data_9J40
# 
_entry.id   9J40 
# 
_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   9J40         pdb_00009j40 10.2210/pdb9j40/pdb 
WWPDB D_1300050291 ?            ?                   
EMDB  EMD-61129    ?            ?                   
# 
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  'EM metadata'     1 0 2025-04-02 ? 
3  'Half map'        1 0 2025-04-02 1 
4  'Half map'        1 0 2025-04-02 2 
5  Image             1 0 2025-04-02 ? 
6  'Primary map'     1 0 2025-04-02 ? 
7  'Structure model' 1 1 2025-04-09 ? 
8  'Half map'        1 0 2025-04-02 1 
9  'Half map'        1 0 2025-04-02 2 
10 Image             1 0 2025-04-02 ? 
11 'Primary map'     1 0 2025-04-02 ? 
12 'Structure model' 1 2 2025-06-18 ? 
13 'EM metadata'     1 1 2025-06-18 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1  1  'Structure model' repository 'Initial release' ? ? 
2  2  'EM metadata'     repository 'Initial release' ? ? 
3  3  'Half map'        repository 'Initial release' ? ? 
4  4  'Half map'        repository 'Initial release' ? ? 
5  5  Image             repository 'Initial release' ? ? 
6  6  'Primary map'     repository 'Initial release' ? ? 
7  8  'Half map'        repository 'Initial release' ? ? 
8  9  'Half map'        repository 'Initial release' ? ? 
9  10 Image             repository 'Initial release' ? ? 
10 11 'Primary map'     repository 'Initial release' ? ? 
# 
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 7  'Structure model' 'Data collection'      
2 7  'Structure model' 'Database references'  
3 12 'Structure model' 'Data collection'      
4 13 'EM metadata'     'Data processing'      
5 13 'EM metadata'     'Experimental summary' 
# 
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 7  'Structure model' citation    
2 7  'Structure model' em_admin    
3 12 'Structure model' em_admin    
4 12 'Structure model' em_software 
5 13 'EM metadata'     em_admin    
6 13 'EM metadata'     em_software 
# 
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 7  'Structure model' '_citation.page_last'               
2 7  'Structure model' '_citation.pdbx_database_id_PubMed' 
3 7  'Structure model' '_citation.title'                   
4 7  'Structure model' '_em_admin.last_update'             
5 12 'Structure model' '_em_admin.last_update'             
6 12 'Structure model' '_em_software.name'                 
7 13 'EM metadata'     '_em_admin.last_update'             
8 13 'EM metadata'     '_em_software.name'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J40 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of lysosome cholesterol sencing protein LYCHOS complexed with IS' 
_pdbx_database_related.db_id          EMD-61129 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hongwuqian@ustc.edu.cn 
_pdbx_contact_author.name_first         Qian 
_pdbx_contact_author.name_last          hongwu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9940-8003 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qian, H.W.' 1 ?                   
'Wang, Z.H.' 2 0000-0001-6476-9781 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2815 
_citation.page_last                 2815 
_citation.title                     'Structural basis for cholesterol sensing of LYCHOS and its interaction with indoxyl sulfate.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58087-9 
_citation.pdbx_database_id_PubMed   40118871 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, Z.' 1 ? 
primary 'He, J.'   2 ? 
primary 'Yang, Y.' 3 ? 
primary 'He, Y.'   4 ? 
primary 'Qian, H.' 5 ? 
# 
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 'G protein-coupled receptor 155,Lysosomal cholesterol signaling protein fusion protein'          96994.695 2 ? ? 
? ? 
2 non-polymer syn '(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' 760.076   6 ? ? 
? ? 
3 non-polymer syn 3-SULFOOXY-1H-INDOLE                                                                             213.210   2 ? ? 
? ? 
4 non-polymer syn CHOLESTEROL                                                                                      386.654   2 ? ? 
? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                                                         221.208   2 ? ? 
? ? 
6 non-polymer syn TRYPTOPHAN                                                                                       204.225   2 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'LYCHOS,G-protein coupled receptor PGR22' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MNSNLPAENLTIAVNMTKTLPTAVTHGFNSTNDPPSMSITRLFPALLECFGIVLCGYIAGRANVITSTQAKGLGNFVSRF
ALPALLFKNMVVLNFSNVDWSFLYSILIAKASVFFIVCVLTLLVASPDSRFSKAGLFPIFATQSNDFALGYPIVEALYQT
TYPEYLQYIYLVAPISLMMLNPIGFIFCEIQKWKDTQNASQNKIKIVGLGLLRVLQNPIVFMVFIGIAFNFILDRKVPVY
VENFLDGLGNSFSGSALFYLGLTMVGKIKRLKKSAFVVLILLITAKLLVLPLLCREMVELLDKGDSVVNHTSLSNYAFLY
GVFPVAPGVAIFATQFNMEVEIITSGMVISTFVSAPIMYVSAWLLTFPTMDPKPLAYAIQNVSFDISIVSLISLIWSLAI
LLLSKKYKQLPHMLTTNLLIAQSIVCAGMMIWNFVKEKNFVGQILVFVLLYSSLYSTYLWTGLLAISLFLLKKRERVQIP
VGIIIISGWGIPALLVGVLLITGKHNGDSIDSAFFYGKEQMITTAVTLFCSILIAGISLMCMNQTAQAGSYEGFDQSQSH
KVVEPGNTAFEESPAPVNEPELFTSSIPETSCCSCSMGNGELHCPSIEPIANTSTSEPVIPSFEKNNHCVSRCNSQSCIL
AQEEEQYLQSGDQQLTRHVLLCLLLIIGLFANLSSCLWWLFNQEPGRLYVELQFFCAVFNFGQGFISFGIFGLDKHLIIL
PFKRRLEFLWNNKDTAENRDSPVSEEIKMTCQQFIHYHRDLCIRNIVKERRCGAKTSAGTFCGCDLVSWLIEVGLASDRG
EAVIYGDRLVQGGVIQHITNEYEFRDEYLFYRFLQKSPEQSPPAINANTLQQERYKEIEHSSPPSHSPKT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNSNLPAENLTIAVNMTKTLPTAVTHGFNSTNDPPSMSITRLFPALLECFGIVLCGYIAGRANVITSTQAKGLGNFVSRF
ALPALLFKNMVVLNFSNVDWSFLYSILIAKASVFFIVCVLTLLVASPDSRFSKAGLFPIFATQSNDFALGYPIVEALYQT
TYPEYLQYIYLVAPISLMMLNPIGFIFCEIQKWKDTQNASQNKIKIVGLGLLRVLQNPIVFMVFIGIAFNFILDRKVPVY
VENFLDGLGNSFSGSALFYLGLTMVGKIKRLKKSAFVVLILLITAKLLVLPLLCREMVELLDKGDSVVNHTSLSNYAFLY
GVFPVAPGVAIFATQFNMEVEIITSGMVISTFVSAPIMYVSAWLLTFPTMDPKPLAYAIQNVSFDISIVSLISLIWSLAI
LLLSKKYKQLPHMLTTNLLIAQSIVCAGMMIWNFVKEKNFVGQILVFVLLYSSLYSTYLWTGLLAISLFLLKKRERVQIP
VGIIIISGWGIPALLVGVLLITGKHNGDSIDSAFFYGKEQMITTAVTLFCSILIAGISLMCMNQTAQAGSYEGFDQSQSH
KVVEPGNTAFEESPAPVNEPELFTSSIPETSCCSCSMGNGELHCPSIEPIANTSTSEPVIPSFEKNNHCVSRCNSQSCIL
AQEEEQYLQSGDQQLTRHVLLCLLLIIGLFANLSSCLWWLFNQEPGRLYVELQFFCAVFNFGQGFISFGIFGLDKHLIIL
PFKRRLEFLWNNKDTAENRDSPVSEEIKMTCQQFIHYHRDLCIRNIVKERRCGAKTSAGTFCGCDLVSWLIEVGLASDRG
EAVIYGDRLVQGGVIQHITNEYEFRDEYLFYRFLQKSPEQSPPAINANTLQQERYKEIEHSSPPSHSPKT
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' POV 
3 3-SULFOOXY-1H-INDOLE                                                                             IOS 
4 CHOLESTEROL                                                                                      CLR 
5 2-acetamido-2-deoxy-beta-D-glucopyranose                                                         NAG 
6 TRYPTOPHAN                                                                                       TRP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   SER n 
1 4   ASN n 
1 5   LEU n 
1 6   PRO n 
1 7   ALA n 
1 8   GLU n 
1 9   ASN n 
1 10  LEU n 
1 11  THR n 
1 12  ILE n 
1 13  ALA n 
1 14  VAL n 
1 15  ASN n 
1 16  MET n 
1 17  THR n 
1 18  LYS n 
1 19  THR n 
1 20  LEU n 
1 21  PRO n 
1 22  THR n 
1 23  ALA n 
1 24  VAL n 
1 25  THR n 
1 26  HIS n 
1 27  GLY n 
1 28  PHE n 
1 29  ASN n 
1 30  SER n 
1 31  THR n 
1 32  ASN n 
1 33  ASP n 
1 34  PRO n 
1 35  PRO n 
1 36  SER n 
1 37  MET n 
1 38  SER n 
1 39  ILE n 
1 40  THR n 
1 41  ARG n 
1 42  LEU n 
1 43  PHE n 
1 44  PRO n 
1 45  ALA n 
1 46  LEU n 
1 47  LEU n 
1 48  GLU n 
1 49  CYS n 
1 50  PHE n 
1 51  GLY n 
1 52  ILE n 
1 53  VAL n 
1 54  LEU n 
1 55  CYS n 
1 56  GLY n 
1 57  TYR n 
1 58  ILE n 
1 59  ALA n 
1 60  GLY n 
1 61  ARG n 
1 62  ALA n 
1 63  ASN n 
1 64  VAL n 
1 65  ILE n 
1 66  THR n 
1 67  SER n 
1 68  THR n 
1 69  GLN n 
1 70  ALA n 
1 71  LYS n 
1 72  GLY n 
1 73  LEU n 
1 74  GLY n 
1 75  ASN n 
1 76  PHE n 
1 77  VAL n 
1 78  SER n 
1 79  ARG n 
1 80  PHE n 
1 81  ALA n 
1 82  LEU n 
1 83  PRO n 
1 84  ALA n 
1 85  LEU n 
1 86  LEU n 
1 87  PHE n 
1 88  LYS n 
1 89  ASN n 
1 90  MET n 
1 91  VAL n 
1 92  VAL n 
1 93  LEU n 
1 94  ASN n 
1 95  PHE n 
1 96  SER n 
1 97  ASN n 
1 98  VAL n 
1 99  ASP n 
1 100 TRP n 
1 101 SER n 
1 102 PHE n 
1 103 LEU n 
1 104 TYR n 
1 105 SER n 
1 106 ILE n 
1 107 LEU n 
1 108 ILE n 
1 109 ALA n 
1 110 LYS n 
1 111 ALA n 
1 112 SER n 
1 113 VAL n 
1 114 PHE n 
1 115 PHE n 
1 116 ILE n 
1 117 VAL n 
1 118 CYS n 
1 119 VAL n 
1 120 LEU n 
1 121 THR n 
1 122 LEU n 
1 123 LEU n 
1 124 VAL n 
1 125 ALA n 
1 126 SER n 
1 127 PRO n 
1 128 ASP n 
1 129 SER n 
1 130 ARG n 
1 131 PHE n 
1 132 SER n 
1 133 LYS n 
1 134 ALA n 
1 135 GLY n 
1 136 LEU n 
1 137 PHE n 
1 138 PRO n 
1 139 ILE n 
1 140 PHE n 
1 141 ALA n 
1 142 THR n 
1 143 GLN n 
1 144 SER n 
1 145 ASN n 
1 146 ASP n 
1 147 PHE n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 TYR n 
1 152 PRO n 
1 153 ILE n 
1 154 VAL n 
1 155 GLU n 
1 156 ALA n 
1 157 LEU n 
1 158 TYR n 
1 159 GLN n 
1 160 THR n 
1 161 THR n 
1 162 TYR n 
1 163 PRO n 
1 164 GLU n 
1 165 TYR n 
1 166 LEU n 
1 167 GLN n 
1 168 TYR n 
1 169 ILE n 
1 170 TYR n 
1 171 LEU n 
1 172 VAL n 
1 173 ALA n 
1 174 PRO n 
1 175 ILE n 
1 176 SER n 
1 177 LEU n 
1 178 MET n 
1 179 MET n 
1 180 LEU n 
1 181 ASN n 
1 182 PRO n 
1 183 ILE n 
1 184 GLY n 
1 185 PHE n 
1 186 ILE n 
1 187 PHE n 
1 188 CYS n 
1 189 GLU n 
1 190 ILE n 
1 191 GLN n 
1 192 LYS n 
1 193 TRP n 
1 194 LYS n 
1 195 ASP n 
1 196 THR n 
1 197 GLN n 
1 198 ASN n 
1 199 ALA n 
1 200 SER n 
1 201 GLN n 
1 202 ASN n 
1 203 LYS n 
1 204 ILE n 
1 205 LYS n 
1 206 ILE n 
1 207 VAL n 
1 208 GLY n 
1 209 LEU n 
1 210 GLY n 
1 211 LEU n 
1 212 LEU n 
1 213 ARG n 
1 214 VAL n 
1 215 LEU n 
1 216 GLN n 
1 217 ASN n 
1 218 PRO n 
1 219 ILE n 
1 220 VAL n 
1 221 PHE n 
1 222 MET n 
1 223 VAL n 
1 224 PHE n 
1 225 ILE n 
1 226 GLY n 
1 227 ILE n 
1 228 ALA n 
1 229 PHE n 
1 230 ASN n 
1 231 PHE n 
1 232 ILE n 
1 233 LEU n 
1 234 ASP n 
1 235 ARG n 
1 236 LYS n 
1 237 VAL n 
1 238 PRO n 
1 239 VAL n 
1 240 TYR n 
1 241 VAL n 
1 242 GLU n 
1 243 ASN n 
1 244 PHE n 
1 245 LEU n 
1 246 ASP n 
1 247 GLY n 
1 248 LEU n 
1 249 GLY n 
1 250 ASN n 
1 251 SER n 
1 252 PHE n 
1 253 SER n 
1 254 GLY n 
1 255 SER n 
1 256 ALA n 
1 257 LEU n 
1 258 PHE n 
1 259 TYR n 
1 260 LEU n 
1 261 GLY n 
1 262 LEU n 
1 263 THR n 
1 264 MET n 
1 265 VAL n 
1 266 GLY n 
1 267 LYS n 
1 268 ILE n 
1 269 LYS n 
1 270 ARG n 
1 271 LEU n 
1 272 LYS n 
1 273 LYS n 
1 274 SER n 
1 275 ALA n 
1 276 PHE n 
1 277 VAL n 
1 278 VAL n 
1 279 LEU n 
1 280 ILE n 
1 281 LEU n 
1 282 LEU n 
1 283 ILE n 
1 284 THR n 
1 285 ALA n 
1 286 LYS n 
1 287 LEU n 
1 288 LEU n 
1 289 VAL n 
1 290 LEU n 
1 291 PRO n 
1 292 LEU n 
1 293 LEU n 
1 294 CYS n 
1 295 ARG n 
1 296 GLU n 
1 297 MET n 
1 298 VAL n 
1 299 GLU n 
1 300 LEU n 
1 301 LEU n 
1 302 ASP n 
1 303 LYS n 
1 304 GLY n 
1 305 ASP n 
1 306 SER n 
1 307 VAL n 
1 308 VAL n 
1 309 ASN n 
1 310 HIS n 
1 311 THR n 
1 312 SER n 
1 313 LEU n 
1 314 SER n 
1 315 ASN n 
1 316 TYR n 
1 317 ALA n 
1 318 PHE n 
1 319 LEU n 
1 320 TYR n 
1 321 GLY n 
1 322 VAL n 
1 323 PHE n 
1 324 PRO n 
1 325 VAL n 
1 326 ALA n 
1 327 PRO n 
1 328 GLY n 
1 329 VAL n 
1 330 ALA n 
1 331 ILE n 
1 332 PHE n 
1 333 ALA n 
1 334 THR n 
1 335 GLN n 
1 336 PHE n 
1 337 ASN n 
1 338 MET n 
1 339 GLU n 
1 340 VAL n 
1 341 GLU n 
1 342 ILE n 
1 343 ILE n 
1 344 THR n 
1 345 SER n 
1 346 GLY n 
1 347 MET n 
1 348 VAL n 
1 349 ILE n 
1 350 SER n 
1 351 THR n 
1 352 PHE n 
1 353 VAL n 
1 354 SER n 
1 355 ALA n 
1 356 PRO n 
1 357 ILE n 
1 358 MET n 
1 359 TYR n 
1 360 VAL n 
1 361 SER n 
1 362 ALA n 
1 363 TRP n 
1 364 LEU n 
1 365 LEU n 
1 366 THR n 
1 367 PHE n 
1 368 PRO n 
1 369 THR n 
1 370 MET n 
1 371 ASP n 
1 372 PRO n 
1 373 LYS n 
1 374 PRO n 
1 375 LEU n 
1 376 ALA n 
1 377 TYR n 
1 378 ALA n 
1 379 ILE n 
1 380 GLN n 
1 381 ASN n 
1 382 VAL n 
1 383 SER n 
1 384 PHE n 
1 385 ASP n 
1 386 ILE n 
1 387 SER n 
1 388 ILE n 
1 389 VAL n 
1 390 SER n 
1 391 LEU n 
1 392 ILE n 
1 393 SER n 
1 394 LEU n 
1 395 ILE n 
1 396 TRP n 
1 397 SER n 
1 398 LEU n 
1 399 ALA n 
1 400 ILE n 
1 401 LEU n 
1 402 LEU n 
1 403 LEU n 
1 404 SER n 
1 405 LYS n 
1 406 LYS n 
1 407 TYR n 
1 408 LYS n 
1 409 GLN n 
1 410 LEU n 
1 411 PRO n 
1 412 HIS n 
1 413 MET n 
1 414 LEU n 
1 415 THR n 
1 416 THR n 
1 417 ASN n 
1 418 LEU n 
1 419 LEU n 
1 420 ILE n 
1 421 ALA n 
1 422 GLN n 
1 423 SER n 
1 424 ILE n 
1 425 VAL n 
1 426 CYS n 
1 427 ALA n 
1 428 GLY n 
1 429 MET n 
1 430 MET n 
1 431 ILE n 
1 432 TRP n 
1 433 ASN n 
1 434 PHE n 
1 435 VAL n 
1 436 LYS n 
1 437 GLU n 
1 438 LYS n 
1 439 ASN n 
1 440 PHE n 
1 441 VAL n 
1 442 GLY n 
1 443 GLN n 
1 444 ILE n 
1 445 LEU n 
1 446 VAL n 
1 447 PHE n 
1 448 VAL n 
1 449 LEU n 
1 450 LEU n 
1 451 TYR n 
1 452 SER n 
1 453 SER n 
1 454 LEU n 
1 455 TYR n 
1 456 SER n 
1 457 THR n 
1 458 TYR n 
1 459 LEU n 
1 460 TRP n 
1 461 THR n 
1 462 GLY n 
1 463 LEU n 
1 464 LEU n 
1 465 ALA n 
1 466 ILE n 
1 467 SER n 
1 468 LEU n 
1 469 PHE n 
1 470 LEU n 
1 471 LEU n 
1 472 LYS n 
1 473 LYS n 
1 474 ARG n 
1 475 GLU n 
1 476 ARG n 
1 477 VAL n 
1 478 GLN n 
1 479 ILE n 
1 480 PRO n 
1 481 VAL n 
1 482 GLY n 
1 483 ILE n 
1 484 ILE n 
1 485 ILE n 
1 486 ILE n 
1 487 SER n 
1 488 GLY n 
1 489 TRP n 
1 490 GLY n 
1 491 ILE n 
1 492 PRO n 
1 493 ALA n 
1 494 LEU n 
1 495 LEU n 
1 496 VAL n 
1 497 GLY n 
1 498 VAL n 
1 499 LEU n 
1 500 LEU n 
1 501 ILE n 
1 502 THR n 
1 503 GLY n 
1 504 LYS n 
1 505 HIS n 
1 506 ASN n 
1 507 GLY n 
1 508 ASP n 
1 509 SER n 
1 510 ILE n 
1 511 ASP n 
1 512 SER n 
1 513 ALA n 
1 514 PHE n 
1 515 PHE n 
1 516 TYR n 
1 517 GLY n 
1 518 LYS n 
1 519 GLU n 
1 520 GLN n 
1 521 MET n 
1 522 ILE n 
1 523 THR n 
1 524 THR n 
1 525 ALA n 
1 526 VAL n 
1 527 THR n 
1 528 LEU n 
1 529 PHE n 
1 530 CYS n 
1 531 SER n 
1 532 ILE n 
1 533 LEU n 
1 534 ILE n 
1 535 ALA n 
1 536 GLY n 
1 537 ILE n 
1 538 SER n 
1 539 LEU n 
1 540 MET n 
1 541 CYS n 
1 542 MET n 
1 543 ASN n 
1 544 GLN n 
1 545 THR n 
1 546 ALA n 
1 547 GLN n 
1 548 ALA n 
1 549 GLY n 
1 550 SER n 
1 551 TYR n 
1 552 GLU n 
1 553 GLY n 
1 554 PHE n 
1 555 ASP n 
1 556 GLN n 
1 557 SER n 
1 558 GLN n 
1 559 SER n 
1 560 HIS n 
1 561 LYS n 
1 562 VAL n 
1 563 VAL n 
1 564 GLU n 
1 565 PRO n 
1 566 GLY n 
1 567 ASN n 
1 568 THR n 
1 569 ALA n 
1 570 PHE n 
1 571 GLU n 
1 572 GLU n 
1 573 SER n 
1 574 PRO n 
1 575 ALA n 
1 576 PRO n 
1 577 VAL n 
1 578 ASN n 
1 579 GLU n 
1 580 PRO n 
1 581 GLU n 
1 582 LEU n 
1 583 PHE n 
1 584 THR n 
1 585 SER n 
1 586 SER n 
1 587 ILE n 
1 588 PRO n 
1 589 GLU n 
1 590 THR n 
1 591 SER n 
1 592 CYS n 
1 593 CYS n 
1 594 SER n 
1 595 CYS n 
1 596 SER n 
1 597 MET n 
1 598 GLY n 
1 599 ASN n 
1 600 GLY n 
1 601 GLU n 
1 602 LEU n 
1 603 HIS n 
1 604 CYS n 
1 605 PRO n 
1 606 SER n 
1 607 ILE n 
1 608 GLU n 
1 609 PRO n 
1 610 ILE n 
1 611 ALA n 
1 612 ASN n 
1 613 THR n 
1 614 SER n 
1 615 THR n 
1 616 SER n 
1 617 GLU n 
1 618 PRO n 
1 619 VAL n 
1 620 ILE n 
1 621 PRO n 
1 622 SER n 
1 623 PHE n 
1 624 GLU n 
1 625 LYS n 
1 626 ASN n 
1 627 ASN n 
1 628 HIS n 
1 629 CYS n 
1 630 VAL n 
1 631 SER n 
1 632 ARG n 
1 633 CYS n 
1 634 ASN n 
1 635 SER n 
1 636 GLN n 
1 637 SER n 
1 638 CYS n 
1 639 ILE n 
1 640 LEU n 
1 641 ALA n 
1 642 GLN n 
1 643 GLU n 
1 644 GLU n 
1 645 GLU n 
1 646 GLN n 
1 647 TYR n 
1 648 LEU n 
1 649 GLN n 
1 650 SER n 
1 651 GLY n 
1 652 ASP n 
1 653 GLN n 
1 654 GLN n 
1 655 LEU n 
1 656 THR n 
1 657 ARG n 
1 658 HIS n 
1 659 VAL n 
1 660 LEU n 
1 661 LEU n 
1 662 CYS n 
1 663 LEU n 
1 664 LEU n 
1 665 LEU n 
1 666 ILE n 
1 667 ILE n 
1 668 GLY n 
1 669 LEU n 
1 670 PHE n 
1 671 ALA n 
1 672 ASN n 
1 673 LEU n 
1 674 SER n 
1 675 SER n 
1 676 CYS n 
1 677 LEU n 
1 678 TRP n 
1 679 TRP n 
1 680 LEU n 
1 681 PHE n 
1 682 ASN n 
1 683 GLN n 
1 684 GLU n 
1 685 PRO n 
1 686 GLY n 
1 687 ARG n 
1 688 LEU n 
1 689 TYR n 
1 690 VAL n 
1 691 GLU n 
1 692 LEU n 
1 693 GLN n 
1 694 PHE n 
1 695 PHE n 
1 696 CYS n 
1 697 ALA n 
1 698 VAL n 
1 699 PHE n 
1 700 ASN n 
1 701 PHE n 
1 702 GLY n 
1 703 GLN n 
1 704 GLY n 
1 705 PHE n 
1 706 ILE n 
1 707 SER n 
1 708 PHE n 
1 709 GLY n 
1 710 ILE n 
1 711 PHE n 
1 712 GLY n 
1 713 LEU n 
1 714 ASP n 
1 715 LYS n 
1 716 HIS n 
1 717 LEU n 
1 718 ILE n 
1 719 ILE n 
1 720 LEU n 
1 721 PRO n 
1 722 PHE n 
1 723 LYS n 
1 724 ARG n 
1 725 ARG n 
1 726 LEU n 
1 727 GLU n 
1 728 PHE n 
1 729 LEU n 
1 730 TRP n 
1 731 ASN n 
1 732 ASN n 
1 733 LYS n 
1 734 ASP n 
1 735 THR n 
1 736 ALA n 
1 737 GLU n 
1 738 ASN n 
1 739 ARG n 
1 740 ASP n 
1 741 SER n 
1 742 PRO n 
1 743 VAL n 
1 744 SER n 
1 745 GLU n 
1 746 GLU n 
1 747 ILE n 
1 748 LYS n 
1 749 MET n 
1 750 THR n 
1 751 CYS n 
1 752 GLN n 
1 753 GLN n 
1 754 PHE n 
1 755 ILE n 
1 756 HIS n 
1 757 TYR n 
1 758 HIS n 
1 759 ARG n 
1 760 ASP n 
1 761 LEU n 
1 762 CYS n 
1 763 ILE n 
1 764 ARG n 
1 765 ASN n 
1 766 ILE n 
1 767 VAL n 
1 768 LYS n 
1 769 GLU n 
1 770 ARG n 
1 771 ARG n 
1 772 CYS n 
1 773 GLY n 
1 774 ALA n 
1 775 LYS n 
1 776 THR n 
1 777 SER n 
1 778 ALA n 
1 779 GLY n 
1 780 THR n 
1 781 PHE n 
1 782 CYS n 
1 783 GLY n 
1 784 CYS n 
1 785 ASP n 
1 786 LEU n 
1 787 VAL n 
1 788 SER n 
1 789 TRP n 
1 790 LEU n 
1 791 ILE n 
1 792 GLU n 
1 793 VAL n 
1 794 GLY n 
1 795 LEU n 
1 796 ALA n 
1 797 SER n 
1 798 ASP n 
1 799 ARG n 
1 800 GLY n 
1 801 GLU n 
1 802 ALA n 
1 803 VAL n 
1 804 ILE n 
1 805 TYR n 
1 806 GLY n 
1 807 ASP n 
1 808 ARG n 
1 809 LEU n 
1 810 VAL n 
1 811 GLN n 
1 812 GLY n 
1 813 GLY n 
1 814 VAL n 
1 815 ILE n 
1 816 GLN n 
1 817 HIS n 
1 818 ILE n 
1 819 THR n 
1 820 ASN n 
1 821 GLU n 
1 822 TYR n 
1 823 GLU n 
1 824 PHE n 
1 825 ARG n 
1 826 ASP n 
1 827 GLU n 
1 828 TYR n 
1 829 LEU n 
1 830 PHE n 
1 831 TYR n 
1 832 ARG n 
1 833 PHE n 
1 834 LEU n 
1 835 GLN n 
1 836 LYS n 
1 837 SER n 
1 838 PRO n 
1 839 GLU n 
1 840 GLN n 
1 841 SER n 
1 842 PRO n 
1 843 PRO n 
1 844 ALA n 
1 845 ILE n 
1 846 ASN n 
1 847 ALA n 
1 848 ASN n 
1 849 THR n 
1 850 LEU n 
1 851 GLN n 
1 852 GLN n 
1 853 GLU n 
1 854 ARG n 
1 855 TYR n 
1 856 LYS n 
1 857 GLU n 
1 858 ILE n 
1 859 GLU n 
1 860 HIS n 
1 861 SER n 
1 862 SER n 
1 863 PRO n 
1 864 PRO n 
1 865 SER n 
1 866 HIS n 
1 867 SER n 
1 868 PRO n 
1 869 LYS n 
1 870 THR 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   520 ?     ? GPR155 ? ? ? ? ? ? 'Nomascus leucogenys' 61853 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? HEK293 ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 521 591 human ? GPR155 ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? HEK293 ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 592 870 ?     ? GPR155 ? ? ? ? ? ? 'Nomascus leucogenys' 61853 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? HEK293 ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CLR non-polymer                  . CHOLESTEROL ? 'C27 H46 O'      386.654 
CYS 'L-peptide linking'          y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
IOS non-polymer                  . 3-SULFOOXY-1H-INDOLE ? 'C8 H7 N O4 S'   213.210 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
POV non-polymer                  . 
'(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate' POPC 'C42 H82 N O8 P' 760.076 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   B . n 
A 1 2   ASN 2   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ASN 4   4   ?   ?   ?   B . n 
A 1 5   LEU 5   5   ?   ?   ?   B . n 
A 1 6   PRO 6   6   ?   ?   ?   B . n 
A 1 7   ALA 7   7   ?   ?   ?   B . n 
A 1 8   GLU 8   8   ?   ?   ?   B . n 
A 1 9   ASN 9   9   ?   ?   ?   B . n 
A 1 10  LEU 10  10  ?   ?   ?   B . n 
A 1 11  THR 11  11  ?   ?   ?   B . n 
A 1 12  ILE 12  12  ?   ?   ?   B . n 
A 1 13  ALA 13  13  ?   ?   ?   B . n 
A 1 14  VAL 14  14  ?   ?   ?   B . n 
A 1 15  ASN 15  15  ?   ?   ?   B . n 
A 1 16  MET 16  16  ?   ?   ?   B . n 
A 1 17  THR 17  17  ?   ?   ?   B . n 
A 1 18  LYS 18  18  ?   ?   ?   B . n 
A 1 19  THR 19  19  ?   ?   ?   B . n 
A 1 20  LEU 20  20  ?   ?   ?   B . n 
A 1 21  PRO 21  21  ?   ?   ?   B . n 
A 1 22  THR 22  22  ?   ?   ?   B . n 
A 1 23  ALA 23  23  ?   ?   ?   B . n 
A 1 24  VAL 24  24  ?   ?   ?   B . n 
A 1 25  THR 25  25  ?   ?   ?   B . n 
A 1 26  HIS 26  26  ?   ?   ?   B . n 
A 1 27  GLY 27  27  ?   ?   ?   B . n 
A 1 28  PHE 28  28  ?   ?   ?   B . n 
A 1 29  ASN 29  29  ?   ?   ?   B . n 
A 1 30  SER 30  30  ?   ?   ?   B . n 
A 1 31  THR 31  31  ?   ?   ?   B . n 
A 1 32  ASN 32  32  ?   ?   ?   B . n 
A 1 33  ASP 33  33  ?   ?   ?   B . n 
A 1 34  PRO 34  34  ?   ?   ?   B . n 
A 1 35  PRO 35  35  ?   ?   ?   B . n 
A 1 36  SER 36  36  36  SER SER B . n 
A 1 37  MET 37  37  37  MET MET B . n 
A 1 38  SER 38  38  38  SER SER B . n 
A 1 39  ILE 39  39  39  ILE ILE B . n 
A 1 40  THR 40  40  40  THR THR B . n 
A 1 41  ARG 41  41  41  ARG ARG B . n 
A 1 42  LEU 42  42  42  LEU LEU B . n 
A 1 43  PHE 43  43  43  PHE PHE B . n 
A 1 44  PRO 44  44  44  PRO PRO B . n 
A 1 45  ALA 45  45  45  ALA ALA B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  LEU 47  47  47  LEU LEU B . n 
A 1 48  GLU 48  48  48  GLU GLU B . n 
A 1 49  CYS 49  49  49  CYS CYS B . n 
A 1 50  PHE 50  50  50  PHE PHE B . n 
A 1 51  GLY 51  51  51  GLY GLY B . n 
A 1 52  ILE 52  52  52  ILE ILE B . n 
A 1 53  VAL 53  53  53  VAL VAL B . n 
A 1 54  LEU 54  54  54  LEU LEU B . n 
A 1 55  CYS 55  55  55  CYS CYS B . n 
A 1 56  GLY 56  56  56  GLY GLY B . n 
A 1 57  TYR 57  57  57  TYR TYR B . n 
A 1 58  ILE 58  58  58  ILE ILE B . n 
A 1 59  ALA 59  59  59  ALA ALA B . n 
A 1 60  GLY 60  60  60  GLY GLY B . n 
A 1 61  ARG 61  61  61  ARG ARG B . n 
A 1 62  ALA 62  62  62  ALA ALA B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  VAL 64  64  64  VAL VAL B . n 
A 1 65  ILE 65  65  65  ILE ILE B . n 
A 1 66  THR 66  66  66  THR THR B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  THR 68  68  68  THR THR B . n 
A 1 69  GLN 69  69  69  GLN GLN B . n 
A 1 70  ALA 70  70  70  ALA ALA B . n 
A 1 71  LYS 71  71  71  LYS LYS B . n 
A 1 72  GLY 72  72  72  GLY GLY B . n 
A 1 73  LEU 73  73  73  LEU LEU B . n 
A 1 74  GLY 74  74  74  GLY GLY B . n 
A 1 75  ASN 75  75  75  ASN ASN B . n 
A 1 76  PHE 76  76  76  PHE PHE B . n 
A 1 77  VAL 77  77  77  VAL VAL B . n 
A 1 78  SER 78  78  78  SER SER B . n 
A 1 79  ARG 79  79  79  ARG ARG B . n 
A 1 80  PHE 80  80  80  PHE PHE B . n 
A 1 81  ALA 81  81  81  ALA ALA B . n 
A 1 82  LEU 82  82  82  LEU LEU B . n 
A 1 83  PRO 83  83  83  PRO PRO B . n 
A 1 84  ALA 84  84  84  ALA ALA B . n 
A 1 85  LEU 85  85  85  LEU LEU B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  PHE 87  87  87  PHE PHE B . n 
A 1 88  LYS 88  88  88  LYS LYS B . n 
A 1 89  ASN 89  89  89  ASN ASN B . n 
A 1 90  MET 90  90  90  MET MET B . n 
A 1 91  VAL 91  91  91  VAL VAL B . n 
A 1 92  VAL 92  92  92  VAL VAL B . n 
A 1 93  LEU 93  93  93  LEU LEU B . n 
A 1 94  ASN 94  94  94  ASN ASN B . n 
A 1 95  PHE 95  95  95  PHE PHE B . n 
A 1 96  SER 96  96  96  SER SER B . n 
A 1 97  ASN 97  97  97  ASN ASN B . n 
A 1 98  VAL 98  98  98  VAL VAL B . n 
A 1 99  ASP 99  99  99  ASP ASP B . n 
A 1 100 TRP 100 100 100 TRP TRP B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 PHE 102 102 102 PHE PHE B . n 
A 1 103 LEU 103 103 103 LEU LEU B . n 
A 1 104 TYR 104 104 104 TYR TYR B . n 
A 1 105 SER 105 105 105 SER SER B . n 
A 1 106 ILE 106 106 106 ILE ILE B . n 
A 1 107 LEU 107 107 107 LEU LEU B . n 
A 1 108 ILE 108 108 108 ILE ILE B . n 
A 1 109 ALA 109 109 109 ALA ALA B . n 
A 1 110 LYS 110 110 110 LYS LYS B . n 
A 1 111 ALA 111 111 111 ALA ALA B . n 
A 1 112 SER 112 112 112 SER SER B . n 
A 1 113 VAL 113 113 113 VAL VAL B . n 
A 1 114 PHE 114 114 114 PHE PHE B . n 
A 1 115 PHE 115 115 115 PHE PHE B . n 
A 1 116 ILE 116 116 116 ILE ILE B . n 
A 1 117 VAL 117 117 117 VAL VAL B . n 
A 1 118 CYS 118 118 118 CYS CYS B . n 
A 1 119 VAL 119 119 119 VAL VAL B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 THR 121 121 121 THR THR B . n 
A 1 122 LEU 122 122 122 LEU LEU B . n 
A 1 123 LEU 123 123 123 LEU LEU B . n 
A 1 124 VAL 124 124 124 VAL VAL B . n 
A 1 125 ALA 125 125 125 ALA ALA B . n 
A 1 126 SER 126 126 126 SER SER B . n 
A 1 127 PRO 127 127 127 PRO PRO B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 SER 129 129 129 SER SER B . n 
A 1 130 ARG 130 130 130 ARG ARG B . n 
A 1 131 PHE 131 131 131 PHE PHE B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 LYS 133 133 133 LYS LYS B . n 
A 1 134 ALA 134 134 134 ALA ALA B . n 
A 1 135 GLY 135 135 135 GLY GLY B . n 
A 1 136 LEU 136 136 136 LEU LEU B . n 
A 1 137 PHE 137 137 137 PHE PHE B . n 
A 1 138 PRO 138 138 138 PRO PRO B . n 
A 1 139 ILE 139 139 139 ILE ILE B . n 
A 1 140 PHE 140 140 140 PHE PHE B . n 
A 1 141 ALA 141 141 141 ALA ALA B . n 
A 1 142 THR 142 142 142 THR THR B . n 
A 1 143 GLN 143 143 143 GLN GLN B . n 
A 1 144 SER 144 144 144 SER SER B . n 
A 1 145 ASN 145 145 145 ASN ASN B . n 
A 1 146 ASP 146 146 146 ASP ASP B . n 
A 1 147 PHE 147 147 147 PHE PHE B . n 
A 1 148 ALA 148 148 148 ALA ALA B . n 
A 1 149 LEU 149 149 149 LEU LEU B . n 
A 1 150 GLY 150 150 150 GLY GLY B . n 
A 1 151 TYR 151 151 151 TYR TYR B . n 
A 1 152 PRO 152 152 152 PRO PRO B . n 
A 1 153 ILE 153 153 153 ILE ILE B . n 
A 1 154 VAL 154 154 154 VAL VAL B . n 
A 1 155 GLU 155 155 155 GLU GLU B . n 
A 1 156 ALA 156 156 156 ALA ALA B . n 
A 1 157 LEU 157 157 157 LEU LEU B . n 
A 1 158 TYR 158 158 158 TYR TYR B . n 
A 1 159 GLN 159 159 159 GLN GLN B . n 
A 1 160 THR 160 160 160 THR THR B . n 
A 1 161 THR 161 161 161 THR THR B . n 
A 1 162 TYR 162 162 162 TYR TYR B . n 
A 1 163 PRO 163 163 163 PRO PRO B . n 
A 1 164 GLU 164 164 164 GLU GLU B . n 
A 1 165 TYR 165 165 165 TYR TYR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 GLN 167 167 167 GLN GLN B . n 
A 1 168 TYR 168 168 168 TYR TYR B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 TYR 170 170 170 TYR TYR B . n 
A 1 171 LEU 171 171 171 LEU LEU B . n 
A 1 172 VAL 172 172 172 VAL VAL B . n 
A 1 173 ALA 173 173 173 ALA ALA B . n 
A 1 174 PRO 174 174 174 PRO PRO B . n 
A 1 175 ILE 175 175 175 ILE ILE B . n 
A 1 176 SER 176 176 176 SER SER B . n 
A 1 177 LEU 177 177 177 LEU LEU B . n 
A 1 178 MET 178 178 178 MET MET B . n 
A 1 179 MET 179 179 179 MET MET B . n 
A 1 180 LEU 180 180 180 LEU LEU B . n 
A 1 181 ASN 181 181 181 ASN ASN B . n 
A 1 182 PRO 182 182 182 PRO PRO B . n 
A 1 183 ILE 183 183 183 ILE ILE B . n 
A 1 184 GLY 184 184 184 GLY GLY B . n 
A 1 185 PHE 185 185 185 PHE PHE B . n 
A 1 186 ILE 186 186 186 ILE ILE B . n 
A 1 187 PHE 187 187 187 PHE PHE B . n 
A 1 188 CYS 188 188 188 CYS CYS B . n 
A 1 189 GLU 189 189 189 GLU GLU B . n 
A 1 190 ILE 190 190 190 ILE ILE B . n 
A 1 191 GLN 191 191 191 GLN GLN B . n 
A 1 192 LYS 192 192 192 LYS LYS B . n 
A 1 193 TRP 193 193 193 TRP TRP B . n 
A 1 194 LYS 194 194 194 LYS LYS B . n 
A 1 195 ASP 195 195 195 ASP ASP B . n 
A 1 196 THR 196 196 196 THR THR B . n 
A 1 197 GLN 197 197 197 GLN GLN B . n 
A 1 198 ASN 198 198 198 ASN ASN B . n 
A 1 199 ALA 199 199 199 ALA ALA B . n 
A 1 200 SER 200 200 200 SER SER B . n 
A 1 201 GLN 201 201 201 GLN GLN B . n 
A 1 202 ASN 202 202 202 ASN ASN B . n 
A 1 203 LYS 203 203 203 LYS LYS B . n 
A 1 204 ILE 204 204 204 ILE ILE B . n 
A 1 205 LYS 205 205 205 LYS LYS B . n 
A 1 206 ILE 206 206 206 ILE ILE B . n 
A 1 207 VAL 207 207 207 VAL VAL B . n 
A 1 208 GLY 208 208 208 GLY GLY B . n 
A 1 209 LEU 209 209 209 LEU LEU B . n 
A 1 210 GLY 210 210 210 GLY GLY B . n 
A 1 211 LEU 211 211 211 LEU LEU B . n 
A 1 212 LEU 212 212 212 LEU LEU B . n 
A 1 213 ARG 213 213 213 ARG ARG B . n 
A 1 214 VAL 214 214 214 VAL VAL B . n 
A 1 215 LEU 215 215 215 LEU LEU B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 ASN 217 217 217 ASN ASN B . n 
A 1 218 PRO 218 218 218 PRO PRO B . n 
A 1 219 ILE 219 219 219 ILE ILE B . n 
A 1 220 VAL 220 220 220 VAL VAL B . n 
A 1 221 PHE 221 221 221 PHE PHE B . n 
A 1 222 MET 222 222 222 MET MET B . n 
A 1 223 VAL 223 223 223 VAL VAL B . n 
A 1 224 PHE 224 224 224 PHE PHE B . n 
A 1 225 ILE 225 225 225 ILE ILE B . n 
A 1 226 GLY 226 226 226 GLY GLY B . n 
A 1 227 ILE 227 227 227 ILE ILE B . n 
A 1 228 ALA 228 228 228 ALA ALA B . n 
A 1 229 PHE 229 229 229 PHE PHE B . n 
A 1 230 ASN 230 230 230 ASN ASN B . n 
A 1 231 PHE 231 231 231 PHE PHE B . n 
A 1 232 ILE 232 232 232 ILE ILE B . n 
A 1 233 LEU 233 233 233 LEU LEU B . n 
A 1 234 ASP 234 234 234 ASP ASP B . n 
A 1 235 ARG 235 235 235 ARG ARG B . n 
A 1 236 LYS 236 236 236 LYS LYS B . n 
A 1 237 VAL 237 237 237 VAL VAL B . n 
A 1 238 PRO 238 238 238 PRO PRO B . n 
A 1 239 VAL 239 239 239 VAL VAL B . n 
A 1 240 TYR 240 240 240 TYR TYR B . n 
A 1 241 VAL 241 241 241 VAL VAL B . n 
A 1 242 GLU 242 242 242 GLU GLU B . n 
A 1 243 ASN 243 243 243 ASN ASN B . n 
A 1 244 PHE 244 244 244 PHE PHE B . n 
A 1 245 LEU 245 245 245 LEU LEU B . n 
A 1 246 ASP 246 246 246 ASP ASP B . n 
A 1 247 GLY 247 247 247 GLY GLY B . n 
A 1 248 LEU 248 248 248 LEU LEU B . n 
A 1 249 GLY 249 249 249 GLY GLY B . n 
A 1 250 ASN 250 250 250 ASN ASN B . n 
A 1 251 SER 251 251 251 SER SER B . n 
A 1 252 PHE 252 252 252 PHE PHE B . n 
A 1 253 SER 253 253 253 SER SER B . n 
A 1 254 GLY 254 254 254 GLY GLY B . n 
A 1 255 SER 255 255 255 SER SER B . n 
A 1 256 ALA 256 256 256 ALA ALA B . n 
A 1 257 LEU 257 257 257 LEU LEU B . n 
A 1 258 PHE 258 258 258 PHE PHE B . n 
A 1 259 TYR 259 259 259 TYR TYR B . n 
A 1 260 LEU 260 260 260 LEU LEU B . n 
A 1 261 GLY 261 261 261 GLY GLY B . n 
A 1 262 LEU 262 262 262 LEU LEU B . n 
A 1 263 THR 263 263 263 THR THR B . n 
A 1 264 MET 264 264 264 MET MET B . n 
A 1 265 VAL 265 265 265 VAL VAL B . n 
A 1 266 GLY 266 266 266 GLY GLY B . n 
A 1 267 LYS 267 267 267 LYS LYS B . n 
A 1 268 ILE 268 268 268 ILE ILE B . n 
A 1 269 LYS 269 269 269 LYS LYS B . n 
A 1 270 ARG 270 270 270 ARG ARG B . n 
A 1 271 LEU 271 271 271 LEU LEU B . n 
A 1 272 LYS 272 272 272 LYS LYS B . n 
A 1 273 LYS 273 273 273 LYS LYS B . n 
A 1 274 SER 274 274 274 SER SER B . n 
A 1 275 ALA 275 275 275 ALA ALA B . n 
A 1 276 PHE 276 276 276 PHE PHE B . n 
A 1 277 VAL 277 277 277 VAL VAL B . n 
A 1 278 VAL 278 278 278 VAL VAL B . n 
A 1 279 LEU 279 279 279 LEU LEU B . n 
A 1 280 ILE 280 280 280 ILE ILE B . n 
A 1 281 LEU 281 281 281 LEU LEU B . n 
A 1 282 LEU 282 282 282 LEU LEU B . n 
A 1 283 ILE 283 283 283 ILE ILE B . n 
A 1 284 THR 284 284 284 THR THR B . n 
A 1 285 ALA 285 285 285 ALA ALA B . n 
A 1 286 LYS 286 286 286 LYS LYS B . n 
A 1 287 LEU 287 287 287 LEU LEU B . n 
A 1 288 LEU 288 288 288 LEU LEU B . n 
A 1 289 VAL 289 289 289 VAL VAL B . n 
A 1 290 LEU 290 290 290 LEU LEU B . n 
A 1 291 PRO 291 291 291 PRO PRO B . n 
A 1 292 LEU 292 292 292 LEU LEU B . n 
A 1 293 LEU 293 293 293 LEU LEU B . n 
A 1 294 CYS 294 294 294 CYS CYS B . n 
A 1 295 ARG 295 295 295 ARG ARG B . n 
A 1 296 GLU 296 296 296 GLU GLU B . n 
A 1 297 MET 297 297 297 MET MET B . n 
A 1 298 VAL 298 298 298 VAL VAL B . n 
A 1 299 GLU 299 299 299 GLU GLU B . n 
A 1 300 LEU 300 300 300 LEU LEU B . n 
A 1 301 LEU 301 301 301 LEU LEU B . n 
A 1 302 ASP 302 302 302 ASP ASP B . n 
A 1 303 LYS 303 303 303 LYS LYS B . n 
A 1 304 GLY 304 304 304 GLY GLY B . n 
A 1 305 ASP 305 305 305 ASP ASP B . n 
A 1 306 SER 306 306 306 SER SER B . n 
A 1 307 VAL 307 307 307 VAL VAL B . n 
A 1 308 VAL 308 308 308 VAL VAL B . n 
A 1 309 ASN 309 309 309 ASN ASN B . n 
A 1 310 HIS 310 310 310 HIS HIS B . n 
A 1 311 THR 311 311 311 THR THR B . n 
A 1 312 SER 312 312 312 SER SER B . n 
A 1 313 LEU 313 313 313 LEU LEU B . n 
A 1 314 SER 314 314 314 SER SER B . n 
A 1 315 ASN 315 315 315 ASN ASN B . n 
A 1 316 TYR 316 316 316 TYR TYR B . n 
A 1 317 ALA 317 317 317 ALA ALA B . n 
A 1 318 PHE 318 318 318 PHE PHE B . n 
A 1 319 LEU 319 319 319 LEU LEU B . n 
A 1 320 TYR 320 320 320 TYR TYR B . n 
A 1 321 GLY 321 321 321 GLY GLY B . n 
A 1 322 VAL 322 322 322 VAL VAL B . n 
A 1 323 PHE 323 323 323 PHE PHE B . n 
A 1 324 PRO 324 324 324 PRO PRO B . n 
A 1 325 VAL 325 325 325 VAL VAL B . n 
A 1 326 ALA 326 326 326 ALA ALA B . n 
A 1 327 PRO 327 327 327 PRO PRO B . n 
A 1 328 GLY 328 328 328 GLY GLY B . n 
A 1 329 VAL 329 329 329 VAL VAL B . n 
A 1 330 ALA 330 330 330 ALA ALA B . n 
A 1 331 ILE 331 331 331 ILE ILE B . n 
A 1 332 PHE 332 332 332 PHE PHE B . n 
A 1 333 ALA 333 333 333 ALA ALA B . n 
A 1 334 THR 334 334 334 THR THR B . n 
A 1 335 GLN 335 335 335 GLN GLN B . n 
A 1 336 PHE 336 336 336 PHE PHE B . n 
A 1 337 ASN 337 337 337 ASN ASN B . n 
A 1 338 MET 338 338 338 MET MET B . n 
A 1 339 GLU 339 339 339 GLU GLU B . n 
A 1 340 VAL 340 340 340 VAL VAL B . n 
A 1 341 GLU 341 341 341 GLU GLU B . n 
A 1 342 ILE 342 342 342 ILE ILE B . n 
A 1 343 ILE 343 343 343 ILE ILE B . n 
A 1 344 THR 344 344 344 THR THR B . n 
A 1 345 SER 345 345 345 SER SER B . n 
A 1 346 GLY 346 346 346 GLY GLY B . n 
A 1 347 MET 347 347 347 MET MET B . n 
A 1 348 VAL 348 348 348 VAL VAL B . n 
A 1 349 ILE 349 349 349 ILE ILE B . n 
A 1 350 SER 350 350 350 SER SER B . n 
A 1 351 THR 351 351 351 THR THR B . n 
A 1 352 PHE 352 352 352 PHE PHE B . n 
A 1 353 VAL 353 353 353 VAL VAL B . n 
A 1 354 SER 354 354 354 SER SER B . n 
A 1 355 ALA 355 355 355 ALA ALA B . n 
A 1 356 PRO 356 356 356 PRO PRO B . n 
A 1 357 ILE 357 357 357 ILE ILE B . n 
A 1 358 MET 358 358 358 MET MET B . n 
A 1 359 TYR 359 359 359 TYR TYR B . n 
A 1 360 VAL 360 360 360 VAL VAL B . n 
A 1 361 SER 361 361 361 SER SER B . n 
A 1 362 ALA 362 362 362 ALA ALA B . n 
A 1 363 TRP 363 363 363 TRP TRP B . n 
A 1 364 LEU 364 364 364 LEU LEU B . n 
A 1 365 LEU 365 365 365 LEU LEU B . n 
A 1 366 THR 366 366 366 THR THR B . n 
A 1 367 PHE 367 367 367 PHE PHE B . n 
A 1 368 PRO 368 368 368 PRO PRO B . n 
A 1 369 THR 369 369 369 THR THR B . n 
A 1 370 MET 370 370 370 MET MET B . n 
A 1 371 ASP 371 371 371 ASP ASP B . n 
A 1 372 PRO 372 372 372 PRO PRO B . n 
A 1 373 LYS 373 373 373 LYS LYS B . n 
A 1 374 PRO 374 374 374 PRO PRO B . n 
A 1 375 LEU 375 375 375 LEU LEU B . n 
A 1 376 ALA 376 376 376 ALA ALA B . n 
A 1 377 TYR 377 377 377 TYR TYR B . n 
A 1 378 ALA 378 378 378 ALA ALA B . n 
A 1 379 ILE 379 379 379 ILE ILE B . n 
A 1 380 GLN 380 380 380 GLN GLN B . n 
A 1 381 ASN 381 381 381 ASN ASN B . n 
A 1 382 VAL 382 382 382 VAL VAL B . n 
A 1 383 SER 383 383 383 SER SER B . n 
A 1 384 PHE 384 384 384 PHE PHE B . n 
A 1 385 ASP 385 385 385 ASP ASP B . n 
A 1 386 ILE 386 386 386 ILE ILE B . n 
A 1 387 SER 387 387 387 SER SER B . n 
A 1 388 ILE 388 388 388 ILE ILE B . n 
A 1 389 VAL 389 389 389 VAL VAL B . n 
A 1 390 SER 390 390 390 SER SER B . n 
A 1 391 LEU 391 391 391 LEU LEU B . n 
A 1 392 ILE 392 392 392 ILE ILE B . n 
A 1 393 SER 393 393 393 SER SER B . n 
A 1 394 LEU 394 394 394 LEU LEU B . n 
A 1 395 ILE 395 395 395 ILE ILE B . n 
A 1 396 TRP 396 396 396 TRP TRP B . n 
A 1 397 SER 397 397 397 SER SER B . n 
A 1 398 LEU 398 398 398 LEU LEU B . n 
A 1 399 ALA 399 399 399 ALA ALA B . n 
A 1 400 ILE 400 400 400 ILE ILE B . n 
A 1 401 LEU 401 401 401 LEU LEU B . n 
A 1 402 LEU 402 402 402 LEU LEU B . n 
A 1 403 LEU 403 403 403 LEU LEU B . n 
A 1 404 SER 404 404 404 SER SER B . n 
A 1 405 LYS 405 405 405 LYS LYS B . n 
A 1 406 LYS 406 406 406 LYS LYS B . n 
A 1 407 TYR 407 407 407 TYR TYR B . n 
A 1 408 LYS 408 408 408 LYS LYS B . n 
A 1 409 GLN 409 409 409 GLN GLN B . n 
A 1 410 LEU 410 410 410 LEU LEU B . n 
A 1 411 PRO 411 411 411 PRO PRO B . n 
A 1 412 HIS 412 412 412 HIS HIS B . n 
A 1 413 MET 413 413 413 MET MET B . n 
A 1 414 LEU 414 414 414 LEU LEU B . n 
A 1 415 THR 415 415 415 THR THR B . n 
A 1 416 THR 416 416 416 THR THR B . n 
A 1 417 ASN 417 417 417 ASN ASN B . n 
A 1 418 LEU 418 418 418 LEU LEU B . n 
A 1 419 LEU 419 419 419 LEU LEU B . n 
A 1 420 ILE 420 420 420 ILE ILE B . n 
A 1 421 ALA 421 421 421 ALA ALA B . n 
A 1 422 GLN 422 422 422 GLN GLN B . n 
A 1 423 SER 423 423 423 SER SER B . n 
A 1 424 ILE 424 424 424 ILE ILE B . n 
A 1 425 VAL 425 425 425 VAL VAL B . n 
A 1 426 CYS 426 426 426 CYS CYS B . n 
A 1 427 ALA 427 427 427 ALA ALA B . n 
A 1 428 GLY 428 428 428 GLY GLY B . n 
A 1 429 MET 429 429 429 MET MET B . n 
A 1 430 MET 430 430 430 MET MET B . n 
A 1 431 ILE 431 431 431 ILE ILE B . n 
A 1 432 TRP 432 432 432 TRP TRP B . n 
A 1 433 ASN 433 433 433 ASN ASN B . n 
A 1 434 PHE 434 434 434 PHE PHE B . n 
A 1 435 VAL 435 435 435 VAL VAL B . n 
A 1 436 LYS 436 436 436 LYS LYS B . n 
A 1 437 GLU 437 437 437 GLU GLU B . n 
A 1 438 LYS 438 438 438 LYS LYS B . n 
A 1 439 ASN 439 439 439 ASN ASN B . n 
A 1 440 PHE 440 440 440 PHE PHE B . n 
A 1 441 VAL 441 441 441 VAL VAL B . n 
A 1 442 GLY 442 442 442 GLY GLY B . n 
A 1 443 GLN 443 443 443 GLN GLN B . n 
A 1 444 ILE 444 444 444 ILE ILE B . n 
A 1 445 LEU 445 445 445 LEU LEU B . n 
A 1 446 VAL 446 446 446 VAL VAL B . n 
A 1 447 PHE 447 447 447 PHE PHE B . n 
A 1 448 VAL 448 448 448 VAL VAL B . n 
A 1 449 LEU 449 449 449 LEU LEU B . n 
A 1 450 LEU 450 450 450 LEU LEU B . n 
A 1 451 TYR 451 451 451 TYR TYR B . n 
A 1 452 SER 452 452 452 SER SER B . n 
A 1 453 SER 453 453 453 SER SER B . n 
A 1 454 LEU 454 454 454 LEU LEU B . n 
A 1 455 TYR 455 455 455 TYR TYR B . n 
A 1 456 SER 456 456 456 SER SER B . n 
A 1 457 THR 457 457 457 THR THR B . n 
A 1 458 TYR 458 458 458 TYR TYR B . n 
A 1 459 LEU 459 459 459 LEU LEU B . n 
A 1 460 TRP 460 460 460 TRP TRP B . n 
A 1 461 THR 461 461 461 THR THR B . n 
A 1 462 GLY 462 462 462 GLY GLY B . n 
A 1 463 LEU 463 463 463 LEU LEU B . n 
A 1 464 LEU 464 464 464 LEU LEU B . n 
A 1 465 ALA 465 465 465 ALA ALA B . n 
A 1 466 ILE 466 466 466 ILE ILE B . n 
A 1 467 SER 467 467 467 SER SER B . n 
A 1 468 LEU 468 468 468 LEU LEU B . n 
A 1 469 PHE 469 469 469 PHE PHE B . n 
A 1 470 LEU 470 470 470 LEU LEU B . n 
A 1 471 LEU 471 471 471 LEU LEU B . n 
A 1 472 LYS 472 472 472 LYS LYS B . n 
A 1 473 LYS 473 473 473 LYS LYS B . n 
A 1 474 ARG 474 474 474 ARG ARG B . n 
A 1 475 GLU 475 475 475 GLU GLU B . n 
A 1 476 ARG 476 476 476 ARG ARG B . n 
A 1 477 VAL 477 477 477 VAL VAL B . n 
A 1 478 GLN 478 478 478 GLN GLN B . n 
A 1 479 ILE 479 479 479 ILE ILE B . n 
A 1 480 PRO 480 480 480 PRO PRO B . n 
A 1 481 VAL 481 481 481 VAL VAL B . n 
A 1 482 GLY 482 482 482 GLY GLY B . n 
A 1 483 ILE 483 483 483 ILE ILE B . n 
A 1 484 ILE 484 484 484 ILE ILE B . n 
A 1 485 ILE 485 485 485 ILE ILE B . n 
A 1 486 ILE 486 486 486 ILE ILE B . n 
A 1 487 SER 487 487 487 SER SER B . n 
A 1 488 GLY 488 488 488 GLY GLY B . n 
A 1 489 TRP 489 489 489 TRP TRP B . n 
A 1 490 GLY 490 490 490 GLY GLY B . n 
A 1 491 ILE 491 491 491 ILE ILE B . n 
A 1 492 PRO 492 492 492 PRO PRO B . n 
A 1 493 ALA 493 493 493 ALA ALA B . n 
A 1 494 LEU 494 494 494 LEU LEU B . n 
A 1 495 LEU 495 495 495 LEU LEU B . n 
A 1 496 VAL 496 496 496 VAL VAL B . n 
A 1 497 GLY 497 497 497 GLY GLY B . n 
A 1 498 VAL 498 498 498 VAL VAL B . n 
A 1 499 LEU 499 499 499 LEU LEU B . n 
A 1 500 LEU 500 500 500 LEU LEU B . n 
A 1 501 ILE 501 501 501 ILE ILE B . n 
A 1 502 THR 502 502 502 THR THR B . n 
A 1 503 GLY 503 503 503 GLY GLY B . n 
A 1 504 LYS 504 504 504 LYS LYS B . n 
A 1 505 HIS 505 505 505 HIS HIS B . n 
A 1 506 ASN 506 506 506 ASN ASN B . n 
A 1 507 GLY 507 507 507 GLY GLY B . n 
A 1 508 ASP 508 508 508 ASP ASP B . n 
A 1 509 SER 509 509 509 SER SER B . n 
A 1 510 ILE 510 510 510 ILE ILE B . n 
A 1 511 ASP 511 511 511 ASP ASP B . n 
A 1 512 SER 512 512 512 SER SER B . n 
A 1 513 ALA 513 513 513 ALA ALA B . n 
A 1 514 PHE 514 514 514 PHE PHE B . n 
A 1 515 PHE 515 515 515 PHE PHE B . n 
A 1 516 TYR 516 516 516 TYR TYR B . n 
A 1 517 GLY 517 517 517 GLY GLY B . n 
A 1 518 LYS 518 518 518 LYS LYS B . n 
A 1 519 GLU 519 519 519 GLU GLU B . n 
A 1 520 GLN 520 520 520 GLN GLN B . n 
A 1 521 MET 521 521 521 MET MET B . n 
A 1 522 ILE 522 522 522 ILE ILE B . n 
A 1 523 THR 523 523 523 THR THR B . n 
A 1 524 THR 524 524 524 THR THR B . n 
A 1 525 ALA 525 525 525 ALA ALA B . n 
A 1 526 VAL 526 526 526 VAL VAL B . n 
A 1 527 THR 527 527 527 THR THR B . n 
A 1 528 LEU 528 528 528 LEU LEU B . n 
A 1 529 PHE 529 529 529 PHE PHE B . n 
A 1 530 CYS 530 530 530 CYS CYS B . n 
A 1 531 SER 531 531 531 SER SER B . n 
A 1 532 ILE 532 532 532 ILE ILE B . n 
A 1 533 LEU 533 533 533 LEU LEU B . n 
A 1 534 ILE 534 534 534 ILE ILE B . n 
A 1 535 ALA 535 535 535 ALA ALA B . n 
A 1 536 GLY 536 536 536 GLY GLY B . n 
A 1 537 ILE 537 537 537 ILE ILE B . n 
A 1 538 SER 538 538 538 SER SER B . n 
A 1 539 LEU 539 539 539 LEU LEU B . n 
A 1 540 MET 540 540 540 MET MET B . n 
A 1 541 CYS 541 541 541 CYS CYS B . n 
A 1 542 MET 542 542 542 MET MET B . n 
A 1 543 ASN 543 543 543 ASN ASN B . n 
A 1 544 GLN 544 544 544 GLN GLN B . n 
A 1 545 THR 545 545 545 THR THR B . n 
A 1 546 ALA 546 546 ?   ?   ?   B . n 
A 1 547 GLN 547 547 ?   ?   ?   B . n 
A 1 548 ALA 548 548 ?   ?   ?   B . n 
A 1 549 GLY 549 549 ?   ?   ?   B . n 
A 1 550 SER 550 550 ?   ?   ?   B . n 
A 1 551 TYR 551 551 ?   ?   ?   B . n 
A 1 552 GLU 552 552 ?   ?   ?   B . n 
A 1 553 GLY 553 553 ?   ?   ?   B . n 
A 1 554 PHE 554 554 ?   ?   ?   B . n 
A 1 555 ASP 555 555 ?   ?   ?   B . n 
A 1 556 GLN 556 556 ?   ?   ?   B . n 
A 1 557 SER 557 557 ?   ?   ?   B . n 
A 1 558 GLN 558 558 ?   ?   ?   B . n 
A 1 559 SER 559 559 ?   ?   ?   B . n 
A 1 560 HIS 560 560 ?   ?   ?   B . n 
A 1 561 LYS 561 561 ?   ?   ?   B . n 
A 1 562 VAL 562 562 ?   ?   ?   B . n 
A 1 563 VAL 563 563 ?   ?   ?   B . n 
A 1 564 GLU 564 564 ?   ?   ?   B . n 
A 1 565 PRO 565 565 ?   ?   ?   B . n 
A 1 566 GLY 566 566 ?   ?   ?   B . n 
A 1 567 ASN 567 567 ?   ?   ?   B . n 
A 1 568 THR 568 568 ?   ?   ?   B . n 
A 1 569 ALA 569 569 ?   ?   ?   B . n 
A 1 570 PHE 570 570 ?   ?   ?   B . n 
A 1 571 GLU 571 571 ?   ?   ?   B . n 
A 1 572 GLU 572 572 ?   ?   ?   B . n 
A 1 573 SER 573 573 ?   ?   ?   B . n 
A 1 574 PRO 574 574 ?   ?   ?   B . n 
A 1 575 ALA 575 575 ?   ?   ?   B . n 
A 1 576 PRO 576 576 ?   ?   ?   B . n 
A 1 577 VAL 577 577 ?   ?   ?   B . n 
A 1 578 ASN 578 578 ?   ?   ?   B . n 
A 1 579 GLU 579 579 ?   ?   ?   B . n 
A 1 580 PRO 580 580 ?   ?   ?   B . n 
A 1 581 GLU 581 581 ?   ?   ?   B . n 
A 1 582 LEU 582 582 ?   ?   ?   B . n 
A 1 583 PHE 583 583 ?   ?   ?   B . n 
A 1 584 THR 584 584 ?   ?   ?   B . n 
A 1 585 SER 585 585 ?   ?   ?   B . n 
A 1 586 SER 586 586 ?   ?   ?   B . n 
A 1 587 ILE 587 587 ?   ?   ?   B . n 
A 1 588 PRO 588 588 ?   ?   ?   B . n 
A 1 589 GLU 589 589 ?   ?   ?   B . n 
A 1 590 THR 590 590 ?   ?   ?   B . n 
A 1 591 SER 591 591 ?   ?   ?   B . n 
A 1 592 CYS 592 592 ?   ?   ?   B . n 
A 1 593 CYS 593 593 ?   ?   ?   B . n 
A 1 594 SER 594 594 ?   ?   ?   B . n 
A 1 595 CYS 595 595 ?   ?   ?   B . n 
A 1 596 SER 596 596 ?   ?   ?   B . n 
A 1 597 MET 597 597 ?   ?   ?   B . n 
A 1 598 GLY 598 598 ?   ?   ?   B . n 
A 1 599 ASN 599 599 ?   ?   ?   B . n 
A 1 600 GLY 600 600 ?   ?   ?   B . n 
A 1 601 GLU 601 601 ?   ?   ?   B . n 
A 1 602 LEU 602 602 ?   ?   ?   B . n 
A 1 603 HIS 603 603 ?   ?   ?   B . n 
A 1 604 CYS 604 604 ?   ?   ?   B . n 
A 1 605 PRO 605 605 ?   ?   ?   B . n 
A 1 606 SER 606 606 ?   ?   ?   B . n 
A 1 607 ILE 607 607 ?   ?   ?   B . n 
A 1 608 GLU 608 608 ?   ?   ?   B . n 
A 1 609 PRO 609 609 ?   ?   ?   B . n 
A 1 610 ILE 610 610 ?   ?   ?   B . n 
A 1 611 ALA 611 611 ?   ?   ?   B . n 
A 1 612 ASN 612 612 ?   ?   ?   B . n 
A 1 613 THR 613 613 ?   ?   ?   B . n 
A 1 614 SER 614 614 ?   ?   ?   B . n 
A 1 615 THR 615 615 ?   ?   ?   B . n 
A 1 616 SER 616 616 ?   ?   ?   B . n 
A 1 617 GLU 617 617 ?   ?   ?   B . n 
A 1 618 PRO 618 618 ?   ?   ?   B . n 
A 1 619 VAL 619 619 ?   ?   ?   B . n 
A 1 620 ILE 620 620 ?   ?   ?   B . n 
A 1 621 PRO 621 621 ?   ?   ?   B . n 
A 1 622 SER 622 622 ?   ?   ?   B . n 
A 1 623 PHE 623 623 ?   ?   ?   B . n 
A 1 624 GLU 624 624 ?   ?   ?   B . n 
A 1 625 LYS 625 625 ?   ?   ?   B . n 
A 1 626 ASN 626 626 ?   ?   ?   B . n 
A 1 627 ASN 627 627 ?   ?   ?   B . n 
A 1 628 HIS 628 628 ?   ?   ?   B . n 
A 1 629 CYS 629 629 ?   ?   ?   B . n 
A 1 630 VAL 630 630 ?   ?   ?   B . n 
A 1 631 SER 631 631 ?   ?   ?   B . n 
A 1 632 ARG 632 632 ?   ?   ?   B . n 
A 1 633 CYS 633 633 ?   ?   ?   B . n 
A 1 634 ASN 634 634 ?   ?   ?   B . n 
A 1 635 SER 635 635 ?   ?   ?   B . n 
A 1 636 GLN 636 636 ?   ?   ?   B . n 
A 1 637 SER 637 637 ?   ?   ?   B . n 
A 1 638 CYS 638 638 ?   ?   ?   B . n 
A 1 639 ILE 639 639 ?   ?   ?   B . n 
A 1 640 LEU 640 640 ?   ?   ?   B . n 
A 1 641 ALA 641 641 ?   ?   ?   B . n 
A 1 642 GLN 642 642 ?   ?   ?   B . n 
A 1 643 GLU 643 643 ?   ?   ?   B . n 
A 1 644 GLU 644 644 ?   ?   ?   B . n 
A 1 645 GLU 645 645 ?   ?   ?   B . n 
A 1 646 GLN 646 646 ?   ?   ?   B . n 
A 1 647 TYR 647 647 ?   ?   ?   B . n 
A 1 648 LEU 648 648 ?   ?   ?   B . n 
A 1 649 GLN 649 649 ?   ?   ?   B . n 
A 1 650 SER 650 650 ?   ?   ?   B . n 
A 1 651 GLY 651 651 ?   ?   ?   B . n 
A 1 652 ASP 652 652 ?   ?   ?   B . n 
A 1 653 GLN 653 653 ?   ?   ?   B . n 
A 1 654 GLN 654 654 654 GLN GLN B . n 
A 1 655 LEU 655 655 655 LEU LEU B . n 
A 1 656 THR 656 656 656 THR THR B . n 
A 1 657 ARG 657 657 657 ARG ARG B . n 
A 1 658 HIS 658 658 658 HIS HIS B . n 
A 1 659 VAL 659 659 659 VAL VAL B . n 
A 1 660 LEU 660 660 660 LEU LEU B . n 
A 1 661 LEU 661 661 661 LEU LEU B . n 
A 1 662 CYS 662 662 662 CYS CYS B . n 
A 1 663 LEU 663 663 663 LEU LEU B . n 
A 1 664 LEU 664 664 664 LEU LEU B . n 
A 1 665 LEU 665 665 665 LEU LEU B . n 
A 1 666 ILE 666 666 666 ILE ILE B . n 
A 1 667 ILE 667 667 667 ILE ILE B . n 
A 1 668 GLY 668 668 668 GLY GLY B . n 
A 1 669 LEU 669 669 669 LEU LEU B . n 
A 1 670 PHE 670 670 670 PHE PHE B . n 
A 1 671 ALA 671 671 671 ALA ALA B . n 
A 1 672 ASN 672 672 672 ASN ASN B . n 
A 1 673 LEU 673 673 673 LEU LEU B . n 
A 1 674 SER 674 674 674 SER SER B . n 
A 1 675 SER 675 675 675 SER SER B . n 
A 1 676 CYS 676 676 676 CYS CYS B . n 
A 1 677 LEU 677 677 677 LEU LEU B . n 
A 1 678 TRP 678 678 678 TRP TRP B . n 
A 1 679 TRP 679 679 679 TRP TRP B . n 
A 1 680 LEU 680 680 680 LEU LEU B . n 
A 1 681 PHE 681 681 681 PHE PHE B . n 
A 1 682 ASN 682 682 682 ASN ASN B . n 
A 1 683 GLN 683 683 683 GLN GLN B . n 
A 1 684 GLU 684 684 684 GLU GLU B . n 
A 1 685 PRO 685 685 685 PRO PRO B . n 
A 1 686 GLY 686 686 686 GLY GLY B . n 
A 1 687 ARG 687 687 687 ARG ARG B . n 
A 1 688 LEU 688 688 688 LEU LEU B . n 
A 1 689 TYR 689 689 689 TYR TYR B . n 
A 1 690 VAL 690 690 690 VAL VAL B . n 
A 1 691 GLU 691 691 691 GLU GLU B . n 
A 1 692 LEU 692 692 692 LEU LEU B . n 
A 1 693 GLN 693 693 693 GLN GLN B . n 
A 1 694 PHE 694 694 694 PHE PHE B . n 
A 1 695 PHE 695 695 695 PHE PHE B . n 
A 1 696 CYS 696 696 696 CYS CYS B . n 
A 1 697 ALA 697 697 697 ALA ALA B . n 
A 1 698 VAL 698 698 698 VAL VAL B . n 
A 1 699 PHE 699 699 699 PHE PHE B . n 
A 1 700 ASN 700 700 700 ASN ASN B . n 
A 1 701 PHE 701 701 701 PHE PHE B . n 
A 1 702 GLY 702 702 702 GLY GLY B . n 
A 1 703 GLN 703 703 703 GLN GLN B . n 
A 1 704 GLY 704 704 704 GLY GLY B . n 
A 1 705 PHE 705 705 705 PHE PHE B . n 
A 1 706 ILE 706 706 706 ILE ILE B . n 
A 1 707 SER 707 707 707 SER SER B . n 
A 1 708 PHE 708 708 708 PHE PHE B . n 
A 1 709 GLY 709 709 709 GLY GLY B . n 
A 1 710 ILE 710 710 710 ILE ILE B . n 
A 1 711 PHE 711 711 711 PHE PHE B . n 
A 1 712 GLY 712 712 712 GLY GLY B . n 
A 1 713 LEU 713 713 713 LEU LEU B . n 
A 1 714 ASP 714 714 714 ASP ASP B . n 
A 1 715 LYS 715 715 715 LYS LYS B . n 
A 1 716 HIS 716 716 716 HIS HIS B . n 
A 1 717 LEU 717 717 717 LEU LEU B . n 
A 1 718 ILE 718 718 718 ILE ILE B . n 
A 1 719 ILE 719 719 ?   ?   ?   B . n 
A 1 720 LEU 720 720 ?   ?   ?   B . n 
A 1 721 PRO 721 721 ?   ?   ?   B . n 
A 1 722 PHE 722 722 ?   ?   ?   B . n 
A 1 723 LYS 723 723 ?   ?   ?   B . n 
A 1 724 ARG 724 724 ?   ?   ?   B . n 
A 1 725 ARG 725 725 ?   ?   ?   B . n 
A 1 726 LEU 726 726 ?   ?   ?   B . n 
A 1 727 GLU 727 727 ?   ?   ?   B . n 
A 1 728 PHE 728 728 ?   ?   ?   B . n 
A 1 729 LEU 729 729 ?   ?   ?   B . n 
A 1 730 TRP 730 730 ?   ?   ?   B . n 
A 1 731 ASN 731 731 ?   ?   ?   B . n 
A 1 732 ASN 732 732 ?   ?   ?   B . n 
A 1 733 LYS 733 733 ?   ?   ?   B . n 
A 1 734 ASP 734 734 ?   ?   ?   B . n 
A 1 735 THR 735 735 ?   ?   ?   B . n 
A 1 736 ALA 736 736 ?   ?   ?   B . n 
A 1 737 GLU 737 737 ?   ?   ?   B . n 
A 1 738 ASN 738 738 ?   ?   ?   B . n 
A 1 739 ARG 739 739 ?   ?   ?   B . n 
A 1 740 ASP 740 740 ?   ?   ?   B . n 
A 1 741 SER 741 741 ?   ?   ?   B . n 
A 1 742 PRO 742 742 ?   ?   ?   B . n 
A 1 743 VAL 743 743 ?   ?   ?   B . n 
A 1 744 SER 744 744 ?   ?   ?   B . n 
A 1 745 GLU 745 745 ?   ?   ?   B . n 
A 1 746 GLU 746 746 ?   ?   ?   B . n 
A 1 747 ILE 747 747 ?   ?   ?   B . n 
A 1 748 LYS 748 748 ?   ?   ?   B . n 
A 1 749 MET 749 749 ?   ?   ?   B . n 
A 1 750 THR 750 750 ?   ?   ?   B . n 
A 1 751 CYS 751 751 ?   ?   ?   B . n 
A 1 752 GLN 752 752 ?   ?   ?   B . n 
A 1 753 GLN 753 753 ?   ?   ?   B . n 
A 1 754 PHE 754 754 ?   ?   ?   B . n 
A 1 755 ILE 755 755 ?   ?   ?   B . n 
A 1 756 HIS 756 756 ?   ?   ?   B . n 
A 1 757 TYR 757 757 ?   ?   ?   B . n 
A 1 758 HIS 758 758 ?   ?   ?   B . n 
A 1 759 ARG 759 759 ?   ?   ?   B . n 
A 1 760 ASP 760 760 ?   ?   ?   B . n 
A 1 761 LEU 761 761 ?   ?   ?   B . n 
A 1 762 CYS 762 762 ?   ?   ?   B . n 
A 1 763 ILE 763 763 ?   ?   ?   B . n 
A 1 764 ARG 764 764 ?   ?   ?   B . n 
A 1 765 ASN 765 765 ?   ?   ?   B . n 
A 1 766 ILE 766 766 ?   ?   ?   B . n 
A 1 767 VAL 767 767 ?   ?   ?   B . n 
A 1 768 LYS 768 768 ?   ?   ?   B . n 
A 1 769 GLU 769 769 ?   ?   ?   B . n 
A 1 770 ARG 770 770 ?   ?   ?   B . n 
A 1 771 ARG 771 771 ?   ?   ?   B . n 
A 1 772 CYS 772 772 ?   ?   ?   B . n 
A 1 773 GLY 773 773 ?   ?   ?   B . n 
A 1 774 ALA 774 774 ?   ?   ?   B . n 
A 1 775 LYS 775 775 ?   ?   ?   B . n 
A 1 776 THR 776 776 ?   ?   ?   B . n 
A 1 777 SER 777 777 ?   ?   ?   B . n 
A 1 778 ALA 778 778 ?   ?   ?   B . n 
A 1 779 GLY 779 779 ?   ?   ?   B . n 
A 1 780 THR 780 780 ?   ?   ?   B . n 
A 1 781 PHE 781 781 ?   ?   ?   B . n 
A 1 782 CYS 782 782 ?   ?   ?   B . n 
A 1 783 GLY 783 783 ?   ?   ?   B . n 
A 1 784 CYS 784 784 ?   ?   ?   B . n 
A 1 785 ASP 785 785 ?   ?   ?   B . n 
A 1 786 LEU 786 786 ?   ?   ?   B . n 
A 1 787 VAL 787 787 ?   ?   ?   B . n 
A 1 788 SER 788 788 ?   ?   ?   B . n 
A 1 789 TRP 789 789 ?   ?   ?   B . n 
A 1 790 LEU 790 790 ?   ?   ?   B . n 
A 1 791 ILE 791 791 ?   ?   ?   B . n 
A 1 792 GLU 792 792 ?   ?   ?   B . n 
A 1 793 VAL 793 793 ?   ?   ?   B . n 
A 1 794 GLY 794 794 ?   ?   ?   B . n 
A 1 795 LEU 795 795 ?   ?   ?   B . n 
A 1 796 ALA 796 796 ?   ?   ?   B . n 
A 1 797 SER 797 797 ?   ?   ?   B . n 
A 1 798 ASP 798 798 ?   ?   ?   B . n 
A 1 799 ARG 799 799 ?   ?   ?   B . n 
A 1 800 GLY 800 800 ?   ?   ?   B . n 
A 1 801 GLU 801 801 ?   ?   ?   B . n 
A 1 802 ALA 802 802 ?   ?   ?   B . n 
A 1 803 VAL 803 803 ?   ?   ?   B . n 
A 1 804 ILE 804 804 ?   ?   ?   B . n 
A 1 805 TYR 805 805 ?   ?   ?   B . n 
A 1 806 GLY 806 806 ?   ?   ?   B . n 
A 1 807 ASP 807 807 ?   ?   ?   B . n 
A 1 808 ARG 808 808 ?   ?   ?   B . n 
A 1 809 LEU 809 809 ?   ?   ?   B . n 
A 1 810 VAL 810 810 ?   ?   ?   B . n 
A 1 811 GLN 811 811 ?   ?   ?   B . n 
A 1 812 GLY 812 812 ?   ?   ?   B . n 
A 1 813 GLY 813 813 ?   ?   ?   B . n 
A 1 814 VAL 814 814 ?   ?   ?   B . n 
A 1 815 ILE 815 815 ?   ?   ?   B . n 
A 1 816 GLN 816 816 ?   ?   ?   B . n 
A 1 817 HIS 817 817 ?   ?   ?   B . n 
A 1 818 ILE 818 818 ?   ?   ?   B . n 
A 1 819 THR 819 819 ?   ?   ?   B . n 
A 1 820 ASN 820 820 ?   ?   ?   B . n 
A 1 821 GLU 821 821 ?   ?   ?   B . n 
A 1 822 TYR 822 822 ?   ?   ?   B . n 
A 1 823 GLU 823 823 ?   ?   ?   B . n 
A 1 824 PHE 824 824 ?   ?   ?   B . n 
A 1 825 ARG 825 825 ?   ?   ?   B . n 
A 1 826 ASP 826 826 ?   ?   ?   B . n 
A 1 827 GLU 827 827 ?   ?   ?   B . n 
A 1 828 TYR 828 828 ?   ?   ?   B . n 
A 1 829 LEU 829 829 ?   ?   ?   B . n 
A 1 830 PHE 830 830 ?   ?   ?   B . n 
A 1 831 TYR 831 831 ?   ?   ?   B . n 
A 1 832 ARG 832 832 ?   ?   ?   B . n 
A 1 833 PHE 833 833 ?   ?   ?   B . n 
A 1 834 LEU 834 834 ?   ?   ?   B . n 
A 1 835 GLN 835 835 ?   ?   ?   B . n 
A 1 836 LYS 836 836 ?   ?   ?   B . n 
A 1 837 SER 837 837 ?   ?   ?   B . n 
A 1 838 PRO 838 838 ?   ?   ?   B . n 
A 1 839 GLU 839 839 ?   ?   ?   B . n 
A 1 840 GLN 840 840 ?   ?   ?   B . n 
A 1 841 SER 841 841 ?   ?   ?   B . n 
A 1 842 PRO 842 842 ?   ?   ?   B . n 
A 1 843 PRO 843 843 ?   ?   ?   B . n 
A 1 844 ALA 844 844 ?   ?   ?   B . n 
A 1 845 ILE 845 845 ?   ?   ?   B . n 
A 1 846 ASN 846 846 ?   ?   ?   B . n 
A 1 847 ALA 847 847 ?   ?   ?   B . n 
A 1 848 ASN 848 848 ?   ?   ?   B . n 
A 1 849 THR 849 849 ?   ?   ?   B . n 
A 1 850 LEU 850 850 ?   ?   ?   B . n 
A 1 851 GLN 851 851 ?   ?   ?   B . n 
A 1 852 GLN 852 852 ?   ?   ?   B . n 
A 1 853 GLU 853 853 ?   ?   ?   B . n 
A 1 854 ARG 854 854 ?   ?   ?   B . n 
A 1 855 TYR 855 855 ?   ?   ?   B . n 
A 1 856 LYS 856 856 ?   ?   ?   B . n 
A 1 857 GLU 857 857 ?   ?   ?   B . n 
A 1 858 ILE 858 858 ?   ?   ?   B . n 
A 1 859 GLU 859 859 ?   ?   ?   B . n 
A 1 860 HIS 860 860 ?   ?   ?   B . n 
A 1 861 SER 861 861 ?   ?   ?   B . n 
A 1 862 SER 862 862 ?   ?   ?   B . n 
A 1 863 PRO 863 863 ?   ?   ?   B . n 
A 1 864 PRO 864 864 ?   ?   ?   B . n 
A 1 865 SER 865 865 ?   ?   ?   B . n 
A 1 866 HIS 866 866 ?   ?   ?   B . n 
A 1 867 SER 867 867 ?   ?   ?   B . n 
A 1 868 PRO 868 868 ?   ?   ?   B . n 
A 1 869 LYS 869 869 ?   ?   ?   B . n 
A 1 870 THR 870 870 ?   ?   ?   B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   ASN 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ASN 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   ?   ?   ?   A . n 
B 1 6   PRO 6   6   ?   ?   ?   A . n 
B 1 7   ALA 7   7   ?   ?   ?   A . n 
B 1 8   GLU 8   8   ?   ?   ?   A . n 
B 1 9   ASN 9   9   ?   ?   ?   A . n 
B 1 10  LEU 10  10  ?   ?   ?   A . n 
B 1 11  THR 11  11  ?   ?   ?   A . n 
B 1 12  ILE 12  12  ?   ?   ?   A . n 
B 1 13  ALA 13  13  ?   ?   ?   A . n 
B 1 14  VAL 14  14  ?   ?   ?   A . n 
B 1 15  ASN 15  15  ?   ?   ?   A . n 
B 1 16  MET 16  16  ?   ?   ?   A . n 
B 1 17  THR 17  17  ?   ?   ?   A . n 
B 1 18  LYS 18  18  ?   ?   ?   A . n 
B 1 19  THR 19  19  ?   ?   ?   A . n 
B 1 20  LEU 20  20  ?   ?   ?   A . n 
B 1 21  PRO 21  21  ?   ?   ?   A . n 
B 1 22  THR 22  22  ?   ?   ?   A . n 
B 1 23  ALA 23  23  ?   ?   ?   A . n 
B 1 24  VAL 24  24  ?   ?   ?   A . n 
B 1 25  THR 25  25  ?   ?   ?   A . n 
B 1 26  HIS 26  26  ?   ?   ?   A . n 
B 1 27  GLY 27  27  ?   ?   ?   A . n 
B 1 28  PHE 28  28  ?   ?   ?   A . n 
B 1 29  ASN 29  29  ?   ?   ?   A . n 
B 1 30  SER 30  30  ?   ?   ?   A . n 
