932 C  CD    . LYS B 135 ? 1.24526 1.68080 0.92398 -0.00944 0.04197  0.01257  135 LYS A CD    
4933 C  CE    . LYS B 135 ? 1.23094 1.69378 0.88405 0.00330  0.04454  -0.00406 135 LYS A CE    
4934 N  NZ    . LYS B 135 ? 1.30602 1.79631 0.93640 0.00432  0.04820  0.01192  135 LYS A NZ    
4935 N  N     . SER B 136 ? 1.03289 1.41370 0.79766 -0.02003 0.05194  0.01028  136 SER A N     
4936 C  CA    . SER B 136 ? 1.16656 1.56316 0.94037 -0.01420 0.06161  0.00442  136 SER A CA    
4937 C  C     . SER B 136 ? 1.09772 1.46979 0.88777 -0.01184 0.05647  -0.01259 136 SER A C     
4938 O  O     . SER B 136 ? 1.11698 1.50014 0.91121 -0.00391 0.06180  -0.02520 136 SER A O     
4939 C  CB    . SER B 136 ? 1.13022 1.54147 0.91858 -0.02095 0.07160  0.02849  136 SER A CB    
4940 O  OG    . SER B 136 ? 1.09647 1.48080 0.90525 -0.03053 0.06626  0.03922  136 SER A OG    
4941 N  N     . TYR B 137 ? 1.04926 1.38921 0.84863 -0.01806 0.04645  -0.01273 137 TYR A N     
4942 C  CA    . TYR B 137 ? 1.08418 1.39994 0.89767 -0.01588 0.04090  -0.02769 137 TYR A CA    
4943 C  C     . TYR B 137 ? 1.02013 1.32740 0.82316 -0.00833 0.03296  -0.05137 137 TYR A C     
4944 O  O     . TYR B 137 ? 0.98722 1.28126 0.80028 -0.00365 0.02998  -0.06650 137 TYR A O     
4945 C  CB    . TYR B 137 ? 1.10692 1.39291 0.93455 -0.02512 0.03404  -0.01733 137 TYR A CB    
4946 C  CG    . TYR B 137 ? 1.15343 1.44109 0.99688 -0.03185 0.03950  0.00198  137 TYR A CG    
4947 C  CD1   . TYR B 137 ? 1.16367 1.47230 1.01586 -0.02929 0.04912  0.00550  137 TYR A CD1   
4948 C  CD2   . TYR B 137 ? 1.15602 1.42447 1.00694 -0.04047 0.03453  0.01621  137 TYR A CD2   
4949 C  CE1   . TYR B 137 ? 1.09421 1.40378 0.96335 -0.03602 0.05281  0.02299  137 TYR A CE1   
4950 C  CE2   . TYR B 137 ? 1.04001 1.30840 0.90629 -0.04639 0.03789  0.03254  137 TYR A CE2   
4951 C  CZ    . TYR B 137 ? 1.06137 1.34991 0.93731 -0.04457 0.04661  0.03602  137 TYR A CZ    
4952 O  OH    . TYR B 137 ? 1.09050 1.37856 0.98406 -0.05102 0.04874  0.05218  137 TYR A OH    
4953 N  N     . GLY B 138 ? 0.90861 1.22268 0.69274 -0.00702 0.02861  -0.05488 138 GLY A N     
4954 C  CA    . GLY B 138 ? 0.86651 1.16882 0.64310 -0.00140 0.01854  -0.07669 138 GLY A CA    
4955 C  C     . GLY B 138 ? 1.07353 1.34425 0.85899 -0.00845 0.00716  -0.07656 138 GLY A C     
4956 O  O     . GLY B 138 ? 1.09824 1.35365 0.88520 -0.00501 -0.00182 -0.09430 138 GLY A O     
4957 N  N     . ILE B 139 ? 1.00329 1.26420 0.79564 -0.01799 0.00721  -0.05696 139 ILE A N     
4958 C  CA    . ILE B 139 ? 0.98767 1.22026 0.78974 -0.02456 -0.00199 -0.05470 139 ILE A CA    
4959 C  C     . ILE B 139 ? 0.93090 1.16701 0.72343 -0.03043 -0.00509 -0.04124 139 ILE A C     
4960 O  O     . ILE B 139 ? 0.96028 1.21729 0.74280 -0.03125 0.00099  -0.02865 139 ILE A O     
4961 C  CB    . ILE B 139 ? 0.90982 1.12407 0.73125 -0.02937 0.00014  -0.04519 139 ILE A CB    
4962 C  CG1   . ILE B 139 ? 0.96892 1.19061 0.79272 -0.03592 0.00613  -0.02281 139 ILE A CG1   
4963 C  CG2   . ILE B 139 ? 0.82395 1.04004 0.65437 -0.02311 0.00454  -0.05592 139 ILE A CG2   
4964 C  CD1   . ILE B 139 ? 0.84629 1.04786 0.68750 -0.04090 0.00586  -0.01356 139 ILE A CD1   
4965 N  N     . PRO B 140 ? 0.82199 1.03886 0.61823 -0.03451 -0.01451 -0.04277 140 PRO A N     
4966 C  CA    . PRO B 140 ? 0.93645 1.15586 0.72563 -0.03982 -0.01816 -0.02998 140 PRO A CA    
4967 C  C     . PRO B 140 ? 0.93316 1.14526 0.73234 -0.04701 -0.01437 -0.00890 140 PRO A C     
4968 O  O     . PRO B 140 ? 0.87703 1.07720 0.68997 -0.04866 -0.01099 -0.00524 140 PRO A O     
4969 C  CB    . PRO B 140 ? 0.80738 1.00840 0.60097 -0.04122 -0.02957 -0.04059 140 PRO A CB    
4970 C  CG    . PRO B 140 ? 0.84510 1.02654 0.65429 -0.04024 -0.03046 -0.05003 140 PRO A CG    
4971 C  CD    . PRO B 140 ? 0.91097 1.10510 0.71779 -0.03376 -0.02275 -0.05727 140 PRO A CD    