B 1 31  THR 31  31  ?   ?   ?   A . n 
B 1 32  ASN 32  32  ?   ?   ?   A . n 
B 1 33  ASP 33  33  ?   ?   ?   A . n 
B 1 34  PRO 34  34  ?   ?   ?   A . n 
B 1 35  PRO 35  35  ?   ?   ?   A . n 
B 1 36  SER 36  36  36  SER SER A . n 
B 1 37  MET 37  37  37  MET MET A . n 
B 1 38  SER 38  38  38  SER SER A . n 
B 1 39  ILE 39  39  39  ILE ILE A . n 
B 1 40  THR 40  40  40  THR THR A . n 
B 1 41  ARG 41  41  41  ARG ARG A . n 
B 1 42  LEU 42  42  42  LEU LEU A . n 
B 1 43  PHE 43  43  43  PHE PHE A . n 
B 1 44  PRO 44  44  44  PRO PRO A . n 
B 1 45  ALA 45  45  45  ALA ALA A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  LEU 47  47  47  LEU LEU A . n 
B 1 48  GLU 48  48  48  GLU GLU A . n 
B 1 49  CYS 49  49  49  CYS CYS A . n 
B 1 50  PHE 50  50  50  PHE PHE A . n 
B 1 51  GLY 51  51  51  GLY GLY A . n 
B 1 52  ILE 52  52  52  ILE ILE A . n 
B 1 53  VAL 53  53  53  VAL VAL A . n 
B 1 54  LEU 54  54  54  LEU LEU A . n 
B 1 55  CYS 55  55  55  CYS CYS A . n 
B 1 56  GLY 56  56  56  GLY GLY A . n 
B 1 57  TYR 57  57  57  TYR TYR A . n 
B 1 58  ILE 58  58  58  ILE ILE A . n 
B 1 59  ALA 59  59  59  ALA ALA A . n 
B 1 60  GLY 60  60  60  GLY GLY A . n 
B 1 61  ARG 61  61  61  ARG ARG A . n 
B 1 62  ALA 62  62  62  ALA ALA A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  VAL 64  64  64  VAL VAL A . n 
B 1 65  ILE 65  65  65  ILE ILE A . n 
B 1 66  THR 66  66  66  THR THR A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  THR 68  68  68  THR THR A . n 
B 1 69  GLN 69  69  69  GLN GLN A . n 
B 1 70  ALA 70  70  70  ALA ALA A . n 
B 1 71  LYS 71  71  71  LYS LYS A . n 
B 1 72  GLY 72  72  72  GLY GLY A . n 
B 1 73  LEU 73  73  73  LEU LEU A . n 
B 1 74  GLY 74  74  74  GLY GLY A . n 
B 1 75  ASN 75  75  75  ASN ASN A . n 
B 1 76  PHE 76  76  76  PHE PHE A . n 
B 1 77  VAL 77  77  77  VAL VAL A . n 
B 1 78  SER 78  78  78  SER SER A . n 
B 1 79  ARG 79  79  79  ARG ARG A . n 
B 1 80  PHE 80  80  80  PHE PHE A . n 
B 1 81  ALA 81  81  81  ALA ALA A . n 
B 1 82  LEU 82  82  82  LEU LEU A . n 
B 1 83  PRO 83  83  83  PRO PRO A . n 
B 1 84  ALA 84  84  84  ALA ALA A . n 
B 1 85  LEU 85  85  85  LEU LEU A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  PHE 87  87  87  PHE PHE A . n 
B 1 88  LYS 88  88  88  LYS LYS A . n 
B 1 89  ASN 89  89  89  ASN ASN A . n 
B 1 90  MET 90  90  90  MET MET A . n 
B 1 91  VAL 91  91  91  VAL VAL A . n 
B 1 92  VAL 92  92  92  VAL VAL A . n 
B 1 93  LEU 93  93  93  LEU LEU A . n 
B 1 94  ASN 94  94  94  ASN ASN A . n 
B 1 95  PHE 95  95  95  PHE PHE A . n 
B 1 96  SER 96  96  96  SER SER A . n 
B 1 97  ASN 97  97  97  ASN ASN A . n 
B 1 98  VAL 98  98  98  VAL VAL A . n 
B 1 99  ASP 99  99  99  ASP ASP A . n 
B 1 100 TRP 100 100 100 TRP TRP A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 PHE 102 102 102 PHE PHE A . n 
B 1 103 LEU 103 103 103 LEU LEU A . n 
B 1 104 TYR 104 104 104 TYR TYR A . n 
B 1 105 SER 105 105 105 SER SER A . n 
B 1 106 ILE 106 106 106 ILE ILE A . n 
B 1 107 LEU 107 107 107 LEU LEU A . n 
B 1 108 ILE 108 108 108 ILE ILE A . n 
B 1 109 ALA 109 109 109 ALA ALA A . n 
B 1 110 LYS 110 110 110 LYS LYS A . n 
B 1 111 ALA 111 111 111 ALA ALA A . n 
B 1 112 SER 112 112 112 SER SER A . n 
B 1 113 VAL 113 113 113 VAL VAL A . n 
B 1 114 PHE 114 114 114 PHE PHE A . n 
B 1 115 PHE 115 115 115 PHE PHE A . n 
B 1 116 ILE 116 116 116 ILE ILE A . n 
B 1 117 VAL 117 117 117 VAL VAL A . n 
B 1 118 CYS 118 118 118 CYS CYS A . n 
B 1 119 VAL 119 119 119 VAL VAL A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 THR 121 121 121 THR THR A . n 
B 1 122 LEU 122 122 122 LEU LEU A . n 
B 1 123 LEU 123 123 123 LEU LEU A . n 
B 1 124 VAL 124 124 124 VAL VAL A . n 
B 1 125 ALA 125 125 125 ALA ALA A . n 
B 1 126 SER 126 126 126 SER SER A . n 
B 1 127 PRO 127 127 127 PRO PRO A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 SER 129 129 129 SER SER A . n 
B 1 130 ARG 130 130 130 ARG ARG A . n 
B 1 131 PHE 131 131 131 PHE PHE A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 LYS 133 133 133 LYS LYS A . n 
B 1 134 ALA 134 134 134 ALA ALA A . n 
B 1 135 GLY 135 135 135 GLY GLY A . n 
B 1 136 LEU 136 136 136 LEU LEU A . n 
B 1 137 PHE 137 137 137 PHE PHE A . n 
B 1 138 PRO 138 138 138 PRO PRO A . n 
B 1 139 ILE 139 139 139 ILE ILE A . n 
B 1 140 PHE 140 140 140 PHE PHE A . n 
B 1 141 ALA 141 141 141 ALA ALA A . n 
B 1 142 THR 142 142 142 THR THR A . n 
B 1 143 GLN 143 143 143 GLN GLN A . n 
B 1 144 SER 144 144 144 SER SER A . n 
B 1 145 ASN 145 145 145 ASN ASN A . n 
B 1 146 ASP 146 146 146 ASP ASP A . n 
B 1 147 PHE 147 147 147 PHE PHE A . n 
B 1 148 ALA 148 148 148 ALA ALA A . n 
B 1 149 LEU 149 149 149 LEU LEU A . n 
B 1 150 GLY 150 150 150 GLY GLY A . n 
B 1 151 TYR 151 151 151 TYR TYR A . n 
B 1 152 PRO 152 152 152 PRO PRO A . n 
B 1 153 ILE 153 153 153 ILE ILE A . n 
B 1 154 VAL 154 154 154 VAL VAL A . n 
B 1 155 GLU 155 155 155 GLU GLU A . n 
B 1 156 ALA 156 156 156 ALA ALA A . n 
B 1 157 LEU 157 157 157 LEU LEU A . n 
B 1 158 TYR 158 158 158 TYR TYR A . n 
B 1 159 GLN 159 159 159 GLN GLN A . n 
B 1 160 THR 160 160 160 THR THR A . n 
B 1 161 THR 161 161 161 THR THR A . n 
B 1 162 TYR 162 162 162 TYR TYR A . n 
B 1 163 PRO 163 163 163 PRO PRO A . n 
B 1 164 GLU 164 164 164 GLU GLU A . n 
B 1 165 TYR 165 165 165 TYR TYR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 GLN 167 167 167 GLN GLN A . n 
B 1 168 TYR 168 168 168 TYR TYR A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 TYR 170 170 170 TYR TYR A . n 
B 1 171 LEU 171 171 171 LEU LEU A . n 
B 1 172 VAL 172 172 172 VAL VAL A . n 
B 1 173 ALA 173 173 173 ALA ALA A . n 
B 1 174 PRO 174 174 174 PRO PRO A . n 
B 1 175 ILE 175 175 175 ILE ILE A . n 
B 1 176 SER 176 176 176 SER SER A . n 
B 1 177 LEU 177 177 177 LEU LEU A . n 
B 1 178 MET 178 178 178 MET MET A . n 
B 1 179 MET 179 179 179 MET MET A . n 
B 1 180 LEU 180 180 180 LEU LEU A . n 
B 1 181 ASN 181 181 181 ASN ASN A . n 
B 1 182 PRO 182 182 182 PRO PRO A . n 
B 1 183 ILE 183 183 183 ILE ILE A . n 
B 1 184 GLY 184 184 184 GLY GLY A . n 
B 1 185 PHE 185 185 185 PHE PHE A . n 
B 1 186 ILE 186 186 186 ILE ILE A . n 
B 1 187 PHE 187 187 187 PHE PHE A . n 
B 1 188 CYS 188 188 188 CYS CYS A . n 
B 1 189 GLU 189 189 189 GLU GLU A . n 
B 1 190 ILE 190 190 190 ILE ILE A . n 
B 1 191 GLN 191 191 191 GLN GLN A . n 
B 1 192 LYS 192 192 192 LYS LYS A . n 
B 1 193 TRP 193 193 193 TRP TRP A . n 
B 1 194 LYS 194 194 194 LYS LYS A . n 
B 1 195 ASP 195 195 195 ASP ASP A . n 
B 1 196 THR 196 196 196 THR THR A . n 
B 1 197 GLN 197 197 197 GLN GLN A . n 
B 1 198 ASN 198 198 198 ASN ASN A . n 
B 1 199 ALA 199 199 199 ALA ALA A . n 
B 1 200 SER 200 200 200 SER SER A . n 
B 1 201 GLN 201 201 201 GLN GLN A . n 
B 1 202 ASN 202 202 202 ASN ASN A . n 
B 1 203 LYS 203 203 203 LYS LYS A . n 
B 1 204 ILE 204 204 204 ILE ILE A . n 
B 1 205 LYS 205 205 205 LYS LYS A . n 
B 1 206 ILE 206 206 206 ILE ILE A . n 
B 1 207 VAL 207 207 207 VAL VAL A . n 
B 1 208 GLY 208 208 208 GLY GLY A . n 
B 1 209 LEU 209 209 209 LEU LEU A . n 
B 1 210 GLY 210 210 210 GLY GLY A . n 
B 1 211 LEU 211 211 211 LEU LEU A . n 
B 1 212 LEU 212 212 212 LEU LEU A . n 
B 1 213 ARG 213 213 213 ARG ARG A . n 
B 1 214 VAL 214 214 214 VAL VAL A . n 
B 1 215 LEU 215 215 215 LEU LEU A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 ASN 217 217 217 ASN ASN A . n 
B 1 218 PRO 218 218 218 PRO PRO A . n 
B 1 219 ILE 219 219 219 ILE ILE A . n 
B 1 220 VAL 220 220 220 VAL VAL A . n 
B 1 221 PHE 221 221 221 PHE PHE A . n 
B 1 222 MET 222 222 222 MET MET A . n 
B 1 223 VAL 223 223 223 VAL VAL A . n 
B 1 224 PHE 224 224 224 PHE PHE A . n 
B 1 225 ILE 225 225 225 ILE ILE A . n 
B 1 226 GLY 226 226 226 GLY GLY A . n 
B 1 227 ILE 227 227 227 ILE ILE A . n 
B 1 228 ALA 228 228 228 ALA ALA A . n 
B 1 229 PHE 229 229 229 PHE PHE A . n 
B 1 230 ASN 230 230 230 ASN ASN A . n 
B 1 231 PHE 231 231 231 PHE PHE A . n 
B 1 232 ILE 232 232 232 ILE ILE A . n 
B 1 233 LEU 233 233 233 LEU LEU A . n 
B 1 234 ASP 234 234 234 ASP ASP A . n 
B 1 235 ARG 235 235 235 ARG ARG A . n 
B 1 236 LYS 236 236 236 LYS LYS A . n 
B 1 237 VAL 237 237 237 VAL VAL A . n 
B 1 238 PRO 238 238 238 PRO PRO A . n 
B 1 239 VAL 239 239 239 VAL VAL A . n 
B 1 240 TYR 240 240 240 TYR TYR A . n 
B 1 241 VAL 241 241 241 VAL VAL A . n 
B 1 242 GLU 242 242 242 GLU GLU A . n 
B 1 243 ASN 243 243 243 ASN ASN A . n 
B 1 244 PHE 244 244 244 PHE PHE A . n 
B 1 245 LEU 245 245 245 LEU LEU A . n 
B 1 246 ASP 246 246 246 ASP ASP A . n 
B 1 247 GLY 247 247 247 GLY GLY A . n 
B 1 248 LEU 248 248 248 LEU LEU A . n 
B 1 249 GLY 249 249 249 GLY GLY A . n 
B 1 250 ASN 250 250 250 ASN ASN A . n 
B 1 251 SER 251 251 251 SER SER A . n 
B 1 252 PHE 252 252 252 PHE PHE A . n 
B 1 253 SER 253 253 253 SER SER A . n 
B 1 254 GLY 254 254 254 GLY GLY A . n 
B 1 255 SER 255 255 255 SER SER A . n 
B 1 256 ALA 256 256 256 ALA ALA A . n 
B 1 257 LEU 257 257 257 LEU LEU A . n 
B 1 258 PHE 258 258 258 PHE PHE A . n 
B 1 259 TYR 259 259 259 TYR TYR A . n 
B 1 260 LEU 260 260 260 LEU LEU A . n 
B 1 261 GLY 261 261 261 GLY GLY A . n 
B 1 262 LEU 262 262 262 LEU LEU A . n 
B 1 263 THR 263 263 263 THR THR A . n 
B 1 264 MET 264 264 264 MET MET A . n 
B 1 265 VAL 265 265 265 VAL VAL A . n 
B 1 266 GLY 266 266 266 GLY GLY A . n 
B 1 267 LYS 267 267 267 LYS LYS A . n 
B 1 268 ILE 268 268 268 ILE ILE A . n 
B 1 269 LYS 269 269 269 LYS LYS A . n 
B 1 270 ARG 270 270 270 ARG ARG A . n 
B 1 271 LEU 271 271 271 LEU LEU A . n 
B 1 272 LYS 272 272 272 LYS LYS A . n 
B 1 273 LYS 273 273 273 LYS LYS A . n 
B 1 274 SER 274 274 274 SER SER A . n 
B 1 275 ALA 275 275 275 ALA ALA A . n 
B 1 276 PHE 276 276 276 PHE PHE A . n 
B 1 277 VAL 277 277 277 VAL VAL A . n 
B 1 278 VAL 278 278 278 VAL VAL A . n 
B 1 279 LEU 279 279 279 LEU LEU A . n 
B 1 280 ILE 280 280 280 ILE ILE A . n 
B 1 281 LEU 281 281 281 LEU LEU A . n 
B 1 282 LEU 282 282 282 LEU LEU A . n 
B 1 283 ILE 283 283 283 ILE ILE A . n 
B 1 284 THR 284 284 284 THR THR A . n 
B 1 285 ALA 285 285 285 ALA ALA A . n 
B 1 286 LYS 286 286 286 LYS LYS A . n 
B 1 287 LEU 287 287 287 LEU LEU A . n 
B 1 288 LEU 288 288 288 LEU LEU A . n 
B 1 289 VAL 289 289 289 VAL VAL A . n 
B 1 290 LEU 290 290 290 LEU LEU A . n 
B 1 291 PRO 291 291 291 PRO PRO A . n 
B 1 292 LEU 292 292 292 LEU LEU A . n 
B 1 293 LEU 293 293 293 LEU LEU A . n 
B 1 294 CYS 294 294 294 CYS CYS A . n 
B 1 295 ARG 295 295 295 ARG ARG A . n 
B 1 296 GLU 296 296 296 GLU GLU A . n 
B 1 297 MET 297 297 297 MET MET A . n 
B 1 298 VAL 298 298 298 VAL VAL A . n 
B 1 299 GLU 299 299 299 GLU GLU A . n 
B 1 300 LEU 300 300 300 LEU LEU A . n 
B 1 301 LEU 301 301 301 LEU LEU A . n 
B 1 302 ASP 302 302 302 ASP ASP A . n 
B 1 303 LYS 303 303 303 LYS LYS A . n 
B 1 304 GLY 304 304 304 GLY GLY A . n 
B 1 305 ASP 305 305 305 ASP ASP A . n 
B 1 306 SER 306 306 306 SER SER A . n 
B 1 307 VAL 307 307 307 VAL VAL A . n 
B 1 308 VAL 308 308 308 VAL VAL A . n 
B 1 309 ASN 309 309 309 ASN ASN A . n 
B 1 310 HIS 310 310 310 HIS HIS A . n 
B 1 311 THR 311 311 311 THR THR A . n 
B 1 312 SER 312 312 312 SER SER A . n 
B 1 313 LEU 313 313 313 LEU LEU A . n 
B 1 314 SER 314 314 314 SER SER A . n 
B 1 315 ASN 315 315 315 ASN ASN A . n 
B 1 316 TYR 316 316 316 TYR TYR A . n 
B 1 317 ALA 317 317 317 ALA ALA A . n 
B 1 318 PHE 318 318 318 PHE PHE A . n 
B 1 319 LEU 319 319 319 LEU LEU A . n 
B 1 320 TYR 320 320 320 TYR TYR A . n 
B 1 321 GLY 321 321 321 GLY GLY A . n 
B 1 322 VAL 322 322 322 VAL VAL A . n 
B 1 323 PHE 323 323 323 PHE PHE A . n 
B 1 324 PRO 324 324 324 PRO PRO A . n 
B 1 325 VAL 325 325 325 VAL VAL A . n 
B 1 326 ALA 326 326 326 ALA ALA A . n 
B 1 327 PRO 327 327 327 PRO PRO A . n 
B 1 328 GLY 328 328 328 GLY GLY A . n 
B 1 329 VAL 329 329 329 VAL VAL A . n 
B 1 330 ALA 330 330 330 ALA ALA A . n 
B 1 331 ILE 331 331 331 ILE ILE A . n 
B 1 332 PHE 332 332 332 PHE PHE A . n 
B 1 333 ALA 333 333 333 ALA ALA A . n 
B 1 334 THR 334 334 334 THR THR A . n 
B 1 335 GLN 335 335 335 GLN GLN A . n 
B 1 336 PHE 336 336 336 PHE PHE A . n 
B 1 337 ASN 337 337 337 ASN ASN A . n 
B 1 338 MET 338 338 338 MET MET A . n 
B 1 339 GLU 339 339 339 GLU GLU A . n 
B 1 340 VAL 340 340 340 VAL VAL A . n 
B 1 341 GLU 341 341 341 GLU GLU A . n 
B 1 342 ILE 342 342 342 ILE ILE A . n 
B 1 343 ILE 343 343 343 ILE ILE A . n 
B 1 344 THR 344 344 344 THR THR A . n 
B 1 345 SER 345 345 345 SER SER A . n 
B 1 346 GLY 346 346 346 GLY GLY A . n 
B 1 347 MET 347 347 347 MET MET A . n 
B 1 348 VAL 348 348 348 VAL VAL A . n 
B 1 349 ILE 349 349 349 ILE ILE A . n 
B 1 350 SER 350 350 350 SER SER A . n 
B 1 351 THR 351 351 351 THR THR A . n 
B 1 352 PHE 352 352 352 PHE PHE A . n 
B 1 353 VAL 353 353 353 VAL VAL A . n 
B 1 354 SER 354 354 354 SER SER A . n 
B 1 355 ALA 355 355 355 ALA ALA A . n 
B 1 356 PRO 356 356 356 PRO PRO A . n 
B 1 357 ILE 357 357 357 ILE ILE A . n 
B 1 358 MET 358 358 358 MET MET A . n 
B 1 359 TYR 359 359 359 TYR TYR A . n 
B 1 360 VAL 360 360 360 VAL VAL A . n 
B 1 361 SER 361 361 361 SER SER A . n 
B 1 362 ALA 362 362 362 ALA ALA A . n 
B 1 363 TRP 363 363 363 TRP TRP A . n 
B 1 364 LEU 364 364 364 LEU LEU A . n 
B 1 365 LEU 365 365 365 LEU LEU A . n 
B 1 366 THR 366 366 366 THR THR A . n 
B 1 367 PHE 367 367 367 PHE PHE A . n 
B 1 368 PRO 368 368 368 PRO PRO A . n 
B 1 369 THR 369 369 369 THR THR A . n 
B 1 370 MET 370 370 370 MET MET A . n 
B 1 371 ASP 371 371 371 ASP ASP A . n 
B 1 372 PRO 372 372 372 PRO PRO A . n 
B 1 373 LYS 373 373 373 LYS LYS A . n 
B 1 374 PRO 374 374 374 PRO PRO A . n 
B 1 375 LEU 375 375 375 LEU LEU A . n 
B 1 376 ALA 376 376 376 ALA ALA A . n 
B 1 377 TYR 377 377 377 TYR TYR A . n 
B 1 378 ALA 378 378 378 ALA ALA A . n 
B 1 379 ILE 379 379 379 ILE ILE A . n 
B 1 380 GLN 380 380 380 GLN GLN A . n 
B 1 381 ASN 381 381 381 ASN ASN A . n 
B 1 382 VAL 382 382 382 VAL VAL A . n 
B 1 383 SER 383 383 383 SER SER A . n 
B 1 384 PHE 384 384 384 PHE PHE A . n 
B 1 385 ASP 385 385 385 ASP ASP A . n 
B 1 386 ILE 386 386 386 ILE ILE A . n 
B 1 387 SER 387 387 387 SER SER A . n 
B 1 388 ILE 388 388 388 ILE ILE A . n 
B 1 389 VAL 389 389 389 VAL VAL A . n 
B 1 390 SER 390 390 390 SER SER A . n 
B 1 391 LEU 391 391 391 LEU LEU A . n 
B 1 392 ILE 392 392 392 ILE ILE A . n 
B 1 393 SER 393 393 393 SER SER A . n 
B 1 394 LEU 394 394 394 LEU LEU A . n 
B 1 395 ILE 395 395 395 ILE ILE A . n 
B 1 396 TRP 396 396 396 TRP TRP A . n 
B 1 397 SER 397 397 397 SER SER A . n 
B 1 398 LEU 398 398 398 LEU LEU A . n 
B 1 399 ALA 399 399 399 ALA ALA A . n 
B 1 400 ILE 400 400 400 ILE ILE A . n 
B 1 401 LEU 401 401 401 LEU LEU A . n 
B 1 402 LEU 402 402 402 LEU LEU A . n 
B 1 403 LEU 403 403 403 LEU LEU A . n 
B 1 404 SER 404 404 404 SER SER A . n 
B 1 405 LYS 405 405 405 LYS LYS A . n 
B 1 406 LYS 406 406 406 LYS LYS A . n 
B 1 407 TYR 407 407 407 TYR TYR A . n 
B 1 408 LYS 408 408 408 LYS LYS A . n 
B 1 409 GLN 409 409 409 GLN GLN A . n 
B 1 410 LEU 410 410 410 LEU LEU A . n 
B 1 411 PRO 411 411 411 PRO PRO A . n 
B 1 412 HIS 412 412 412 HIS HIS A . n 
B 1 413 MET 413 413 413 MET MET A . n 
B 1 414 LEU 414 414 414 LEU LEU A . n 
B 1 415 THR 415 415 415 THR THR A . n 
B 1 416 THR 416 416 416 THR THR A . n 
B 1 417 ASN 417 417 417 ASN ASN A . n 
B 1 418 LEU 418 418 418 LEU LEU A . n 
B 1 419 LEU 419 419 419 LEU LEU A . n 
B 1 420 ILE 420 420 420 ILE ILE A . n 
B 1 421 ALA 421 421 421 ALA ALA A . n 
B 1 422 GLN 422 422 422 GLN GLN A . n 
B 1 423 SER 423 423 423 SER SER A . n 
B 1 424 ILE 424 424 424 ILE ILE A . n 
B 1 425 VAL 425 425 425 VAL VAL A . n 
B 1 426 CYS 426 426 426 CYS CYS A . n 
B 1 427 ALA 427 427 427 ALA ALA A . n 
B 1 428 GLY 428 428 428 GLY GLY A . n 
B 1 429 MET 429 429 429 MET MET A . n 
B 1 430 MET 430 430 430 MET MET A . n 
B 1 431 ILE 431 431 431 ILE ILE A . n 
B 1 432 TRP 432 432 432 TRP TRP A . n 
B 1 433 ASN 433 433 433 ASN ASN A . n 
B 1 434 PHE 434 434 434 PHE PHE A . n 
B 1 435 VAL 435 435 435 VAL VAL A . n 
B 1 436 LYS 436 436 436 LYS LYS A . n 
B 1 437 GLU 437 437 437 GLU GLU A . n 
B 1 438 LYS 438 438 438 LYS LYS A . n 
B 1 439 ASN 439 439 439 ASN ASN A . n 
B 1 440 PHE 440 440 440 PHE PHE A . n 
B 1 441 VAL 441 441 441 VAL VAL A . n 
B 1 442 GLY 442 442 442 GLY GLY A . n 
B 1 443 GLN 443 443 443 GLN GLN A . n 
B 1 444 ILE 444 444 444 ILE ILE A . n 
B 1 445 LEU 445 445 445 LEU LEU A . n 
B 1 446 VAL 446 446 446 VAL VAL A . n 
B 1 447 PHE 447 447 447 PHE PHE A . n 
B 1 448 VAL 448 448 448 VAL VAL A . n 
B 1 449 LEU 449 449 449 LEU LEU A . n 
B 1 450 LEU 450 450 450 LEU LEU A . n 
B 1 451 TYR 451 451 451 TYR TYR A . n 
B 1 452 SER 452 452 452 SER SER A . n 
B 1 453 SER 453 453 453 SER SER A . n 
B 1 454 LEU 454 454 454 LEU LEU A . n 
B 1 455 TYR 455 455 455 TYR TYR A . n 
B 1 456 SER 456 456 456 SER SER A . n 
B 1 457 THR 457 457 457 THR THR A . n 
B 1 458 TYR 458 458 458 TYR TYR A . n 
B 1 459 LEU 459 459 459 LEU LEU A . n 
B 1 460 TRP 460 460 460 TRP TRP A . n 
B 1 461 THR 461 461 461 THR THR A . n 
B 1 462 GLY 462 462 462 GLY GLY A . n 
B 1 463 LEU 463 463 463 LEU LEU A . n 
B 1 464 LEU 464 464 464 LEU LEU A . n 
B 1 465 ALA 465 465 465 ALA ALA A . n 
B 1 466 ILE 466 466 466 ILE ILE A . n 
B 1 467 SER 467 467 467 SER SER A . n 
B 1 468 LEU 468 468 468 LEU LEU A . n 
B 1 469 PHE 469 469 469 PHE PHE A . n 
B 1 470 LEU 470 470 470 LEU LEU A . n 
B 1 471 LEU 471 471 471 LEU LEU A . n 
B 1 472 LYS 472 472 472 LYS LYS A . n 
B 1 473 LYS 473 473 473 LYS LYS A . n 
B 1 474 ARG 474 474 474 ARG ARG A . n 
B 1 475 GLU 475 475 475 GLU GLU A . n 
B 1 476 ARG 476 476 476 ARG ARG A . n 
B 1 477 VAL 477 477 477 VAL VAL A . n 
B 1 478 GLN 478 478 478 GLN GLN A . n 
B 1 479 ILE 479 479 479 ILE ILE A . n 
B 1 480 PRO 480 480 480 PRO PRO A . n 
B 1 481 VAL 481 481 481 VAL VAL A . n 
B 1 482 GLY 482 482 482 GLY GLY A . n 
B 1 483 ILE 483 483 483 ILE ILE A . n 
B 1 484 ILE 484 484 484 ILE ILE A . n 
B 1 485 ILE 485 485 485 ILE ILE A . n 
B 1 486 ILE 486 486 486 ILE ILE A . n 
B 1 487 SER 487 487 487 SER SER A . n 
B 1 488 GLY 488 488 488 GLY GLY A . n 
B 1 489 TRP 489 489 489 TRP TRP A . n 
B 1 490 GLY 490 490 490 GLY GLY A . n 
B 1 491 ILE 491 491 491 ILE ILE A . n 
B 1 492 PRO 492 492 492 PRO PRO A . n 
B 1 493 ALA 493 493 493 ALA ALA A . n 
B 1 494 LEU 494 494 494 LEU LEU A . n 
B 1 495 LEU 495 495 495 LEU LEU A . n 
B 1 496 VAL 496 496 496 VAL VAL A . n 
B 1 497 GLY 497 497 497 GLY GLY A . n 
B 1 498 VAL 498 498 498 VAL VAL A . n 
B 1 499 LEU 499 499 499 LEU LEU A . n 
B 1 500 LEU 500 500 500 LEU LEU A . n 
B 1 501 ILE 501 501 501 ILE ILE A . n 
B 1 502 THR 502 502 502 THR THR A . n 
B 1 503 GLY 503 503 503 GLY GLY A . n 
B 1 504 LYS 504 504 504 LYS LYS A . n 
B 1 505 HIS 505 505 505 HIS HIS A . n 
B 1 506 ASN 506 506 506 ASN ASN A . n 
B 1 507 GLY 507 507 507 GLY GLY A . n 
B 1 508 ASP 508 508 508 ASP ASP A . n 
B 1 509 SER 509 509 509 SER SER A . n 
B 1 510 ILE 510 510 510 ILE ILE A . n 
B 1 511 ASP 511 511 511 ASP ASP A . n 
B 1 512 SER 512 512 512 SER SER A . n 
B 1 513 ALA 513 513 513 ALA ALA A . n 
B 1 514 PHE 514 514 514 PHE PHE A . n 
B 1 515 PHE 515 515 515 PHE PHE A . n 
B 1 516 TYR 516 516 516 TYR TYR A . n 
B 1 517 GLY 517 517 517 GLY GLY A . n 
B 1 518 LYS 518 518 518 LYS LYS A . n 
B 1 519 GLU 519 519 519 GLU GLU A . n 
B 1 520 GLN 520 520 520 GLN GLN A . n 
B 1 521 MET 521 521 521 MET MET A . n 
B 1 522 ILE 522 522 522 ILE ILE A . n 
B 1 523 THR 523 523 523 THR THR A . n 
B 1 524 THR 524 524 524 THR THR A . n 
B 1 525 ALA 525 525 525 ALA ALA A . n 
B 1 526 VAL 526 526 526 VAL VAL A . n 
B 1 527 THR 527 527 527 THR THR A . n 
B 1 528 LEU 528 528 528 LEU LEU A . n 
B 1 529 PHE 529 529 529 PHE PHE A . n 
B 1 530 CYS 530 530 530 CYS CYS A . n 
B 1 531 SER 531 531 531 SER SER A . n 
B 1 532 ILE 532 532 532 ILE ILE A . n 
B 1 533 LEU 533 533 533 LEU LEU A . n 
B 1 534 ILE 534 534 534 ILE ILE A . n 
B 1 535 ALA 535 535 535 ALA ALA A . n 
B 1 536 GLY 536 536 536 GLY GLY A . n 
B 1 537 ILE 537 537 537 ILE ILE A . n 
B 1 538 SER 538 538 538 SER SER A . n 
B 1 539 LEU 539 539 539 LEU LEU A . n 
B 1 540 MET 540 540 540 MET MET A . n 
B 1 541 CYS 541 541 541 CYS CYS A . n 
B 1 542 MET 542 542 542 MET MET A . n 
B 1 543 ASN 543 543 543 ASN ASN A . n 
B 1 544 GLN 544 544 544 GLN GLN A . n 
B 1 545 THR 545 545 545 THR THR A . n 
B 1 546 ALA 546 546 ?   ?   ?   A . n 
B 1 547 GLN 547 547 ?   ?   ?   A . n 
B 1 548 ALA 548 548 ?   ?   ?   A . n 
B 1 549 GLY 549 549 ?   ?   ?   A . n 
B 1 550 SER 550 550 ?   ?   ?   A . n 
B 1 551 TYR 551 551 ?   ?   ?   A . n 
B 1 552 GLU 552 552 ?   ?   ?   A . n 
B 1 553 GLY 553 553 ?   ?   ?   A . n 
B 1 554 PHE 554 554 ?   ?   ?   A . n 
B 1 555 ASP 555 555 ?   ?   ?   A . n 
B 1 556 GLN 556 556 ?   ?   ?   A . n 
B 1 557 SER 557 557 ?   ?   ?   A . n 
B 1 558 GLN 558 558 ?   ?   ?   A . n 
B 1 559 SER 559 559 ?   ?   ?   A . n 
B 1 560 HIS 560 560 ?   ?   ?   A . n 
B 1 561 LYS 561 561 ?   ?   ?   A . n 
B 1 562 VAL 562 562 ?   ?   ?   A . n 
B 1 563 VAL 563 563 ?   ?   ?   A . n 
B 1 564 GLU 564 564 ?   ?   ?   A . n 
B 1 565 PRO 565 565 ?   ?   ?   A . n 
B 1 566 GLY 566 566 ?   ?   ?   A . n 
B 1 567 ASN 567 567 ?   ?   ?   A . n 
B 1 568 THR 568 568 ?   ?   ?   A . n 
B 1 569 ALA 569 569 ?   ?   ?   A . n 
B 1 570 PHE 570 570 ?   ?   ?   A . n 
B 1 571 GLU 571 571 ?   ?   ?   A . n 
B 1 572 GLU 572 572 ?   ?   ?   A . n 
B 1 573 SER 573 573 ?   ?   ?   A . n 
B 1 574 PRO 574 574 ?   ?   ?   A . n 
B 1 575 ALA 575 575 ?   ?   ?   A . n 
B 1 576 PRO 576 576 ?   ?   ?   A . n 
B 1 577 VAL 577 577 ?   ?   ?   A . n 
B 1 578 ASN 578 578 ?   ?   ?   A . n 
B 1 579 GLU 579 579 ?   ?   ?   A . n 
B 1 580 PRO 580 580 ?   ?   ?   A . n 
B 1 581 GLU 581 581 ?   ?   ?   A . n 
B 1 582 LEU 582 582 ?   ?   ?   A . n 
B 1 583 PHE 583 583 ?   ?   ?   A . n 
B 1 584 THR 584 584 ?   ?   ?   A . n 
B 1 585 SER 585 585 ?   ?   ?   A . n 
B 1 586 SER 586 586 ?   ?   ?   A . n 
B 1 587 ILE 587 587 ?   ?   ?   A . n 
B 1 588 PRO 588 588 ?   ?   ?   A . n 
B 1 589 GLU 589 589 ?   ?   ?   A . n 
B 1 590 THR 590 590 ?   ?   ?   A . n 
B 1 591 SER 591 591 ?   ?   ?   A . n 
B 1 592 CYS 592 592 ?   ?   ?   A . n 
B 1 593 CYS 593 593 ?   ?   ?   A . n 
B 1 594 SER 594 594 ?   ?   ?   A . n 
B 1 595 CYS 595 595 ?   ?   ?   A . n 
B 1 596 SER 596 596 ?   ?   ?   A . n 
B 1 597 MET 597 597 ?   ?   ?   A . n 
B 1 598 GLY 598 598 ?   ?   ?   A . n 
B 1 599 ASN 599 599 ?   ?   ?   A . n 
B 1 600 GLY 600 600 ?   ?   ?   A . n 
B 1 601 GLU 601 601 ?   ?   ?   A . n 
B 1 602 LEU 602 602 ?   ?   ?   A . n 
B 1 603 HIS 603 603 ?   ?   ?   A . n 
B 1 604 CYS 604 604 ?   ?   ?   A . n 
B 1 605 PRO 605 605 ?   ?   ?   A . n 
B 1 606 SER 606 606 ?   ?   ?   A . n 
B 1 607 ILE 607 607 ?   ?   ?   A . n 
B 1 608 GLU 608 608 ?   ?   ?   A . n 
B 1 609 PRO 609 609 ?   ?   ?   A . n 
B 1 610 ILE 610 610 ?   ?   ?   A . n 
B 1 611 ALA 611 611 ?   ?   ?   A . n 
B 1 612 ASN 612 612 ?   ?   ?   A . n 
B 1 613 THR 613 613 ?   ?   ?   A . n 
B 1 614 SER 614 614 ?   ?   ?   A . n 
B 1 615 THR 615 615 ?   ?   ?   A . n 
B 1 616 SER 616 616 ?   ?   ?   A . n 
B 1 617 GLU 617 617 ?   ?   ?   A . n 
B 1 618 PRO 618 618 ?   ?   ?   A . n 
B 1 619 VAL 619 619 ?   ?   ?   A . n 
B 1 620 ILE 620 620 ?   ?   ?   A . n 
B 1 621 PRO 621 621 ?   ?   ?   A . n 
B 1 622 SER 622 622 ?   ?   ?   A . n 
B 1 623 PHE 623 623 ?   ?   ?   A . n 
B 1 624 GLU 624 624 ?   ?   ?   A . n 
B 1 625 LYS 625 625 ?   ?   ?   A . n 
B 1 626 ASN 626 626 ?   ?   ?   A . n 
B 1 627 ASN 627 627 ?   ?   ?   A . n 
B 1 628 HIS 628 628 ?   ?   ?   A . n 
B 1 629 CYS 629 629 ?   ?   ?   A . n 
B 1 630 VAL 630 630 ?   ?   ?   A . n 
B 1 631 SER 631 631 ?   ?   ?   A . n 
B 1 632 ARG 632 632 ?   ?   ?   A . n 
B 1 633 CYS 633 633 ?   ?   ?   A . n 
B 1 634 ASN 634 634 ?   ?   ?   A . n 
B 1 635 SER 635 635 ?   ?   ?   A . n 
B 1 636 GLN 636 636 ?   ?   ?   A . n 
B 1 637 SER 637 637 ?   ?   ?   A . n 
B 1 638 CYS 638 638 ?   ?   ?   A . n 
B 1 639 ILE 639 639 ?   ?   ?   A . n 
B 1 640 LEU 640 640 ?   ?   ?   A . n 
B 1 641 ALA 641 641 ?   ?   ?   A . n 
B 1 642 GLN 642 642 ?   ?   ?   A . n 
B 1 643 GLU 643 643 ?   ?   ?   A . n 
B 1 644 GLU 644 644 ?   ?   ?   A . n 
B 1 645 GLU 645 645 ?   ?   ?   A . n 
B 1 646 GLN 646 646 ?   ?   ?   A . n 
B 1 647 TYR 647 647 ?   ?   ?   A . n 
B 1 648 LEU 648 648 ?   ?   ?   A . n 
B 1 649 GLN 649 649 ?   ?   ?   A . n 
B 1 650 SER 650 650 ?   ?   ?   A . n 
B 1 651 GLY 651 651 ?   ?   ?   A . n 
B 1 652 ASP 652 652 ?   ?   ?   A . n 
B 1 653 GLN 653 653 ?   ?   ?   A . n 
B 1 654 GLN 654 654 654 GLN GLN A . n 
B 1 655 LEU 655 655 655 LEU LEU A . n 
B 1 656 THR 656 656 656 THR THR A . n 
B 1 657 ARG 657 657 657 ARG ARG A . n 
B 1 658 HIS 658 658 658 HIS HIS A . n 
B 1 659 VAL 659 659 659 VAL VAL A . n 
B 1 660 LEU 660 660 660 LEU LEU A . n 
B 1 661 LEU 661 661 661 LEU LEU A . n 
B 1 662 CYS 662 662 662 CYS CYS A . n 
B 1 663 LEU 663 663 663 LEU LEU A . n 
B 1 664 LEU 664 664 664 LEU LEU A . n 
B 1 665 LEU 665 665 665 LEU LEU A . n 
B 1 666 ILE 666 666 666 ILE ILE A . n 
B 1 667 ILE 667 667 667 ILE ILE A . n 
B 1 668 GLY 668 668 668 GLY GLY A . n 
B 1 669 LEU 669 669 669 LEU LEU A . n 
B 1 670 PHE 670 670 670 PHE PHE A . n 
B 1 671 ALA 671 671 671 ALA ALA A . n 
B 1 672 ASN 672 672 672 ASN ASN A . n 
B 1 673 LEU 673 673 673 LEU LEU A . n 
B 1 674 SER 674 674 674 SER SER A . n 
B 1 675 SER 675 675 675 SER SER A . n 
B 1 676 CYS 676 676 676 CYS CYS A . n 
B 1 677 LEU 677 677 677 LEU LEU A . n 
B 1 678 TRP 678 678 678 TRP TRP A . n 
B 1 679 TRP 679 679 679 TRP TRP A . n 
B 1 680 LEU 680 680 680 LEU LEU A . n 
B 1 681 PHE 681 681 681 PHE PHE A . n 
B 1 682 ASN 682 682 682 ASN ASN A . n 
B 1 683 GLN 683 683 683 GLN GLN A . n 
B 1 684 GLU 684 684 684 GLU GLU A . n 
B 1 685 PRO 685 685 685 PRO PRO A . n 
B 1 686 GLY 686 686 686 GLY GLY A . n 
B 1 687 ARG 687 687 687 ARG ARG A . n 
B 1 688 LEU 688 688 688 LEU LEU A . n 
B 1 689 TYR 689 689 689 TYR TYR A . n 
B 1 690 VAL 690 690 690 VAL VAL A . n 
B 1 691 GLU 691 691 691 GLU GLU A . n 
B 1 692 LEU 692 692 692 LEU LEU A . n 
B 1 693 GLN 693 693 693 GLN GLN A . n 
B 1 694 PHE 694 694 694 PHE PHE A . n 
B 1 695 PHE 695 695 695 PHE PHE A . n 
B 1 696 CYS 696 696 696 CYS CYS A . n 
B 1 697 ALA 697 697 697 ALA ALA A . n 
B 1 698 VAL 698 698 698 VAL VAL A . n 
B 1 699 PHE 699 699 699 PHE PHE A . n 
B 1 700 ASN 700 700 700 ASN ASN A . n 
B 1 701 PHE 701 701 701 PHE PHE A . n 
B 1 702 GLY 702 702 702 GLY GLY A . n 
B 1 703 GLN 703 703 703 GLN GLN A . n 
B 1 704 GLY 704 704 704 GLY GLY A . n 
B 1 705 PHE 705 705 705 PHE PHE A . n 
B 1 706 ILE 706 706 706 ILE ILE A . n 
B 1 707 SER 707 707 707 SER SER A . n 
B 1 708 PHE 708 708 708 PHE PHE A . n 
B 1 709 GLY 709 709 709 GLY GLY A . n 
B 1 710 ILE 710 710 710 ILE ILE A . n 
B 1 711 PHE 711 711 711 PHE PHE A . n 
B 1 712 GLY 712 712 712 GLY GLY A . n 
B 1 713 LEU 713 713 713 LEU LEU A . n 
B 1 714 ASP 714 714 714 ASP ASP A . n 
B 1 715 LYS 715 715 715 LYS LYS A . n 
B 1 716 HIS 716 716 716 HIS HIS A . n 
B 1 717 LEU 717 717 717 LEU LEU A . n 
B 1 718 ILE 718 718 718 ILE ILE A . n 
B 1 719 ILE 719 719 ?   ?   ?   A . n 
B 1 720 LEU 720 720 ?   ?   ?   A . n 
B 1 721 PRO 721 721 ?   ?   ?   A . n 
B 1 722 PHE 722 722 ?   ?   ?   A . n 
B 1 723 LYS 723 723 ?   ?   ?   A . n 
B 1 724 ARG 724 724 ?   ?   ?   A . n 
B 1 725 ARG 725 725 ?   ?   ?   A . n 
B 1 726 LEU 726 726 ?   ?   ?   A . n 
B 1 727 GLU 727 727 ?   ?   ?   A . n 
B 1 728 PHE 728 728 ?   ?   ?   A . n 
B 1 729 LEU 729 729 ?   ?   ?   A . n 
B 1 730 TRP 730 730 ?   ?   ?   A . n 
B 1 731 ASN 731 731 ?   ?   ?   A . n 
B 1 732 ASN 732 732 ?   ?   ?   A . n 
B 1 733 LYS 733 733 ?   ?   ?   A . n 
B 1 734 ASP 734 734 ?   ?   ?   A . n 
B 1 735 THR 735 735 ?   ?   ?   A . n 
B 1 736 ALA 736 736 ?   ?   ?   A . n 
B 1 737 GLU 737 737 ?   ?   ?   A . n 
B 1 738 ASN 738 738 ?   ?   ?   A . n 
B 1 739 ARG 739 739 ?   ?   ?   A . n 
B 1 740 ASP 740 740 ?   ?   ?   A . n 
B 1 741 SER 741 741 ?   ?   ?   A . n 
B 1 742 PRO 742 742 ?   ?   ?   A . n 
B 1 743 VAL 743 743 ?   ?   ?   A . n 
B 1 744 SER 744 744 ?   ?   ?   A . n 
B 1 745 GLU 745 745 ?   ?   ?   A . n 
B 1 746 GLU 746 746 ?   ?   ?   A . n 
B 1 747 ILE 747 747 ?   ?   ?   A . n 
B 1 748 LYS 748 748 ?   ?   ?   A . n 
B 1 749 MET 749 749 ?   ?   ?   A . n 
B 1 750 THR 750 750 ?   ?   ?   A . n 
B 1 751 CYS 751 751 ?   ?   ?   A . n 
B 1 752 GLN 752 752 ?   ?   ?   A . n 
B 1 753 GLN 753 753 ?   ?   ?   A . n 
B 1 754 PHE 754 754 ?   ?   ?   A . n 
B 1 755 ILE 755 755 ?   ?   ?   A . n 
B 1 756 HIS 756 756 ?   ?   ?   A . n 
B 1 757 TYR 757 757 ?   ?   ?   A . n 
B 1 758 HIS 758 758 ?   ?   ?   A . n 
B 1 759 ARG 759 759 ?   ?   ?   A . n 
B 1 760 ASP 760 760 ?   ?   ?   A . n 
B 1 761 LEU 761 761 ?   ?   ?   A . n 
B 1 762 CYS 762 762 ?   ?   ?   A . n 
B 1 763 ILE 763 763 ?   ?   ?   A . n 
B 1 764 ARG 764 764 ?   ?   ?   A . n 
B 1 765 ASN 765 765 ?   ?   ?   A . n 
B 1 766 ILE 766 766 ?   ?   ?   A . n 
B 1 767 VAL 767 767 ?   ?   ?   A . n 
B 1 768 LYS 768 768 ?   ?   ?   A . n 
B 1 769 GLU 769 769 ?   ?   ?   A . n 
B 1 770 ARG 770 770 ?   ?   ?   A . n 
B 1 771 ARG 771 771 ?   ?   ?   A . n 
B 1 772 CYS 772 772 ?   ?   ?   A . n 
B 1 773 GLY 773 773 ?   ?   ?   A . n 
B 1 774 ALA 774 774 ?   ?   ?   A . n 
B 1 775 LYS 775 775 ?   ?   ?   A . n 
B 1 776 THR 776 776 ?   ?   ?   A . n 
B 1 777 SER 777 777 ?   ?   ?   A . n 
B 1 778 ALA 778 778 ?   ?   ?   A . n 
B 1 779 GLY 779 779 ?   ?   ?   A . n 
B 1 780 THR 780 780 ?   ?   ?   A . n 
B 1 781 PHE 781 781 ?   ?   ?   A . n 
B 1 782 CYS 782 782 ?   ?   ?   A . n 
B 1 783 GLY 783 783 ?   ?   ?   A . n 
B 1 784 CYS 784 784 ?   ?   ?   A . n 
B 1 785 ASP 785 785 ?   ?   ?   A . n 
B 1 786 LEU 786 786 ?   ?   ?   A . n 
B 1 787 VAL 787 787 ?   ?   ?   A . n 
B 1 788 SER 788 788 ?   ?   ?   A . n 
B 1 789 TRP 789 789 ?   ?   ?   A . n 
B 1 790 LEU 790 790 ?   ?   ?   A . n 
B 1 791 ILE 791 791 ?   ?   ?   A . n 
B 1 792 GLU 792 792 ?   ?   ?   A . n 
B 1 793 VAL 793 793 ?   ?   ?   A . n 
B 1 794 GLY 794 794 ?   ?   ?   A . n 
B 1 795 LEU 795 795 ?   ?   ?   A . n 
B 1 796 ALA 796 796 ?   ?   ?   A . n 
B 1 797 SER 797 797 ?   ?   ?   A . n 
B 1 798 ASP 798 798 ?   ?   ?   A . n 
B 1 799 ARG 799 799 ?   ?   ?   A . n 
B 1 800 GLY 800 800 ?   ?   ?   A . n 
B 1 801 GLU 801 801 ?   ?   ?   A . n 
B 1 802 ALA 802 802 ?   ?   ?   A . n 
B 1 803 VAL 803 803 ?   ?   ?   A . n 
B 1 804 ILE 804 804 ?   ?   ?   A . n 
B 1 805 TYR 805 805 ?   ?   ?   A . n 
B 1 806 GLY 806 806 ?   ?   ?   A . n 
B 1 807 ASP 807 807 ?   ?   ?   A . n 
B 1 808 ARG 808 808 ?   ?   ?   A . n 
B 1 809 LEU 809 809 ?   ?   ?   A . n 
B 1 810 VAL 810 810 ?   ?   ?   A . n 
B 1 811 GLN 811 811 ?   ?   ?   A . n 
B 1 812 GLY 812 812 ?   ?   ?   A . n 
B 1 813 GLY 813 813 ?   ?   ?   A . n 
B 1 814 VAL 814 814 ?   ?   ?   A . n 
B 1 815 ILE 815 815 ?   ?   ?   A . n 
B 1 816 GLN 816 816 ?   ?   ?   A . n 
B 1 817 HIS 817 817 ?   ?   ?   A . n 
B 1 818 ILE 818 818 ?   ?   ?   A . n 
B 1 819 THR 819 819 ?   ?   ?   A . n 
B 1 820 ASN 820 820 ?   ?   ?   A . n 
B 1 821 GLU 821 821 ?   ?   ?   A . n 
B 1 822 TYR 822 822 ?   ?   ?   A . n 
B 1 823 GLU 823 823 ?   ?   ?   A . n 
B 1 824 PHE 824 824 ?   ?   ?   A . n 
B 1 825 ARG 825 825 ?   ?   ?   A . n 
B 1 826 ASP 826 826 ?   ?   ?   A . n 
B 1 827 GLU 827 827 ?   ?   ?   A . n 
B 1 828 TYR 828 828 ?   ?   ?   A . n 
B 1 829 LEU 829 829 ?   ?   ?   A . n 
B 1 830 PHE 830 830 ?   ?   ?   A . n 
B 1 831 TYR 831 831 ?   ?   ?   A . n 
B 1 832 ARG 832 832 ?   ?   ?   A . n 
B 1 833 PHE 833 833 ?   ?   ?   A . n 
B 1 834 LEU 834 834 ?   ?   ?   A . n 
B 1 835 GLN 835 835 ?   ?   ?   A . n 
B 1 836 LYS 836 836 ?   ?   ?   A . n 
B 1 837 SER 837 837 ?   ?   ?   A . n 
B 1 838 PRO 838 838 ?   ?   ?   A . n 
B 1 839 GLU 839 839 ?   ?   ?   A . n 
B 1 840 GLN 840 840 ?   ?   ?   A . n 
B 1 841 SER 841 841 ?   ?   ?   A . n 
B 1 842 PRO 842 842 ?   ?   ?   A . n 
B 1 843 PRO 843 843 ?   ?   ?   A . n 
B 1 844 ALA 844 844 ?   ?   ?   A . n 
B 1 845 ILE 845 845 ?   ?   ?   A . n 
B 1 846 ASN 846 846 ?   ?   ?   A . n 
B 1 847 ALA 847 847 ?   ?   ?   A . n 
B 1 848 ASN 848 848 ?   ?   ?   A . n 
B 1 849 THR 849 849 ?   ?   ?   A . n 
B 1 850 LEU 850 850 ?   ?   ?   A . n 
B 1 851 GLN 851 851 ?   ?   ?   A . n 
B 1 852 GLN 852 852 ?   ?   ?   A . n 
B 1 853 GLU 853 853 ?   ?   ?   A . n 
B 1 854 ARG 854 854 ?   ?   ?   A . n 
B 1 855 TYR 855 855 ?   ?   ?   A . n 
B 1 856 LYS 856 856 ?   ?   ?   A . n 
B 1 857 GLU 857 857 ?   ?   ?   A . n 
B 1 858 ILE 858 858 ?   ?   ?   A . n 
B 1 859 GLU 859 859 ?   ?   ?   A . n 
B 1 860 HIS 860 860 ?   ?   ?   A . n 
B 1 861 SER 861 861 ?   ?   ?   A . n 
B 1 862 SER 862 862 ?   ?   ?   A . n 
B 1 863 PRO 863 863 ?   ?   ?   A . n 
B 1 864 PRO 864 864 ?   ?   ?   A . n 
B 1 865 SER 865 865 ?   ?   ?   A . n 
B 1 866 HIS 866 866 ?   ?   ?   A . n 
B 1 867 SER 867 867 ?   ?   ?   A . n 
B 1 868 PRO 868 868 ?   ?   ?   A . n 
B 1 869 LYS 869 869 ?   ?   ?   A . n 
B 1 870 THR 870 870 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        POV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   POV 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 POV 1 1101 1101 POV POV B . 
D 3 IOS 1 1102 1102 IOS IOS B . 
E 4 CLR 1 1103 902  CLR CLR B . 
F 2 POV 1 1104 903  POV POV B . 
G 2 POV 1 1105 1001 POV POV B . 
H 5 NAG 1 1106 1002 NAG NAG B . 
I 6 TRP 1 1107 1003 TRP TRP B . 
J 2 POV 1 1101 1101 POV POV A . 
K 3 IOS 1 1102 1102 IOS IOS A . 
L 4 CLR 1 1103 902  CLR CLR A . 
M 2 POV 1 1104 903  POV POV A . 
N 2 POV 1 1105 1001 POV POV A . 
O 5 NAG 1 1106 1002 NAG NAG A . 
P 6 TRP 1 1107 1003 TRP TRP A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B TRP 193  ? CG   ? A TRP 193 CG   
2   1 Y 1 B TRP 193  ? CD1  ? A TRP 193 CD1  
3   1 Y 1 B TRP 193  ? CD2  ? A TRP 193 CD2  
4   1 Y 1 B TRP 193  ? NE1  ? A TRP 193 NE1  
5   1 Y 1 B TRP 193  ? CE2  ? A TRP 193 CE2  
6   1 Y 1 B TRP 193  ? CE3  ? A TRP 193 CE3  
7   1 Y 1 B TRP 193  ? CZ2  ? A TRP 193 CZ2  
8   1 Y 1 B TRP 193  ? CZ3  ? A TRP 193 CZ3  
9   1 Y 1 B TRP 193  ? CH2  ? A TRP 193 CH2  
10  1 Y 1 B LYS 194  ? CG   ? A LYS 194 CG   
11  1 Y 1 B LYS 194  ? CD   ? A LYS 194 CD   
12  1 Y 1 B LYS 194  ? CE   ? A LYS 194 CE   
13  1 Y 1 B LYS 194  ? NZ   ? A LYS 194 NZ   
14  1 Y 1 B ASP 195  ? CG   ? A ASP 195 CG   
15  1 Y 1 B ASP 195  ? OD1  ? A ASP 195 OD1  
16  1 Y 1 B ASP 195  ? OD2  ? A ASP 195 OD2  
17  1 Y 1 B THR 196  ? OG1  ? A THR 196 OG1  
18  1 Y 1 B THR 196  ? CG2  ? A THR 196 CG2  
19  1 Y 1 B GLN 197  ? CG   ? A GLN 197 CG   
20  1 Y 1 B GLN 197  ? CD   ? A GLN 197 CD   
21  1 Y 1 B GLN 197  ? OE1  ? A GLN 197 OE1  
22  1 Y 1 B GLN 197  ? NE2  ? A GLN 197 NE2  
23  1 Y 1 B ASN 198  ? CG   ? A ASN 198 CG   
24  1 Y 1 B ASN 198  ? OD1  ? A ASN 198 OD1  
25  1 Y 1 B ASN 198  ? ND2  ? A ASN 198 ND2  
26  1 Y 1 B SER 200  ? OG   ? A SER 200 OG   
27  1 Y 1 B GLN 201  ? CG   ? A GLN 201 CG   
28  1 Y 1 B GLN 201  ? CD   ? A GLN 201 CD   
29  1 Y 1 B GLN 201  ? OE1  ? A GLN 201 OE1  
30  1 Y 1 B GLN 201  ? NE2  ? A GLN 201 NE2  
31  1 Y 1 B ASN 202  ? CG   ? A ASN 202 CG   
32  1 Y 1 B ASN 202  ? OD1  ? A ASN 202 OD1  
33  1 Y 1 B ASN 202  ? ND2  ? A ASN 202 ND2  
34  1 Y 1 B LYS 203  ? CG   ? A LYS 203 CG   
35  1 Y 1 B LYS 203  ? CD   ? A LYS 203 CD   
36  1 Y 1 B LYS 203  ? CE   ? A LYS 203 CE   
37  1 Y 1 B LYS 203  ? NZ   ? A LYS 203 NZ   
38  1 Y 1 B VAL 435  ? CG1  ? A VAL 435 CG1  
39  1 Y 1 B VAL 435  ? CG2  ? A VAL 435 CG2  
40  1 Y 1 B LYS 436  ? CG   ? A LYS 436 CG   
41  1 Y 1 B LYS 436  ? CD   ? A LYS 436 CD   
42  1 Y 1 B LYS 436  ? CE   ? A LYS 436 CE   
43  1 Y 1 B LYS 436  ? NZ   ? A LYS 436 NZ   
44  1 Y 1 B GLU 437  ? CG   ? A GLU 437 CG   
45  1 Y 1 B GLU 437  ? CD   ? A GLU 437 CD   
46  1 Y 1 B GLU 437  ? OE1  ? A GLU 437 OE1  
47  1 Y 1 B GLU 437  ? OE2  ? A GLU 437 OE2  
48  1 Y 1 B LYS 438  ? CG   ? A LYS 438 CG   
49  1 Y 1 B LYS 438  ? CD   ? A LYS 438 CD   
50  1 Y 1 B LYS 438  ? CE   ? A LYS 438 CE   
51  1 Y 1 B LYS 438  ? NZ   ? A LYS 438 NZ   
52  1 Y 1 B ASN 439  ? CG   ? A ASN 439 CG   
53  1 Y 1 B ASN 439  ? OD1  ? A ASN 439 OD1  
54  1 Y 1 B ASN 439  ? ND2  ? A ASN 439 ND2  
55  1 Y 1 B LYS 472  ? CG   ? A LYS 472 CG   
56  1 Y 1 B LYS 472  ? CD   ? A LYS 472 CD   
57  1 Y 1 B LYS 472  ? CE   ? A LYS 472 CE   
58  1 Y 1 B LYS 472  ? NZ   ? A LYS 472 NZ   
59  1 Y 1 B LYS 473  ? CG   ? A LYS 473 CG   
60  1 Y 1 B LYS 473  ? CD   ? A LYS 473 CD   
61  1 Y 1 B LYS 473  ? CE   ? A LYS 473 CE   
62  1 Y 1 B LYS 473  ? NZ   ? A LYS 473 NZ   
63  1 Y 1 B ARG 474  ? CG   ? A ARG 474 CG   
64  1 Y 1 B ARG 474  ? CD   ? A ARG 474 CD   
65  1 Y 1 B ARG 474  ? NE   ? A ARG 474 NE   
66  1 Y 1 B ARG 474  ? CZ   ? A ARG 474 CZ   
67  1 Y 1 B ARG 474  ? NH1  ? A ARG 474 NH1  
68  1 Y 1 B ARG 474  ? NH2  ? A ARG 474 NH2  
69  1 Y 1 B GLU 475  ? CG   ? A GLU 475 CG   
70  1 Y 1 B GLU 475  ? CD   ? A GLU 475 CD   
71  1 Y 1 B GLU 475  ? OE1  ? A GLU 475 OE1  
72  1 Y 1 B GLU 475  ? OE2  ? A GLU 475 OE2  
73  1 Y 1 B ARG 476  ? CG   ? A ARG 476 CG   
74  1 Y 1 B ARG 476  ? CD   ? A ARG 476 CD   
75  1 Y 1 B ARG 476  ? NE   ? A ARG 476 NE   
76  1 Y 1 B ARG 476  ? CZ   ? A ARG 476 CZ   
77  1 Y 1 B ARG 476  ? NH1  ? A ARG 476 NH1  
78  1 Y 1 B ARG 476  ? NH2  ? A ARG 476 NH2  
79  1 Y 1 B VAL 477  ? CG1  ? A VAL 477 CG1  
80  1 Y 1 B VAL 477  ? CG2  ? A VAL 477 CG2  
81  1 Y 1 B GLN 478  ? CG   ? A GLN 478 CG   
82  1 Y 1 B GLN 478  ? CD   ? A GLN 478 CD   
83  1 Y 1 B GLN 478  ? OE1  ? A GLN 478 OE1  
84  1 Y 1 B GLN 478  ? NE2  ? A GLN 478 NE2  
85  1 Y 1 B ILE 479  ? CG1  ? A ILE 479 CG1  
86  1 Y 1 B ILE 479  ? CG2  ? A ILE 479 CG2  
87  1 Y 1 B ILE 479  ? CD1  ? A ILE 479 CD1  
88  1 Y 1 B LEU 495  ? CG   ? A LEU 495 CG   
89  1 Y 1 B LEU 495  ? CD1  ? A LEU 495 CD1  
90  1 Y 1 B LEU 495  ? CD2  ? A LEU 495 CD2  
91  1 Y 1 B VAL 496  ? CG1  ? A VAL 496 CG1  
92  1 Y 1 B VAL 496  ? CG2  ? A VAL 496 CG2  
93  1 Y 1 B VAL 498  ? CG1  ? A VAL 498 CG1  
94  1 Y 1 B VAL 498  ? CG2  ? A VAL 498 CG2  
95  1 Y 1 B LEU 499  ? CG   ? A LEU 499 CG   
96  1 Y 1 B LEU 499  ? CD1  ? A LEU 499 CD1  
97  1 Y 1 B LEU 499  ? CD2  ? A LEU 499 CD2  
98  1 Y 1 B LEU 500  ? CG   ? A LEU 500 CG   
99  1 Y 1 B LEU 500  ? CD1  ? A LEU 500 CD1  
100 1 Y 1 B LEU 500  ? CD2  ? A LEU 500 CD2  
101 1 Y 1 B ILE 501  ? CG1  ? A ILE 501 CG1  
102 1 Y 1 B ILE 501  ? CG2  ? A ILE 501 CG2  
103 1 Y 1 B ILE 501  ? CD1  ? A ILE 501 CD1  
104 1 Y 1 B THR 502  ? OG1  ? A THR 502 OG1  
105 1 Y 1 B THR 502  ? CG2  ? A THR 502 CG2  
106 1 Y 1 B LYS 504  ? CG   ? A LYS 504 CG   
107 1 Y 1 B LYS 504  ? CD   ? A LYS 504 CD   
108 1 Y 1 B LYS 504  ? CE   ? A LYS 504 CE   
109 1 Y 1 B LYS 504  ? NZ   ? A LYS 504 NZ   
110 1 Y 1 B HIS 505  ? CG   ? A HIS 505 CG   
111 1 Y 1 B HIS 505  ? ND1  ? A HIS 505 ND1  
112 1 Y 1 B HIS 505  ? CD2  ? A HIS 505 CD2  
113 1 Y 1 B HIS 505  ? CE1  ? A HIS 505 CE1  
114 1 Y 1 B HIS 505  ? NE2  ? A HIS 505 NE2  
115 1 Y 1 B ASN 506  ? CG   ? A ASN 506 CG   
116 1 Y 1 B ASN 506  ? OD1  ? A ASN 506 OD1  
117 1 Y 1 B ASN 506  ? ND2  ? A ASN 506 ND2  
118 1 Y 1 B ASP 508  ? CG   ? A ASP 508 CG   
119 1 Y 1 B ASP 508  ? OD1  ? A ASP 508 OD1  
120 1 Y 1 B ASP 508  ? OD2  ? A ASP 508 OD2  
121 1 Y 1 B SER 509  ? OG   ? A SER 509 OG   
122 1 Y 1 B ILE 510  ? CG1  ? A ILE 510 CG1  
123 1 Y 1 B ILE 510  ? CG2  ? A ILE 510 CG2  
124 1 Y 1 B ILE 510  ? CD1  ? A ILE 510 CD1  
125 1 Y 1 B ASP 511  ? CG   ? A ASP 511 CG   
126 1 Y 1 B ASP 511  ? OD1  ? A ASP 511 OD1  
127 1 Y 1 B ASP 511  ? OD2  ? A ASP 511 OD2  
128 1 Y 1 B SER 512  ? OG   ? A SER 512 OG   
129 1 Y 1 B PHE 514  ? CG   ? A PHE 514 CG   
130 1 Y 1 B PHE 514  ? CD1  ? A PHE 514 CD1  
131 1 Y 1 B PHE 514  ? CD2  ? A PHE 514 CD2  
132 1 Y 1 B PHE 514  ? CE1  ? A PHE 514 CE1  
133 1 Y 1 B PHE 514  ? CE2  ? A PHE 514 CE2  
134 1 Y 1 B PHE 514  ? CZ   ? A PHE 514 CZ   
135 1 Y 1 B PHE 515  ? CG   ? A PHE 515 CG   
136 1 Y 1 B PHE 515  ? CD1  ? A PHE 515 CD1  
137 1 Y 1 B PHE 515  ? CD2  ? A PHE 515 CD2  
138 1 Y 1 B PHE 515  ? CE1  ? A PHE 515 CE1  
139 1 Y 1 B PHE 515  ? CE2  ? A PHE 515 CE2  
140 1 Y 1 B PHE 515  ? CZ   ? A PHE 515 CZ   
141 1 Y 1 B TYR 516  ? CG   ? A TYR 516 CG   
142 1 Y 1 B TYR 516  ? CD1  ? A TYR 516 CD1  
143 1 Y 1 B TYR 516  ? CD2  ? A TYR 516 CD2  
144 1 Y 1 B TYR 516  ? CE1  ? A TYR 516 CE1  
145 1 Y 1 B TYR 516  ? CE2  ? A TYR 516 CE2  
146 1 Y 1 B TYR 516  ? CZ   ? A TYR 516 CZ   
147 1 Y 1 B TYR 516  ? OH   ? A TYR 516 OH   
148 1 Y 1 B LYS 518  ? CG   ? A LYS 518 CG   
149 1 Y 1 B LYS 518  ? CD   ? A LYS 518 CD   
150 1 Y 1 B LYS 518  ? CE   ? A LYS 518 CE   
151 1 Y 1 B LYS 518  ? NZ   ? A LYS 518 NZ   
152 1 Y 1 B GLU 519  ? CG   ? A GLU 519 CG   
153 1 Y 1 B GLU 519  ? CD   ? A GLU 519 CD   
154 1 Y 1 B GLU 519  ? OE1  ? A GLU 519 OE1  
155 1 Y 1 B GLU 519  ? OE2  ? A GLU 519 OE2  
156 1 Y 1 B ILE 537  ? CG1  ? A ILE 537 CG1  
157 1 Y 1 B ILE 537  ? CG2  ? A ILE 537 CG2  
158 1 Y 1 B ILE 537  ? CD1  ? A ILE 537 CD1  
159 1 Y 1 B SER 538  ? OG   ? A SER 538 OG   
160 1 Y 1 B LEU 539  ? CG   ? A LEU 539 CG   
161 1 Y 1 B LEU 539  ? CD1  ? A LEU 539 CD1  
162 1 Y 1 B LEU 539  ? CD2  ? A LEU 539 CD2  
163 1 Y 1 B MET 540  ? CG   ? A MET 540 CG   
164 1 Y 1 B MET 540  ? SD   ? A MET 540 SD   
165 1 Y 1 B MET 540  ? CE   ? A MET 540 CE   
166 1 Y 1 B CYS 541  ? SG   ? A CYS 541 SG   
167 1 Y 1 B MET 542  ? CG   ? A MET 542 CG   
168 1 Y 1 B MET 542  ? SD   ? A MET 542 SD   
169 1 Y 1 B MET 542  ? CE   ? A MET 542 CE   
170 1 Y 1 B ASN 543  ? CG   ? A ASN 543 CG   
171 1 Y 1 B ASN 543  ? OD1  ? A ASN 543 OD1  
172 1 Y 1 B ASN 543  ? ND2  ? A ASN 543 ND2  
173 1 Y 1 B GLN 544  ? CG   ? A GLN 544 CG   
174 1 Y 1 B GLN 544  ? CD   ? A GLN 544 CD   
175 1 Y 1 B GLN 544  ? OE1  ? A GLN 544 OE1  
176 1 Y 1 B GLN 544  ? NE2  ? A GLN 544 NE2  
177 1 Y 1 B THR 545  ? OG1  ? A THR 545 OG1  
178 1 Y 1 B THR 545  ? CG2  ? A THR 545 CG2  
179 1 Y 1 B GLN 683  ? CG   ? A GLN 683 CG   
180 1 Y 1 B GLN 683  ? CD   ? A GLN 683 CD   
181 1 Y 1 B GLN 683  ? OE1  ? A GLN 683 OE1  
182 1 Y 1 B GLN 683  ? NE2  ? A GLN 683 NE2  
183 1 Y 1 B GLU 684  ? CG   ? A GLU 684 CG   
184 1 Y 1 B GLU 684  ? CD   ? A GLU 684 CD   
185 1 Y 1 B GLU 684  ? OE1  ? A GLU 684 OE1  
186 1 Y 1 B GLU 684  ? OE2  ? A GLU 684 OE2  
187 1 Y 1 B PRO 685  ? CG   ? A PRO 685 CG   
188 1 Y 1 B PRO 685  ? CD   ? A PRO 685 CD   
189 1 Y 1 B ARG 687  ? CG   ? A ARG 687 CG   
190 1 Y 1 B ARG 687  ? CD   ? A ARG 687 CD   
191 1 Y 1 B ARG 687  ? NE   ? A ARG 687 NE   
192 1 Y 1 B ARG 687  ? CZ   ? A ARG 687 CZ   
193 1 Y 1 B ARG 687  ? NH1  ? A ARG 687 NH1  
194 1 Y 1 B ARG 687  ? NH2  ? A ARG 687 NH2  
195 1 Y 1 B LEU 688  ? CG   ? A LEU 688 CG   
196 1 Y 1 B LEU 688  ? CD1  ? A LEU 688 CD1  
197 1 Y 1 B LEU 688  ? CD2  ? A LEU 688 CD2  
198 1 Y 1 B TYR 689  ? CG   ? A TYR 689 CG   
199 1 Y 1 B TYR 689  ? CD1  ? A TYR 689 CD1  
200 1 Y 1 B TYR 689  ? CD2  ? A TYR 689 CD2  
201 1 Y 1 B TYR 689  ? CE1  ? A TYR 689 CE1  
202 1 Y 1 B TYR 689  ? CE2  ? A TYR 689 CE2  
203 1 Y 1 B TYR 689  ? CZ   ? A TYR 689 CZ   
204 1 Y 1 B TYR 689  ? OH   ? A TYR 689 OH   
205 1 Y 1 A TRP 193  ? CG   ? B TRP 193 CG   
206 1 Y 1 A TRP 193  ? CD1  ? B TRP 193 CD1  
207 1 Y 1 A TRP 193  ? CD2  ? B TRP 193 CD2  
208 1 Y 1 A TRP 193  ? NE1  ? B TRP 193 NE1  
209 1 Y 1 A TRP 193  ? CE2  ? B TRP 193 CE2  
210 1 Y 1 A TRP 193  ? CE3  ? B TRP 193 CE3  
211 1 Y 1 A TRP 193  ? CZ2  ? B TRP 193 CZ2  
212 1 Y 1 A TRP 193  ? CZ3  ? B TRP 193 CZ3  
213 1 Y 1 A TRP 193  ? CH2  ? B TRP 193 CH2  
214 1 Y 1 A LYS 194  ? CG   ? B LYS 194 CG   
215 1 Y 1 A LYS 194  ? CD   ? B LYS 194 CD   
216 1 Y 1 A LYS 194  ? CE   ? B LYS 194 CE   
217 1 Y 1 A LYS 194  ? NZ   ? B LYS 194 NZ   
218 1 Y 1 A ASP 195  ? CG   ? B ASP 195 CG   
219 1 Y 1 A ASP 195  ? OD1  ? B ASP 195 OD1  
220 1 Y 1 A ASP 195  ? OD2  ? B ASP 195 OD2  
221 1 Y 1 A THR 196  ? OG1  ? B THR 196 OG1  
222 1 Y 1 A THR 196  ? CG2  ? B THR 196 CG2  
223 1 Y 1 A GLN 197  ? CG   ? B GLN 197 CG   
224 1 Y 1 A GLN 197  ? CD   ? B GLN 197 CD   
225 1 Y 1 A GLN 197  ? OE1  ? B GLN 197 OE1  
226 1 Y 1 A GLN 197  ? NE2  ? B GLN 197 NE2  
227 1 Y 1 A ASN 198  ? CG   ? B ASN 198 CG   
228 1 Y 1 A ASN 198  ? OD1  ? B ASN 198 OD1  
229 1 Y 1 A ASN 198  ? ND2  ? B ASN 198 ND2  
230 1 Y 1 A SER 200  ? OG   ? B SER 200 OG   
231 1 Y 1 A GLN 201  ? CG   ? B GLN 201 CG   
232 1 Y 1 A GLN 201  ? CD   ? B GLN 201 CD   
233 1 Y 1 A GLN 201  ? OE1  ? B GLN 201 OE1  
234 1 Y 1 A GLN 201  ? NE2  ? B GLN 201 NE2  
235 1 Y 1 A ASN 202  ? CG   ? B ASN 202 CG   
236 1 Y 1 A ASN 202  ? OD1  ? B ASN 202 OD1  
237 1 Y 1 A ASN 202  ? ND2  ? B ASN 202 ND2  
238 1 Y 1 A LYS 203  ? CG   ? B LYS 203 CG   
239 1 Y 1 A LYS 203  ? CD   ? B LYS 203 CD   
240 1 Y 1 A LYS 203  ? CE   ? B LYS 203 CE   
241 1 Y 1 A LYS 203  ? NZ   ? B LYS 203 NZ   
242 1 Y 1 A VAL 435  ? CG1  ? B VAL 435 CG1  
243 1 Y 1 A VAL 435  ? CG2  ? B VAL 435 CG2  
244 1 Y 1 A LYS 436  ? CG   ? B LYS 436 CG   
245 1 Y 1 A LYS 436  ? CD   ? B LYS 436 CD   
246 1 Y 1 A LYS 436  ? CE   ? B LYS 436 CE   
247 1 Y 1 A LYS 436  ? NZ   ? B LYS 436 NZ   
248 1 Y 1 A GLU 437  ? CG   ? B GLU 437 CG   
249 1 Y 1 A GLU 437  ? CD   ? B GLU 437 CD   
250 1 Y 1 A GLU 437  ? OE1  ? B GLU 437 OE1  
251 1 Y 1 A GLU 437  ? OE2  ? B GLU 437 OE2  
252 1 Y 1 A LYS 438  ? CG   ? B LYS 438 CG   
253 1 Y 1 A LYS 438  ? CD   ? B LYS 438 CD   
254 1 Y 1 A LYS 438  ? CE   ? B LYS 438 CE   
255 1 Y 1 A LYS 438  ? NZ   ? B LYS 438 NZ   
256 1 Y 1 A ASN 439  ? CG   ? B ASN 439 CG   
257 1 Y 1 A ASN 439  ? OD1  ? B ASN 439 OD1  
258 1 Y 1 A ASN 439  ? ND2  ? B ASN 439 ND2  
259 1 Y 1 A LYS 472  ? CG   ? B LYS 472 CG   
260 1 Y 1 A LYS 472  ? CD   ? B LYS 472 CD   
261 1 Y 1 A LYS 472  ? CE   ? B LYS 472 CE   
262 1 Y 1 A LYS 472  ? NZ   ? B LYS 472 NZ   
263 1 Y 1 A LYS 473  ? CG   ? B LYS 473 CG   
264 1 Y 1 A LYS 473  ? CD   ? B LYS 473 CD   
265 1 Y 1 A LYS 473  ? CE   ? B LYS 473 CE   
266 1 Y 1 A LYS 473  ? NZ   ? B LYS 473 NZ   
267 1 Y 1 A ARG 474  ? CG   ? B ARG 474 CG   
268 1 Y 1 A ARG 474  ? CD   ? B ARG 474 CD   
269 1 Y 1 A ARG 474  ? NE   ? B ARG 474 NE   
270 1 Y 1 A ARG 474  ? CZ   ? B ARG 474 CZ   
271 1 Y 1 A ARG 474  ? NH1  ? B ARG 474 NH1  
272 1 Y 1 A ARG 474  ? NH2  ? B ARG 474 NH2  
273 1 Y 1 A GLU 475  ? CG   ? B GLU 475 CG   
274 1 Y 1 A GLU 475  ? CD   ? B GLU 475 CD   
275 1 Y 1 A GLU 475  ? OE1  ? B GLU 475 OE1  
276 1 Y 1 A GLU 475  ? OE2  ? B GLU 475 OE2  
277 1 Y 1 A ARG 476  ? CG   ? B ARG 476 CG   
278 1 Y 1 A ARG 476  ? CD   ? B ARG 476 CD   
279 1 Y 1 A ARG 476  ? NE   ? B ARG 476 NE   
280 1 Y 1 A ARG 476  ? CZ   ? B ARG 476 CZ   
281 1 Y 1 A ARG 476  ? NH1  ? B ARG 476 NH1  
282 1 Y 1 A ARG 476  ? NH2  ? B ARG 476 NH2  
283 1 Y 1 A VAL 477  ? CG1  ? B VAL 477 CG1  
284 1 Y 1 A VAL 477  ? CG2  ? B VAL 477 CG2  
285 1 Y 1 A GLN 478  ? CG   ? B GLN 478 CG   
286 1 Y 1 A GLN 478  ? CD   ? B GLN 478 CD   
287 1 Y 1 A GLN 478  ? OE1  ? B GLN 478 OE1  
288 1 Y 1 A GLN 478  ? NE2  ? B GLN 478 NE2  
289 1 Y 1 A ILE 479  ? CG1  ? B ILE 479 CG1  
290 1 Y 1 A ILE 479  ? CG2  ? B ILE 479 CG2  
291 1 Y 1 A ILE 479  ? CD1  ? B ILE 479 CD1  
292 1 Y 1 A LEU 495  ? CG   ? B LEU 495 CG   
293 1 Y 1 A LEU 495  ? CD1  ? B LEU 495 CD1  
294 1 Y 1 A LEU 495  ? CD2  ? B LEU 495 CD2  
295 1 Y 1 A VAL 496  ? CG1  ? B VAL 496 CG1  
296 1 Y 1 A VAL 496  ? CG2  ? B VAL 496 CG2  
297 1 Y 1 A VAL 498  ? CG1  ? B VAL 498 CG1  
298 1 Y 1 A VAL 498  ? CG2  ? B VAL 498 CG2  
299 1 Y 1 A LEU 499  ? CG   ? B LEU 499 CG   
300 1 Y 1 A LEU 499  ? CD1  ? B LEU 499 CD1  
301 1 Y 1 A LEU 499  ? CD2  ? B LEU 499 CD2  
302 1 Y 1 A LEU 500  ? CG   ? B LEU 500 CG   
303 1 Y 1 A LEU 500  ? CD1  ? B LEU 500 CD1  
304 1 Y 1 A LEU 500  ? CD2  ? B LEU 500 CD2  
305 1 Y 1 A ILE 501  ? CG1  ? B ILE 501 CG1  
306 1 Y 1 A ILE 501  ? CG2  ? B ILE 501 CG2  
307 1 Y 1 A ILE 501  ? CD1  ? B ILE 501 CD1  
308 1 Y 1 A THR 502  ? OG1  ? B THR 502 OG1  
309 1 Y 1 A THR 502  ? CG2  ? B THR 502 CG2  
310 1 Y 1 A LYS 504  ? CG   ? B LYS 504 CG   
311 1 Y 1 A LYS 504  ? CD   ? B LYS 504 CD   
312 1 Y 1 A LYS 504  ? CE   ? B LYS 504 CE   
313 1 Y 1 A LYS 504  ? NZ   ? B LYS 504 NZ   
314 1 Y 1 A HIS 505  ? CG   ? B HIS 505 CG   
315 1 Y 1 A HIS 505  ? ND1  ? B HIS 505 ND1  
316 1 Y 1 A HIS 505  ? CD2  ? B HIS 505 CD2  
317 1 Y 1 A HIS 505  ? CE1  ? B HIS 505 CE1  
318 1 Y 1 A HIS 505  ? NE2  ? B HIS 505 NE2  
319 1 Y 1 A ASN 506  ? CG   ? B ASN 506 CG   
320 1 Y 1 A ASN 506  ? OD1  ? B ASN 506 OD1  
321 1 Y 1 A ASN 506  ? ND2  ? B ASN 506 ND2  
322 1 Y 1 A ASP 508  ? CG   ? B ASP 508 CG   
323 1 Y 1 A ASP 508  ? OD1  ? B ASP 508 OD1  
324 1 Y 1 A ASP 508  ? OD2  ? B ASP 508 OD2  
325 1 Y 1 A SER 509  ? OG   ? B SER 509 OG   
326 1 Y 1 A ILE 510  ? CG1  ? B ILE 510 CG1  
327 1 Y 1 A ILE 510  ? CG2  ? B ILE 510 CG2  
328 1 Y 1 A ILE 510  ? CD1  ? B ILE 510 CD1  
329 1 Y 1 A ASP 511  ? CG   ? B ASP 511 CG   
330 1 Y 1 A ASP 511  ? OD1  ? B ASP 511 OD1  
331 1 Y 1 A ASP 511  ? OD2  ? B ASP 511 OD2  
332 1 Y 1 A SER 512  ? OG   ? B SER 512 OG   
333 1 Y 1 A PHE 514  ? CG   ? B PHE 514 CG   
334 1 Y 1 A PHE 514  ? CD1  ? B PHE 514 CD1  
335 1 Y 1 A PHE 514  ? CD2  ? B PHE 514 CD2  
336 1 Y 1 A PHE 514  ? CE1  ? B PHE 514 CE1  
337 1 Y 1 A PHE 514  ? CE2  ? B PHE 514 CE2  
338 1 Y 1 A PHE 514  ? CZ   ? B PHE 514 CZ   
339 1 Y 1 A PHE 515  ? CG   ? B PHE 515 CG   
340 1 Y 1 A PHE 515  ? CD1  ? B PHE 515 CD1  
341 1 Y 1 A PHE 515  ? CD2  ? B PHE 515 CD2  
342 1 Y 1 A PHE 515  ? CE1  ? B PHE 515 CE1  
343 1 Y 1 A PHE 515  ? CE2  ? B PHE 515 CE2  
344 1 Y 1 A PHE 515  ? CZ   ? B PHE 515 CZ   
345 1 Y 1 A TYR 516  ? CG   ? B TYR 516 CG   
346 1 Y 1 A TYR 516  ? CD1  ? B TYR 516 CD1  
347 1 Y 1 A TYR 516  ? CD2  ? B TYR 516 CD2  
348 1 Y 1 A TYR 516  ? CE1  ? B TYR 516 CE1  
349 1 Y 1 A TYR 516  ? CE2  ? B TYR 516 CE2  
350 1 Y 1 A TYR 516  ? CZ   ? B TYR 516 CZ   
351 1 Y 1 A TYR 516  ? OH   ? B TYR 516 OH   
352 1 Y 1 A LYS 518  ? CG   ? B LYS 518 CG   
353 1 Y 1 A LYS 518  ? CD   ? B LYS 518 CD   
354 1 Y 1 A LYS 518  ? CE   ? B LYS 518 CE   
355 1 Y 1 A LYS 518  ? NZ   ? B LYS 518 NZ   
356 1 Y 1 A GLU 519  ? CG   ? B GLU 519 CG   
357 1 Y 1 A GLU 519  ? CD   ? B GLU 519 CD   
358 1 Y 1 A GLU 519  ? OE1  ? B GLU 519 OE1  
359 1 Y 1 A GLU 519  ? OE2  ? B GLU 519 OE2  
360 1 Y 1 A ILE 537  ? CG1  ? B ILE 537 CG1  
361 1 Y 1 A ILE 537  ? CG2  ? B ILE 537 CG2  
362 1 Y 1 A ILE 537  ? CD1  ? B ILE 537 CD1  
363 1 Y 1 A SER 538  ? OG   ? B SER 538 OG   
364 1 Y 1 A LEU 539  ? CG   ? B LEU 539 CG   
365 1 Y 1 A LEU 539  ? CD1  ? B LEU 539 CD1  
366 1 Y 1 A LEU 539  ? CD2  ? B LEU 539 CD2  
367 1 Y 1 A MET 540  ? CG   ? B MET 540 CG   
368 1 Y 1 A MET 540  ? SD   ? B MET 540 SD   
369 1 Y 1 A MET 540  ? CE   ? B MET 540 CE   
370 1 Y 1 A CYS 541  ? SG   ? B CYS 541 SG   
371 1 Y 1 A MET 542  ? CG   ? B MET 542 CG   
372 1 Y 1 A MET 542  ? SD   ? B MET 542 SD   
373 1 Y 1 A MET 542  ? CE   ? B MET 542 CE   
374 1 Y 1 A ASN 543  ? CG   ? B ASN 543 CG   
375 1 Y 1 A ASN 543  ? OD1  ? B ASN 543 OD1  
376 1 Y 1 A ASN 543  ? ND2  ? B ASN 543 ND2  
377 1 Y 1 A GLN 544  ? CG   ? B GLN 544 CG   
378 1 Y 1 A GLN 544  ? CD   ? B GLN 544 CD   
379 1 Y 1 A GLN 544  ? OE1  ? B GLN 544 OE1  
380 1 Y 1 A GLN 544  ? NE2  ? B GLN 544 NE2  
381 1 Y 1 A THR 545  ? OG1  ? B THR 545 OG1  
382 1 Y 1 A THR 545  ? CG2  ? B THR 545 CG2  
383 1 Y 1 A GLN 683  ? CG   ? B GLN 683 CG   
384 1 Y 1 A GLN 683  ? CD   ? B GLN 683 CD   
385 1 Y 1 A GLN 683  ? OE1  ? B GLN 683 OE1  
386 1 Y 1 A GLN 683  ? NE2  ? B GLN 683 NE2  
387 1 Y 1 A GLU 684  ? CG   ? B GLU 684 CG   
388 1 Y 1 A GLU 684  ? CD   ? B GLU 684 CD   
389 1 Y 1 A GLU 684  ? OE1  ? B GLU 684 OE1  
390 1 Y 1 A GLU 684  ? OE2  ? B GLU 684 OE2  
391 1 Y 1 A PRO 685  ? CG   ? B PRO 685 CG   
392 1 Y 1 A PRO 685  ? CD   ? B PRO 685 CD   
393 1 Y 1 A ARG 687  ? CG   ? B ARG 687 CG   
394 1 Y 1 A ARG 687  ? CD   ? B ARG 687 CD   
395 1 Y 1 A ARG 687  ? NE   ? B ARG 687 NE   
396 1 Y 1 A ARG 687  ? CZ   ? B ARG 687 CZ   
397 1 Y 1 A ARG 687  ? NH1  ? B ARG 687 NH1  
398 1 Y 1 A ARG 687  ? NH2  ? B ARG 687 NH2  
399 1 Y 1 A LEU 688  ? CG   ? B LEU 688 CG   
400 1 Y 1 A LEU 688  ? CD1  ? B LEU 688 CD1  
401 1 Y 1 A LEU 688  ? CD2  ? B LEU 688 CD2  
402 1 Y 1 A TYR 689  ? CG   ? B TYR 689 CG   
403 1 Y 1 A TYR 689  ? CD1  ? B TYR 689 CD1  
404 1 Y 1 A TYR 689  ? CD2  ? B TYR 689 CD2  
405 1 Y 1 A TYR 689  ? CE1  ? B TYR 689 CE1  
406 1 Y 1 A TYR 689  ? CE2  ? B TYR 689 CE2  
407 1 Y 1 A TYR 689  ? CZ   ? B TYR 689 CZ   
408 1 Y 1 A TYR 689  ? OH   ? B TYR 689 OH   
409 1 N 1 B POV 1105 ? N    ? G POV 1   N    
410 1 N 1 B POV 1105 ? C11  ? G POV 1   C11  
411 1 N 1 B POV 1105 ? C12  ? G POV 1   C12  
412 1 N 1 B POV 1105 ? C13  ? G POV 1   C13  
413 1 N 1 B POV 1105 ? C213 ? G POV 1   C213 
414 1 N 1 B POV 1105 ? C14  ? G POV 1   C14  
415 1 N 1 B POV 1105 ? C214 ? G POV 1   C214 
416 1 N 1 B POV 1105 ? C15  ? G POV 1   C15  
417 1 N 1 B POV 1105 ? C215 ? G POV 1   C215 
418 1 N 1 B POV 1105 ? C216 ? G POV 1   C216 
419 1 N 1 B POV 1105 ? C217 ? G POV 1   C217 
420 1 N 1 B POV 1105 ? C218 ? G POV 1   C218 
421 1 N 1 A POV 1105 ? N    ? N POV 1   N    
422 1 N 1 A POV 1105 ? C11  ? N POV 1   C11  
423 1 N 1 A POV 1105 ? C12  ? N POV 1   C12  
424 1 N 1 A POV 1105 ? C13  ? N POV 1   C13  
425 1 N 1 A POV 1105 ? C213 ? N POV 1   C213 
426 1 N 1 A POV 1105 ? C14  ? N POV 1   C14  
427 1 N 1 A POV 1105 ? C214 ? N POV 1   C214 
428 1 N 1 A POV 1105 ? C15  ? N POV 1   C15  
429 1 N 1 A POV 1105 ? C215 ? N POV 1   C215 
430 1 N 1 A POV 1105 ? C216 ? N POV 1   C216 
431 1 N 1 A POV 1105 ? C217 ? N POV 1   C217 
432 1 N 1 A POV 1105 ? C218 ? N POV 1   C218 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J40 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9J40 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J40 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9J40 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.009  ? 9254  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.284  ? 12576 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 14.090 ? 1436  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.058  ? 1514  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.011  ? 1488  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9J40 
_struct.title                        'Cryo-EM structure of lysosome cholesterol sencing protein complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9J40 
_struct_keywords.text            'lipid binding protein' 
_struct_keywords.pdbx_keywords   'LIPID BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 2 ? 
H N N 5 ? 
I N N 6 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 2 ? 
N N N 2 ? 
O N N 5 ? 
P N N 6 ? 
# 
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 G1R1S1_NOMLE G1R1S1 ? 1 
;AVNMTKTLPTAVTHGFNSTNDPPSMSITRLFPALLECFGIVLCGYIAGRANVITSTQAKGLGNFVSRFALPALLFKNMVV
LNFSNVDWSFLYSILIAKACVFFTVCVLTLLVASPDSRFSKAGLFPIFATQSNDFALGYPIVEALYQTTYPEYLQYIYLV
APISLMMLNPIGFIFCEIQKWKDTQNASQNKIKIVGLGLLRVLQNPIVFMVFIGIAFNFILDRKVPVYVENFLDGLGNSF
SGSALFYLGLTMMGKIKRLKKSAFVVLILLITAKLLVLPLLCREMVELLDKGDSVVNHTSLSNYAFLYGVFPVAPGVAIF
ATQFNMEVEIITSGMVISTFVSAPIMYVSAWLLTFPTMDPKPLAYAIQNVSFDISIVSLISLIWSLAILLLSKKYKQLPH
MLTTNLLIAQSIVCAGMMIWNFVKEKNFVGQILVFVLLYSSLYSTYLWTGLLAISLFLLKKRERVQIPVGIIIISGWGIP
ALLVGVLLITGKHNGDSIDSAFFYGKEQ
;
15  
2 UNP LYCHS_HUMAN  Q7Z3F1 ? 1 MITTAVTLFCSILIAGISLMCMNQTAQAGSYEGFDQSQSHKVVEPGNTAFEESPAPVNEPELFTSSIPETS 521 
3 UNP G1R1S1_NOMLE G1R1S1 ? 1 
;CCSCSMGNGELHCPSIEPIANTSTSEPVIPSFEKNNHCVSRCNSQSCILAQEEEQYLQSGDQQLTRHVLLCLLLIIGLFA
NLSSCLWWLFNQEPGRLYVELQFFCAVFNFGQGFISFGIFGLDKHLIILPFKRRLEFLWNNKEIAENRDSPVSEEIKMTC
QQFIHYHRDLCIRNIVKERRCGAKTSAGTFCGCDLVNWLIEVGLASDRGEAVIYGDRLVQGGVIQHITNEYEFRDEYLFY
RFLQKSPEQSPPAINANTLQQERYKEIEHSSPPSRSPKT
;
523 
# 
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 9J40 B 13  ? 520 ? G1R1S1 15  ? 522 ? 13  520 
2 2 9J40 B 521 ? 591 ? Q7Z3F1 521 ? 591 ? 521 591 
3 3 9J40 B 592 ? 870 ? G1R1S1 523 ? 801 ? 592 870 
4 1 9J40 A 13  ? 520 ? G1R1S1 15  ? 522 ? 13  520 
5 2 9J40 A 521 ? 591 ? Q7Z3F1 521 ? 591 ? 521 591 
6 3 9J40 A 592 ? 870 ? G1R1S1 523 ? 801 ? 592 870 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9J40 MET B 1   ? UNP G1R1S1 ?   ?   'initiating methionine' 1   1  
1 9J40 ASN B 2   ? UNP G1R1S1 ?   ?   'expression tag'        2   2  
1 9J40 SER B 3   ? UNP G1R1S1 ?   ?   'expression tag'        3   3  
1 9J40 ASN B 4   ? UNP G1R1S1 ?   ?   'expression tag'        4   4  
1 9J40 LEU B 5   ? UNP G1R1S1 ?   ?   'expression tag'        5   5  
1 9J40 PRO B 6   ? UNP G1R1S1 ?   ?   'expression tag'        6   6  
1 9J40 ALA B 7   ? UNP G1R1S1 ?   ?   'expression tag'        7   7  
1 9J40 GLU B 8   ? UNP G1R1S1 ?   ?   'expression tag'        8   8  
1 9J40 ASN B 9   ? UNP G1R1S1 ?   ?   'expression tag'        9   9  
1 9J40 LEU B 10  ? UNP G1R1S1 ?   ?   'expression tag'        10  10 
1 9J40 THR B 11  ? UNP G1R1S1 ?   ?   'expression tag'        11  11 
1 9J40 ILE B 12  ? UNP G1R1S1 ?   ?   'expression tag'        12  12 
1 9J40 SER B 112 ? UNP G1R1S1 CYS 114 conflict                112 13 
1 9J40 ILE B 116 ? UNP G1R1S1 THR 118 conflict                116 14 
1 9J40 VAL B 265 ? UNP G1R1S1 MET 267 conflict                265 15 
3 9J40 ASP B 734 ? UNP G1R1S1 GLU 665 conflict                734 16 
3 9J40 THR B 735 ? UNP G1R1S1 ILE 666 conflict                735 17 
3 9J40 SER B 788 ? UNP G1R1S1 ASN 719 conflict                788 18 
3 9J40 HIS B 866 ? UNP G1R1S1 ARG 797 conflict                866 19 
4 9J40 MET A 1   ? UNP G1R1S1 ?   ?   'initiating methionine' 1   20 
4 9J40 ASN A 2   ? UNP G1R1S1 ?   ?   'expression tag'        2   21 
4 9J40 SER A 3   ? UNP G1R1S1 ?   ?   'expression tag'        3   22 
4 9J40 ASN A 4   ? UNP G1R1S1 ?   ?   'expression tag'        4   23 
4 9J40 LEU A 5   ? UNP G1R1S1 ?   ?   'expression tag'        5   24 
4 9J40 PRO A 6   ? UNP G1R1S1 ?   ?   'expression tag'        6   25 
4 9J40 ALA A 7   ? UNP G1R1S1 ?   ?   'expression tag'        7   26 
4 9J40 GLU A 8   ? UNP G1R1S1 ?   ?   'expression tag'        8   27 
4 9J40 ASN A 9   ? UNP G1R1S1 ?   ?   'expression tag'        9   28 
4 9J40 LEU A 10  ? UNP G1R1S1 ?   ?   'expression tag'        10  29 
4 9J40 THR A 11  ? UNP G1R1S1 ?   ?   'expression tag'        11  30 
4 9J40 ILE A 12  ? UNP G1R1S1 ?   ?   'expression tag'        12  31 
4 9J40 SER A 112 ? UNP G1R1S1 CYS 114 conflict                112 32 
4 9J40 ILE A 116 ? UNP G1R1S1 THR 118 conflict                116 33 
4 9J40 VAL A 265 ? UNP G1R1S1 MET 267 conflict                265 34 
6 9J40 ASP A 734 ? UNP G1R1S1 GLU 665 conflict                734 35 
6 9J40 THR A 735 ? UNP G1R1S1 ILE 666 conflict                735 36 
6 9J40 SER A 788 ? UNP G1R1S1 ASN 719 conflict                788 37 
6 9J40 HIS A 866 ? UNP G1R1S1 ARG 797 conflict                866 38 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 38  ? ARG A 41  ? SER B 38  ARG B 41  5 ? 4  
HELX_P HELX_P2  AA2 LEU A 42  ? ALA A 62  ? LEU B 42  ALA B 62  1 ? 21 
HELX_P HELX_P3  AA3 THR A 66  ? PHE A 80  ? THR B 66  PHE B 80  1 ? 15 
HELX_P HELX_P4  AA4 PHE A 80  ? LEU A 93  ? PHE B 80  LEU B 93  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 99  ? ALA A 125 ? ASP B 99  ALA B 125 1 ? 27 
HELX_P HELX_P6  AA6 ARG A 130 ? ALA A 141 ? ARG B 130 ALA B 141 1 ? 12 
HELX_P HELX_P7  AA7 LEU A 149 ? GLN A 159 ? LEU B 149 GLN B 159 1 ? 11 
HELX_P HELX_P8  AA8 TYR A 162 ? GLN A 167 ? TYR B 162 GLN B 167 5 ? 6  
HELX_P HELX_P9  AA9 TYR A 168 ? THR A 196 ? TYR B 168 THR B 196 1 ? 29 
HELX_P HELX_P10 AB1 ASN A 202 ? GLN A 216 ? ASN B 202 GLN B 216 1 ? 15 
HELX_P HELX_P11 AB2 ILE A 219 ? LEU A 233 ? ILE B 219 LEU B 233 1 ? 15 
HELX_P HELX_P12 AB3 PRO A 238 ? SER A 251 ? PRO B 238 SER B 251 1 ? 14 
HELX_P HELX_P13 AB4 SER A 251 ? MET A 264 ? SER B 251 MET B 264 1 ? 14 
HELX_P HELX_P14 AB5 LYS A 272 ? LEU A 288 ? LYS B 272 LEU B 288 1 ? 17 
HELX_P HELX_P15 AB6 LEU A 288 ? ASP A 302 ? LEU B 288 ASP B 302 1 ? 15 
HELX_P HELX_P16 AB7 SER A 306 ? VAL A 322 ? SER B 306 VAL B 322 1 ? 17 
HELX_P HELX_P17 AB8 PRO A 327 ? ASN A 337 ? PRO B 327 ASN B 337 1 ? 11 
HELX_P HELX_P18 AB9 GLU A 339 ? THR A 366 ? GLU B 339 THR B 366 1 ? 28 
HELX_P HELX_P19 AC1 PRO A 372 ? SER A 404 ? PRO B 372 SER B 404 1 ? 33 
HELX_P HELX_P20 AC2 LYS A 405 ? LYS A 408 ? LYS B 405 LYS B 408 5 ? 4  
HELX_P HELX_P21 AC3 GLN A 409 ? LYS A 436 ? GLN B 409 LYS B 436 1 ? 28 
HELX_P HELX_P22 AC4 ASN A 439 ? LYS A 473 ? ASN B 439 LYS B 473 1 ? 35 
HELX_P HELX_P23 AC5 PRO A 480 ? THR A 502 ? PRO B 480 THR B 502 1 ? 23 
HELX_P HELX_P24 AC6 ASP A 511 ? PHE A 515 ? ASP B 511 PHE B 515 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 517 ? THR A 545 ? GLY B 517 THR B 545 1 ? 29 
HELX_P HELX_P26 AC8 LEU A 655 ? ASN A 682 ? LEU B 655 ASN B 682 1 ? 28 
HELX_P HELX_P27 AC9 LEU A 688 ? GLY A 702 ? LEU B 688 GLY B 702 1 ? 15 
HELX_P HELX_P28 AD1 GLY A 702 ? GLY A 712 ? GLY B 702 GLY B 712 1 ? 11 
HELX_P HELX_P29 AD2 SER B 38  ? ARG B 41  ? SER A 38  ARG A 41  5 ? 4  
HELX_P HELX_P30 AD3 LEU B 42  ? ALA B 62  ? LEU A 42  ALA A 62  1 ? 21 
HELX_P HELX_P31 AD4 THR B 66  ? LEU B 93  ? THR A 66  LEU A 93  1 ? 28 
HELX_P HELX_P32 AD5 ASP B 99  ? ALA B 125 ? ASP A 99  ALA A 125 1 ? 27 
HELX_P HELX_P33 AD6 ARG B 130 ? ALA B 141 ? ARG A 130 ALA A 141 1 ? 12 
HELX_P HELX_P34 AD7 LEU B 149 ? GLN B 159 ? LEU A 149 GLN A 159 1 ? 11 
HELX_P HELX_P35 AD8 TYR B 162 ? GLN B 167 ? TYR A 162 GLN A 167 5 ? 6  
HELX_P HELX_P36 AD9 TYR B 168 ? THR B 196 ? TYR A 168 THR A 196 1 ? 29 
HELX_P HELX_P37 AE1 ASN B 202 ? GLN B 216 ? ASN A 202 GLN A 216 1 ? 15 
HELX_P HELX_P38 AE2 ILE B 219 ? LEU B 233 ? ILE A 219 LEU A 233 1 ? 15 
HELX_P HELX_P39 AE3 PRO B 238 ? SER B 251 ? PRO A 238 SER A 251 1 ? 14 
HELX_P HELX_P40 AE4 SER B 251 ? MET B 264 ? SER A 251 MET A 264 1 ? 14 
HELX_P HELX_P41 AE5 LYS B 272 ? ASP B 302 ? LYS A 272 ASP A 302 1 ? 31 
HELX_P HELX_P42 AE6 SER B 306 ? VAL B 322 ? SER A 306 VAL A 322 1 ? 17 
HELX_P HELX_P43 AE7 PRO B 327 ? ASN B 337 ? PRO A 327 ASN A 337 1 ? 11 
HELX_P HELX_P44 AE8 GLU B 339 ? THR B 366 ? GLU A 339 THR A 366 1 ? 28 
HELX_P HELX_P45 AE9 ASP B 371 ? SER B 404 ? ASP A 371 SER A 404 1 ? 34 
HELX_P HELX_P46 AF1 LYS B 405 ? LYS B 408 ? LYS A 405 LYS A 408 5 ? 4  
HELX_P HELX_P47 AF2 GLN B 409 ? PHE B 434 ? GLN A 409 PHE A 434 1 ? 26 
HELX_P HELX_P48 AF3 ASN B 439 ? LYS B 473 ? ASN A 439 LYS A 473 1 ? 35 
HELX_P HELX_P49 AF4 PRO B 480 ? THR B 502 ? PRO A 480 THR A 502 1 ? 23 
HELX_P HELX_P50 AF5 ASP B 511 ? PHE B 515 ? ASP A 511 PHE A 515 5 ? 5  
HELX_P HELX_P51 AF6 GLY B 517 ? THR B 545 ? GLY A 517 THR A 545 1 ? 29 
HELX_P HELX_P52 AF7 LEU B 655 ? ASN B 682 ? LEU A 655 ASN A 682 1 ? 28 
HELX_P HELX_P53 AF8 LEU B 688 ? GLY B 702 ? LEU A 688 GLY A 702 1 ? 15 
HELX_P HELX_P54 AF9 GLY B 702 ? GLY B 712 ? GLY A 702 GLY A 712 1 ? 11 
# 
_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 
covale1 covale one ? A ASN 309 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 309 B NAG 1106 1_555 ? ? ? ? ? ? ? 1.463 ? N-Glycosylation 
covale2 covale one ? B ASN 309 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 309 A NAG 1106 1_555 ? ? ? ? ? ? ? 1.465 ? N-Glycosylation 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG H . ? ASN A 309 ? NAG B 1106 ? 1_555 ASN B 309 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate 
2 NAG O . ? ASN B 309 ? NAG A 1106 ? 1_555 ASN A 309 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate 
# 
_pdbx_entry_details.entry_id                   9J40 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB B PRO 182 ? ? CG B PRO 182 ? ? 0.895 1.495 -0.600 0.050 N 
2 1 CG B PRO 182 ? ? CD B PRO 182 ? ? 1.224 1.502 -0.278 0.033 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA B PRO 182 ? ? N  B PRO 182 ? ? CD  B PRO 182 ? ? 101.04 111.70 -10.66 1.40 N 
2  1 CA B PRO 182 ? ? CB B PRO 182 ? ? CG  B PRO 182 ? ? 69.66  104.80 -35.14 1.90 N 
3  1 CB B PRO 182 ? ? CG B PRO 182 ? ? CD  B PRO 182 ? ? 154.28 106.50 47.78  3.90 N 
4  1 N  B PRO 182 ? ? CD B PRO 182 ? ? CG  B PRO 182 ? ? 75.81  103.20 -27.39 1.50 N 
5  1 CA B LEU 233 ? ? CB B LEU 233 ? ? CG  B LEU 233 ? ? 131.55 115.30 16.25  2.30 N 
6  1 CB B ASP 234 ? ? CG B ASP 234 ? ? OD1 B ASP 234 ? ? 124.53 118.30 6.23   0.90 N 
7  1 CA B PRO 368 ? ? N  B PRO 368 ? ? CD  B PRO 368 ? ? 103.15 111.70 -8.55  1.40 N 
8  1 CA B LEU 445 ? ? CB B LEU 445 ? ? CG  B LEU 445 ? ? 129.74 115.30 14.44  2.30 N 
9  1 CA A LEU 233 ? ? CB A LEU 233 ? ? CG  A LEU 233 ? ? 131.70 115.30 16.40  2.30 N 
10 1 CB A ASP 234 ? ? CG A ASP 234 ? ? OD1 A ASP 234 ? ? 124.56 118.30 6.26   0.90 N 
11 1 CA A LEU 445 ? ? CB A LEU 445 ? ? CG  A LEU 445 ? ? 129.90 115.30 14.60  2.30 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 ASN B 63  ? ? 82.34   9.82    
2  1 PHE B 95  ? ? -69.96  55.36   
3  1 TYR B 162 ? ? 57.38   76.71   
4  1 GLN B 197 ? ? 66.23   70.04   
5  1 ALA B 199 ? ? -145.25 -154.16 
6  1 PRO B 218 ? ? -63.83  42.01   
7  1 ILE B 219 ? ? -130.41 -46.04  
8  1 LYS B 269 ? ? 61.76   -177.44 
9  1 LEU B 288 ? ? -95.24  -61.32  
10 1 MET B 338 ? ? -149.01 -26.02  
11 1 GLU B 339 ? ? -140.89 37.53   
12 1 MET B 370 ? ? -163.68 -169.06 
13 1 GLN B 409 ? ? -103.19 -169.72 
14 1 LYS B 438 ? ? -124.73 -162.04 
15 1 LYS B 473 ? ? -126.59 -163.76 
16 1 ARG B 474 ? ? 64.60   77.12   
17 1 ARG B 476 ? ? 69.04   -179.56 
18 1 ASP B 511 ? ? -174.84 143.00  
19 1 THR B 656 ? ? -36.21  -35.16  
20 1 ARG B 657 ? ? -103.01 -60.15  
21 1 HIS B 658 ? ? -24.88  -57.61  
22 1 GLN B 683 ? ? 39.25   -139.15 
23 1 PRO B 685 ? ? 63.27   108.65  
24 1 ALA A 62  ? ? -59.76  -9.83   
25 1 ASN A 63  ? ? 81.79   9.51    
26 1 PHE A 95  ? ? -69.92  57.01   
27 1 TYR A 162 ? ? 57.03   76.66   
28 1 GLN A 197 ? ? 66.23   69.47   
29 1 ALA A 199 ? ? -145.11 -154.47 
30 1 PRO A 218 ? ? -63.83  44.60   
31 1 ILE A 219 ? ? -130.44 -46.09  
32 1 LYS A 269 ? ? 61.85   -177.39 
33 1 LEU A 288 ? ? -93.13  -60.19  
34 1 MET A 338 ? ? -148.48 -25.91  
35 1 GLU A 339 ? ? -140.89 38.24   
36 1 MET A 370 ? ? -167.22 -169.91 
37 1 GLN A 409 ? ? -102.43 -166.79 
38 1 LYS A 438 ? ? -124.56 -163.97 
39 1 LYS A 473 ? ? -126.21 -164.50 
40 1 ARG A 474 ? ? 64.69   77.42   
41 1 ARG A 476 ? ? 69.69   -179.77 
42 1 VAL A 477 ? ? 55.01   71.43   
43 1 ASP A 511 ? ? -175.07 143.09  
44 1 THR A 656 ? ? -36.23  -35.12  
45 1 HIS A 658 ? ? -24.87  -57.81  
46 1 GLN A 683 ? ? 39.42   -138.86 
47 1 PRO A 685 ? ? 62.89   108.47  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             PHE 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              147 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -10.79 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9J40 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9J40 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.4 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               295023 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Lysosomal cholesterol signaling protein LYCHOS complexed with IS' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9J40 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1500 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9J40 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9J40 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 MET 1   ? A MET 1   
2   1 Y 1 B ASN 2   ? A ASN 2   
3   1 Y 1 B SER 3   ? A SER 3   
4   1 Y 1 B ASN 4   ? A ASN 4   
5   1 Y 1 B LEU 5   ? A LEU 5   
6   1 Y 1 B PRO 6   ? A PRO 6   
7   1 Y 1 B ALA 7   ? A ALA 7   
8   1 Y 1 B GLU 8   ? A GLU 8   
9   1 Y 1 B ASN 9   ? A ASN 9   
10  1 Y 1 B LEU 10  ? A LEU 10  
11  1 Y 1 B THR 11  ? A THR 11  
12  1 Y 1 B ILE 12  ? A ILE 12  
13  1 Y 1 B ALA 13  ? A ALA 13  
14  1 Y 1 B VAL 14  ? A VAL 14  
15  1 Y 1 B ASN 15  ? A ASN 15  
16  1 Y 1 B MET 16  ? A MET 16  
17  1 Y 1 B THR 17  ? A THR 17  
18  1 Y 1 B LYS 18  ? A LYS 18  
19  1 Y 1 B THR 19  ? A THR 19  
20  1 Y 1 B LEU 20  ? A LEU 20  
21  1 Y 1 B PRO 21  ? A PRO 21  
22  1 Y 1 B THR 22  ? A THR 22  
23  1 Y 1 B ALA 23  ? A ALA 23  
24  1 Y 1 B VAL 24  ? A VAL 24  
25  1 Y 1 B THR 25  ? A THR 25  
26  1 Y 1 B HIS 26  ? A HIS 26  
27  1 Y 1 B GLY 27  ? A GLY 27  
28  1 Y 1 B PHE 28  ? A PHE 28  
29  1 Y 1 B ASN 29  ? A ASN 29  
30  1 Y 1 B SER 30  ? A SER 30  
31  1 Y 1 B THR 31  ? A THR 31  
32  1 Y 1 B ASN 32  ? A ASN 32  
33  1 Y 1 B ASP 33  ? A ASP 33  
34  1 Y 1 B PRO 34  ? A PRO 34  
35  1 Y 1 B PRO 35  ? A PRO 35  
36  1 Y 1 B ALA 546 ? A ALA 546 
37  1 Y 1 B GLN 547 ? A GLN 547 
38  1 Y 1 B ALA 548 ? A ALA 548 
39  1 Y 1 B GLY 549 ? A GLY 549 
40  1 Y 1 B SER 550 ? A SER 550 
41  1 Y 1 B TYR 551 ? A TYR 551 
42  1 Y 1 B GLU 552 ? A GLU 552 
43  1 Y 1 B GLY 553 ? A GLY 553 
44  1 Y 1 B PHE 554 ? A PHE 554 
45  1 Y 1 B ASP 555 ? A ASP 555 
46  1 Y 1 B GLN 556 ? A GLN 556 
47  1 Y 1 B SER 557 ? A SER 557 
48  1 Y 1 B GLN 558 ? A GLN 558 
49  1 Y 1 B SER 559 ? A SER 559 
50  1 Y 1 B HIS 560 ? A HIS 560 
51  1 Y 1 B LYS 561 ? A LYS 561 
52  1 Y 1 B VAL 562 ? A VAL 562 
53  1 Y 1 B VAL 563 ? A VAL 563 
54  1 Y 1 B GLU 564 ? A GLU 564 
55  1 Y 1 B PRO 565 ? A PRO 565 
56  1 Y 1 B GLY 566 ? A GLY 566 
57  1 Y 1 B ASN 567 ? A ASN 567 
58  1 Y 1 B THR 568 ? A THR 568 
59  1 Y 1 B ALA 569 ? A ALA 569 
60  1 Y 1 B PHE 570 ? A PHE 570 
61  1 Y 1 B GLU 571 ? A GLU 571 
62  1 Y 1 B GLU 572 ? A GLU 572 
63  1 Y 1 B SER 573 ? A SER 573 
64  1 Y 1 B PRO 574 ? A PRO 574 
65  1 Y 1 B ALA 575 ? A ALA 575 
66  1 Y 1 B PRO 576 ? A PRO 576 
67  1 Y 1 B VAL 577 ? A VAL 577 
68  1 Y 1 B ASN 578 ? A ASN 578 
69  1 Y 1 B GLU 579 ? A GLU 579 
70  1 Y 1 B PRO 580 ? A PRO 580 
71  1 Y 1 B GLU 581 ? A GLU 581 
72  1 Y 1 B LEU 582 ? A LEU 582 
73  1 Y 1 B PHE 583 ? A PHE 583 
74  1 Y 1 B THR 584 ? A THR 584 
75  1 Y 1 B SER 585 ? A SER 585 
76  1 Y 1 B SER 586 ? A SER 586 
77  1 Y 1 B ILE 587 ? A ILE 587 
78  1 Y 1 B PRO 588 ? A PRO 588 
79  1 Y 1 B GLU 589 ? A GLU 589 
80  1 Y 1 B THR 590 ? A THR 590 
81  1 Y 1 B SER 591 ? A SER 591 
82  1 Y 1 B CYS 592 ? A CYS 592 
83  1 Y 1 B CYS 593 ? A CYS 593 
84  1 Y 1 B SER 594 ? A SER 594 
85  1 Y 1 B CYS 595 ? A CYS 595 
86  1 Y 1 B SER 596 ? A SER 596 
87  1 Y 1 B MET 597 ? A MET 597 
88  1 Y 1 B GLY 598 ? A GLY 598 
89  1 Y 1 B ASN 599 ? A ASN 599 
90  1 Y 1 B GLY 600 ? A GLY 600 
91  1 Y 1 B GLU 601 ? A GLU 601 
92  1 Y 1 B LEU 602 ? A LEU 602 
93  1 Y 1 B HIS 603 ? A HIS 603 
94  1 Y 1 B CYS 604 ? A CYS 604 
95  1 Y 1 B PRO 605 ? A PRO 605 
96  1 Y 1 B SER 606 ? A SER 606 
97  1 Y 1 B ILE 607 ? A ILE 607 
98  1 Y 1 B GLU 608 ? A GLU 608 
99  1 Y 1 B PRO 609 ? A PRO 609 
100 1 Y 1 B ILE 610 ? A ILE 610 
101 1 Y 1 B ALA 611 ? A ALA 611 
102 1 Y 1 B ASN 612 ? A ASN 612 
103 1 Y 1 B THR 613 ? A THR 613 
104 1 Y 1 B SER 614 ? A SER 614 
105 1 Y 1 B THR 615 ? A THR 615 
106 1 Y 1 B SER 616 ? A SER 616 
107 1 Y 1 B GLU 617 ? A GLU 617 
108 1 Y 1 B PRO 618 ? A PRO 618 
109 1 Y 1 B VAL 619 ? A VAL 619 
110 1 Y 1 B ILE 620 ? A ILE 620 
111 1 Y 1 B PRO 621 ? A PRO 621 
112 1 Y 1 B SER 622 ? A SER 622 
113 1 Y 1 B PHE 623 ? A PHE 623 
114 1 Y 1 B GLU 624 ? A GLU 624 
115 1 Y 1 B LYS 625 ? A LYS 625 
116 1 Y 1 B ASN 626 ? A ASN 626 
117 1 Y 1 B ASN 627 ? A ASN 627 
118 1 Y 1 B HIS 628 ? A HIS 628 
119 1 Y 1 B CYS 629 ? A CYS 629 
120 1 Y 1 B VAL 630 ? A VAL 630 
121 1 Y 1 B SER 631 ? A SER 631 
122 1 Y 1 B ARG 632 ? A ARG 632 
123 1 Y 1 B CYS 633 ? A CYS 633 
124 1 Y 1 B ASN 634 ? A ASN 634 
125 1 Y 1 B SER 635 ? A SER 635 
126 1 Y 1 B GLN 636 ? A GLN 636 
127 1 Y 1 B SER 637 ? A SER 637 
128 1 Y 1 B CYS 638 ? A CYS 638 
129 1 Y 1 B ILE 639 ? A ILE 639 
130 1 Y 1 B LEU 640 ? A LEU 640 
131 1 Y 1 B ALA 641 ? A ALA 641 
132 1 Y 1 B GLN 642 ? A GLN 642 
133 1 Y 1 B GLU 643 ? A GLU 643 
134 1 Y 1 B GLU 644 ? A GLU 644 
135 1 Y 1 B GLU 645 ? A GLU 645 
136 1 Y 1 B GLN 646 ? A GLN 646 
137 1 Y 1 B TYR 647 ? A TYR 647 
138 1 Y 1 B LEU 648 ? A LEU 648 
139 1 Y 1 B GLN 649 ? A GLN 649 
140 1 Y 1 B SER 650 ? A SER 650 
141 1 Y 1 B GLY 651 ? A GLY 651 
142 1 Y 1 B ASP 652 ? A ASP 652 
143 1 Y 1 B GLN 653 ? A GLN 653 
144 1 Y 1 B ILE 719 ? A ILE 719 
145 1 Y 1 B LEU 720 ? A LEU 720 
146 1 Y 1 B PRO 721 ? A PRO 721 
147 1 Y 1 B PHE 722 ? A PHE 722 
148 1 Y 1 B LYS 723 ? A LYS 723 
149 1 Y 1 B ARG 724 ? A ARG 724 
150 1 Y 1 B ARG 725 ? A ARG 725 
151 1 Y 1 B LEU 726 ? A LEU 726 
152 1 Y 1 B GLU 727 ? A GLU 727 
153 1 Y 1 B PHE 728 ? A PHE 728 
154 1 Y 1 B LEU 729 ? A LEU 729 
155 1 Y 1 B TRP 730 ? A TRP 730 
156 1 Y 1 B ASN 731 ? A ASN 731 
157 1 Y 1 B ASN 732 ? A ASN 732 
158 1 Y 1 B LYS 733 ? A LYS 733 
159 1 Y 1 B ASP 734 ? A ASP 734 
160 1 Y 1 B THR 735 ? A THR 735 
161 1 Y 1 B ALA 736 ? A ALA 736 
162 1 Y 1 B GLU 737 ? A GLU 737 
163 1 Y 1 B ASN 738 ? A ASN 738 
164 1 Y 1 B ARG 739 ? A ARG 739 
165 1 Y 1 B ASP 740 ? A ASP 740 
166 1 Y 1 B SER 741 ? A SER 741 
167 1 Y 1 B PRO 742 ? A PRO 742 
168 1 Y 1 B VAL 743 ? A VAL 743 
169 1 Y 1 B SER 744 ? A SER 744 
170 1 Y 1 B GLU 745 ? A GLU 745 
171 1 Y 1 B GLU 746 ? A GLU 746 
172 1 Y 1 B ILE 747 ? A ILE 747 
173 1 Y 1 B LYS 748 ? A LYS 748 
174 1 Y 1 B MET 749 ? A MET 749 
175 1 Y 1 B THR 750 ? A THR 750 
176 1 Y 1 B CYS 751 ? A CYS 751 
177 1 Y 1 B GLN 752 ? A GLN 752 
178 1 Y 1 B GLN 753 ? A GLN 753 
179 1 Y 1 B PHE 754 ? A PHE 754 
180 1 Y 1 B ILE 755 ? A ILE 755 
181 1 Y 1 B HIS 756 ? A HIS 756 
182 1 Y 1 B TYR 757 ? A TYR 757 
183 1 Y 1 B HIS 758 ? A HIS 758 
184 1 Y 1 B ARG 759 ? A ARG 759 
185 1 Y 1 B ASP 760 ? A ASP 760 
186 1 Y 1 B LEU 761 ? A LEU 761 
187 1 Y 1 B CYS 762 ? A CYS 762 
188 1 Y 1 B ILE 763 ? A ILE 763 
189 1 Y 1 B ARG 764 ? A ARG 764 
190 1 Y 1 B ASN 765 ? A ASN 765 
191 1 Y 1 B ILE 766 ? A ILE 766 
192 1 Y 1 B VAL 767 ? A VAL 767 
193 1 Y 1 B LYS 768 ? A LYS 768 
194 1 Y 1 B GLU 769 ? A GLU 769 
195 1 Y 1 B ARG 770 ? A ARG 770 
196 1 Y 1 B ARG 771 ? A ARG 771 
197 1 Y 1 B CYS 772 ? A CYS 772 
198 1 Y 1 B GLY 773 ? A GLY 773 
199 1 Y 1 B ALA 774 ? A ALA 774 
200 1 Y 1 B LYS 775 ? A LYS 775 
201 1 Y 1 B THR 776 ? A THR 776 
202 1 Y 1 B SER 777 ? A SER 777 
203 1 Y 1 B ALA 778 ? A ALA 778 
204 1 Y 1 B GLY 779 ? A GLY 779 
205 1 Y 1 B THR 780 ? A THR 780 
206 1 Y 1 B PHE 781 ? A PHE 781 
207 1 Y 1 B CYS 782 ? A CYS 782 
208 1 Y 1 B GLY 783 ? A GLY 783 
209 1 Y 1 B CYS 784 ? A CYS 784 
210 1 Y 1 B ASP 785 ? A ASP 785 
211 1 Y 1 B LEU 786 ? A LEU 786 
212 1 Y 1 B VAL 787 ? A VAL 787 
213 1 Y 1 B SER 788 ? A SER 788 
214 1 Y 1 B TRP 789 ? A TRP 789 
215 1 Y 1 B LEU 790 ? A LEU 790 
216 1 Y 1 B ILE 791 ? A ILE 791 
217 1 Y 1 B GLU 792 ? A GLU 792 
218 1 Y 1 B VAL 793 ? A VAL 793 
219 1 Y 1 B GLY 794 ? A GLY 794 
220 1 Y 1 B LEU 795 ? A LEU 795 
221 1 Y 1 B ALA 796 ? A ALA 796 
222 1 Y 1 B SER 797 ? A SER 797 
223 1 Y 1 B ASP 798 ? A ASP 798 
224 1 Y 1 B ARG 799 ? A ARG 799 
225 1 Y 1 B GLY 800 ? A GLY 800 
226 1 Y 1 B GLU 801 ? A GLU 801 
227 1 Y 1 B ALA 802 ? A ALA 802 
228 1 Y 1 B VAL 803 ? A VAL 803 
229 1 Y 1 B ILE 804 ? A ILE 804 
230 1 Y 1 B TYR 805 ? A TYR 805 
231 1 Y 1 B GLY 806 ? A GLY 806 
232 1 Y 1 B ASP 807 ? A ASP 807 
233 1 Y 1 B ARG 808 ? A ARG 808 
234 1 Y 1 B LEU 809 ? A LEU 809 
235 1 Y 1 B VAL 810 ? A VAL 810 
236 1 Y 1 B GLN 811 ? A GLN 811 
237 1 Y 1 B GLY 812 ? A GLY 812 
238 1 Y 1 B GLY 813 ? A GLY 813 
239 1 Y 1 B VAL 814 ? A VAL 814 
240 1 Y 1 B ILE 815 ? A ILE 815 
241 1 Y 1 B GLN 816 ? A GLN 816 
242 1 Y 1 B HIS 817 ? A HIS 817 
243 1 Y 1 B ILE 818 ? A ILE 818 
244 1 Y 1 B THR 819 ? A THR 819 
245 1 Y 1 B ASN 820 ? A ASN 820 
246 1 Y 1 B GLU 821 ? A GLU 821 
247 1 Y 1 B TYR 822 ? A TYR 822 
248 1 Y 1 B GLU 823 ? A GLU 823 
249 1 Y 1 B PHE 824 ? A PHE 824 
250 1 Y 1 B ARG 825 ? A ARG 825 
251 1 Y 1 B ASP 826 ? A ASP 826 
252 1 Y 1 B GLU 827 ? A GLU 827 
253 1 Y 1 B TYR 828 ? A TYR 828 
254 1 Y 1 B LEU 829 ? A LEU 829 
255 1 Y 1 B PHE 830 ? A PHE 830 
256 1 Y 1 B TYR 831 ? A TYR 831 
257 1 Y 1 B ARG 832 ? A ARG 832 
258 1 Y 1 B PHE 833 ? A PHE 833 
259 1 Y 1 B LEU 834 ? A LEU 834 
260 1 Y 1 B GLN 835 ? A GLN 835 
261 1 Y 1 B LYS 836 ? A LYS 836 
262 1 Y 1 B SER 837 ? A SER 837 
263 1 Y 1 B PRO 838 ? A PRO 838 
264 1 Y 1 B GLU 839 ? A GLU 839 
265 1 Y 1 B GLN 840 ? A GLN 840 
266 1 Y 1 B SER 841 ? A SER 841 
267 1 Y 1 B PRO 842 ? A PRO 842 
268 1 Y 1 B PRO 843 ? A PRO 843 
269 1 Y 1 B ALA 844 ? A ALA 844 
270 1 Y 1 B ILE 845 ? A ILE 845 
271 1 Y 1 B ASN 846 ? A ASN 846 
272 1 Y 1 B ALA 847 ? A ALA 847 
273 1 Y 1 B ASN 848 ? A ASN 848 
274 1 Y 1 B THR 849 ? A THR 849 
275 1 Y 1 B LEU 850 ? A LEU 850 
276 1 Y 1 B GLN 851 ? A GLN 851 
277 1 Y 1 B GLN 852 ? A GLN 852 
278 1 Y 1 B GLU 853 ? A GLU 853 
279 1 Y 1 B ARG 854 ? A ARG 854 
280 1 Y 1 B TYR 855 ? A TYR 855 
281 1 Y 1 B LYS 856 ? A LYS 856 
282 1 Y 1 B GLU 857 ? A GLU 857 
283 1 Y 1 B ILE 858 ? A ILE 858 
284 1 Y 1 B GLU 859 ? A GLU 859 
285 1 Y 1 B HIS 860 ? A HIS 860 
286 1 Y 1 B SER 861 ? A SER 861 
287 1 Y 1 B SER 862 ? A SER 862 
288 1 Y 1 B PRO 863 ? A PRO 863 
289 1 Y 1 B PRO 864 ? A PRO 864 
290 1 Y 1 B SER 865 ? A SER 865 
291 1 Y 1 B HIS 866 ? A HIS 866 
292 1 Y 1 B SER 867 ? A SER 867 
293 1 Y 1 B PRO 868 ? A PRO 868 
294 1 Y 1 B LYS 869 ? A LYS 869 
295 1 Y 1 B THR 870 ? A THR 870 
296 1 Y 1 A MET 1   ? B MET 1   
297 1 Y 1 A ASN 2   ? B ASN 2   
298 1 Y 1 A SER 3   ? B SER 3   
299 1 Y 1 A ASN 4   ? B ASN 4   
300 1 Y 1 A LEU 5   ? B LEU 5   
301 1 Y 1 A PRO 6   ? B PRO 6   
302 1 Y 1 A ALA 7   ? B ALA 7   
303 1 Y 1 A GLU 8   ? B GLU 8   
304 1 Y 1 A ASN 9   ? B ASN 9   
305 1 Y 1 A LEU 10  ? B LEU 10  
306 1 Y 1 A THR 11  ? B THR 11  
307 1 Y 1 A ILE 12  ? B ILE 12  
308 1 Y 1 A ALA 13  ? B ALA 13  
309 1 Y 1 A VAL 14  ? B VAL 14  
310 1 Y 1 A ASN 15  ? B ASN 15  
311 1 Y 1 A MET 16  ? B MET 16  
312 1 Y 1 A THR 17  ? B THR 17  
313 1 Y 1 A LYS 18  ? B LYS 18  
314 1 Y 1 A THR 19  ? B THR 19  
315 1 Y 1 A LEU 20  ? B LEU 20  
316 1 Y 1 A PRO 21  ? B PRO 21  
317 1 Y 1 A THR 22  ? B THR 22  
318 1 Y 1 A ALA 23  ? B ALA 23  
319 1 Y 1 A VAL 24  ? B VAL 24  
320 1 Y 1 A THR 25  ? B THR 25  
321 1 Y 1 A HIS 26  ? B HIS 26  
322 1 Y 1 A GLY 27  ? B GLY 27  
323 1 Y 1 A PHE 28  ? B PHE 28  
324 1 Y 1 A ASN 29  ? B ASN 29  
325 1 Y 1 A SER 30  ? B SER 30  
326 1 Y 1 A THR 31  ? B THR 31  
327 1 Y 1 A ASN 32  ? B ASN 32  
328 1 Y 1 A ASP 33  ? B ASP 33  
329 1 Y 1 A PRO 34  ? B PRO 34  
330 1 Y 1 A PRO 35  ? B PRO 35  
331 1 Y 1 A ALA 546 ? B ALA 546 
332 1 Y 1 A GLN 547 ? B GLN 547 
333 1 Y 1 A ALA 548 ? B ALA 548 
334 1 Y 1 A GLY 549 ? B GLY 549 
335 1 Y 1 A SER 550 ? B SER 550 
336 1 Y 1 A TYR 551 ? B TYR 551 
337 1 Y 1 A GLU 552 ? B GLU 552 
338 1 Y 1 A GLY 553 ? B GLY 553 
339 1 Y 1 A PHE 554 ? B PHE 554 
340 1 Y 1 A ASP 555 ? B ASP 555 
341 1 Y 1 A GLN 556 ? B GLN 556 
342 1 Y 1 A SER 557 ? B SER 557 
343 1 Y 1 A GLN 558 ? B GLN 558 
344 1 Y 1 A SER 559 ? B SER 559 
345 1 Y 1 A HIS 560 ? B HIS 560 
346 1 Y 1 A LYS 561 ? B LYS 561 
347 1 Y 1 A VAL 562 ? B VAL 562 
348 1 Y 1 A VAL 563 ? B VAL 563 
349 1 Y 1 A GLU 564 ? B GLU 564 
350 1 Y 1 A PRO 565 ? B PRO 565 
351 1 Y 1 A GLY 566 ? B GLY 566 
352 1 Y 1 A ASN 567 ? B ASN 567 
353 1 Y 1 A THR 568 ? B THR 568 
354 1 Y 1 A ALA 569 ? B ALA 569 
355 1 Y 1 A PHE 570 ? B PHE 570 
356 1 Y 1 A GLU 571 ? B GLU 571 
357 1 Y 1 A GLU 572 ? B GLU 572 
358 1 Y 1 A SER 573 ? B SER 573 
359 1 Y 1 A PRO 574 ? B PRO 574 
360 1 Y 1 A ALA 575 ? B ALA 575 
361 1 Y 1 A PRO 576 ? B PRO 576 
362 1 Y 1 A VAL 577 ? B VAL 577 
363 1 Y 1 A ASN 578 ? B ASN 578 
364 1 Y 1 A GLU 579 ? B GLU 579 
365 1 Y 1 A PRO 580 ? B PRO 580 
366 1 Y 1 A GLU 581 ? B GLU 581 
367 1 Y 1 A LEU 582 ? B LEU 582 
368 1 Y 1 A PHE 583 ? B PHE 583 
369 1 Y 1 A THR 584 ? B THR 584 
370 1 Y 1 A SER 585 ? B SER 585 
371 1 Y 1 A SER 586 ? B SER 586 
372 1 Y 1 A ILE 587 ? B ILE 587 
373 1 Y 1 A PRO 588 ? B PRO 588 
374 1 Y 1 A GLU 589 ? B GLU 589 
375 1 Y 1 A THR 590 ? B THR 590 
376 1 Y 1 A SER 591 ? B SER 591 
377 1 Y 1 A CYS 592 ? B CYS 592 
378 1 Y 1 A CYS 593 ? B CYS 593 
379 1 Y 1 A SER 594 ? B SER 594 
380 1 Y 1 A CYS 595 ? B CYS 595 
381 1 Y 1 A SER 596 ? B SER 596 
382 1 Y 1 A MET 597 ? B MET 597 
383 1 Y 1 A GLY 598 ? B GLY 598 
384 1 Y 1 A ASN 599 ? B ASN 599 
385 1 Y 1 A GLY 600 ? B GLY 600 
386 1 Y 1 A GLU 601 ? B GLU 601 
387 1 Y 1 A LEU 602 ? B LEU 602 
388 1 Y 1 A HIS 603 ? B HIS 603 
389 1 Y 1 A CYS 604 ? B CYS 604 
390 1 Y 1 A PRO 605 ? B PRO 605 
391 1 Y 1 A SER 606 ? B SER 606 
392 1 Y 1 A ILE 607 ? B ILE 607 
393 1 Y 1 A GLU 608 ? B GLU 608 
394 1 Y 1 A PRO 609 ? B PRO 609 
395 1 Y 1 A ILE 610 ? B ILE 610 
396 1 Y 1 A ALA 611 ? B ALA 611 
397 1 Y 1 A ASN 612 ? B ASN 612 
398 1 Y 1 A THR 613 ? B THR 613 
399 1 Y 1 A SER 614 ? B SER 614 
400 1 Y 1 A THR 615 ? B THR 615 
401 1 Y 1 A SER 616 ? B SER 616 
402 1 Y 1 A GLU 617 ? B GLU 617 
403 1 Y 1 A PRO 618 ? B PRO 618 
404 1 Y 1 A VAL 619 ? B VAL 619 
405 1 Y 1 A ILE 620 ? B ILE 620 
406 1 Y 1 A PRO 621 ? B PRO 621 
407 1 Y 1 A SER 622 ? B SER 622 
408 1 Y 1 A PHE 623 ? B PHE 623 
409 1 Y 1 A GLU 624 ? B GLU 624 
410 1 Y 1 A LYS 625 ? B LYS 625 
411 1 Y 1 A ASN 626 ? B ASN 626 
412 1 Y 1 A ASN 627 ? B ASN 627 
413 1 Y 1 A HIS 628 ? B HIS 628 
414 1 Y 1 A CYS 629 ? B CYS 629 
415 1 Y 1 A VAL 630 ? B VAL 630 
416 1 Y 1 A SER 631 ? B SER 631 
417 1 Y 1 A ARG 632 ? B ARG 632 
418 1 Y 1 A CYS 633 ? B CYS 633 
419 1 Y 1 A ASN 634 ? B ASN 634 
420 1 Y 1 A SER 635 ? B SER 635 
421 1 Y 1 A GLN 636 ? B GLN 636 
422 1 Y 1 A SER 637 ? B SER 637 
423 1 Y 1 A CYS 638 ? B CYS 638 
424 1 Y 1 A ILE 639 ? B ILE 639 
425 1 Y 1 A LEU 640 ? B LEU 640 
426 1 Y 1 A ALA 641 ? B ALA 641 
427 1 Y 1 A GLN 642 ? B GLN 642 
428 1 Y 1 A GLU 643 ? B GLU 643 
429 1 Y 1 A GLU 644 ? B GLU 644 
430 1 Y 1 A GLU 645 ? B GLU 645 
431 1 Y 1 A GLN 646 ? B GLN 646 
432 1 Y 1 A TYR 647 ? B TYR 647 
433 1 Y 1 A LEU 648 ? B LEU 648 
434 1 Y 1 A GLN 649 ? B GLN 649 
435 1 Y 1 A SER 650 ? B SER 650 
436 1 Y 1 A GLY 651 ? B GLY 651 
437 1 Y 1 A ASP 652 ? B ASP 652 
438 1 Y 1 A GLN 653 ? B GLN 653 
439 1 Y 1 A ILE 719 ? B ILE 719 
440 1 Y 1 A LEU 720 ? B LEU 720 
441 1 Y 1 A PRO 721 ? B PRO 721 
442 1 Y 1 A PHE 722 ? B PHE 722 
443 1 Y 1 A LYS 723 ? B LYS 723 
444 1 Y 1 A ARG 724 ? B ARG 724 
445 1 Y 1 A ARG 725 ? B ARG 725 
446 1 Y 1 A LEU 726 ? B LEU 726 
447 1 Y 1 A GLU 727 ? B GLU 727 
448 1 Y 1 A PHE 728 ? B PHE 728 
449 1 Y 1 A LEU 729 ? B LEU 729 
450 1 Y 1 A TRP 730 ? B TRP 730 
451 1 Y 1 A ASN 731 ? B ASN 731 
452 1 Y 1 A ASN 732 ? B ASN 732 
453 1 Y 1 A LYS 733 ? B LYS 733 
454 1 Y 1 A ASP 734 ? B ASP 734 
455 1 Y 1 A THR 735 ? B THR 735 
456 1 Y 1 A ALA 736 ? B ALA 736 
457 1 Y 1 A GLU 737 ? B GLU 737 
458 1 Y 1 A ASN 738 ? B ASN 738 
459 1 Y 1 A ARG 739 ? B ARG 739 
460 1 Y 1 A ASP 740 ? B ASP 740 
461 1 Y 1 A SER 741 ? B SER 741 
462 1 Y 1 A PRO 742 ? B PRO 742 
463 1 Y 1 A VAL 743 ? B VAL 743 
464 1 Y 1 A SER 744 ? B SER 744 
465 1 Y 1 A GLU 745 ? B GLU 745 
466 1 Y 1 A GLU 746 ? B GLU 746 
467 1 Y 1 A ILE 747 ? B ILE 747 
468 1 Y 1 A LYS 748 ? B LYS 748 
469 1 Y 1 A MET 749 ? B MET 749 
470 1 Y 1 A THR 750 ? B THR 750 
471 1 Y 1 A CYS 751 ? B CYS 751 
472 1 Y 1 A GLN 752 ? B GLN 752 
473 1 Y 1 A GLN 753 ? B GLN 753 
474 1 Y 1 A PHE 754 ? B PHE 754 
475 1 Y 1 A ILE 755 ? B ILE 755 
476 1 Y 1 A HIS 756 ? B HIS 756 
477 1 Y 1 A TYR 757 ? B TYR 757 
478 1 Y 1 A HIS 758 ? B HIS 758 
479 1 Y 1 A ARG 759 ? B ARG 759 
480 1 Y 1 A ASP 760 ? B ASP 760 
481 1 Y 1 A LEU 761 ? B LEU 761 
482 1 Y 1 A CYS 762 ? B CYS 762 
483 1 Y 1 A ILE 763 ? B ILE 763 
484 1 Y 1 A ARG 764 ? B ARG 764 
485 1 Y 1 A ASN 765 ? B ASN 765 
486 1 Y 1 A ILE 766 ? B ILE 766 
487 1 Y 1 A VAL 767 ? B VAL 767 
488 1 Y 1 A LYS 768 ? B LYS 768 
489 1 Y 1 A GLU 769 ? B GLU 769 
490 1 Y 1 A ARG 770 ? B ARG 770 
491 1 Y 1 A ARG 771 ? B ARG 771 
492 1 Y 1 A CYS 772 ? B CYS 772 
493 1 Y 1 A GLY 773 ? B GLY 773 
494 1 Y 1 A ALA 774 ? B ALA 774 
495 1 Y 1 A LYS 775 ? B LYS 775 
496 1 Y 1 A THR 776 ? B THR 776 
497 1 Y 1 A SER 777 ? B SER 777 
498 1 Y 1 A ALA 778 ? B ALA 778 
499 1 Y 1 A GLY 779 ? B GLY 779 
500 1 Y 1 A THR 780 ? B THR 780 
501 1 Y 1 A PHE 781 ? B PHE 781 
502 1 Y 1 A CYS 782 ? B CYS 782 
503 1 Y 1 A GLY 783 ? B GLY 783 
504 1 Y 1 A CYS 784 ? B CYS 784 
505 1 Y 1 A ASP 785 ? B ASP 785 
506 1 Y 1 A LEU 786 ? B LEU 786 
507 1 Y 1 A VAL 787 ? B VAL 787 
508 1 Y 1 A SER 788 ? B SER 788 
509 1 Y 1 A TRP 789 ? B TRP 789 
510 1 Y 1 A LEU 790 ? B LEU 790 
511 1 Y 1 A ILE 791 ? B ILE 791 
512 1 Y 1 A GLU 792 ? B GLU 792 
513 1 Y 1 A VAL 793 ? B VAL 793 
514 1 Y 1 A GLY 794 ? B GLY 794 
515 1 Y 1 A LEU 795 ? B LEU 795 
516 1 Y 1 A ALA 796 ? B ALA 796 
517 1 Y 1 A SER 797 ? B SER 797 
518 1 Y 1 A ASP 798 ? B ASP 798 
519 1 Y 1 A ARG 799 ? B ARG 799 
520 1 Y 1 A GLY 800 ? B GLY 800 
521 1 Y 1 A GLU 801 ? B GLU 801 
522 1 Y 1 A ALA 802 ? B ALA 802 
523 1 Y 1 A VAL 803 ? B VAL 803 
524 1 Y 1 A ILE 804 ? B ILE 804 
525 1 Y 1 A TYR 805 ? B TYR 805 
526 1 Y 1 A GLY 806 ? B GLY 806 
527 1 Y 1 A ASP 807 ? B ASP 807 
528 1 Y 1 A ARG 808 ? B ARG 808 
529 1 Y 1 A LEU 809 ? B LEU 809 
530 1 Y 1 A VAL 810 ? B VAL 810 
531 1 Y 1 A GLN 811 ? B GLN 811 
532 1 Y 1 A GLY 812 ? B GLY 812 
533 1 Y 1 A GLY 813 ? B GLY 813 
534 1 Y 1 A VAL 814 ? B VAL 814 
535 1 Y 1 A ILE 815 ? B ILE 815 
536 1 Y 1 A GLN 816 ? B GLN 816 
537 1 Y 1 A HIS 817 ? B HIS 817 
538 1 Y 1 A ILE 818 ? B ILE 818 
539 1 Y 1 A THR 819 ? B THR 819 
540 1 Y 1 A ASN 820 ? B ASN 820 
541 1 Y 1 A GLU 821 ? B GLU 821 
542 1 Y 1 A TYR 822 ? B TYR 822 
543 1 Y 1 A GLU 823 ? B GLU 823 
544 1 Y 1 A PHE 824 ? B PHE 824 
545 1 Y 1 A ARG 825 ? B ARG 825 
546 1 Y 1 A ASP 826 ? B ASP 826 
547 1 Y 1 A GLU 827 ? B GLU 827 
548 1 Y 1 A TYR 828 ? B TYR 828 
549 1 Y 1 A LEU 829 ? B LEU 829 
550 1 Y 1 A PHE 830 ? B PHE 830 
551 1 Y 1 A TYR 831 ? B TYR 831 
552 1 Y 1 A ARG 832 ? B ARG 832 
553 1 Y 1 A PHE 833 ? B PHE 833 
554 1 Y 1 A LEU 834 ? B LEU 834 
555 1 Y 1 A GLN 835 ? B GLN 835 
556 1 Y 1 A LYS 836 ? B LYS 836 
557 1 Y 1 A SER 837 ? B SER 837 
558 1 Y 1 A PRO 838 ? B PRO 838 
559 1 Y 1 A GLU 839 ? B GLU 839 
560 1 Y 1 A GLN 840 ? B GLN 840 
561 1 Y 1 A SER 841 ? B SER 841 
562 1 Y 1 A PRO 842 ? B PRO 842 
563 1 Y 1 A PRO 843 ? B PRO 843 
564 1 Y 1 A ALA 844 ? B ALA 844 
565 1 Y 1 A ILE 845 ? B ILE 845 
566 1 Y 1 A ASN 846 ? B ASN 846 
567 1 Y 1 A ALA 847 ? B ALA 847 
568 1 Y 1 A ASN 848 ? B ASN 848 
569 1 Y 1 A THR 849 ? B THR 849 
570 1 Y 1 A LEU 850 ? B LEU 850 
571 1 Y 1 A GLN 851 ? B GLN 851 
572 1 Y 1 A GLN 852 ? B GLN 852 
573 1 Y 1 A GLU 853 ? B GLU 853 
574 1 Y 1 A ARG 854 ? B ARG 854 
575 1 Y 1 A TYR 855 ? B TYR 855 
576 1 Y 1 A LYS 856 ? B LYS 856 
577 1 Y 1 A GLU 857 ? B GLU 857 
578 1 Y 1 A ILE 858 ? B ILE 858 
579 1 Y 1 A GLU 859 ? B GLU 859 
580 1 Y 1 A HIS 860 ? B HIS 860 
581 1 Y 1 A SER 861 ? B SER 861 
582 1 Y 1 A SER 862 ? B SER 862 
583 1 Y 1 A PRO 863 ? B PRO 863 
584 1 Y 1 A PRO 864 ? B PRO 864 
585 1 Y 1 A SER 865 ? B SER 865 
586 1 Y 1 A HIS 866 ? B HIS 866 
587 1 Y 1 A SER 867 ? B SER 867 
588 1 Y 1 A PRO 868 ? B PRO 868 
589 1 Y 1 A LYS 869 ? B LYS 869 
590 1 Y 1 A THR 870 ? B THR 870 
# 
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  
CLR C1   C N N 74  
CLR C2   C N N 75  
CLR C3   C N S 76  
CLR C4   C N N 77  
CLR C5   C N N 78  
CLR C6   C N N 79  
CLR C7   C N N 80  
CLR C8   C N S 81  
CLR C9   C N S 82  
CLR C10  C N R 83  
CLR C11  C N N 84  
CLR C12  C N N 85  
CLR C13  C N R 86  
CLR C14  C N S 87  
CLR C15  C N N 88  
CLR C16  C N N 89  
CLR C17  C N R 90  
CLR C18  C N N 91  
CLR C19  C N N 92  
CLR C20  C N R 93  
CLR C21  C N N 94  
CLR C22  C N N 95  
CLR C23  C N N 96  
CLR C24  C N N 97  
CLR C25  C N N 98  
CLR C26  C N N 99  
CLR C27  C N N 100 
CLR O1   O N N 101 
CLR H11  H N N 102 
CLR H12  H N N 103 
CLR H21  H N N 104 
CLR H22  H N N 105 
CLR H3   H N N 106 
CLR H41  H N N 107 
CLR H42  H N N 108 
CLR H6   H N N 109 
CLR H71  H N N 110 
CLR H72  H N N 111 
CLR H8   H N N 112 
CLR H9   H N N 113 
CLR H111 H N N 114 
CLR H112 H N N 115 
CLR H121 H N N 116 
CLR H122 H N N 117 
CLR H14  H N N 118 
CLR H151 H N N 119 
CLR H152 H N N 120 
CLR H161 H N N 121 
CLR H162 H N N 122 
CLR H17  H N N 123 
CLR H181 H N N 124 
CLR H182 H N N 125 
CLR H183 H N N 126 
CLR H191 H N N 127 
CLR H192 H N N 128 
CLR H193 H N N 129 
CLR H20  H N N 130 
CLR H211 H N N 131 
CLR H212 H N N 132 
CLR H213 H N N 133 
CLR H221 H N N 134 
CLR H222 H N N 135 
CLR H231 H N N 136 
CLR H232 H N N 137 
CLR H241 H N N 138 
CLR H242 H N N 139 
CLR H25  H N N 140 
CLR H261 H N N 141 
CLR H262 H N N 142 
CLR H263 H N N 143 
CLR H271 H N N 144 
CLR H272 H N N 145 
CLR H273 H N N 146 
CLR H1   H N N 147 
CYS N    N N N 148 
CYS CA   C N R 149 
CYS C    C N N 150 
CYS O    O N N 151 
CYS CB   C N N 152 
CYS SG   S N N 153 
CYS OXT  O N N 154 
CYS H    H N N 155 
CYS H2   H N N 156 
CYS HA   H N N 157 
CYS HB2  H N N 158 
CYS HB3  H N N 159 
CYS HG   H N N 160 
CYS HXT  H N N 161 
GLN N    N N N 162 
GLN CA   C N S 163 
GLN C    C N N 164 
GLN O    O N N 165 
GLN CB   C N N 166 
GLN CG   C N N 167 
GLN CD   C N N 168 
GLN OE1  O N N 169 
GLN NE2  N N N 170 
GLN OXT  O N N 171 
GLN H    H N N 172 
GLN H2   H N N 173 
GLN HA   H N N 174 
GLN HB2  H N N 175 
GLN HB3  H N N 176 
GLN HG2  H N N 177 
GLN HG3  H N N 178 
GLN HE21 H N N 179 
GLN HE22 H N N 180 
GLN HXT  H N N 181 
GLU N    N N N 182 
GLU CA   C N S 183 
GLU C    C N N 184 
GLU O    O N N 185 
GLU CB   C N N 186 
GLU CG   C N N 187 
GLU CD   C N N 188 
GLU OE1  O N N 189 
GLU OE2  O N N 190 
GLU OXT  O N N 191 
GLU H    H N N 192 
GLU H2   H N N 193 
GLU HA   H N N 194 
GLU HB2  H N N 195 
GLU HB3  H N N 196 
GLU HG2  H N N 197 
GLU HG3  H N N 198 
GLU HE2  H N N 199 
GLU HXT  H N N 200 
GLY N    N N N 201 
GLY CA   C N N 202 
GLY C    C N N 203 
GLY O    O N N 204 
GLY OXT  O N N 205 
GLY H    H N N 206 
GLY H2   H N N 207 
GLY HA2  H N N 208 
GLY HA3  H N N 209 
GLY HXT  H N N 210 
HIS N    N N N 211 
HIS CA   C N S 212 
HIS C    C N N 213 
HIS O    O N N 214 
HIS CB   C N N 215 
HIS CG   C Y N 216 
HIS ND1  N Y N 217 
HIS CD2  C Y N 218 
HIS CE1  C Y N 219 
HIS NE2  N Y N 220 
HIS OXT  O N N 221 
HIS H    H N N 222 
HIS H2   H N N 223 
HIS HA   H N N 224 
HIS HB2  H N N 225 
HIS HB3  H N N 226 
HIS HD1  H N N 227 
HIS HD2  H N N 228 
HIS HE1  H N N 229 
HIS HE2  H N N 230 
HIS HXT  H N N 231 
ILE N    N N N 232 
ILE CA   C N S 233 
ILE C    C N N 234 
ILE O    O N N 235 
ILE CB   C N S 236 
ILE CG1  C N N 237 
ILE CG2  C N N 238 
ILE CD1  C N N 239 
ILE OXT  O N N 240 
ILE H    H N N 241 
ILE H2   H N N 242 
ILE HA   H N N 243 
ILE HB   H N N 244 
ILE HG12 H N N 245 
ILE HG13 H N N 246 
ILE HG21 H N N 247 
ILE HG22 H N N 248 
ILE HG23 H N N 249 
ILE HD11 H N N 250 
ILE HD12 H N N 251 
ILE HD13 H N N 252 
ILE HXT  H N N 253 
IOS O1   O N N 254 
IOS N1   N Y N 255 
IOS C1   C Y N 256 
IOS C2   C Y N 257 
IOS C3   C Y N 258 
IOS C4   C Y N 259 
IOS C5   C Y N 260 
IOS C6   C Y N 261 
IOS C7   C Y N 262 
IOS C8   C Y N 263 
IOS S    S N N 264 
IOS O2   O N N 265 
IOS O3   O N N 266 
IOS O4   O N N 267 
IOS H1   H N N 268 
IOS HA   H N N 269 
IOS H4   H N N 270 
IOS H5   H N N 271 
IOS H6   H N N 272 
IOS H7   H N N 273 
IOS HB   H N N 274 
LEU N    N N N 275 
LEU CA   C N S 276 
LEU C    C N N 277 
LEU O    O N N 278 
LEU CB   C N N 279 
LEU CG   C N N 280 
LEU CD1  C N N 281 
LEU CD2  C N N 282 
LEU OXT  O N N 283 
LEU H    H N N 284 
LEU H2   H N N 285 
LEU HA   H N N 286 
LEU HB2  H N N 287 
LEU HB3  H N N 288 
LEU HG   H N N 289 
LEU HD11 H N N 290 
LEU HD12 H N N 291 
LEU HD13 H N N 292 
LEU HD21 H N N 293 
LEU HD22 H N N 294 
LEU HD23 H N N 295 
LEU HXT  H N N 296 
LYS N    N N N 297 
LYS CA   C N S 298 
LYS C    C N N 299 
LYS O    O N N 300 
LYS CB   C N N 301 
LYS CG   C N N 302 
LYS CD   C N N 303 
LYS CE   C N N 304 
LYS NZ   N N N 305 
LYS OXT  O N N 306 
LYS H    H N N 307 
LYS H2   H N N 308 
LYS HA   H N N 309 
LYS HB2  H N N 310 
LYS HB3  H N N 311 
LYS HG2  H N N 312 
LYS HG3  H N N 313 
LYS HD2  H N N 314 
LYS HD3  H N N 315 
LYS HE2  H N N 316 
LYS HE3  H N N 317 
LYS HZ1  H N N 318 
LYS HZ2  H N N 319 
LYS HZ3  H N N 320 
LYS HXT  H N N 321 
MET N    N N N 322 
MET CA   C N S 323 
MET C    C N N 324 
MET O    O N N 325 
MET CB   C N N 326 
MET CG   C N N 327 
MET SD   S N N 328 
MET CE   C N N 329 
MET OXT  O N N 330 
MET H    H N N 331 
MET H2   H N N 332 
MET HA   H N N 333 
MET HB2  H N N 334 
MET HB3  H N N 335 
MET HG2  H N N 336 
MET HG3  H N N 337 
MET HE1  H N N 338 
MET HE2  H N N 339 
MET HE3  H N N 340 
MET HXT  H N N 341 
NAG C1   C N R 342 
NAG C2   C N R 343 
NAG C3   C N R 344 
NAG C4   C N S 345 
NAG C5   C N R 346 
NAG C6   C N N 347 
NAG C7   C N N 348 
NAG C8   C N N 349 
NAG N2   N N N 350 
NAG O1   O N N 351 
NAG O3   O N N 352 
NAG O4   O N N 353 
NAG O5   O N N 354 
NAG O6   O N N 355 
NAG O7   O N N 356 
NAG H1   H N N 357 
NAG H2   H N N 358 
NAG H3   H N N 359 
NAG H4   H N N 360 
NAG H5   H N N 361 
NAG H61  H N N 362 
NAG H62  H N N 363 
NAG H81  H N N 364 
NAG H82  H N N 365 
NAG H83  H N N 366 
NAG HN2  H N N 367 
NAG HO1  H N N 368 
NAG HO3  H N N 369 
NAG HO4  H N N 370 
NAG HO6  H N N 371 
PHE N    N N N 372 
PHE CA   C N S 373 
PHE C    C N N 374 
PHE O    O N N 375 
PHE CB   C N N 376 
PHE CG   C Y N 377 
PHE CD1  C Y N 378 
PHE CD2  C Y N 379 
PHE CE1  C Y N 380 
PHE CE2  C Y N 381 
PHE CZ   C Y N 382 
PHE OXT  O N N 383 
PHE H    H N N 384 
PHE H2   H N N 385 
PHE HA   H N N 386 
PHE HB2  H N N 387 
PHE HB3  H N N 388 
PHE HD1  H N N 389 
PHE HD2  H N N 390 
PHE HE1  H N N 391 
PHE HE2  H N N 392 
PHE HZ   H N N 393 
PHE HXT  H N N 394 
POV N    N N N 395 
POV P    P N N 396 
POV C1   C N N 397 
POV C2   C N S 398 
POV C3   C N N 399 
POV C210 C N N 400 
POV C310 C N N 401 
POV C11  C N N 402 
POV O11  O N N 403 
POV C211 C N N 404 
POV C311 C N N 405 
POV C12  C N N 406 
POV O12  O N N 407 
POV C212 C N N 408 
POV C312 C N N 409 
POV C13  C N N 410 
POV O13  O N N 411 
POV C213 C N N 412 
POV C313 C N N 413 
POV C14  C N N 414 
POV O14  O N N 415 
POV C214 C N N 416 
POV C314 C N N 417 
POV C15  C N N 418 
POV C215 C N N 419 
POV C315 C N N 420 
POV C216 C N N 421 
POV C316 C N N 422 
POV C217 C N N 423 
POV C218 C N N 424 
POV C21  C N N 425 
POV O21  O N N 426 
POV C22  C N N 427 
POV O22  O N N 428 
POV C23  C N N 429 
POV C24  C N N 430 
POV C25  C N N 431 
POV C26  C N N 432 
POV C27  C N N 433 
POV C28  C N N 434 
POV C29  C N N 435 
POV C31  C N N 436 
POV O31  O N N 437 
POV C32  C N N 438 
POV O32  O N N 439 
POV C33  C N N 440 
POV C34  C N N 441 
POV C35  C N N 442 
POV C36  C N N 443 
POV C37  C N N 444 
POV C38  C N N 445 
POV C39  C N N 446 
POV H29  H N N 447 
POV H1   H N N 448 
POV H1A  H N N 449 
POV H2   H N N 450 
POV H3   H N N 451 
POV H3A  H N N 452 
POV H310 H N N 453 
POV H31A H N N 454 
POV H210 H N N 455 
POV H11  H N N 456 
POV H11A H N N 457 
POV H211 H N N 458 
POV H21A H N N 459 
POV H311 H N N 460 
POV H31B H N N 461 
POV H12  H N N 462 
POV H12A H N N 463 
POV H22  H N N 464 
POV H212 H N N 465 
POV H22A H N N 466 
POV H21B H N N 467 
POV H32  H N N 468 
POV H312 H N N 469 
POV H32A H N N 470 
POV H31C H N N 471 
POV H13  H N N 472 
POV H13A H N N 473 
POV H13B H N N 474 
POV H23  H N N 475 
POV H213 H N N 476 
POV H23A H N N 477 
POV H21C H N N 478 
POV H33  H N N 479 
POV H313 H N N 480 
POV H33A H N N 481 
POV H31D H N N 482 
POV H14  H N N 483 
POV H14A H N N 484 
POV H14B H N N 485 
POV H24  H N N 486 
POV H214 H N N 487 
POV H24A H N N 488 
POV H21D H N N 489 
POV H34  H N N 490 
POV H314 H N N 491 
POV H34A H N N 492 
POV H31E H N N 493 
POV H15  H N N 494 
POV H15A H N N 495 
POV H15B H N N 496 
POV H25  H N N 497 
POV H215 H N N 498 
POV H25A H N N 499 
POV H21E H N N 500 
POV H35  H N N 501 
POV H315 H N N 502 
POV H35A H N N 503 
POV H31F H N N 504 
POV H26  H N N 505 
POV H216 H N N 506 
POV H26A H N N 507 
POV H21F H N N 508 
POV H36  H N N 509 
POV H316 H N N 510 
POV H36A H N N 511 
POV H31G H N N 512 
POV H31H H N N 513 
POV H27  H N N 514 
POV H217 H N N 515 
POV H27A H N N 516 
POV H21G H N N 517 
POV H37  H N N 518 
POV H37A H N N 519 
POV H28  H N N 520 
POV H218 H N N 521 
POV H28A H N N 522 
POV H21H H N N 523 
POV H21J H N N 524 
POV H38  H N N 525 
POV H38A H N N 526 
POV H39  H N N 527 
POV H39A H N N 528 
PRO N    N N N 529 
PRO CA   C N S 530 
PRO C    C N N 531 
PRO O    O N N 532 
PRO CB   C N N 533 
PRO CG   C N N 534 
PRO CD   C N N 535 
PRO OXT  O N N 536 
PRO H    H N N 537 
PRO HA   H N N 538 
PRO HB2  H N N 539 
PRO HB3  H N N 540 
PRO HG2  H N N 541 
PRO HG3  H N N 542 
PRO HD2  H N N 543 
PRO HD3  H N N 544 
PRO HXT  H N N 545 
SER N    N N N 546 
SER CA   C N S 547 
SER C    C N N 548 
SER O    O N N 549 
SER CB   C N N 550 
SER OG   O N N 551 
SER OXT  O N N 552 
SER H    H N N 553 
SER H2   H N N 554 
SER HA   H N N 555 
SER HB2  H N N 556 
SER HB3  H N N 557 
SER HG   H N N 558 
SER HXT  H N N 559 
THR N    N N N 560 
THR CA   C N S 561 
THR C    C N N 562 
THR O    O N N 563 
THR CB   C N R 564 
THR OG1  O N N 565 
THR CG2  C N N 566 
THR OXT  O N N 567 
THR H    H N N 568 
THR H2   H N N 569 
THR HA   H N N 570 
THR HB   H N N 571 
THR HG1  H N N 572 
THR HG21 H N N 573 
THR HG22 H N N 574 
THR HG23 H N N 575 
THR HXT  H N N 576 
TRP N    N N N 577 
TRP CA   C N S 578 
TRP C    C N N 579 
TRP O    O N N 580 
TRP CB   C N N 581 
TRP CG   C Y N 582 
TRP CD1  C Y N 583 
TRP CD2  C Y N 584 
TRP NE1  N Y N 585 
TRP CE2  C Y N 586 
TRP CE3  C Y N 587 
TRP CZ2  C Y N 588 
TRP CZ3  C Y N 589 
TRP CH2  C Y N 590 
TRP OXT  O N N 591 
TRP H    H N N 592 
TRP H2   H N N 593 
TRP HA   H N N 594 
TRP HB2  H N N 595 
TRP HB3  H N N 596 
TRP HD1  H N N 597 
TRP HE1  H N N 598 
TRP HE3  H N N 599 
TRP HZ2  H N N 600 
TRP HZ3  H N N 601 
TRP HH2  H N N 602 
TRP HXT  H N N 603 
TYR N    N N N 604 
TYR CA   C N S 605 
TYR C    C N N 606 
TYR O    O N N 607 
TYR CB   C N N 608 
TYR CG   C Y N 609 
TYR CD1  C Y N 610 
TYR CD2  C Y N 611 
TYR CE1  C Y N 612 
TYR CE2  C Y N 613 
TYR CZ   C Y N 614 
TYR OH   O N N 615 
TYR OXT  O N N 616 
TYR H    H N N 617 
TYR H2   H N N 618 
TYR HA   H N N 619 
TYR HB2  H N N 620 
TYR HB3  H N N 621 
TYR HD1  H N N 622 
TYR HD2  H N N 623 
TYR HE1  H N N 624 
TYR HE2  H N N 625 
TYR HH   H N N 626 
TYR HXT  H N N 627 
VAL N    N N N 628 
VAL CA   C N S 629 
VAL C    C N N 630 
VAL O    O N N 631 
VAL CB   C N N 632 
VAL CG1  C N N 633 
VAL CG2  C N N 634 
VAL OXT  O N N 635 
VAL H    H N N 636 
VAL H2   H N N 637 
VAL HA   H N N 638 
VAL HB   H N N 639 
VAL HG11 H N N 640 
VAL HG12 H N N 641 
VAL HG13 H N N 642 
VAL HG21 H N N 643 
VAL HG22 H N N 644 
VAL HG23 H N N 645 
VAL HXT  H N N 646 
# 
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  
CLR C1   C2   sing N N 70  
CLR C1   C10  sing N N 71  
CLR C1   H11  sing N N 72  
CLR C1   H12  sing N N 73  
CLR C2   C3   sing N N 74  
CLR C2   H21  sing N N 75  
CLR C2   H22  sing N N 76  
CLR C3   C4   sing N N 77  
CLR C3   O1   sing N N 78  
CLR C3   H3   sing N N 79  
CLR C4   C5   sing N N 80  
CLR C4   H41  sing N N 81  
CLR C4   H42  sing N N 82  
CLR C5   C6   doub N N 83  
CLR C5   C10  sing N N 84  
CLR C6   C7   sing N N 85  
CLR C6   H6   sing N N 86  
CLR C7   C8   sing N N 87  
CLR C7   H71  sing N N 88  
CLR C7   H72  sing N N 89  
CLR C8   C9   sing N N 90  
CLR C8   C14  sing N N 91  
CLR C8   H8   sing N N 92  
CLR C9   C10  sing N N 93  
CLR C9   C11  sing N N 94  
CLR C9   H9   sing N N 95  
CLR C10  C19  sing N N 96  
CLR C11  C12  sing N N 97  
CLR C11  H111 sing N N 98  
CLR C11  H112 sing N N 99  
CLR C12  C13  sing N N 100 
CLR C12  H121 sing N N 101 
CLR C12  H122 sing N N 102 
CLR C13  C14  sing N N 103 
CLR C13  C17  sing N N 104 
CLR C13  C18  sing N N 105 
CLR C14  C15  sing N N 106 
CLR C14  H14  sing N N 107 
CLR C15  C16  sing N N 108 
CLR C15  H151 sing N N 109 
CLR C15  H152 sing N N 110 
CLR C16  C17  sing N N 111 
CLR C16  H161 sing N N 112 
CLR C16  H162 sing N N 113 
CLR C17  C20  sing N N 114 
CLR C17  H17  sing N N 115 
CLR C18  H181 sing N N 116 
CLR C18  H182 sing N N 117 
CLR C18  H183 sing N N 118 
CLR C19  H191 sing N N 119 
CLR C19  H192 sing N N 120 
CLR C19  H193 sing N N 121 
CLR C20  C21  sing N N 122 
CLR C20  C22  sing N N 123 
CLR C20  H20  sing N N 124 
CLR C21  H211 sing N N 125 
CLR C21  H212 sing N N 126 
CLR C21  H213 sing N N 127 
CLR C22  C23  sing N N 128 
CLR C22  H221 sing N N 129 
CLR C22  H222 sing N N 130 
CLR C23  C24  sing N N 131 
CLR C23  H231 sing N N 132 
CLR C23  H232 sing N N 133 
CLR C24  C25  sing N N 134 
CLR C24  H241 sing N N 135 
CLR C24  H242 sing N N 136 
CLR C25  C26  sing N N 137 
CLR C25  C27  sing N N 138 
CLR C25  H25  sing N N 139 
CLR C26  H261 sing N N 140 
CLR C26  H262 sing N N 141 
CLR C26  H263 sing N N 142 
CLR C27  H271 sing N N 143 
CLR C27  H272 sing N N 144 
CLR C27  H273 sing N N 145 
CLR O1   H1   sing N N 146 
CYS N    CA   sing N N 147 
CYS N    H    sing N N 148 
CYS N    H2   sing N N 149 
CYS CA   C    sing N N 150 
CYS CA   CB   sing N N 151 
CYS CA   HA   sing N N 152 
CYS C    O    doub N N 153 
CYS C    OXT  sing N N 154 
CYS CB   SG   sing N N 155 
CYS CB   HB2  sing N N 156 
CYS CB   HB3  sing N N 157 
CYS SG   HG   sing N N 158 
CYS OXT  HXT  sing N N 159 
GLN N    CA   sing N N 160 
GLN N    H    sing N N 161 
GLN N    H2   sing N N 162 
GLN CA   C    sing N N 163 
GLN CA   CB   sing N N 164 
GLN CA   HA   sing N N 165 
GLN C    O    doub N N 166 
GLN C    OXT  sing N N 167 
GLN CB   CG   sing N N 168 
GLN CB   HB2  sing N N 169 
GLN CB   HB3  sing N N 170 
GLN CG   CD   sing N N 171 
GLN CG   HG2  sing N N 172 
GLN CG   HG3  sing N N 173 
GLN CD   OE1  doub N N 174 
GLN CD   NE2  sing N N 175 
GLN NE2  HE21 sing N N 176 
GLN NE2  HE22 sing N N 177 
GLN OXT  HXT  sing N N 178 
GLU N    CA   sing N N 179 
GLU N    H    sing N N 180 
GLU N    H2   sing N N 181 
GLU CA   C    sing N N 182 
GLU CA   CB   sing N N 183 
GLU CA   HA   sing N N 184 
GLU C    O    doub N N 185 
GLU C    OXT  sing N N 186 
GLU CB   CG   sing N N 187 
GLU CB   HB2  sing N N 188 
GLU CB   HB3  sing N N 189 
GLU CG   CD   sing N N 190 
GLU CG   HG2  sing N N 191 
GLU CG   HG3  sing N N 192 
GLU CD   OE1  doub N N 193 
GLU CD   OE2  sing N N 194 
GLU OE2  HE2  sing N N 195 
GLU OXT  HXT  sing N N 196 
GLY N    CA   sing N N 197 
GLY N    H    sing N N 198 
GLY N    H2   sing N N 199 
GLY CA   C    sing N N 200 
GLY CA   HA2  sing N N 201 
GLY CA   HA3  sing N N 202 
GLY C    O    doub N N 203 
GLY C    OXT  sing N N 204 
GLY OXT  HXT  sing N N 205 
HIS N    CA   sing N N 206 
HIS N    H    sing N N 207 
HIS N    H2   sing N N 208 
HIS CA   C    sing N N 209 
HIS CA   CB   sing N N 210 
HIS CA   HA   sing N N 211 
HIS C    O    doub N N 212 
HIS C    OXT  sing N N 213 
HIS CB   CG   sing N N 214 
HIS CB   HB2  sing N N 215 
HIS CB   HB3  sing N N 216 
HIS CG   ND1  sing Y N 217 
HIS CG   CD2  doub Y N 218 
HIS ND1  CE1  doub Y N 219 
HIS ND1  HD1  sing N N 220 
HIS CD2  NE2  sing Y N 221 
HIS CD2  HD2  sing N N 222 
HIS CE1  NE2  sing Y N 223 
HIS CE1  HE1  sing N N 224 
HIS NE2  HE2  sing N N 225 
HIS OXT  HXT  sing N N 226 
ILE N    CA   sing N N 227 
ILE N    H    sing N N 228 
ILE N    H2   sing N N 229 
ILE CA   C    sing N N 230 
ILE CA   CB   sing N N 231 
ILE CA   HA   sing N N 232 
ILE C    O    doub N N 233 
ILE C    OXT  sing N N 234 
ILE CB   CG1  sing N N 235 
ILE CB   CG2  sing N N 236 
ILE CB   HB   sing N N 237 
ILE CG1  CD1  sing N N 238 
ILE CG1  HG12 sing N N 239 
ILE CG1  HG13 sing N N 240 
ILE CG2  HG21 sing N N 241 
ILE CG2  HG22 sing N N 242 
ILE CG2  HG23 sing N N 243 
ILE CD1  HD11 sing N N 244 
ILE CD1  HD12 sing N N 245 
ILE CD1  HD13 sing N N 246 
ILE OXT  HXT  sing N N 247 
IOS O1   C2   sing N N 248 
IOS O1   S    sing N N 249 
IOS N1   C1   sing Y N 250 
IOS N1   C8   sing Y N 251 
IOS N1   H1   sing N N 252 
IOS C1   C2   doub Y N 253 
IOS C1   HA   sing N N 254 
IOS C2   C3   sing Y N 255 
IOS C3   C4   doub Y N 256 
IOS C3   C8   sing Y N 257 
IOS C4   C5   sing Y N 258 
IOS C4   H4   sing N N 259 
IOS C5   C6   doub Y N 260 
IOS C5   H5   sing N N 261 
IOS C6   C7   sing Y N 262 
IOS C6   H6   sing N N 263 
IOS C7   C8   doub Y N 264 
IOS C7   H7   sing N N 265 
IOS S    O2   doub N N 266 
IOS S    O3   doub N N 267 
IOS S    O4   sing N N 268 
IOS O4   HB   sing N N 269 
LEU N    CA   sing N N 270 
LEU N    H    sing N N 271 
LEU N    H2   sing N N 272 
LEU CA   C    sing N N 273 
LEU CA   CB   sing N N 274 
LEU CA   HA   sing N N 275 
LEU C    O    doub N N 276 
LEU C    OXT  sing N N 277 
LEU CB   CG   sing N N 278 
LEU CB   HB2  sing N N 279 
LEU CB   HB3  sing N N 280 
LEU CG   CD1  sing N N 281 
LEU CG   CD2  sing N N 282 
LEU CG   HG   sing N N 283 
LEU CD1  HD11 sing N N 284 
LEU CD1  HD12 sing N N 285 
LEU CD1  HD13 sing N N 286 
LEU CD2  HD21 sing N N 287 
LEU CD2  HD22 sing N N 288 
LEU CD2  HD23 sing N N 289 
LEU OXT  HXT  sing N N 290 
LYS N    CA   sing N N 291 
LYS N    H    sing N N 292 
LYS N    H2   sing N N 293 
LYS CA   C    sing N N 294 
LYS CA   CB   sing N N 295 
LYS CA   HA   sing N N 296 
LYS C    O    doub N N 297 
LYS C    OXT  sing N N 298 
LYS CB   CG   sing N N 299 
LYS CB   HB2  sing N N 300 
LYS CB   HB3  sing N N 301 
LYS CG   CD   sing N N 302 
LYS CG   HG2  sing N N 303 
LYS CG   HG3  sing N N 304 
LYS CD   CE   sing N N 305 
LYS CD   HD2  sing N N 306 
LYS CD   HD3  sing N N 307 
LYS CE   NZ   sing N N 308 
LYS CE   HE2  sing N N 309 
LYS CE   HE3  sing N N 310 
LYS NZ   HZ1  sing N N 311 
LYS NZ   HZ2  sing N N 312 
LYS NZ   HZ3  sing N N 313 
LYS OXT  HXT  sing N N 314 
MET N    CA   sing N N 315 
MET N    H    sing N N 316 
MET N    H2   sing N N 317 
MET CA   C    sing N N 318 
MET CA   CB   sing N N 319 
MET CA   HA   sing N N 320 
MET C    O    doub N N 321 
MET C    OXT  sing N N 322 
MET CB   CG   sing N N 323 
MET CB   HB2  sing N N 324 
MET CB   HB3  sing N N 325 
MET CG   SD   sing N N 326 
MET CG   HG2  sing N N 327 
MET CG   HG3  sing N N 328 
MET SD   CE   sing N N 329 
MET CE   HE1  sing N N 330 
MET CE   HE2  sing N N 331 
MET CE   HE3  sing N N 332 
MET OXT  HXT  sing N N 333 
NAG C1   C2   sing N N 334 
NAG C1   O1   sing N N 335 
NAG C1   O5   sing N N 336 
NAG C1   H1   sing N N 337 
NAG C2   C3   sing N N 338 
NAG C2   N2   sing N N 339 
NAG C2   H2   sing N N 340 
NAG C3   C4   sing N N 341 
NAG C3   O3   sing N N 342 
NAG C3   H3   sing N N 343 
NAG C4   C5   sing N N 344 
NAG C4   O4   sing N N 345 
NAG C4   H4   sing N N 346 
NAG C5   C6   sing N N 347 
NAG C5   O5   sing N N 348 
NAG C5   H5   sing N N 349 
NAG C6   O6   sing N N 350 
NAG C6   H61  sing N N 351 
NAG C6   H62  sing N N 352 
NAG C7   C8   sing N N 353 
NAG C7   N2   sing N N 354 
NAG C7   O7   doub N N 355 
NAG C8   H81  sing N N 356 
NAG C8   H82  sing N N 357 
NAG C8   H83  sing N N 358 
NAG N2   HN2  sing N N 359 