4972 N  N     . PHE B 141 ? 0.95648 1.17574 0.74838 -0.05080 -0.01588 0.00457  141 PHE A N     
4973 C  CA    . PHE B 141 ? 0.86766 1.07915 0.66847 -0.05728 -0.01436 0.02406  141 PHE A CA    
4974 C  C     . PHE B 141 ? 0.98575 1.18721 0.78644 -0.06090 -0.02282 0.02830  141 PHE A C     
4975 O  O     . PHE B 141 ? 1.05891 1.27009 0.84753 -0.05924 -0.02797 0.02336  141 PHE A O     
4976 C  CB    . PHE B 141 ? 0.99267 1.22487 0.78730 -0.05851 -0.00689 0.04013  141 PHE A CB    
4977 C  CG    . PHE B 141 ? 1.06777 1.29321 0.86908 -0.06488 -0.00807 0.05987  141 PHE A CG    
4978 C  CD1   . PHE B 141 ? 0.99013 1.19753 0.80816 -0.06853 -0.00743 0.06682  141 PHE A CD1   
4979 C  CD2   . PHE B 141 ? 1.03379 1.27061 0.82448 -0.06656 -0.01057 0.07099  141 PHE A CD2   
4980 C  CE1   . PHE B 141 ? 1.02875 1.22898 0.85335 -0.07346 -0.00938 0.08346  141 PHE A CE1   
4981 C  CE2   . PHE B 141 ? 1.06856 1.29810 0.86666 -0.07185 -0.01240 0.08877  141 PHE A CE2   
4982 C  CZ    . PHE B 141 ? 1.02567 1.23661 0.84102 -0.07517 -0.01186 0.09449  141 PHE A CZ    
4983 N  N     . ILE B 142 ? 1.04217 1.22501 0.85636 -0.06527 -0.02449 0.03698  142 ILE A N     
4984 C  CA    . ILE B 142 ? 0.93653 1.10840 0.75424 -0.06822 -0.03202 0.04020  142 ILE A CA    
4985 C  C     . ILE B 142 ? 1.00990 1.17383 0.83607 -0.07231 -0.03076 0.05781  142 ILE A C     
4986 O  O     . ILE B 142 ? 0.96285 1.11516 0.79958 -0.07317 -0.02725 0.06123  142 ILE A O     
4987 C  CB    . ILE B 142 ? 0.91326 1.06676 0.74110 -0.06785 -0.03690 0.02749  142 ILE A CB    
4988 C  CG1   . ILE B 142 ? 0.94305 1.10264 0.76402 -0.06366 -0.04009 0.00901  142 ILE A CG1   
4989 C  CG2   . ILE B 142 ? 0.90951 1.05317 0.74382 -0.07116 -0.04344 0.03289  142 ILE A CG2   
4990 C  CD1   . ILE B 142 ? 1.01666 1.15798 0.84966 -0.06354 -0.04470 -0.00291 142 ILE A CD1   
4991 N  N     . GLU B 143 ? 1.06702 1.23681 0.88873 -0.07432 -0.03446 0.06838  143 GLU A N     
4992 C  CA    . GLU B 143 ? 0.99654 1.15706 0.82723 -0.07750 -0.03509 0.08379  143 GLU A CA    
4993 C  C     . GLU B 143 ? 0.96453 1.10725 0.80578 -0.07808 -0.04018 0.08054  143 GLU A C     
4994 O  O     . GLU B 143 ? 1.04941 1.19321 0.88880 -0.07777 -0.04584 0.07377  143 GLU A O     
4995 C  CB    . GLU B 143 ? 1.13070 1.30497 0.95318 -0.07894 -0.03726 0.09729  143 GLU A CB    
4996 C  CG    . GLU B 143 ? 1.27331 1.46694 1.08606 -0.07880 -0.03126 0.10486  143 GLU A CG    
4997 C  CD    . GLU B 143 ? 1.43085 1.63651 1.23648 -0.08050 -0.03377 0.12083  143 GLU A CD    
4998 O  OE1   . GLU B 143 ? 1.39666 1.59132 1.21134 -0.08284 -0.03792 0.13154  143 GLU A OE1   
4999 O  OE2   . GLU B 143 ? 1.47137 1.69779 1.26199 -0.07888 -0.03176 0.12262  143 GLU A OE2   
5000 N  N     . THR B 144 ? 0.97438 1.10164 0.82709 -0.07869 -0.03834 0.08538  144 THR A N     
5001 C  CA    . THR B 144 ? 1.00145 1.11298 0.86406 -0.07844 -0.04151 0.08303  144 THR A CA    
5002 C  C     . THR B 144 ? 1.02578 1.12875 0.89577 -0.07894 -0.04233 0.09587  144 THR A C     
5003 O  O     . THR B 144 ? 0.96141 1.06817 0.83064 -0.07999 -0.04097 0.10631  144 THR A O     
5004 C  CB    . THR B 144 ? 0.85005 0.94896 0.71886 -0.07689 -0.03881 0.07294  144 THR A CB    
5005 O  OG1   . THR B 144 ? 1.00126 1.09432 0.87374 -0.07640 -0.03438 0.07767  144 THR A OG1   
5006 C  CG2   . THR B 144 ? 0.85993 0.96597 0.72280 -0.07568 -0.03859 0.05930  144 THR A CG2   
5007 N  N     . SER B 145 ? 0.96027 1.05187 0.83840 -0.07792 -0.04472 0.09500  145 SER A N     
5008 C  CA    . SER B 145 ? 0.95997 1.04167 0.84573 -0.07672 -0.04566 0.10448  145 SER A CA    
5009 C  C     . SER B 145 ? 0.97068 1.03994 0.86440 -0.07443 -0.04539 0.09935  145 SER A C     
5010 O  O     . SER B 145 ? 1.06389 1.13563 0.96064 -0.07475 -0.04808 0.09660  145 SER A O     
5011 C  CB    . SER B 145 ? 1.07238 1.16175 0.95745 -0.07746 -0.05034 0.11414  145 SER A CB    