NAG O1   HO1  sing N N 360 
NAG O3   HO3  sing N N 361 
NAG O4   HO4  sing N N 362 
NAG O6   HO6  sing N N 363 
PHE N    CA   sing N N 364 
PHE N    H    sing N N 365 
PHE N    H2   sing N N 366 
PHE CA   C    sing N N 367 
PHE CA   CB   sing N N 368 
PHE CA   HA   sing N N 369 
PHE C    O    doub N N 370 
PHE C    OXT  sing N N 371 
PHE CB   CG   sing N N 372 
PHE CB   HB2  sing N N 373 
PHE CB   HB3  sing N N 374 
PHE CG   CD1  doub Y N 375 
PHE CG   CD2  sing Y N 376 
PHE CD1  CE1  sing Y N 377 
PHE CD1  HD1  sing N N 378 
PHE CD2  CE2  doub Y N 379 
PHE CD2  HD2  sing N N 380 
PHE CE1  CZ   doub Y N 381 
PHE CE1  HE1  sing N N 382 
PHE CE2  CZ   sing Y N 383 
PHE CE2  HE2  sing N N 384 
PHE CZ   HZ   sing N N 385 
PHE OXT  HXT  sing N N 386 
POV N    C12  sing N N 387 
POV N    C13  sing N N 388 
POV N    C14  sing N N 389 
POV N    C15  sing N N 390 
POV P    O11  sing N N 391 
POV P    O12  sing N N 392 
POV P    O13  sing N N 393 
POV P    O14  doub N N 394 
POV C1   C2   sing N N 395 
POV C1   O11  sing N N 396 
POV C1   H1   sing N N 397 
POV C1   H1A  sing N N 398 
POV C2   C3   sing N N 399 
POV C2   O21  sing N N 400 
POV C2   H2   sing N N 401 
POV C3   O31  sing N N 402 
POV C3   H3   sing N N 403 
POV C3   H3A  sing N N 404 
POV C210 C211 sing N N 405 
POV C210 C29  doub N Z 406 
POV C210 H210 sing N N 407 
POV C310 C311 sing N N 408 
POV C310 C39  sing N N 409 
POV C310 H310 sing N N 410 
POV C310 H31A sing N N 411 
POV C11  C12  sing N N 412 
POV C11  O12  sing N N 413 
POV C11  H11  sing N N 414 
POV C11  H11A sing N N 415 
POV C211 C212 sing N N 416 
POV C211 H211 sing N N 417 
POV C211 H21A sing N N 418 
POV C311 C312 sing N N 419 
POV C311 H311 sing N N 420 
POV C311 H31B sing N N 421 
POV C12  H12  sing N N 422 
POV C12  H12A sing N N 423 
POV C212 C213 sing N N 424 
POV C212 H212 sing N N 425 
POV C212 H21B sing N N 426 
POV C312 C313 sing N N 427 
POV C312 H312 sing N N 428 
POV C312 H31C sing N N 429 
POV C13  H13  sing N N 430 
POV C13  H13A sing N N 431 
POV C13  H13B sing N N 432 
POV C213 C214 sing N N 433 
POV C213 H213 sing N N 434 
POV C213 H21C sing N N 435 
POV C313 C314 sing N N 436 
POV C313 H313 sing N N 437 
POV C313 H31D sing N N 438 
POV C14  H14  sing N N 439 
POV C14  H14A sing N N 440 
POV C14  H14B sing N N 441 
POV C214 C215 sing N N 442 
POV C214 H214 sing N N 443 
POV C214 H21D sing N N 444 
POV C314 C315 sing N N 445 
POV C314 H314 sing N N 446 
POV C314 H31E sing N N 447 
POV C15  H15  sing N N 448 
POV C15  H15A sing N N 449 
POV C15  H15B sing N N 450 
POV C215 C216 sing N N 451 
POV C215 H215 sing N N 452 
POV C215 H21E sing N N 453 
POV C315 C316 sing N N 454 
POV C315 H315 sing N N 455 
POV C315 H31F sing N N 456 
POV C216 C217 sing N N 457 
POV C216 H216 sing N N 458 
POV C216 H21F sing N N 459 
POV C316 H316 sing N N 460 
POV C316 H31G sing N N 461 
POV C316 H31H sing N N 462 
POV C217 C218 sing N N 463 
POV C217 H217 sing N N 464 
POV C217 H21G sing N N 465 
POV C218 H218 sing N N 466 
POV C218 H21H sing N N 467 
POV C218 H21J sing N N 468 
POV C21  O21  sing N N 469 
POV C21  C22  sing N N 470 
POV C21  O22  doub N N 471 
POV C22  C23  sing N N 472 
POV C22  H22  sing N N 473 
POV C22  H22A sing N N 474 
POV C23  C24  sing N N 475 
POV C23  H23  sing N N 476 
POV C23  H23A sing N N 477 
POV C24  C25  sing N N 478 
POV C24  H24  sing N N 479 
POV C24  H24A sing N N 480 
POV C25  C26  sing N N 481 
POV C25  H25  sing N N 482 
POV C25  H25A sing N N 483 
POV C26  C27  sing N N 484 
POV C26  H26  sing N N 485 
POV C26  H26A sing N N 486 
POV C27  C28  sing N N 487 
POV C27  H27  sing N N 488 
POV C27  H27A sing N N 489 
POV C28  C29  sing N N 490 
POV C28  H28  sing N N 491 
POV C28  H28A sing N N 492 
POV C29  H29  sing N N 493 
POV C31  O31  sing N N 494 
POV C31  C32  sing N N 495 
POV C31  O32  doub N N 496 
POV C32  C33  sing N N 497 
POV C32  H32  sing N N 498 
POV C32  H32A sing N N 499 
POV C33  C34  sing N N 500 
POV C33  H33  sing N N 501 
POV C33  H33A sing N N 502 
POV C34  C35  sing N N 503 
POV C34  H34  sing N N 504 
POV C34  H34A sing N N 505 
POV C35  C36  sing N N 506 
POV C35  H35  sing N N 507 
POV C35  H35A sing N N 508 
POV C36  C37  sing N N 509 
POV C36  H36  sing N N 510 
POV C36  H36A sing N N 511 
POV C37  C38  sing N N 512 
POV C37  H37  sing N N 513 
POV C37  H37A sing N N 514 
POV C38  C39  sing N N 515 
POV C38  H38  sing N N 516 
POV C38  H38A sing N N 517 
POV C39  H39  sing N N 518 
POV C39  H39A sing N N 519 
PRO N    CA   sing N N 520 
PRO N    CD   sing N N 521 
PRO N    H    sing N N 522 
PRO CA   C    sing N N 523 
PRO CA   CB   sing N N 524 
PRO CA   HA   sing N N 525 
PRO C    O    doub N N 526 
PRO C    OXT  sing N N 527 
PRO CB   CG   sing N N 528 
PRO CB   HB2  sing N N 529 
PRO CB   HB3  sing N N 530 
PRO CG   CD   sing N N 531 
PRO CG   HG2  sing N N 532 
PRO CG   HG3  sing N N 533 
PRO CD   HD2  sing N N 534 
PRO CD   HD3  sing N N 535 
PRO OXT  HXT  sing N N 536 
SER N    CA   sing N N 537 
SER N    H    sing N N 538 
SER N    H2   sing N N 539 
SER CA   C    sing N N 540 
SER CA   CB   sing N N 541 
SER CA   HA   sing N N 542 
SER C    O    doub N N 543 
SER C    OXT  sing N N 544 
SER CB   OG   sing N N 545 
SER CB   HB2  sing N N 546 
SER CB   HB3  sing N N 547 
SER OG   HG   sing N N 548 
SER OXT  HXT  sing N N 549 
THR N    CA   sing N N 550 
THR N    H    sing N N 551 
THR N    H2   sing N N 552 
THR CA   C    sing N N 553 
THR CA   CB   sing N N 554 
THR CA   HA   sing N N 555 
THR C    O    doub N N 556 
THR C    OXT  sing N N 557 
THR CB   OG1  sing N N 558 
THR CB   CG2  sing N N 559 
THR CB   HB   sing N N 560 
THR OG1  HG1  sing N N 561 
THR CG2  HG21 sing N N 562 
THR CG2  HG22 sing N N 563 
THR CG2  HG23 sing N N 564 
THR OXT  HXT  sing N N 565 
TRP N    CA   sing N N 566 
TRP N    H    sing N N 567 
TRP N    H2   sing N N 568 
TRP CA   C    sing N N 569 
TRP CA   CB   sing N N 570 
TRP CA   HA   sing N N 571 
TRP C    O    doub N N 572 
TRP C    OXT  sing N N 573 
TRP CB   CG   sing N N 574 
TRP CB   HB2  sing N N 575 
TRP CB   HB3  sing N N 576 
TRP CG   CD1  doub Y N 577 
TRP CG   CD2  sing Y N 578 
TRP CD1  NE1  sing Y N 579 
TRP CD1  HD1  sing N N 580 
TRP CD2  CE2  doub Y N 581 
TRP CD2  CE3  sing Y N 582 
TRP NE1  CE2  sing Y N 583 
TRP NE1  HE1  sing N N 584 
TRP CE2  CZ2  sing Y N 585 
TRP CE3  CZ3  doub Y N 586 
TRP CE3  HE3  sing N N 587 
TRP CZ2  CH2  doub Y N 588 
TRP CZ2  HZ2  sing N N 589 
TRP CZ3  CH2  sing Y N 590 
TRP CZ3  HZ3  sing N N 591 
TRP CH2  HH2  sing N N 592 
TRP OXT  HXT  sing N N 593 
TYR N    CA   sing N N 594 
TYR N    H    sing N N 595 
TYR N    H2   sing N N 596 
TYR CA   C    sing N N 597 
TYR CA   CB   sing N N 598 
TYR CA   HA   sing N N 599 
TYR C    O    doub N N 600 
TYR C    OXT  sing N N 601 
TYR CB   CG   sing N N 602 
TYR CB   HB2  sing N N 603 
TYR CB   HB3  sing N N 604 
TYR CG   CD1  doub Y N 605 
TYR CG   CD2  sing Y N 606 
TYR CD1  CE1  sing Y N 607 
TYR CD1  HD1  sing N N 608 
TYR CD2  CE2  doub Y N 609 
TYR CD2  HD2  sing N N 610 
TYR CE1  CZ   doub Y N 611 
TYR CE1  HE1  sing N N 612 
TYR CE2  CZ   sing Y N 613 
TYR CE2  HE2  sing N N 614 
TYR CZ   OH   sing N N 615 
TYR OH   HH   sing N N 616 
TYR OXT  HXT  sing N N 617 
VAL N    CA   sing N N 618 
VAL N    H    sing N N 619 
VAL N    H2   sing N N 620 
VAL CA   C    sing N N 621 
VAL CA   CB   sing N N 622 
VAL CA   HA   sing N N 623 
VAL C    O    doub N N 624 
VAL C    OXT  sing N N 625 
VAL CB   CG1  sing N N 626 
VAL CB   CG2  sing N N 627 
VAL CB   HB   sing N N 628 
VAL CG1  HG11 sing N N 629 
VAL CG1  HG12 sing N N 630 
VAL CG1  HG13 sing N N 631 
VAL CG2  HG21 sing N N 632 
VAL CG2  HG22 sing N N 633 
VAL CG2  HG23 sing N N 634 
VAL OXT  HXT  sing N N 635 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-08 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9J40 
_em_admin.last_update        2025-06-18 
_em_admin.map_release_date   2025-04-02 
_em_admin.title              'Cryo-EM structure of lysosome cholesterol sencing protein complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 1 2 9606  'Homo sapiens'        ? ? ? ? ? 
? ? 1 3 61853 'Nomascus leucogenys' ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 1 2 9606 'Homo sapiens' ? ? 
? 1 3 9606 'Homo sapiens' ? ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?      ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ?      ? 
MASKING                    ? 3  ? ? ? ?      ? 
'CTF CORRECTION'           ? 4  1 ? ? ?      ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?      ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?      ? 
'MODEL FITTING'            ? 7  ? ? ? ?      ? 
'MODEL REFINEMENT'         ? 8  ? ? ? PHENIX ? 
OTHER                      ? 9  ? ? ? ?      ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ? 
CLASSIFICATION             ? 12 1 ? ? ?      ? 
RECONSTRUCTION             ? 13 1 ? ? ?      ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           KY9100000034 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9J40 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
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 36  ? 110.626 135.171 106.121 1.00 69.65  ? 36   SER B N    1 
ATOM   2    C CA   . SER A 1 36  ? 110.193 135.792 107.365 1.00 68.97  ? 36   SER B CA   1 
ATOM   3    C C    . SER A 1 36  ? 110.790 135.060 108.562 1.00 63.74  ? 36   SER B C    1 
ATOM   4    O O    . SER A 1 36  ? 111.956 134.666 108.545 1.00 63.02  ? 36   SER B O    1 
ATOM   5    C CB   . SER A 1 36  ? 108.665 135.794 107.461 1.00 69.61  ? 36   SER B CB   1 
ATOM   6    O OG   . SER A 1 36  ? 108.094 136.760 106.598 1.00 76.22  ? 36   SER B OG   1 
ATOM   7    N N    . MET A 1 37  ? 109.974 134.897 109.600 1.00 58.01  ? 37   MET B N    1 
ATOM   8    C CA   . MET A 1 37  ? 110.364 134.175 110.805 1.00 61.53  ? 37   MET B CA   1 
ATOM   9    C C    . MET A 1 37  ? 110.730 132.736 110.444 1.00 62.08  ? 37   MET B C    1 
ATOM   10   O O    . MET A 1 37  ? 109.917 132.005 109.870 1.00 66.27  ? 37   MET B O    1 
ATOM   11   C CB   . MET A 1 37  ? 109.245 134.221 111.843 1.00 64.47  ? 37   MET B CB   1 
ATOM   12   C CG   . MET A 1 37  ? 108.841 135.621 112.286 1.00 66.98  ? 37   MET B CG   1 
ATOM   13   S SD   . MET A 1 37  ? 107.267 135.654 113.167 1.00 75.46  ? 37   MET B SD   1 
ATOM   14   C CE   . MET A 1 37  ? 107.792 136.275 114.763 1.00 55.47  ? 37   MET B CE   1 
ATOM   15   N N    . SER A 1 38  ? 111.972 132.352 110.743 1.00 44.95  ? 38   SER B N    1 
ATOM   16   C CA   . SER A 1 38  ? 112.468 130.978 110.610 1.00 41.58  ? 38   SER B CA   1 
ATOM   17   C C    . SER A 1 38  ? 112.139 130.141 111.851 1.00 43.34  ? 38   SER B C    1 
ATOM   18   O O    . SER A 1 38  ? 113.015 129.606 112.530 1.00 48.81  ? 38   SER B O    1 
ATOM   19   C CB   . SER A 1 38  ? 113.965 130.982 110.330 1.00 44.28  ? 38   SER B CB   1 
ATOM   20   O OG   . SER A 1 38  ? 114.222 131.013 108.938 1.00 46.24  ? 38   SER B OG   1 
ATOM   21   N N    . ILE A 1 39  ? 110.836 130.038 112.134 1.00 37.85  ? 39   ILE B N    1 
ATOM   22   C CA   . ILE A 1 39  ? 110.339 129.407 113.355 1.00 42.57  ? 39   ILE B CA   1 
ATOM   23   C C    . ILE A 1 39  ? 110.686 127.925 113.420 1.00 40.95  ? 39   ILE B C    1 
ATOM   24   O O    . ILE A 1 39  ? 110.626 127.327 114.501 1.00 45.94  ? 39   ILE B O    1 
ATOM   25   C CB   . ILE A 1 39  ? 108.811 129.573 113.468 1.00 41.46  ? 39   ILE B CB   1 
ATOM   26   C CG1  . ILE A 1 39  ? 108.388 130.976 113.095 1.00 45.03  ? 39   ILE B CG1  1 
ATOM   27   C CG2  . ILE A 1 39  ? 108.362 129.428 114.895 1.00 41.44  ? 39   ILE B CG2  1 
ATOM   28   C CD1  . ILE A 1 39  ? 107.577 130.988 111.841 1.00 37.53  ? 39   ILE B CD1  1 
ATOM   29   N N    . THR A 1 40  ? 111.059 127.311 112.290 1.00 42.59  ? 40   THR B N    1 
ATOM   30   C CA   . THR A 1 40  ? 111.521 125.925 112.323 1.00 40.74  ? 40   THR B CA   1 
ATOM   31   C C    . THR A 1 40  ? 112.722 125.760 113.246 1.00 45.94  ? 40   THR B C    1 
ATOM   32   O O    . THR A 1 40  ? 112.914 124.683 113.822 1.00 52.62  ? 40   THR B O    1 
ATOM   33   C CB   . THR A 1 40  ? 111.860 125.437 110.915 1.00 41.12  ? 40   THR B CB   1 
ATOM   34   O OG1  . THR A 1 40  ? 113.127 125.971 110.515 1.00 45.25  ? 40   THR B OG1  1 
ATOM   35   C CG2  . THR A 1 40  ? 110.789 125.876 109.927 1.00 49.01  ? 40   THR B CG2  1 
ATOM   36   N N    . ARG A 1 41  ? 113.531 126.809 113.417 1.00 41.41  ? 41   ARG B N    1 
ATOM   37   C CA   . ARG A 1 41  ? 114.718 126.729 114.257 1.00 41.78  ? 41   ARG B CA   1 
ATOM   38   C C    . ARG A 1 41  ? 114.580 127.615 115.491 1.00 43.71  ? 41   ARG B C    1 
ATOM   39   O O    . ARG A 1 41  ? 115.538 128.272 115.903 1.00 49.70  ? 41   ARG B O    1 
ATOM   40   C CB   . ARG A 1 41  ? 115.973 127.121 113.478 1.00 42.26  ? 41   ARG B CB   1 
ATOM   41   C CG   . ARG A 1 41  ? 115.908 126.862 111.987 1.00 46.41  ? 41   ARG B CG   1 
ATOM   42   C CD   . ARG A 1 41  ? 117.210 127.259 111.300 1.00 47.97  ? 41   ARG B CD   1 
ATOM   43   N NE   . ARG A 1 41  ? 117.304 128.698 111.081 1.00 50.41  ? 41   ARG B NE   1 
ATOM   44   C CZ   . ARG A 1 41  ? 118.320 129.454 111.474 1.00 52.32  ? 41   ARG B CZ   1 
ATOM   45   N NH1  . ARG A 1 41  ? 119.358 128.941 112.114 1.00 47.55  ? 41   ARG B NH1  1 
ATOM   46   N NH2  . ARG A 1 41  ? 118.295 130.759 111.217 1.00 49.27  ? 41   ARG B NH2  1 
ATOM   47   N N    . LEU A 1 42  ? 113.388 127.640 116.089 1.00 34.40  ? 42   LEU B N    1 
ATOM   48   C CA   . LEU A 1 42  ? 113.146 128.373 117.325 1.00 31.71  ? 42   LEU B CA   1 
ATOM   49   C C    . LEU A 1 42  ? 113.152 127.466 118.546 1.00 45.75  ? 42   LEU B C    1 
ATOM   50   O O    . LEU A 1 42  ? 113.600 127.884 119.618 1.00 51.50  ? 42   LEU B O    1 
ATOM   51   C CB   . LEU A 1 42  ? 111.806 129.116 117.242 1.00 22.08  ? 42   LEU B CB   1 
ATOM   52   C CG   . LEU A 1 42  ? 111.138 129.689 118.498 1.00 23.87  ? 42   LEU B CG   1 
ATOM   53   C CD1  . LEU A 1 42  ? 112.043 130.684 119.213 1.00 28.64  ? 42   LEU B CD1  1 
ATOM   54   C CD2  . LEU A 1 42  ? 109.810 130.335 118.154 1.00 29.08  ? 42   LEU B CD2  1 
ATOM   55   N N    . PHE A 1 43  ? 112.683 126.226 118.390 1.00 34.04  ? 43   PHE B N    1 
ATOM   56   C CA   . PHE A 1 43  ? 112.699 125.265 119.492 1.00 18.25  ? 43   PHE B CA   1 
ATOM   57   C C    . PHE A 1 43  ? 114.117 124.930 119.954 1.00 18.47  ? 43   PHE B C    1 
ATOM   58   O O    . PHE A 1 43  ? 114.341 124.907 121.177 1.00 23.98  ? 43   PHE B O    1 
ATOM   59   C CB   . PHE A 1 43  ? 111.873 124.029 119.110 1.00 20.74  ? 43   PHE B CB   1 
ATOM   60   C CG   . PHE A 1 43  ? 111.600 123.101 120.256 1.00 29.13  ? 43   PHE B CG   1 
ATOM   61   C CD1  . PHE A 1 43  ? 111.081 123.584 121.443 1.00 31.23  ? 43   PHE B CD1  1 
ATOM   62   C CD2  . PHE A 1 43  ? 111.849 121.745 120.142 1.00 32.44  ? 43   PHE B CD2  1 
ATOM   63   C CE1  . PHE A 1 43  ? 110.823 122.732 122.499 1.00 30.34  ? 43   PHE B CE1  1 
ATOM   64   C CE2  . PHE A 1 43  ? 111.594 120.889 121.195 1.00 24.06  ? 43   PHE B CE2  1 
ATOM   65   C CZ   . PHE A 1 43  ? 111.080 121.383 122.375 1.00 23.33  ? 43   PHE B CZ   1 
ATOM   66   N N    . PRO A 1 44  ? 115.089 124.609 119.077 1.00 14.35  ? 44   PRO B N    1 
ATOM   67   C CA   . PRO A 1 44  ? 116.462 124.387 119.572 1.00 26.95  ? 44   PRO B CA   1 
ATOM   68   C C    . PRO A 1 44  ? 117.032 125.564 120.348 1.00 32.94  ? 44   PRO B C    1 
ATOM   69   O O    . PRO A 1 44  ? 117.795 125.359 121.300 1.00 48.38  ? 44   PRO B O    1 
ATOM   70   C CB   . PRO A 1 44  ? 117.269 124.137 118.293 1.00 31.38  ? 44   PRO B CB   1 
ATOM   71   C CG   . PRO A 1 44  ? 116.317 123.646 117.315 1.00 28.77  ? 44   PRO B CG   1 
ATOM   72   C CD   . PRO A 1 44  ? 114.959 124.156 117.674 1.00 23.05  ? 44   PRO B CD   1 
ATOM   73   N N    . ALA A 1 45  ? 116.684 126.793 119.963 1.00 17.05  ? 45   ALA B N    1 
ATOM   74   C CA   . ALA A 1 45  ? 117.099 127.974 120.709 1.00 16.46  ? 45   ALA B CA   1 
ATOM   75   C C    . ALA A 1 45  ? 116.422 128.088 122.069 1.00 12.34  ? 45   ALA B C    1 
ATOM   76   O O    . ALA A 1 45  ? 116.953 128.773 122.948 1.00 23.36  ? 45   ALA B O    1 
ATOM   77   C CB   . ALA A 1 45  ? 116.821 129.235 119.891 1.00 19.39  ? 45   ALA B CB   1 
ATOM   78   N N    . LEU A 1 46  ? 115.273 127.445 122.270 1.00 11.56  ? 46   LEU B N    1 
ATOM   79   C CA   . LEU A 1 46  ? 114.641 127.426 123.583 1.00 23.05  ? 46   LEU B CA   1 
ATOM   80   C C    . LEU A 1 46  ? 115.063 126.234 124.432 1.00 25.95  ? 46   LEU B C    1 
ATOM   81   O O    . LEU A 1 46  ? 114.822 126.238 125.644 1.00 31.34  ? 46   LEU B O    1 
ATOM   82   C CB   . LEU A 1 46  ? 113.116 127.427 123.439 1.00 22.64  ? 46   LEU B CB   1 
ATOM   83   C CG   . LEU A 1 46  ? 112.449 128.782 123.197 1.00 21.69  ? 46   LEU B CG   1 
ATOM   84   C CD1  . LEU A 1 46  ? 111.104 128.606 122.516 1.00 22.38  ? 46   LEU B CD1  1 
ATOM   85   C CD2  . LEU A 1 46  ? 112.292 129.542 124.502 1.00 24.72  ? 46   LEU B CD2  1 
ATOM   86   N N    . LEU A 1 47  ? 115.682 125.220 123.828 1.00 17.82  ? 47   LEU B N    1 
ATOM   87   C CA   . LEU A 1 47  ? 116.257 124.104 124.570 1.00 17.07  ? 47   LEU B CA   1 
ATOM   88   C C    . LEU A 1 47  ? 117.620 124.435 125.166 1.00 27.76  ? 47   LEU B C    1 
ATOM   89   O O    . LEU A 1 47  ? 118.051 123.760 126.106 1.00 41.29  ? 47   LEU B O    1 
ATOM   90   C CB   . LEU A 1 47  ? 116.369 122.873 123.671 1.00 18.67  ? 47   LEU B CB   1 
ATOM   91   C CG   . LEU A 1 47  ? 115.064 122.116 123.420 1.00 15.66  ? 47   LEU B CG   1 
ATOM   92   C CD1  . LEU A 1 47  ? 115.294 120.943 122.484 1.00 19.85  ? 47   LEU B CD1  1 
ATOM   93   C CD2  . LEU A 1 47  ? 114.450 121.650 124.728 1.00 25.04  ? 47   LEU B CD2  1 
ATOM   94   N N    . GLU A 1 48  ? 118.303 125.451 124.639 1.00 18.69  ? 48   GLU B N    1 
ATOM   95   C CA   . GLU A 1 48  ? 119.593 125.880 125.172 1.00 23.58  ? 48   GLU B CA   1 
ATOM   96   C C    . GLU A 1 48  ? 119.426 126.875 126.314 1.00 30.37  ? 48   GLU B C    1 
ATOM   97   O O    . GLU A 1 48  ? 120.026 126.713 127.381 1.00 32.39  ? 48   GLU B O    1 
ATOM   98   C CB   . GLU A 1 48  ? 120.427 126.515 124.061 1.00 30.06  ? 48   GLU B CB   1 
ATOM   99   C CG   . GLU A 1 48  ? 121.632 127.291 124.565 1.00 35.08  ? 48   GLU B CG   1 
ATOM   100  C CD   . GLU A 1 48  ? 122.076 128.369 123.598 1.00 41.21  ? 48   GLU B CD   1 
ATOM   101  O OE1  . GLU A 1 48  ? 121.466 128.482 122.515 1.00 38.30  ? 48   GLU B OE1  1 
ATOM   102  O OE2  . GLU A 1 48  ? 123.030 129.108 123.923 1.00 37.98  ? 48   GLU B OE2  1 
ATOM   103  N N    . CYS A 1 49  ? 118.628 127.919 126.086 1.00 29.32  ? 49   CYS B N    1 
ATOM   104  C CA   . CYS A 1 49  ? 118.442 128.988 127.065 1.00 20.82  ? 49   CYS B CA   1 
ATOM   105  C C    . CYS A 1 49  ? 117.909 128.467 128.396 1.00 16.32  ? 49   CYS B C    1 
ATOM   106  O O    . CYS A 1 49  ? 118.392 128.867 129.460 1.00 21.10  ? 49   CYS B O    1 
ATOM   107  C CB   . CYS A 1 49  ? 117.515 130.058 126.495 1.00 22.48  ? 49   CYS B CB   1 
ATOM   108  S SG   . CYS A 1 49  ? 118.135 130.870 125.007 1.00 28.58  ? 49   CYS B SG   1 
ATOM   109  N N    . PHE A 1 50  ? 116.922 127.577 128.362 1.00 17.90  ? 50   PHE B N    1 
ATOM   110  C CA   . PHE A 1 50  ? 116.373 126.994 129.579 1.00 23.48  ? 50   PHE B CA   1 
ATOM   111  C C    . PHE A 1 50  ? 116.988 125.648 129.937 1.00 29.93  ? 50   PHE B C    1 
ATOM   112  O O    . PHE A 1 50  ? 116.778 125.168 131.055 1.00 27.60  ? 50   PHE B O    1 
ATOM   113  C CB   . PHE A 1 50  ? 114.854 126.830 129.449 1.00 14.26  ? 50   PHE B CB   1 
ATOM   114  C CG   . PHE A 1 50  ? 114.107 128.129 129.358 1.00 19.42  ? 50   PHE B CG   1 
ATOM   115  C CD1  . PHE A 1 50  ? 113.912 128.748 128.134 1.00 23.04  ? 50   PHE B CD1  1 
ATOM   116  C CD2  . PHE A 1 50  ? 113.599 128.732 130.495 1.00 23.52  ? 50   PHE B CD2  1 
ATOM   117  C CE1  . PHE A 1 50  ? 113.227 129.942 128.047 1.00 20.09  ? 50   PHE B CE1  1 
ATOM   118  C CE2  . PHE A 1 50  ? 112.913 129.927 130.413 1.00 24.83  ? 50   PHE B CE2  1 
ATOM   119  C CZ   . PHE A 1 50  ? 112.727 130.532 129.188 1.00 19.67  ? 50   PHE B CZ   1 
ATOM   120  N N    . GLY A 1 51  ? 117.729 125.025 129.021 1.00 29.64  ? 51   GLY B N    1 
ATOM   121  C CA   . GLY A 1 51  ? 118.508 123.853 129.386 1.00 21.15  ? 51   GLY B CA   1 
ATOM   122  C C    . GLY A 1 51  ? 119.656 124.163 130.331 1.00 23.32  ? 51   GLY B C    1 
ATOM   123  O O    . GLY A 1 51  ? 119.917 123.407 131.270 1.00 24.82  ? 51   GLY B O    1 
ATOM   124  N N    . ILE A 1 52  ? 120.359 125.274 130.099 1.00 23.89  ? 52   ILE B N    1 
ATOM   125  C CA   . ILE A 1 52  ? 121.441 125.675 130.997 1.00 18.28  ? 52   ILE B CA   1 
ATOM   126  C C    . ILE A 1 52  ? 120.891 126.188 132.326 1.00 21.45  ? 52   ILE B C    1 
ATOM   127  O O    . ILE A 1 52  ? 121.497 125.978 133.383 1.00 30.10  ? 52   ILE B O    1 
ATOM   128  C CB   . ILE A 1 52  ? 122.339 126.720 130.310 1.00 5.78   ? 52   ILE B CB   1 
ATOM   129  C CG1  . ILE A 1 52  ? 122.821 126.203 128.956 1.00 11.46  ? 52   ILE B CG1  1 
ATOM   130  C CG2  . ILE A 1 52  ? 123.535 127.067 131.175 1.00 8.97   ? 52   ILE B CG2  1 
ATOM   131  C CD1  . ILE A 1 52  ? 123.314 127.290 128.035 1.00 15.92  ? 52   ILE B CD1  1 
ATOM   132  N N    . VAL A 1 53  ? 119.742 126.870 132.298 1.00 11.80  ? 53   VAL B N    1 
ATOM   133  C CA   . VAL A 1 53  ? 119.108 127.338 133.531 1.00 7.89   ? 53   VAL B CA   1 
ATOM   134  C C    . VAL A 1 53  ? 118.729 126.165 134.431 1.00 20.76  ? 53   VAL B C    1 
ATOM   135  O O    . VAL A 1 53  ? 118.846 126.251 135.661 1.00 25.80  ? 53   VAL B O    1 
ATOM   136  C CB   . VAL A 1 53  ? 117.891 128.226 133.189 1.00 14.45  ? 53   VAL B CB   1 
ATOM   137  C CG1  . VAL A 1 53  ? 117.014 128.464 134.407 1.00 15.20  ? 53   VAL B CG1  1 
ATOM   138  C CG2  . VAL A 1 53  ? 118.354 129.554 132.626 1.00 13.74  ? 53   VAL B CG2  1 
ATOM   139  N N    . LEU A 1 54  ? 118.305 125.045 133.839 1.00 21.46  ? 54   LEU B N    1 
ATOM   140  C CA   . LEU A 1 54  ? 118.038 123.835 134.613 1.00 27.12  ? 54   LEU B CA   1 
ATOM   141  C C    . LEU A 1 54  ? 119.299 123.304 135.290 1.00 26.24  ? 54   LEU B C    1 
ATOM   142  O O    . LEU A 1 54  ? 119.241 122.841 136.436 1.00 24.83  ? 54   LEU B O    1 
ATOM   143  C CB   . LEU A 1 54  ? 117.422 122.767 133.711 1.00 22.96  ? 54   LEU B CB   1 
ATOM   144  C CG   . LEU A 1 54  ? 116.968 121.479 134.395 1.00 18.96  ? 54   LEU B CG   1 
ATOM   145  C CD1  . LEU A 1 54  ? 115.598 121.667 135.020 1.00 24.21  ? 54   LEU B CD1  1 
ATOM   146  C CD2  . LEU A 1 54  ? 116.953 120.330 133.403 1.00 23.34  ? 54   LEU B CD2  1 
ATOM   147  N N    . CYS A 1 55  ? 120.437 123.338 134.592 1.00 24.01  ? 55   CYS B N    1 
ATOM   148  C CA   . CYS A 1 55  ? 121.700 122.892 135.177 1.00 19.99  ? 55   CYS B CA   1 
ATOM   149  C C    . CYS A 1 55  ? 122.082 123.737 136.387 1.00 13.98  ? 55   CYS B C    1 
ATOM   150  O O    . CYS A 1 55  ? 122.577 123.218 137.393 1.00 28.07  ? 55   CYS B O    1 
ATOM   151  C CB   . CYS A 1 55  ? 122.808 122.929 134.124 1.00 14.02  ? 55   CYS B CB   1 
ATOM   152  S SG   . CYS A 1 55  ? 122.591 121.754 132.771 1.00 43.22  ? 55   CYS B SG   1 
ATOM   153  N N    . GLY A 1 56  ? 121.874 125.051 136.292 1.00 10.40  ? 56   GLY B N    1 
ATOM   154  C CA   . GLY A 1 56  ? 122.131 125.926 137.426 1.00 4.02   ? 56   GLY B CA   1 
ATOM   155  C C    . GLY A 1 56  ? 121.262 125.611 138.628 1.00 8.52   ? 56   GLY B C    1 
ATOM   156  O O    . GLY A 1 56  ? 121.708 125.704 139.774 1.00 23.58  ? 56   GLY B O    1 
ATOM   157  N N    . TYR A 1 57  ? 120.004 125.242 138.384 1.00 12.17  ? 57   TYR B N    1 
ATOM   158  C CA   . TYR A 1 57  ? 119.101 124.892 139.477 1.00 16.81  ? 57   TYR B CA   1 
ATOM   159  C C    . TYR A 1 57  ? 119.508 123.570 140.118 1.00 28.69  ? 57   TYR B C    1 
ATOM   160  O O    . TYR A 1 57  ? 119.540 123.446 141.348 1.00 32.91  ? 57   TYR B O    1 
ATOM   161  C CB   . TYR A 1 57  ? 117.663 124.818 138.964 1.00 15.82  ? 57   TYR B CB   1 
ATOM   162  C CG   . TYR A 1 57  ? 116.648 124.546 140.048 1.00 20.54  ? 57   TYR B CG   1 
ATOM   163  C CD1  . TYR A 1 57  ? 116.452 125.454 141.076 1.00 12.75  ? 57   TYR B CD1  1 
ATOM   164  C CD2  . TYR A 1 57  ? 115.905 123.374 140.059 1.00 29.95  ? 57   TYR B CD2  1 
ATOM   165  C CE1  . TYR A 1 57  ? 115.533 125.216 142.076 1.00 7.01   ? 57   TYR B CE1  1 
ATOM   166  C CE2  . TYR A 1 57  ? 114.981 123.126 141.056 1.00 23.74  ? 57   TYR B CE2  1 
ATOM   167  C CZ   . TYR A 1 57  ? 114.801 124.051 142.063 1.00 11.84  ? 57   TYR B CZ   1 
ATOM   168  O OH   . TYR A 1 57  ? 113.886 123.814 143.060 1.00 12.96  ? 57   TYR B OH   1 
ATOM   169  N N    . ILE A 1 58  ? 119.792 122.559 139.291 1.00 15.61  ? 58   ILE B N    1 
ATOM   170  C CA   . ILE A 1 58  ? 120.119 121.222 139.790 1.00 2.52   ? 58   ILE B CA   1 
ATOM   171  C C    . ILE A 1 58  ? 121.385 121.274 140.640 1.00 14.76  ? 58   ILE B C    1 
ATOM   172  O O    . ILE A 1 58  ? 121.447 120.708 141.737 1.00 25.02  ? 58   ILE B O    1 
ATOM   173  C CB   . ILE A 1 58  ? 120.254 120.233 138.617 1.00 6.85   ? 58   ILE B CB   1 
ATOM   174  C CG1  . ILE A 1 58  ? 118.880 119.694 138.223 1.00 19.51  ? 58   ILE B CG1  1 
ATOM   175  C CG2  . ILE A 1 58  ? 121.174 119.078 138.972 1.00 24.41  ? 58   ILE B CG2  1 
ATOM   176  C CD1  . ILE A 1 58  ? 118.859 119.012 136.875 1.00 23.35  ? 58   ILE B CD1  1 
ATOM   177  N N    . ALA A 1 59  ? 122.407 121.972 140.141 1.00 18.60  ? 59   ALA B N    1 
ATOM   178  C CA   . ALA A 1 59  ? 123.684 122.108 140.838 1.00 3.87   ? 59   ALA B CA   1 
ATOM   179  C C    . ALA A 1 59  ? 123.506 122.813 142.178 1.00 7.80   ? 59   ALA B C    1 
ATOM   180  O O    . ALA A 1 59  ? 124.105 122.423 143.186 1.00 20.22  ? 59   ALA B O    1 
ATOM   181  C CB   . ALA A 1 59  ? 124.683 122.860 139.960 1.00 7.01   ? 59   ALA B CB   1 
ATOM   182  N N    . GLY A 1 60  ? 122.704 123.877 142.193 1.00 21.54  ? 60   GLY B N    1 
ATOM   183  C CA   . GLY A 1 60  ? 122.492 124.636 143.416 1.00 17.70  ? 60   GLY B CA   1 
ATOM   184  C C    . GLY A 1 60  ? 121.845 123.831 144.527 1.00 20.40  ? 60   GLY B C    1 
ATOM   185  O O    . GLY A 1 60  ? 122.278 123.896 145.680 1.00 24.86  ? 60   GLY B O    1 
ATOM   186  N N    . ARG A 1 61  ? 120.788 123.076 144.212 1.00 28.37  ? 61   ARG B N    1 
ATOM   187  C CA   . ARG A 1 61  ? 120.116 122.329 145.271 1.00 38.53  ? 61   ARG B CA   1 
ATOM   188  C C    . ARG A 1 61  ? 120.928 121.103 145.673 1.00 37.42  ? 61   ARG B C    1 
ATOM   189  O O    . ARG A 1 61  ? 120.875 120.666 146.828 1.00 31.05  ? 61   ARG B O    1 
ATOM   190  C CB   . ARG A 1 61  ? 118.724 121.908 144.801 1.00 28.94  ? 61   ARG B CB   1 
ATOM   191  C CG   . ARG A 1 61  ? 117.583 122.757 145.319 1.00 35.74  ? 61   ARG B CG   1 
ATOM   192  C CD   . ARG A 1 61  ? 116.255 122.213 144.816 1.00 36.71  ? 61   ARG B CD   1 
ATOM   193  N NE   . ARG A 1 61  ? 115.780 121.084 145.605 1.00 32.73  ? 61   ARG B NE   1 
ATOM   194  C CZ   . ARG A 1 61  ? 114.521 120.669 145.634 1.00 37.28  ? 61   ARG B CZ   1 
ATOM   195  N NH1  . ARG A 1 61  ? 113.579 121.270 144.928 1.00 38.48  ? 61   ARG B NH1  1 
ATOM   196  N NH2  . ARG A 1 61  ? 114.200 119.622 146.389 1.00 40.40  ? 61   ARG B NH2  1 
ATOM   197  N N    . ALA A 1 62  ? 121.667 120.518 144.722 1.00 35.91  ? 62   ALA B N    1 
ATOM   198  C CA   . ALA A 1 62  ? 122.582 119.413 145.017 1.00 25.74  ? 62   ALA B CA   1 
ATOM   199  C C    . ALA A 1 62  ? 123.661 119.804 146.030 1.00 30.50  ? 62   ALA B C    1 
ATOM   200  O O    . ALA A 1 62  ? 124.419 118.943 146.492 1.00 36.47  ? 62   ALA B O    1 
ATOM   201  C CB   . ALA A 1 62  ? 123.218 118.896 143.729 1.00 25.26  ? 62   ALA B CB   1 
ATOM   202  N N    . ASN A 1 63  ? 123.794 121.109 146.312 1.00 32.32  ? 63   ASN B N    1 
ATOM   203  C CA   . ASN A 1 63  ? 124.564 121.725 147.395 1.00 25.51  ? 63   ASN B CA   1 
ATOM   204  C C    . ASN A 1 63  ? 126.029 121.836 146.988 1.00 22.10  ? 63   ASN B C    1 
ATOM   205  O O    . ASN A 1 63  ? 126.895 122.137 147.816 1.00 27.41  ? 63   ASN B O    1 
ATOM   206  C CB   . ASN A 1 63  ? 124.413 120.974 148.723 1.00 23.71  ? 63   ASN B CB   1 
ATOM   207  C CG   . ASN A 1 63  ? 123.997 121.884 149.859 1.00 38.30  ? 63   ASN B CG   1 
ATOM   208  O OD1  . ASN A 1 63  ? 124.678 122.862 150.167 1.00 37.21  ? 63   ASN B OD1  1 
ATOM   209  N ND2  . ASN A 1 63  ? 122.871 121.568 150.489 1.00 39.52  ? 63   ASN B ND2  1 
ATOM   210  N N    . VAL A 1 64  ? 126.302 121.566 145.710 1.00 17.70  ? 64   VAL B N    1 
ATOM   211  C CA   . VAL A 1 64  ? 127.658 121.593 145.165 1.00 20.51  ? 64   VAL B CA   1 
ATOM   212  C C    . VAL A 1 64  ? 128.269 122.986 145.278 1.00 27.71  ? 64   VAL B C    1 
ATOM   213  O O    . VAL A 1 64  ? 129.423 123.141 145.693 1.00 40.33  ? 64   VAL B O    1 
ATOM   214  C CB   . VAL A 1 64  ? 127.665 121.095 143.708 1.00 14.11  ? 64   VAL B CB   1 
ATOM   215  C CG1  . VAL A 1 64  ? 129.058 120.652 143.311 1.00 18.33  ? 64   VAL B CG1  1 
ATOM   216  C CG2  . VAL A 1 64  ? 126.700 119.946 143.543 1.00 24.36  ? 64   VAL B CG2  1 
ATOM   217  N N    . ILE A 1 65  ? 127.506 124.016 144.917 1.00 16.59  ? 65   ILE B N    1 
ATOM   218  C CA   . ILE A 1 65  ? 127.948 125.409 144.968 1.00 17.59  ? 65   ILE B CA   1 
ATOM   219  C C    . ILE A 1 65  ? 126.957 126.189 145.822 1.00 27.88  ? 65   ILE B C    1 
ATOM   220  O O    . ILE A 1 65  ? 125.907 126.628 145.338 1.00 42.49  ? 65   ILE B O    1 
ATOM   221  C CB   . ILE A 1 65  ? 128.072 126.030 143.571 1.00 8.30   ? 65   ILE B CB   1 
ATOM   222  C CG1  . ILE A 1 65  ? 128.514 124.991 142.539 1.00 14.07  ? 65   ILE B CG1  1 
ATOM   223  C CG2  . ILE A 1 65  ? 129.008 127.218 143.593 1.00 15.35  ? 65   ILE B CG2  1 
ATOM   224  C CD1  . ILE A 1 65  ? 128.304 125.424 141.111 1.00 21.56  ? 65   ILE B CD1  1 
ATOM   225  N N    . THR A 1 66  ? 127.291 126.353 147.101 1.00 18.42  ? 66   THR B N    1 
ATOM   226  C CA   . THR A 1 66  ? 126.415 126.964 148.091 1.00 18.40  ? 66   THR B CA   1 
ATOM   227  C C    . THR A 1 66  ? 126.192 128.451 147.794 1.00 20.21  ? 66   THR B C    1 
ATOM   228  O O    . THR A 1 66  ? 126.711 129.015 146.827 1.00 36.13  ? 66   THR B O    1 
ATOM   229  C CB   . THR A 1 66  ? 126.989 126.771 149.493 1.00 30.48  ? 66   THR B CB   1 
ATOM   230  O OG1  . THR A 1 66  ? 126.005 127.138 150.468 1.00 41.58  ? 66   THR B OG1  1 
ATOM   231  C CG2  . THR A 1 66  ? 128.227 127.628 149.688 1.00 28.36  ? 66   THR B CG2  1 
ATOM   232  N N    . SER A 1 67  ? 125.390 129.081 148.658 1.00 23.63  ? 67   SER B N    1 
ATOM   233  C CA   . SER A 1 67  ? 125.005 130.481 148.484 1.00 33.19  ? 67   SER B CA   1 
ATOM   234  C C    . SER A 1 67  ? 126.198 131.432 148.533 1.00 34.15  ? 67   SER B C    1 
ATOM   235  O O    . SER A 1 67  ? 126.271 132.379 147.741 1.00 31.59  ? 67   SER B O    1 
ATOM   236  C CB   . SER A 1 67  ? 123.978 130.868 149.547 1.00 31.36  ? 67   SER B CB   1 
ATOM   237  O OG   . SER A 1 67  ? 122.961 129.888 149.652 1.00 34.84  ? 67   SER B OG   1 
ATOM   238  N N    . THR A 1 68  ? 127.133 131.214 149.463 1.00 31.87  ? 68   THR B N    1 
ATOM   239  C CA   . THR A 1 68  ? 128.302 132.087 149.559 1.00 27.01  ? 68   THR B CA   1 
ATOM   240  C C    . THR A 1 68  ? 129.194 131.984 148.326 1.00 28.80  ? 68   THR B C    1 
ATOM   241  O O    . THR A 1 68  ? 129.656 133.004 147.801 1.00 35.58  ? 68   THR B O    1 
ATOM   242  C CB   . THR A 1 68  ? 129.099 131.755 150.820 1.00 27.06  ? 68   THR B CB   1 
ATOM   243  O OG1  . THR A 1 68  ? 128.228 131.785 151.957 1.00 35.95  ? 68   THR B OG1  1 
ATOM   244  C CG2  . THR A 1 68  ? 130.218 132.762 151.024 1.00 26.49  ? 68   THR B CG2  1 
ATOM   245  N N    . GLN A 1 69  ? 129.459 130.763 147.860 1.00 29.01  ? 69   GLN B N    1 
ATOM   246  C CA   . GLN A 1 69  ? 130.280 130.570 146.668 1.00 22.01  ? 69   GLN B CA   1 
ATOM   247  C C    . GLN A 1 69  ? 129.619 131.165 145.427 1.00 21.01  ? 69   GLN B C    1 
ATOM   248  O O    . GLN A 1 69  ? 130.304 131.672 144.531 1.00 31.45  ? 69   GLN B O    1 
ATOM   249  C CB   . GLN A 1 69  ? 130.583 129.086 146.468 1.00 23.56  ? 69   GLN B CB   1 
ATOM   250  C CG   . GLN A 1 69  ? 131.567 128.516 147.477 1.00 29.38  ? 69   GLN B CG   1 
ATOM   251  C CD   . GLN A 1 69  ? 131.459 127.011 147.622 1.00 38.20  ? 69   GLN B CD   1 
ATOM   252  O OE1  . GLN A 1 69  ? 131.107 126.502 148.684 1.00 40.63  ? 69   GLN B OE1  1 
ATOM   253  N NE2  . GLN A 1 69  ? 131.769 126.291 146.551 1.00 28.64  ? 69   GLN B NE2  1 
ATOM   254  N N    . ALA A 1 70  ? 128.288 131.089 145.353 1.00 17.81  ? 70   ALA B N    1 
ATOM   255  C CA   . ALA A 1 70  ? 127.529 131.640 144.230 1.00 14.47  ? 70   ALA B CA   1 
ATOM   256  C C    . ALA A 1 70  ? 127.727 133.141 144.049 1.00 15.71  ? 70   ALA B C    1 
ATOM   257  O O    . ALA A 1 70  ? 127.610 133.641 142.924 1.00 23.30  ? 70   ALA B O    1 
ATOM   258  C CB   . ALA A 1 70  ? 126.045 131.341 144.414 1.00 17.46  ? 70   ALA B CB   1 
ATOM   259  N N    . LYS A 1 71  ? 127.991 133.878 145.130 1.00 9.69   ? 71   LYS B N    1 
ATOM   260  C CA   . LYS A 1 71  ? 128.227 135.316 145.016 1.00 16.47  ? 71   LYS B CA   1 
ATOM   261  C C    . LYS A 1 71  ? 129.441 135.639 144.152 1.00 16.85  ? 71   LYS B C    1 
ATOM   262  O O    . LYS A 1 71  ? 129.470 136.688 143.500 1.00 26.85  ? 71   LYS B O    1 
ATOM   263  C CB   . LYS A 1 71  ? 128.395 135.938 146.402 1.00 18.44  ? 71   LYS B CB   1 
ATOM   264  C CG   . LYS A 1 71  ? 127.384 135.460 147.423 1.00 23.58  ? 71   LYS B CG   1 
ATOM   265  C CD   . LYS A 1 71  ? 126.187 136.390 147.487 1.00 22.05  ? 71   LYS B CD   1 
ATOM   266  C CE   . LYS A 1 71  ? 125.019 135.737 148.207 1.00 27.80  ? 71   LYS B CE   1 
ATOM   267  N NZ   . LYS A 1 71  ? 124.356 134.702 147.365 1.00 28.34  ? 71   LYS B NZ   1 
ATOM   268  N N    . GLY A 1 72  ? 130.451 134.770 144.139 1.00 11.99  ? 72   GLY B N    1 
ATOM   269  C CA   . GLY A 1 72  ? 131.613 135.018 143.301 1.00 7.03   ? 72   GLY B CA   1 
ATOM   270  C C    . GLY A 1 72  ? 131.316 134.931 141.816 1.00 12.77  ? 72   GLY B C    1 
ATOM   271  O O    . GLY A 1 72  ? 131.844 135.718 141.026 1.00 20.53  ? 72   GLY B O    1 
ATOM   272  N N    . LEU A 1 73  ? 130.492 133.963 141.411 1.00 13.41  ? 73   LEU B N    1 
ATOM   273  C CA   . LEU A 1 73  ? 130.096 133.882 140.009 1.00 13.45  ? 73   LEU B CA   1 
ATOM   274  C C    . LEU A 1 73  ? 129.235 135.066 139.584 1.00 16.26  ? 73   LEU B C    1 
ATOM   275  O O    . LEU A 1 73  ? 129.243 135.438 138.406 1.00 11.34  ? 73   LEU B O    1 
ATOM   276  C CB   . LEU A 1 73  ? 129.352 132.567 139.764 1.00 6.84   ? 73   LEU B CB   1 
ATOM   277  C CG   . LEU A 1 73  ? 128.881 132.193 138.358 1.00 0.00   ? 73   LEU B CG   1 
ATOM   278  C CD1  . LEU A 1 73  ? 130.017 132.181 137.370 1.00 9.38   ? 73   LEU B CD1  1 
ATOM   279  C CD2  . LEU A 1 73  ? 128.200 130.836 138.390 1.00 9.24   ? 73   LEU B CD2  1 
ATOM   280  N N    . GLY A 1 74  ? 128.493 135.674 140.512 1.00 12.61  ? 74   GLY B N    1 
ATOM   281  C CA   . GLY A 1 74  ? 127.770 136.889 140.174 1.00 9.46   ? 74   GLY B CA   1 
ATOM   282  C C    . GLY A 1 74  ? 128.669 138.091 139.946 1.00 18.53  ? 74   GLY B C    1 
ATOM   283  O O    . GLY A 1 74  ? 128.425 138.893 139.041 1.00 27.36  ? 74   GLY B O    1 
ATOM   284  N N    . ASN A 1 75  ? 129.707 138.244 140.774 1.00 14.21  ? 75   ASN B N    1 
ATOM   285  C CA   . ASN A 1 75  ? 130.612 139.386 140.654 1.00 10.20  ? 75   ASN B CA   1 
ATOM   286  C C    . ASN A 1 75  ? 131.386 139.379 139.340 1.00 18.59  ? 75   ASN B C    1 
ATOM   287  O O    . ASN A 1 75  ? 131.626 140.439 138.752 1.00 27.30  ? 75   ASN B O    1 
ATOM   288  C CB   . ASN A 1 75  ? 131.574 139.421 141.840 1.00 8.66   ? 75   ASN B CB   1 
ATOM   289  C CG   . ASN A 1 75  ? 130.952 140.043 143.072 1.00 16.71  ? 75   ASN B CG   1 
ATOM   290  O OD1  . ASN A 1 75  ? 130.034 140.855 142.972 1.00 29.36  ? 75   ASN B OD1  1 
ATOM   291  N ND2  . ASN A 1 75  ? 131.456 139.673 144.242 1.00 13.93  ? 75   ASN B ND2  1 
ATOM   292  N N    . PHE A 1 76  ? 131.797 138.198 138.874 1.00 0.04   ? 76   PHE B N    1 
ATOM   293  C CA   . PHE A 1 76  ? 132.493 138.093 137.594 1.00 0.00   ? 76   PHE B CA   1 
ATOM   294  C C    . PHE A 1 76  ? 131.583 138.477 136.432 1.00 9.83   ? 76   PHE B C    1 
ATOM   295  O O    . PHE A 1 76  ? 131.980 139.243 135.548 1.00 16.79  ? 76   PHE B O    1 
ATOM   296  C CB   . PHE A 1 76  ? 133.050 136.676 137.423 1.00 13.80  ? 76   PHE B CB   1 
ATOM   297  C CG   . PHE A 1 76  ? 133.254 136.257 135.990 1.00 17.02  ? 76   PHE B CG   1 
ATOM   298  C CD1  . PHE A 1 76  ? 134.190 136.896 135.190 1.00 9.45   ? 76   PHE B CD1  1 
ATOM   299  C CD2  . PHE A 1 76  ? 132.531 135.208 135.452 1.00 13.81  ? 76   PHE B CD2  1 
ATOM   300  C CE1  . PHE A 1 76  ? 134.384 136.507 133.881 1.00 4.32   ? 76   PHE B CE1  1 
ATOM   301  C CE2  . PHE A 1 76  ? 132.723 134.816 134.143 1.00 5.68   ? 76   PHE B CE2  1 
ATOM   302  C CZ   . PHE A 1 76  ? 133.651 135.467 133.357 1.00 7.81   ? 76   PHE B CZ   1 
ATOM   303  N N    . VAL A 1 77  ? 130.360 137.946 136.412 1.00 20.65  ? 77   VAL B N    1 
ATOM   304  C CA   . VAL A 1 77  ? 129.461 138.171 135.283 1.00 14.61  ? 77   VAL B CA   1 
ATOM   305  C C    . VAL A 1 77  ? 128.979 139.618 135.249 1.00 21.00  ? 77   VAL B C    1 
ATOM   306  O O    . VAL A 1 77  ? 128.973 140.263 134.194 1.00 27.03  ? 77   VAL B O    1 
ATOM   307  C CB   . VAL A 1 77  ? 128.281 137.184 135.346 1.00 5.38   ? 77   VAL B CB   1 
ATOM   308  C CG1  . VAL A 1 77  ? 127.214 137.551 134.334 1.00 9.40   ? 77   VAL B CG1  1 
ATOM   309  C CG2  . VAL A 1 77  ? 128.767 135.767 135.122 1.00 10.50  ? 77   VAL B CG2  1 
ATOM   310  N N    . SER A 1 78  ? 128.577 140.152 136.399 1.00 5.82   ? 78   SER B N    1 
ATOM   311  C CA   . SER A 1 78  ? 127.946 141.466 136.463 1.00 0.70   ? 78   SER B CA   1 
ATOM   312  C C    . SER A 1 78  ? 128.915 142.632 136.294 1.00 21.20  ? 78   SER B C    1 
ATOM   313  O O    . SER A 1 78  ? 128.498 143.732 135.920 1.00 40.12  ? 78   SER B O    1 
ATOM   314  C CB   . SER A 1 78  ? 127.199 141.620 137.788 1.00 13.80  ? 78   SER B CB   1 
ATOM   315  O OG   . SER A 1 78  ? 126.121 140.706 137.871 1.00 22.57  ? 78   SER B OG   1 
ATOM   316  N N    . ARG A 1 79  ? 130.204 142.416 136.566 1.00 14.56  ? 79   ARG B N    1 
ATOM   317  C CA   . ARG A 1 79  ? 131.155 143.523 136.527 1.00 10.86  ? 79   ARG B CA   1 
ATOM   318  C C    . ARG A 1 79  ? 132.228 143.376 135.454 1.00 11.92  ? 79   ARG B C    1 
ATOM   319  O O    . ARG A 1 79  ? 132.875 144.370 135.110 1.00 20.33  ? 79   ARG B O    1 
ATOM   320  C CB   . ARG A 1 79  ? 131.812 143.691 137.897 1.00 6.75   ? 79   ARG B CB   1 
ATOM   321  C CG   . ARG A 1 79  ? 130.841 144.120 138.982 1.00 15.53  ? 79   ARG B CG   1 
ATOM   322  C CD   . ARG A 1 79  ? 131.384 143.840 140.377 1.00 21.18  ? 79   ARG B CD   1 
ATOM   323  N NE   . ARG A 1 79  ? 131.041 144.889 141.332 1.00 29.65  ? 79   ARG B NE   1 
ATOM   324  C CZ   . ARG A 1 79  ? 129.827 145.106 141.824 1.00 33.53  ? 79   ARG B CZ   1 
ATOM   325  N NH1  . ARG A 1 79  ? 128.790 144.363 141.471 1.00 24.80  ? 79   ARG B NH1  1 
ATOM   326  N NH2  . ARG A 1 79  ? 129.647 146.099 142.690 1.00 29.49  ? 79   ARG B NH2  1 
ATOM   327  N N    . PHE A 1 80  ? 132.455 142.173 134.935 1.00 16.47  ? 80   PHE B N    1 
ATOM   328  C CA   . PHE A 1 80  ? 133.509 141.946 133.951 1.00 12.39  ? 80   PHE B CA   1 
ATOM   329  C C    . PHE A 1 80  ? 132.993 141.527 132.584 1.00 7.91   ? 80   PHE B C    1 
ATOM   330  O O    . PHE A 1 80  ? 133.337 142.166 131.583 1.00 13.40  ? 80   PHE B O    1 
ATOM   331  C CB   . PHE A 1 80  ? 134.519 140.927 134.492 1.00 10.41  ? 80   PHE B CB   1 
ATOM   332  C CG   . PHE A 1 80  ? 135.431 141.501 135.534 1.00 4.42   ? 80   PHE B CG   1 
ATOM   333  C CD1  . PHE A 1 80  ? 136.366 142.460 135.188 1.00 9.93   ? 80   PHE B CD1  1 
ATOM   334  C CD2  . PHE A 1 80  ? 135.330 141.116 136.858 1.00 12.77  ? 80   PHE B CD2  1 
ATOM   335  C CE1  . PHE A 1 80  ? 137.200 143.008 136.137 1.00 19.69  ? 80   PHE B CE1  1 
ATOM   336  C CE2  . PHE A 1 80  ? 136.162 141.663 137.813 1.00 16.66  ? 80   PHE B CE2  1 
ATOM   337  C CZ   . PHE A 1 80  ? 137.095 142.613 137.449 1.00 22.83  ? 80   PHE B CZ   1 
ATOM   338  N N    . ALA A 1 81  ? 132.188 140.466 132.498 1.00 0.00   ? 81   ALA B N    1 
ATOM   339  C CA   . ALA A 1 81  ? 131.759 139.984 131.188 1.00 9.86   ? 81   ALA B CA   1 
ATOM   340  C C    . ALA A 1 81  ? 130.746 140.927 130.550 1.00 18.36  ? 81   ALA B C    1 
ATOM   341  O O    . ALA A 1 81  ? 130.853 141.238 129.358 1.00 21.17  ? 81   ALA B O    1 
ATOM   342  C CB   . ALA A 1 81  ? 131.177 138.577 131.312 1.00 15.60  ? 81   ALA B CB   1 
ATOM   343  N N    . LEU A 1 82  ? 129.746 141.372 131.311 1.00 17.48  ? 82   LEU B N    1 
ATOM   344  C CA   . LEU A 1 82  ? 128.717 142.251 130.755 1.00 15.07  ? 82   LEU B CA   1 
ATOM   345  C C    . LEU A 1 82  ? 129.271 143.596 130.278 1.00 24.41  ? 82   LEU B C    1 
ATOM   346  O O    . LEU A 1 82  ? 128.909 144.015 129.166 1.00 26.13  ? 82   LEU B O    1 
ATOM   347  C CB   . LEU A 1 82  ? 127.569 142.418 131.760 1.00 23.59  ? 82   LEU B CB   1 
ATOM   348  C CG   . LEU A 1 82  ? 126.441 143.371 131.355 1.00 34.36  ? 82   LEU B CG   1 
ATOM   349  C CD1  . LEU A 1 82  ? 125.809 142.939 130.040 1.00 24.20  ? 82   LEU B CD1  1 
ATOM   350  C CD2  . LEU A 1 82  ? 125.393 143.470 132.452 1.00 31.85  ? 82   LEU B CD2  1 
ATOM   351  N N    . PRO A 1 83  ? 130.095 144.335 131.048 1.00 27.31  ? 83   PRO B N    1 
ATOM   352  C CA   . PRO A 1 83  ? 130.634 145.607 130.523 1.00 18.22  ? 83   PRO B CA   1 
ATOM   353  C C    . PRO A 1 83  ? 131.440 145.473 129.240 1.00 18.72  ? 83   PRO B C    1 
ATOM   354  O O    . PRO A 1 83  ? 131.457 146.410 128.432 1.00 23.36  ? 83   PRO B O    1 
ATOM   355  C CB   . PRO A 1 83  ? 131.521 146.100 131.670 1.00 19.40  ? 83   PRO B CB   1 
ATOM   356  C CG   . PRO A 1 83  ? 130.873 145.582 132.862 1.00 26.53  ? 83   PRO B CG   1 
ATOM   357  C CD   . PRO A 1 83  ? 130.418 144.206 132.485 1.00 21.93  ? 83   PRO B CD   1 
ATOM   358  N N    . ALA A 1 84  ? 132.111 144.342 129.026 1.00 22.45  ? 84   ALA B N    1 
ATOM   359  C CA   . ALA A 1 84  ? 132.887 144.143 127.807 1.00 19.92  ? 84   ALA B CA   1 
ATOM   360  C C    . ALA A 1 84  ? 132.003 143.831 126.607 1.00 21.39  ? 84   ALA B C    1 
ATOM   361  O O    . ALA A 1 84  ? 132.380 144.141 125.472 1.00 27.41  ? 84   ALA B O    1 
ATOM   362  C CB   . ALA A 1 84  ? 133.906 143.023 128.009 1.00 24.46  ? 84   ALA B CB   1 
ATOM   363  N N    . LEU A 1 85  ? 130.843 143.214 126.830 1.00 24.29  ? 85   LEU B N    1 
ATOM   364  C CA   . LEU A 1 85  ? 129.941 142.898 125.727 1.00 25.33  ? 85   LEU B CA   1 
ATOM   365  C C    . LEU A 1 85  ? 129.314 144.160 125.144 1.00 27.24  ? 85   LEU B C    1 
ATOM   366  O O    . LEU A 1 85  ? 129.275 144.334 123.920 1.00 19.98  ? 85   LEU B O    1 
ATOM   367  C CB   . LEU A 1 85  ? 128.856 141.929 126.199 1.00 22.40  ? 85   LEU B CB   1 
ATOM   368  C CG   . LEU A 1 85  ? 127.808 141.549 125.153 1.00 21.44  ? 85   LEU B CG   1 
ATOM   369  C CD1  . LEU A 1 85  ? 128.451 140.780 124.014 1.00 19.03  ? 85   LEU B CD1  1 
ATOM   370  C CD2  . LEU A 1 85  ? 126.683 140.746 125.780 1.00 23.76  ? 85   LEU B CD2  1 
ATOM   371  N N    . LEU A 1 86  ? 128.794 145.040 126.004 1.00 25.45  ? 86   LEU B N    1 
ATOM   372  C CA   . LEU A 1 86  ? 128.180 146.277 125.526 1.00 20.55  ? 86   LEU B CA   1 
ATOM   373  C C    . LEU A 1 86  ? 129.197 147.193 124.854 1.00 34.23  ? 86   LEU B C    1 
ATOM   374  O O    . LEU A 1 86  ? 128.889 147.831 123.841 1.00 40.59  ? 86   LEU B O    1 
ATOM   375  C CB   . LEU A 1 86  ? 127.495 147.004 126.681 1.00 14.31  ? 86   LEU B CB   1 
ATOM   376  C CG   . LEU A 1 86  ? 126.491 146.200 127.504 1.00 27.33  ? 86   LEU B CG   1 
ATOM   377  C CD1  . LEU A 1 86  ? 125.828 147.087 128.541 1.00 37.93  ? 86   LEU B CD1  1 
ATOM   378  C CD2  . LEU A 1 86  ? 125.452 145.570 126.598 1.00 22.46  ? 86   LEU B CD2  1 
ATOM   379  N N    . PHE A 1 87  ? 130.405 147.291 125.419 1.00 36.60  ? 87   PHE B N    1 
ATOM   380  C CA   . PHE A 1 87  ? 131.399 148.231 124.906 1.00 28.16  ? 87   PHE B CA   1 
ATOM   381  C C    . PHE A 1 87  ? 131.828 147.882 123.485 1.00 26.49  ? 87   PHE B C    1 
ATOM   382  O O    . PHE A 1 87  ? 131.985 148.773 122.645 1.00 35.04  ? 87   PHE B O    1 
ATOM   383  C CB   . PHE A 1 87  ? 132.613 148.255 125.835 1.00 33.30  ? 87   PHE B CB   1 
ATOM   384  C CG   . PHE A 1 87  ? 133.763 149.065 125.314 1.00 31.73  ? 87   PHE B CG   1 
ATOM   385  C CD1  . PHE A 1 87  ? 133.673 150.441 125.220 1.00 36.04  ? 87   PHE B CD1  1 
ATOM   386  C CD2  . PHE A 1 87  ? 134.935 148.446 124.911 1.00 30.85  ? 87   PHE B CD2  1 
ATOM   387  C CE1  . PHE A 1 87  ? 134.731 151.188 124.738 1.00 38.42  ? 87   PHE B CE1  1 
ATOM   388  C CE2  . PHE A 1 87  ? 135.995 149.188 124.427 1.00 37.17  ? 87   PHE B CE2  1 
ATOM   389  C CZ   . PHE A 1 87  ? 135.893 150.561 124.341 1.00 39.07  ? 87   PHE B CZ   1 
ATOM   390  N N    . LYS A 1 88  ? 132.027 146.593 123.205 1.00 20.71  ? 88   LYS B N    1 
ATOM   391  C CA   . LYS A 1 88  ? 132.433 146.156 121.871 1.00 17.87  ? 88   LYS B CA   1 
ATOM   392  C C    . LYS A 1 88  ? 131.368 146.471 120.825 1.00 28.56  ? 88   LYS B C    1 
ATOM   393  O O    . LYS A 1 88  ? 131.664 147.046 119.772 1.00 28.67  ? 88   LYS B O    1 
ATOM   394  C CB   . LYS A 1 88  ? 132.745 144.660 121.887 1.00 22.83  ? 88   LYS B CB   1 
ATOM   395  C CG   . LYS A 1 88  ? 133.142 144.092 120.533 1.00 27.22  ? 88   LYS B CG   1 
ATOM   396  C CD   . LYS A 1 88  ? 133.177 142.569 120.546 1.00 27.70  ? 88   LYS B CD   1 
ATOM   397  C CE   . LYS A 1 88  ? 131.946 141.980 121.217 1.00 27.17  ? 88   LYS B CE   1 
ATOM   398  N NZ   . LYS A 1 88  ? 131.981 140.493 121.243 1.00 28.07  ? 88   LYS B NZ   1 
ATOM   399  N N    . ASN A 1 89  ? 130.121 146.078 121.099 1.00 31.39  ? 89   ASN B N    1 
ATOM   400  C CA   . ASN A 1 89  ? 129.033 146.220 120.133 1.00 22.54  ? 89   ASN B CA   1 
ATOM   401  C C    . ASN A 1 89  ? 128.715 147.679 119.818 1.00 27.35  ? 89   ASN B C    1 
ATOM   402  O O    . ASN A 1 89  ? 128.478 148.027 118.657 1.00 31.60  ? 89   ASN B O    1 
ATOM   403  C CB   . ASN A 1 89  ? 127.789 145.504 120.653 1.00 14.32  ? 89   ASN B CB   1 
ATOM   404  C CG   . ASN A 1 89  ? 127.908 143.999 120.561 1.00 18.99  ? 89   ASN B CG   1 
ATOM   405  O OD1  . ASN A 1 89  ? 127.793 143.420 119.482 1.00 21.26  ? 89   ASN B OD1  1 
ATOM   406  N ND2  . ASN A 1 89  ? 128.146 143.356 121.696 1.00 22.64  ? 89   ASN B ND2  1 
ATOM   407  N N    . MET A 1 90  ? 128.748 148.552 120.828 1.00 21.47  ? 90   MET B N    1 
ATOM   408  C CA   . MET A 1 90  ? 128.482 149.975 120.617 1.00 26.70  ? 90   MET B CA   1 
ATOM   409  C C    . MET A 1 90  ? 129.512 150.634 119.705 1.00 36.82  ? 90   MET B C    1 
ATOM   410  O O    . MET A 1 90  ? 129.183 151.581 118.980 1.00 31.20  ? 90   MET B O    1 
ATOM   411  C CB   . MET A 1 90  ? 128.434 150.696 121.964 1.00 18.07  ? 90   MET B CB   1 
ATOM   412  C CG   . MET A 1 90  ? 127.265 151.647 122.117 1.00 32.06  ? 90   MET B CG   1 
ATOM   413  S SD   . MET A 1 90  ? 125.673 150.809 122.046 1.00 26.72  ? 90   MET B SD   1 
ATOM   414  C CE   . MET A 1 90  ? 125.879 149.590 123.339 1.00 25.26  ? 90   MET B CE   1 
ATOM   415  N N    . VAL A 1 91  ? 130.753 150.156 119.733 1.00 41.93  ? 91   VAL B N    1 
ATOM   416  C CA   . VAL A 1 91  ? 131.797 150.668 118.848 1.00 33.86  ? 91   VAL B CA   1 
ATOM   417  C C    . VAL A 1 91  ? 131.471 150.385 117.383 1.00 32.59  ? 91   VAL B C    1 
ATOM   418  O O    . VAL A 1 91  ? 131.678 151.240 116.514 1.00 44.66  ? 91   VAL B O    1 
ATOM   419  C CB   . VAL A 1 91  ? 133.168 150.091 119.253 1.00 39.69  ? 91   VAL B CB   1 
ATOM   420  C CG1  . VAL A 1 91  ? 134.222 150.397 118.203 1.00 41.95  ? 91   VAL B CG1  1 
ATOM   421  C CG2  . VAL A 1 91  ? 133.602 150.670 120.585 1.00 37.88  ? 91   VAL B CG2  1 
ATOM   422  N N    . VAL A 1 92  ? 130.918 149.205 117.084 1.00 35.45  ? 92   VAL B N    1 
ATOM   423  C CA   . VAL A 1 92  ? 130.740 148.807 115.687 1.00 40.68  ? 92   VAL B CA   1 
ATOM   424  C C    . VAL A 1 92  ? 129.410 149.255 115.071 1.00 48.22  ? 92   VAL B C    1 
ATOM   425  O O    . VAL A 1 92  ? 129.225 149.099 113.853 1.00 52.14  ? 92   VAL B O    1 
ATOM   426  C CB   . VAL A 1 92  ? 130.935 147.272 115.637 1.00 38.44  ? 92   VAL B CB   1 
ATOM   427  C CG1  . VAL A 1 92  ? 131.068 146.726 114.212 1.00 42.43  ? 92   VAL B CG1  1 
ATOM   428  C CG2  . VAL A 1 92  ? 132.139 146.868 116.472 1.00 40.68  ? 92   VAL B CG2  1 
ATOM   429  N N    . LEU A 1 93  ? 128.492 149.838 115.850 1.00 50.18  ? 93   LEU B N    1 
ATOM   430  C CA   . LEU A 1 93  ? 127.195 150.224 115.292 1.00 47.27  ? 93   LEU B CA   1 
ATOM   431  C C    . LEU A 1 93  ? 127.369 151.286 114.211 1.00 54.16  ? 93   LEU B C    1 
ATOM   432  O O    . LEU A 1 93  ? 128.163 152.219 114.357 1.00 55.96  ? 93   LEU B O    1 
ATOM   433  C CB   . LEU A 1 93  ? 126.266 150.755 116.386 1.00 46.33  ? 93   LEU B CB   1 
ATOM   434  C CG   . LEU A 1 93  ? 125.152 149.903 117.003 1.00 46.76  ? 93   LEU B CG   1 
ATOM   435  C CD1  . LEU A 1 93  ? 125.622 148.565 117.510 1.00 48.26  ? 93   LEU B CD1  1 
ATOM   436  C CD2  . LEU A 1 93  ? 124.518 150.696 118.136 1.00 45.62  ? 93   LEU B CD2  1 
ATOM   437  N N    . ASN A 1 94  ? 126.624 151.138 113.117 1.00 66.20  ? 94   ASN B N    1 
ATOM   438  C CA   . ASN A 1 94  ? 126.667 152.077 111.997 1.00 69.67  ? 94   ASN B CA   1 
ATOM   439  C C    . ASN A 1 94  ? 125.389 152.919 112.040 1.00 67.64  ? 94   ASN B C    1 
ATOM   440  O O    . ASN A 1 94  ? 124.312 152.453 111.657 1.00 64.87  ? 94   ASN B O    1 
ATOM   441  C CB   . ASN A 1 94  ? 126.878 151.305 110.687 1.00 70.21  ? 94   ASN B CB   1 
ATOM   442  C CG   . ASN A 1 94  ? 126.334 152.015 109.455 1.00 69.85  ? 94   ASN B CG   1 
ATOM   443  O OD1  . ASN A 1 94  ? 125.142 151.968 109.152 1.00 66.32  ? 94   ASN B OD1  1 
ATOM   444  N ND2  . ASN A 1 94  ? 127.226 152.681 108.731 1.00 69.61  ? 94   ASN B ND2  1 
ATOM   445  N N    . PHE A 1 95  ? 125.484 154.120 112.611 1.00 64.17  ? 95   PHE B N    1 
ATOM   446  C CA   . PHE A 1 95  ? 124.318 154.987 112.771 1.00 61.88  ? 95   PHE B CA   1 
ATOM   447  C C    . PHE A 1 95  ? 123.774 155.571 111.467 1.00 66.56  ? 95   PHE B C    1 
ATOM   448  O O    . PHE A 1 95  ? 123.655 156.795 111.348 1.00 64.53  ? 95   PHE B O    1 
ATOM   449  C CB   . PHE A 1 95  ? 124.639 156.132 113.737 1.00 60.38  ? 95   PHE B CB   1 
ATOM   450  C CG   . PHE A 1 95  ? 124.823 155.695 115.162 1.00 59.86  ? 95   PHE B CG   1 
ATOM   451  C CD1  . PHE A 1 95  ? 126.087 155.531 115.701 1.00 66.05  ? 95   PHE B CD1  1 
ATOM   452  C CD2  . PHE A 1 95  ? 123.722 155.467 115.969 1.00 59.98  ? 95   PHE B CD2  1 
ATOM   453  C CE1  . PHE A 1 95  ? 126.248 155.136 117.018 1.00 65.04  ? 95   PHE B CE1  1 
ATOM   454  C CE2  . PHE A 1 95  ? 123.876 155.074 117.283 1.00 64.69  ? 95   PHE B CE2  1 
ATOM   455  C CZ   . PHE A 1 95  ? 125.141 154.908 117.809 1.00 65.92  ? 95   PHE B CZ   1 
ATOM   456  N N    . SER A 1 96  ? 123.443 154.731 110.485 1.00 72.95  ? 96   SER B N    1 
ATOM   457  C CA   . SER A 1 96  ? 122.875 155.223 109.229 1.00 70.91  ? 96   SER B CA   1 
ATOM   458  C C    . SER A 1 96  ? 121.727 154.378 108.701 1.00 72.19  ? 96   SER B C    1 
ATOM   459  O O    . SER A 1 96  ? 120.921 154.890 107.918 1.00 75.09  ? 96   SER B O    1 
ATOM   460  C CB   . SER A 1 96  ? 123.951 155.331 108.142 1.00 69.39  ? 96   SER B CB   1 
ATOM   461  O OG   . SER A 1 96  ? 124.760 154.175 108.100 1.00 71.43  ? 96   SER B OG   1 
ATOM   462  N N    . ASN A 1 97  ? 121.622 153.110 109.094 1.00 66.43  ? 97   ASN B N    1 
ATOM   463  C CA   . ASN A 1 97  ? 120.632 152.172 108.581 1.00 66.93  ? 97   ASN B CA   1 
ATOM   464  C C    . ASN A 1 97  ? 119.568 151.851 109.620 1.00 71.25  ? 97   ASN B C    1 
ATOM   465  O O    . ASN A 1 97  ? 118.748 150.953 109.403 1.00 72.17  ? 97   ASN B O    1 
ATOM   466  C CB   . ASN A 1 97  ? 121.310 150.886 108.105 1.00 66.82  ? 97   ASN B CB   1 
ATOM   467  C CG   . ASN A 1 97  ? 121.919 150.094 109.243 1.00 65.31  ? 97   ASN B CG   1 
ATOM   468  O OD1  . ASN A 1 97  ? 122.665 150.632 110.060 1.00 64.58  ? 97   ASN B OD1  1 
ATOM   469  N ND2  . ASN A 1 97  ? 121.601 148.807 109.304 1.00 63.41  ? 97   ASN B ND2  1 
ATOM   470  N N    . VAL A 1 98  ? 119.564 152.566 110.739 1.00 67.00  ? 98   VAL B N    1 
ATOM   471  C CA   . VAL A 1 98  ? 118.627 152.309 111.825 1.00 65.59  ? 98   VAL B CA   1 
ATOM   472  C C    . VAL A 1 98  ? 117.289 152.980 111.539 1.00 64.16  ? 98   VAL B C    1 
ATOM   473  O O    . VAL A 1 98  ? 117.214 154.184 111.264 1.00 64.51  ? 98   VAL B O    1 
ATOM   474  C CB   . VAL A 1 98  ? 119.218 152.758 113.174 1.00 62.35  ? 98   VAL B CB   1 
ATOM   475  C CG1  . VAL A 1 98  ? 120.356 151.836 113.571 1.00 62.52  ? 98   VAL B CG1  1 
ATOM   476  C CG2  . VAL A 1 98  ? 119.735 154.187 113.103 1.00 57.67  ? 98   VAL B CG2  1 
ATOM   477  N N    . ASP A 1 99  ? 116.230 152.175 111.557 1.00 58.14  ? 99   ASP B N    1 
ATOM   478  C CA   . ASP A 1 99  ? 114.861 152.641 111.366 1.00 59.48  ? 99   ASP B CA   1 
ATOM   479  C C    . ASP A 1 99  ? 114.395 153.249 112.681 1.00 63.64  ? 99   ASP B C    1 
ATOM   480  O O    . ASP A 1 99  ? 114.098 152.532 113.641 1.00 70.23  ? 99   ASP B O    1 
ATOM   481  C CB   . ASP A 1 99  ? 113.952 151.498 110.925 1.00 57.85  ? 99   ASP B CB   1 
ATOM   482  C CG   . ASP A 1 99  ? 114.419 150.848 109.639 1.00 59.86  ? 99   ASP B CG   1 
ATOM   483  O OD1  . ASP A 1 99  ? 115.207 151.479 108.903 1.00 63.45  ? 99   ASP B OD1  1 
ATOM   484  O OD2  . ASP A 1 99  ? 114.000 149.704 109.365 1.00 62.18  ? 99   ASP B OD2  1 
ATOM   485  N N    . TRP A 1 100 ? 114.333 154.579 112.718 1.00 55.74  ? 100  TRP B N    1 
ATOM   486  C CA   . TRP A 1 100 ? 113.991 155.302 113.934 1.00 51.80  ? 100  TRP B CA   1 
ATOM   487  C C    . TRP A 1 100 ? 112.517 155.175 114.291 1.00 51.99  ? 100  TRP B C    1 
ATOM   488  O O    . TRP A 1 100 ? 112.155 155.425 115.446 1.00 54.56  ? 100  TRP B O    1 
ATOM   489  C CB   . TRP A 1 100 ? 114.358 156.778 113.764 1.00 53.94  ? 100  TRP B CB   1 
ATOM   490  C CG   . TRP A 1 100 ? 115.837 157.028 113.657 1.00 61.66  ? 100  TRP B CG   1 
ATOM   491  C CD1  . TRP A 1 100 ? 116.557 157.163 112.505 1.00 62.25  ? 100  TRP B CD1  1 
ATOM   492  C CD2  . TRP A 1 100 ? 116.770 157.205 114.733 1.00 61.91  ? 100  TRP B CD2  1 
ATOM   493  N NE1  . TRP A 1 100 ? 117.879 157.392 112.795 1.00 59.76  ? 100  TRP B NE1  1 
ATOM   494  C CE2  . TRP A 1 100 ? 118.036 157.424 114.155 1.00 58.50  ? 100  TRP B CE2  1 
ATOM   495  C CE3  . TRP A 1 100 ? 116.659 157.193 116.125 1.00 59.85  ? 100  TRP B CE3  1 
ATOM   496  C CZ2  . TRP A 1 100 ? 119.181 157.629 114.920 1.00 58.30  ? 100  TRP B CZ2  1 
ATOM   497  C CZ3  . TRP A 1 100 ? 117.799 157.397 116.884 1.00 57.77  ? 100  TRP B CZ3  1 
ATOM   498  C CH2  . TRP A 1 100 ? 119.042 157.610 116.280 1.00 58.72  ? 100  TRP B CH2  1 
ATOM   499  N N    . SER A 1 101 ? 111.656 154.827 113.328 1.00 48.62  ? 101  SER B N    1 
ATOM   500  C CA   . SER A 1 101 ? 110.250 154.595 113.648 1.00 55.00  ? 101  SER B CA   1 
ATOM   501  C C    . SER A 1 101 ? 110.087 153.446 114.639 1.00 57.16  ? 101  SER B C    1 
ATOM   502  O O    . SER A 1 101 ? 109.278 153.535 115.571 1.00 61.51  ? 101  SER B O    1 
ATOM   503  C CB   . SER A 1 101 ? 109.462 154.314 112.369 1.00 52.75  ? 101  SER B CB   1 
ATOM   504  O OG   . SER A 1 101 ? 108.084 154.585 112.548 1.00 55.71  ? 101  SER B OG   1 
ATOM   505  N N    . PHE A 1 102 ? 110.831 152.351 114.446 1.00 40.16  ? 102  PHE B N    1 
ATOM   506  C CA   . PHE A 1 102 ? 110.789 151.252 115.407 1.00 37.22  ? 102  PHE B CA   1 
ATOM   507  C C    . PHE A 1 102 ? 111.341 151.683 116.759 1.00 42.63  ? 102  PHE B C    1 
ATOM   508  O O    . PHE A 1 102 ? 110.786 151.340 117.806 1.00 46.11  ? 102  PHE B O    1 
ATOM   509  C CB   . PHE A 1 102 ? 111.563 150.047 114.870 1.00 31.60  ? 102  PHE B CB   1 
ATOM   510  C CG   . PHE A 1 102 ? 111.562 148.864 115.797 1.00 35.71  ? 102  PHE B CG   1 
ATOM   511  C CD1  . PHE A 1 102 ? 110.467 148.024 115.872 1.00 41.85  ? 102  PHE B CD1  1 
ATOM   512  C CD2  . PHE A 1 102 ? 112.666 148.585 116.587 1.00 37.82  ? 102  PHE B CD2  1 
ATOM   513  C CE1  . PHE A 1 102 ? 110.468 146.934 116.722 1.00 46.23  ? 102  PHE B CE1  1 
ATOM   514  C CE2  . PHE A 1 102 ? 112.672 147.498 117.440 1.00 36.22  ? 102  PHE B CE2  1 
ATOM   515  C CZ   . PHE A 1 102 ? 111.573 146.672 117.507 1.00 36.30  ? 102  PHE B CZ   1 
ATOM   516  N N    . LEU A 1 103 ? 112.422 152.461 116.748 1.00 44.34  ? 103  LEU B N    1 
ATOM   517  C CA   . LEU A 1 103 ? 113.071 152.898 117.979 1.00 40.95  ? 103  LEU B CA   1 
ATOM   518  C C    . LEU A 1 103 ? 112.165 153.793 118.814 1.00 40.70  ? 103  LEU B C    1 
ATOM   519  O O    . LEU A 1 103 ? 112.078 153.638 120.038 1.00 45.40  ? 103  LEU B O    1 
ATOM   520  C CB   . LEU A 1 103 ? 114.377 153.621 117.659 1.00 35.57  ? 103  LEU B CB   1 
ATOM   521  C CG   . LEU A 1 103 ? 115.368 153.665 118.821 1.00 34.17  ? 103  LEU B CG   1 
ATOM   522  C CD1  . LEU A 1 103 ? 115.798 152.267 119.183 1.00 34.25  ? 103  LEU B CD1  1 
ATOM   523  C CD2  . LEU A 1 103 ? 116.574 154.508 118.488 1.00 47.68  ? 103  LEU B CD2  1 
ATOM   524  N N    . TYR A 1 104 ? 111.491 154.741 118.166 1.00 47.44  ? 104  TYR B N    1 
ATOM   525  C CA   . TYR A 1 104 ? 110.595 155.658 118.863 1.00 49.91  ? 104  TYR B CA   1 
ATOM   526  C C    . TYR A 1 104 ? 109.360 154.966 119.440 1.00 50.06  ? 104  TYR B C    1 
ATOM   527  O O    . TYR A 1 104 ? 108.873 155.357 120.507 1.00 50.69  ? 104  TYR B O    1 
ATOM   528  C CB   . TYR A 1 104 ? 110.133 156.735 117.875 1.00 45.93  ? 104  TYR B CB   1 
ATOM   529  C CG   . TYR A 1 104 ? 111.167 157.758 117.438 1.00 47.34  ? 104  TYR B CG   1 
ATOM   530  C CD1  . TYR A 1 104 ? 110.823 158.766 116.545 1.00 44.68  ? 104  TYR B CD1  1 
ATOM   531  C CD2  . TYR A 1 104 ? 112.474 157.721 117.907 1.00 51.36  ? 104  TYR B CD2  1 
ATOM   532  C CE1  . TYR A 1 104 ? 111.749 159.702 116.129 1.00 47.82  ? 104  TYR B CE1  1 
ATOM   533  C CE2  . TYR A 1 104 ? 113.408 158.656 117.497 1.00 47.38  ? 104  TYR B CE2  1 
ATOM   534  C CZ   . TYR A 1 104 ? 113.039 159.644 116.609 1.00 49.90  ? 104  TYR B CZ   1 
ATOM   535  O OH   . TYR A 1 104 ? 113.962 160.578 116.197 1.00 51.65  ? 104  TYR B OH   1 
ATOM   536  N N    . SER A 1 105 ? 108.830 153.951 118.754 1.00 35.84  ? 105  SER B N    1 
ATOM   537  C CA   . SER A 1 105 ? 107.636 153.251 119.235 1.00 33.89  ? 105  SER B CA   1 
ATOM   538  C C    . SER A 1 105 ? 107.826 152.517 120.566 1.00 41.64  ? 105  SER B C    1 
ATOM   539  O O    . SER A 1 105 ? 106.975 152.615 121.455 1.00 48.15  ? 105  SER B O    1 
ATOM   540  C CB   . SER A 1 105 ? 107.156 152.278 118.162 1.00 31.22  ? 105  SER B CB   1 
ATOM   541  O OG   . SER A 1 105 ? 106.775 152.971 116.988 1.00 37.12  ? 105  SER B OG   1 
ATOM   542  N N    . ILE A 1 106 ? 108.926 151.782 120.732 1.00 28.92  ? 106  ILE B N    1 
ATOM   543  C CA   . ILE A 1 106 ? 109.159 151.058 121.989 1.00 26.15  ? 106  ILE B CA   1 
ATOM   544  C C    . ILE A 1 106 ? 109.364 151.992 123.183 1.00 30.23  ? 106  ILE B C    1 
ATOM   545  O O    . ILE A 1 106 ? 108.804 151.754 124.262 1.00 24.31  ? 106  ILE B O    1 
ATOM   546  C CB   . ILE A 1 106 ? 110.303 150.025 121.866 1.00 13.57  ? 106  ILE B CB   1 
ATOM   547  C CG1  . ILE A 1 106 ? 109.957 148.814 120.969 1.00 19.47  ? 106  ILE B CG1  1 
ATOM   548  C CG2  . ILE A 1 106 ? 110.690 149.490 123.228 1.00 29.89  ? 106  ILE B CG2  1 
ATOM   549  C CD1  . ILE A 1 106 ? 109.658 149.011 119.517 1.00 31.34  ? 106  ILE B CD1  1 
ATOM   550  N N    . LEU A 1 107 ? 110.140 153.066 123.023 1.00 36.52  ? 107  LEU B N    1 
ATOM   551  C CA   . LEU A 1 107 ? 110.382 153.954 124.160 1.00 32.95  ? 107  LEU B CA   1 
ATOM   552  C C    . LEU A 1 107 ? 109.106 154.621 124.664 1.00 29.55  ? 107  LEU B C    1 
ATOM   553  O O    . LEU A 1 107 ? 108.923 154.776 125.877 1.00 22.66  ? 107  LEU B O    1 
ATOM   554  C CB   . LEU A 1 107 ? 111.402 155.019 123.764 1.00 38.74  ? 107  LEU B CB   1 
ATOM   555  C CG   . LEU A 1 107 ? 112.855 154.579 123.599 1.00 40.38  ? 107  LEU B CG   1 
ATOM   556  C CD1  . LEU A 1 107 ? 113.675 155.749 123.090 1.00 35.06  ? 107  LEU B CD1  1 
ATOM   557  C CD2  . LEU A 1 107 ? 113.420 154.040 124.905 1.00 29.38  ? 107  LEU B CD2  1 
ATOM   558  N N    . ILE A 1 108 ? 108.226 155.046 123.757 1.00 38.54  ? 108  ILE B N    1 
ATOM   559  C CA   . ILE A 1 108 ? 106.954 155.626 124.182 1.00 40.29  ? 108  ILE B CA   1 
ATOM   560  C C    . ILE A 1 108 ? 106.101 154.579 124.902 1.00 46.18  ? 108  ILE B C    1 
ATOM   561  O O    . ILE A 1 108 ? 105.484 154.860 125.938 1.00 49.66  ? 108  ILE B O    1 
ATOM   562  C CB   . ILE A 1 108 ? 106.224 156.248 122.979 1.00 34.82  ? 108  ILE B CB   1 
ATOM   563  C CG1  . ILE A 1 108 ? 106.919 157.536 122.556 1.00 43.74  ? 108  ILE B CG1  1 
ATOM   564  C CG2  . ILE A 1 108 ? 104.826 156.666 123.372 1.00 36.06  ? 108  ILE B CG2  1 
ATOM   565  C CD1  . ILE A 1 108 ? 106.472 158.043 121.205 1.00 37.31  ? 108  ILE B CD1  1 
ATOM   566  N N    . ALA A 1 109 ? 106.074 153.351 124.367 1.00 32.06  ? 109  ALA B N    1 
ATOM   567  C CA   . ALA A 1 109 ? 105.326 152.240 124.958 1.00 28.35  ? 109  ALA B CA   1 
ATOM   568  C C    . ALA A 1 109 ? 105.811 151.884 126.357 1.00 36.07  ? 109  ALA B C    1 
ATOM   569  O O    . ALA A 1 109 ? 104.999 151.642 127.258 1.00 30.40  ? 109  ALA B O    1 
ATOM   570  C CB   . ALA A 1 109 ? 105.410 151.014 124.051 1.00 17.18  ? 109  ALA B CB   1 
ATOM   571  N N    . LYS A 1 110 ? 107.129 151.827 126.552 1.00 37.92  ? 110  LYS B N    1 
ATOM   572  C CA   . LYS A 1 110 ? 107.683 151.526 127.870 1.00 22.14  ? 110  LYS B CA   1 
ATOM   573  C C    . LYS A 1 110 ? 107.335 152.614 128.876 1.00 28.21  ? 110  LYS B C    1 
ATOM   574  O O    . LYS A 1 110 ? 107.113 152.328 130.058 1.00 16.57  ? 110  LYS B O    1 
ATOM   575  C CB   . LYS A 1 110 ? 109.196 151.341 127.773 1.00 21.97  ? 110  LYS B CB   1 
ATOM   576  C CG   . LYS A 1 110 ? 109.611 149.944 127.350 1.00 24.31  ? 110  LYS B CG   1 
ATOM   577  C CD   . LYS A 1 110 ? 111.082 149.701 127.606 1.00 23.77  ? 110  LYS B CD   1 
ATOM   578  C CE   . LYS A 1 110 ? 111.452 148.262 127.326 1.00 20.79  ? 110  LYS B CE   1 
ATOM   579  N NZ   . LYS A 1 110 ? 112.881 148.144 126.942 1.00 25.42  ? 110  LYS B NZ   1 
ATOM   580  N N    . ALA A 1 111 ? 107.319 153.870 128.429 1.00 44.71  ? 111  ALA B N    1 
ATOM   581  C CA   . ALA A 1 111 ? 106.976 154.983 129.308 1.00 40.55  ? 111  ALA B CA   1 
ATOM   582  C C    . ALA A 1 111 ? 105.547 154.866 129.828 1.00 33.00  ? 111  ALA B C    1 
ATOM   583  O O    . ALA A 1 111 ? 105.296 155.087 131.017 1.00 39.98  ? 111  ALA B O    1 
ATOM   584  C CB   . ALA A 1 111 ? 107.172 156.308 128.574 1.00 44.32  ? 111  ALA B CB   1 
ATOM   585  N N    . SER A 1 112 ? 104.600 154.508 128.953 1.00 21.26  ? 112  SER B N    1 
ATOM   586  C CA   . SER A 1 112 ? 103.197 154.406 129.353 1.00 36.00  ? 112  SER B CA   1 
ATOM   587  C C    . SER A 1 112 ? 102.989 153.336 130.422 1.00 47.64  ? 112  SER B C    1 
ATOM   588  O O    . SER A 1 112 ? 102.241 153.554 131.382 1.00 47.74  ? 112  SER B O    1 
ATOM   589  C CB   . SER A 1 112 ? 102.327 154.117 128.131 1.00 29.17  ? 112  SER B CB   1 
ATOM   590  O OG   . SER A 1 112 ? 102.454 155.147 127.167 1.00 33.44  ? 112  SER B OG   1 
ATOM   591  N N    . VAL A 1 113 ? 103.618 152.170 130.260 1.00 42.09  ? 113  VAL B N    1 
ATOM   592  C CA   . VAL A 1 113 ? 103.499 151.096 131.247 1.00 34.72  ? 113  VAL B CA   1 
ATOM   593  C C    . VAL A 1 113 ? 104.043 151.563 132.594 1.00 31.95  ? 113  VAL B C    1 
ATOM   594  O O    . VAL A 1 113 ? 103.455 151.298 133.650 1.00 23.62  ? 113  VAL B O    1 
ATOM   595  C CB   . VAL A 1 113 ? 104.208 149.825 130.740 1.00 27.56  ? 113  VAL B CB   1 
ATOM   596  C CG1  . VAL A 1 113 ? 104.568 148.897 131.889 1.00 24.42  ? 113  VAL B CG1  1 
ATOM   597  C CG2  . VAL A 1 113 ? 103.330 149.103 129.736 1.00 16.96  ? 113  VAL B CG2  1 
ATOM   598  N N    . PHE A 1 114 ? 105.163 152.290 132.567 1.00 40.80  ? 114  PHE B N    1 
ATOM   599  C CA   . PHE A 1 114 ? 105.771 152.844 133.775 1.00 36.44  ? 114  PHE B CA   1 
ATOM   600  C C    . PHE A 1 114 ? 104.821 153.824 134.460 1.00 37.66  ? 114  PHE B C    1 
ATOM   601  O O    . PHE A 1 114 ? 104.733 153.859 135.693 1.00 39.91  ? 114  PHE B O    1 
ATOM   602  C CB   . PHE A 1 114 ? 107.089 153.529 133.389 1.00 43.29  ? 114  PHE B CB   1 
ATOM   603  C CG   . PHE A 1 114 ? 107.931 154.000 134.552 1.00 45.25  ? 114  PHE B CG   1 
ATOM   604  C CD1  . PHE A 1 114 ? 107.661 155.194 135.205 1.00 43.31  ? 114  PHE B CD1  1 
ATOM   605  C CD2  . PHE A 1 114 ? 109.047 153.274 134.938 1.00 39.51  ? 114  PHE B CD2  1 
ATOM   606  C CE1  . PHE A 1 114 ? 108.453 155.621 136.253 1.00 45.25  ? 114  PHE B CE1  1 
ATOM   607  C CE2  . PHE A 1 114 ? 109.845 153.701 135.980 1.00 37.31  ? 114  PHE B CE2  1 
ATOM   608  C CZ   . PHE A 1 114 ? 109.546 154.875 136.639 1.00 45.48  ? 114  PHE B CZ   1 
ATOM   609  N N    . PHE A 1 115 ? 104.110 154.632 133.670 1.00 54.07  ? 115  PHE B N    1 
ATOM   610  C CA   . PHE A 1 115 ? 103.248 155.685 134.205 1.00 57.70  ? 115  PHE B CA   1 
ATOM   611  C C    . PHE A 1 115 ? 102.054 155.122 134.971 1.00 55.54  ? 115  PHE B C    1 
ATOM   612  O O    . PHE A 1 115 ? 101.727 155.609 136.059 1.00 57.02  ? 115  PHE B O    1 
ATOM   613  C CB   . PHE A 1 115 ? 102.755 156.581 133.066 1.00 50.26  ? 115  PHE B CB   1 
ATOM   614  C CG   . PHE A 1 115 ? 103.561 157.837 132.874 1.00 51.52  ? 115  PHE B CG   1 
ATOM   615  C CD1  . PHE A 1 115 ? 104.838 157.790 132.342 1.00 52.19  ? 115  PHE B CD1  1 
ATOM   616  C CD2  . PHE A 1 115 ? 103.024 159.072 133.200 1.00 59.81  ? 115  PHE B CD2  1 
ATOM   617  C CE1  . PHE A 1 115 ? 105.574 158.945 132.156 1.00 54.06  ? 115  PHE B CE1  1 
ATOM   618  C CE2  . PHE A 1 115 ? 103.754 160.232 133.016 1.00 62.75  ? 115  PHE B CE2  1 
ATOM   619  C CZ   . PHE A 1 115 ? 105.031 160.167 132.493 1.00 56.39  ? 115  PHE B CZ   1 
ATOM   620  N N    . ILE A 1 116 ? 101.394 154.098 134.426 1.00 45.99  ? 116  ILE B N    1 
ATOM   621  C CA   . ILE A 1 116 ? 100.176 153.570 135.040 1.00 53.67  ? 116  ILE B CA   1 
ATOM   622  C C    . ILE A 1 116 ? 100.470 152.848 136.353 1.00 58.48  ? 116  ILE B C    1 
ATOM   623  O O    . ILE A 1 116 ? 99.698  152.955 137.312 1.00 60.85  ? 116  ILE B O    1 
ATOM   624  C CB   . ILE A 1 116 ? 99.439  152.653 134.046 1.00 55.05  ? 116  ILE B CB   1 
ATOM   625  C CG1  . ILE A 1 116 ? 99.267  153.350 132.695 1.00 54.81  ? 116  ILE B CG1  1 
ATOM   626  C CG2  . ILE A 1 116 ? 98.085  152.239 134.597 1.00 55.17  ? 116  ILE B CG2  1 
ATOM   627  C CD1  . ILE A 1 116 ? 98.477  154.636 132.765 1.00 56.12  ? 116  ILE B CD1  1 
ATOM   628  N N    . VAL A 1 117 ? 101.585 152.120 136.433 1.00 55.36  ? 117  VAL B N    1 
ATOM   629  C CA   . VAL A 1 117 ? 101.895 151.369 137.650 1.00 48.84  ? 117  VAL B CA   1 
ATOM   630  C C    . VAL A 1 117 ? 102.228 152.305 138.810 1.00 44.98  ? 117  VAL B C    1 
ATOM   631  O O    . VAL A 1 117 ? 101.793 152.081 139.946 1.00 45.12  ? 117  VAL B O    1 
ATOM   632  C CB   . VAL A 1 117 ? 103.029 150.361 137.385 1.00 47.16  ? 117  VAL B CB   1 
ATOM   633  C CG1  . VAL A 1 117 ? 103.296 149.525 138.623 1.00 39.35  ? 117  VAL B CG1  1 
ATOM   634  C CG2  . VAL A 1 117 ? 102.662 149.458 136.221 1.00 47.99  ? 117  VAL B CG2  1 
ATOM   635  N N    . CYS A 1 118 ? 103.003 153.361 138.551 1.00 57.13  ? 118  CYS B N    1 
ATOM   636  C CA   . CYS A 1 118 ? 103.370 154.297 139.613 1.00 59.79  ? 118  CYS B CA   1 
ATOM   637  C C    . CYS A 1 118 ? 102.163 155.064 140.145 1.00 59.89  ? 118  CYS B C    1 
ATOM   638  O O    . CYS A 1 118 ? 102.070 155.315 141.352 1.00 52.93  ? 118  CYS B O    1 
ATOM   639  C CB   . CYS A 1 118 ? 104.438 155.270 139.113 1.00 59.94  ? 118  CYS B CB   1 
ATOM   640  S SG   . CYS A 1 118 ? 105.512 155.923 140.413 1.00 52.43  ? 118  CYS B SG   1 
ATOM   641  N N    . VAL A 1 119 ? 101.249 155.474 139.259 1.00 68.60  ? 119  VAL B N    1 
ATOM   642  C CA   . VAL A 1 119 ? 100.113 156.303 139.667 1.00 68.28  ? 119  VAL B CA   1 
ATOM   643  C C    . VAL A 1 119 ? 99.217  155.552 140.649 1.00 65.06  ? 119  VAL B C    1 
ATOM   644  O O    . VAL A 1 119 ? 98.874  156.066 141.720 1.00 68.18  ? 119  VAL B O    1 
ATOM   645  C CB   . VAL A 1 119 ? 99.328  156.777 138.429 1.00 65.24  ? 119  VAL B CB   1 
ATOM   646  C CG1  . VAL A 1 119 ? 97.930  157.231 138.815 1.00 66.01  ? 119  VAL B CG1  1 
ATOM   647  C CG2  . VAL A 1 119 ? 100.075 157.900 137.729 1.00 62.60  ? 119  VAL B CG2  1 
ATOM   648  N N    . LEU A 1 120 ? 98.832  154.321 140.303 1.00 65.21  ? 120  LEU B N    1 
ATOM   649  C CA   . LEU A 1 120 ? 97.939  153.550 141.166 1.00 67.55  ? 120  LEU B CA   1 
ATOM   650  C C    . LEU A 1 120 ? 98.632  153.085 142.441 1.00 73.20  ? 120  LEU B C    1 
ATOM   651  O O    . LEU A 1 120 ? 97.963  152.867 143.457 1.00 77.59  ? 120  LEU B O    1 
ATOM   652  C CB   . LEU A 1 120 ? 97.352  152.353 140.417 1.00 69.97  ? 120  LEU B CB   1 
ATOM   653  C CG   . LEU A 1 120 ? 96.947  152.540 138.956 1.00 74.64  ? 120  LEU B CG   1 
ATOM   654  C CD1  . LEU A 1 120 ? 97.013  151.219 138.212 1.00 73.96  ? 120  LEU B CD1  1 
ATOM   655  C CD2  . LEU A 1 120 ? 95.555  153.139 138.861 1.00 73.67  ? 120  LEU B CD2  1 
ATOM   656  N N    . THR A 1 121 ? 99.957  152.910 142.405 1.00 67.13  ? 121  THR B N    1 
ATOM   657  C CA   . THR A 1 121 ? 100.689 152.517 143.607 1.00 66.63  ? 121  THR B CA   1 
ATOM   658  C C    . THR A 1 121 ? 100.579 153.570 144.704 1.00 68.08  ? 121  THR B C    1 
ATOM   659  O O    . THR A 1 121 ? 100.405 153.231 145.880 1.00 64.55  ? 121  THR B O    1 
ATOM   660  C CB   . THR A 1 121 ? 102.157 152.264 143.261 1.00 63.05  ? 121  THR B CB   1 
ATOM   661  O OG1  . THR A 1 121 ? 102.242 151.284 142.221 1.00 66.81  ? 121  THR B OG1  1 
ATOM   662  C CG2  . THR A 1 121 ? 102.914 151.761 144.478 1.00 57.76  ? 121  THR B CG2  1 
ATOM   663  N N    . LEU A 1 122 ? 100.673 154.851 144.343 1.00 77.48  ? 122  LEU B N    1 
ATOM   664  C CA   . LEU A 1 122 ? 100.563 155.907 145.345 1.00 77.03  ? 122  LEU B CA   1 
ATOM   665  C C    . LEU A 1 122 ? 99.163  155.968 145.946 1.00 74.34  ? 122  LEU B C    1 
ATOM   666  O O    . LEU A 1 122 ? 99.007  156.300 147.127 1.00 75.60  ? 122  LEU B O    1 
ATOM   667  C CB   . LEU A 1 122 ? 100.936 157.256 144.731 1.00 74.04  ? 122  LEU B CB   1 
ATOM   668  C CG   . LEU A 1 122 ? 102.390 157.416 144.281 1.00 71.89  ? 122  LEU B CG   1 
ATOM   669  C CD1  . LEU A 1 122 ? 102.495 158.412 143.135 1.00 69.74  ? 122  LEU B CD1  1 
ATOM   670  C CD2  . LEU A 1 122 ? 103.268 157.837 145.450 1.00 70.28  ? 122  LEU B CD2  1 
ATOM   671  N N    . LEU A 1 123 ? 98.141  155.653 145.150 1.00 72.33  ? 123  LEU B N    1 
ATOM   672  C CA   . LEU A 1 123 ? 96.754  155.795 145.579 1.00 73.01  ? 123  LEU B CA   1 
ATOM   673  C C    . LEU A 1 123 ? 96.312  154.696 146.540 1.00 77.47  ? 123  LEU B C    1 
ATOM   674  O O    . LEU A 1 123 ? 95.423  154.929 147.366 1.00 80.91  ? 123  LEU B O    1 
ATOM   675  C CB   . LEU A 1 123 ? 95.831  155.813 144.358 1.00 75.41  ? 123  LEU B CB   1 
ATOM   676  C CG   . LEU A 1 123 ? 95.300  157.173 143.895 1.00 78.74  ? 123  LEU B CG   1 
ATOM   677  C CD1  . LEU A 1 123 ? 96.431  158.175 143.706 1.00 74.92  ? 123  LEU B CD1  1 
ATOM   678  C CD2  . LEU A 1 123 ? 94.493  157.025 142.614 1.00 77.95  ? 123  LEU B CD2  1 
ATOM   679  N N    . VAL A 1 124 ? 96.907  153.506 146.457 1.00 79.10  ? 124  VAL B N    1 
ATOM   680  C CA   . VAL A 1 124 ? 96.403  152.347 147.175 1.00 81.68  ? 124  VAL B CA   1 
ATOM   681  C C    . VAL A 1 124 ? 97.313  151.906 148.322 1.00 81.35  ? 124  VAL B C    1 
ATOM   682  O O    . VAL A 1 124 ? 96.803  151.471 149.362 1.00 80.10  ? 124  VAL B O    1 
ATOM   683  C CB   . VAL A 1 124 ? 96.159  151.182 146.190 1.00 79.21  ? 124  VAL B CB   1 
ATOM   684  C CG1  . VAL A 1 124 ? 95.513  149.992 146.886 1.00 81.20  ? 124  VAL B CG1  1 
ATOM   685  C CG2  . VAL A 1 124 ? 95.303  151.646 145.021 1.00 76.77  ? 124  VAL B CG2  1 
ATOM   686  N N    . ALA A 1 125 ? 98.634  152.016 148.171 1.00 90.49  ? 125  ALA B N    1 
ATOM   687  C CA   . ALA A 1 125 ? 99.581  151.514 149.164 1.00 91.27  ? 125  ALA B CA   1 
ATOM   688  C C    . ALA A 1 125 ? 99.373  152.163 150.530 1.00 92.71  ? 125  ALA B C    1 
ATOM   689  O O    . ALA A 1 125 ? 98.882  153.290 150.642 1.00 92.96  ? 125  ALA B O    1 
ATOM   690  C CB   . ALA A 1 125 ? 101.017 151.748 148.697 1.00 90.05  ? 125  ALA B CB   1 
ATOM   691  N N    . SER A 1 126 ? 99.738  151.419 151.576 1.00 104.81 ? 126  SER B N    1 
ATOM   692  C CA   . SER A 1 126 ? 99.565  151.885 152.943 1.00 108.11 ? 126  SER B CA   1 
ATOM   693  C C    . SER A 1 126 ? 100.443 153.113 153.191 1.00 104.93 ? 126  SER B C    1 
ATOM   694  O O    . SER A 1 126 ? 101.516 153.243 152.595 1.00 102.94 ? 126  SER B O    1 
ATOM   695  C CB   . SER A 1 126 ? 99.928  150.765 153.920 1.00 106.34 ? 126  SER B CB   1 
ATOM   696  O OG   . SER A 1 126 ? 99.830  151.177 155.271 1.00 104.85 ? 126  SER B OG   1 
ATOM   697  N N    . PRO A 1 127 ? 99.991  154.046 154.041 1.00 101.92 ? 127  PRO B N    1 
ATOM   698  C CA   . PRO A 1 127 ? 100.779 155.274 154.260 1.00 102.85 ? 127  PRO B CA   1 
ATOM   699  C C    . PRO A 1 127 ? 102.189 155.060 154.790 1.00 105.31 ? 127  PRO B C    1 
ATOM   700  O O    . PRO A 1 127 ? 103.092 155.811 154.399 1.00 104.97 ? 127  PRO B O    1 
ATOM   701  C CB   . PRO A 1 127 ? 99.917  156.064 155.257 1.00 104.48 ? 127  PRO B CB   1 
ATOM   702  C CG   . PRO A 1 127 ? 98.537  155.535 155.070 1.00 104.15 ? 127  PRO B CG   1 
ATOM   703  C CD   . PRO A 1 127 ? 98.698  154.088 154.747 1.00 101.97 ? 127  PRO B CD   1 
ATOM   704  N N    . ASP A 1 128 ? 102.417 154.087 155.679 1.00 109.93 ? 128  ASP B N    1 
ATOM   705  C CA   . ASP A 1 128 ? 103.773 153.928 156.199 1.00 109.35 ? 128  ASP B CA   1 
ATOM   706  C C    . ASP A 1 128 ? 104.727 153.397 155.136 1.00 108.80 ? 128  ASP B C    1 
ATOM   707  O O    . ASP A 1 128 ? 105.928 153.688 155.181 1.00 108.62 ? 128  ASP B O    1 
ATOM   708  C CB   . ASP A 1 128 ? 103.762 153.003 157.415 1.00 110.25 ? 128  ASP B CB   1 
ATOM   709  C CG   . ASP A 1 128 ? 104.869 153.323 158.401 1.00 109.76 ? 128  ASP B CG   1 
ATOM   710  O OD1  . ASP A 1 128 ? 105.538 154.363 158.226 1.00 106.82 ? 128  ASP B OD1  1 
ATOM   711  O OD2  . ASP A 1 128 ? 105.069 152.536 159.349 1.00 111.08 ? 128  ASP B OD2  1 
ATOM   712  N N    . SER A 1 129 ? 104.214 152.625 154.179 1.00 108.24 ? 129  SER B N    1 
ATOM   713  C CA   . SER A 1 129 ? 105.035 152.038 153.122 1.00 108.84 ? 129  SER B CA   1 
ATOM   714  C C    . SER A 1 129 ? 104.384 152.373 151.786 1.00 107.47 ? 129  SER B C    1 
ATOM   715  O O    . SER A 1 129 ? 103.633 151.553 151.250 1.00 107.05 ? 129  SER B O    1 
ATOM   716  C CB   . SER A 1 129 ? 105.186 150.532 153.316 1.00 107.86 ? 129  SER B CB   1 
ATOM   717  O OG   . SER A 1 129 ? 103.937 149.872 153.214 1.00 108.56 ? 129  SER B OG   1 
ATOM   718  N N    . ARG A 1 130 ? 104.664 153.557 151.245 1.00 91.92  ? 130  ARG B N    1 
ATOM   719  C CA   . ARG A 1 130 ? 104.064 153.962 149.978 1.00 92.11  ? 130  ARG B CA   1 
ATOM   720  C C    . ARG A 1 130 ? 105.110 154.457 148.985 1.00 90.87  ? 130  ARG B C    1 
ATOM   721  O O    . ARG A 1 130 ? 104.993 154.211 147.781 1.00 91.57  ? 130  ARG B O    1 
ATOM   722  C CB   . ARG A 1 130 ? 102.946 154.987 150.196 1.00 93.37  ? 130  ARG B CB   1 
ATOM   723  C CG   . ARG A 1 130 ? 103.211 156.138 151.145 1.00 92.30  ? 130  ARG B CG   1 
ATOM   724  C CD   . ARG A 1 130 ? 101.956 157.010 151.190 1.00 91.97  ? 130  ARG B CD   1 
ATOM   725  N NE   . ARG A 1 130 ? 101.990 158.031 152.229 1.00 92.99  ? 130  ARG B NE   1 
ATOM   726  C CZ   . ARG A 1 130 ? 102.273 159.307 152.013 1.00 93.02  ? 130  ARG B CZ   1 
ATOM   727  N NH1  . ARG A 1 130 ? 102.550 159.758 150.802 1.00 93.51  ? 130  ARG B NH1  1 
ATOM   728  N NH2  . ARG A 1 130 ? 102.276 160.153 153.039 1.00 92.09  ? 130  ARG B NH2  1 
ATOM   729  N N    . PHE A 1 131 ? 106.130 155.161 149.473 1.00 89.16  ? 131  PHE B N    1 
ATOM   730  C CA   . PHE A 1 131 ? 107.142 155.714 148.578 1.00 92.29  ? 131  PHE B CA   1 
ATOM   731  C C    . PHE A 1 131 ? 108.087 154.625 148.076 1.00 92.68  ? 131  PHE B C    1 
ATOM   732  O O    . PHE A 1 131 ? 108.541 154.672 146.926 1.00 89.96  ? 131  PHE B O    1 
ATOM   733  C CB   . PHE A 1 131 ? 107.950 156.796 149.292 1.00 88.62  ? 131  PHE B CB   1 
ATOM   734  C CG   . PHE A 1 131 ? 107.147 157.978 149.756 1.00 87.90  ? 131  PHE B CG   1 
ATOM   735  C CD1  . PHE A 1 131 ? 106.940 159.061 148.920 1.00 87.64  ? 131  PHE B CD1  1 
ATOM   736  C CD2  . PHE A 1 131 ? 106.643 158.028 151.047 1.00 88.02  ? 131  PHE B CD2  1 
ATOM   737  C CE1  . PHE A 1 131 ? 106.219 160.159 149.350 1.00 88.70  ? 131  PHE B CE1  1 
ATOM   738  C CE2  . PHE A 1 131 ? 105.921 159.126 151.485 1.00 89.46  ? 131  PHE B CE2  1 
ATOM   739  C CZ   . PHE A 1 131 ? 105.712 160.193 150.633 1.00 88.93  ? 131  PHE B CZ   1 
ATOM   740  N N    . SER A 1 132 ? 108.406 153.651 148.933 1.00 89.31  ? 132  SER B N    1 
ATOM   741  C CA   . SER A 1 132 ? 109.265 152.530 148.548 1.00 85.81  ? 132  SER B CA   1 
ATOM   742  C C    . SER A 1 132 ? 108.665 151.702 147.412 1.00 82.98  ? 132  SER B C    1 
ATOM   743  O O    . SER A 1 132 ? 109.384 151.282 146.498 1.00 77.88  ? 132  SER B O    1 
ATOM   744  C CB   . SER A 1 132 ? 109.537 151.642 149.761 1.00 86.27  ? 132  SER B CB   1 
ATOM   745  O OG   . SER A 1 132 ? 109.834 152.419 150.907 1.00 85.45  ? 132  SER B OG   1 
ATOM   746  N N    . LYS A 1 133 ? 107.354 151.457 147.450 1.00 68.21  ? 133  LYS B N    1 
ATOM   747  C CA   . LYS A 1 133 ? 106.712 150.658 146.405 1.00 68.64  ? 133  LYS B CA   1 
ATOM   748  C C    . LYS A 1 133 ? 106.645 151.396 145.074 1.00 65.37  ? 133  LYS B C    1 
ATOM   749  O O    . LYS A 1 133 ? 106.878 150.793 144.019 1.00 68.28  ? 133  LYS B O    1 
ATOM   750  C CB   . LYS A 1 133 ? 105.311 150.219 146.826 1.00 70.01  ? 133  LYS B CB   1 
ATOM   751  C CG   . LYS A 1 133 ? 105.249 149.254 147.990 1.00 64.08  ? 133  LYS B CG   1 
ATOM   752  C CD   . LYS A 1 133 ? 103.816 149.102 148.465 1.00 69.96  ? 133  LYS B CD   1 
ATOM   753  C CE   . LYS A 1 133 ? 103.706 148.102 149.595 1.00 67.85  ? 133  LYS B CE   1 
ATOM   754  N NZ   . LYS A 1 133 ? 104.167 148.665 150.879 1.00 70.04  ? 133  LYS B NZ   1 
ATOM   755  N N    . ALA A 1 134 ? 106.311 152.687 145.091 1.00 51.40  ? 134  ALA B N    1 
ATOM   756  C CA   . ALA A 1 134 ? 106.213 153.446 143.848 1.00 55.13  ? 134  ALA B CA   1 
ATOM   757  C C    . ALA A 1 134 ? 107.548 153.569 143.124 1.00 51.73  ? 134  ALA B C    1 
ATOM   758  O O    . ALA A 1 134 ? 107.559 153.809 141.914 1.00 43.99  ? 134  ALA B O    1 
ATOM   759  C CB   . ALA A 1 134 ? 105.649 154.838 144.131 1.00 63.46  ? 134  ALA B CB   1 
ATOM   760  N N    . GLY A 1 135 ? 108.665 153.439 143.831 1.00 56.22  ? 135  GLY B N    1 
ATOM   761  C CA   . GLY A 1 135 ? 109.974 153.543 143.216 1.00 60.77  ? 135  GLY B CA   1 
ATOM   762  C C    . GLY A 1 135 ? 110.500 152.260 142.595 1.00 61.04  ? 135  GLY B C    1 
ATOM   763  O O    . GLY A 1 135 ? 111.424 152.302 141.776 1.00 54.40  ? 135  GLY B O    1 
ATOM   764  N N    . LEU A 1 136 ? 109.923 151.115 142.959 1.00 57.54  ? 136  LEU B N    1 
ATOM   765  C CA   . LEU A 1 136 ? 110.395 149.808 142.505 1.00 51.66  ? 136  LEU B CA   1 
ATOM   766  C C    . LEU A 1 136 ? 109.425 149.050 141.610 1.00 55.88  ? 136  LEU B C    1 
ATOM   767  O O    . LEU A 1 136 ? 109.872 148.321 140.723 1.00 60.37  ? 136  LEU B O    1 
ATOM   768  C CB   . LEU A 1 136 ? 110.737 148.927 143.711 1.00 48.77  ? 136  LEU B CB   1 
ATOM   769  C CG   . LEU A 1 136 ? 111.917 149.372 144.571 1.00 48.09  ? 136  LEU B CG   1 
ATOM   770  C CD1  . LEU A 1 136 ? 112.038 148.495 145.804 1.00 48.10  ? 136  LEU B CD1  1 
ATOM   771  C CD2  . LEU A 1 136 ? 113.193 149.322 143.757 1.00 50.56  ? 136  LEU B CD2  1 
ATOM   772  N N    . PHE A 1 137 ? 108.113 149.164 141.832 1.00 47.09  ? 137  PHE B N    1 
ATOM   773  C CA   . PHE A 1 137 ? 107.148 148.435 141.007 1.00 40.61  ? 137  PHE B CA   1 
ATOM   774  C C    . PHE A 1 137 ? 107.215 148.825 139.526 1.00 42.35  ? 137  PHE B C    1 
ATOM   775  O O    . PHE A 1 137 ? 107.252 147.911 138.685 1.00 48.53  ? 137  PHE B O    1 
ATOM   776  C CB   . PHE A 1 137 ? 105.735 148.552 141.605 1.00 40.07  ? 137  PHE B CB   1 
ATOM   777  C CG   . PHE A 1 137 ? 105.495 147.678 142.806 1.00 45.42  ? 137  PHE B CG   1 
ATOM   778  C CD1  . PHE A 1 137 ? 106.495 146.866 143.310 1.00 43.52  ? 137  PHE B CD1  1 
ATOM   779  C CD2  . PHE A 1 137 ? 104.257 147.673 143.431 1.00 48.79  ? 137  PHE B CD2  1 
ATOM   780  C CE1  . PHE A 1 137 ? 106.264 146.063 144.410 1.00 47.49  ? 137  PHE B CE1  1 
ATOM   781  C CE2  . PHE A 1 137 ? 104.024 146.874 144.534 1.00 45.36  ? 137  PHE B CE2  1 
ATOM   782  C CZ   . PHE A 1 137 ? 105.031 146.070 145.023 1.00 47.75  ? 137  PHE B CZ   1 
ATOM   783  N N    . PRO A 1 138 ? 107.187 150.108 139.126 1.00 29.41  ? 138  PRO B N    1 
ATOM   784  C CA   . PRO A 1 138 ? 107.332 150.418 137.693 1.00 30.60  ? 138  PRO B CA   1 
ATOM   785  C C    . PRO A 1 138 ? 108.620 149.914 137.052 1.00 40.77  ? 138  PRO B C    1 
ATOM   786  O O    . PRO A 1 138 ? 108.619 149.598 135.856 1.00 45.45  ? 138  PRO B O    1 
ATOM   787  C CB   . PRO A 1 138 ? 107.317 151.955 137.682 1.00 40.10  ? 138  PRO B CB   1 
ATOM   788  C CG   . PRO A 1 138 ? 107.051 152.357 139.113 1.00 47.11  ? 138  PRO B CG   1 
ATOM   789  C CD   . PRO A 1 138 ? 106.399 151.209 139.709 1.00 42.27  ? 138  PRO B CD   1 
ATOM   790  N N    . ILE A 1 139 ? 109.724 149.855 137.801 1.00 44.48  ? 139  ILE B N    1 
ATOM   791  C CA   . ILE A 1 139 ? 110.953 149.242 137.296 1.00 43.28  ? 139  ILE B CA   1 
ATOM   792  C C    . ILE A 1 139 ? 110.771 147.742 137.068 1.00 40.27  ? 139  ILE B C    1 
ATOM   793  O O    . ILE A 1 139 ? 111.319 147.179 136.113 1.00 39.68  ? 139  ILE B O    1 
ATOM   794  C CB   . ILE A 1 139 ? 112.118 149.537 138.261 1.00 41.36  ? 139  ILE B CB   1 
ATOM   795  C CG1  . ILE A 1 139 ? 112.405 151.037 138.302 1.00 46.90  ? 139  ILE B CG1  1 
ATOM   796  C CG2  . ILE A 1 139 ? 113.383 148.798 137.847 1.00 32.86  ? 139  ILE B CG2  1 
ATOM   797  C CD1  . ILE A 1 139 ? 113.533 151.416 139.235 1.00 44.95  ? 139  ILE B CD1  1 
ATOM   798  N N    . PHE A 1 140 ? 109.987 147.076 137.922 1.00 27.80  ? 140  PHE B N    1 
ATOM   799  C CA   . PHE A 1 140 ? 109.754 145.642 137.757 1.00 19.64  ? 140  PHE B CA   1 
ATOM   800  C C    . PHE A 1 140 ? 109.023 145.328 136.457 1.00 27.92  ? 140  PHE B C    1 
ATOM   801  O O    . PHE A 1 140 ? 109.323 144.329 135.795 1.00 47.73  ? 140  PHE B O    1 
ATOM   802  C CB   . PHE A 1 140 ? 108.960 145.106 138.948 1.00 23.66  ? 140  PHE B CB   1 
ATOM   803  C CG   . PHE A 1 140 ? 108.703 143.628 138.892 1.00 24.12  ? 140  PHE B CG   1 
ATOM   804  C CD1  . PHE A 1 140 ? 109.744 142.721 138.956 1.00 28.02  ? 140  PHE B CD1  1 
ATOM   805  C CD2  . PHE A 1 140 ? 107.411 143.147 138.772 1.00 20.57  ? 140  PHE B CD2  1 
ATOM   806  C CE1  . PHE A 1 140 ? 109.499 141.363 138.902 1.00 33.78  ? 140  PHE B CE1  1 
ATOM   807  C CE2  . PHE A 1 140 ? 107.162 141.793 138.717 1.00 20.37  ? 140  PHE B CE2  1 
ATOM   808  C CZ   . PHE A 1 140 ? 108.206 140.900 138.782 1.00 24.37  ? 140  PHE B CZ   1 
ATOM   809  N N    . ALA A 1 141 ? 108.061 146.161 136.079 1.00 12.56  ? 141  ALA B N    1 
ATOM   810  C CA   . ALA A 1 141 ? 107.180 145.880 134.955 1.00 10.63  ? 141  ALA B CA   1 
ATOM   811  C C    . ALA A 1 141 ? 107.719 146.381 133.619 1.00 11.14  ? 141  ALA B C    1 
ATOM   812  O O    . ALA A 1 141 ? 106.989 146.338 132.625 1.00 29.21  ? 141  ALA B O    1 
ATOM   813  C CB   . ALA A 1 141 ? 105.798 146.484 135.209 1.00 17.73  ? 141  ALA B CB   1 
ATOM   814  N N    . THR A 1 142 ? 108.962 146.868 133.562 1.00 15.23  ? 142  THR B N    1 
ATOM   815  C CA   . THR A 1 142 ? 109.469 147.381 132.293 1.00 19.14  ? 142  THR B CA   1 
ATOM   816  C C    . THR A 1 142 ? 110.890 146.938 131.925 1.00 31.12  ? 142  THR B C    1 
ATOM   817  O O    . THR A 1 142 ? 111.295 147.159 130.779 1.00 31.58  ? 142  THR B O    1 
ATOM   818  C CB   . THR A 1 142 ? 109.397 148.923 132.343 1.00 21.04  ? 142  THR B CB   1 
ATOM   819  O OG1  . THR A 1 142 ? 108.127 149.311 132.876 1.00 31.62  ? 142  THR B OG1  1 
ATOM   820  C CG2  . THR A 1 142 ? 109.478 149.554 130.964 1.00 24.08  ? 142  THR B CG2  1 
ATOM   821  N N    . GLN A 1 143 ? 111.632 146.251 132.792 1.00 16.11  ? 143  GLN B N    1 
ATOM   822  C CA   . GLN A 1 143 ? 113.032 145.930 132.502 1.00 2.16   ? 143  GLN B CA   1 
ATOM   823  C C    . GLN A 1 143 ? 113.171 144.489 132.018 1.00 6.70   ? 143  GLN B C    1 
ATOM   824  O O    . GLN A 1 143 ? 113.277 143.557 132.818 1.00 14.77  ? 143  GLN B O    1 
ATOM   825  C CB   . GLN A 1 143 ? 113.906 146.182 133.726 1.00 16.49  ? 143  GLN B CB   1 
ATOM   826  C CG   . GLN A 1 143 ? 115.364 146.457 133.381 1.00 21.55  ? 143  GLN B CG   1 
ATOM   827  C CD   . GLN A 1 143 ? 116.139 147.071 134.531 1.00 26.81  ? 143  GLN B CD   1 
ATOM   828  O OE1  . GLN A 1 143 ? 115.718 148.067 135.116 1.00 34.06  ? 143  GLN B OE1  1 
ATOM   829  N NE2  . GLN A 1 143 ? 117.281 146.478 134.856 1.00 25.68  ? 143  GLN B NE2  1 
ATOM   830  N N    . SER A 1 144 ? 113.177 144.319 130.698 1.00 19.49  ? 144  SER B N    1 
ATOM   831  C CA   . SER A 1 144 ? 113.222 143.011 130.061 1.00 13.28  ? 144  SER B CA   1 
ATOM   832  C C    . SER A 1 144 ? 114.612 142.387 130.206 1.00 16.92  ? 144  SER B C    1 
ATOM   833  O O    . SER A 1 144 ? 115.613 143.068 130.445 1.00 33.58  ? 144  SER B O    1 
ATOM   834  C CB   . SER A 1 144 ? 112.829 143.124 128.590 1.00 19.12  ? 144  SER B CB   1 
ATOM   835  O OG   . SER A 1 144 ? 111.479 143.530 128.453 1.00 25.83  ? 144  SER B OG   1 
ATOM   836  N N    . ASN A 1 145 ? 114.668 141.062 130.062 1.00 17.44  ? 145  ASN B N    1 
ATOM   837  C CA   . ASN A 1 145 ? 115.917 140.307 130.021 1.00 22.21  ? 145  ASN B CA   1 
ATOM   838  C C    . ASN A 1 145 ? 116.444 140.178 128.592 1.00 16.71  ? 145  ASN B C    1 
ATOM   839  O O    . ASN A 1 145 ? 116.469 139.081 128.031 1.00 6.44   ? 145  ASN B O    1 
ATOM   840  C CB   . ASN A 1 145 ? 115.716 138.928 130.644 1.00 12.12  ? 145  ASN B CB   1 
ATOM   841  C CG   . ASN A 1 145 ? 117.020 138.257 131.013 1.00 13.79  ? 145  ASN B CG   1 
ATOM   842  O OD1  . ASN A 1 145 ? 117.036 137.146 131.538 1.00 33.89  ? 145  ASN B OD1  1 
ATOM   843  N ND2  . ASN A 1 145 ? 118.128 138.931 130.732 1.00 4.84   ? 145  ASN B ND2  1 
ATOM   844  N N    . ASP A 1 146 ? 116.867 141.294 127.994 1.00 16.79  ? 146  ASP B N    1 
ATOM   845  C CA   . ASP A 1 146 ? 117.216 141.338 126.577 1.00 11.26  ? 146  ASP B CA   1 
ATOM   846  C C    . ASP A 1 146 ? 118.568 140.737 126.206 1.00 23.78  ? 146  ASP B C    1 
ATOM   847  O O    . ASP A 1 146 ? 118.693 140.116 125.147 1.00 29.28  ? 146  ASP B O    1 
ATOM   848  C CB   . ASP A 1 146 ? 117.188 142.787 126.087 1.00 16.57  ? 146  ASP B CB   1 
ATOM   849  C CG   . ASP A 1 146 ? 116.004 143.559 126.617 1.00 27.19  ? 146  ASP B CG   1 
ATOM   850  O OD1  . ASP A 1 146 ? 116.171 144.294 127.612 1.00 16.70  ? 146  ASP B OD1  1 
ATOM   851  O OD2  . ASP A 1 146 ? 114.905 143.432 126.040 1.00 33.77  ? 146  ASP B OD2  1 
ATOM   852  N N    . PHE A 1 147 ? 119.592 140.919 127.039 1.00 22.61  ? 147  PHE B N    1 
ATOM   853  C CA   . PHE A 1 147 ? 120.917 140.437 126.660 1.00 10.33  ? 147  PHE B CA   1 
ATOM   854  C C    . PHE A 1 147 ? 121.077 138.932 126.831 1.00 17.80  ? 147  PHE B C    1 
ATOM   855  O O    . PHE A 1 147 ? 121.590 138.253 125.937 1.00 21.75  ? 147  PHE B O    1 
ATOM   856  C CB   . PHE A 1 147 ? 121.990 141.166 127.472 1.00 16.83  ? 147  PHE B CB   1 
ATOM   857  C CG   . PHE A 1 147 ? 121.899 142.660 127.387 1.00 12.55  ? 147  PHE B CG   1 
ATOM   858  C CD1  . PHE A 1 147 ? 122.059 143.309 126.176 1.00 14.29  ? 147  PHE B CD1  1 
ATOM   859  C CD2  . PHE A 1 147 ? 121.654 143.417 128.520 1.00 21.66  ? 147  PHE B CD2  1 
ATOM   860  C CE1  . PHE A 1 147 ? 121.970 144.684 126.094 1.00 24.94  ? 147  PHE B CE1  1 
ATOM   861  C CE2  . PHE A 1 147 ? 121.568 144.792 128.445 1.00 19.61  ? 147  PHE B CE2  1 
ATOM   862  C CZ   . PHE A 1 147 ? 121.726 145.426 127.230 1.00 20.90  ? 147  PHE B CZ   1 
ATOM   863  N N    . ALA A 1 148 ? 120.651 138.405 127.976 1.00 18.87  ? 148  ALA B N    1 
ATOM   864  C CA   . ALA A 1 148 ? 120.818 136.991 128.288 1.00 14.47  ? 148  ALA B CA   1 
ATOM   865  C C    . ALA A 1 148 ? 119.911 136.088 127.460 1.00 14.42  ? 148  ALA B C    1 
ATOM   866  O O    . ALA A 1 148 ? 120.367 135.094 126.888 1.00 15.26  ? 148  ALA B O    1 
ATOM   867  C CB   . ALA A 1 148 ? 120.570 136.748 129.778 1.00 23.36  ? 148  ALA B CB   1 
ATOM   868  N N    . LEU A 1 149 ? 118.624 136.435 127.389 1.00 13.32  ? 149  LEU B N    1 
ATOM   869  C CA   . LEU A 1 149 ? 117.651 135.580 126.716 1.00 14.03  ? 149  LEU B CA   1 
ATOM   870  C C    . LEU A 1 149 ? 117.197 136.139 125.373 1.00 18.24  ? 149  LEU B C    1 
ATOM   871  O O    . LEU A 1 149 ? 116.975 135.369 124.433 1.00 30.39  ? 149  LEU B O    1 
ATOM   872  C CB   . LEU A 1 149 ? 116.441 135.379 127.628 1.00 8.99   ? 149  LEU B CB   1 
ATOM   873  C CG   . LEU A 1 149 ? 116.452 134.194 128.590 1.00 11.47  ? 149  LEU B CG   1 
ATOM   874  C CD1  . LEU A 1 149 ? 115.556 134.465 129.775 1.00 17.24  ? 149  LEU B CD1  1 
ATOM   875  C CD2  . LEU A 1 149 ? 115.970 132.967 127.870 1.00 16.24  ? 149  LEU B CD2  1 
ATOM   876  N N    . GLY A 1 150 ? 117.026 137.458 125.270 1.00 12.56  ? 150  GLY B N    1 
ATOM   877  C CA   . GLY A 1 150 ? 116.500 138.033 124.041 1.00 5.83   ? 150  GLY B CA   1 
ATOM   878  C C    . GLY A 1 150 ? 117.394 137.865 122.826 1.00 7.52   ? 150  GLY B C    1 
ATOM   879  O O    . GLY A 1 150 ? 116.917 137.500 121.749 1.00 22.26  ? 150  GLY B O    1 
ATOM   880  N N    . TYR A 1 151 ? 118.690 138.136 122.972 1.00 9.05   ? 151  TYR B N    1 
ATOM   881  C CA   . TYR A 1 151 ? 119.612 138.086 121.835 1.00 16.43  ? 151  TYR B CA   1 
ATOM   882  C C    . TYR A 1 151 ? 119.755 136.694 121.206 1.00 21.41  ? 151  TYR B C    1 
ATOM   883  O O    . TYR A 1 151 ? 119.706 136.601 119.973 1.00 22.99  ? 151  TYR B O    1 
ATOM   884  C CB   . TYR A 1 151 ? 120.986 138.652 122.215 1.00 18.13  ? 151  TYR B CB   1 
ATOM   885  C CG   . TYR A 1 151 ? 121.945 138.718 121.044 1.00 17.64  ? 151  TYR B CG   1 
ATOM   886  C CD1  . TYR A 1 151 ? 121.911 139.790 120.162 1.00 19.93  ? 151  TYR B CD1  1 
ATOM   887  C CD2  . TYR A 1 151 ? 122.889 137.722 120.826 1.00 20.06  ? 151  TYR B CD2  1 
ATOM   888  C CE1  . TYR A 1 151 ? 122.778 139.864 119.091 1.00 23.09  ? 151  TYR B CE1  1 
ATOM   889  C CE2  . TYR A 1 151 ? 123.761 137.787 119.755 1.00 28.07  ? 151  TYR B CE2  1 
ATOM   890  C CZ   . TYR A 1 151 ? 123.701 138.861 118.893 1.00 29.12  ? 151  TYR B CZ   1 
ATOM   891  O OH   . TYR A 1 151 ? 124.566 138.934 117.826 1.00 27.05  ? 151  TYR B OH   1 
ATOM   892  N N    . PRO A 1 152 ? 119.978 135.603 121.968 1.00 17.24  ? 152  PRO B N    1 
ATOM   893  C CA   . PRO A 1 152 ? 120.081 134.282 121.316 1.00 8.44   ? 152  PRO B CA   1 
ATOM   894  C C    . PRO A 1 152 ? 118.852 133.867 120.525 1.00 8.86   ? 152  PRO B C    1 
ATOM   895  O O    . PRO A 1 152 ? 118.993 133.233 119.472 1.00 19.41  ? 152  PRO B O    1 
ATOM   896  C CB   . PRO A 1 152 ? 120.331 133.326 122.489 1.00 13.99  ? 152  PRO B CB   1 
ATOM   897  C CG   . PRO A 1 152 ? 120.905 134.156 123.541 1.00 16.51  ? 152  PRO B CG   1 
ATOM   898  C CD   . PRO A 1 152 ? 120.247 135.484 123.416 1.00 22.58  ? 152  PRO B CD   1 
ATOM   899  N N    . ILE A 1 153 ? 117.649 134.196 120.997 1.00 10.32  ? 153  ILE B N    1 
ATOM   900  C CA   . ILE A 1 153 ? 116.426 133.837 120.285 1.00 12.40  ? 153  ILE B CA   1 
ATOM   901  C C    . ILE A 1 153 ? 116.211 134.666 119.023 1.00 18.20  ? 153  ILE B C    1 
ATOM   902  O O    . ILE A 1 153 ? 115.824 134.100 117.987 1.00 24.37  ? 153  ILE B O    1 
ATOM   903  C CB   . ILE A 1 153 ? 115.203 133.959 121.222 1.00 8.42   ? 153  ILE B CB   1 
ATOM   904  C CG1  . ILE A 1 153 ? 115.270 132.891 122.314 1.00 10.74  ? 153  ILE B CG1  1 
ATOM   905  C CG2  . ILE A 1 153 ? 113.897 133.822 120.460 1.00 8.95   ? 153  ILE B CG2  1 
ATOM   906  C CD1  . ILE A 1 153 ? 114.184 133.011 123.350 1.00 20.35  ? 153  ILE B CD1  1 
ATOM   907  N N    . VAL A 1 154 ? 116.470 135.973 119.064 1.00 26.64  ? 154  VAL B N    1 
ATOM   908  C CA   . VAL A 1 154 ? 116.314 136.814 117.877 1.00 17.18  ? 154  VAL B CA   1 
ATOM   909  C C    . VAL A 1 154 ? 117.296 136.396 116.786 1.00 20.27  ? 154  VAL B C    1 
ATOM   910  O O    . VAL A 1 154 ? 116.963 136.396 115.596 1.00 25.85  ? 154  VAL B O    1 
ATOM   911  C CB   . VAL A 1 154 ? 116.478 138.300 118.252 1.00 16.40  ? 154  VAL B CB   1 
ATOM   912  C CG1  . VAL A 1 154 ? 116.473 139.180 117.016 1.00 20.81  ? 154  VAL B CG1  1 
ATOM   913  C CG2  . VAL A 1 154 ? 115.360 138.723 119.182 1.00 28.47  ? 154  VAL B CG2  1 
ATOM   914  N N    . GLU A 1 155 ? 118.509 136.005 117.180 1.00 18.57  ? 155  GLU B N    1 
ATOM   915  C CA   . GLU A 1 155 ? 119.529 135.571 116.233 1.00 16.57  ? 155  GLU B CA   1 
ATOM   916  C C    . GLU A 1 155 ? 119.097 134.313 115.486 1.00 24.96  ? 155  GLU B C    1 
ATOM   917  O O    . GLU A 1 155 ? 119.299 134.214 114.274 1.00 28.16  ? 155  GLU B O    1 
ATOM   918  C CB   . GLU A 1 155 ? 120.868 135.356 116.948 1.00 12.40  ? 155  GLU B CB   1 
ATOM   919  C CG   . GLU A 1 155 ? 121.678 134.169 116.457 1.00 22.50  ? 155  GLU B CG   1 
ATOM   920  C CD   . GLU A 1 155 ? 123.073 134.135 117.040 1.00 31.69  ? 155  GLU B CD   1 
ATOM   921  O OE1  . GLU A 1 155 ? 123.826 135.108 116.833 1.00 28.89  ? 155  GLU B OE1  1 
ATOM   922  O OE2  . GLU A 1 155 ? 123.424 133.131 117.698 1.00 33.30  ? 155  GLU B OE2  1 
ATOM   923  N N    . ALA A 1 156 ? 118.490 133.356 116.196 1.00 30.85  ? 156  ALA B N    1 
ATOM   924  C CA   . ALA A 1 156 ? 118.081 132.101 115.567 1.00 26.92  ? 156  ALA B CA   1 
ATOM   925  C C    . ALA A 1 156 ? 117.036 132.342 114.486 1.00 20.83  ? 156  ALA B C    1 
ATOM   926  O O    . ALA A 1 156 ? 117.105 131.760 113.399 1.00 30.94  ? 156  ALA B O    1 
ATOM   927  C CB   . ALA A 1 156 ? 117.550 131.134 116.623 1.00 17.39  ? 156  ALA B CB   1 
ATOM   928  N N    . LEU A 1 157 ? 116.061 133.201 114.771 1.00 17.38  ? 157  LEU B N    1 
ATOM   929  C CA   . LEU A 1 157 ? 114.961 133.468 113.855 1.00 29.09  ? 157  LEU B CA   1 
ATOM   930  C C    . LEU A 1 157 ? 115.373 134.386 112.711 1.00 34.07  ? 157  LEU B C    1 
ATOM   931  O O    . LEU A 1 157 ? 114.880 134.228 111.590 1.00 32.73  ? 157  LEU B O    1 
ATOM   932  C CB   . LEU A 1 157 ? 113.792 134.098 114.613 1.00 27.20  ? 157  LEU B CB   1 
ATOM   933  C CG   . LEU A 1 157 ? 113.013 133.252 115.617 1.00 24.62  ? 157  LEU B CG   1 
ATOM   934  C CD1  . LEU A 1 157 ? 112.125 134.140 116.469 1.00 18.01  ? 157  LEU B CD1  1 
ATOM   935  C CD2  . LEU A 1 157 ? 112.184 132.219 114.896 1.00 32.45  ? 157  LEU B CD2  1 
ATOM   936  N N    . TYR A 1 158 ? 116.261 135.344 112.975 1.00 35.00  ? 158  TYR B N    1 
ATOM   937  C CA   . TYR A 1 158 ? 116.500 136.474 112.085 1.00 21.81  ? 158  TYR B CA   1 
ATOM   938  C C    . TYR A 1 158 ? 117.920 136.583 111.535 1.00 26.77  ? 158  TYR B C    1 
ATOM   939  O O    . TYR A 1 158 ? 118.229 137.602 110.907 1.00 30.41  ? 158  TYR B O    1 
ATOM   940  C CB   . TYR A 1 158 ? 116.132 137.784 112.790 1.00 26.09  ? 158  TYR B CB   1 
ATOM   941  C CG   . TYR A 1 158 ? 114.646 138.038 112.878 1.00 31.01  ? 158  TYR B CG   1 
ATOM   942  C CD1  . TYR A 1 158 ? 113.883 138.200 111.730 1.00 35.76  ? 158  TYR B CD1  1 
ATOM   943  C CD2  . TYR A 1 158 ? 114.005 138.117 114.105 1.00 27.72  ? 158  TYR B CD2  1 
ATOM   944  C CE1  . TYR A 1 158 ? 112.526 138.435 111.801 1.00 30.87  ? 158  TYR B CE1  1 
ATOM   945  C CE2  . TYR A 1 158 ? 112.647 138.349 114.185 1.00 26.11  ? 158  TYR B CE2  1 
ATOM   946  C CZ   . TYR A 1 158 ? 111.913 138.507 113.030 1.00 26.31  ? 158  TYR B CZ   1 
ATOM   947  O OH   . TYR A 1 158 ? 110.561 138.738 113.102 1.00 30.86  ? 158  TYR B OH   1 
ATOM   948  N N    . GLN A 1 159 ? 118.815 135.617 111.780 1.00 45.51  ? 159  GLN B N    1 
ATOM   949  C CA   . GLN A 1 159 ? 120.160 135.788 111.230 1.00 37.15  ? 159  GLN B CA   1 
ATOM   950  C C    . GLN A 1 159 ? 120.147 135.707 109.709 1.00 41.25  ? 159  GLN B C    1 
ATOM   951  O O    . GLN A 1 159 ? 120.825 136.498 109.043 1.00 39.77  ? 159  GLN B O    1 
ATOM   952  C CB   . GLN A 1 159 ? 121.111 134.734 111.798 1.00 34.86  ? 159  GLN B CB   1 
ATOM   953  C CG   . GLN A 1 159 ? 122.597 134.820 111.391 1.00 38.70  ? 159  GLN B CG   1 
ATOM   954  C CD   . GLN A 1 159 ? 123.159 136.234 111.301 1.00 45.18  ? 159  GLN B CD   1 
ATOM   955  O OE1  . GLN A 1 159 ? 123.808 136.705 112.235 1.00 47.51  ? 159  GLN B OE1  1 
ATOM   956  N NE2  . GLN A 1 159 ? 122.994 136.878 110.149 1.00 46.31  ? 159  GLN B NE2  1 
ATOM   957  N N    . THR A 1 160 ? 119.394 134.772 109.128 1.00 53.95  ? 160  THR B N    1 
ATOM   958  C CA   . THR A 1 160 ? 119.513 134.634 107.686 1.00 48.80  ? 160  THR B CA   1 
ATOM   959  C C    . THR A 1 160 ? 118.456 135.458 106.971 1.00 44.07  ? 160  THR B C    1 
ATOM   960  O O    . THR A 1 160 ? 118.589 135.725 105.772 1.00 46.33  ? 160  THR B O    1 
ATOM   961  C CB   . THR A 1 160 ? 119.390 133.165 107.270 1.00 43.94  ? 160  THR B CB   1 
ATOM   962  O OG1  . THR A 1 160 ? 118.195 132.607 107.831 1.00 41.76  ? 160  THR B OG1  1 
ATOM   963  C CG2  . THR A 1 160 ? 120.592 132.372 107.757 1.00 43.33  ? 160  THR B CG2  1 
ATOM   964  N N    . THR A 1 161 ? 117.414 135.853 107.698 1.00 50.76  ? 161  THR B N    1 
ATOM   965  C CA   . THR A 1 161 ? 116.288 136.619 107.183 1.00 52.93  ? 161  THR B CA   1 
ATOM   966  C C    . THR A 1 161 ? 116.355 138.001 107.819 1.00 56.75  ? 161  THR B C    1 
ATOM   967  O O    . THR A 1 161 ? 116.229 138.112 109.044 1.00 55.51  ? 161  THR B O    1 
ATOM   968  C CB   . THR A 1 161 ? 114.956 135.939 107.484 1.00 56.10  ? 161  THR B CB   1 
ATOM   969  O OG1  . THR A 1 161 ? 114.833 134.757 106.685 1.00 54.81  ? 161  THR B OG1  1 
ATOM   970  C CG2  . THR A 1 161 ? 113.811 136.881 107.150 1.00 52.09  ? 161  THR B CG2  1 
ATOM   971  N N    . TYR A 1 162 ? 116.535 139.043 107.003 1.00 50.58  ? 162  TYR B N    1 
ATOM   972  C CA   . TYR A 1 162 ? 116.552 140.429 107.474 1.00 44.13  ? 162  TYR B CA   1 
ATOM   973  C C    . TYR A 1 162 ? 117.632 140.621 108.540 1.00 43.07  ? 162  TYR B C    1 
ATOM   974  O O    . TYR A 1 162 ? 117.324 140.688 109.736 1.00 47.87  ? 162  TYR B O    1 
ATOM   975  C CB   . TYR A 1 162 ? 115.176 140.810 108.019 1.00 47.15  ? 162  TYR B CB   1 
ATOM   976  C CG   . TYR A 1 162 ? 114.077 140.880 106.980 1.00 48.22  ? 162  TYR B CG   1 
ATOM   977  C CD1  . TYR A 1 162 ? 114.367 141.018 105.630 1.00 51.07  ? 162  TYR B CD1  1 
ATOM   978  C CD2  . TYR A 1 162 ? 112.743 140.785 107.355 1.00 47.84  ? 162  TYR B CD2  1 
ATOM   979  C CE1  . TYR A 1 162 ? 113.357 141.070 104.686 1.00 52.56  ? 162  TYR B CE1  1 
ATOM   980  C CE2  . TYR A 1 162 ? 111.730 140.839 106.419 1.00 50.80  ? 162  TYR B CE2  1 
ATOM   981  C CZ   . TYR A 1 162 ? 112.042 140.983 105.087 1.00 50.02  ? 162  TYR B CZ   1 
ATOM   982  O OH   . TYR A 1 162 ? 111.037 141.035 104.150 1.00 52.03  ? 162  TYR B OH   1 
ATOM   983  N N    . PRO A 1 163 ? 118.902 140.707 108.138 1.00 39.16  ? 163  PRO B N    1 
ATOM   984  C CA   . PRO A 1 163 ? 120.007 140.849 109.111 1.00 38.14  ? 163  PRO B CA   1 
ATOM   985  C C    . PRO A 1 163 ? 119.984 142.099 109.988 1.00 38.10  ? 163  PRO B C    1 
ATOM   986  O O    . PRO A 1 163 ? 120.595 142.079 111.063 1.00 35.87  ? 163  PRO B O    1 
ATOM   987  C CB   . PRO A 1 163 ? 121.256 140.837 108.218 1.00 41.41  ? 163  PRO B CB   1 
ATOM   988  C CG   . PRO A 1 163 ? 120.768 141.272 106.879 1.00 46.82  ? 163  PRO B CG   1 
ATOM   989  C CD   . PRO A 1 163 ? 119.389 140.710 106.749 1.00 44.93  ? 163  PRO B CD   1 
ATOM   990  N N    . GLU A 1 164 ? 119.309 143.174 109.582 1.00 46.73  ? 164  GLU B N    1 
ATOM   991  C CA   . GLU A 1 164 ? 119.275 144.402 110.375 1.00 46.03  ? 164  GLU B CA   1 
ATOM   992  C C    . GLU A 1 164 ? 118.465 144.321 111.666 1.00 43.50  ? 164  GLU B C    1 
ATOM   993  O O    . GLU A 1 164 ? 118.532 145.268 112.456 1.00 50.71  ? 164  GLU B O    1 
ATOM   994  C CB   . GLU A 1 164 ? 118.710 145.550 109.534 1.00 44.24  ? 164  GLU B CB   1 
ATOM   995  C CG   . GLU A 1 164 ? 117.334 145.266 108.951 1.00 43.73  ? 164  GLU B CG   1 
ATOM   996  C CD   . GLU A 1 164 ? 117.342 145.183 107.439 1.00 52.84  ? 164  GLU B CD   1 
ATOM   997  O OE1  . GLU A 1 164 ? 118.305 144.615 106.887 1.00 54.58  ? 164  GLU B OE1  1 
ATOM   998  O OE2  . GLU A 1 164 ? 116.379 145.667 106.807 1.00 51.18  ? 164  GLU B OE2  1 
ATOM   999  N N    . TYR A 1 165 ? 117.706 143.254 111.917 1.00 31.92  ? 165  TYR B N    1 
ATOM   1000 C CA   . TYR A 1 165 ? 116.959 143.211 113.172 1.00 35.23  ? 165  TYR B CA   1 
ATOM   1001 C C    . TYR A 1 165 ? 117.818 142.899 114.394 1.00 35.81  ? 165  TYR B C    1 
ATOM   1002 O O    . TYR A 1 165 ? 117.402 143.226 115.510 1.00 43.13  ? 165  TYR B O    1 
ATOM   1003 C CB   . TYR A 1 165 ? 115.811 142.209 113.081 1.00 39.96  ? 165  TYR B CB   1 
ATOM   1004 C CG   . TYR A 1 165 ? 114.658 142.723 112.259 1.00 40.93  ? 165  TYR B CG   1 
ATOM   1005 C CD1  . TYR A 1 165 ? 113.947 143.840 112.665 1.00 35.84  ? 165  TYR B CD1  1 
ATOM   1006 C CD2  . TYR A 1 165 ? 114.277 142.097 111.088 1.00 42.57  ? 165  TYR B CD2  1 
ATOM   1007 C CE1  . TYR A 1 165 ? 112.894 144.319 111.925 1.00 39.69  ? 165  TYR B CE1  1 
ATOM   1008 C CE2  . TYR A 1 165 ? 113.221 142.572 110.338 1.00 41.68  ? 165  TYR B CE2  1 
ATOM   1009 C CZ   . TYR A 1 165 ? 112.534 143.683 110.761 1.00 43.25  ? 165  TYR B CZ   1 
ATOM   1010 O OH   . TYR A 1 165 ? 111.481 144.159 110.016 1.00 46.90  ? 165  TYR B OH   1 
ATOM   1011 N N    . LEU A 1 166 ? 118.978 142.259 114.228 1.00 27.76  ? 166  LEU B N    1 
ATOM   1012 C CA   . LEU A 1 166 ? 119.795 141.921 115.394 1.00 28.86  ? 166  LEU B CA   1 
ATOM   1013 C C    . LEU A 1 166 ? 120.322 143.173 116.089 1.00 33.31  ? 166  LEU B C    1 
ATOM   1014 O O    . LEU A 1 166 ? 120.406 143.217 117.322 1.00 33.95  ? 166  LEU B O    1 
ATOM   1015 C CB   . LEU A 1 166 ? 120.956 141.011 114.990 1.00 33.99  ? 166  LEU B CB   1 
ATOM   1016 C CG   . LEU A 1 166 ? 120.689 139.531 114.693 1.00 31.13  ? 166  LEU B CG   1 
ATOM   1017 C CD1  . LEU A 1 166 ? 120.057 139.311 113.325 1.00 27.70  ? 166  LEU B CD1  1 
ATOM   1018 C CD2  . LEU A 1 166 ? 121.977 138.736 114.820 1.00 31.55  ? 166  LEU B CD2  1 
ATOM   1019 N N    . GLN A 1 167 ? 120.693 144.193 115.310 1.00 37.83  ? 167  GLN B N    1 
ATOM   1020 C CA   . GLN A 1 167 ? 121.315 145.401 115.844 1.00 35.98  ? 167  GLN B CA   1 
ATOM   1021 C C    . GLN A 1 167 ? 120.365 146.227 116.711 1.00 41.18  ? 167  GLN B C    1 
ATOM   1022 O O    . GLN A 1 167 ? 120.831 146.989 117.563 1.00 43.19  ? 167  GLN B O    1 
ATOM   1023 C CB   . GLN A 1 167 ? 121.849 146.233 114.669 1.00 37.80  ? 167  GLN B CB   1 
ATOM   1024 C CG   . GLN A 1 167 ? 122.565 147.531 115.015 1.00 42.82  ? 167  GLN B CG   1 
ATOM   1025 C CD   . GLN A 1 167 ? 123.131 148.226 113.789 1.00 50.00  ? 167  GLN B CD   1 
ATOM   1026 O OE1  . GLN A 1 167 ? 124.329 148.500 113.713 1.00 49.10  ? 167  GLN B OE1  1 
ATOM   1027 N NE2  . GLN A 1 167 ? 122.271 148.503 112.816 1.00 47.13  ? 167  GLN B NE2  1 