5012 O  OG    . SER B 145 ? 0.99127 1.07016 0.88532 -0.07505 -0.05209 0.12033  145 SER A OG    
5013 N  N     . ALA B 146 ? 0.88301 0.93985 0.78045 -0.07211 -0.04233 0.09854  146 ALA A N     
5014 C  CA    . ALA B 146 ? 0.85049 0.89648 0.75396 -0.06931 -0.04115 0.09480  146 ALA A CA    
5015 C  C     . ALA B 146 ? 0.96735 1.01064 0.87682 -0.06672 -0.04317 0.10139  146 ALA A C     
5016 O  O     . ALA B 146 ? 0.93973 0.97910 0.85463 -0.06480 -0.04210 0.09940  146 ALA A O     
5017 C  CB    . ALA B 146 ? 0.78836 0.82259 0.69230 -0.06668 -0.03793 0.09219  146 ALA A CB    
5018 N  N     . LYS B 147 ? 0.97039 1.01621 0.87997 -0.06639 -0.04594 0.10967  147 LYS A N     
5019 C  CA    . LYS B 147 ? 1.00360 1.04747 0.91965 -0.06302 -0.04830 0.11540  147 LYS A CA    
5020 C  C     . LYS B 147 ? 0.93523 0.99005 0.85431 -0.06495 -0.05110 0.11551  147 LYS A C     
5021 O  O     . LYS B 147 ? 0.92026 0.97421 0.84690 -0.06254 -0.05066 0.11523  147 LYS A O     
5022 C  CB    . LYS B 147 ? 1.05185 1.09388 0.96863 -0.06202 -0.05156 0.12428  147 LYS A CB    
5023 C  CG    . LYS B 147 ? 0.96527 1.00392 0.88944 -0.05715 -0.05446 0.12954  147 LYS A CG    
5024 C  CD    . LYS B 147 ? 0.95661 0.99216 0.88286 -0.05652 -0.05893 0.13844  147 LYS A CD    
5025 C  CE    . LYS B 147 ? 0.92361 0.95443 0.85797 -0.05032 -0.06225 0.14238  147 LYS A CE    
5026 N  NZ    . LYS B 147 ? 1.03943 1.06595 0.97756 -0.04987 -0.06787 0.15141  147 LYS A NZ    
5027 N  N     . THR B 148 ? 0.97233 1.03858 0.88585 -0.06904 -0.05411 0.11600  148 THR A N     
5028 C  CA    . THR B 148 ? 0.87167 0.94906 0.78755 -0.07098 -0.05851 0.11557  148 THR A CA    
5029 C  C     . THR B 148 ? 0.92163 1.00257 0.83699 -0.07391 -0.05834 0.10529  148 THR A C     
5030 O  O     . THR B 148 ? 0.99074 1.08068 0.90904 -0.07591 -0.06307 0.10330  148 THR A O     
5031 C  CB    . THR B 148 ? 0.83007 0.91864 0.73899 -0.07297 -0.06313 0.12207  148 THR A CB    
5032 O  OG1   . THR B 148 ? 0.94211 1.03557 0.83995 -0.07562 -0.06119 0.11876  148 THR A OG1   
5033 C  CG2   . THR B 148 ? 0.86200 0.94573 0.77391 -0.07034 -0.06447 0.13306  148 THR A CG2   
5034 N  N     . ARG B 149 ? 0.90336 0.97701 0.81611 -0.07406 -0.05396 0.09852  149 ARG A N     
5035 C  CA    . ARG B 149 ? 0.90200 0.97639 0.81509 -0.07639 -0.05409 0.08811  149 ARG A CA    
5036 C  C     . ARG B 149 ? 0.88307 0.96961 0.78692 -0.07901 -0.05807 0.08278  149 ARG A C     
5037 O  O     . ARG B 149 ? 0.89638 0.98446 0.80088 -0.08063 -0.06015 0.07286  149 ARG A O     
5038 C  CB    . ARG B 149 ? 0.85493 0.92800 0.78085 -0.07703 -0.05560 0.08656  149 ARG A CB    
5039 C  CG    . ARG B 149 ? 1.05417 1.12109 0.98422 -0.07862 -0.05425 0.07753  149 ARG A CG    
5040 C  CD    . ARG B 149 ? 1.06289 1.13177 1.00733 -0.08100 -0.05731 0.07649  149 ARG A CD    
5041 N  NE    . ARG B 149 ? 0.93192 0.99625 0.88030 -0.08361 -0.05860 0.06696  149 ARG A NE    
5042 C  CZ    . ARG B 149 ? 0.84876 0.90193 0.80137 -0.08271 -0.05402 0.06576  149 ARG A CZ    
5043 N  NH1   . ARG B 149 ? 0.89065 0.93668 0.84280 -0.07897 -0.04769 0.07281  149 ARG A NH1   
5044 N  NH2   . ARG B 149 ? 0.86558 0.91435 0.82280 -0.08516 -0.05650 0.05702  149 ARG A NH2   
5045 N  N     . GLN B 150 ? 0.78687 0.88213 0.68201 -0.07908 -0.05946 0.08913  150 GLN A N     
5046 C  CA    . GLN B 150 ? 0.88470 0.99352 0.76838 -0.08049 -0.06263 0.08478  150 GLN A CA    
5047 C  C     . GLN B 150 ? 0.96804 1.07626 0.84473 -0.08016 -0.05847 0.07545  150 GLN A C     
5048 O  O     . GLN B 150 ? 0.93391 1.03719 0.80905 -0.07923 -0.05295 0.07858  150 GLN A O     
5049 C  CB    . GLN B 150 ? 0.93605 1.05422 0.81194 -0.08041 -0.06382 0.09627  150 GLN A CB    
5050 C  CG    . GLN B 150 ? 1.04286 1.17595 0.90358 -0.08087 -0.06436 0.09378  150 GLN A CG    
5051 C  CD    . GLN B 150 ? 1.24990 1.38914 1.10407 -0.08107 -0.06189 0.10708  150 GLN A CD    