ATOM   1028 N N    . TYR A 1 168 ? 119.052 146.027 116.575 1.00 34.81  ? 168  TYR B N    1 
ATOM   1029 C CA   . TYR A 1 168 ? 118.062 146.772 117.350 1.00 21.80  ? 168  TYR B CA   1 
ATOM   1030 C C    . TYR A 1 168 ? 118.084 146.447 118.838 1.00 16.82  ? 168  TYR B C    1 
ATOM   1031 O O    . TYR A 1 168 ? 117.599 147.254 119.637 1.00 30.66  ? 168  TYR B O    1 
ATOM   1032 C CB   . TYR A 1 168 ? 116.669 146.526 116.774 1.00 22.65  ? 168  TYR B CB   1 
ATOM   1033 C CG   . TYR A 1 168 ? 116.466 147.203 115.438 1.00 24.86  ? 168  TYR B CG   1 
ATOM   1034 C CD1  . TYR A 1 168 ? 117.215 148.316 115.083 1.00 25.42  ? 168  TYR B CD1  1 
ATOM   1035 C CD2  . TYR A 1 168 ? 115.542 146.719 114.524 1.00 36.08  ? 168  TYR B CD2  1 
ATOM   1036 C CE1  . TYR A 1 168 ? 117.043 148.933 113.862 1.00 25.02  ? 168  TYR B CE1  1 
ATOM   1037 C CE2  . TYR A 1 168 ? 115.363 147.331 113.299 1.00 36.92  ? 168  TYR B CE2  1 
ATOM   1038 C CZ   . TYR A 1 168 ? 116.116 148.437 112.975 1.00 34.78  ? 168  TYR B CZ   1 
ATOM   1039 O OH   . TYR A 1 168 ? 115.938 149.046 111.756 1.00 36.83  ? 168  TYR B OH   1 
ATOM   1040 N N    . ILE A 1 169 ? 118.618 145.289 119.224 1.00 14.68  ? 169  ILE B N    1 
ATOM   1041 C CA   . ILE A 1 169 ? 118.687 144.911 120.635 1.00 24.57  ? 169  ILE B CA   1 
ATOM   1042 C C    . ILE A 1 169 ? 119.597 145.860 121.411 1.00 34.97  ? 169  ILE B C    1 
ATOM   1043 O O    . ILE A 1 169 ? 119.280 146.262 122.538 1.00 38.55  ? 169  ILE B O    1 
ATOM   1044 C CB   . ILE A 1 169 ? 119.137 143.443 120.762 1.00 26.96  ? 169  ILE B CB   1 
ATOM   1045 C CG1  . ILE A 1 169 ? 118.012 142.504 120.321 1.00 36.35  ? 169  ILE B CG1  1 
ATOM   1046 C CG2  . ILE A 1 169 ? 119.582 143.118 122.181 1.00 26.48  ? 169  ILE B CG2  1 
ATOM   1047 C CD1  . ILE A 1 169 ? 116.899 142.354 121.336 1.00 30.62  ? 169  ILE B CD1  1 
ATOM   1048 N N    . TYR A 1 170 ? 120.719 146.262 120.814 1.00 35.85  ? 170  TYR B N    1 
ATOM   1049 C CA   . TYR A 1 170 ? 121.689 147.130 121.474 1.00 24.64  ? 170  TYR B CA   1 
ATOM   1050 C C    . TYR A 1 170 ? 121.321 148.609 121.443 1.00 29.66  ? 170  TYR B C    1 
ATOM   1051 O O    . TYR A 1 170 ? 122.031 149.410 122.056 1.00 38.24  ? 170  TYR B O    1 
ATOM   1052 C CB   . TYR A 1 170 ? 123.078 146.918 120.872 1.00 16.42  ? 170  TYR B CB   1 
ATOM   1053 C CG   . TYR A 1 170 ? 123.560 145.497 121.021 1.00 20.97  ? 170  TYR B CG   1 
ATOM   1054 C CD1  . TYR A 1 170 ? 123.868 144.985 122.274 1.00 19.42  ? 170  TYR B CD1  1 
ATOM   1055 C CD2  . TYR A 1 170 ? 123.691 144.662 119.922 1.00 26.81  ? 170  TYR B CD2  1 
ATOM   1056 C CE1  . TYR A 1 170 ? 124.302 143.688 122.430 1.00 20.11  ? 170  TYR B CE1  1 
ATOM   1057 C CE2  . TYR A 1 170 ? 124.127 143.359 120.068 1.00 27.29  ? 170  TYR B CE2  1 
ATOM   1058 C CZ   . TYR A 1 170 ? 124.431 142.879 121.325 1.00 28.56  ? 170  TYR B CZ   1 
ATOM   1059 O OH   . TYR A 1 170 ? 124.864 141.584 121.482 1.00 36.59  ? 170  TYR B OH   1 
ATOM   1060 N N    . LEU A 1 171 ? 120.275 149.002 120.718 1.00 32.39  ? 171  LEU B N    1 
ATOM   1061 C CA   . LEU A 1 171 ? 119.831 150.392 120.755 1.00 33.97  ? 171  LEU B CA   1 
ATOM   1062 C C    . LEU A 1 171 ? 118.697 150.606 121.751 1.00 38.73  ? 171  LEU B C    1 
ATOM   1063 O O    . LEU A 1 171 ? 118.721 151.576 122.516 1.00 34.69  ? 171  LEU B O    1 
ATOM   1064 C CB   . LEU A 1 171 ? 119.373 150.873 119.373 1.00 20.70  ? 171  LEU B CB   1 
ATOM   1065 C CG   . LEU A 1 171 ? 120.384 151.310 118.313 1.00 19.97  ? 171  LEU B CG   1 
ATOM   1066 C CD1  . LEU A 1 171 ? 120.961 150.138 117.572 1.00 29.96  ? 171  LEU B CD1  1 
ATOM   1067 C CD2  . LEU A 1 171 ? 119.735 152.279 117.342 1.00 26.12  ? 171  LEU B CD2  1 
ATOM   1068 N N    . VAL A 1 172 ? 117.699 149.719 121.748 1.00 45.57  ? 172  VAL B N    1 
ATOM   1069 C CA   . VAL A 1 172 ? 116.525 149.898 122.596 1.00 32.45  ? 172  VAL B CA   1 
ATOM   1070 C C    . VAL A 1 172 ? 116.866 149.714 124.073 1.00 40.50  ? 172  VAL B C    1 
ATOM   1071 O O    . VAL A 1 172 ? 116.394 150.472 124.930 1.00 49.96  ? 172  VAL B O    1 
ATOM   1072 C CB   . VAL A 1 172 ? 115.428 148.907 122.163 1.00 26.02  ? 172  VAL B CB   1 
ATOM   1073 C CG1  . VAL A 1 172 ? 114.242 148.991 123.088 1.00 38.97  ? 172  VAL B CG1  1 
ATOM   1074 C CG2  . VAL A 1 172 ? 115.014 149.135 120.725 1.00 32.75  ? 172  VAL B CG2  1 
ATOM   1075 N N    . ALA A 1 173 ? 117.696 148.721 124.392 1.00 46.00  ? 173  ALA B N    1 
ATOM   1076 C CA   . ALA A 1 173 ? 118.013 148.426 125.791 1.00 52.20  ? 173  ALA B CA   1 
ATOM   1077 C C    . ALA A 1 173 ? 118.746 149.543 126.538 1.00 54.89  ? 173  ALA B C    1 
ATOM   1078 O O    . ALA A 1 173 ? 118.271 149.931 127.620 1.00 53.57  ? 173  ALA B O    1 
ATOM   1079 C CB   . ALA A 1 173 ? 118.754 147.084 125.876 1.00 50.86  ? 173  ALA B CB   1 
ATOM   1080 N N    . PRO A 1 174 ? 119.887 150.084 126.068 1.00 54.60  ? 174  PRO B N    1 
ATOM   1081 C CA   . PRO A 1 174 ? 120.548 151.150 126.851 1.00 53.54  ? 174  PRO B CA   1 
ATOM   1082 C C    . PRO A 1 174 ? 119.750 152.431 127.024 1.00 52.76  ? 174  PRO B C    1 
ATOM   1083 O O    . PRO A 1 174 ? 119.816 153.041 128.099 1.00 51.92  ? 174  PRO B O    1 
ATOM   1084 C CB   . PRO A 1 174 ? 121.833 151.419 126.057 1.00 54.88  ? 174  PRO B CB   1 
ATOM   1085 C CG   . PRO A 1 174 ? 122.072 150.202 125.277 1.00 56.06  ? 174  PRO B CG   1 
ATOM   1086 C CD   . PRO A 1 174 ? 120.715 149.704 124.908 1.00 47.03  ? 174  PRO B CD   1 
ATOM   1087 N N    . ILE A 1 175 ? 119.022 152.877 125.998 1.00 51.33  ? 175  ILE B N    1 
ATOM   1088 C CA   . ILE A 1 175 ? 118.277 154.128 126.115 1.00 57.63  ? 175  ILE B CA   1 
ATOM   1089 C C    . ILE A 1 175 ? 117.169 154.013 127.159 1.00 55.68  ? 175  ILE B C    1 
ATOM   1090 O O    . ILE A 1 175 ? 116.958 154.936 127.956 1.00 60.43  ? 175  ILE B O    1 
ATOM   1091 C CB   . ILE A 1 175 ? 117.733 154.555 124.739 1.00 61.04  ? 175  ILE B CB   1 
ATOM   1092 C CG1  . ILE A 1 175 ? 118.887 154.903 123.799 1.00 53.43  ? 175  ILE B CG1  1 
ATOM   1093 C CG2  . ILE A 1 175 ? 116.839 155.769 124.873 1.00 60.63  ? 175  ILE B CG2  1 
ATOM   1094 C CD1  . ILE A 1 175 ? 118.475 155.066 122.354 1.00 50.65  ? 175  ILE B CD1  1 
ATOM   1095 N N    . SER A 1 176 ? 116.441 152.891 127.171 1.00 49.15  ? 176  SER B N    1 
ATOM   1096 C CA   . SER A 1 176 ? 115.381 152.705 128.160 1.00 58.28  ? 176  SER B CA   1 
ATOM   1097 C C    . SER A 1 176 ? 115.942 152.692 129.577 1.00 58.99  ? 176  SER B C    1 
ATOM   1098 O O    . SER A 1 176 ? 115.339 153.254 130.499 1.00 63.29  ? 176  SER B O    1 
ATOM   1099 C CB   . SER A 1 176 ? 114.619 151.412 127.878 1.00 66.03  ? 176  SER B CB   1 
ATOM   1100 O OG   . SER A 1 176 ? 113.699 151.138 128.919 1.00 69.71  ? 176  SER B OG   1 
ATOM   1101 N N    . LEU A 1 177 ? 117.089 152.038 129.767 1.00 52.82  ? 177  LEU B N    1 
ATOM   1102 C CA   . LEU A 1 177 ? 117.725 151.985 131.080 1.00 58.42  ? 177  LEU B CA   1 
ATOM   1103 C C    . LEU A 1 177 ? 118.143 153.374 131.546 1.00 62.78  ? 177  LEU B C    1 
ATOM   1104 O O    . LEU A 1 177 ? 118.029 153.703 132.732 1.00 62.47  ? 177  LEU B O    1 
ATOM   1105 C CB   . LEU A 1 177 ? 118.924 151.037 131.027 1.00 57.19  ? 177  LEU B CB   1 
ATOM   1106 C CG   . LEU A 1 177 ? 119.975 151.040 132.137 1.00 50.15  ? 177  LEU B CG   1 
ATOM   1107 C CD1  . LEU A 1 177 ? 119.360 150.753 133.496 1.00 55.71  ? 177  LEU B CD1  1 
ATOM   1108 C CD2  . LEU A 1 177 ? 121.045 150.018 131.816 1.00 50.21  ? 177  LEU B CD2  1 
ATOM   1109 N N    . MET A 1 178 ? 118.643 154.197 130.622 1.00 71.38  ? 178  MET B N    1 
ATOM   1110 C CA   . MET A 1 178 ? 119.154 155.521 130.968 1.00 68.72  ? 178  MET B CA   1 
ATOM   1111 C C    . MET A 1 178 ? 118.036 156.477 131.376 1.00 70.30  ? 178  MET B C    1 
ATOM   1112 O O    . MET A 1 178 ? 118.230 157.327 132.253 1.00 70.57  ? 178  MET B O    1 
ATOM   1113 C CB   . MET A 1 178 ? 119.938 156.092 129.785 1.00 63.34  ? 178  MET B CB   1 
ATOM   1114 C CG   . MET A 1 178 ? 121.438 156.184 130.011 1.00 69.33  ? 178  MET B CG   1 
ATOM   1115 S SD   . MET A 1 178 ? 122.365 156.406 128.477 1.00 79.97  ? 178  MET B SD   1 
ATOM   1116 C CE   . MET A 1 178 ? 121.616 157.901 127.835 1.00 68.00  ? 178  MET B CE   1 
ATOM   1117 N N    . MET A 1 179 ? 116.865 156.365 130.749 1.00 61.87  ? 179  MET B N    1 
ATOM   1118 C CA   . MET A 1 179 ? 115.808 157.353 130.914 1.00 57.47  ? 179  MET B CA   1 
ATOM   1119 C C    . MET A 1 179 ? 114.794 157.024 132.004 1.00 56.77  ? 179  MET B C    1 
ATOM   1120 O O    . MET A 1 179 ? 114.132 157.942 132.500 1.00 65.26  ? 179  MET B O    1 
ATOM   1121 C CB   . MET A 1 179 ? 115.055 157.535 129.591 1.00 56.10  ? 179  MET B CB   1 
ATOM   1122 C CG   . MET A 1 179 ? 115.800 158.337 128.539 1.00 57.94  ? 179  MET B CG   1 
ATOM   1123 S SD   . MET A 1 179 ? 114.848 158.483 127.016 1.00 68.32  ? 179  MET B SD   1 
ATOM   1124 C CE   . MET A 1 179 ? 115.693 159.846 126.226 1.00 62.35  ? 179  MET B CE   1 
ATOM   1125 N N    . LEU A 1 180 ? 114.641 155.762 132.395 1.00 45.00  ? 180  LEU B N    1 
ATOM   1126 C CA   . LEU A 1 180 ? 113.608 155.395 133.362 1.00 54.89  ? 180  LEU B CA   1 
ATOM   1127 C C    . LEU A 1 180 ? 114.129 155.021 134.744 1.00 60.53  ? 180  LEU B C    1 
ATOM   1128 O O    . LEU A 1 180 ? 113.505 155.388 135.741 1.00 59.72  ? 180  LEU B O    1 
ATOM   1129 C CB   . LEU A 1 180 ? 112.761 154.237 132.816 1.00 56.32  ? 180  LEU B CB   1 
ATOM   1130 C CG   . LEU A 1 180 ? 111.556 154.589 131.935 1.00 53.14  ? 180  LEU B CG   1 
ATOM   1131 C CD1  . LEU A 1 180 ? 110.655 155.602 132.633 1.00 53.19  ? 180  LEU B CD1  1 
ATOM   1132 C CD2  . LEU A 1 180 ? 111.968 155.086 130.563 1.00 52.15  ? 180  LEU B CD2  1 
ATOM   1133 N N    . ASN A 1 181 ? 115.230 154.274 134.830 1.00 53.45  ? 181  ASN B N    1 
ATOM   1134 C CA   . ASN A 1 181 ? 115.777 153.884 136.131 1.00 49.03  ? 181  ASN B CA   1 
ATOM   1135 C C    . ASN A 1 181 ? 116.134 155.058 137.042 1.00 56.96  ? 181  ASN B C    1 
ATOM   1136 O O    . ASN A 1 181 ? 115.880 154.954 138.254 1.00 54.75  ? 181  ASN B O    1 
ATOM   1137 C CB   . ASN A 1 181 ? 116.989 152.973 135.920 1.00 47.71  ? 181  ASN B CB   1 
ATOM   1138 C CG   . ASN A 1 181 ? 116.592 151.555 135.542 1.00 48.10  ? 181  ASN B CG   1 
ATOM   1139 O OD1  . ASN A 1 181 ? 116.266 151.276 134.389 1.00 47.27  ? 181  ASN B OD1  1 
ATOM   1140 N ND2  . ASN A 1 181 ? 116.612 150.654 136.518 1.00 51.77  ? 181  ASN B ND2  1 
ATOM   1141 N N    . PRO A 1 182 ? 116.740 156.152 136.562 1.00 63.25  ? 182  PRO B N    1 
ATOM   1142 C CA   . PRO A 1 182 ? 117.068 157.316 137.475 1.00 56.94  ? 182  PRO B CA   1 
ATOM   1143 C C    . PRO A 1 182 ? 115.868 157.884 138.220 1.00 54.81  ? 182  PRO B C    1 
ATOM   1144 O O    . PRO A 1 182 ? 115.999 158.335 139.365 1.00 54.05  ? 182  PRO B O    1 
ATOM   1145 C CB   . PRO A 1 182 ? 117.644 158.293 136.422 1.00 53.35  ? 182  PRO B CB   1 
ATOM   1146 C CG   . PRO A 1 182 ? 117.693 157.450 136.124 1.00 54.17  ? 182  PRO B CG   1 
ATOM   1147 C CD   . PRO A 1 182 ? 117.458 156.544 135.336 1.00 57.38  ? 182  PRO B CD   1 
ATOM   1148 N N    . ILE A 1 183 ? 114.700 157.870 137.577 1.00 56.09  ? 183  ILE B N    1 
ATOM   1149 C CA   . ILE A 1 183 ? 113.459 158.334 138.189 1.00 59.22  ? 183  ILE B CA   1 
ATOM   1150 C C    . ILE A 1 183 ? 113.066 157.474 139.386 1.00 61.23  ? 183  ILE B C    1 
ATOM   1151 O O    . ILE A 1 183 ? 112.665 158.001 140.430 1.00 72.63  ? 183  ILE B O    1 
ATOM   1152 C CB   . ILE A 1 183 ? 112.336 158.390 137.137 1.00 57.97  ? 183  ILE B CB   1 
ATOM   1153 C CG1  . ILE A 1 183 ? 112.773 159.230 135.936 1.00 57.24  ? 183  ILE B CG1  1 
ATOM   1154 C CG2  . ILE A 1 183 ? 111.064 158.960 137.744 1.00 60.88  ? 183  ILE B CG2  1 
ATOM   1155 C CD1  . ILE A 1 183 ? 111.794 159.219 134.793 1.00 58.55  ? 183  ILE B CD1  1 
ATOM   1156 N N    . GLY A 1 184 ? 113.173 156.148 139.265 1.00 54.98  ? 184  GLY B N    1 
ATOM   1157 C CA   . GLY A 1 184 ? 112.811 155.288 140.384 1.00 61.23  ? 184  GLY B CA   1 
ATOM   1158 C C    . GLY A 1 184 ? 113.690 155.470 141.610 1.00 62.78  ? 184  GLY B C    1 
ATOM   1159 O O    . GLY A 1 184 ? 113.190 155.480 142.739 1.00 59.32  ? 184  GLY B O    1 
ATOM   1160 N N    . PHE A 1 185 ? 115.007 155.592 141.417 1.00 63.10  ? 185  PHE B N    1 
ATOM   1161 C CA   . PHE A 1 185 ? 115.896 155.773 142.566 1.00 63.51  ? 185  PHE B CA   1 
ATOM   1162 C C    . PHE A 1 185 ? 115.635 157.097 143.275 1.00 65.64  ? 185  PHE B C    1 
ATOM   1163 O O    . PHE A 1 185 ? 115.930 157.226 144.470 1.00 65.27  ? 185  PHE B O    1 
ATOM   1164 C CB   . PHE A 1 185 ? 117.370 155.657 142.164 1.00 62.98  ? 185  PHE B CB   1 
ATOM   1165 C CG   . PHE A 1 185 ? 117.817 154.249 141.842 1.00 62.16  ? 185  PHE B CG   1 
ATOM   1166 C CD1  . PHE A 1 185 ? 116.908 153.210 141.715 1.00 64.05  ? 185  PHE B CD1  1 
ATOM   1167 C CD2  . PHE A 1 185 ? 119.166 153.966 141.697 1.00 66.12  ? 185  PHE B CD2  1 
ATOM   1168 C CE1  . PHE A 1 185 ? 117.333 151.928 141.436 1.00 68.48  ? 185  PHE B CE1  1 
ATOM   1169 C CE2  . PHE A 1 185 ? 119.596 152.685 141.417 1.00 69.30  ? 185  PHE B CE2  1 
ATOM   1170 C CZ   . PHE A 1 185 ? 118.677 151.666 141.288 1.00 68.19  ? 185  PHE B CZ   1 
ATOM   1171 N N    . ILE A 1 186 ? 115.117 158.094 142.552 1.00 67.67  ? 186  ILE B N    1 
ATOM   1172 C CA   . ILE A 1 186 ? 114.771 159.369 143.173 1.00 64.62  ? 186  ILE B CA   1 
ATOM   1173 C C    . ILE A 1 186 ? 113.665 159.169 144.201 1.00 62.72  ? 186  ILE B C    1 
ATOM   1174 O O    . ILE A 1 186 ? 113.738 159.695 145.318 1.00 64.36  ? 186  ILE B O    1 
ATOM   1175 C CB   . ILE A 1 186 ? 114.372 160.396 142.095 1.00 62.42  ? 186  ILE B CB   1 
ATOM   1176 C CG1  . ILE A 1 186 ? 115.605 160.881 141.329 1.00 64.01  ? 186  ILE B CG1  1 
ATOM   1177 C CG2  . ILE A 1 186 ? 113.630 161.576 142.706 1.00 64.32  ? 186  ILE B CG2  1 
ATOM   1178 C CD1  . ILE A 1 186 ? 115.277 161.590 140.033 1.00 62.00  ? 186  ILE B CD1  1 
ATOM   1179 N N    . PHE A 1 187 ? 112.642 158.383 143.851 1.00 63.63  ? 187  PHE B N    1 
ATOM   1180 C CA   . PHE A 1 187 ? 111.496 158.201 144.739 1.00 65.83  ? 187  PHE B CA   1 
ATOM   1181 C C    . PHE A 1 187 ? 111.900 157.462 146.009 1.00 71.36  ? 187  PHE B C    1 
ATOM   1182 O O    . PHE A 1 187 ? 111.489 157.835 147.113 1.00 77.70  ? 187  PHE B O    1 
ATOM   1183 C CB   . PHE A 1 187 ? 110.371 157.457 144.017 1.00 64.91  ? 187  PHE B CB   1 
ATOM   1184 C CG   . PHE A 1 187 ? 109.543 158.329 143.114 1.00 65.66  ? 187  PHE B CG   1 
ATOM   1185 C CD1  . PHE A 1 187 ? 110.024 158.732 141.881 1.00 64.98  ? 187  PHE B CD1  1 
ATOM   1186 C CD2  . PHE A 1 187 ? 108.275 158.736 143.497 1.00 65.44  ? 187  PHE B CD2  1 
ATOM   1187 C CE1  . PHE A 1 187 ? 109.262 159.530 141.049 1.00 65.27  ? 187  PHE B CE1  1 
ATOM   1188 C CE2  . PHE A 1 187 ? 107.508 159.533 142.670 1.00 68.52  ? 187  PHE B CE2  1 
ATOM   1189 C CZ   . PHE A 1 187 ? 108.003 159.931 141.444 1.00 68.48  ? 187  PHE B CZ   1 
ATOM   1190 N N    . CYS A 1 188 ? 112.670 156.379 145.864 1.00 76.34  ? 188  CYS B N    1 
ATOM   1191 C CA   . CYS A 1 188 ? 113.067 155.585 147.023 1.00 77.90  ? 188  CYS B CA   1 
ATOM   1192 C C    . CYS A 1 188 ? 113.931 156.396 147.985 1.00 78.86  ? 188  CYS B C    1 
ATOM   1193 O O    . CYS A 1 188 ? 113.801 156.265 149.208 1.00 81.80  ? 188  CYS B O    1 
ATOM   1194 C CB   . CYS A 1 188 ? 113.800 154.324 146.569 1.00 76.83  ? 188  CYS B CB   1 
ATOM   1195 S SG   . CYS A 1 188 ? 113.759 152.984 147.775 1.00 77.39  ? 188  CYS B SG   1 
ATOM   1196 N N    . GLU A 1 189 ? 114.842 157.215 147.448 1.00 78.15  ? 189  GLU B N    1 
ATOM   1197 C CA   . GLU A 1 189 ? 115.649 158.101 148.286 1.00 78.52  ? 189  GLU B CA   1 
ATOM   1198 C C    . GLU A 1 189 ? 114.781 159.093 149.053 1.00 77.92  ? 189  GLU B C    1 
ATOM   1199 O O    . GLU A 1 189 ? 115.103 159.461 150.190 1.00 76.71  ? 189  GLU B O    1 
ATOM   1200 C CB   . GLU A 1 189 ? 116.680 158.841 147.430 1.00 79.03  ? 189  GLU B CB   1 
ATOM   1201 C CG   . GLU A 1 189 ? 117.939 158.039 147.087 1.00 81.85  ? 189  GLU B CG   1 
ATOM   1202 C CD   . GLU A 1 189 ? 118.787 157.646 148.295 1.00 83.15  ? 189  GLU B CD   1 
ATOM   1203 O OE1  . GLU A 1 189 ? 118.566 158.167 149.410 1.00 80.42  ? 189  GLU B OE1  1 
ATOM   1204 O OE2  . GLU A 1 189 ? 119.687 156.799 148.124 1.00 83.42  ? 189  GLU B OE2  1 
ATOM   1205 N N    . ILE A 1 190 ? 113.693 159.558 148.433 1.00 75.58  ? 190  ILE B N    1 
ATOM   1206 C CA   . ILE A 1 190 ? 112.736 160.427 149.115 1.00 73.30  ? 190  ILE B CA   1 
ATOM   1207 C C    . ILE A 1 190 ? 112.139 159.725 150.330 1.00 77.54  ? 190  ILE B C    1 
ATOM   1208 O O    . ILE A 1 190 ? 111.944 160.342 151.386 1.00 83.81  ? 190  ILE B O    1 
ATOM   1209 C CB   . ILE A 1 190 ? 111.651 160.913 148.133 1.00 74.92  ? 190  ILE B CB   1 
ATOM   1210 C CG1  . ILE A 1 190 ? 112.257 161.871 147.107 1.00 76.67  ? 190  ILE B CG1  1 
ATOM   1211 C CG2  . ILE A 1 190 ? 110.504 161.595 148.863 1.00 77.27  ? 190  ILE B CG2  1 
ATOM   1212 C CD1  . ILE A 1 190 ? 111.374 162.124 145.908 1.00 80.08  ? 190  ILE B CD1  1 
ATOM   1213 N N    . GLN A 1 191 ? 111.851 158.423 150.209 1.00 86.23  ? 191  GLN B N    1 
ATOM   1214 C CA   . GLN A 1 191 ? 111.377 157.672 151.368 1.00 88.05  ? 191  GLN B CA   1 
ATOM   1215 C C    . GLN A 1 191 ? 112.419 157.639 152.478 1.00 87.20  ? 191  GLN B C    1 
ATOM   1216 O O    . GLN A 1 191 ? 112.075 157.772 153.659 1.00 89.15  ? 191  GLN B O    1 
ATOM   1217 C CB   . GLN A 1 191 ? 111.012 156.247 150.949 1.00 89.70  ? 191  GLN B CB   1 
ATOM   1218 C CG   . GLN A 1 191 ? 111.090 155.210 152.059 1.00 88.57  ? 191  GLN B CG   1 
ATOM   1219 C CD   . GLN A 1 191 ? 109.830 155.162 152.898 1.00 90.80  ? 191  GLN B CD   1 
ATOM   1220 O OE1  . GLN A 1 191 ? 108.721 155.076 152.370 1.00 87.89  ? 191  GLN B OE1  1 
ATOM   1221 N NE2  . GLN A 1 191 ? 109.993 155.220 154.215 1.00 92.10  ? 191  GLN B NE2  1 
ATOM   1222 N N    . LYS A 1 192 ? 113.695 157.453 152.124 1.00 87.09  ? 192  LYS B N    1 
ATOM   1223 C CA   . LYS A 1 192 ? 114.734 157.467 153.148 1.00 90.78  ? 192  LYS B CA   1 
ATOM   1224 C C    . LYS A 1 192 ? 114.803 158.831 153.824 1.00 92.90  ? 192  LYS B C    1 
ATOM   1225 O O    . LYS A 1 192 ? 114.969 158.923 155.046 1.00 91.09  ? 192  LYS B O    1 
ATOM   1226 C CB   . LYS A 1 192 ? 116.084 157.097 152.534 1.00 92.96  ? 192  LYS B CB   1 
ATOM   1227 C CG   . LYS A 1 192 ? 117.074 156.503 153.522 1.00 93.57  ? 192  LYS B CG   1 
ATOM   1228 C CD   . LYS A 1 192 ? 118.243 155.850 152.803 1.00 91.56  ? 192  LYS B CD   1 
ATOM   1229 C CE   . LYS A 1 192 ? 117.772 154.745 151.870 1.00 90.14  ? 192  LYS B CE   1 
ATOM   1230 N NZ   . LYS A 1 192 ? 117.670 153.433 152.567 1.00 90.72  ? 192  LYS B NZ   1 
ATOM   1231 N N    . TRP A 1 193 ? 114.687 159.902 153.032 1.00 96.24  ? 193  TRP B N    1 
ATOM   1232 C CA   . TRP A 1 193 ? 114.638 161.253 153.580 1.00 94.57  ? 193  TRP B CA   1 
ATOM   1233 C C    . TRP A 1 193 ? 113.396 161.464 154.439 1.00 92.99  ? 193  TRP B C    1 
ATOM   1234 O O    . TRP A 1 193 ? 113.467 162.083 155.507 1.00 93.23  ? 193  TRP B O    1 
ATOM   1235 C CB   . TRP A 1 193 ? 114.689 162.278 152.447 1.00 94.19  ? 193  TRP B CB   1 
ATOM   1236 N N    . LYS A 1 194 ? 112.241 160.975 153.970 1.00 98.39  ? 194  LYS B N    1 
ATOM   1237 C CA   . LYS A 1 194 ? 110.998 161.148 154.717 1.00 98.51  ? 194  LYS B CA   1 
ATOM   1238 C C    . LYS A 1 194 ? 111.050 160.447 156.067 1.00 100.12 ? 194  LYS B C    1 
ATOM   1239 O O    . LYS A 1 194 ? 110.638 161.017 157.085 1.00 100.15 ? 194  LYS B O    1 
ATOM   1240 C CB   . LYS A 1 194 ? 109.816 160.635 153.894 1.00 99.22  ? 194  LYS B CB   1 
ATOM   1241 N N    . ASP A 1 195 ? 111.536 159.203 156.096 1.00 109.02 ? 195  ASP B N    1 
ATOM   1242 C CA   . ASP A 1 195 ? 111.581 158.465 157.354 1.00 111.13 ? 195  ASP B CA   1 
ATOM   1243 C C    . ASP A 1 195 ? 112.609 159.070 158.302 1.00 111.47 ? 195  ASP B C    1 
ATOM   1244 O O    . ASP A 1 195 ? 112.544 158.864 159.520 1.00 111.01 ? 195  ASP B O    1 
ATOM   1245 C CB   . ASP A 1 195 ? 111.892 156.992 157.089 1.00 108.34 ? 195  ASP B CB   1 
ATOM   1246 N N    . THR A 1 196 ? 113.566 159.822 157.755 1.00 114.36 ? 196  THR B N    1 
ATOM   1247 C CA   . THR A 1 196 ? 114.596 160.490 158.537 1.00 114.53 ? 196  THR B CA   1 
ATOM   1248 C C    . THR A 1 196 ? 114.123 161.783 159.189 1.00 114.96 ? 196  THR B C    1 
ATOM   1249 O O    . THR A 1 196 ? 114.968 162.499 159.739 1.00 114.77 ? 196  THR B O    1 
ATOM   1250 C CB   . THR A 1 196 ? 115.814 160.785 157.659 1.00 114.99 ? 196  THR B CB   1 
ATOM   1251 N N    . GLN A 1 197 ? 112.829 162.120 159.090 1.00 120.82 ? 197  GLN B N    1 
ATOM   1252 C CA   . GLN A 1 197 ? 112.256 163.302 159.735 1.00 120.67 ? 197  GLN B CA   1 
ATOM   1253 C C    . GLN A 1 197 ? 112.854 164.550 159.096 1.00 122.72 ? 197  GLN B C    1 
ATOM   1254 O O    . GLN A 1 197 ? 113.640 165.262 159.729 1.00 122.18 ? 197  GLN B O    1 
ATOM   1255 C CB   . GLN A 1 197 ? 112.460 163.291 161.256 1.00 120.51 ? 197  GLN B CB   1 
ATOM   1256 N N    . ASN A 1 198 ? 112.488 164.821 157.846 1.00 131.43 ? 198  ASN B N    1 
ATOM   1257 C CA   . ASN A 1 198 ? 113.063 165.940 157.111 1.00 131.32 ? 198  ASN B CA   1 
ATOM   1258 C C    . ASN A 1 198 ? 111.966 166.678 156.358 1.00 131.55 ? 198  ASN B C    1 
ATOM   1259 O O    . ASN A 1 198 ? 110.777 166.549 156.658 1.00 131.79 ? 198  ASN B O    1 
ATOM   1260 C CB   . ASN A 1 198 ? 114.158 165.466 156.149 1.00 129.38 ? 198  ASN B CB   1 
ATOM   1261 N N    . ALA A 1 199 ? 112.393 167.458 155.366 1.00 135.57 ? 199  ALA B N    1 
ATOM   1262 C CA   . ALA A 1 199 ? 111.502 168.282 154.559 1.00 135.53 ? 199  ALA B CA   1 
ATOM   1263 C C    . ALA A 1 199 ? 111.985 168.366 153.118 1.00 135.24 ? 199  ALA B C    1 
ATOM   1264 O O    . ALA A 1 199 ? 112.679 167.466 152.635 1.00 135.62 ? 199  ALA B O    1 
ATOM   1265 C CB   . ALA A 1 199 ? 111.379 169.684 155.160 1.00 135.41 ? 199  ALA B CB   1 
ATOM   1266 N N    . SER A 1 200 ? 111.624 169.443 152.424 1.00 128.79 ? 200  SER B N    1 
ATOM   1267 C CA   . SER A 1 200 ? 112.123 169.688 151.072 1.00 127.66 ? 200  SER B CA   1 
ATOM   1268 C C    . SER A 1 200 ? 113.488 170.360 151.044 1.00 129.28 ? 200  SER B C    1 
ATOM   1269 O O    . SER A 1 200 ? 113.818 171.059 150.076 1.00 128.65 ? 200  SER B O    1 
ATOM   1270 C CB   . SER A 1 200 ? 111.117 170.535 150.291 1.00 127.84 ? 200  SER B CB   1 
ATOM   1271 N N    . GLN A 1 201 ? 114.278 170.150 152.095 1.00 131.01 ? 201  GLN B N    1 
ATOM   1272 C CA   . GLN A 1 201 ? 115.550 170.840 152.238 1.00 130.25 ? 201  GLN B CA   1 
ATOM   1273 C C    . GLN A 1 201 ? 116.608 170.065 151.465 1.00 129.18 ? 201  GLN B C    1 
ATOM   1274 O O    . GLN A 1 201 ? 116.629 168.830 151.497 1.00 127.95 ? 201  GLN B O    1 
ATOM   1275 C CB   . GLN A 1 201 ? 115.935 170.958 153.712 1.00 128.32 ? 201  GLN B CB   1 
ATOM   1276 N N    . ASN A 1 202 ? 117.453 170.798 150.737 1.00 117.17 ? 202  ASN B N    1 
ATOM   1277 C CA   . ASN A 1 202 ? 118.530 170.231 149.923 1.00 115.75 ? 202  ASN B CA   1 
ATOM   1278 C C    . ASN A 1 202 ? 117.952 169.370 148.800 1.00 115.09 ? 202  ASN B C    1 
ATOM   1279 O O    . ASN A 1 202 ? 118.248 168.180 148.668 1.00 114.86 ? 202  ASN B O    1 
ATOM   1280 C CB   . ASN A 1 202 ? 119.538 169.447 150.771 1.00 116.98 ? 202  ASN B CB   1 
ATOM   1281 N N    . LYS A 1 203 ? 117.098 170.003 147.987 1.00 115.35 ? 203  LYS B N    1 
ATOM   1282 C CA   . LYS A 1 203 ? 116.428 169.340 146.871 1.00 115.80 ? 203  LYS B CA   1 
ATOM   1283 C C    . LYS A 1 203 ? 117.437 168.888 145.823 1.00 114.77 ? 203  LYS B C    1 
ATOM   1284 O O    . LYS A 1 203 ? 117.179 167.971 145.037 1.00 112.34 ? 203  LYS B O    1 
ATOM   1285 C CB   . LYS A 1 203 ? 115.389 170.280 146.253 1.00 113.63 ? 203  LYS B CB   1 
ATOM   1286 N N    . ILE A 1 204 ? 118.598 169.543 145.808 1.00 116.20 ? 204  ILE B N    1 
ATOM   1287 C CA   . ILE A 1 204 ? 119.677 169.200 144.886 1.00 116.85 ? 204  ILE B CA   1 
ATOM   1288 C C    . ILE A 1 204 ? 120.237 167.826 145.230 1.00 115.81 ? 204  ILE B C    1 
ATOM   1289 O O    . ILE A 1 204 ? 120.487 166.995 144.349 1.00 116.68 ? 204  ILE B O    1 
ATOM   1290 C CB   . ILE A 1 204 ? 120.774 170.277 144.916 1.00 116.15 ? 204  ILE B CB   1 
ATOM   1291 C CG1  . ILE A 1 204 ? 120.204 171.633 144.495 1.00 116.32 ? 204  ILE B CG1  1 
ATOM   1292 C CG2  . ILE A 1 204 ? 121.939 169.890 144.015 1.00 115.39 ? 204  ILE B CG2  1 
ATOM   1293 C CD1  . ILE A 1 204 ? 119.452 171.600 143.181 1.00 116.88 ? 204  ILE B CD1  1 
ATOM   1294 N N    . LYS A 1 205 ? 120.440 167.568 146.520 1.00 106.12 ? 205  LYS B N    1 
ATOM   1295 C CA   . LYS A 1 205 ? 121.100 166.342 146.944 1.00 106.07 ? 205  LYS B CA   1 
ATOM   1296 C C    . LYS A 1 205 ? 120.248 165.098 146.706 1.00 106.01 ? 205  LYS B C    1 
ATOM   1297 O O    . LYS A 1 205 ? 120.793 164.040 146.371 1.00 103.85 ? 205  LYS B O    1 
ATOM   1298 C CB   . LYS A 1 205 ? 121.443 166.458 148.436 1.00 109.45 ? 205  LYS B CB   1 
ATOM   1299 C CG   . LYS A 1 205 ? 121.558 165.138 149.193 1.00 110.78 ? 205  LYS B CG   1 
ATOM   1300 C CD   . LYS A 1 205 ? 121.973 165.345 150.642 1.00 108.17 ? 205  LYS B CD   1 
ATOM   1301 C CE   . LYS A 1 205 ? 123.306 166.058 150.765 1.00 106.74 ? 205  LYS B CE   1 
ATOM   1302 N NZ   . LYS A 1 205 ? 123.852 165.965 152.149 1.00 106.06 ? 205  LYS B NZ   1 
ATOM   1303 N N    . ILE A 1 206 ? 118.923 165.200 146.849 1.00 103.26 ? 206  ILE B N    1 
ATOM   1304 C CA   . ILE A 1 206 ? 118.076 164.054 146.520 1.00 103.46 ? 206  ILE B CA   1 
ATOM   1305 C C    . ILE A 1 206 ? 118.161 163.717 145.028 1.00 102.49 ? 206  ILE B C    1 
ATOM   1306 O O    . ILE A 1 206 ? 118.258 162.542 144.652 1.00 101.38 ? 206  ILE B O    1 
ATOM   1307 C CB   . ILE A 1 206 ? 116.626 164.273 147.023 1.00 102.72 ? 206  ILE B CB   1 
ATOM   1308 C CG1  . ILE A 1 206 ? 115.738 165.067 146.055 1.00 101.43 ? 206  ILE B CG1  1 
ATOM   1309 C CG2  . ILE A 1 206 ? 116.634 164.937 148.393 1.00 101.91 ? 206  ILE B CG2  1 
ATOM   1310 C CD1  . ILE A 1 206 ? 114.262 164.964 146.357 1.00 101.37 ? 206  ILE B CD1  1 
ATOM   1311 N N    . VAL A 1 207 ? 118.110 164.732 144.158 1.00 94.83  ? 207  VAL B N    1 
ATOM   1312 C CA   . VAL A 1 207 ? 118.301 164.516 142.725 1.00 92.93  ? 207  VAL B CA   1 
ATOM   1313 C C    . VAL A 1 207 ? 119.702 163.995 142.430 1.00 93.89  ? 207  VAL B C    1 
ATOM   1314 O O    . VAL A 1 207 ? 119.882 163.039 141.665 1.00 95.53  ? 207  VAL B O    1 
ATOM   1315 C CB   . VAL A 1 207 ? 118.007 165.811 141.946 1.00 92.82  ? 207  VAL B CB   1 
ATOM   1316 C CG1  . VAL A 1 207 ? 118.397 165.662 140.484 1.00 94.31  ? 207  VAL B CG1  1 
ATOM   1317 C CG2  . VAL A 1 207 ? 116.539 166.179 142.067 1.00 93.27  ? 207  VAL B CG2  1 
ATOM   1318 N N    . GLY A 1 208 ? 120.715 164.611 143.045 1.00 95.78  ? 208  GLY B N    1 
ATOM   1319 C CA   . GLY A 1 208 ? 122.080 164.155 142.839 1.00 97.43  ? 208  GLY B CA   1 
ATOM   1320 C C    . GLY A 1 208 ? 122.358 162.749 143.331 1.00 96.82  ? 208  GLY B C    1 
ATOM   1321 O O    . GLY A 1 208 ? 123.152 162.024 142.727 1.00 97.31  ? 208  GLY B O    1 
ATOM   1322 N N    . LEU A 1 209 ? 121.744 162.353 144.451 1.00 93.81  ? 209  LEU B N    1 
ATOM   1323 C CA   . LEU A 1 209 ? 121.999 161.008 144.957 1.00 95.18  ? 209  LEU B CA   1 
ATOM   1324 C C    . LEU A 1 209 ? 121.506 159.937 143.991 1.00 95.90  ? 209  LEU B C    1 
ATOM   1325 O O    . LEU A 1 209 ? 122.179 158.919 143.792 1.00 95.55  ? 209  LEU B O    1 
ATOM   1326 C CB   . LEU A 1 209 ? 121.349 160.832 146.329 1.00 96.50  ? 209  LEU B CB   1 
ATOM   1327 C CG   . LEU A 1 209 ? 122.288 160.836 147.538 1.00 96.94  ? 209  LEU B CG   1 
ATOM   1328 C CD1  . LEU A 1 209 ? 123.214 162.045 147.512 1.00 96.27  ? 209  LEU B CD1  1 
ATOM   1329 C CD2  . LEU A 1 209 ? 121.497 160.792 148.837 1.00 94.96  ? 209  LEU B CD2  1 
ATOM   1330 N N    . GLY A 1 210 ? 120.327 160.139 143.397 1.00 95.31  ? 210  GLY B N    1 
ATOM   1331 C CA   . GLY A 1 210 ? 119.836 159.176 142.427 1.00 95.77  ? 210  GLY B CA   1 
ATOM   1332 C C    . GLY A 1 210 ? 120.691 159.084 141.178 1.00 94.59  ? 210  GLY B C    1 
ATOM   1333 O O    . GLY A 1 210 ? 120.961 157.988 140.679 1.00 97.03  ? 210  GLY B O    1 
ATOM   1334 N N    . LEU A 1 211 ? 121.111 160.237 140.645 1.00 82.24  ? 211  LEU B N    1 
ATOM   1335 C CA   . LEU A 1 211 ? 121.934 160.237 139.439 1.00 84.11  ? 211  LEU B CA   1 
ATOM   1336 C C    . LEU A 1 211 ? 123.293 159.591 139.670 1.00 86.78  ? 211  LEU B C    1 
ATOM   1337 O O    . LEU A 1 211 ? 123.782 158.848 138.811 1.00 91.48  ? 211  LEU B O    1 
ATOM   1338 C CB   . LEU A 1 211 ? 122.100 161.665 138.909 1.00 84.43  ? 211  LEU B CB   1 
ATOM   1339 C CG   . LEU A 1 211 ? 121.067 162.205 137.908 1.00 81.68  ? 211  LEU B CG   1 
ATOM   1340 C CD1  . LEU A 1 211 ? 119.649 162.168 138.454 1.00 83.10  ? 211  LEU B CD1  1 
ATOM   1341 C CD2  . LEU A 1 211 ? 121.427 163.619 137.471 1.00 81.75  ? 211  LEU B CD2  1 
ATOM   1342 N N    . LEU A 1 212 ? 123.928 159.879 140.811 1.00 84.93  ? 212  LEU B N    1 
ATOM   1343 C CA   . LEU A 1 212 ? 125.256 159.328 141.067 1.00 84.60  ? 212  LEU B CA   1 
ATOM   1344 C C    . LEU A 1 212 ? 125.239 157.808 141.176 1.00 85.30  ? 212  LEU B C    1 
ATOM   1345 O O    . LEU A 1 212 ? 126.146 157.138 140.671 1.00 84.87  ? 212  LEU B O    1 
ATOM   1346 C CB   . LEU A 1 212 ? 125.844 159.945 142.335 1.00 85.69  ? 212  LEU B CB   1 
ATOM   1347 C CG   . LEU A 1 212 ? 127.296 159.571 142.640 1.00 84.32  ? 212  LEU B CG   1 
ATOM   1348 C CD1  . LEU A 1 212 ? 128.261 160.568 142.007 1.00 83.65  ? 212  LEU B CD1  1 
ATOM   1349 C CD2  . LEU A 1 212 ? 127.526 159.463 144.138 1.00 87.26  ? 212  LEU B CD2  1 
ATOM   1350 N N    . ARG A 1 213 ? 124.209 157.245 141.816 1.00 86.20  ? 213  ARG B N    1 
ATOM   1351 C CA   . ARG A 1 213 ? 124.145 155.794 141.967 1.00 87.77  ? 213  ARG B CA   1 
ATOM   1352 C C    . ARG A 1 213 ? 123.952 155.066 140.642 1.00 88.20  ? 213  ARG B C    1 
ATOM   1353 O O    . ARG A 1 213 ? 124.461 153.953 140.471 1.00 89.27  ? 213  ARG B O    1 
ATOM   1354 C CB   . ARG A 1 213 ? 123.028 155.413 142.940 1.00 86.09  ? 213  ARG B CB   1 
ATOM   1355 C CG   . ARG A 1 213 ? 123.209 154.038 143.566 1.00 89.28  ? 213  ARG B CG   1 
ATOM   1356 C CD   . ARG A 1 213 ? 121.995 153.614 144.377 1.00 89.22  ? 213  ARG B CD   1 
ATOM   1357 N NE   . ARG A 1 213 ? 121.591 154.632 145.338 1.00 90.52  ? 213  ARG B NE   1 
ATOM   1358 C CZ   . ARG A 1 213 ? 122.038 154.693 146.585 1.00 90.20  ? 213  ARG B CZ   1 
ATOM   1359 N NH1  . ARG A 1 213 ? 122.900 153.806 147.053 1.00 88.47  ? 213  ARG B NH1  1 
ATOM   1360 N NH2  . ARG A 1 213 ? 121.607 155.665 147.382 1.00 90.54  ? 213  ARG B NH2  1 
ATOM   1361 N N    . VAL A 1 214 ? 123.215 155.664 139.706 1.00 83.09  ? 214  VAL B N    1 
ATOM   1362 C CA   . VAL A 1 214 ? 123.031 155.055 138.392 1.00 86.45  ? 214  VAL B CA   1 
ATOM   1363 C C    . VAL A 1 214 ? 124.332 155.038 137.597 1.00 87.62  ? 214  VAL B C    1 
ATOM   1364 O O    . VAL A 1 214 ? 124.691 154.024 136.983 1.00 89.68  ? 214  VAL B O    1 
ATOM   1365 C CB   . VAL A 1 214 ? 121.914 155.797 137.635 1.00 85.26  ? 214  VAL B CB   1 
ATOM   1366 C CG1  . VAL A 1 214 ? 121.935 155.456 136.156 1.00 89.14  ? 214  VAL B CG1  1 
ATOM   1367 C CG2  . VAL A 1 214 ? 120.557 155.486 138.246 1.00 84.29  ? 214  VAL B CG2  1 
ATOM   1368 N N    . LEU A 1 215 ? 125.067 156.150 137.614 1.00 75.77  ? 215  LEU B N    1 
ATOM   1369 C CA   . LEU A 1 215 ? 126.324 156.244 136.876 1.00 73.90  ? 215  LEU B CA   1 
ATOM   1370 C C    . LEU A 1 215 ? 127.411 155.302 137.395 1.00 76.98  ? 215  LEU B C    1 
ATOM   1371 O O    . LEU A 1 215 ? 128.159 154.728 136.594 1.00 80.42  ? 215  LEU B O    1 
ATOM   1372 C CB   . LEU A 1 215 ? 126.802 157.701 136.894 1.00 75.37  ? 215  LEU B CB   1 
ATOM   1373 C CG   . LEU A 1 215 ? 127.768 158.261 135.840 1.00 78.57  ? 215  LEU B CG   1 
ATOM   1374 C CD1  . LEU A 1 215 ? 127.710 159.778 135.872 1.00 76.65  ? 215  LEU B CD1  1 
ATOM   1375 C CD2  . LEU A 1 215 ? 129.209 157.809 136.036 1.00 77.15  ? 215  LEU B CD2  1 
ATOM   1376 N N    . GLN A 1 216 ? 127.531 155.117 138.716 1.00 68.87  ? 216  GLN B N    1 
ATOM   1377 C CA   . GLN A 1 216 ? 128.594 154.211 139.162 1.00 68.01  ? 216  GLN B CA   1 
ATOM   1378 C C    . GLN A 1 216 ? 128.337 152.735 138.874 1.00 60.97  ? 216  GLN B C    1 
ATOM   1379 O O    . GLN A 1 216 ? 129.253 151.938 139.086 1.00 62.27  ? 216  GLN B O    1 
ATOM   1380 C CB   . GLN A 1 216 ? 128.850 154.333 140.665 1.00 70.75  ? 216  GLN B CB   1 
ATOM   1381 C CG   . GLN A 1 216 ? 127.614 154.407 141.533 1.00 72.25  ? 216  GLN B CG   1 
ATOM   1382 C CD   . GLN A 1 216 ? 127.951 154.704 142.980 1.00 70.32  ? 216  GLN B CD   1 
ATOM   1383 O OE1  . GLN A 1 216 ? 128.373 155.810 143.314 1.00 68.62  ? 216  GLN B OE1  1 
ATOM   1384 N NE2  . GLN A 1 216 ? 127.773 153.711 143.850 1.00 67.02  ? 216  GLN B NE2  1 
ATOM   1385 N N    . ASN A 1 217 ? 127.139 152.349 138.443 1.00 58.55  ? 217  ASN B N    1 
ATOM   1386 C CA   . ASN A 1 217 ? 126.877 150.955 138.063 1.00 65.11  ? 217  ASN B CA   1 
ATOM   1387 C C    . ASN A 1 217 ? 127.692 150.550 136.836 1.00 64.98  ? 217  ASN B C    1 
ATOM   1388 O O    . ASN A 1 217 ? 127.695 151.282 135.841 1.00 63.68  ? 217  ASN B O    1 
ATOM   1389 C CB   . ASN A 1 217 ? 125.385 150.745 137.790 1.00 63.63  ? 217  ASN B CB   1 
ATOM   1390 C CG   . ASN A 1 217 ? 124.979 149.279 137.859 1.00 62.27  ? 217  ASN B CG   1 
ATOM   1391 O OD1  . ASN A 1 217 ? 125.707 148.450 138.396 1.00 63.43  ? 217  ASN B OD1  1 
ATOM   1392 N ND2  . ASN A 1 217 ? 123.803 148.959 137.322 1.00 65.03  ? 217  ASN B ND2  1 
ATOM   1393 N N    . PRO A 1 218 ? 128.403 149.401 136.860 1.00 64.74  ? 218  PRO B N    1 
ATOM   1394 C CA   . PRO A 1 218 ? 129.221 149.010 135.701 1.00 58.41  ? 218  PRO B CA   1 
ATOM   1395 C C    . PRO A 1 218 ? 128.435 148.735 134.422 1.00 64.96  ? 218  PRO B C    1 
ATOM   1396 O O    . PRO A 1 218 ? 128.735 147.761 133.729 1.00 68.21  ? 218  PRO B O    1 
ATOM   1397 C CB   . PRO A 1 218 ? 129.854 147.690 136.188 1.00 60.14  ? 218  PRO B CB   1 
ATOM   1398 C CG   . PRO A 1 218 ? 129.489 147.623 137.708 1.00 64.05  ? 218  PRO B CG   1 
ATOM   1399 C CD   . PRO A 1 218 ? 129.184 149.019 138.037 1.00 67.66  ? 218  PRO B CD   1 
ATOM   1400 N N    . ILE A 1 219 ? 127.434 149.545 134.087 1.00 66.40  ? 219  ILE B N    1 
ATOM   1401 C CA   . ILE A 1 219 ? 126.679 149.363 132.851 1.00 59.31  ? 219  ILE B CA   1 
ATOM   1402 C C    . ILE A 1 219 ? 126.607 150.698 132.127 1.00 64.43  ? 219  ILE B C    1 
ATOM   1403 O O    . ILE A 1 219 ? 126.832 150.781 130.916 1.00 65.38  ? 219  ILE B O    1 
ATOM   1404 C CB   . ILE A 1 219 ? 125.275 148.793 133.116 1.00 57.43  ? 219  ILE B CB   1 
ATOM   1405 C CG1  . ILE A 1 219 ? 125.367 147.391 133.726 1.00 59.34  ? 219  ILE B CG1  1 
ATOM   1406 C CG2  . ILE A 1 219 ? 124.486 148.739 131.828 1.00 57.75  ? 219  ILE B CG2  1 
ATOM   1407 C CD1  . ILE A 1 219 ? 124.038 146.821 134.172 1.00 64.59  ? 219  ILE B CD1  1 
ATOM   1408 N N    . VAL A 1 220 ? 126.289 151.747 132.885 1.00 74.93  ? 220  VAL B N    1 
ATOM   1409 C CA   . VAL A 1 220 ? 126.128 153.086 132.334 1.00 75.35  ? 220  VAL B CA   1 
ATOM   1410 C C    . VAL A 1 220 ? 127.475 153.641 131.898 1.00 71.75  ? 220  VAL B C    1 
ATOM   1411 O O    . VAL A 1 220 ? 127.586 154.292 130.854 1.00 67.79  ? 220  VAL B O    1 
ATOM   1412 C CB   . VAL A 1 220 ? 125.429 153.999 133.356 1.00 69.74  ? 220  VAL B CB   1 
ATOM   1413 C CG1  . VAL A 1 220 ? 125.149 155.363 132.747 1.00 68.62  ? 220  VAL B CG1  1 
ATOM   1414 C CG2  . VAL A 1 220 ? 124.139 153.359 133.828 1.00 65.50  ? 220  VAL B CG2  1 
ATOM   1415 N N    . PHE A 1 221 ? 128.507 153.446 132.719 1.00 68.77  ? 221  PHE B N    1 
ATOM   1416 C CA   . PHE A 1 221 ? 129.810 154.025 132.420 1.00 65.46  ? 221  PHE B CA   1 
ATOM   1417 C C    . PHE A 1 221 ? 130.399 153.443 131.139 1.00 73.98  ? 221  PHE B C    1 
ATOM   1418 O O    . PHE A 1 221 ? 131.007 154.171 130.348 1.00 79.19  ? 221  PHE B O    1 
ATOM   1419 C CB   . PHE A 1 221 ? 130.757 153.803 133.598 1.00 64.25  ? 221  PHE B CB   1 
ATOM   1420 C CG   . PHE A 1 221 ? 132.103 154.443 133.425 1.00 74.90  ? 221  PHE B CG   1 
ATOM   1421 C CD1  . PHE A 1 221 ? 132.236 155.821 133.429 1.00 78.96  ? 221  PHE B CD1  1 
ATOM   1422 C CD2  . PHE A 1 221 ? 133.238 153.664 133.262 1.00 77.61  ? 221  PHE B CD2  1 
ATOM   1423 C CE1  . PHE A 1 221 ? 133.476 156.415 133.270 1.00 77.07  ? 221  PHE B CE1  1 
ATOM   1424 C CE2  . PHE A 1 221 ? 134.482 154.252 133.103 1.00 79.23  ? 221  PHE B CE2  1 
ATOM   1425 C CZ   . PHE A 1 221 ? 134.600 155.628 133.107 1.00 77.50  ? 221  PHE B CZ   1 
ATOM   1426 N N    . MET A 1 222 ? 130.234 152.135 130.910 1.00 55.16  ? 222  MET B N    1 
ATOM   1427 C CA   . MET A 1 222 ? 130.824 151.541 129.715 1.00 52.91  ? 222  MET B CA   1 
ATOM   1428 C C    . MET A 1 222 ? 130.005 151.773 128.447 1.00 49.44  ? 222  MET B C    1 
ATOM   1429 O O    . MET A 1 222 ? 130.539 151.595 127.347 1.00 45.96  ? 222  MET B O    1 
ATOM   1430 C CB   . MET A 1 222 ? 131.023 150.038 129.919 1.00 48.37  ? 222  MET B CB   1 
ATOM   1431 C CG   . MET A 1 222 ? 131.964 149.693 131.057 1.00 52.98  ? 222  MET B CG   1 
ATOM   1432 S SD   . MET A 1 222 ? 133.562 150.510 130.910 1.00 58.76  ? 222  MET B SD   1 
ATOM   1433 C CE   . MET A 1 222 ? 134.410 149.390 129.800 1.00 58.39  ? 222  MET B CE   1 
ATOM   1434 N N    . VAL A 1 223 ? 128.732 152.154 128.562 1.00 50.57  ? 223  VAL B N    1 
ATOM   1435 C CA   . VAL A 1 223 ? 127.965 152.510 127.370 1.00 53.59  ? 223  VAL B CA   1 
ATOM   1436 C C    . VAL A 1 223 ? 128.378 153.895 126.873 1.00 50.75  ? 223  VAL B C    1 
ATOM   1437 O O    . VAL A 1 223 ? 128.500 154.121 125.664 1.00 50.09  ? 223  VAL B O    1 
ATOM   1438 C CB   . VAL A 1 223 ? 126.438 152.364 127.588 1.00 54.72  ? 223  VAL B CB   1 
ATOM   1439 C CG1  . VAL A 1 223 ? 125.817 153.485 128.408 1.00 52.23  ? 223  VAL B CG1  1 
ATOM   1440 C CG2  . VAL A 1 223 ? 125.727 152.242 126.246 1.00 51.81  ? 223  VAL B CG2  1 
ATOM   1441 N N    . PHE A 1 224 ? 128.578 154.839 127.800 1.00 51.20  ? 224  PHE B N    1 
ATOM   1442 C CA   . PHE A 1 224 ? 129.021 156.185 127.450 1.00 50.23  ? 224  PHE B CA   1 
ATOM   1443 C C    . PHE A 1 224 ? 130.394 156.173 126.793 1.00 55.09  ? 224  PHE B C    1 
ATOM   1444 O O    . PHE A 1 224 ? 130.623 156.888 125.810 1.00 56.31  ? 224  PHE B O    1 
ATOM   1445 C CB   . PHE A 1 224 ? 129.058 157.055 128.707 1.00 52.25  ? 224  PHE B CB   1 
ATOM   1446 C CG   . PHE A 1 224 ? 127.760 157.737 129.020 1.00 54.37  ? 224  PHE B CG   1 
ATOM   1447 C CD1  . PHE A 1 224 ? 126.651 157.001 129.397 1.00 55.10  ? 224  PHE B CD1  1 
ATOM   1448 C CD2  . PHE A 1 224 ? 127.655 159.116 128.958 1.00 54.89  ? 224  PHE B CD2  1 
ATOM   1449 C CE1  . PHE A 1 224 ? 125.457 157.627 129.694 1.00 58.21  ? 224  PHE B CE1  1 
ATOM   1450 C CE2  . PHE A 1 224 ? 126.463 159.748 129.253 1.00 52.58  ? 224  PHE B CE2  1 
ATOM   1451 C CZ   . PHE A 1 224 ? 125.363 159.002 129.622 1.00 55.22  ? 224  PHE B CZ   1 
ATOM   1452 N N    . ILE A 1 225 ? 131.329 155.392 127.338 1.00 64.46  ? 225  ILE B N    1 
ATOM   1453 C CA   . ILE A 1 225 ? 132.666 155.310 126.756 1.00 63.35  ? 225  ILE B CA   1 
ATOM   1454 C C    . ILE A 1 225 ? 132.616 154.720 125.351 1.00 61.64  ? 225  ILE B C    1 
ATOM   1455 O O    . ILE A 1 225 ? 133.280 155.217 124.432 1.00 62.82  ? 225  ILE B O    1 
ATOM   1456 C CB   . ILE A 1 225 ? 133.591 154.494 127.682 1.00 58.37  ? 225  ILE B CB   1 
ATOM   1457 C CG1  . ILE A 1 225 ? 133.912 155.283 128.952 1.00 55.74  ? 225  ILE B CG1  1 
ATOM   1458 C CG2  . ILE A 1 225 ? 134.876 154.099 126.972 1.00 57.34  ? 225  ILE B CG2  1 
ATOM   1459 C CD1  . ILE A 1 225 ? 134.394 156.692 128.693 1.00 61.19  ? 225  ILE B CD1  1 
ATOM   1460 N N    . GLY A 1 226 ? 131.830 153.656 125.158 1.00 58.15  ? 226  GLY B N    1 
ATOM   1461 C CA   . GLY A 1 226 ? 131.727 153.056 123.835 1.00 56.73  ? 226  GLY B CA   1 
ATOM   1462 C C    . GLY A 1 226 ? 131.168 153.989 122.777 1.00 59.87  ? 226  GLY B C    1 
ATOM   1463 O O    . GLY A 1 226 ? 131.632 153.991 121.634 1.00 62.56  ? 226  GLY B O    1 
ATOM   1464 N N    . ILE A 1 227 ? 130.158 154.786 123.135 1.00 60.57  ? 227  ILE B N    1 
ATOM   1465 C CA   . ILE A 1 227 ? 129.605 155.748 122.184 1.00 59.60  ? 227  ILE B CA   1 
ATOM   1466 C C    . ILE A 1 227 ? 130.622 156.840 121.871 1.00 59.30  ? 227  ILE B C    1 
ATOM   1467 O O    . ILE A 1 227 ? 130.774 157.257 120.715 1.00 55.82  ? 227  ILE B O    1 
ATOM   1468 C CB   . ILE A 1 227 ? 128.289 156.332 122.732 1.00 56.55  ? 227  ILE B CB   1 
ATOM   1469 C CG1  . ILE A 1 227 ? 127.198 155.262 122.761 1.00 54.24  ? 227  ILE B CG1  1 
ATOM   1470 C CG2  . ILE A 1 227 ? 127.823 157.515 121.898 1.00 59.39  ? 227  ILE B CG2  1 
ATOM   1471 C CD1  . ILE A 1 227 ? 125.992 155.647 123.588 1.00 54.51  ? 227  ILE B CD1  1 
ATOM   1472 N N    . ALA A 1 228 ? 131.337 157.310 122.897 1.00 64.79  ? 228  ALA B N    1 
ATOM   1473 C CA   . ALA A 1 228 ? 132.344 158.353 122.719 1.00 62.09  ? 228  ALA B CA   1 
ATOM   1474 C C    . ALA A 1 228 ? 133.473 157.905 121.799 1.00 62.72  ? 228  ALA B C    1 
ATOM   1475 O O    . ALA A 1 228 ? 133.894 158.647 120.905 1.00 67.74  ? 228  ALA B O    1 
ATOM   1476 C CB   . ALA A 1 228 ? 132.897 158.778 124.079 1.00 64.22  ? 228  ALA B CB   1 
ATOM   1477 N N    . PHE A 1 229 ? 133.972 156.685 122.001 1.00 72.57  ? 229  PHE B N    1 
ATOM   1478 C CA   . PHE A 1 229 ? 135.044 156.168 121.159 1.00 78.13  ? 229  PHE B CA   1 
ATOM   1479 C C    . PHE A 1 229 ? 134.582 155.777 119.761 1.00 81.93  ? 229  PHE B C    1 
ATOM   1480 O O    . PHE A 1 229 ? 135.431 155.578 118.885 1.00 86.05  ? 229  PHE B O    1 
ATOM   1481 C CB   . PHE A 1 229 ? 135.691 154.960 121.837 1.00 79.47  ? 229  PHE B CB   1 
ATOM   1482 C CG   . PHE A 1 229 ? 136.796 155.316 122.790 1.00 84.34  ? 229  PHE B CG   1 
ATOM   1483 C CD1  . PHE A 1 229 ? 136.517 155.963 123.983 1.00 83.90  ? 229  PHE B CD1  1 
ATOM   1484 C CD2  . PHE A 1 229 ? 138.110 154.985 122.503 1.00 83.25  ? 229  PHE B CD2  1 
ATOM   1485 C CE1  . PHE A 1 229 ? 137.529 156.288 124.865 1.00 79.76  ? 229  PHE B CE1  1 
ATOM   1486 C CE2  . PHE A 1 229 ? 139.127 155.306 123.383 1.00 81.73  ? 229  PHE B CE2  1 
ATOM   1487 C CZ   . PHE A 1 229 ? 138.835 155.958 124.566 1.00 80.28  ? 229  PHE B CZ   1 
ATOM   1488 N N    . ASN A 1 230 ? 133.273 155.638 119.532 1.00 71.98  ? 230  ASN B N    1 
ATOM   1489 C CA   . ASN A 1 230 ? 132.796 155.317 118.190 1.00 70.12  ? 230  ASN B CA   1 
ATOM   1490 C C    . ASN A 1 230 ? 133.111 156.422 117.187 1.00 70.23  ? 230  ASN B C    1 
ATOM   1491 O O    . ASN A 1 230 ? 133.545 156.140 116.065 1.00 69.42  ? 230  ASN B O    1 
ATOM   1492 C CB   . ASN A 1 230 ? 131.294 155.042 118.221 1.00 72.08  ? 230  ASN B CB   1 
ATOM   1493 C CG   . ASN A 1 230 ? 130.762 154.578 116.883 1.00 74.96  ? 230  ASN B CG   1 
ATOM   1494 O OD1  . ASN A 1 230 ? 131.511 154.070 116.052 1.00 77.57  ? 230  ASN B OD1  1 
ATOM   1495 N ND2  . ASN A 1 230 ? 129.465 154.751 116.666 1.00 71.90  ? 230  ASN B ND2  1 
ATOM   1496 N N    . PHE A 1 231 ? 132.896 157.682 117.563 1.00 77.99  ? 231  PHE B N    1 
ATOM   1497 C CA   . PHE A 1 231 ? 133.190 158.775 116.644 1.00 76.90  ? 231  PHE B CA   1 
ATOM   1498 C C    . PHE A 1 231 ? 134.675 159.104 116.599 1.00 78.43  ? 231  PHE B C    1 
ATOM   1499 O O    . PHE A 1 231 ? 135.191 159.485 115.543 1.00 78.65  ? 231  PHE B O    1 
ATOM   1500 C CB   . PHE A 1 231 ? 132.399 160.022 117.041 1.00 78.60  ? 231  PHE B CB   1 
ATOM   1501 C CG   . PHE A 1 231 ? 130.909 159.847 116.967 1.00 83.23  ? 231  PHE B CG   1 
ATOM   1502 C CD1  . PHE A 1 231 ? 130.284 159.586 115.758 1.00 81.39  ? 231  PHE B CD1  1 
ATOM   1503 C CD2  . PHE A 1 231 ? 130.133 159.949 118.110 1.00 82.52  ? 231  PHE B CD2  1 
ATOM   1504 C CE1  . PHE A 1 231 ? 128.911 159.423 115.695 1.00 80.86  ? 231  PHE B CE1  1 
ATOM   1505 C CE2  . PHE A 1 231 ? 128.762 159.790 118.053 1.00 80.33  ? 231  PHE B CE2  1 
ATOM   1506 C CZ   . PHE A 1 231 ? 128.150 159.526 116.843 1.00 80.56  ? 231  PHE B CZ   1 
ATOM   1507 N N    . ILE A 1 232 ? 135.364 158.968 117.731 1.00 82.10  ? 232  ILE B N    1 
ATOM   1508 C CA   . ILE A 1 232 ? 136.770 159.351 117.810 1.00 82.40  ? 232  ILE B CA   1 
ATOM   1509 C C    . ILE A 1 232 ? 137.644 158.414 116.986 1.00 82.25  ? 232  ILE B C    1 
ATOM   1510 O O    . ILE A 1 232 ? 138.500 158.859 116.212 1.00 86.24  ? 232  ILE B O    1 
ATOM   1511 C CB   . ILE A 1 232 ? 137.223 159.398 119.281 1.00 79.41  ? 232  ILE B CB   1 
ATOM   1512 C CG1  . ILE A 1 232 ? 136.539 160.556 120.007 1.00 82.83  ? 232  ILE B CG1  1 
ATOM   1513 C CG2  . ILE A 1 232 ? 138.735 159.519 119.378 1.00 81.99  ? 232  ILE B CG2  1 
ATOM   1514 C CD1  . ILE A 1 232 ? 136.622 160.468 121.512 1.00 83.64  ? 232  ILE B CD1  1 
ATOM   1515 N N    . LEU A 1 233 ? 137.434 157.107 117.120 1.00 76.62  ? 233  LEU B N    1 
ATOM   1516 C CA   . LEU A 1 233 ? 138.312 156.136 116.482 1.00 79.90  ? 233  LEU B CA   1 
ATOM   1517 C C    . LEU A 1 233 ? 137.825 155.724 115.085 1.00 78.81  ? 233  LEU B C    1 
ATOM   1518 O O    . LEU A 1 233 ? 138.502 154.950 114.402 1.00 78.35  ? 233  LEU B O    1 
ATOM   1519 C CB   . LEU A 1 233 ? 138.482 154.954 117.450 1.00 79.34  ? 233  LEU B CB   1 
ATOM   1520 C CG   . LEU A 1 233 ? 138.778 153.486 117.204 1.00 79.23  ? 233  LEU B CG   1 
ATOM   1521 C CD1  . LEU A 1 233 ? 140.157 153.359 116.561 1.00 79.03  ? 233  LEU B CD1  1 
ATOM   1522 C CD2  . LEU A 1 233 ? 138.709 152.707 118.503 1.00 76.39  ? 233  LEU B CD2  1 
ATOM   1523 N N    . ASP A 1 234 ? 136.693 156.273 114.639 1.00 80.08  ? 234  ASP B N    1 
ATOM   1524 C CA   . ASP A 1 234 ? 136.038 156.020 113.347 1.00 85.21  ? 234  ASP B CA   1 
ATOM   1525 C C    . ASP A 1 234 ? 135.703 154.525 113.176 1.00 86.10  ? 234  ASP B C    1 
ATOM   1526 O O    . ASP A 1 234 ? 136.358 153.771 112.452 1.00 85.87  ? 234  ASP B O    1 
ATOM   1527 C CB   . ASP A 1 234 ? 136.914 156.643 112.228 1.00 83.57  ? 234  ASP B CB   1 
ATOM   1528 C CG   . ASP A 1 234 ? 136.638 156.136 110.778 1.00 85.00  ? 234  ASP B CG   1 
ATOM   1529 O OD1  . ASP A 1 234 ? 135.724 155.342 110.467 1.00 82.17  ? 234  ASP B OD1  1 
ATOM   1530 O OD2  . ASP A 1 234 ? 137.408 156.573 109.898 1.00 86.20  ? 234  ASP B OD2  1 
ATOM   1531 N N    . ARG A 1 235 ? 134.773 154.083 114.026 1.00 76.69  ? 235  ARG B N    1 
ATOM   1532 C CA   . ARG A 1 235 ? 134.057 152.797 113.917 1.00 71.03  ? 235  ARG B CA   1 
ATOM   1533 C C    . ARG A 1 235 ? 134.925 151.548 113.709 1.00 72.39  ? 235  ARG B C    1 
ATOM   1534 O O    . ARG A 1 235 ? 134.416 150.529 113.234 1.00 78.04  ? 235  ARG B O    1 
ATOM   1535 C CB   . ARG A 1 235 ? 133.012 152.864 112.796 1.00 70.92  ? 235  ARG B CB   1 
ATOM   1536 C CG   . ARG A 1 235 ? 131.594 152.546 113.238 1.00 67.88  ? 235  ARG B CG   1 
ATOM   1537 C CD   . ARG A 1 235 ? 130.668 152.323 112.053 1.00 68.17  ? 235  ARG B CD   1 
ATOM   1538 N NE   . ARG A 1 235 ? 130.975 153.202 110.931 1.00 77.02  ? 235  ARG B NE   1 
ATOM   1539 C CZ   . ARG A 1 235 ? 130.446 154.405 110.755 1.00 78.56  ? 235  ARG B CZ   1 
ATOM   1540 N NH1  . ARG A 1 235 ? 129.589 154.917 111.624 1.00 75.18  ? 235  ARG B NH1  1 
ATOM   1541 N NH2  . ARG A 1 235 ? 130.786 155.113 109.682 1.00 76.86  ? 235  ARG B NH2  1 
ATOM   1542 N N    . LYS A 1 236 ? 136.215 151.542 114.031 1.00 74.60  ? 236  LYS B N    1 
ATOM   1543 C CA   . LYS A 1 236 ? 137.028 150.351 113.788 1.00 78.31  ? 236  LYS B CA   1 
ATOM   1544 C C    . LYS A 1 236 ? 137.810 150.036 115.051 1.00 77.84  ? 236  LYS B C    1 
ATOM   1545 O O    . LYS A 1 236 ? 138.582 150.869 115.521 1.00 82.70  ? 236  LYS B O    1 
ATOM   1546 C CB   . LYS A 1 236 ? 137.972 150.560 112.602 1.00 80.91  ? 236  LYS B CB   1 
ATOM   1547 C CG   . LYS A 1 236 ? 138.604 149.280 112.068 1.00 79.14  ? 236  LYS B CG   1 
ATOM   1548 C CD   . LYS A 1 236 ? 138.673 149.259 110.540 1.00 80.54  ? 236  LYS B CD   1 
ATOM   1549 C CE   . LYS A 1 236 ? 138.812 150.656 109.943 1.00 78.80  ? 236  LYS B CE   1 
ATOM   1550 N NZ   . LYS A 1 236 ? 138.878 150.618 108.457 1.00 80.61  ? 236  LYS B NZ   1 
ATOM   1551 N N    . VAL A 1 237 ? 137.665 148.817 115.561 1.00 66.43  ? 237  VAL B N    1 
ATOM   1552 C CA   . VAL A 1 237 ? 138.399 148.405 116.756 1.00 69.53  ? 237  VAL B CA   1 
ATOM   1553 C C    . VAL A 1 237 ? 139.871 148.100 116.469 1.00 74.93  ? 237  VAL B C    1 
ATOM   1554 O O    . VAL A 1 237 ? 140.208 147.559 115.403 1.00 75.35  ? 237  VAL B O    1 
ATOM   1555 C CB   . VAL A 1 237 ? 137.671 147.211 117.415 1.00 65.78  ? 237  VAL B CB   1 
ATOM   1556 C CG1  . VAL A 1 237 ? 137.995 145.886 116.739 1.00 70.54  ? 237  VAL B CG1  1 
ATOM   1557 C CG2  . VAL A 1 237 ? 137.938 147.132 118.916 1.00 63.17  ? 237  VAL B CG2  1 
ATOM   1558 N N    . PRO A 1 238 ? 140.781 148.522 117.352 1.00 72.87  ? 238  PRO B N    1 
ATOM   1559 C CA   . PRO A 1 238 ? 142.208 148.207 117.180 1.00 68.13  ? 238  PRO B CA   1 
ATOM   1560 C C    . PRO A 1 238 ? 142.480 146.708 117.202 1.00 66.25  ? 238  PRO B C    1 
ATOM   1561 O O    . PRO A 1 238 ? 141.799 145.943 117.888 1.00 70.50  ? 238  PRO B O    1 
ATOM   1562 C CB   . PRO A 1 238 ? 142.878 148.932 118.354 1.00 64.64  ? 238  PRO B CB   1 
ATOM   1563 C CG   . PRO A 1 238 ? 141.917 150.010 118.719 1.00 63.63  ? 238  PRO B CG   1 
ATOM   1564 C CD   . PRO A 1 238 ? 140.559 149.456 118.469 1.00 66.29  ? 238  PRO B CD   1 
ATOM   1565 N N    . VAL A 1 239 ? 143.482 146.293 116.420 1.00 57.03  ? 239  VAL B N    1 
ATOM   1566 C CA   . VAL A 1 239 ? 143.788 144.870 116.257 1.00 61.75  ? 239  VAL B CA   1 
ATOM   1567 C C    . VAL A 1 239 ? 144.209 144.232 117.582 1.00 67.64  ? 239  VAL B C    1 
ATOM   1568 O O    . VAL A 1 239 ? 143.817 143.102 117.891 1.00 61.54  ? 239  VAL B O    1 
ATOM   1569 C CB   . VAL A 1 239 ? 144.868 144.683 115.174 1.00 63.33  ? 239  VAL B CB   1 
ATOM   1570 C CG1  . VAL A 1 239 ? 145.144 143.205 114.937 1.00 61.15  ? 239  VAL B CG1  1 
ATOM   1571 C CG2  . VAL A 1 239 ? 144.448 145.367 113.883 1.00 62.66  ? 239  VAL B CG2  1 
ATOM   1572 N N    . TYR A 1 240 ? 145.056 144.912 118.359 1.00 70.29  ? 240  TYR B N    1 
ATOM   1573 C CA   . TYR A 1 240 ? 145.510 144.340 119.628 1.00 68.29  ? 240  TYR B CA   1 
ATOM   1574 C C    . TYR A 1 240 ? 144.384 144.141 120.639 1.00 66.19  ? 240  TYR B C    1 
ATOM   1575 O O    . TYR A 1 240 ? 144.492 143.273 121.513 1.00 64.83  ? 240  TYR B O    1 
ATOM   1576 C CB   . TYR A 1 240 ? 146.631 145.181 120.242 1.00 67.89  ? 240  TYR B CB   1 
ATOM   1577 C CG   . TYR A 1 240 ? 147.877 145.257 119.392 1.00 63.27  ? 240  TYR B CG   1 
ATOM   1578 C CD1  . TYR A 1 240 ? 148.737 146.342 119.478 1.00 65.41  ? 240  TYR B CD1  1 
ATOM   1579 C CD2  . TYR A 1 240 ? 148.210 144.226 118.521 1.00 59.43  ? 240  TYR B CD2  1 
ATOM   1580 C CE1  . TYR A 1 240 ? 149.883 146.407 118.710 1.00 71.48  ? 240  TYR B CE1  1 
ATOM   1581 C CE2  . TYR A 1 240 ? 149.352 144.283 117.748 1.00 62.13  ? 240  TYR B CE2  1 
ATOM   1582 C CZ   . TYR A 1 240 ? 150.184 145.375 117.846 1.00 69.17  ? 240  TYR B CZ   1 
ATOM   1583 O OH   . TYR A 1 240 ? 151.323 145.434 117.079 1.00 67.11  ? 240  TYR B OH   1 
ATOM   1584 N N    . VAL A 1 241 ? 143.299 144.916 120.550 1.00 54.69  ? 241  VAL B N    1 
ATOM   1585 C CA   . VAL A 1 241 ? 142.249 144.836 121.563 1.00 53.82  ? 241  VAL B CA   1 
ATOM   1586 C C    . VAL A 1 241 ? 141.003 144.086 121.105 1.00 53.60  ? 241  VAL B C    1 
ATOM   1587 O O    . VAL A 1 241 ? 140.102 143.865 121.931 1.00 53.53  ? 241  VAL B O    1 
ATOM   1588 C CB   . VAL A 1 241 ? 141.844 146.239 122.061 1.00 54.84  ? 241  VAL B CB   1 
ATOM   1589 C CG1  . VAL A 1 241 ? 143.072 147.024 122.495 1.00 52.31  ? 241  VAL B CG1  1 