5052 O  OE1   . GLN B 150 ? 1.16145 1.29951 1.01318 -0.08115 -0.05595 0.10863  150 GLN A OE1   
5053 N  NE2   . GLN B 150 ? 1.30256 1.44853 1.15540 -0.08132 -0.06684 0.11744  150 GLN A NE2   
5054 N  N     . GLY B 151 ? 0.97223 1.08528 0.84600 -0.08059 -0.06180 0.06339  151 GLY A N     
5055 C  CA    . GLY B 151 ? 0.76672 0.88089 0.63376 -0.07929 -0.05866 0.05304  151 GLY A CA    
5056 C  C     . GLY B 151 ? 0.85039 0.94959 0.72609 -0.07855 -0.05440 0.04805  151 GLY A C     
5057 O  O     . GLY B 151 ? 0.80235 0.90186 0.67376 -0.07691 -0.05159 0.03978  151 GLY A O     
5058 N  N     . VAL B 152 ? 0.89991 0.98686 0.78737 -0.07908 -0.05375 0.05292  152 VAL A N     
5059 C  CA    . VAL B 152 ? 0.75807 0.83098 0.65233 -0.07785 -0.04963 0.04980  152 VAL A CA    
5060 C  C     . VAL B 152 ? 0.82682 0.89600 0.72561 -0.07836 -0.05259 0.03711  152 VAL A C     
5061 O  O     . VAL B 152 ? 0.86159 0.92542 0.75950 -0.07664 -0.05002 0.03009  152 VAL A O     
5062 C  CB    . VAL B 152 ? 0.65669 0.71930 0.56059 -0.07734 -0.04789 0.05870  152 VAL A CB    
5063 C  CG1   . VAL B 152 ? 0.73006 0.77901 0.64023 -0.07586 -0.04451 0.05529  152 VAL A CG1   
5064 C  CG2   . VAL B 152 ? 0.71517 0.77836 0.61525 -0.07590 -0.04538 0.06939  152 VAL A CG2   
5065 N  N     . GLU B 153 ? 0.90623 0.97782 0.81154 -0.08070 -0.05876 0.03389  153 GLU A N     
5066 C  CA    . GLU B 153 ? 0.86130 0.92896 0.77244 -0.08153 -0.06329 0.02122  153 GLU A CA    
5067 C  C     . GLU B 153 ? 0.82415 0.90083 0.72283 -0.07927 -0.06502 0.00953  153 GLU A C     
5068 O  O     . GLU B 153 ? 0.86759 0.93846 0.76822 -0.07770 -0.06570 -0.00154 153 GLU A O     
5069 C  CB    . GLU B 153 ? 0.80944 0.87901 0.73198 -0.08504 -0.07072 0.02043  153 GLU A CB    
5070 C  CG    . GLU B 153 ? 0.81414 0.87477 0.75233 -0.08693 -0.06854 0.02982  153 GLU A CG    
5071 C  CD    . GLU B 153 ? 1.00028 1.06280 0.95375 -0.09103 -0.07607 0.02773  153 GLU A CD    
5072 O  OE1   . GLU B 153 ? 1.04300 1.10901 0.99652 -0.09236 -0.08382 0.01607  153 GLU A OE1   
5073 O  OE2   . GLU B 153 ? 1.10919 1.17035 1.07523 -0.09262 -0.07449 0.03740  153 GLU A OE2   
5074 N  N     . ASP B 154 ? 0.86722 0.95869 0.75289 -0.07851 -0.06559 0.01217  154 ASP A N     
5075 C  CA    . ASP B 154 ? 0.84145 0.94476 0.71327 -0.07544 -0.06633 0.00183  154 ASP A CA    
5076 C  C     . ASP B 154 ? 0.89520 0.99521 0.76389 -0.07229 -0.05905 -0.00138 154 ASP A C     
5077 O  O     . ASP B 154 ? 0.85497 0.95720 0.71997 -0.06912 -0.06008 -0.01483 154 ASP A O     
5078 C  CB    . ASP B 154 ? 0.76964 0.89006 0.62752 -0.07511 -0.06659 0.00928  154 ASP A CB    
5079 C  CG    . ASP B 154 ? 0.96027 1.09622 0.80238 -0.07143 -0.06856 -0.00186 154 ASP A CG    
5080 O  OD1   . ASP B 154 ? 1.07452 1.20742 0.91715 -0.06877 -0.07036 -0.01690 154 ASP A OD1   
5081 O  OD2   . ASP B 154 ? 0.94531 1.09683 0.77419 -0.07067 -0.06844 0.00451  154 ASP A OD2   
5082 N  N     . ALA B 155 ? 0.89289 0.98745 0.76400 -0.07268 -0.05232 0.01012  155 ALA A N     
5083 C  CA    . ALA B 155 ? 0.81173 0.90483 0.68084 -0.06990 -0.04580 0.00836  155 ALA A CA    
5084 C  C     . ALA B 155 ? 0.87393 0.95319 0.75232 -0.06828 -0.04666 -0.00220 155 ALA A C     
5085 O  O     . ALA B 155 ? 0.76980 0.85241 0.64495 -0.06476 -0.04577 -0.01326 155 ALA A O     
5086 C  CB    . ALA B 155 ? 0.81401 0.90282 0.68552 -0.07095 -0.04035 0.02271  155 ALA A CB    
5087 N  N     . PHE B 156 ? 0.80489 0.86906 0.69516 -0.07038 -0.04824 0.00154  156 PHE A N     
5088 C  CA    . PHE B 156 ? 0.75794 0.80788 0.65788 -0.06910 -0.04904 -0.00591 156 PHE A CA    
5089 C  C     . PHE B 156 ? 0.89200 0.94231 0.79454 -0.06856 -0.05601 -0.02077 156 PHE A C     
5090 O  O     . PHE B 156 ? 0.91701 0.96075 0.82316 -0.06563 -0.05670 -0.03099 156 PHE A O     
5091 C  CB    . PHE B 156 ? 0.74952 0.78530 0.66082 -0.07140 -0.04866 0.00331  156 PHE A CB    
5092 C  CG    . PHE B 156 ? 0.84668 0.87878 0.75601 -0.07036 -0.04263 0.01503  156 PHE A CG    