ATOM   1590 C CG2  . VAL A 1 241 ? 141.070 146.972 120.997 1.00 57.13  ? 241  VAL B CG2  1 
ATOM   1591 N N    . GLU A 1 242 ? 140.899 143.719 119.824 1.00 48.78  ? 242  GLU B N    1 
ATOM   1592 C CA   . GLU A 1 242 ? 139.695 143.036 119.350 1.00 48.27  ? 242  GLU B CA   1 
ATOM   1593 C C    . GLU A 1 242 ? 139.534 141.690 120.051 1.00 48.27  ? 242  GLU B C    1 
ATOM   1594 O O    . GLU A 1 242 ? 138.462 141.378 120.581 1.00 60.50  ? 242  GLU B O    1 
ATOM   1595 C CB   . GLU A 1 242 ? 139.697 142.879 117.823 1.00 50.48  ? 242  GLU B CB   1 
ATOM   1596 C CG   . GLU A 1 242 ? 140.926 142.272 117.180 1.00 54.75  ? 242  GLU B CG   1 
ATOM   1597 C CD   . GLU A 1 242 ? 140.792 140.780 116.943 1.00 57.35  ? 242  GLU B CD   1 
ATOM   1598 O OE1  . GLU A 1 242 ? 139.649 140.278 116.926 1.00 58.85  ? 242  GLU B OE1  1 
ATOM   1599 O OE2  . GLU A 1 242 ? 141.832 140.108 116.778 1.00 55.27  ? 242  GLU B OE2  1 
ATOM   1600 N N    . ASN A 1 243 ? 140.592 140.876 120.051 1.00 33.93  ? 243  ASN B N    1 
ATOM   1601 C CA   . ASN A 1 243 ? 140.514 139.531 120.606 1.00 43.84  ? 243  ASN B CA   1 
ATOM   1602 C C    . ASN A 1 243 ? 140.360 139.558 122.123 1.00 38.27  ? 243  ASN B C    1 
ATOM   1603 O O    . ASN A 1 243 ? 139.744 138.650 122.694 1.00 33.18  ? 243  ASN B O    1 
ATOM   1604 C CB   . ASN A 1 243 ? 141.761 138.739 120.212 1.00 43.07  ? 243  ASN B CB   1 
ATOM   1605 C CG   . ASN A 1 243 ? 141.512 137.246 120.145 1.00 44.38  ? 243  ASN B CG   1 
ATOM   1606 O OD1  . ASN A 1 243 ? 140.612 136.722 120.800 1.00 37.25  ? 243  ASN B OD1  1 
ATOM   1607 N ND2  . ASN A 1 243 ? 142.319 136.549 119.353 1.00 48.74  ? 243  ASN B ND2  1 
ATOM   1608 N N    . PHE A 1 244 ? 140.919 140.572 122.790 1.00 29.40  ? 244  PHE B N    1 
ATOM   1609 C CA   . PHE A 1 244 ? 140.749 140.690 124.236 1.00 28.27  ? 244  PHE B CA   1 
ATOM   1610 C C    . PHE A 1 244 ? 139.288 140.920 124.607 1.00 39.70  ? 244  PHE B C    1 
ATOM   1611 O O    . PHE A 1 244 ? 138.801 140.378 125.606 1.00 51.56  ? 244  PHE B O    1 
ATOM   1612 C CB   . PHE A 1 244 ? 141.629 141.822 124.769 1.00 31.36  ? 244  PHE B CB   1 
ATOM   1613 C CG   . PHE A 1 244 ? 141.339 142.204 126.192 1.00 26.18  ? 244  PHE B CG   1 
ATOM   1614 C CD1  . PHE A 1 244 ? 141.776 141.411 127.239 1.00 20.69  ? 244  PHE B CD1  1 
ATOM   1615 C CD2  . PHE A 1 244 ? 140.653 143.371 126.483 1.00 21.48  ? 244  PHE B CD2  1 
ATOM   1616 C CE1  . PHE A 1 244 ? 141.514 141.766 128.548 1.00 16.54  ? 244  PHE B CE1  1 
ATOM   1617 C CE2  . PHE A 1 244 ? 140.391 143.730 127.789 1.00 24.51  ? 244  PHE B CE2  1 
ATOM   1618 C CZ   . PHE A 1 244 ? 140.821 142.927 128.822 1.00 21.71  ? 244  PHE B CZ   1 
ATOM   1619 N N    . LEU A 1 245 ? 138.574 141.719 123.812 1.00 35.84  ? 245  LEU B N    1 
ATOM   1620 C CA   . LEU A 1 245 ? 137.157 141.964 124.063 1.00 23.43  ? 245  LEU B CA   1 
ATOM   1621 C C    . LEU A 1 245 ? 136.312 140.734 123.757 1.00 20.47  ? 245  LEU B C    1 
ATOM   1622 O O    . LEU A 1 245 ? 135.311 140.485 124.437 1.00 30.29  ? 245  LEU B O    1 
ATOM   1623 C CB   . LEU A 1 245 ? 136.672 143.165 123.253 1.00 21.09  ? 245  LEU B CB   1 
ATOM   1624 C CG   . LEU A 1 245 ? 137.326 144.501 123.605 1.00 27.06  ? 245  LEU B CG   1 
ATOM   1625 C CD1  . LEU A 1 245 ? 136.825 145.603 122.688 1.00 29.67  ? 245  LEU B CD1  1 
ATOM   1626 C CD2  . LEU A 1 245 ? 137.065 144.852 125.060 1.00 27.08  ? 245  LEU B CD2  1 
ATOM   1627 N N    . ASP A 1 246 ? 136.695 139.965 122.736 1.00 17.16  ? 246  ASP B N    1 
ATOM   1628 C CA   . ASP A 1 246 ? 135.922 138.793 122.338 1.00 30.80  ? 246  ASP B CA   1 
ATOM   1629 C C    . ASP A 1 246 ? 136.029 137.669 123.363 1.00 30.49  ? 246  ASP B C    1 
ATOM   1630 O O    . ASP A 1 246 ? 135.069 136.916 123.561 1.00 31.43  ? 246  ASP B O    1 
ATOM   1631 C CB   . ASP A 1 246 ? 136.384 138.307 120.965 1.00 26.98  ? 246  ASP B CB   1 
ATOM   1632 C CG   . ASP A 1 246 ? 135.888 139.190 119.839 1.00 33.64  ? 246  ASP B CG   1 
ATOM   1633 O OD1  . ASP A 1 246 ? 135.734 140.408 120.064 1.00 30.75  ? 246  ASP B OD1  1 
ATOM   1634 O OD2  . ASP A 1 246 ? 135.653 138.668 118.730 1.00 34.00  ? 246  ASP B OD2  1 
ATOM   1635 N N    . GLY A 1 247 ? 137.193 137.518 123.998 1.00 21.11  ? 247  GLY B N    1 
ATOM   1636 C CA   . GLY A 1 247 ? 137.329 136.513 125.042 1.00 16.90  ? 247  GLY B CA   1 
ATOM   1637 C C    . GLY A 1 247 ? 136.408 136.751 126.225 1.00 19.19  ? 247  GLY B C    1 
ATOM   1638 O O    . GLY A 1 247 ? 135.795 135.816 126.744 1.00 33.74  ? 247  GLY B O    1 
ATOM   1639 N N    . LEU A 1 248 ? 136.301 138.004 126.673 1.00 13.08  ? 248  LEU B N    1 
ATOM   1640 C CA   . LEU A 1 248 ? 135.384 138.335 127.760 1.00 23.92  ? 248  LEU B CA   1 
ATOM   1641 C C    . LEU A 1 248 ? 133.934 138.410 127.296 1.00 30.30  ? 248  LEU B C    1 
ATOM   1642 O O    . LEU A 1 248 ? 133.026 138.076 128.064 1.00 18.19  ? 248  LEU B O    1 
ATOM   1643 C CB   . LEU A 1 248 ? 135.785 139.664 128.405 1.00 20.26  ? 248  LEU B CB   1 
ATOM   1644 C CG   . LEU A 1 248 ? 137.070 139.721 129.230 1.00 6.13   ? 248  LEU B CG   1 
ATOM   1645 C CD1  . LEU A 1 248 ? 137.018 140.889 130.195 1.00 11.42  ? 248  LEU B CD1  1 
ATOM   1646 C CD2  . LEU A 1 248 ? 137.274 138.424 129.989 1.00 14.73  ? 248  LEU B CD2  1 
ATOM   1647 N N    . GLY A 1 249 ? 133.703 138.854 126.060 1.00 27.92  ? 249  GLY B N    1 
ATOM   1648 C CA   . GLY A 1 249 ? 132.343 138.997 125.565 1.00 10.89  ? 249  GLY B CA   1 
ATOM   1649 C C    . GLY A 1 249 ? 131.602 137.683 125.403 1.00 20.92  ? 249  GLY B C    1 
ATOM   1650 O O    . GLY A 1 249 ? 130.430 137.574 125.773 1.00 37.29  ? 249  GLY B O    1 
ATOM   1651 N N    . ASN A 1 250 ? 132.268 136.668 124.850 1.00 12.98  ? 250  ASN B N    1 
ATOM   1652 C CA   . ASN A 1 250 ? 131.610 135.391 124.596 1.00 26.06  ? 250  ASN B CA   1 
ATOM   1653 C C    . ASN A 1 250 ? 131.384 134.566 125.858 1.00 35.64  ? 250  ASN B C    1 
ATOM   1654 O O    . ASN A 1 250 ? 130.561 133.646 125.835 1.00 41.36  ? 250  ASN B O    1 
ATOM   1655 C CB   . ASN A 1 250 ? 132.430 134.577 123.596 1.00 23.76  ? 250  ASN B CB   1 
ATOM   1656 C CG   . ASN A 1 250 ? 132.449 135.200 122.216 1.00 32.27  ? 250  ASN B CG   1 
ATOM   1657 O OD1  . ASN A 1 250 ? 131.593 136.016 121.878 1.00 42.51  ? 250  ASN B OD1  1 
ATOM   1658 N ND2  . ASN A 1 250 ? 133.430 134.817 121.408 1.00 37.07  ? 250  ASN B ND2  1 
ATOM   1659 N N    . SER A 1 251 ? 132.086 134.862 126.950 1.00 18.26  ? 251  SER B N    1 
ATOM   1660 C CA   . SER A 1 251 ? 131.894 134.129 128.195 1.00 11.92  ? 251  SER B CA   1 
ATOM   1661 C C    . SER A 1 251 ? 130.661 134.572 128.976 1.00 17.00  ? 251  SER B C    1 
ATOM   1662 O O    . SER A 1 251 ? 130.333 133.944 129.987 1.00 29.21  ? 251  SER B O    1 
ATOM   1663 C CB   . SER A 1 251 ? 133.134 134.264 129.081 1.00 5.77   ? 251  SER B CB   1 
ATOM   1664 O OG   . SER A 1 251 ? 133.277 135.590 129.556 1.00 18.29  ? 251  SER B OG   1 
ATOM   1665 N N    . PHE A 1 252 ? 129.979 135.633 128.541 1.00 8.74   ? 252  PHE B N    1 
ATOM   1666 C CA   . PHE A 1 252 ? 128.823 136.134 129.279 1.00 4.40   ? 252  PHE B CA   1 
ATOM   1667 C C    . PHE A 1 252 ? 127.603 135.235 129.115 1.00 22.71  ? 252  PHE B C    1 
ATOM   1668 O O    . PHE A 1 252 ? 126.912 134.945 130.097 1.00 36.41  ? 252  PHE B O    1 
ATOM   1669 C CB   . PHE A 1 252 ? 128.493 137.554 128.825 1.00 12.31  ? 252  PHE B CB   1 
ATOM   1670 C CG   . PHE A 1 252 ? 127.208 138.089 129.390 1.00 16.21  ? 252  PHE B CG   1 
ATOM   1671 C CD1  . PHE A 1 252 ? 127.096 138.386 130.737 1.00 15.95  ? 252  PHE B CD1  1 
ATOM   1672 C CD2  . PHE A 1 252 ? 126.109 138.292 128.573 1.00 18.65  ? 252  PHE B CD2  1 
ATOM   1673 C CE1  . PHE A 1 252 ? 125.915 138.880 131.255 1.00 7.01   ? 252  PHE B CE1  1 
ATOM   1674 C CE2  . PHE A 1 252 ? 124.927 138.782 129.088 1.00 15.37  ? 252  PHE B CE2  1 
ATOM   1675 C CZ   . PHE A 1 252 ? 124.831 139.076 130.430 1.00 14.81  ? 252  PHE B CZ   1 
ATOM   1676 N N    . SER A 1 253 ? 127.321 134.797 127.885 1.00 22.44  ? 253  SER B N    1 
ATOM   1677 C CA   . SER A 1 253 ? 126.069 134.104 127.578 1.00 18.34  ? 253  SER B CA   1 
ATOM   1678 C C    . SER A 1 253 ? 125.907 132.812 128.376 1.00 14.92  ? 253  SER B C    1 
ATOM   1679 O O    . SER A 1 253 ? 124.864 132.582 128.997 1.00 17.94  ? 253  SER B O    1 
ATOM   1680 C CB   . SER A 1 253 ? 125.988 133.819 126.079 1.00 21.30  ? 253  SER B CB   1 
ATOM   1681 O OG   . SER A 1 253 ? 124.750 133.219 125.746 1.00 34.06  ? 253  SER B OG   1 
ATOM   1682 N N    . GLY A 1 254 ? 126.927 131.954 128.365 1.00 16.14  ? 254  GLY B N    1 
ATOM   1683 C CA   . GLY A 1 254 ? 126.844 130.705 129.107 1.00 9.48   ? 254  GLY B CA   1 
ATOM   1684 C C    . GLY A 1 254 ? 126.811 130.884 130.614 1.00 12.18  ? 254  GLY B C    1 
ATOM   1685 O O    . GLY A 1 254 ? 126.081 130.176 131.313 1.00 14.90  ? 254  GLY B O    1 
ATOM   1686 N N    . SER A 1 255 ? 127.601 131.820 131.139 1.00 7.30   ? 255  SER B N    1 
ATOM   1687 C CA   . SER A 1 255 ? 127.717 131.975 132.585 1.00 2.83   ? 255  SER B CA   1 
ATOM   1688 C C    . SER A 1 255 ? 126.555 132.749 133.198 1.00 7.11   ? 255  SER B C    1 
ATOM   1689 O O    . SER A 1 255 ? 126.188 132.483 134.348 1.00 26.27  ? 255  SER B O    1 
ATOM   1690 C CB   . SER A 1 255 ? 129.041 132.656 132.931 1.00 8.48   ? 255  SER B CB   1 
ATOM   1691 O OG   . SER A 1 255 ? 129.093 133.967 132.401 1.00 14.90  ? 255  SER B OG   1 
ATOM   1692 N N    . ALA A 1 256 ? 125.983 133.715 132.473 1.00 2.71   ? 256  ALA B N    1 
ATOM   1693 C CA   . ALA A 1 256 ? 124.832 134.457 132.988 1.00 6.69   ? 256  ALA B CA   1 
ATOM   1694 C C    . ALA A 1 256 ? 123.613 133.560 133.170 1.00 14.82  ? 256  ALA B C    1 
ATOM   1695 O O    . ALA A 1 256 ? 122.900 133.674 134.174 1.00 13.18  ? 256  ALA B O    1 
ATOM   1696 C CB   . ALA A 1 256 ? 124.494 135.622 132.062 1.00 15.17  ? 256  ALA B CB   1 
ATOM   1697 N N    . LEU A 1 257 ? 123.345 132.681 132.202 1.00 18.08  ? 257  LEU B N    1 
ATOM   1698 C CA   . LEU A 1 257 ? 122.233 131.742 132.330 1.00 3.85   ? 257  LEU B CA   1 
ATOM   1699 C C    . LEU A 1 257 ? 122.448 130.773 133.486 1.00 3.18   ? 257  LEU B C    1 
ATOM   1700 O O    . LEU A 1 257 ? 121.510 130.477 134.235 1.00 19.90  ? 257  LEU B O    1 
ATOM   1701 C CB   . LEU A 1 257 ? 122.036 130.980 131.021 1.00 4.72   ? 257  LEU B CB   1 
ATOM   1702 C CG   . LEU A 1 257 ? 121.590 131.820 129.825 1.00 0.00   ? 257  LEU B CG   1 
ATOM   1703 C CD1  . LEU A 1 257 ? 121.769 131.049 128.530 1.00 1.77   ? 257  LEU B CD1  1 
ATOM   1704 C CD2  . LEU A 1 257 ? 120.148 132.253 129.994 1.00 0.00   ? 257  LEU B CD2  1 
ATOM   1705 N N    . PHE A 1 258 ? 123.668 130.249 133.632 1.00 6.05   ? 258  PHE B N    1 
ATOM   1706 C CA   . PHE A 1 258 ? 123.956 129.313 134.717 1.00 4.21   ? 258  PHE B CA   1 
ATOM   1707 C C    . PHE A 1 258 ? 123.762 129.967 136.080 1.00 6.75   ? 258  PHE B C    1 
ATOM   1708 O O    . PHE A 1 258 ? 123.158 129.376 136.982 1.00 18.68  ? 258  PHE B O    1 
ATOM   1709 C CB   . PHE A 1 258 ? 125.382 128.775 134.567 1.00 6.79   ? 258  PHE B CB   1 
ATOM   1710 C CG   . PHE A 1 258 ? 125.703 127.617 135.475 1.00 11.97  ? 258  PHE B CG   1 
ATOM   1711 C CD1  . PHE A 1 258 ? 126.120 127.833 136.781 1.00 12.50  ? 258  PHE B CD1  1 
ATOM   1712 C CD2  . PHE A 1 258 ? 125.585 126.315 135.026 1.00 18.43  ? 258  PHE B CD2  1 
ATOM   1713 C CE1  . PHE A 1 258 ? 126.414 126.777 137.615 1.00 12.61  ? 258  PHE B CE1  1 
ATOM   1714 C CE2  . PHE A 1 258 ? 125.877 125.254 135.858 1.00 18.61  ? 258  PHE B CE2  1 
ATOM   1715 C CZ   . PHE A 1 258 ? 126.291 125.488 137.154 1.00 12.08  ? 258  PHE B CZ   1 
ATOM   1716 N N    . TYR A 1 259 ? 124.280 131.185 136.254 1.00 5.57   ? 259  TYR B N    1 
ATOM   1717 C CA   . TYR A 1 259 ? 124.112 131.879 137.526 1.00 0.00   ? 259  TYR B CA   1 
ATOM   1718 C C    . TYR A 1 259 ? 122.658 132.249 137.785 1.00 20.36  ? 259  TYR B C    1 
ATOM   1719 O O    . TYR A 1 259 ? 122.238 132.324 138.945 1.00 29.74  ? 259  TYR B O    1 
ATOM   1720 C CB   . TYR A 1 259 ? 124.983 133.134 137.566 1.00 2.76   ? 259  TYR B CB   1 
ATOM   1721 C CG   . TYR A 1 259 ? 124.749 133.993 138.786 1.00 9.30   ? 259  TYR B CG   1 
ATOM   1722 C CD1  . TYR A 1 259 ? 124.964 133.494 140.063 1.00 7.76   ? 259  TYR B CD1  1 
ATOM   1723 C CD2  . TYR A 1 259 ? 124.297 135.299 138.663 1.00 23.40  ? 259  TYR B CD2  1 
ATOM   1724 C CE1  . TYR A 1 259 ? 124.746 134.273 141.181 1.00 10.23  ? 259  TYR B CE1  1 
ATOM   1725 C CE2  . TYR A 1 259 ? 124.075 136.087 139.776 1.00 17.80  ? 259  TYR B CE2  1 
ATOM   1726 C CZ   . TYR A 1 259 ? 124.301 135.568 141.032 1.00 10.08  ? 259  TYR B CZ   1 
ATOM   1727 O OH   . TYR A 1 259 ? 124.083 136.348 142.144 1.00 8.29   ? 259  TYR B OH   1 
ATOM   1728 N N    . LEU A 1 260 ? 121.875 132.473 136.725 1.00 24.65  ? 260  LEU B N    1 
ATOM   1729 C CA   . LEU A 1 260 ? 120.450 132.744 136.897 1.00 15.12  ? 260  LEU B CA   1 
ATOM   1730 C C    . LEU A 1 260 ? 119.719 131.562 137.520 1.00 4.96   ? 260  LEU B C    1 
ATOM   1731 O O    . LEU A 1 260 ? 118.816 131.750 138.342 1.00 11.26  ? 260  LEU B O    1 
ATOM   1732 C CB   . LEU A 1 260 ? 119.827 133.113 135.550 1.00 16.65  ? 260  LEU B CB   1 
ATOM   1733 C CG   . LEU A 1 260 ? 118.315 133.338 135.485 1.00 7.26   ? 260  LEU B CG   1 
ATOM   1734 C CD1  . LEU A 1 260 ? 117.887 134.424 136.452 1.00 11.70  ? 260  LEU B CD1  1 
ATOM   1735 C CD2  . LEU A 1 260 ? 117.893 133.689 134.068 1.00 8.87   ? 260  LEU B CD2  1 
ATOM   1736 N N    . GLY A 1 261 ? 120.021 130.343 137.082 1.00 11.92  ? 261  GLY B N    1 
ATOM   1737 C CA   . GLY A 1 261 ? 119.391 129.192 137.703 1.00 23.84  ? 261  GLY B CA   1 
ATOM   1738 C C    . GLY A 1 261 ? 119.747 129.016 139.170 1.00 25.50  ? 261  GLY B C    1 
ATOM   1739 O O    . GLY A 1 261 ? 118.891 128.676 139.989 1.00 29.49  ? 261  GLY B O    1 
ATOM   1740 N N    . LEU A 1 262 ? 121.020 129.241 139.521 1.00 30.41  ? 262  LEU B N    1 
ATOM   1741 C CA   . LEU A 1 262 ? 121.467 129.045 140.899 1.00 22.22  ? 262  LEU B CA   1 
ATOM   1742 C C    . LEU A 1 262 ? 120.895 130.055 141.896 1.00 19.27  ? 262  LEU B C    1 
ATOM   1743 O O    . LEU A 1 262 ? 120.822 129.745 143.090 1.00 22.71  ? 262  LEU B O    1 
ATOM   1744 C CB   . LEU A 1 262 ? 123.001 129.089 140.915 1.00 12.10  ? 262  LEU B CB   1 
ATOM   1745 C CG   . LEU A 1 262 ? 123.865 128.301 141.910 1.00 4.57   ? 262  LEU B CG   1 
ATOM   1746 C CD1  . LEU A 1 262 ? 125.307 128.327 141.434 1.00 13.35  ? 262  LEU B CD1  1 
ATOM   1747 C CD2  . LEU A 1 262 ? 123.782 128.765 143.346 1.00 15.47  ? 262  LEU B CD2  1 
ATOM   1748 N N    . THR A 1 263 ? 120.438 131.225 141.449 1.00 12.67  ? 263  THR B N    1 
ATOM   1749 C CA   . THR A 1 263 ? 119.954 132.238 142.386 1.00 24.97  ? 263  THR B CA   1 
ATOM   1750 C C    . THR A 1 263 ? 118.489 132.061 142.746 1.00 29.39  ? 263  THR B C    1 
ATOM   1751 O O    . THR A 1 263 ? 118.011 132.708 143.680 1.00 28.24  ? 263  THR B O    1 
ATOM   1752 C CB   . THR A 1 263 ? 120.184 133.666 141.869 1.00 26.20  ? 263  THR B CB   1 
ATOM   1753 O OG1  . THR A 1 263 ? 119.426 134.585 142.664 1.00 32.60  ? 263  THR B OG1  1 
ATOM   1754 C CG2  . THR A 1 263 ? 119.752 133.815 140.444 1.00 18.13  ? 263  THR B CG2  1 
ATOM   1755 N N    . MET A 1 264 ? 117.771 131.216 142.020 1.00 24.02  ? 264  MET B N    1 
ATOM   1756 C CA   . MET A 1 264 ? 116.353 130.980 142.234 1.00 16.73  ? 264  MET B CA   1 
ATOM   1757 C C    . MET A 1 264 ? 116.064 129.908 143.279 1.00 16.05  ? 264  MET B C    1 
ATOM   1758 O O    . MET A 1 264 ? 114.896 129.706 143.624 1.00 20.40  ? 264  MET B O    1 
ATOM   1759 C CB   . MET A 1 264 ? 115.732 130.624 140.884 1.00 13.70  ? 264  MET B CB   1 
ATOM   1760 C CG   . MET A 1 264 ? 115.761 131.819 139.946 1.00 27.35  ? 264  MET B CG   1 
ATOM   1761 S SD   . MET A 1 264 ? 115.311 131.521 138.230 1.00 43.50  ? 264  MET B SD   1 
ATOM   1762 C CE   . MET A 1 264 ? 114.230 130.119 138.371 1.00 22.64  ? 264  MET B CE   1 
ATOM   1763 N N    . VAL A 1 265 ? 117.093 129.228 143.779 1.00 36.52  ? 265  VAL B N    1 
ATOM   1764 C CA   . VAL A 1 265 ? 116.956 128.047 144.629 1.00 41.01  ? 265  VAL B CA   1 
ATOM   1765 C C    . VAL A 1 265 ? 116.351 128.472 145.969 1.00 40.97  ? 265  VAL B C    1 
ATOM   1766 O O    . VAL A 1 265 ? 116.985 129.196 146.743 1.00 43.00  ? 265  VAL B O    1 
ATOM   1767 C CB   . VAL A 1 265 ? 118.303 127.337 144.825 1.00 38.94  ? 265  VAL B CB   1 
ATOM   1768 C CG1  . VAL A 1 265 ? 118.322 126.506 146.115 1.00 34.46  ? 265  VAL B CG1  1 
ATOM   1769 C CG2  . VAL A 1 265 ? 118.640 126.480 143.623 1.00 36.37  ? 265  VAL B CG2  1 
ATOM   1770 N N    . GLY A 1 266 ? 115.095 128.096 146.213 1.00 43.25  ? 266  GLY B N    1 
ATOM   1771 C CA   . GLY A 1 266 ? 114.481 128.332 147.508 1.00 41.47  ? 266  GLY B CA   1 
ATOM   1772 C C    . GLY A 1 266 ? 114.006 129.737 147.793 1.00 46.15  ? 266  GLY B C    1 
ATOM   1773 O O    . GLY A 1 266 ? 113.643 130.026 148.939 1.00 46.56  ? 266  GLY B O    1 
ATOM   1774 N N    . LYS A 1 267 ? 113.982 130.619 146.797 1.00 52.45  ? 267  LYS B N    1 
ATOM   1775 C CA   . LYS A 1 267 ? 113.644 132.017 147.034 1.00 49.80  ? 267  LYS B CA   1 
ATOM   1776 C C    . LYS A 1 267 ? 112.144 132.283 147.035 1.00 47.82  ? 267  LYS B C    1 
ATOM   1777 O O    . LYS A 1 267 ? 111.721 133.308 147.579 1.00 45.24  ? 267  LYS B O    1 
ATOM   1778 C CB   . LYS A 1 267 ? 114.339 132.909 146.008 1.00 43.04  ? 267  LYS B CB   1 
ATOM   1779 C CG   . LYS A 1 267 ? 115.839 132.713 145.992 1.00 49.21  ? 267  LYS B CG   1 
ATOM   1780 C CD   . LYS A 1 267 ? 116.582 133.984 146.354 1.00 51.06  ? 267  LYS B CD   1 
ATOM   1781 C CE   . LYS A 1 267 ? 117.934 133.665 146.969 1.00 53.19  ? 267  LYS B CE   1 
ATOM   1782 N NZ   . LYS A 1 267 ? 117.811 132.755 148.142 1.00 51.70  ? 267  LYS B NZ   1 
ATOM   1783 N N    . ILE A 1 268 ? 111.343 131.407 146.420 1.00 54.59  ? 268  ILE B N    1 
ATOM   1784 C CA   . ILE A 1 268 ? 109.904 131.647 146.294 1.00 58.53  ? 268  ILE B CA   1 
ATOM   1785 C C    . ILE A 1 268 ? 109.240 131.736 147.671 1.00 61.75  ? 268  ILE B C    1 
ATOM   1786 O O    . ILE A 1 268 ? 108.330 132.551 147.871 1.00 57.15  ? 268  ILE B O    1 
ATOM   1787 C CB   . ILE A 1 268 ? 109.248 130.598 145.366 1.00 55.29  ? 268  ILE B CB   1 
ATOM   1788 C CG1  . ILE A 1 268 ? 108.013 131.188 144.681 1.00 58.48  ? 268  ILE B CG1  1 
ATOM   1789 C CG2  . ILE A 1 268 ? 108.883 129.303 146.076 1.00 52.86  ? 268  ILE B CG2  1 
ATOM   1790 C CD1  . ILE A 1 268 ? 107.536 130.384 143.495 1.00 55.97  ? 268  ILE B CD1  1 
ATOM   1791 N N    . LYS A 1 269 ? 109.672 130.901 148.632 1.00 80.51  ? 269  LYS B N    1 
ATOM   1792 C CA   . LYS A 1 269 ? 109.269 131.003 150.037 1.00 80.91  ? 269  LYS B CA   1 
ATOM   1793 C C    . LYS A 1 269 ? 107.769 130.822 150.250 1.00 80.76  ? 269  LYS B C    1 
ATOM   1794 O O    . LYS A 1 269 ? 107.027 130.530 149.306 1.00 81.45  ? 269  LYS B O    1 
ATOM   1795 C CB   . LYS A 1 269 ? 109.726 132.337 150.639 1.00 77.20  ? 269  LYS B CB   1 
ATOM   1796 C CG   . LYS A 1 269 ? 111.141 132.311 151.195 1.00 77.31  ? 269  LYS B CG   1 
ATOM   1797 C CD   . LYS A 1 269 ? 111.380 131.075 152.050 1.00 76.50  ? 269  LYS B CD   1 
ATOM   1798 C CE   . LYS A 1 269 ? 112.622 131.228 152.912 1.00 77.97  ? 269  LYS B CE   1 
ATOM   1799 N NZ   . LYS A 1 269 ? 112.893 132.652 153.252 1.00 77.49  ? 269  LYS B NZ   1 
ATOM   1800 N N    . ARG A 1 270 ? 107.315 130.953 151.495 1.00 91.24  ? 270  ARG B N    1 
ATOM   1801 C CA   . ARG A 1 270 ? 105.883 130.951 151.739 1.00 94.17  ? 270  ARG B CA   1 
ATOM   1802 C C    . ARG A 1 270 ? 105.354 132.360 151.459 1.00 92.35  ? 270  ARG B C    1 
ATOM   1803 O O    . ARG A 1 270 ? 106.113 133.266 151.103 1.00 90.09  ? 270  ARG B O    1 
ATOM   1804 C CB   . ARG A 1 270 ? 105.604 130.453 153.161 1.00 93.71  ? 270  ARG B CB   1 
ATOM   1805 C CG   . ARG A 1 270 ? 104.155 130.058 153.480 1.00 92.12  ? 270  ARG B CG   1 
ATOM   1806 C CD   . ARG A 1 270 ? 103.696 128.914 152.584 1.00 95.63  ? 270  ARG B CD   1 
ATOM   1807 N NE   . ARG A 1 270 ? 103.035 129.396 151.376 1.00 95.96  ? 270  ARG B NE   1 
ATOM   1808 C CZ   . ARG A 1 270 ? 102.364 128.627 150.531 1.00 95.46  ? 270  ARG B CZ   1 
ATOM   1809 N NH1  . ARG A 1 270 ? 102.239 127.326 150.732 1.00 93.66  ? 270  ARG B NH1  1 
ATOM   1810 N NH2  . ARG A 1 270 ? 101.805 129.177 149.457 1.00 95.29  ? 270  ARG B NH2  1 
ATOM   1811 N N    . LEU A 1 271 ? 104.054 132.581 151.634 1.00 95.70  ? 271  LEU B N    1 
ATOM   1812 C CA   . LEU A 1 271 ? 103.503 133.899 151.364 1.00 97.96  ? 271  LEU B CA   1 
ATOM   1813 C C    . LEU A 1 271 ? 102.316 134.179 152.280 1.00 99.47  ? 271  LEU B C    1 
ATOM   1814 O O    . LEU A 1 271 ? 102.098 133.501 153.288 1.00 102.25 ? 271  LEU B O    1 
ATOM   1815 C CB   . LEU A 1 271 ? 103.111 134.014 149.885 1.00 97.66  ? 271  LEU B CB   1 
ATOM   1816 C CG   . LEU A 1 271 ? 104.125 134.707 148.969 1.00 100.27 ? 271  LEU B CG   1 
ATOM   1817 C CD1  . LEU A 1 271 ? 103.707 134.606 147.508 1.00 97.54  ? 271  LEU B CD1  1 
ATOM   1818 C CD2  . LEU A 1 271 ? 104.371 136.146 149.379 1.00 97.14  ? 271  LEU B CD2  1 
ATOM   1819 N N    . LYS A 1 272 ? 101.557 135.203 151.898 1.00 91.79  ? 272  LYS B N    1 
ATOM   1820 C CA   . LYS A 1 272 ? 100.437 135.803 152.609 1.00 89.02  ? 272  LYS B CA   1 
ATOM   1821 C C    . LYS A 1 272 ? 99.434  136.183 151.528 1.00 92.72  ? 272  LYS B C    1 
ATOM   1822 O O    . LYS A 1 272 ? 99.780  136.209 150.343 1.00 96.85  ? 272  LYS B O    1 
ATOM   1823 C CB   . LYS A 1 272 ? 100.850 136.991 153.490 1.00 88.65  ? 272  LYS B CB   1 
ATOM   1824 C CG   . LYS A 1 272 ? 101.185 138.263 152.760 1.00 90.48  ? 272  LYS B CG   1 
ATOM   1825 C CD   . LYS A 1 272 ? 101.013 139.481 153.655 1.00 91.11  ? 272  LYS B CD   1 
ATOM   1826 C CE   . LYS A 1 272 ? 99.581  139.617 154.144 1.00 91.17  ? 272  LYS B CE   1 
ATOM   1827 N NZ   . LYS A 1 272 ? 99.461  140.645 155.214 1.00 91.83  ? 272  LYS B NZ   1 
ATOM   1828 N N    . LYS A 1 273 ? 98.186  136.437 151.928 1.00 83.32  ? 273  LYS B N    1 
ATOM   1829 C CA   . LYS A 1 273 ? 97.192  136.931 150.975 1.00 81.38  ? 273  LYS B CA   1 
ATOM   1830 C C    . LYS A 1 273 ? 97.633  138.206 150.265 1.00 78.17  ? 273  LYS B C    1 
ATOM   1831 O O    . LYS A 1 273 ? 97.770  138.179 149.038 1.00 76.17  ? 273  LYS B O    1 
ATOM   1832 C CB   . LYS A 1 273 ? 95.862  137.174 151.692 1.00 81.92  ? 273  LYS B CB   1 
ATOM   1833 C CG   . LYS A 1 273 ? 94.915  135.982 151.693 1.00 82.93  ? 273  LYS B CG   1 
ATOM   1834 C CD   . LYS A 1 273 ? 94.828  135.320 150.327 1.00 82.92  ? 273  LYS B CD   1 
ATOM   1835 C CE   . LYS A 1 273 ? 93.888  136.080 149.406 1.00 82.18  ? 273  LYS B CE   1 
ATOM   1836 N NZ   . LYS A 1 273 ? 93.546  135.288 148.193 1.00 82.98  ? 273  LYS B NZ   1 
ATOM   1837 N N    . SER A 1 274 ? 97.841  139.320 150.975 1.00 76.67  ? 274  SER B N    1 
ATOM   1838 C CA   . SER A 1 274 ? 97.784  140.620 150.307 1.00 78.43  ? 274  SER B CA   1 
ATOM   1839 C C    . SER A 1 274 ? 98.979  140.790 149.373 1.00 77.29  ? 274  SER B C    1 
ATOM   1840 O O    . SER A 1 274 ? 98.928  141.571 148.425 1.00 77.18  ? 274  SER B O    1 
ATOM   1841 C CB   . SER A 1 274 ? 97.737  141.748 151.337 1.00 81.36  ? 274  SER B CB   1 
ATOM   1842 O OG   . SER A 1 274 ? 99.042  142.159 151.704 1.00 79.61  ? 274  SER B OG   1 
ATOM   1843 N N    . ALA A 1 275 ? 100.061 140.071 149.665 1.00 67.49  ? 275  ALA B N    1 
ATOM   1844 C CA   . ALA A 1 275 ? 101.258 139.959 148.830 1.00 66.26  ? 275  ALA B CA   1 
ATOM   1845 C C    . ALA A 1 275 ? 100.971 139.397 147.437 1.00 68.44  ? 275  ALA B C    1 
ATOM   1846 O O    . ALA A 1 275 ? 101.145 140.079 146.422 1.00 73.52  ? 275  ALA B O    1 
ATOM   1847 C CB   . ALA A 1 275 ? 102.313 139.109 149.529 1.00 67.76  ? 275  ALA B CB   1 
ATOM   1848 N N    . PHE A 1 276 ? 100.572 138.124 147.392 1.00 52.65  ? 276  PHE B N    1 
ATOM   1849 C CA   . PHE A 1 276 ? 100.223 137.388 146.174 1.00 51.40  ? 276  PHE B CA   1 
ATOM   1850 C C    . PHE A 1 276 ? 99.294  138.119 145.200 1.00 52.67  ? 276  PHE B C    1 
ATOM   1851 O O    . PHE A 1 276 ? 99.578  138.135 143.996 1.00 53.02  ? 276  PHE B O    1 
ATOM   1852 C CB   . PHE A 1 276 ? 99.590  136.055 146.585 1.00 51.96  ? 276  PHE B CB   1 
ATOM   1853 C CG   . PHE A 1 276 ? 99.470  135.059 145.468 1.00 52.67  ? 276  PHE B CG   1 
ATOM   1854 C CD1  . PHE A 1 276 ? 100.593 134.615 144.793 1.00 52.62  ? 276  PHE B CD1  1 
ATOM   1855 C CD2  . PHE A 1 276 ? 98.232  134.553 145.109 1.00 52.92  ? 276  PHE B CD2  1 
ATOM   1856 C CE1  . PHE A 1 276 ? 100.482 133.694 143.772 1.00 54.22  ? 276  PHE B CE1  1 
ATOM   1857 C CE2  . PHE A 1 276 ? 98.114  133.631 144.088 1.00 50.47  ? 276  PHE B CE2  1 
ATOM   1858 C CZ   . PHE A 1 276 ? 99.240  133.200 143.419 1.00 52.55  ? 276  PHE B CZ   1 
ATOM   1859 N N    . VAL A 1 277 ? 98.156  138.654 145.653 1.00 48.64  ? 277  VAL B N    1 
ATOM   1860 C CA   . VAL A 1 277 ? 97.289  139.389 144.718 1.00 43.59  ? 277  VAL B CA   1 
ATOM   1861 C C    . VAL A 1 277 ? 98.048  140.517 144.004 1.00 48.27  ? 277  VAL B C    1 
ATOM   1862 O O    . VAL A 1 277 ? 97.849  140.745 142.806 1.00 44.81  ? 277  VAL B O    1 
ATOM   1863 C CB   . VAL A 1 277 ? 96.031  139.903 145.446 1.00 47.30  ? 277  VAL B CB   1 
ATOM   1864 C CG1  . VAL A 1 277 ? 96.392  140.612 146.733 1.00 48.11  ? 277  VAL B CG1  1 
ATOM   1865 C CG2  . VAL A 1 277 ? 95.195  140.803 144.542 1.00 48.31  ? 277  VAL B CG2  1 
ATOM   1866 N N    . VAL A 1 278 ? 98.951  141.212 144.708 1.00 54.15  ? 278  VAL B N    1 
ATOM   1867 C CA   . VAL A 1 278 ? 99.835  142.190 144.055 1.00 43.11  ? 278  VAL B CA   1 
ATOM   1868 C C    . VAL A 1 278 ? 100.693 141.529 142.981 1.00 42.69  ? 278  VAL B C    1 
ATOM   1869 O O    . VAL A 1 278 ? 100.857 142.066 141.878 1.00 54.33  ? 278  VAL B O    1 
ATOM   1870 C CB   . VAL A 1 278 ? 100.700 142.967 145.061 1.00 39.99  ? 278  VAL B CB   1 
ATOM   1871 C CG1  . VAL A 1 278 ? 101.210 144.218 144.401 1.00 50.54  ? 278  VAL B CG1  1 
ATOM   1872 C CG2  . VAL A 1 278 ? 99.865  143.418 146.198 1.00 43.46  ? 278  VAL B CG2  1 
ATOM   1873 N N    . LEU A 1 279 ? 101.263 140.365 143.298 1.00 28.01  ? 279  LEU B N    1 
ATOM   1874 C CA   . LEU A 1 279 ? 102.112 139.633 142.360 1.00 29.23  ? 279  LEU B CA   1 
ATOM   1875 C C    . LEU A 1 279 ? 101.345 139.235 141.107 1.00 38.40  ? 279  LEU B C    1 
ATOM   1876 O O    . LEU A 1 279 ? 101.919 139.178 140.013 1.00 47.47  ? 279  LEU B O    1 
ATOM   1877 C CB   . LEU A 1 279 ? 102.693 138.397 143.048 1.00 35.22  ? 279  LEU B CB   1 
ATOM   1878 C CG   . LEU A 1 279 ? 103.911 137.745 142.401 1.00 33.85  ? 279  LEU B CG   1 
ATOM   1879 C CD1  . LEU A 1 279 ? 104.876 138.807 141.923 1.00 30.81  ? 279  LEU B CD1  1 
ATOM   1880 C CD2  . LEU A 1 279 ? 104.594 136.795 143.373 1.00 42.21  ? 279  LEU B CD2  1 
ATOM   1881 N N    . ILE A 1 280 ? 100.057 138.919 141.251 1.00 36.61  ? 280  ILE B N    1 
ATOM   1882 C CA   . ILE A 1 280 ? 99.249  138.497 140.105 1.00 34.36  ? 280  ILE B CA   1 
ATOM   1883 C C    . ILE A 1 280 ? 99.172  139.630 139.084 1.00 37.14  ? 280  ILE B C    1 
ATOM   1884 O O    . ILE A 1 280 ? 99.333  139.419 137.877 1.00 34.39  ? 280  ILE B O    1 
ATOM   1885 C CB   . ILE A 1 280 ? 97.850  138.057 140.567 1.00 35.84  ? 280  ILE B CB   1 
ATOM   1886 C CG1  . ILE A 1 280 ? 97.902  136.666 141.202 1.00 43.95  ? 280  ILE B CG1  1 
ATOM   1887 C CG2  . ILE A 1 280 ? 96.871  138.062 139.406 1.00 28.71  ? 280  ILE B CG2  1 
ATOM   1888 C CD1  . ILE A 1 280 ? 98.500  135.605 140.315 1.00 37.89  ? 280  ILE B CD1  1 
ATOM   1889 N N    . LEU A 1 281 ? 98.940  140.855 139.562 1.00 40.72  ? 281  LEU B N    1 
ATOM   1890 C CA   . LEU A 1 281 ? 98.780  142.017 138.694 1.00 38.02  ? 281  LEU B CA   1 
ATOM   1891 C C    . LEU A 1 281 ? 100.101 142.429 138.048 1.00 40.14  ? 281  LEU B C    1 
ATOM   1892 O O    . LEU A 1 281 ? 100.125 142.872 136.898 1.00 47.27  ? 281  LEU B O    1 
ATOM   1893 C CB   . LEU A 1 281 ? 98.190  143.205 139.462 1.00 40.70  ? 281  LEU B CB   1 
ATOM   1894 C CG   . LEU A 1 281 ? 96.824  143.031 140.125 1.00 42.17  ? 281  LEU B CG   1 
ATOM   1895 C CD1  . LEU A 1 281 ? 96.864  143.515 141.557 1.00 37.89  ? 281  LEU B CD1  1 
ATOM   1896 C CD2  . LEU A 1 281 ? 95.746  143.759 139.348 1.00 42.49  ? 281  LEU B CD2  1 
ATOM   1897 N N    . LEU A 1 282 ? 101.182 142.442 138.820 1.00 33.96  ? 282  LEU B N    1 
ATOM   1898 C CA   . LEU A 1 282 ? 102.458 142.919 138.294 1.00 31.19  ? 282  LEU B CA   1 
ATOM   1899 C C    . LEU A 1 282 ? 102.968 142.099 137.103 1.00 39.15  ? 282  LEU B C    1 
ATOM   1900 O O    . LEU A 1 282 ? 103.410 142.659 136.094 1.00 49.99  ? 282  LEU B O    1 
ATOM   1901 C CB   . LEU A 1 282 ? 103.503 142.928 139.409 1.00 20.72  ? 282  LEU B CB   1 
ATOM   1902 C CG   . LEU A 1 282 ? 103.500 144.138 140.341 1.00 25.32  ? 282  LEU B CG   1 
ATOM   1903 C CD1  . LEU A 1 282 ? 104.753 144.150 141.200 1.00 31.87  ? 282  LEU B CD1  1 
ATOM   1904 C CD2  . LEU A 1 282 ? 103.378 145.422 139.544 1.00 28.33  ? 282  LEU B CD2  1 
ATOM   1905 N N    . ILE A 1 283 ? 102.919 140.767 137.210 1.00 24.44  ? 283  ILE B N    1 
ATOM   1906 C CA   . ILE A 1 283 ? 103.293 139.882 136.099 1.00 14.84  ? 283  ILE B CA   1 
ATOM   1907 C C    . ILE A 1 283 ? 102.374 140.001 134.875 1.00 23.20  ? 283  ILE B C    1 
ATOM   1908 O O    . ILE A 1 283 ? 102.852 139.940 133.734 1.00 27.13  ? 283  ILE B O    1 
ATOM   1909 C CB   . ILE A 1 283 ? 103.370 138.433 136.617 1.00 6.50   ? 283  ILE B CB   1 
ATOM   1910 C CG1  . ILE A 1 283 ? 104.598 138.270 137.508 1.00 16.30  ? 283  ILE B CG1  1 
ATOM   1911 C CG2  . ILE A 1 283 ? 103.434 137.428 135.489 1.00 17.25  ? 283  ILE B CG2  1 
ATOM   1912 C CD1  . ILE A 1 283 ? 104.564 137.032 138.358 1.00 36.08  ? 283  ILE B CD1  1 
ATOM   1913 N N    . THR A 1 284 ? 101.063 140.197 135.063 1.00 29.97  ? 284  THR B N    1 
ATOM   1914 C CA   . THR A 1 284 ? 100.199 140.406 133.890 1.00 40.10  ? 284  THR B CA   1 
ATOM   1915 C C    . THR A 1 284 ? 100.543 141.705 133.163 1.00 31.73  ? 284  THR B C    1 
ATOM   1916 O O    . THR A 1 284 ? 100.478 141.777 131.933 1.00 23.13  ? 284  THR B O    1 
ATOM   1917 C CB   . THR A 1 284 ? 98.694  140.299 134.195 1.00 36.43  ? 284  THR B CB   1 
ATOM   1918 O OG1  . THR A 1 284 ? 97.958  140.669 133.022 1.00 43.36  ? 284  THR B OG1  1 
ATOM   1919 C CG2  . THR A 1 284 ? 98.244  141.180 135.283 1.00 28.11  ? 284  THR B CG2  1 
ATOM   1920 N N    . ALA A 1 285 ? 100.893 142.749 133.913 1.00 30.01  ? 285  ALA B N    1 
ATOM   1921 C CA   . ALA A 1 285 ? 101.266 144.035 133.332 1.00 27.45  ? 285  ALA B CA   1 
ATOM   1922 C C    . ALA A 1 285 ? 102.485 143.903 132.426 1.00 22.50  ? 285  ALA B C    1 
ATOM   1923 O O    . ALA A 1 285 ? 102.482 144.433 131.312 1.00 38.48  ? 285  ALA B O    1 
ATOM   1924 C CB   . ALA A 1 285 ? 101.537 145.062 134.433 1.00 23.41  ? 285  ALA B CB   1 
ATOM   1925 N N    . LYS A 1 286 ? 103.540 143.235 132.881 1.00 3.92   ? 286  LYS B N    1 
ATOM   1926 C CA   . LYS A 1 286 ? 104.730 143.103 132.048 1.00 9.21   ? 286  LYS B CA   1 
ATOM   1927 C C    . LYS A 1 286 ? 104.453 142.244 130.815 1.00 25.17  ? 286  LYS B C    1 
ATOM   1928 O O    . LYS A 1 286 ? 104.629 142.707 129.685 1.00 26.50  ? 286  LYS B O    1 
ATOM   1929 C CB   . LYS A 1 286 ? 105.901 142.528 132.843 1.00 10.87  ? 286  LYS B CB   1 
ATOM   1930 C CG   . LYS A 1 286 ? 107.038 142.062 131.953 1.00 12.53  ? 286  LYS B CG   1 
ATOM   1931 C CD   . LYS A 1 286 ? 108.376 142.545 132.463 1.00 16.18  ? 286  LYS B CD   1 
ATOM   1932 C CE   . LYS A 1 286 ? 109.422 142.498 131.367 1.00 22.44  ? 286  LYS B CE   1 
ATOM   1933 N NZ   . LYS A 1 286 ? 108.875 142.958 130.062 1.00 10.65  ? 286  LYS B NZ   1 
ATOM   1934 N N    . LEU A 1 287 ? 104.045 140.991 131.011 1.00 26.51  ? 287  LEU B N    1 
ATOM   1935 C CA   . LEU A 1 287 ? 103.907 140.031 129.917 1.00 17.24  ? 287  LEU B CA   1 
ATOM   1936 C C    . LEU A 1 287 ? 102.741 140.295 128.962 1.00 21.61  ? 287  LEU B C    1 
ATOM   1937 O O    . LEU A 1 287 ? 102.869 140.046 127.760 1.00 25.65  ? 287  LEU B O    1 
ATOM   1938 C CB   . LEU A 1 287 ? 103.787 138.611 130.475 1.00 10.57  ? 287  LEU B CB   1 
ATOM   1939 C CG   . LEU A 1 287 ? 105.022 138.060 131.191 1.00 15.22  ? 287  LEU B CG   1 
ATOM   1940 C CD1  . LEU A 1 287 ? 104.644 136.910 132.098 1.00 29.66  ? 287  LEU B CD1  1 
ATOM   1941 C CD2  . LEU A 1 287 ? 106.072 137.623 130.198 1.00 16.37  ? 287  LEU B CD2  1 
ATOM   1942 N N    . LEU A 1 288 ? 101.598 140.766 129.467 1.00 30.61  ? 288  LEU B N    1 
ATOM   1943 C CA   . LEU A 1 288 ? 100.406 140.870 128.623 1.00 27.05  ? 288  LEU B CA   1 
ATOM   1944 C C    . LEU A 1 288 ? 100.227 142.260 128.011 1.00 34.15  ? 288  LEU B C    1 
ATOM   1945 O O    . LEU A 1 288 ? 100.191 142.402 126.784 1.00 34.09  ? 288  LEU B O    1 
ATOM   1946 C CB   . LEU A 1 288 ? 99.158  140.480 129.422 1.00 31.53  ? 288  LEU B CB   1 
ATOM   1947 C CG   . LEU A 1 288 ? 97.743  140.676 128.853 1.00 39.11  ? 288  LEU B CG   1 
ATOM   1948 C CD1  . LEU A 1 288 ? 97.606  140.252 127.386 1.00 37.87  ? 288  LEU B CD1  1 
ATOM   1949 C CD2  . LEU A 1 288 ? 96.716  139.961 129.720 1.00 41.21  ? 288  LEU B CD2  1 
ATOM   1950 N N    . VAL A 1 289 ? 100.069 143.295 128.841 1.00 36.88  ? 289  VAL B N    1 
ATOM   1951 C CA   . VAL A 1 289 ? 99.629  144.583 128.302 1.00 36.48  ? 289  VAL B CA   1 
ATOM   1952 C C    . VAL A 1 289 ? 100.782 145.365 127.677 1.00 32.18  ? 289  VAL B C    1 
ATOM   1953 O O    . VAL A 1 289 ? 100.551 146.261 126.860 1.00 39.21  ? 289  VAL B O    1 
ATOM   1954 C CB   . VAL A 1 289 ? 98.903  145.411 129.382 1.00 35.45  ? 289  VAL B CB   1 
ATOM   1955 C CG1  . VAL A 1 289 ? 97.803  144.590 130.038 1.00 45.53  ? 289  VAL B CG1  1 
ATOM   1956 C CG2  . VAL A 1 289 ? 99.870  145.969 130.406 1.00 21.29  ? 289  VAL B CG2  1 
ATOM   1957 N N    . LEU A 1 290 ? 102.030 145.057 128.030 1.00 13.11  ? 290  LEU B N    1 
ATOM   1958 C CA   . LEU A 1 290 ? 103.141 145.733 127.357 1.00 8.83   ? 290  LEU B CA   1 
ATOM   1959 C C    . LEU A 1 290 ? 103.241 145.382 125.871 1.00 29.87  ? 290  LEU B C    1 
ATOM   1960 O O    . LEU A 1 290 ? 103.331 146.317 125.055 1.00 31.65  ? 290  LEU B O    1 
ATOM   1961 C CB   . LEU A 1 290 ? 104.450 145.471 128.113 1.00 7.05   ? 290  LEU B CB   1 
ATOM   1962 C CG   . LEU A 1 290 ? 105.757 145.906 127.447 1.00 14.58  ? 290  LEU B CG   1 
ATOM   1963 C CD1  . LEU A 1 290 ? 105.996 147.388 127.650 1.00 19.43  ? 290  LEU B CD1  1 
ATOM   1964 C CD2  . LEU A 1 290 ? 106.929 145.100 127.987 1.00 10.17  ? 290  LEU B CD2  1 
ATOM   1965 N N    . PRO A 1 291 ? 103.263 144.104 125.443 1.00 28.89  ? 291  PRO B N    1 
ATOM   1966 C CA   . PRO A 1 291 ? 103.366 143.823 123.993 1.00 19.40  ? 291  PRO B CA   1 
ATOM   1967 C C    . PRO A 1 291 ? 102.228 144.372 123.136 1.00 21.89  ? 291  PRO B C    1 
ATOM   1968 O O    . PRO A 1 291 ? 102.453 144.732 121.974 1.00 21.52  ? 291  PRO B O    1 
ATOM   1969 C CB   . PRO A 1 291 ? 103.422 142.290 123.947 1.00 17.98  ? 291  PRO B CB   1 
ATOM   1970 C CG   . PRO A 1 291 ? 103.953 141.904 125.261 1.00 24.59  ? 291  PRO B CG   1 
ATOM   1971 C CD   . PRO A 1 291 ? 103.286 142.838 126.201 1.00 18.64  ? 291  PRO B CD   1 
ATOM   1972 N N    . LEU A 1 292 ? 101.006 144.418 123.673 1.00 32.91  ? 292  LEU B N    1 
ATOM   1973 C CA   . LEU A 1 292 ? 99.870  144.983 122.943 1.00 33.66  ? 292  LEU B CA   1 
ATOM   1974 C C    . LEU A 1 292 ? 100.063 146.464 122.624 1.00 30.26  ? 292  LEU B C    1 
ATOM   1975 O O    . LEU A 1 292 ? 99.753  146.910 121.513 1.00 29.25  ? 292  LEU B O    1 
ATOM   1976 C CB   . LEU A 1 292 ? 98.585  144.765 123.740 1.00 35.46  ? 292  LEU B CB   1 
ATOM   1977 C CG   . LEU A 1 292 ? 98.046  143.333 123.722 1.00 30.26  ? 292  LEU B CG   1 
ATOM   1978 C CD1  . LEU A 1 292 ? 96.970  143.146 124.778 1.00 33.18  ? 292  LEU B CD1  1 
ATOM   1979 C CD2  . LEU A 1 292 ? 97.519  142.975 122.342 1.00 31.12  ? 292  LEU B CD2  1 
ATOM   1980 N N    . LEU A 1 293 ? 100.556 147.248 123.586 1.00 27.03  ? 293  LEU B N    1 
ATOM   1981 C CA   . LEU A 1 293 ? 100.868 148.651 123.305 1.00 33.13  ? 293  LEU B CA   1 
ATOM   1982 C C    . LEU A 1 293 ? 101.986 148.770 122.277 1.00 41.53  ? 293  LEU B C    1 
ATOM   1983 O O    . LEU A 1 293 ? 101.949 149.649 121.408 1.00 44.23  ? 293  LEU B O    1 
ATOM   1984 C CB   . LEU A 1 293 ? 101.211 149.421 124.584 1.00 22.93  ? 293  LEU B CB   1 
ATOM   1985 C CG   . LEU A 1 293 ? 100.097 149.933 125.515 1.00 26.69  ? 293  LEU B CG   1 
ATOM   1986 C CD1  . LEU A 1 293 ? 99.085  148.894 125.967 1.00 32.37  ? 293  LEU B CD1  1 
ATOM   1987 C CD2  . LEU A 1 293 ? 100.713 150.635 126.720 1.00 29.90  ? 293  LEU B CD2  1 
ATOM   1988 N N    . CYS A 1 294 ? 103.007 147.918 122.385 1.00 38.10  ? 294  CYS B N    1 
ATOM   1989 C CA   . CYS A 1 294 ? 104.133 147.979 121.458 1.00 28.89  ? 294  CYS B CA   1 
ATOM   1990 C C    . CYS A 1 294 ? 103.684 147.721 120.021 1.00 27.00  ? 294  CYS B C    1 
ATOM   1991 O O    . CYS A 1 294 ? 104.092 148.434 119.102 1.00 28.33  ? 294  CYS B O    1 
ATOM   1992 C CB   . CYS A 1 294 ? 105.211 146.977 121.875 1.00 27.44  ? 294  CYS B CB   1 
ATOM   1993 S SG   . CYS A 1 294 ? 106.223 147.487 123.285 1.00 45.93  ? 294  CYS B SG   1 
ATOM   1994 N N    . ARG A 1 295 ? 102.820 146.725 119.810 1.00 34.60  ? 295  ARG B N    1 
ATOM   1995 C CA   . ARG A 1 295 ? 102.343 146.431 118.458 1.00 35.36  ? 295  ARG B CA   1 
ATOM   1996 C C    . ARG A 1 295 ? 101.432 147.519 117.904 1.00 44.64  ? 295  ARG B C    1 
ATOM   1997 O O    . ARG A 1 295 ? 101.550 147.885 116.729 1.00 48.28  ? 295  ARG B O    1 
ATOM   1998 C CB   . ARG A 1 295 ? 101.596 145.102 118.429 1.00 43.84  ? 295  ARG B CB   1 
ATOM   1999 C CG   . ARG A 1 295 ? 102.356 143.956 117.811 1.00 46.91  ? 295  ARG B CG   1 
ATOM   2000 C CD   . ARG A 1 295 ? 101.441 142.756 117.647 1.00 42.48  ? 295  ARG B CD   1 
ATOM   2001 N NE   . ARG A 1 295 ? 100.767 142.757 116.355 1.00 47.79  ? 295  ARG B NE   1 
ATOM   2002 C CZ   . ARG A 1 295 ? 99.468  142.956 116.190 1.00 49.58  ? 295  ARG B CZ   1 
ATOM   2003 N NH1  . ARG A 1 295 ? 98.667  143.181 117.218 1.00 38.23  ? 295  ARG B NH1  1 
ATOM   2004 N NH2  . ARG A 1 295 ? 98.960  142.937 114.961 1.00 53.16  ? 295  ARG B NH2  1 
ATOM   2005 N N    . GLU A 1 296 ? 100.492 148.015 118.713 1.00 53.20  ? 296  GLU B N    1 
ATOM   2006 C CA   . GLU A 1 296 ? 99.538  149.005 118.219 1.00 52.87  ? 296  GLU B CA   1 
ATOM   2007 C C    . GLU A 1 296 ? 100.224 150.296 117.780 1.00 55.65  ? 296  GLU B C    1 
ATOM   2008 O O    . GLU A 1 296 ? 99.908  150.841 116.716 1.00 52.26  ? 296  GLU B O    1 
ATOM   2009 C CB   . GLU A 1 296 ? 98.504  149.289 119.312 1.00 49.19  ? 296  GLU B CB   1 
ATOM   2010 C CG   . GLU A 1 296 ? 97.925  150.694 119.312 1.00 55.20  ? 296  GLU B CG   1 
ATOM   2011 C CD   . GLU A 1 296 ? 97.474  151.136 120.694 1.00 59.64  ? 296  GLU B CD   1 
ATOM   2012 O OE1  . GLU A 1 296 ? 98.250  151.838 121.379 1.00 59.80  ? 296  GLU B OE1  1 
ATOM   2013 O OE2  . GLU A 1 296 ? 96.351  150.775 121.102 1.00 56.32  ? 296  GLU B OE2  1 
ATOM   2014 N N    . MET A 1 297 ? 101.160 150.797 118.584 1.00 47.23  ? 297  MET B N    1 
ATOM   2015 C CA   . MET A 1 297 ? 101.914 151.996 118.231 1.00 43.93  ? 297  MET B CA   1 
ATOM   2016 C C    . MET A 1 297 ? 102.765 151.815 116.980 1.00 38.76  ? 297  MET B C    1 
ATOM   2017 O O    . MET A 1 297 ? 102.861 152.741 116.169 1.00 45.96  ? 297  MET B O    1 
ATOM   2018 C CB   . MET A 1 297 ? 102.718 152.449 119.437 1.00 41.84  ? 297  MET B CB   1 
ATOM   2019 C CG   . MET A 1 297 ? 101.770 152.829 120.566 1.00 46.67  ? 297  MET B CG   1 
ATOM   2020 S SD   . MET A 1 297 ? 102.372 154.199 121.535 1.00 60.76  ? 297  MET B SD   1 
ATOM   2021 C CE   . MET A 1 297 ? 104.007 153.569 121.790 1.00 40.23  ? 297  MET B CE   1 
ATOM   2022 N N    . VAL A 1 298 ? 103.405 150.654 116.821 1.00 34.23  ? 298  VAL B N    1 
ATOM   2023 C CA   . VAL A 1 298 ? 104.201 150.389 115.624 1.00 37.22  ? 298  VAL B CA   1 
ATOM   2024 C C    . VAL A 1 298 ? 103.317 150.431 114.387 1.00 44.07  ? 298  VAL B C    1 
ATOM   2025 O O    . VAL A 1 298 ? 103.692 151.001 113.361 1.00 44.51  ? 298  VAL B O    1 
ATOM   2026 C CB   . VAL A 1 298 ? 104.953 149.051 115.739 1.00 35.97  ? 298  VAL B CB   1 
ATOM   2027 C CG1  . VAL A 1 298 ? 105.618 148.717 114.425 1.00 33.32  ? 298  VAL B CG1  1 
ATOM   2028 C CG2  . VAL A 1 298 ? 106.022 149.150 116.788 1.00 42.15  ? 298  VAL B CG2  1 
ATOM   2029 N N    . GLU A 1 299 ? 102.088 149.934 114.509 1.00 64.44  ? 299  GLU B N    1 
ATOM   2030 C CA   . GLU A 1 299 ? 101.121 149.984 113.417 1.00 65.13  ? 299  GLU B CA   1 
ATOM   2031 C C    . GLU A 1 299 ? 100.645 151.409 113.162 1.00 61.33  ? 299  GLU B C    1 
ATOM   2032 O O    . GLU A 1 299 ? 100.166 151.727 112.068 1.00 61.53  ? 299  GLU B O    1 
ATOM   2033 C CB   . GLU A 1 299 ? 99.929  149.079 113.736 1.00 63.49  ? 299  GLU B CB   1 
ATOM   2034 C CG   . GLU A 1 299 ? 100.221 147.588 113.700 1.00 63.59  ? 299  GLU B CG   1 
ATOM   2035 C CD   . GLU A 1 299 ? 100.303 147.048 112.288 1.00 66.16  ? 299  GLU B CD   1 
ATOM   2036 O OE1  . GLU A 1 299 ? 99.889  147.763 111.351 1.00 66.09  ? 299  GLU B OE1  1 
ATOM   2037 O OE2  . GLU A 1 299 ? 100.767 145.904 112.110 1.00 64.93  ? 299  GLU B OE2  1 
ATOM   2038 N N    . LEU A 1 300 ? 100.766 152.279 114.162 1.00 56.22  ? 300  LEU B N    1 
ATOM   2039 C CA   . LEU A 1 300 ? 100.277 153.645 114.024 1.00 57.99  ? 300  LEU B CA   1 
ATOM   2040 C C    . LEU A 1 300 ? 101.338 154.573 113.433 1.00 65.63  ? 300  LEU B C    1 
ATOM   2041 O O    . LEU A 1 300 ? 101.007 155.490 112.672 1.00 66.21  ? 300  LEU B O    1 
ATOM   2042 C CB   . LEU A 1 300 ? 99.807  154.147 115.396 1.00 55.35  ? 300  LEU B CB   1 
ATOM   2043 C CG   . LEU A 1 300 ? 98.933  155.388 115.627 1.00 57.81  ? 300  LEU B CG   1 
ATOM   2044 C CD1  . LEU A 1 300 ? 98.387  155.344 117.043 1.00 64.79  ? 300  LEU B CD1  1 
ATOM   2045 C CD2  . LEU A 1 300 ? 99.675  156.703 115.424 1.00 57.34  ? 300  LEU B CD2  1 
ATOM   2046 N N    . LEU A 1 301 ? 102.614 154.352 113.750 1.00 70.14  ? 301  LEU B N    1 
ATOM   2047 C CA   . LEU A 1 301 ? 103.649 155.296 113.325 1.00 64.07  ? 301  LEU B CA   1 
ATOM   2048 C C    . LEU A 1 301 ? 104.423 154.915 112.059 1.00 65.97  ? 301  LEU B C    1 
ATOM   2049 O O    . LEU A 1 301 ? 104.803 155.801 111.287 1.00 72.24  ? 301  LEU B O    1 
ATOM   2050 C CB   . LEU A 1 301 ? 104.643 155.515 114.473 1.00 57.99  ? 301  LEU B CB   1 
ATOM   2051 C CG   . LEU A 1 301 ? 104.106 156.142 115.759 1.00 62.35  ? 301  LEU B CG   1 
ATOM   2052 C CD1  . LEU A 1 301 ? 105.180 156.143 116.831 1.00 65.21  ? 301  LEU B CD1  1 
ATOM   2053 C CD2  . LEU A 1 301 ? 103.602 157.551 115.504 1.00 65.15  ? 301  LEU B CD2  1 
ATOM   2054 N N    . ASP A 1 302 ? 104.675 153.627 111.820 1.00 72.18  ? 302  ASP B N    1 
ATOM   2055 C CA   . ASP A 1 302 ? 105.370 153.259 110.583 1.00 73.77  ? 302  ASP B CA   1 
ATOM   2056 C C    . ASP A 1 302 ? 104.495 153.380 109.333 1.00 76.06  ? 302  ASP B C    1 
ATOM   2057 O O    . ASP A 1 302 ? 103.381 152.855 109.268 1.00 76.16  ? 302  ASP B O    1 
ATOM   2058 C CB   . ASP A 1 302 ? 106.038 151.868 110.698 1.00 71.20  ? 302  ASP B CB   1 
ATOM   2059 C CG   . ASP A 1 302 ? 105.071 150.675 110.736 1.00 75.58  ? 302  ASP B CG   1 
ATOM   2060 O OD1  . ASP A 1 302 ? 103.834 150.797 110.728 1.00 74.07  ? 302  ASP B OD1  1 
ATOM   2061 O OD2  . ASP A 1 302 ? 105.597 149.544 110.790 1.00 79.09  ? 302  ASP B OD2  1 
ATOM   2062 N N    . LYS A 1 303 ? 104.950 154.198 108.389 1.00 84.76  ? 303  LYS B N    1 
ATOM   2063 C CA   . LYS A 1 303 ? 104.252 154.426 107.126 1.00 85.66  ? 303  LYS B CA   1 
ATOM   2064 C C    . LYS A 1 303 ? 105.230 154.081 106.004 1.00 86.38  ? 303  LYS B C    1 
ATOM   2065 O O    . LYS A 1 303 ? 105.936 154.956 105.498 1.00 86.17  ? 303  LYS B O    1 
ATOM   2066 C CB   . LYS A 1 303 ? 103.746 155.863 107.020 1.00 85.89  ? 303  LYS B CB   1 
ATOM   2067 C CG   . LYS A 1 303 ? 102.637 156.201 108.005 1.00 84.67  ? 303  LYS B CG   1 
ATOM   2068 C CD   . LYS A 1 303 ? 103.042 157.333 108.933 1.00 84.33  ? 303  LYS B CD   1 
ATOM   2069 C CE   . LYS A 1 303 ? 101.924 157.674 109.904 1.00 83.37  ? 303  LYS B CE   1 
ATOM   2070 N NZ   . LYS A 1 303 ? 102.306 158.785 110.819 1.00 83.67  ? 303  LYS B NZ   1 
ATOM   2071 N N    . GLY A 1 304 ? 105.273 152.809 105.616 1.00 101.70 ? 304  GLY B N    1 
ATOM   2072 C CA   . GLY A 1 304 ? 106.148 152.359 104.550 1.00 100.97 ? 304  GLY B CA   1 
ATOM   2073 C C    . GLY A 1 304 ? 105.397 151.618 103.460 1.00 100.83 ? 304  GLY B C    1 
ATOM   2074 O O    . GLY A 1 304 ? 104.345 151.024 103.700 1.00 102.03 ? 304  GLY B O    1 
ATOM   2075 N N    . ASP A 1 305 ? 105.958 151.660 102.250 1.00 101.43 ? 305  ASP B N    1 
ATOM   2076 C CA   . ASP A 1 305 ? 105.369 151.033 101.072 1.00 102.59 ? 305  ASP B CA   1 
ATOM   2077 C C    . ASP A 1 305 ? 105.645 149.536 100.968 1.00 102.88 ? 305  ASP B C    1 
ATOM   2078 O O    . ASP A 1 305 ? 105.075 148.880 100.089 1.00 102.38 ? 305  ASP B O    1 
ATOM   2079 C CB   . ASP A 1 305 ? 105.880 151.736 99.810  1.00 101.52 ? 305  ASP B CB   1 
ATOM   2080 C CG   . ASP A 1 305 ? 104.981 151.515 98.610  1.00 103.97 ? 305  ASP B CG   1 
ATOM   2081 O OD1  . ASP A 1 305 ? 103.757 151.358 98.803  1.00 104.74 ? 305  ASP B OD1  1 
ATOM   2082 O OD2  . ASP A 1 305 ? 105.499 151.495 97.474  1.00 105.75 ? 305  ASP B OD2  1 
ATOM   2083 N N    . SER A 1 306 ? 106.481 148.972 101.836 1.00 91.50  ? 306  SER B N    1 
ATOM   2084 C CA   . SER A 1 306 ? 106.800 147.548 101.801 1.00 87.45  ? 306  SER B CA   1 
ATOM   2085 C C    . SER A 1 306 ? 105.912 146.793 102.781 1.00 89.70  ? 306  SER B C    1 
ATOM   2086 O O    . SER A 1 306 ? 106.078 146.917 103.999 1.00 92.92  ? 306  SER B O    1 
ATOM   2087 C CB   . SER A 1 306 ? 108.272 147.325 102.127 1.00 85.58  ? 306  SER B CB   1 
ATOM   2088 O OG   . SER A 1 306 ? 108.585 145.943 102.149 1.00 83.55  ? 306  SER B OG   1 
ATOM   2089 N N    . VAL A 1 307 ? 104.965 146.018 102.247 1.00 85.79  ? 307  VAL B N    1 
ATOM   2090 C CA   . VAL A 1 307 ? 104.054 145.267 103.103 1.00 85.75  ? 307  VAL B CA   1 
ATOM   2091 C C    . VAL A 1 307 ? 104.792 144.167 103.859 1.00 80.51  ? 307  VAL B C    1 
ATOM   2092 O O    . VAL A 1 307 ? 104.516 143.922 105.040 1.00 78.59  ? 307  VAL B O    1 
ATOM   2093 C CB   . VAL A 1 307 ? 102.886 144.702 102.273 1.00 83.37  ? 307  VAL B CB   1 
ATOM   2094 C CG1  . VAL A 1 307 ? 101.818 145.764 102.075 1.00 81.40  ? 307  VAL B CG1  1 
ATOM   2095 C CG2  . VAL A 1 307 ? 103.383 144.194 100.927 1.00 81.13  ? 307  VAL B CG2  1 
ATOM   2096 N N    . VAL A 1 308 ? 105.714 143.464 103.188 1.00 72.97  ? 308  VAL B N    1 
ATOM   2097 C CA   . VAL A 1 308 ? 106.445 142.378 103.842 1.00 73.68  ? 308  VAL B CA   1 
ATOM   2098 C C    . VAL A 1 308 ? 107.281 142.913 104.999 1.00 73.60  ? 308  VAL B C    1 
ATOM   2099 O O    . VAL A 1 308 ? 107.316 142.326 106.087 1.00 73.40  ? 308  VAL B O    1 
ATOM   2100 C CB   . VAL A 1 308 ? 107.314 141.624 102.819 1.00 78.24  ? 308  VAL B CB   1 
ATOM   2101 C CG1  . VAL A 1 308 ? 107.795 140.305 103.403 1.00 77.65  ? 308  VAL B CG1  1 
ATOM   2102 C CG2  . VAL A 1 308 ? 106.536 141.393 101.535 1.00 75.18  ? 308  VAL B CG2  1 
ATOM   2103 N N    . ASN A 1 309 ? 107.981 144.030 104.774 1.00 76.12  ? 309  ASN B N    1 
ATOM   2104 C CA   . ASN A 1 309 ? 108.724 144.669 105.856 1.00 79.17  ? 309  ASN B CA   1 
ATOM   2105 C C    . ASN A 1 309 ? 107.786 145.174 106.947 1.00 78.15  ? 309  ASN B C    1 
ATOM   2106 O O    . ASN A 1 309 ? 108.121 145.120 108.136 1.00 77.79  ? 309  ASN B O    1 
ATOM   2107 C CB   . ASN A 1 309 ? 109.622 145.783 105.310 1.00 80.19  ? 309  ASN B CB   1 
ATOM   2108 C CG   . ASN A 1 309 ? 110.812 145.239 104.517 1.00 81.00  ? 309  ASN B CG   1 
ATOM   2109 O OD1  . ASN A 1 309 ? 110.970 144.024 104.386 1.00 76.26  ? 309  ASN B OD1  1 
ATOM   2110 N ND2  . ASN A 1 309 ? 111.661 146.147 104.006 1.00 83.99  ? 309  ASN B ND2  1 
ATOM   2111 N N    . HIS A 1 310 ? 106.615 145.689 106.558 1.00 74.97  ? 310  HIS B N    1 
ATOM   2112 C CA   . HIS A 1 310 ? 105.631 146.148 107.536 1.00 74.50  ? 310  HIS B CA   1 
ATOM   2113 C C    . HIS A 1 310 ? 105.140 145.001 108.412 1.00 77.94  ? 310  HIS B C    1 
ATOM   2114 O O    . HIS A 1 310 ? 104.994 145.156 109.630 1.00 74.22  ? 310  HIS B O    1 
ATOM   2115 C CB   . HIS A 1 310 ? 104.453 146.802 106.815 1.00 71.04  ? 310  HIS B CB   1 
ATOM   2116 C CG   . HIS A 1 310 ? 103.601 147.658 107.696 1.00 77.24  ? 310  HIS B CG   1 
ATOM   2117 N ND1  . HIS A 1 310 ? 102.291 147.350 107.993 1.00 80.81  ? 310  HIS B ND1  1 
ATOM   2118 C CD2  . HIS A 1 310 ? 103.866 148.824 108.331 1.00 77.04  ? 310  HIS B CD2  1 
ATOM   2119 C CE1  . HIS A 1 310 ? 101.789 148.283 108.783 1.00 76.67  ? 310  HIS B CE1  1 
ATOM   2120 N NE2  . HIS A 1 310 ? 102.725 149.189 109.003 1.00 74.61  ? 310  HIS B NE2  1 
ATOM   2121 N N    . THR A 1 311 ? 104.866 143.847 107.801 1.00 68.72  ? 311  THR B N    1 
ATOM   2122 C CA   . THR A 1 311 ? 104.382 142.684 108.539 1.00 58.89  ? 311  THR B CA   1 
ATOM   2123 C C    . THR A 1 311 ? 105.434 142.160 109.511 1.00 61.84  ? 311  THR B C    1 
ATOM   2124 O O    . THR A 1 311 ? 105.139 141.906 110.685 1.00 65.24  ? 311  THR B O    1 
ATOM   2125 C CB   . THR A 1 311 ? 103.955 141.585 107.568 1.00 65.22  ? 311  THR B CB   1 
ATOM   2126 O OG1  . THR A 1 311 ? 103.035 142.124 106.610 1.00 73.30  ? 311  THR B OG1  1 
ATOM   2127 C CG2  . THR A 1 311 ? 103.283 140.446 108.319 1.00 63.76  ? 311  THR B CG2  1 
ATOM   2128 N N    . SER A 1 312 ? 106.665 141.981 109.028 1.00 58.55  ? 312  SER B N    1 
ATOM   2129 C CA   . SER A 1 312 ? 107.753 141.491 109.870 1.00 58.95  ? 312  SER B CA   1 
ATOM   2130 C C    . SER A 1 312 ? 108.085 142.449 111.010 1.00 56.62  ? 312  SER B C    1 
ATOM   2131 O O    . SER A 1 312 ? 108.335 142.009 112.138 1.00 57.31  ? 312  SER B O    1 
ATOM   2132 C CB   . SER A 1 312 ? 108.993 141.230 109.017 1.00 52.34  ? 312  SER B CB   1 
ATOM   2133 O OG   . SER A 1 312 ? 109.019 139.891 108.557 1.00 54.32  ? 312  SER B OG   1 
ATOM   2134 N N    . LEU A 1 313 ? 108.122 143.756 110.736 1.00 46.20  ? 313  LEU B N    1 
ATOM   2135 C CA   . LEU A 1 313 ? 108.417 144.715 111.798 1.00 41.76  ? 313  LEU B CA   1 
ATOM   2136 C C    . LEU A 1 313 ? 107.345 144.712 112.881 1.00 44.00  ? 313  LEU B C    1 
ATOM   2137 O O    . LEU A 1 313 ? 107.659 144.836 114.070 1.00 54.05  ? 313  LEU B O    1 
ATOM   2138 C CB   . LEU A 1 313 ? 108.554 146.117 111.205 1.00 51.71  ? 313  LEU B CB   1 
ATOM   2139 C CG   . LEU A 1 313 ? 109.155 147.209 112.089 1.00 50.03  ? 313  LEU B CG   1 
ATOM   2140 C CD1  . LEU A 1 313 ? 110.521 146.799 112.581 1.00 44.39  ? 313  LEU B CD1  1 
ATOM   2141 C CD2  . LEU A 1 313 ? 109.229 148.528 111.339 1.00 52.97  ? 313  LEU B CD2  1 
ATOM   2142 N N    . SER A 1 314 ? 106.075 144.592 112.491 1.00 35.61  ? 314  SER B N    1 
ATOM   2143 C CA   . SER A 1 314 ? 105.001 144.514 113.479 1.00 44.22  ? 314  SER B CA   1 
ATOM   2144 C C    . SER A 1 314 ? 105.107 143.261 114.343 1.00 44.52  ? 314  SER B C    1 
ATOM   2145 O O    . SER A 1 314 ? 104.909 143.319 115.563 1.00 33.41  ? 314  SER B O    1 
ATOM   2146 C CB   . SER A 1 314 ? 103.644 144.571 112.780 1.00 46.14  ? 314  SER B CB   1 
ATOM   2147 O OG   . SER A 1 314 ? 103.694 143.932 111.519 1.00 50.57  ? 314  SER B OG   1 
ATOM   2148 N N    . ASN A 1 315 ? 105.408 142.115 113.724 1.00 38.15  ? 315  ASN B N    1 
ATOM   2149 C CA   . ASN A 1 315 ? 105.573 140.868 114.469 1.00 31.88  ? 315  ASN B CA   1 
ATOM   2150 C C    . ASN A 1 315 ? 106.776 140.901 115.406 1.00 44.84  ? 315  ASN B C    1 
ATOM   2151 O O    . ASN A 1 315 ? 106.702 140.388 116.528 1.00 54.16  ? 315  ASN B O    1 
ATOM   2152 C CB   . ASN A 1 315 ? 105.687 139.697 113.496 1.00 30.01  ? 315  ASN B CB   1 