5093 C  CD1   . PHE B 156 ? 0.84534 0.88355 0.75095 -0.07174 -0.04141 0.02564  156 PHE A CD1   
5094 C  CD2   . PHE B 156 ? 0.88230 0.90419 0.79406 -0.06760 -0.03921 0.01492  156 PHE A CD2   
5095 C  CE1   . PHE B 156 ? 0.62259 0.65613 0.52721 -0.07032 -0.03720 0.03503  156 PHE A CE1   
5096 C  CE2   . PHE B 156 ? 0.87031 0.88830 0.78030 -0.06625 -0.03509 0.02437  156 PHE A CE2   
5097 C  CZ    . PHE B 156 ? 0.59645 0.61992 0.50304 -0.06758 -0.03424 0.03399  156 PHE A CZ    
5098 N  N     . TYR B 157 ? 0.84139 0.89897 0.74284 -0.07099 -0.06214 -0.02279 157 TYR A N     
5099 C  CA    . TYR B 157 ? 0.84274 0.89959 0.74786 -0.07048 -0.07060 -0.03800 157 TYR A CA    
5100 C  C     . TYR B 157 ? 0.89361 0.96253 0.78510 -0.06494 -0.07046 -0.05124 157 TYR A C     
5101 O  O     . TYR B 157 ? 0.85224 0.91611 0.74736 -0.06187 -0.07495 -0.06611 157 TYR A O     
5102 C  CB    . TYR B 157 ? 0.93724 0.99919 0.84579 -0.07452 -0.07826 -0.03676 157 TYR A CB    
5103 C  CG    . TYR B 157 ? 0.92286 0.97406 0.84812 -0.07963 -0.07917 -0.02584 157 TYR A CG    
5104 C  CD1   . TYR B 157 ? 0.83417 0.87248 0.76764 -0.07995 -0.07289 -0.01716 157 TYR A CD1   
5105 C  CD2   . TYR B 157 ? 0.83657 0.89186 0.76941 -0.08368 -0.08631 -0.02414 157 TYR A CD2   
5106 C  CE1   . TYR B 157 ? 0.88047 0.91125 0.82809 -0.08375 -0.07267 -0.00676 157 TYR A CE1   
5107 C  CE2   . TYR B 157 ? 0.85377 0.90169 0.80309 -0.08802 -0.08620 -0.01358 157 TYR A CE2   
5108 C  CZ    . TYR B 157 ? 0.86780 0.90392 0.82391 -0.08783 -0.07886 -0.00477 157 TYR A CZ    
5109 O  OH    . TYR B 157 ? 0.86708 0.89797 0.83848 -0.09131 -0.07769 0.00620  157 TYR A OH    
5110 N  N     . THR B 158 ? 0.90065 0.98596 0.77694 -0.06325 -0.06528 -0.04578 158 THR A N     
5111 C  CA    . THR B 158 ? 0.86805 0.96781 0.73065 -0.05736 -0.06309 -0.05651 158 THR A CA    
5112 C  C     . THR B 158 ? 0.77608 0.86894 0.64332 -0.05334 -0.05787 -0.06206 158 THR A C     
5113 O  O     . THR B 158 ? 0.84934 0.94661 0.71288 -0.04770 -0.05936 -0.07737 158 THR A O     
5114 C  CB    . THR B 158 ? 0.85017 0.96891 0.69767 -0.05715 -0.05720 -0.04554 158 THR A CB    
5115 O  OG1   . THR B 158 ? 0.82703 0.95264 0.66986 -0.06017 -0.06310 -0.04110 158 THR A OG1   
5116 C  CG2   . THR B 158 ? 0.67848 0.81494 0.51171 -0.05070 -0.05339 -0.05515 158 THR A CG2   
5117 N  N     . LEU B 159 ? 0.73828 0.82049 0.61366 -0.05547 -0.05227 -0.05045 159 LEU A N     
5118 C  CA    . LEU B 159 ? 0.73028 0.80485 0.61157 -0.05174 -0.04831 -0.05501 159 LEU A CA    
5119 C  C     . LEU B 159 ? 0.76779 0.82700 0.66048 -0.05012 -0.05524 -0.06829 159 LEU A C     
5120 O  O     . LEU B 159 ? 0.89277 0.95171 0.78648 -0.04456 -0.05508 -0.08045 159 LEU A O     
5121 C  CB    . LEU B 159 ? 0.76205 0.82707 0.64961 -0.05435 -0.04273 -0.04003 159 LEU A CB    
5122 C  CG    . LEU B 159 ? 0.75976 0.81537 0.65462 -0.05080 -0.03952 -0.04302 159 LEU A CG    
5123 C  CD1   . LEU B 159 ? 0.77912 0.85017 0.66738 -0.04527 -0.03530 -0.05169 159 LEU A CD1   
5124 C  CD2   . LEU B 159 ? 0.71752 0.76502 0.61641 -0.05307 -0.03514 -0.02838 159 LEU A CD2   
5125 N  N     . VAL B 160 ? 0.83802 0.88466 0.74091 -0.05487 -0.06153 -0.06577 160 VAL A N     
5126 C  CA    . VAL B 160 ? 0.75790 0.78929 0.67413 -0.05442 -0.06920 -0.07701 160 VAL A CA    
5127 C  C     . VAL B 160 ? 0.85064 0.89012 0.76122 -0.04967 -0.07580 -0.09636 160 VAL A C     
5128 O  O     . VAL B 160 ? 0.85310 0.88428 0.77027 -0.04522 -0.07952 -0.10981 160 VAL A O     
5129 C  CB    . VAL B 160 ? 0.84936 0.86917 0.77864 -0.06124 -0.07434 -0.06877 160 VAL A CB    
5130 C  CG1   . VAL B 160 ? 0.79413 0.79939 0.73896 -0.06174 -0.08372 -0.08024 160 VAL A CG1   
5131 C  CG2   . VAL B 160 ? 0.87599 0.88675 0.81058 -0.06398 -0.06762 -0.05168 160 VAL A CG2   
5132 N  N     . ARG B 161 ? 0.79510 0.85100 0.69289 -0.04979 -0.07780 -0.09846 161 ARG A N     
5133 C  CA    . ARG B 161 ? 0.83213 0.89802 0.72112 -0.04398 -0.08404 -0.11762 161 ARG A CA    
5134 C  C     . ARG B 161 ? 0.94696 1.02300 0.82653 -0.03561 -0.07741 -0.12663 161 ARG A C     
5135 O  O     . ARG B 161 ? 1.05623 1.13262 0.93505 -0.02903 -0.08267 -0.14549 161 ARG A O     
5136 C  CB    . ARG B 161 ? 0.84997 0.93341 0.72453 -0.04524 -0.08676 -0.11605 161 ARG A CB    
5137 C  CG    . ARG B 161 ? 0.83095 0.90683 0.71586 -0.05302 -0.09391 -0.10802 161 ARG A CG    
5138 C  CD    . ARG B 161 ? 0.86493 0.95839 0.73556 -0.05320 -0.09839 -0.10872 161 ARG A CD    
5139 N  NE    . ARG B 161 ? 1.12348 1.21260 1.00405 -0.06077 -0.10258 -0.09654 161 ARG A NE    
5140 C  CZ    . ARG B 161 ? 1.12246 1.21821 0.99867 -0.06424 -0.09639 -0.07868 161 ARG A CZ    
5141 N  NH1   . ARG B 161 ? 1.08278 1.18933 0.94530 -0.06171 -0.08631 -0.07007 161 ARG A NH1   
5142 N  NH2   . ARG B 161 ? 1.06237 1.15401 0.94971 -0.07031 -0.10071 -0.06919 161 ARG A NH2   
5143 N  N     . GLU B 162 ? 0.86932 0.95398 0.74298 -0.03544 -0.06629 -0.11384 162 GLU A N     
5144 C  CA    . GLU B 162 ? 0.86943 0.96505 0.73717 -0.02789 -0.05926 -0.12085 162 GLU A CA    
5145 C  C     . GLU B 162 ? 0.82805 0.90591 0.71100 -0.02466 -0.06092 -0.12889 162 GLU A C     
5146 O  O     . GLU B 162 ? 1.05999 1.14418 0.94103 -0.01661 -0.05952 -0.14251 162 GLU A O     
5147 C  CB    . GLU B 162 ? 0.76240 0.87108 0.62344 -0.02967 -0.04788 -0.10383 162 GLU A CB    
5148 C  CG    . GLU B 162 ? 0.80724 0.93536 0.65265 -0.03193 -0.04553 -0.09505 162 GLU A CG    
5149 C  CD    . GLU B 162 ? 0.99760 1.14866 0.82640 -0.02443 -0.04429 -0.10753 162 GLU A CD    
5150 O  OE1   . GLU B 162 ? 0.94434 1.10834 0.76971 -0.01887 -0.03626 -0.11001 162 GLU A OE1   
5151 O  OE2   . GLU B 162 ? 0.96096 1.11807 0.78020 -0.02370 -0.05143 -0.11498 162 GLU A OE2   
5152 N  N     . ILE B 163 ? 0.95448 1.01099 0.85250 -0.03027 -0.06370 -0.12028 163 ILE A N     
5153 C  CA    . ILE B 163 ? 0.84420 0.88242 0.75714 -0.02745 -0.06640 -0.12667 163 ILE A CA    
5154 C  C     . ILE B 163 ? 0.93407 0.96327 0.85392 -0.02413 -0.07763 -0.14584 163 ILE A C     
5155 O  O     . ILE B 163 ? 0.93412 0.95661 0.86084 -0.01757 -0.08003 -0.15877 163 ILE A O     
5156 C  CB    . ILE B 163 ? 0.85931 0.87879 0.78472 -0.03410 -0.06570 -0.11039 163 ILE A CB    
5157 C  CG1   . ILE B 163 ? 0.81152 0.83880 0.73054 -0.03600 -0.05570 -0.09392 163 ILE A CG1   
5158 C  CG2   . ILE B 163 ? 0.87397 0.87361 0.81492 -0.03142 -0.06967 -0.11593 163 ILE A CG2   
5159 C  CD1   . ILE B 163 ? 0.75722 0.76733 0.68614 -0.04038 -0.05451 -0.07951 163 ILE A CD1   
5160 N  N     . ARG B 164 ? 0.98094 1.00943 0.90039 -0.02842 -0.08554 -0.14835 164 ARG A N     
5161 C  CA    . ARG B 164 ? 1.08517 1.10540 1.01175 -0.02552 -0.09791 -0.16765 164 ARG A CA    
5162 C  C     . ARG B 164 ? 1.13889 1.17457 1.05245 -0.01465 -0.09800 -0.18768 164 ARG A C     
5163 O  O     . ARG B 164 ? 1.19394 1.21991 1.11594 -0.00828 -0.10459 -0.20484 164 ARG A O     
5164 C  CB    . ARG B 164 ? 0.99692 1.01757 0.92425 -0.03209 -0.10634 -0.16631 164 ARG A CB    
5165 C  CG    . ARG B 164 ? 0.95556 0.95973 0.89995 -0.04205 -0.10828 -0.14979 164 ARG A CG    
5166 C  CD    . ARG B 164 ? 1.03339 1.04399 0.97644 -0.04816 -0.11449 -0.14645 164 ARG A CD    
5167 N  NE    . ARG B 164 ? 0.90184 0.89889 0.86269 -0.05726 -0.11612 -0.13103 164 ARG A NE    
5168 C  CZ    . ARG B 164 ? 0.88737 0.89003 0.84975 -0.06363 -0.11879 -0.12222 164 ARG A CZ    
5169 N  NH1   . ARG B 164 ? 0.86584 0.88629 0.81247 -0.06228 -0.12077 -0.12650 164 ARG A NH1   
5170 N  NH2   . ARG B 164 ? 0.83920 0.83036 0.81936 -0.07113 -0.11929 -0.10824 164 ARG A NH2   
5171 N  N     . GLN B 165 ? 1.10443 1.16479 0.99752 -0.01199 -0.09065 -0.18545 165 GLN A N     
5172 C  CA    . GLN B 165 ? 1.11352 1.19274 0.99204 -0.00092 -0.08856 -0.20274 165 GLN A CA    
5173 C  C     . GLN B 165 ? 1.05134 1.12760 0.93710 0.00630  -0.08291 -0.20840 165 GLN A C     
5174 O  O     . GLN B 165 ? 1.08164 1.16249 0.96510 0.01650  -0.08602 -0.22869 165 GLN A O     
5175 C  CB    . GLN B 165 ? 0.94150 1.04849 0.79803 -0.00047 -0.07921 -0.19355 165 GLN A CB    
5176 C  CG    . GLN B 165 ? 1.07252 1.20358 0.91156 0.01123  -0.07518 -0.20915 165 GLN A CG    
5177 C  CD    . GLN B 165 ? 1.19521 1.32766 1.02720 0.01762  -0.08769 -0.23231 165 GLN A CD    
5178 O  OE1   . GLN B 165 ? 1.29270 1.41596 1.12719 0.01185  -0.09829 -0.23302 165 GLN A OE1   
5179 N  NE2   . GLN B 165 ? 1.03863 1.18310 0.86240 0.03003  -0.08693 -0.25202 165 GLN A NE2   
5180 N  N     . TYR B 166 ? 0.98186 1.05044 0.87671 0.00179  -0.07531 -0.19151 166 TYR A N     
5181 C  CA    . TYR B 166 ? 1.01078 1.07587 0.91430 0.00820  -0.07064 -0.19551 166 TYR A CA    
5182 C  C     . TYR B 166 ? 1.09871 1.13928 1.02026 0.01112  -0.08162 -0.20922 166 TYR A C     
5183 O  O     . TYR B 166 ? 1.20855 1.25024 1.13341 0.02100  -0.08284 -0.22549 166 TYR A O     
5184 C  CB    . TYR B 166 ? 0.94862 1.01050 0.85729 0.00221  -0.06154 -0.17380 166 TYR A CB    
5185 C  CG    . TYR B 166 ? 1.01935 1.07848 0.93762 0.00818  -0.05685 -0.17577 166 TYR A CG    
5186 C  CD1   . TYR B 166 ? 1.05011 1.08463 0.98590 0.00840  -0.06301 -0.17767 166 TYR A CD1   
5187 C  CD2   . TYR B 166 ? 1.08160 1.16339 0.99253 0.01338  -0.04634 -0.17447 166 TYR A CD2   
5188 C  CE1   . TYR B 166 ? 1.16614 1.19824 1.11097 0.01422  -0.05954 -0.17928 166 TYR A CE1   
5189 C  CE2   . TYR B 166 ? 1.15029 1.23063 1.07175 0.01885  -0.04254 -0.17621 166 TYR A CE2   
5190 C  CZ    . TYR B 166 ? 1.10105 1.15624 1.03900 0.01949  -0.04949 -0.17902 166 TYR A CZ    
5191 O  OH    . TYR B 166 ? 1.08367 1.13745 1.03231 0.02533  -0.04654 -0.18070 166 TYR A OH    
5192 N  N     . ARG B 167 ? 1.06893 1.08746 1.00354 0.00275  -0.08968 -0.20227 167 ARG A N     
5193 C  CA    . ARG B 167 ? 1.11880 1.11254 1.07299 0.00425  -0.10053 -0.21252 167 ARG A CA    
5194 C  C     . ARG B 167 ? 1.15609 1.14930 1.10984 0.01024  -0.11238 -0.23651 167 ARG A C     
5195 O  O     . ARG B 167 ? 1.22104 1.19857 1.18872 0.01584  -0.12087 -0.25122 167 ARG A O     
5196 C  CB    . ARG B 167 ? 0.99941 0.97184 0.96852 -0.00689 -0.10476 -0.19596 167 ARG A CB    
5197 C  CG    . ARG B 167 ? 0.87755 0.84867 0.84671 -0.01212 -0.09444 -0.17337 167 ARG A CG    
5198 C  CD    . ARG B 167 ? 0.83016 0.78516 0.81050 -0.02254 -0.09775 -0.15728 167 ARG A CD    
5199 N  NE    . ARG B 167 ? 0.97501 0.92718 0.95514 -0.02622 -0.08884 -0.13724 167 ARG A NE    
5200 C  CZ    . ARG B 167 ? 0.99664 0.93897 0.98312 -0.03426 -0.08842 -0.12047 167 ARG A CZ    
5201 N  NH1   . ARG B 167 ? 1.04907 0.98427 1.04434 -0.04045 -0.09578 -0.11958 167 ARG A NH1   
5202 N  NH2   . ARG B 167 ? 1.04565 0.98605 1.03005 -0.03575 -0.08063 -0.10452 167 ARG A NH2   
5203 N  N     . MET B 168 ? 1.09818 1.10771 1.03631 0.00959  -0.11397 -0.24109 168 MET A N     
5204 C  CA    . MET B 168 ? 1.20294 1.21218 1.13920 0.01505  -0.12672 -0.26425 168 MET A CA    
5205 C  C     . MET B 168 ? 1.06246 1.09913 0.97590 0.02691  -0.12159 -0.27990 168 MET A C     
5206 O  O     . MET B 168 ? 1.19158 1.23256 1.09839 0.03374  -0.13123 -0.30113 168 MET A O     
5207 C  CB    . MET B 168 ? 1.24955 1.25524 1.18681 0.00542  -0.13521 -0.25897 168 MET A CB    
5208 C  CG    . MET B 168 ? 1.22607 1.20839 1.18547 -0.00662 -0.13861 -0.24118 168 MET A CG    
5209 S  SD    . MET B 168 ? 1.36671 1.35211 1.32566 -0.01885 -0.14295 -0.22746 168 MET A SD    
5210 C  CE    . MET B 168 ? 1.06102 1.04609 1.02030 -0.01449 -0.16112 -0.25444 168 MET A CE    
5211 P  PG    . GTP C .   ? 0.87107 0.83904 0.79428 -0.04861 -0.04232 0.07051  201 GTP A PG    
5212 O  O1G   . GTP C .   ? 0.95549 0.91727 0.88704 -0.04791 -0.04817 0.07181  201 GTP A O1G   
5213 O  O2G   . GTP C .   ? 0.84648 0.80303 0.76160 -0.04231 -0.04241 0.06640  201 GTP A O2G   
5214 O  O3G   . GTP C .   ? 0.74429 0.72368 0.66922 -0.05169 -0.03791 0.06667  201 GTP A O3G   
5215 O  O3B   . GTP C .   ? 0.92055 0.89550 0.84285 -0.05228 -0.04149 0.07796  201 GTP A O3B   
5216 P  PB    . GTP C .   ? 0.83708 0.82057 0.75276 -0.05419 -0.03695 0.07771  201 GTP A PB    
5217 O  O1B   . GTP C .   ? 0.76984 0.74524 0.68009 -0.04971 -0.03553 0.07213  201 GTP A O1B   
5218 O  O2B   . GTP C .   ? 0.84170 0.84010 0.75783 -0.05893 -0.03316 0.07637  201 GTP A O2B   
5219 O  O3A   . GTP C .   ? 0.84477 0.82915 0.76038 -0.05506 -0.03903 0.08547  201 GTP A O3A   
5220 P  PA    . GTP C .   ? 0.87751 0.85659 0.78843 -0.05112 -0.03887 0.08570  201 GTP A PA    
5221 O  O1A   . GTP C .   ? 0.92235 0.88787 0.83082 -0.04423 -0.04007 0.08159  201 GTP A O1A   
5222 O  O2A   . GTP C .   ? 0.81975 0.80710 0.72715 -0.05342 -0.03513 0.08316  201 GTP A O2A   
5223 O  "O5'" . GTP C .   ? 0.83060 0.81028 0.74476 -0.05162 -0.04244 0.09377  201 GTP A "O5'" 
5224 C  "C5'" . GTP C .   ? 0.90298 0.88261 0.82362 -0.05420 -0.04614 0.09926  201 GTP A "C5'" 
5225 C  "C4'" . GTP C .   ? 0.85192 0.82821 0.77526 -0.05248 -0.05014 0.10576  201 GTP A "C4'" 
5226 O  "O4'" . GTP C .   ? 0.92002 0.90942 0.84300 -0.05772 -0.04883 0.11219  201 GTP A "O4'" 
5227 C  "C3'" . GTP C .   ? 0.96199 0.93198 0.88076 -0.04586 -0.04946 0.10224  201 GTP A "C3'" 
5228 O  "O3'" . GTP C .   ? 0.96902 0.92766 0.89107 -0.04019 -0.05471 0.10324  201 GTP A "O3'" 
5229 C  "C2'" . GTP C .   ? 0.87769 0.85868 0.79515 -0.04848 -0.04751 0.10634  201 GTP A "C2'" 
5230 O  "O2'" . GTP C .   ? 1.03621 1.01304 0.95547 -0.04338 -0.04985 0.10893  201 GTP A "O2'" 
5231 C  "C1'" . GTP C .   ? 0.90549 0.89653 0.82581 -0.05534 -0.04875 0.11329  201 GTP A "C1'" 
5232 N  N9    . GTP C .   ? 0.97850 0.98349 0.89399 -0.05973 -0.04515 0.11268  201 GTP A N9    
5233 C  C8    . GTP C .   ? 0.94930 0.95840 0.86034 -0.06096 -0.04104 0.10524  201 GTP A C8    
5234 N  N7    . GTP C .   ? 0.92124 0.94322 0.82883 -0.06467 -0.04005 0.10588  201 GTP A N7    
5235 C  C5    . GTP C .   ? 0.98102 1.00783 0.89016 -0.06590 -0.04322 0.11443  201 GTP A C5    
5236 C  C6    . GTP C .   ? 1.03544 1.07502 0.94158 -0.06897 -0.04453 0.11869  201 GTP A C6    
5237 O  O6    . GTP C .   ? 0.99742 1.04641 0.89834 -0.07110 -0.04287 0.11336  201 GTP A O6    
5238 N  N1    . GTP C .   ? 1.08871 1.12992 0.99788 -0.06919 -0.04857 0.12862  201 GTP A N1    
5239 C  C2    . GTP C .   ? 0.95731 0.98662 0.87340 -0.06635 -0.05152 0.13348  201 GTP A C2    
5240 N  N2    . GTP C .   ? 1.06273 1.09236 0.98311 -0.06627 -0.05614 0.14307  201 GTP A N2    
5241 N  N3    . GTP C .   ? 0.88395 0.90052 0.80265 -0.06311 -0.05057 0.12800  201 GTP A N3    
5242 C  C4    . GTP C .   ? 0.93621 0.95201 0.85101 -0.06292 -0.04637 0.11903  201 GTP A C4    
5243 MG MG    . MG  D .   ? 0.81860 0.78076 0.72603 -0.04331 -0.03575 0.06467  202 MG  A MG    
5244 O  O     . HOH E .   ? 0.85266 0.92725 0.81335 -0.05373 -0.12061 0.24125  601 HOH B O     
5245 O  O     . HOH E .   ? 0.87474 0.76516 0.73365 0.00767  -0.04432 0.05475  602 HOH B O     
5246 O  O     . HOH E .   ? 0.94455 0.80711 0.68006 0.18366  -0.07913 -0.01547 603 HOH B O     
5247 O  O     . HOH F .   ? 0.77032 0.93349 0.61145 -0.02435 -0.01924 -0.08114 301 HOH A O     
5248 O  O     . HOH F .   ? 0.75677 0.69495 0.64922 -0.02806 -0.03305 0.06370  302 HOH A O     
5249 O  O     . HOH F .   ? 0.82450 0.77553 0.72751 -0.03684 -0.03895 0.07008  303 HOH A O     
5250 O  O     . HOH F .   ? 0.82820 0.62627 0.99652 -0.08784 -0.13708 -0.03905 304 HOH A O     
5251 O  O     . HOH F .   ? 0.81402 0.78689 0.72342 -0.04739 -0.03181 0.05809  305 HOH A O     
5252 O  O     . HOH F .   ? 0.74823 0.65710 0.88146 -0.10958 -0.16281 -0.08620 306 HOH A O     
# 