ATOM   2153 C CG   . ASN A 1 315 ? 104.397 139.437 112.750 1.00 35.98  ? 315  ASN B CG   1 
ATOM   2154 O OD1  . ASN A 1 315 ? 103.319 139.824 113.199 1.00 39.97  ? 315  ASN B OD1  1 
ATOM   2155 N ND2  . ASN A 1 315 ? 104.499 138.778 111.602 1.00 43.77  ? 315  ASN B ND2  1 
ATOM   2156 N N    . TYR A 1 316 ? 107.900 141.465 114.955 1.00 32.34  ? 316  TYR B N    1 
ATOM   2157 C CA   . TYR A 1 316 ? 109.094 141.527 115.796 1.00 23.01  ? 316  TYR B CA   1 
ATOM   2158 C C    . TYR A 1 316 ? 108.862 142.376 117.042 1.00 24.77  ? 316  TYR B C    1 
ATOM   2159 O O    . TYR A 1 316 ? 109.424 142.096 118.107 1.00 35.71  ? 316  TYR B O    1 
ATOM   2160 C CB   . TYR A 1 316 ? 110.274 142.066 114.987 1.00 26.33  ? 316  TYR B CB   1 
ATOM   2161 C CG   . TYR A 1 316 ? 111.536 142.279 115.793 1.00 28.63  ? 316  TYR B CG   1 
ATOM   2162 C CD1  . TYR A 1 316 ? 112.091 141.247 116.536 1.00 20.69  ? 316  TYR B CD1  1 
ATOM   2163 C CD2  . TYR A 1 316 ? 112.175 143.511 115.804 1.00 32.35  ? 316  TYR B CD2  1 
ATOM   2164 C CE1  . TYR A 1 316 ? 113.245 141.437 117.270 1.00 21.58  ? 316  TYR B CE1  1 
ATOM   2165 C CE2  . TYR A 1 316 ? 113.328 143.710 116.536 1.00 27.91  ? 316  TYR B CE2  1 
ATOM   2166 C CZ   . TYR A 1 316 ? 113.858 142.671 117.266 1.00 28.09  ? 316  TYR B CZ   1 
ATOM   2167 O OH   . TYR A 1 316 ? 115.006 142.866 117.995 1.00 37.37  ? 316  TYR B OH   1 
ATOM   2168 N N    . ALA A 1 317 ? 108.055 143.431 116.918 1.00 14.92  ? 317  ALA B N    1 
ATOM   2169 C CA   . ALA A 1 317 ? 107.756 144.295 118.056 1.00 11.38  ? 317  ALA B CA   1 
ATOM   2170 C C    . ALA A 1 317 ? 107.020 143.552 119.167 1.00 26.46  ? 317  ALA B C    1 
ATOM   2171 O O    . ALA A 1 317 ? 107.283 143.784 120.353 1.00 41.37  ? 317  ALA B O    1 
ATOM   2172 C CB   . ALA A 1 317 ? 106.940 145.500 117.592 1.00 27.94  ? 317  ALA B CB   1 
ATOM   2173 N N    . PHE A 1 318 ? 106.081 142.673 118.806 1.00 23.34  ? 318  PHE B N    1 
ATOM   2174 C CA   . PHE A 1 318 ? 105.344 141.900 119.805 1.00 23.39  ? 318  PHE B CA   1 
ATOM   2175 C C    . PHE A 1 318 ? 106.257 140.963 120.588 1.00 20.74  ? 318  PHE B C    1 
ATOM   2176 O O    . PHE A 1 318 ? 106.205 140.919 121.823 1.00 28.93  ? 318  PHE B O    1 
ATOM   2177 C CB   . PHE A 1 318 ? 104.225 141.109 119.122 1.00 15.98  ? 318  PHE B CB   1 
ATOM   2178 C CG   . PHE A 1 318 ? 103.366 140.304 120.066 1.00 16.82  ? 318  PHE B CG   1 
ATOM   2179 C CD1  . PHE A 1 318 ? 103.697 139.003 120.413 1.00 20.07  ? 318  PHE B CD1  1 
ATOM   2180 C CD2  . PHE A 1 318 ? 102.211 140.854 120.597 1.00 27.03  ? 318  PHE B CD2  1 
ATOM   2181 C CE1  . PHE A 1 318 ? 102.903 138.279 121.279 1.00 28.49  ? 318  PHE B CE1  1 
ATOM   2182 C CE2  . PHE A 1 318 ? 101.411 140.129 121.460 1.00 29.74  ? 318  PHE B CE2  1 
ATOM   2183 C CZ   . PHE A 1 318 ? 101.758 138.841 121.801 1.00 28.20  ? 318  PHE B CZ   1 
ATOM   2184 N N    . LEU A 1 319 ? 107.083 140.187 119.883 1.00 18.84  ? 319  LEU B N    1 
ATOM   2185 C CA   . LEU A 1 319 ? 107.949 139.211 120.540 1.00 20.88  ? 319  LEU B CA   1 
ATOM   2186 C C    . LEU A 1 319 ? 108.959 139.861 121.480 1.00 17.05  ? 319  LEU B C    1 
ATOM   2187 O O    . LEU A 1 319 ? 109.396 139.229 122.448 1.00 23.68  ? 319  LEU B O    1 
ATOM   2188 C CB   . LEU A 1 319 ? 108.666 138.373 119.480 1.00 16.47  ? 319  LEU B CB   1 
ATOM   2189 C CG   . LEU A 1 319 ? 109.622 137.266 119.929 1.00 22.34  ? 319  LEU B CG   1 
ATOM   2190 C CD1  . LEU A 1 319 ? 108.854 136.116 120.559 1.00 26.17  ? 319  LEU B CD1  1 
ATOM   2191 C CD2  . LEU A 1 319 ? 110.463 136.779 118.760 1.00 21.43  ? 319  LEU B CD2  1 
ATOM   2192 N N    . TYR A 1 320 ? 109.345 141.112 121.215 1.00 15.82  ? 320  TYR B N    1 
ATOM   2193 C CA   . TYR A 1 320 ? 110.339 141.776 122.055 1.00 11.40  ? 320  TYR B CA   1 
ATOM   2194 C C    . TYR A 1 320 ? 109.837 141.980 123.483 1.00 14.26  ? 320  TYR B C    1 
ATOM   2195 O O    . TYR A 1 320 ? 110.593 141.792 124.441 1.00 33.09  ? 320  TYR B O    1 
ATOM   2196 C CB   . TYR A 1 320 ? 110.754 143.113 121.437 1.00 20.83  ? 320  TYR B CB   1 
ATOM   2197 C CG   . TYR A 1 320 ? 111.382 144.069 122.428 1.00 17.02  ? 320  TYR B CG   1 
ATOM   2198 C CD1  . TYR A 1 320 ? 112.726 143.953 122.752 1.00 22.17  ? 320  TYR B CD1  1 
ATOM   2199 C CD2  . TYR A 1 320 ? 110.649 145.090 123.026 1.00 16.54  ? 320  TYR B CD2  1 
ATOM   2200 C CE1  . TYR A 1 320 ? 113.322 144.808 123.646 1.00 25.83  ? 320  TYR B CE1  1 
ATOM   2201 C CE2  . TYR A 1 320 ? 111.241 145.949 123.933 1.00 22.50  ? 320  TYR B CE2  1 
ATOM   2202 C CZ   . TYR A 1 320 ? 112.579 145.802 124.235 1.00 22.95  ? 320  TYR B CZ   1 
ATOM   2203 O OH   . TYR A 1 320 ? 113.188 146.646 125.129 1.00 28.38  ? 320  TYR B OH   1 
ATOM   2204 N N    . GLY A 1 321 ? 108.571 142.370 123.651 1.00 5.25   ? 321  GLY B N    1 
ATOM   2205 C CA   . GLY A 1 321 ? 108.070 142.686 124.980 1.00 25.37  ? 321  GLY B CA   1 
ATOM   2206 C C    . GLY A 1 321 ? 107.800 141.488 125.867 1.00 25.03  ? 321  GLY B C    1 
ATOM   2207 O O    . GLY A 1 321 ? 107.697 141.646 127.088 1.00 32.57  ? 321  GLY B O    1 
ATOM   2208 N N    . VAL A 1 322 ? 107.674 140.296 125.282 1.00 16.36  ? 322  VAL B N    1 
ATOM   2209 C CA   . VAL A 1 322 ? 107.356 139.083 126.029 1.00 3.96   ? 322  VAL B CA   1 
ATOM   2210 C C    . VAL A 1 322 ? 108.498 138.629 126.939 1.00 10.19  ? 322  VAL B C    1 
ATOM   2211 O O    . VAL A 1 322 ? 108.278 137.803 127.834 1.00 27.89  ? 322  VAL B O    1 
ATOM   2212 C CB   . VAL A 1 322 ? 106.917 138.037 124.976 1.00 11.54  ? 322  VAL B CB   1 
ATOM   2213 C CG1  . VAL A 1 322 ? 106.676 136.661 125.559 1.00 23.63  ? 322  VAL B CG1  1 
ATOM   2214 C CG2  . VAL A 1 322 ? 105.669 138.519 124.257 1.00 18.66  ? 322  VAL B CG2  1 
ATOM   2215 N N    . PHE A 1 323 ? 109.693 139.198 126.782 1.00 2.19   ? 323  PHE B N    1 
ATOM   2216 C CA   . PHE A 1 323 ? 110.864 138.756 127.535 1.00 6.47   ? 323  PHE B CA   1 
ATOM   2217 C C    . PHE A 1 323 ? 110.660 138.898 129.046 1.00 14.50  ? 323  PHE B C    1 
ATOM   2218 O O    . PHE A 1 323 ? 110.013 139.847 129.503 1.00 19.20  ? 323  PHE B O    1 
ATOM   2219 C CB   . PHE A 1 323 ? 112.090 139.564 127.103 1.00 9.21   ? 323  PHE B CB   1 
ATOM   2220 C CG   . PHE A 1 323 ? 112.496 139.344 125.669 1.00 18.72  ? 323  PHE B CG   1 
ATOM   2221 C CD1  . PHE A 1 323 ? 112.121 138.197 124.989 1.00 18.24  ? 323  PHE B CD1  1 
ATOM   2222 C CD2  . PHE A 1 323 ? 113.246 140.296 124.999 1.00 22.96  ? 323  PHE B CD2  1 
ATOM   2223 C CE1  . PHE A 1 323 ? 112.489 138.004 123.671 1.00 15.63  ? 323  PHE B CE1  1 
ATOM   2224 C CE2  . PHE A 1 323 ? 113.612 140.109 123.681 1.00 18.88  ? 323  PHE B CE2  1 
ATOM   2225 C CZ   . PHE A 1 323 ? 113.234 138.961 123.018 1.00 10.64  ? 323  PHE B CZ   1 
ATOM   2226 N N    . PRO A 1 324 ? 111.188 137.965 129.840 1.00 5.51   ? 324  PRO B N    1 
ATOM   2227 C CA   . PRO A 1 324 ? 111.009 138.006 131.300 1.00 5.70   ? 324  PRO B CA   1 
ATOM   2228 C C    . PRO A 1 324 ? 111.747 139.165 131.959 1.00 13.48  ? 324  PRO B C    1 
ATOM   2229 O O    . PRO A 1 324 ? 112.578 139.848 131.358 1.00 30.46  ? 324  PRO B O    1 
ATOM   2230 C CB   . PRO A 1 324 ? 111.562 136.657 131.763 1.00 6.75   ? 324  PRO B CB   1 
ATOM   2231 C CG   . PRO A 1 324 ? 112.517 136.265 130.715 1.00 13.18  ? 324  PRO B CG   1 
ATOM   2232 C CD   . PRO A 1 324 ? 111.977 136.795 129.420 1.00 15.23  ? 324  PRO B CD   1 
ATOM   2233 N N    . VAL A 1 325 ? 111.402 139.384 133.233 1.00 8.80   ? 325  VAL B N    1 
ATOM   2234 C CA   . VAL A 1 325 ? 112.002 140.455 134.023 1.00 11.76  ? 325  VAL B CA   1 
ATOM   2235 C C    . VAL A 1 325 ? 113.495 140.204 134.199 1.00 29.86  ? 325  VAL B C    1 
ATOM   2236 O O    . VAL A 1 325 ? 113.928 139.081 134.488 1.00 32.79  ? 325  VAL B O    1 
ATOM   2237 C CB   . VAL A 1 325 ? 111.308 140.557 135.393 1.00 5.76   ? 325  VAL B CB   1 
ATOM   2238 C CG1  . VAL A 1 325 ? 111.903 141.686 136.223 1.00 0.00   ? 325  VAL B CG1  1 
ATOM   2239 C CG2  . VAL A 1 325 ? 109.815 140.732 135.229 1.00 12.45  ? 325  VAL B CG2  1 
ATOM   2240 N N    . ALA A 1 326 ? 114.291 141.256 134.000 1.00 33.36  ? 326  ALA B N    1 
ATOM   2241 C CA   . ALA A 1 326 ? 115.740 141.136 134.083 1.00 16.78  ? 326  ALA B CA   1 
ATOM   2242 C C    . ALA A 1 326 ? 116.174 140.812 135.513 1.00 22.24  ? 326  ALA B C    1 
ATOM   2243 O O    . ALA A 1 326 ? 115.619 141.363 136.469 1.00 24.17  ? 326  ALA B O    1 
ATOM   2244 C CB   . ALA A 1 326 ? 116.393 142.440 133.617 1.00 8.63   ? 326  ALA B CB   1 
ATOM   2245 N N    . PRO A 1 327 ? 117.149 139.912 135.694 1.00 27.35  ? 327  PRO B N    1 
ATOM   2246 C CA   . PRO A 1 327 ? 117.598 139.579 137.054 1.00 22.47  ? 327  PRO B CA   1 
ATOM   2247 C C    . PRO A 1 327 ? 118.258 140.713 137.835 1.00 20.77  ? 327  PRO B C    1 
ATOM   2248 O O    . PRO A 1 327 ? 118.359 140.607 139.063 1.00 29.00  ? 327  PRO B O    1 
ATOM   2249 C CB   . PRO A 1 327 ? 118.545 138.393 136.812 1.00 18.40  ? 327  PRO B CB   1 
ATOM   2250 C CG   . PRO A 1 327 ? 118.868 138.440 135.301 1.00 26.22  ? 327  PRO B CG   1 
ATOM   2251 C CD   . PRO A 1 327 ? 118.280 139.706 134.776 1.00 29.83  ? 327  PRO B CD   1 
ATOM   2252 N N    . GLY A 1 328 ? 118.716 141.782 137.179 1.00 16.98  ? 328  GLY B N    1 
ATOM   2253 C CA   . GLY A 1 328 ? 119.347 142.889 137.882 1.00 22.01  ? 328  GLY B CA   1 
ATOM   2254 C C    . GLY A 1 328 ? 118.439 143.624 138.847 1.00 24.73  ? 328  GLY B C    1 
ATOM   2255 O O    . GLY A 1 328 ? 118.933 144.284 139.766 1.00 33.15  ? 328  GLY B O    1 
ATOM   2256 N N    . VAL A 1 329 ? 117.122 143.543 138.646 1.00 25.25  ? 329  VAL B N    1 
ATOM   2257 C CA   . VAL A 1 329 ? 116.171 144.200 139.540 1.00 24.66  ? 329  VAL B CA   1 
ATOM   2258 C C    . VAL A 1 329 ? 116.258 143.630 140.952 1.00 32.30  ? 329  VAL B C    1 
ATOM   2259 O O    . VAL A 1 329 ? 116.228 144.377 141.938 1.00 42.32  ? 329  VAL B O    1 
ATOM   2260 C CB   . VAL A 1 329 ? 114.743 144.094 138.973 1.00 25.60  ? 329  VAL B CB   1 
ATOM   2261 C CG1  . VAL A 1 329 ? 113.794 144.970 139.769 1.00 19.52  ? 329  VAL B CG1  1 
ATOM   2262 C CG2  . VAL A 1 329 ? 114.727 144.490 137.510 1.00 27.79  ? 329  VAL B CG2  1 
ATOM   2263 N N    . ALA A 1 330 ? 116.348 142.302 141.076 1.00 34.21  ? 330  ALA B N    1 
ATOM   2264 C CA   . ALA A 1 330 ? 116.551 141.689 142.387 1.00 31.94  ? 330  ALA B CA   1 
ATOM   2265 C C    . ALA A 1 330 ? 117.871 142.101 143.033 1.00 39.79  ? 330  ALA B C    1 
ATOM   2266 O O    . ALA A 1 330 ? 117.950 142.188 144.264 1.00 40.63  ? 330  ALA B O    1 
ATOM   2267 C CB   . ALA A 1 330 ? 116.481 140.167 142.266 1.00 31.63  ? 330  ALA B CB   1 
ATOM   2268 N N    . ILE A 1 331 ? 118.917 142.332 142.235 1.00 43.29  ? 331  ILE B N    1 
ATOM   2269 C CA   . ILE A 1 331 ? 120.172 142.852 142.778 1.00 37.01  ? 331  ILE B CA   1 
ATOM   2270 C C    . ILE A 1 331 ? 119.952 144.225 143.403 1.00 34.41  ? 331  ILE B C    1 
ATOM   2271 O O    . ILE A 1 331 ? 120.470 144.526 144.486 1.00 40.52  ? 331  ILE B O    1 
ATOM   2272 C CB   . ILE A 1 331 ? 121.261 142.876 141.689 1.00 44.97  ? 331  ILE B CB   1 
ATOM   2273 C CG1  . ILE A 1 331 ? 121.592 141.449 141.245 1.00 40.27  ? 331  ILE B CG1  1 
ATOM   2274 C CG2  . ILE A 1 331 ? 122.517 143.567 142.191 1.00 43.77  ? 331  ILE B CG2  1 
ATOM   2275 C CD1  . ILE A 1 331 ? 122.419 141.374 139.982 1.00 40.81  ? 331  ILE B CD1  1 
ATOM   2276 N N    . PHE A 1 332 ? 119.173 145.076 142.729 1.00 40.74  ? 332  PHE B N    1 
ATOM   2277 C CA   . PHE A 1 332 ? 118.842 146.398 143.260 1.00 46.87  ? 332  PHE B CA   1 
ATOM   2278 C C    . PHE A 1 332 ? 118.041 146.290 144.551 1.00 47.31  ? 332  PHE B C    1 
ATOM   2279 O O    . PHE A 1 332 ? 118.232 147.082 145.481 1.00 47.27  ? 332  PHE B O    1 
ATOM   2280 C CB   . PHE A 1 332 ? 118.056 147.217 142.227 1.00 42.40  ? 332  PHE B CB   1 
ATOM   2281 C CG   . PHE A 1 332 ? 118.833 147.602 140.980 1.00 45.71  ? 332  PHE B CG   1 
ATOM   2282 C CD1  . PHE A 1 332 ? 118.284 148.508 140.088 1.00 37.07  ? 332  PHE B CD1  1 
ATOM   2283 C CD2  . PHE A 1 332 ? 120.110 147.119 140.722 1.00 53.52  ? 332  PHE B CD2  1 
ATOM   2284 C CE1  . PHE A 1 332 ? 118.965 148.891 138.949 1.00 40.21  ? 332  PHE B CE1  1 
ATOM   2285 C CE2  . PHE A 1 332 ? 120.796 147.498 139.583 1.00 53.27  ? 332  PHE B CE2  1 
ATOM   2286 C CZ   . PHE A 1 332 ? 120.223 148.388 138.698 1.00 46.88  ? 332  PHE B CZ   1 
ATOM   2287 N N    . ALA A 1 333 ? 117.104 145.343 144.609 1.00 51.82  ? 333  ALA B N    1 
ATOM   2288 C CA   . ALA A 1 333 ? 116.333 145.126 145.828 1.00 44.14  ? 333  ALA B CA   1 
ATOM   2289 C C    . ALA A 1 333 ? 117.209 144.641 146.980 1.00 49.67  ? 333  ALA B C    1 
ATOM   2290 O O    . ALA A 1 333 ? 117.024 145.074 148.124 1.00 55.28  ? 333  ALA B O    1 
ATOM   2291 C CB   . ALA A 1 333 ? 115.206 144.131 145.561 1.00 44.46  ? 333  ALA B CB   1 
ATOM   2292 N N    . THR A 1 334 ? 118.149 143.728 146.708 1.00 59.08  ? 334  THR B N    1 
ATOM   2293 C CA   . THR A 1 334 ? 119.022 143.226 147.768 1.00 62.20  ? 334  THR B CA   1 
ATOM   2294 C C    . THR A 1 334 ? 119.905 144.325 148.349 1.00 56.21  ? 334  THR B C    1 
ATOM   2295 O O    . THR A 1 334 ? 120.041 144.437 149.575 1.00 49.66  ? 334  THR B O    1 
ATOM   2296 C CB   . THR A 1 334 ? 119.872 142.070 147.228 1.00 63.73  ? 334  THR B CB   1 
ATOM   2297 O OG1  . THR A 1 334 ? 119.099 140.863 147.239 1.00 58.67  ? 334  THR B OG1  1 
ATOM   2298 C CG2  . THR A 1 334 ? 121.130 141.860 148.063 1.00 60.09  ? 334  THR B CG2  1 
ATOM   2299 N N    . GLN A 1 335 ? 120.496 145.157 147.493 1.00 67.94  ? 335  GLN B N    1 
ATOM   2300 C CA   . GLN A 1 335 ? 121.317 146.276 147.948 1.00 70.77  ? 335  GLN B CA   1 
ATOM   2301 C C    . GLN A 1 335 ? 120.516 147.289 148.770 1.00 73.33  ? 335  GLN B C    1 
ATOM   2302 O O    . GLN A 1 335 ? 121.005 147.783 149.791 1.00 77.61  ? 335  GLN B O    1 
ATOM   2303 C CB   . GLN A 1 335 ? 122.058 146.932 146.769 1.00 71.12  ? 335  GLN B CB   1 
ATOM   2304 C CG   . GLN A 1 335 ? 121.269 147.823 145.836 1.00 71.67  ? 335  GLN B CG   1 
ATOM   2305 C CD   . GLN A 1 335 ? 122.164 148.751 145.040 1.00 78.60  ? 335  GLN B CD   1 
ATOM   2306 O OE1  . GLN A 1 335 ? 121.910 149.951 144.947 1.00 78.91  ? 335  GLN B OE1  1 
ATOM   2307 N NE2  . GLN A 1 335 ? 123.224 148.196 144.462 1.00 75.95  ? 335  GLN B NE2  1 
ATOM   2308 N N    . PHE A 1 336 ? 119.287 147.614 148.346 1.00 76.74  ? 336  PHE B N    1 
ATOM   2309 C CA   . PHE A 1 336 ? 118.499 148.554 149.136 1.00 76.26  ? 336  PHE B CA   1 
ATOM   2310 C C    . PHE A 1 336 ? 117.845 147.923 150.364 1.00 74.46  ? 336  PHE B C    1 
ATOM   2311 O O    . PHE A 1 336 ? 117.455 148.659 151.277 1.00 70.57  ? 336  PHE B O    1 
ATOM   2312 C CB   . PHE A 1 336 ? 117.426 149.175 148.238 1.00 74.04  ? 336  PHE B CB   1 
ATOM   2313 C CG   . PHE A 1 336 ? 117.798 150.522 147.692 1.00 73.88  ? 336  PHE B CG   1 
ATOM   2314 C CD1  . PHE A 1 336 ? 118.996 150.702 147.020 1.00 74.73  ? 336  PHE B CD1  1 
ATOM   2315 C CD2  . PHE A 1 336 ? 116.947 151.603 147.834 1.00 72.47  ? 336  PHE B CD2  1 
ATOM   2316 C CE1  . PHE A 1 336 ? 119.343 151.938 146.511 1.00 77.17  ? 336  PHE B CE1  1 
ATOM   2317 C CE2  . PHE A 1 336 ? 117.286 152.842 147.326 1.00 73.85  ? 336  PHE B CE2  1 
ATOM   2318 C CZ   . PHE A 1 336 ? 118.486 153.010 146.663 1.00 77.39  ? 336  PHE B CZ   1 
ATOM   2319 N N    . ASN A 1 337 ? 117.734 146.593 150.417 1.00 80.51  ? 337  ASN B N    1 
ATOM   2320 C CA   . ASN A 1 337 ? 117.085 145.869 151.522 1.00 80.78  ? 337  ASN B CA   1 
ATOM   2321 C C    . ASN A 1 337 ? 115.689 146.395 151.884 1.00 81.93  ? 337  ASN B C    1 
ATOM   2322 O O    . ASN A 1 337 ? 115.477 146.896 152.990 1.00 83.44  ? 337  ASN B O    1 
ATOM   2323 C CB   . ASN A 1 337 ? 117.989 145.874 152.758 1.00 82.14  ? 337  ASN B CB   1 
ATOM   2324 C CG   . ASN A 1 337 ? 118.463 144.487 153.140 1.00 83.63  ? 337  ASN B CG   1 
ATOM   2325 O OD1  . ASN A 1 337 ? 117.790 143.492 152.871 1.00 82.73  ? 337  ASN B OD1  1 
ATOM   2326 N ND2  . ASN A 1 337 ? 119.625 144.414 153.779 1.00 84.70  ? 337  ASN B ND2  1 
ATOM   2327 N N    . MET A 1 338 ? 114.722 146.296 150.968 1.00 71.10  ? 338  MET B N    1 
ATOM   2328 C CA   . MET A 1 338 ? 113.387 146.811 151.272 1.00 72.00  ? 338  MET B CA   1 
ATOM   2329 C C    . MET A 1 338 ? 112.258 146.047 150.583 1.00 76.20  ? 338  MET B C    1 
ATOM   2330 O O    . MET A 1 338 ? 111.152 145.977 151.121 1.00 80.39  ? 338  MET B O    1 
ATOM   2331 C CB   . MET A 1 338 ? 113.363 148.297 150.886 1.00 69.56  ? 338  MET B CB   1 
ATOM   2332 C CG   . MET A 1 338 ? 112.066 149.085 151.119 1.00 70.29  ? 338  MET B CG   1 
ATOM   2333 S SD   . MET A 1 338 ? 111.114 148.649 152.591 1.00 75.11  ? 338  MET B SD   1 
ATOM   2334 C CE   . MET A 1 338 ? 109.445 148.662 151.941 1.00 70.78  ? 338  MET B CE   1 
ATOM   2335 N N    . GLU A 1 339 ? 112.503 145.403 149.446 1.00 61.88  ? 339  GLU B N    1 
ATOM   2336 C CA   . GLU A 1 339 ? 111.462 144.618 148.774 1.00 56.71  ? 339  GLU B CA   1 
ATOM   2337 C C    . GLU A 1 339 ? 112.023 143.331 148.187 1.00 56.70  ? 339  GLU B C    1 
ATOM   2338 O O    . GLU A 1 339 ? 111.621 142.891 147.109 1.00 52.55  ? 339  GLU B O    1 
ATOM   2339 C CB   . GLU A 1 339 ? 110.761 145.451 147.707 1.00 54.84  ? 339  GLU B CB   1 
ATOM   2340 C CG   . GLU A 1 339 ? 109.619 146.288 148.260 1.00 56.14  ? 339  GLU B CG   1 
ATOM   2341 C CD   . GLU A 1 339 ? 108.505 146.487 147.262 1.00 58.62  ? 339  GLU B CD   1 
ATOM   2342 O OE1  . GLU A 1 339 ? 108.814 146.681 146.069 1.00 64.09  ? 339  GLU B OE1  1 
ATOM   2343 O OE2  . GLU A 1 339 ? 107.324 146.448 147.667 1.00 55.04  ? 339  GLU B OE2  1 
ATOM   2344 N N    . VAL A 1 340 ? 112.961 142.702 148.894 1.00 54.32  ? 340  VAL B N    1 
ATOM   2345 C CA   . VAL A 1 340 ? 113.606 141.492 148.381 1.00 49.47  ? 340  VAL B CA   1 
ATOM   2346 C C    . VAL A 1 340 ? 112.615 140.344 148.209 1.00 45.87  ? 340  VAL B C    1 
ATOM   2347 O O    . VAL A 1 340 ? 112.663 139.616 147.213 1.00 46.44  ? 340  VAL B O    1 
ATOM   2348 C CB   . VAL A 1 340 ? 114.767 141.077 149.301 1.00 50.14  ? 340  VAL B CB   1 
ATOM   2349 C CG1  . VAL A 1 340 ? 115.974 141.908 149.006 1.00 52.70  ? 340  VAL B CG1  1 
ATOM   2350 C CG2  . VAL A 1 340 ? 114.377 141.242 150.761 1.00 51.52  ? 340  VAL B CG2  1 
ATOM   2351 N N    . GLU A 1 341 ? 111.713 140.148 149.173 1.00 46.41  ? 341  GLU B N    1 
ATOM   2352 C CA   . GLU A 1 341 ? 110.794 139.013 149.091 1.00 50.02  ? 341  GLU B CA   1 
ATOM   2353 C C    . GLU A 1 341 ? 109.845 139.087 147.889 1.00 51.23  ? 341  GLU B C    1 
ATOM   2354 O O    . GLU A 1 341 ? 109.634 138.089 147.192 1.00 49.17  ? 341  GLU B O    1 
ATOM   2355 C CB   . GLU A 1 341 ? 110.009 138.867 150.407 1.00 49.51  ? 341  GLU B CB   1 
ATOM   2356 C CG   . GLU A 1 341 ? 109.105 140.032 150.841 1.00 55.71  ? 341  GLU B CG   1 
ATOM   2357 C CD   . GLU A 1 341 ? 109.850 141.240 151.393 1.00 58.69  ? 341  GLU B CD   1 
ATOM   2358 O OE1  . GLU A 1 341 ? 109.180 142.145 151.932 1.00 57.39  ? 341  GLU B OE1  1 
ATOM   2359 O OE2  . GLU A 1 341 ? 111.095 141.285 151.310 1.00 53.46  ? 341  GLU B OE2  1 
ATOM   2360 N N    . ILE A 1 342 ? 109.252 140.258 147.635 1.00 46.26  ? 342  ILE B N    1 
ATOM   2361 C CA   . ILE A 1 342 ? 108.300 140.389 146.529 1.00 36.92  ? 342  ILE B CA   1 
ATOM   2362 C C    . ILE A 1 342 ? 108.992 140.335 145.167 1.00 39.53  ? 342  ILE B C    1 
ATOM   2363 O O    . ILE A 1 342 ? 108.557 139.614 144.261 1.00 49.55  ? 342  ILE B O    1 
ATOM   2364 C CB   . ILE A 1 342 ? 107.469 141.674 146.690 1.00 41.15  ? 342  ILE B CB   1 
ATOM   2365 C CG1  . ILE A 1 342 ? 106.822 141.714 148.074 1.00 39.17  ? 342  ILE B CG1  1 
ATOM   2366 C CG2  . ILE A 1 342 ? 106.403 141.754 145.617 1.00 40.18  ? 342  ILE B CG2  1 
ATOM   2367 C CD1  . ILE A 1 342 ? 107.192 142.929 148.886 1.00 42.21  ? 342  ILE B CD1  1 
ATOM   2368 N N    . ILE A 1 343 ? 110.074 141.101 144.999 1.00 30.97  ? 343  ILE B N    1 
ATOM   2369 C CA   . ILE A 1 343 ? 110.749 141.196 143.701 1.00 32.28  ? 343  ILE B CA   1 
ATOM   2370 C C    . ILE A 1 343 ? 111.421 139.885 143.302 1.00 28.27  ? 343  ILE B C    1 
ATOM   2371 O O    . ILE A 1 343 ? 111.356 139.475 142.137 1.00 21.37  ? 343  ILE B O    1 
ATOM   2372 C CB   . ILE A 1 343 ? 111.743 142.373 143.694 1.00 32.86  ? 343  ILE B CB   1 
ATOM   2373 C CG1  . ILE A 1 343 ? 111.036 143.663 144.110 1.00 31.86  ? 343  ILE B CG1  1 
ATOM   2374 C CG2  . ILE A 1 343 ? 112.372 142.539 142.324 1.00 30.41  ? 343  ILE B CG2  1 
ATOM   2375 C CD1  . ILE A 1 343 ? 110.062 144.185 143.078 1.00 32.16  ? 343  ILE B CD1  1 
ATOM   2376 N N    . THR A 1 344 ? 112.093 139.219 144.244 1.00 30.65  ? 344  THR B N    1 
ATOM   2377 C CA   . THR A 1 344 ? 112.697 137.922 143.939 1.00 35.61  ? 344  THR B CA   1 
ATOM   2378 C C    . THR A 1 344 ? 111.654 136.886 143.539 1.00 41.38  ? 344  THR B C    1 
ATOM   2379 O O    . THR A 1 344 ? 111.877 136.114 142.603 1.00 51.71  ? 344  THR B O    1 
ATOM   2380 C CB   . THR A 1 344 ? 113.520 137.414 145.117 1.00 39.93  ? 344  THR B CB   1 
ATOM   2381 O OG1  . THR A 1 344 ? 114.232 138.508 145.708 1.00 44.03  ? 344  THR B OG1  1 
ATOM   2382 C CG2  . THR A 1 344 ? 114.518 136.387 144.632 1.00 41.12  ? 344  THR B CG2  1 
ATOM   2383 N N    . SER A 1 345 ? 110.516 136.848 144.233 1.00 32.98  ? 345  SER B N    1 
ATOM   2384 C CA   . SER A 1 345 ? 109.438 135.942 143.844 1.00 28.42  ? 345  SER B CA   1 
ATOM   2385 C C    . SER A 1 345 ? 108.905 136.286 142.457 1.00 36.15  ? 345  SER B C    1 
ATOM   2386 O O    . SER A 1 345 ? 108.567 135.395 141.670 1.00 39.69  ? 345  SER B O    1 
ATOM   2387 C CB   . SER A 1 345 ? 108.316 135.991 144.879 1.00 29.53  ? 345  SER B CB   1 
ATOM   2388 O OG   . SER A 1 345 ? 108.801 135.661 146.167 1.00 45.05  ? 345  SER B OG   1 
ATOM   2389 N N    . GLY A 1 346 ? 108.802 137.580 142.154 1.00 32.26  ? 346  GLY B N    1 
ATOM   2390 C CA   . GLY A 1 346 ? 108.275 138.002 140.865 1.00 15.38  ? 346  GLY B CA   1 
ATOM   2391 C C    . GLY A 1 346 ? 109.140 137.585 139.688 1.00 21.88  ? 346  GLY B C    1 
ATOM   2392 O O    . GLY A 1 346 ? 108.631 137.120 138.667 1.00 35.66  ? 346  GLY B O    1 
ATOM   2393 N N    . MET A 1 347 ? 110.458 137.773 139.807 1.00 6.43   ? 347  MET B N    1 
ATOM   2394 C CA   . MET A 1 347 ? 111.372 137.443 138.713 1.00 10.93  ? 347  MET B CA   1 
ATOM   2395 C C    . MET A 1 347 ? 111.415 135.942 138.434 1.00 22.16  ? 347  MET B C    1 
ATOM   2396 O O    . MET A 1 347 ? 111.501 135.523 137.273 1.00 21.39  ? 347  MET B O    1 
ATOM   2397 C CB   . MET A 1 347 ? 112.772 137.975 139.029 1.00 19.52  ? 347  MET B CB   1 
ATOM   2398 C CG   . MET A 1 347 ? 113.886 137.416 138.150 1.00 19.41  ? 347  MET B CG   1 
ATOM   2399 S SD   . MET A 1 347 ? 115.457 137.177 138.997 1.00 40.33  ? 347  MET B SD   1 
ATOM   2400 C CE   . MET A 1 347 ? 115.245 135.524 139.644 1.00 23.73  ? 347  MET B CE   1 
ATOM   2401 N N    . VAL A 1 348 ? 111.339 135.117 139.481 1.00 21.87  ? 348  VAL B N    1 
ATOM   2402 C CA   . VAL A 1 348 ? 111.377 133.664 139.307 1.00 12.83  ? 348  VAL B CA   1 
ATOM   2403 C C    . VAL A 1 348 ? 110.142 133.172 138.562 1.00 27.93  ? 348  VAL B C    1 
ATOM   2404 O O    . VAL A 1 348 ? 110.244 132.412 137.593 1.00 43.53  ? 348  VAL B O    1 
ATOM   2405 C CB   . VAL A 1 348 ? 111.515 132.962 140.669 1.00 3.18   ? 348  VAL B CB   1 
ATOM   2406 C CG1  . VAL A 1 348 ? 111.516 131.470 140.481 1.00 17.22  ? 348  VAL B CG1  1 
ATOM   2407 C CG2  . VAL A 1 348 ? 112.794 133.375 141.348 1.00 13.73  ? 348  VAL B CG2  1 
ATOM   2408 N N    . ILE A 1 349 ? 108.961 133.622 138.987 1.00 18.40  ? 349  ILE B N    1 
ATOM   2409 C CA   . ILE A 1 349 ? 107.710 133.208 138.357 1.00 8.32   ? 349  ILE B CA   1 
ATOM   2410 C C    . ILE A 1 349 ? 107.617 133.743 136.932 1.00 14.34  ? 349  ILE B C    1 
ATOM   2411 O O    . ILE A 1 349 ? 107.082 133.072 136.041 1.00 26.12  ? 349  ILE B O    1 
ATOM   2412 C CB   . ILE A 1 349 ? 106.522 133.670 139.225 1.00 7.79   ? 349  ILE B CB   1 
ATOM   2413 C CG1  . ILE A 1 349 ? 106.535 132.949 140.572 1.00 17.32  ? 349  ILE B CG1  1 
ATOM   2414 C CG2  . ILE A 1 349 ? 105.202 133.391 138.542 1.00 20.41  ? 349  ILE B CG2  1 
ATOM   2415 C CD1  . ILE A 1 349 ? 105.684 133.623 141.624 1.00 28.21  ? 349  ILE B CD1  1 
ATOM   2416 N N    . SER A 1 350 ? 108.153 134.941 136.691 1.00 5.22   ? 350  SER B N    1 
ATOM   2417 C CA   . SER A 1 350 ? 108.081 135.563 135.372 1.00 0.00   ? 350  SER B CA   1 
ATOM   2418 C C    . SER A 1 350 ? 108.816 134.751 134.313 1.00 4.95   ? 350  SER B C    1 
ATOM   2419 O O    . SER A 1 350 ? 108.357 134.679 133.168 1.00 33.90  ? 350  SER B O    1 
ATOM   2420 C CB   . SER A 1 350 ? 108.650 136.978 135.429 1.00 9.13   ? 350  SER B CB   1 
ATOM   2421 O OG   . SER A 1 350 ? 107.776 137.845 136.126 1.00 25.05  ? 350  SER B OG   1 
ATOM   2422 N N    . THR A 1 351 ? 109.961 134.160 134.662 1.00 2.74   ? 351  THR B N    1 
ATOM   2423 C CA   . THR A 1 351 ? 110.728 133.366 133.706 1.00 17.32  ? 351  THR B CA   1 
ATOM   2424 C C    . THR A 1 351 ? 109.975 132.133 133.212 1.00 25.02  ? 351  THR B C    1 
ATOM   2425 O O    . THR A 1 351 ? 109.966 131.879 132.004 1.00 32.29  ? 351  THR B O    1 
ATOM   2426 C CB   . THR A 1 351 ? 112.057 132.938 134.334 1.00 5.38   ? 351  THR B CB   1 
ATOM   2427 O OG1  . THR A 1 351 ? 112.785 134.099 134.750 1.00 5.24   ? 351  THR B OG1  1 
ATOM   2428 C CG2  . THR A 1 351 ? 112.897 132.160 133.337 1.00 5.65   ? 351  THR B CG2  1 
ATOM   2429 N N    . PHE A 1 352 ? 109.344 131.369 134.105 1.00 14.73  ? 352  PHE B N    1 
ATOM   2430 C CA   . PHE A 1 352 ? 108.621 130.161 133.714 1.00 19.98  ? 352  PHE B CA   1 
ATOM   2431 C C    . PHE A 1 352 ? 107.440 130.433 132.799 1.00 18.91  ? 352  PHE B C    1 
ATOM   2432 O O    . PHE A 1 352 ? 107.266 129.731 131.799 1.00 29.48  ? 352  PHE B O    1 
ATOM   2433 C CB   . PHE A 1 352 ? 108.120 129.401 134.937 1.00 22.79  ? 352  PHE B CB   1 
ATOM   2434 C CG   . PHE A 1 352 ? 109.168 129.157 135.951 1.00 29.91  ? 352  PHE B CG   1 
ATOM   2435 C CD1  . PHE A 1 352 ? 110.322 128.483 135.609 1.00 33.49  ? 352  PHE B CD1  1 
ATOM   2436 C CD2  . PHE A 1 352 ? 108.990 129.563 137.255 1.00 35.72  ? 352  PHE B CD2  1 
ATOM   2437 C CE1  . PHE A 1 352 ? 111.294 128.255 136.541 1.00 39.60  ? 352  PHE B CE1  1 
ATOM   2438 C CE2  . PHE A 1 352 ? 109.955 129.326 138.194 1.00 38.14  ? 352  PHE B CE2  1 
ATOM   2439 C CZ   . PHE A 1 352 ? 111.108 128.673 137.835 1.00 38.84  ? 352  PHE B CZ   1 
ATOM   2440 N N    . VAL A 1 353 ? 106.610 131.422 133.136 1.00 20.83  ? 353  VAL B N    1 
ATOM   2441 C CA   . VAL A 1 353 ? 105.418 131.693 132.341 1.00 24.24  ? 353  VAL B CA   1 
ATOM   2442 C C    . VAL A 1 353 ? 105.803 132.179 130.949 1.00 22.99  ? 353  VAL B C    1 
ATOM   2443 O O    . VAL A 1 353 ? 105.063 131.966 129.982 1.00 36.40  ? 353  VAL B O    1 
ATOM   2444 C CB   . VAL A 1 353 ? 104.534 132.712 133.095 1.00 22.71  ? 353  VAL B CB   1 
ATOM   2445 C CG1  . VAL A 1 353 ? 103.320 133.133 132.280 1.00 26.00  ? 353  VAL B CG1  1 
ATOM   2446 C CG2  . VAL A 1 353 ? 104.107 132.144 134.438 1.00 27.39  ? 353  VAL B CG2  1 
ATOM   2447 N N    . SER A 1 354 ? 106.970 132.814 130.814 1.00 15.10  ? 354  SER B N    1 
ATOM   2448 C CA   . SER A 1 354 ? 107.362 133.350 129.515 1.00 11.45  ? 354  SER B CA   1 
ATOM   2449 C C    . SER A 1 354 ? 107.646 132.248 128.496 1.00 30.92  ? 354  SER B C    1 
ATOM   2450 O O    . SER A 1 354 ? 107.479 132.472 127.292 1.00 40.85  ? 354  SER B O    1 
ATOM   2451 C CB   . SER A 1 354 ? 108.585 134.249 129.669 1.00 13.90  ? 354  SER B CB   1 
ATOM   2452 O OG   . SER A 1 354 ? 109.778 133.517 129.462 1.00 20.09  ? 354  SER B OG   1 
ATOM   2453 N N    . ALA A 1 355 ? 108.104 131.074 128.952 1.00 17.98  ? 355  ALA B N    1 
ATOM   2454 C CA   . ALA A 1 355 ? 108.460 129.995 128.028 1.00 12.39  ? 355  ALA B CA   1 
ATOM   2455 C C    . ALA A 1 355 ? 107.302 129.516 127.151 1.00 16.96  ? 355  ALA B C    1 
ATOM   2456 O O    . ALA A 1 355 ? 107.482 129.464 125.923 1.00 24.64  ? 355  ALA B O    1 
ATOM   2457 C CB   . ALA A 1 355 ? 109.115 128.843 128.802 1.00 17.82  ? 355  ALA B CB   1 
ATOM   2458 N N    . PRO A 1 356 ? 106.119 129.147 127.676 1.00 12.45  ? 356  PRO B N    1 
ATOM   2459 C CA   . PRO A 1 356 ? 105.037 128.762 126.756 1.00 10.93  ? 356  PRO B CA   1 
ATOM   2460 C C    . PRO A 1 356 ? 104.487 129.935 125.971 1.00 15.21  ? 356  PRO B C    1 
ATOM   2461 O O    . PRO A 1 356 ? 103.960 129.738 124.870 1.00 29.01  ? 356  PRO B O    1 
ATOM   2462 C CB   . PRO A 1 356 ? 103.979 128.153 127.684 1.00 17.93  ? 356  PRO B CB   1 
ATOM   2463 C CG   . PRO A 1 356 ? 104.202 128.808 128.966 1.00 21.54  ? 356  PRO B CG   1 
ATOM   2464 C CD   . PRO A 1 356 ? 105.684 128.977 129.077 1.00 19.56  ? 356  PRO B CD   1 
ATOM   2465 N N    . ILE A 1 357 ? 104.583 131.149 126.517 1.00 19.93  ? 357  ILE B N    1 
ATOM   2466 C CA   . ILE A 1 357 ? 104.004 132.321 125.869 1.00 13.69  ? 357  ILE B CA   1 
ATOM   2467 C C    . ILE A 1 357 ? 104.757 132.646 124.583 1.00 12.65  ? 357  ILE B C    1 
ATOM   2468 O O    . ILE A 1 357 ? 104.146 132.970 123.559 1.00 24.07  ? 357  ILE B O    1 
ATOM   2469 C CB   . ILE A 1 357 ? 103.974 133.511 126.844 1.00 17.61  ? 357  ILE B CB   1 
ATOM   2470 C CG1  . ILE A 1 357 ? 102.943 133.257 127.946 1.00 25.18  ? 357  ILE B CG1  1 
ATOM   2471 C CG2  . ILE A 1 357 ? 103.602 134.786 126.119 1.00 19.46  ? 357  ILE B CG2  1 
ATOM   2472 C CD1  . ILE A 1 357 ? 102.680 134.455 128.833 1.00 16.20  ? 357  ILE B CD1  1 
ATOM   2473 N N    . MET A 1 358 ? 106.090 132.558 124.613 1.00 11.67  ? 358  MET B N    1 
ATOM   2474 C CA   . MET A 1 358 ? 106.893 132.851 123.428 1.00 20.45  ? 358  MET B CA   1 
ATOM   2475 C C    . MET A 1 358 ? 106.602 131.859 122.309 1.00 35.59  ? 358  MET B C    1 
ATOM   2476 O O    . MET A 1 358 ? 106.516 132.233 121.135 1.00 39.27  ? 358  MET B O    1 
ATOM   2477 C CB   . MET A 1 358 ? 108.380 132.810 123.787 1.00 13.98  ? 358  MET B CB   1 
ATOM   2478 C CG   . MET A 1 358 ? 108.898 133.995 124.573 1.00 21.03  ? 358  MET B CG   1 
ATOM   2479 S SD   . MET A 1 358 ? 110.667 134.240 124.330 1.00 52.50  ? 358  MET B SD   1 
ATOM   2480 C CE   . MET A 1 358 ? 111.227 134.447 126.019 1.00 23.51  ? 358  MET B CE   1 
ATOM   2481 N N    . TYR A 1 359 ? 106.454 130.583 122.656 1.00 27.99  ? 359  TYR B N    1 
ATOM   2482 C CA   . TYR A 1 359 ? 106.163 129.543 121.678 1.00 15.75  ? 359  TYR B CA   1 
ATOM   2483 C C    . TYR A 1 359 ? 104.781 129.663 121.046 1.00 27.17  ? 359  TYR B C    1 
ATOM   2484 O O    . TYR A 1 359 ? 104.646 129.581 119.821 1.00 41.12  ? 359  TYR B O    1 
ATOM   2485 C CB   . TYR A 1 359 ? 106.298 128.162 122.322 1.00 21.37  ? 359  TYR B CB   1 
ATOM   2486 C CG   . TYR A 1 359 ? 106.631 127.070 121.335 1.00 22.16  ? 359  TYR B CG   1 
ATOM   2487 C CD1  . TYR A 1 359 ? 107.853 127.045 120.682 1.00 22.30  ? 359  TYR B CD1  1 
ATOM   2488 C CD2  . TYR A 1 359 ? 105.713 126.069 121.047 1.00 25.56  ? 359  TYR B CD2  1 
ATOM   2489 C CE1  . TYR A 1 359 ? 108.156 126.047 119.774 1.00 32.32  ? 359  TYR B CE1  1 
ATOM   2490 C CE2  . TYR A 1 359 ? 106.006 125.068 120.141 1.00 30.80  ? 359  TYR B CE2  1 
ATOM   2491 C CZ   . TYR A 1 359 ? 107.228 125.061 119.508 1.00 34.80  ? 359  TYR B CZ   1 
ATOM   2492 O OH   . TYR A 1 359 ? 107.519 124.063 118.605 1.00 35.95  ? 359  TYR B OH   1 
ATOM   2493 N N    . VAL A 1 360 ? 103.751 129.854 121.874 1.00 22.59  ? 360  VAL B N    1 
ATOM   2494 C CA   . VAL A 1 360 ? 102.381 129.959 121.370 1.00 21.44  ? 360  VAL B CA   1 
ATOM   2495 C C    . VAL A 1 360 ? 102.190 131.222 120.538 1.00 24.92  ? 360  VAL B C    1 
ATOM   2496 O O    . VAL A 1 360 ? 101.590 131.186 119.457 1.00 32.13  ? 360  VAL B O    1 
ATOM   2497 C CB   . VAL A 1 360 ? 101.381 129.898 122.539 1.00 30.22  ? 360  VAL B CB   1 
ATOM   2498 C CG1  . VAL A 1 360 ? 99.978  130.258 122.072 1.00 33.30  ? 360  VAL B CG1  1 
ATOM   2499 C CG2  . VAL A 1 360 ? 101.395 128.517 123.169 1.00 29.07  ? 360  VAL B CG2  1 
ATOM   2500 N N    . SER A 1 361 ? 102.694 132.357 121.028 1.00 30.23  ? 361  SER B N    1 
ATOM   2501 C CA   . SER A 1 361 ? 102.538 133.620 120.309 1.00 33.77  ? 361  SER B CA   1 
ATOM   2502 C C    . SER A 1 361 ? 103.239 133.598 118.955 1.00 31.99  ? 361  SER B C    1 
ATOM   2503 O O    . SER A 1 361 ? 102.733 134.150 117.974 1.00 36.87  ? 361  SER B O    1 
ATOM   2504 C CB   . SER A 1 361 ? 103.065 134.772 121.164 1.00 33.59  ? 361  SER B CB   1 
ATOM   2505 O OG   . SER A 1 361 ? 102.746 134.580 122.531 1.00 38.78  ? 361  SER B OG   1 
ATOM   2506 N N    . ALA A 1 362 ? 104.420 132.979 118.893 1.00 33.12  ? 362  ALA B N    1 
ATOM   2507 C CA   . ALA A 1 362 ? 105.206 132.985 117.662 1.00 32.42  ? 362  ALA B CA   1 
ATOM   2508 C C    . ALA A 1 362 ? 104.482 132.273 116.524 1.00 40.36  ? 362  ALA B C    1 
ATOM   2509 O O    . ALA A 1 362 ? 104.484 132.744 115.381 1.00 52.24  ? 362  ALA B O    1 
ATOM   2510 C CB   . ALA A 1 362 ? 106.573 132.346 117.904 1.00 30.21  ? 362  ALA B CB   1 
ATOM   2511 N N    . TRP A 1 363 ? 103.857 131.130 116.818 1.00 30.32  ? 363  TRP B N    1 
ATOM   2512 C CA   . TRP A 1 363 ? 103.199 130.368 115.762 1.00 26.87  ? 363  TRP B CA   1 
ATOM   2513 C C    . TRP A 1 363 ? 101.810 130.907 115.442 1.00 32.02  ? 363  TRP B C    1 
ATOM   2514 O O    . TRP A 1 363 ? 101.245 130.581 114.393 1.00 37.37  ? 363  TRP B O    1 
ATOM   2515 C CB   . TRP A 1 363 ? 103.082 128.894 116.149 1.00 30.66  ? 363  TRP B CB   1 
ATOM   2516 C CG   . TRP A 1 363 ? 104.339 128.105 116.021 1.00 31.19  ? 363  TRP B CG   1 
ATOM   2517 C CD1  . TRP A 1 363 ? 105.431 128.173 116.830 1.00 33.89  ? 363  TRP B CD1  1 
ATOM   2518 C CD2  . TRP A 1 363 ? 104.670 127.181 114.979 1.00 30.77  ? 363  TRP B CD2  1 
ATOM   2519 N NE1  . TRP A 1 363 ? 106.400 127.307 116.392 1.00 31.13  ? 363  TRP B NE1  1 
ATOM   2520 C CE2  . TRP A 1 363 ? 105.963 126.697 115.247 1.00 32.37  ? 363  TRP B CE2  1 
ATOM   2521 C CE3  . TRP A 1 363 ? 103.992 126.705 113.854 1.00 31.73  ? 363  TRP B CE3  1 
ATOM   2522 C CZ2  . TRP A 1 363 ? 106.593 125.761 114.433 1.00 42.40  ? 363  TRP B CZ2  1 
ATOM   2523 C CZ3  . TRP A 1 363 ? 104.620 125.777 113.046 1.00 33.53  ? 363  TRP B CZ3  1 
ATOM   2524 C CH2  . TRP A 1 363 ? 105.906 125.314 113.340 1.00 42.01  ? 363  TRP B CH2  1 
ATOM   2525 N N    . LEU A 1 364 ? 101.239 131.735 116.318 1.00 40.27  ? 364  LEU B N    1 
ATOM   2526 C CA   . LEU A 1 364 ? 99.954  132.349 115.992 1.00 42.30  ? 364  LEU B CA   1 
ATOM   2527 C C    . LEU A 1 364 ? 100.085 133.497 114.998 1.00 43.36  ? 364  LEU B C    1 
ATOM   2528 O O    . LEU A 1 364 ? 99.190  133.709 114.172 1.00 39.48  ? 364  LEU B O    1 
ATOM   2529 C CB   . LEU A 1 364 ? 99.262  132.830 117.267 1.00 39.57  ? 364  LEU B CB   1 
ATOM   2530 C CG   . LEU A 1 364 ? 98.609  131.742 118.118 1.00 43.63  ? 364  LEU B CG   1 
ATOM   2531 C CD1  . LEU A 1 364 ? 97.860  132.353 119.289 1.00 44.11  ? 364  LEU B CD1  1 
ATOM   2532 C CD2  . LEU A 1 364 ? 97.676  130.897 117.269 1.00 44.55  ? 364  LEU B CD2  1 
ATOM   2533 N N    . LEU A 1 365 ? 101.183 134.252 115.052 1.00 43.83  ? 365  LEU B N    1 
ATOM   2534 C CA   . LEU A 1 365 ? 101.346 135.328 114.079 1.00 41.11  ? 365  LEU B CA   1 
ATOM   2535 C C    . LEU A 1 365 ? 101.732 134.798 112.703 1.00 43.83  ? 365  LEU B C    1 
ATOM   2536 O O    . LEU A 1 365 ? 101.469 135.454 111.690 1.00 52.86  ? 365  LEU B O    1 
ATOM   2537 C CB   . LEU A 1 365 ? 102.378 136.345 114.571 1.00 36.16  ? 365  LEU B CB   1 
ATOM   2538 C CG   . LEU A 1 365 ? 102.397 136.740 116.049 1.00 32.63  ? 365  LEU B CG   1 
ATOM   2539 C CD1  . LEU A 1 365 ? 103.419 137.832 116.286 1.00 40.76  ? 365  LEU B CD1  1 
ATOM   2540 C CD2  . LEU A 1 365 ? 101.025 137.211 116.506 1.00 34.59  ? 365  LEU B CD2  1 
ATOM   2541 N N    . THR A 1 366 ? 102.390 133.637 112.640 1.00 41.53  ? 366  THR B N    1 
ATOM   2542 C CA   . THR A 1 366 ? 102.749 133.082 111.338 1.00 45.53  ? 366  THR B CA   1 
ATOM   2543 C C    . THR A 1 366 ? 101.653 132.171 110.777 1.00 50.67  ? 366  THR B C    1 
ATOM   2544 O O    . THR A 1 366 ? 101.793 131.643 109.667 1.00 52.83  ? 366  THR B O    1 
ATOM   2545 C CB   . THR A 1 366 ? 104.087 132.343 111.447 1.00 41.20  ? 366  THR B CB   1 
ATOM   2546 O OG1  . THR A 1 366 ? 104.981 133.117 112.253 1.00 39.26  ? 366  THR B OG1  1 
ATOM   2547 C CG2  . THR A 1 366 ? 104.745 132.213 110.073 1.00 45.82  ? 366  THR B CG2  1 
ATOM   2548 N N    . PHE A 1 367 ? 100.532 132.005 111.483 1.00 66.73  ? 367  PHE B N    1 
ATOM   2549 C CA   . PHE A 1 367 ? 99.499  131.172 110.868 1.00 66.58  ? 367  PHE B CA   1 
ATOM   2550 C C    . PHE A 1 367 ? 98.670  131.787 109.737 1.00 65.57  ? 367  PHE B C    1 
ATOM   2551 O O    . PHE A 1 367 ? 98.286  131.039 108.829 1.00 65.46  ? 367  PHE B O    1 
ATOM   2552 C CB   . PHE A 1 367 ? 98.538  130.661 111.945 1.00 65.73  ? 367  PHE B CB   1 
ATOM   2553 C CG   . PHE A 1 367 ? 99.022  129.427 112.654 1.00 65.14  ? 367  PHE B CG   1 
ATOM   2554 C CD1  . PHE A 1 367 ? 100.095 128.705 112.158 1.00 63.11  ? 367  PHE B CD1  1 
ATOM   2555 C CD2  . PHE A 1 367 ? 98.409  128.990 113.817 1.00 66.14  ? 367  PHE B CD2  1 
ATOM   2556 C CE1  . PHE A 1 367 ? 100.547 127.572 112.806 1.00 63.05  ? 367  PHE B CE1  1 
ATOM   2557 C CE2  . PHE A 1 367 ? 98.857  127.853 114.470 1.00 65.77  ? 367  PHE B CE2  1 
ATOM   2558 C CZ   . PHE A 1 367 ? 99.928  127.145 113.963 1.00 63.99  ? 367  PHE B CZ   1 
ATOM   2559 N N    . PRO A 1 368 ? 98.345  133.089 109.722 1.00 72.22  ? 368  PRO B N    1 
ATOM   2560 C CA   . PRO A 1 368 ? 97.286  133.518 108.795 1.00 73.76  ? 368  PRO B CA   1 
ATOM   2561 C C    . PRO A 1 368 ? 97.630  133.479 107.299 1.00 75.04  ? 368  PRO B C    1 
ATOM   2562 O O    . PRO A 1 368 ? 96.705  133.515 106.478 1.00 77.20  ? 368  PRO B O    1 
ATOM   2563 C CB   . PRO A 1 368 ? 96.937  134.906 109.351 1.00 74.23  ? 368  PRO B CB   1 
ATOM   2564 C CG   . PRO A 1 368 ? 98.281  135.402 109.976 1.00 73.08  ? 368  PRO B CG   1 
ATOM   2565 C CD   . PRO A 1 368 ? 99.253  134.255 109.758 1.00 73.18  ? 368  PRO B CD   1 
ATOM   2566 N N    . THR A 1 369 ? 98.906  133.404 106.913 1.00 83.01  ? 369  THR B N    1 
ATOM   2567 C CA   . THR A 1 369 ? 99.392  133.747 105.578 1.00 89.08  ? 369  THR B CA   1 
ATOM   2568 C C    . THR A 1 369 ? 100.312 132.606 105.161 1.00 89.73  ? 369  THR B C    1 
ATOM   2569 O O    . THR A 1 369 ? 101.536 132.726 105.243 1.00 89.57  ? 369  THR B O    1 
ATOM   2570 C CB   . THR A 1 369 ? 100.143 135.119 105.546 1.00 90.85  ? 369  THR B CB   1 
ATOM   2571 O OG1  . THR A 1 369 ? 101.468 134.952 106.065 1.00 90.40  ? 369  THR B OG1  1 
ATOM   2572 C CG2  . THR A 1 369 ? 99.412  136.184 106.355 1.00 86.27  ? 369  THR B CG2  1 
ATOM   2573 N N    . MET A 1 370 ? 99.717  131.520 104.679 1.00 92.44  ? 370  MET B N    1 
ATOM   2574 C CA   . MET A 1 370 ? 100.440 130.344 104.202 1.00 92.42  ? 370  MET B CA   1 
ATOM   2575 C C    . MET A 1 370 ? 99.479  129.504 103.370 1.00 95.33  ? 370  MET B C    1 
ATOM   2576 O O    . MET A 1 370 ? 98.375  129.943 103.029 1.00 94.63  ? 370  MET B O    1 
ATOM   2577 C CB   . MET A 1 370 ? 101.023 129.527 105.363 1.00 89.71  ? 370  MET B CB   1 
ATOM   2578 C CG   . MET A 1 370 ? 102.499 129.768 105.651 1.00 93.72  ? 370  MET B CG   1 
ATOM   2579 S SD   . MET A 1 370 ? 103.204 128.559 106.788 1.00 98.19  ? 370  MET B SD   1 
ATOM   2580 C CE   . MET A 1 370 ? 102.025 128.626 108.134 1.00 91.32  ? 370  MET B CE   1 
ATOM   2581 N N    . ASP A 1 371 ? 99.901  128.292 103.046 1.00 106.30 ? 371  ASP B N    1 
ATOM   2582 C CA   . ASP A 1 371 ? 99.159  127.398 102.172 1.00 105.78 ? 371  ASP B CA   1 
ATOM   2583 C C    . ASP A 1 371 ? 98.087  126.686 102.983 1.00 105.84 ? 371  ASP B C    1 
ATOM   2584 O O    . ASP A 1 371 ? 98.047  126.788 104.212 1.00 107.65 ? 371  ASP B O    1 
ATOM   2585 C CB   . ASP A 1 371 ? 100.137 126.423 101.519 1.00 104.59 ? 371  ASP B CB   1 
ATOM   2586 C CG   . ASP A 1 371 ? 99.732  126.008 100.115 1.00 104.82 ? 371  ASP B CG   1 
ATOM   2587 O OD1  . ASP A 1 371 ? 98.881  125.108 99.968  1.00 106.25 ? 371  ASP B OD1  1 
ATOM   2588 O OD2  . ASP A 1 371 ? 100.272 126.588 99.150  1.00 103.43 ? 371  ASP B OD2  1 
ATOM   2589 N N    . PRO A 1 372 ? 97.188  125.946 102.335 1.00 103.99 ? 372  PRO B N    1 
ATOM   2590 C CA   . PRO A 1 372 ? 96.420  124.933 103.073 1.00 102.84 ? 372  PRO B CA   1 
ATOM   2591 C C    . PRO A 1 372 ? 97.247  123.812 103.688 1.00 101.68 ? 372  PRO B C    1 
ATOM   2592 O O    . PRO A 1 372 ? 97.187  123.617 104.906 1.00 100.79 ? 372  PRO B O    1 
ATOM   2593 C CB   . PRO A 1 372 ? 95.468  124.380 102.005 1.00 101.91 ? 372  PRO B CB   1 
ATOM   2594 C CG   . PRO A 1 372 ? 95.332  125.475 100.986 1.00 102.45 ? 372  PRO B CG   1 
ATOM   2595 C CD   . PRO A 1 372 ? 96.408  126.503 101.216 1.00 102.96 ? 372  PRO B CD   1 
ATOM   2596 N N    . LYS A 1 373 ? 98.009  123.064 102.889 1.00 102.38 ? 373  LYS B N    1 
ATOM   2597 C CA   . LYS A 1 373 ? 98.528  121.809 103.427 1.00 103.89 ? 373  LYS B CA   1 
ATOM   2598 C C    . LYS A 1 373 ? 99.777  122.019 104.289 1.00 103.96 ? 373  LYS B C    1 
ATOM   2599 O O    . LYS A 1 373 ? 99.899  121.353 105.323 1.00 104.88 ? 373  LYS B O    1 
ATOM   2600 C CB   . LYS A 1 373 ? 98.795  120.792 102.309 1.00 103.64 ? 373  LYS B CB   1 
ATOM   2601 C CG   . LYS A 1 373 ? 97.882  120.913 101.105 1.00 104.68 ? 373  LYS B CG   1 
ATOM   2602 C CD   . LYS A 1 373 ? 98.375  120.025 99.974  1.00 103.63 ? 373  LYS B CD   1 
ATOM   2603 C CE   . LYS A 1 373 ? 97.712  120.379 98.655  1.00 101.44 ? 373  LYS B CE   1 
ATOM   2604 N NZ   . LYS A 1 373 ? 97.557  119.182 97.783  1.00 101.48 ? 373  LYS B NZ   1 
ATOM   2605 N N    . PRO A 1 374 ? 100.754 122.858 103.895 1.00 101.98 ? 374  PRO B N    1 
ATOM   2606 C CA   . PRO A 1 374 ? 101.770 123.295 104.871 1.00 103.04 ? 374  PRO B CA   1 
ATOM   2607 C C    . PRO A 1 374 ? 101.256 123.760 106.231 1.00 101.51 ? 374  PRO B C    1 
ATOM   2608 O O    . PRO A 1 374 ? 102.004 123.647 107.211 1.00 100.71 ? 374  PRO B O    1 
ATOM   2609 C CB   . PRO A 1 374 ? 102.475 124.431 104.125 1.00 100.75 ? 374  PRO B CB   1 
ATOM   2610 C CG   . PRO A 1 374 ? 102.495 123.952 102.737 1.00 100.28 ? 374  PRO B CG   1 
ATOM   2611 C CD   . PRO A 1 374 ? 101.195 123.199 102.526 1.00 99.89  ? 374  PRO B CD   1 
ATOM   2612 N N    . LEU A 1 375 ? 100.032 124.294 106.340 1.00 95.30  ? 375  LEU B N    1 
ATOM   2613 C CA   . LEU A 1 375 ? 99.484  124.515 107.676 1.00 96.59  ? 375  LEU B CA   1 
ATOM   2614 C C    . LEU A 1 375 ? 99.277  123.216 108.448 1.00 98.85  ? 375  LEU B C    1 
ATOM   2615 O O    . LEU A 1 375 ? 99.324  123.232 109.683 1.00 97.04  ? 375  LEU B O    1 
ATOM   2616 C CB   . LEU A 1 375 ? 98.161  125.277 107.586 1.00 95.80  ? 375  LEU B CB   1 
ATOM   2617 C CG   . LEU A 1 375 ? 98.211  126.798 107.732 1.00 97.86  ? 375  LEU B CG   1 
ATOM   2618 C CD1  . LEU A 1 375 ? 96.849  127.404 107.436 1.00 96.82  ? 375  LEU B CD1  1 
ATOM   2619 C CD2  . LEU A 1 375 ? 98.677  127.183 109.125 1.00 96.53  ? 375  LEU B CD2  1 
ATOM   2620 N N    . ALA A 1 376 ? 98.991  122.104 107.758 1.00 91.94  ? 376  ALA B N    1 
ATOM   2621 C CA   . ALA A 1 376 ? 98.669  120.870 108.473 1.00 88.87  ? 376  ALA B CA   1 
ATOM   2622 C C    . ALA A 1 376 ? 99.861  120.398 109.295 1.00 86.88  ? 376  ALA B C    1 
ATOM   2623 O O    . ALA A 1 376 ? 99.710  119.954 110.439 1.00 87.79  ? 376  ALA B O    1 
ATOM   2624 C CB   . ALA A 1 376 ? 98.215  119.782 107.501 1.00 87.18  ? 376  ALA B CB   1 
ATOM   2625 N N    . TYR A 1 377 ? 101.054 120.480 108.699 1.00 78.64  ? 377  TYR B N    1 
ATOM   2626 C CA   . TYR A 1 377 ? 102.302 120.124 109.366 1.00 84.13  ? 377  TYR B CA   1 
ATOM   2627 C C    . TYR A 1 377 ? 102.567 120.987 110.592 1.00 84.97  ? 377  TYR B C    1 
ATOM   2628 O O    . TYR A 1 377 ? 103.177 120.519 111.559 1.00 87.55  ? 377  TYR B O    1 
ATOM   2629 C CB   . TYR A 1 377 ? 103.472 120.236 108.382 1.00 82.78  ? 377  TYR B CB   1 
ATOM   2630 C CG   . TYR A 1 377 ? 103.567 119.134 107.335 1.00 82.30  ? 377  TYR B CG   1 
ATOM   2631 C CD1  . TYR A 1 377 ? 102.465 118.353 106.997 1.00 82.86  ? 377  TYR B CD1  1 
ATOM   2632 C CD2  . TYR A 1 377 ? 104.764 118.887 106.676 1.00 84.05  ? 377  TYR B CD2  1 
ATOM   2633 C CE1  . TYR A 1 377 ? 102.555 117.359 106.042 1.00 84.71  ? 377  TYR B CE1  1 
ATOM   2634 C CE2  . TYR A 1 377 ? 104.863 117.893 105.718 1.00 87.35  ? 377  TYR B CE2  1 
ATOM   2635 C CZ   . TYR A 1 377 ? 103.756 117.133 105.406 1.00 88.15  ? 377  TYR B CZ   1 
ATOM   2636 O OH   . TYR A 1 377 ? 103.849 116.143 104.456 1.00 85.70  ? 377  TYR B OH   1 
ATOM   2637 N N    . ALA A 1 378 ? 102.122 122.246 110.563 1.00 73.88  ? 378  ALA B N    1 
ATOM   2638 C CA   . ALA A 1 378 ? 102.289 123.149 111.700 1.00 73.03  ? 378  ALA B CA   1 
ATOM   2639 C C    . ALA A 1 378 ? 101.595 122.633 112.955 1.00 75.47  ? 378  ALA B C    1 
ATOM   2640 O O    . ALA A 1 378 ? 102.188 122.623 114.040 1.00 78.86  ? 378  ALA B O    1 
ATOM   2641 C CB   . ALA A 1 378 ? 101.773 124.540 111.336 1.00 74.80  ? 378  ALA B CB   1 
ATOM   2642 N N    . ILE A 1 379 ? 100.331 122.223 112.835 1.00 73.67  ? 379  ILE B N    1 
ATOM   2643 C CA   . ILE A 1 379 ? 99.627  121.661 113.985 1.00 74.20  ? 379  ILE B CA   1 
ATOM   2644 C C    . ILE A 1 379 ? 100.282 120.360 114.437 1.00 72.25  ? 379  ILE B C    1 
ATOM   2645 O O    . ILE A 1 379 ? 100.444 120.116 115.640 1.00 70.29  ? 379  ILE B O    1 
ATOM   2646 C CB   . ILE A 1 379 ? 98.137  121.465 113.645 1.00 72.75  ? 379  ILE B CB   1 
ATOM   2647 C CG1  . ILE A 1 379 ? 97.427  122.816 113.574 1.00 71.30  ? 379  ILE B CG1  1 
ATOM   2648 C CG2  . ILE A 1 379 ? 97.448  120.575 114.668 1.00 71.61  ? 379  ILE B CG2  1 
ATOM   2649 C CD1  . ILE A 1 379 ? 97.117  123.264 112.166 1.00 72.33  ? 379  ILE B CD1  1 
ATOM   2650 N N    . GLN A 1 380 ? 100.677 119.508 113.486 1.00 69.56  ? 380  GLN B N    1 
ATOM   2651 C CA   . GLN A 1 380 ? 101.352 118.264 113.845 1.00 68.40  ? 380  GLN B CA   1 
ATOM   2652 C C    . GLN A 1 380 ? 102.691 118.523 114.529 1.00 68.68  ? 380  GLN B C    1 
ATOM   2653 O O    . GLN A 1 380 ? 103.019 117.873 115.528 1.00 75.05  ? 380  GLN B O    1 
ATOM   2654 C CB   . GLN A 1 380 ? 101.543 117.397 112.602 1.00 66.81  ? 380  GLN B CB   1 
ATOM   2655 C CG   . GLN A 1 380 ? 100.246 116.899 111.979 1.00 68.38  ? 380  GLN B CG   1 
ATOM   2656 C CD   . GLN A 1 380 ? 99.199  116.523 113.010 1.00 74.29  ? 380  GLN B CD   1 
ATOM   2657 O OE1  . GLN A 1 380 ? 98.292  117.302 113.306 1.00 75.49  ? 380  GLN B OE1  1 
ATOM   2658 N NE2  . GLN A 1 380 ? 99.318  115.321 113.561 1.00 75.90  ? 380  GLN B NE2  1 
ATOM   2659 N N    . ASN A 1 381 ? 103.486 119.455 113.992 1.00 65.31  ? 381  ASN B N    1 
ATOM   2660 C CA   . ASN A 1 381 ? 104.813 119.722 114.544 1.00 68.61  ? 381  ASN B CA   1 
ATOM   2661 C C    . ASN A 1 381 ? 104.739 120.309 115.948 1.00 71.46  ? 381  ASN B C    1 
ATOM   2662 O O    . ASN A 1 381 ? 105.515 119.920 116.829 1.00 80.93  ? 381  ASN B O    1 
ATOM   2663 C CB   . ASN A 1 381 ? 105.597 120.653 113.620 1.00 68.06  ? 381  ASN B CB   1 
ATOM   2664 C CG   . ASN A 1 381 ? 106.188 119.927 112.428 1.00 70.67  ? 381  ASN B CG   1 
ATOM   2665 O OD1  . ASN A 1 381 ? 105.808 118.797 112.124 1.00 70.43  ? 381  ASN B OD1  1 
ATOM   2666 N ND2  . ASN A 1 381 ? 107.124 120.576 111.746 1.00 74.29  ? 381  ASN B ND2  1 
ATOM   2667 N N    . VAL A 1 382 ? 103.832 121.265 116.166 1.00 52.54  ? 382  VAL B N    1 
ATOM   2668 C CA   . VAL A 1 382 ? 103.679 121.877 117.485 1.00 51.77  ? 382  VAL B CA   1 
ATOM   2669 C C    . VAL A 1 382 ? 103.238 120.846 118.517 1.00 60.73  ? 382  VAL B C    1 
ATOM   2670 O O    . VAL A 1 382 ? 103.757 120.812 119.640 1.00 60.51  ? 382  VAL B O    1 
ATOM   2671 C CB   . VAL A 1 382 ? 102.698 123.060 117.403 1.00 56.26  ? 382  VAL B CB   1 
ATOM   2672 C CG1  . VAL A 1 382 ? 102.151 123.403 118.775 1.00 61.65  ? 382  VAL B CG1  1 
ATOM   2673 C CG2  . VAL A 1 382 ? 103.381 124.259 116.780 1.00 60.41  ? 382  VAL B CG2  1 
ATOM   2674 N N    . SER A 1 383 ? 102.280 119.988 118.156 1.00 61.94  ? 383  SER B N    1 
ATOM   2675 C CA   . SER A 1 383 ? 101.849 118.938 119.074 1.00 59.47  ? 383  SER B CA   1 
ATOM   2676 C C    . SER A 1 383 ? 102.989 117.977 119.383 1.00 58.51  ? 383  SER B C    1 
ATOM   2677 O O    . SER A 1 383 ? 103.115 117.496 120.515 1.00 63.16  ? 383  SER B O    1 
ATOM   2678 C CB   . SER A 1 383 ? 100.654 118.187 118.490 1.00 58.41  ? 383  SER B CB   1 
ATOM   2679 O OG   . SER A 1 383 ? 99.560  119.061 118.274 1.00 55.13  ? 383  SER B OG   1 
ATOM   2680 N N    . PHE A 1 384 ? 103.812 117.669 118.381 1.00 58.19  ? 384  PHE B N    1 
ATOM   2681 C CA   . PHE A 1 384 ? 104.963 116.797 118.593 1.00 54.59  ? 384  PHE B CA   1 
ATOM   2682 C C    . PHE A 1 384 ? 105.965 117.427 119.559 1.00 57.10  ? 384  PHE B C    1 
ATOM   2683 O O    . PHE A 1 384 ? 106.471 116.759 120.467 1.00 63.64  ? 384  PHE B O    1 
ATOM   2684 C CB   . PHE A 1 384 ? 105.615 116.469 117.248 1.00 56.92  ? 384  PHE B CB   1 
ATOM   2685 C CG   . PHE A 1 384 ? 106.850 115.622 117.356 1.00 59.73  ? 384  PHE B CG   1 
ATOM   2686 C CD1  . PHE A 1 384 ? 106.754 114.245 117.486 1.00 63.13  ? 384  PHE B CD1  1 
ATOM   2687 C CD2  . PHE A 1 384 ? 108.107 116.199 117.315 1.00 64.28  ? 384  PHE B CD2  1 
ATOM   2688 C CE1  . PHE A 1 384 ? 107.891 113.463 117.580 1.00 63.69  ? 384  PHE B CE1  1 
ATOM   2689 C CE2  . PHE A 1 384 ? 109.245 115.424 117.411 1.00 68.72  ? 384  PHE B CE2  1 
ATOM   2690 C CZ   . PHE A 1 384 ? 109.138 114.056 117.543 1.00 66.82  ? 384  PHE B CZ   1 
ATOM   2691 N N    . ASP A 1 385 ? 106.283 118.711 119.360 1.00 52.52  ? 385  ASP B N    1 
ATOM   2692 C CA   . ASP A 1 385 ? 107.278 119.376 120.202 1.00 49.85  ? 385  ASP B CA   1 
ATOM   2693 C C    . ASP A 1 385 ? 106.815 119.497 121.651 1.00 53.63  ? 385  ASP B C    1 
ATOM   2694 O O    . ASP A 1 385 ? 107.611 119.295 122.575 1.00 57.62  ? 385  ASP B O    1 
ATOM   2695 C CB   . ASP A 1 385 ? 107.618 120.748 119.625 1.00 56.37  ? 385  ASP B CB   1 
ATOM   2696 C CG   . ASP A 1 385 ? 108.254 120.660 118.250 1.00 66.45  ? 385  ASP B CG   1 
ATOM   2697 O OD1  . ASP A 1 385 ? 108.961 119.665 117.978 1.00 65.09  ? 385  ASP B OD1  1 
ATOM   2698 O OD2  . ASP A 1 385 ? 108.044 121.583 117.437 1.00 65.34  ? 385  ASP B OD2  1 
ATOM   2699 N N    . ILE A 1 386 ? 105.545 119.852 121.873 1.00 56.18  ? 386  ILE B N    1 
ATOM   2700 C CA   . ILE A 1 386 ? 105.054 120.010 123.241 1.00 57.66  ? 386  ILE B CA   1 
ATOM   2701 C C    . ILE A 1 386 ? 105.067 118.676 123.980 1.00 60.09  ? 386  ILE B C    1 
ATOM   2702 O O    . ILE A 1 386 ? 105.369 118.625 125.180 1.00 59.00  ? 386  ILE B O    1 
ATOM   2703 C CB   . ILE A 1 386 ? 103.651 120.654 123.221 1.00 53.43  ? 386  ILE B CB   1 
ATOM   2704 C CG1  . ILE A 1 386 ? 103.769 122.169 123.087 1.00 54.64  ? 386  ILE B CG1  1 
ATOM   2705 C CG2  . ILE A 1 386 ? 102.835 120.305 124.463 1.00 59.57  ? 386  ILE B CG2  1 
ATOM   2706 C CD1  . ILE A 1 386 ? 102.627 122.794 122.344 1.00 57.39  ? 386  ILE B CD1  1 
ATOM   2707 N N    . SER A 1 387 ? 104.790 117.576 123.273 1.00 61.85  ? 387  SER B N    1 
ATOM   2708 C CA   . SER A 1 387 ? 104.765 116.255 123.895 1.00 56.62  ? 387  SER B CA   1 
ATOM   2709 C C    . SER A 1 387 ? 106.121 115.846 124.459 1.00 54.86  ? 387  SER B C    1 
ATOM   2710 O O    . SER A 1 387 ? 106.178 115.104 125.445 1.00 56.91  ? 387  SER B O    1 
ATOM   2711 C CB   . SER A 1 387 ? 104.286 115.211 122.887 1.00 59.60  ? 387  SER B CB   1 
ATOM   2712 O OG   . SER A 1 387 ? 103.292 115.743 122.031 1.00 59.14  ? 387  SER B OG   1 
ATOM   2713 N N    . ILE A 1 388 ? 107.217 116.288 123.835 1.00 49.78  ? 388  ILE B N    1 
ATOM   2714 C CA   . ILE A 1 388 ? 108.552 115.932 124.318 1.00 46.93  ? 388  ILE B CA   1 
ATOM   2715 C C    . ILE A 1 388 ? 108.793 116.492 125.717 1.00 49.12  ? 388  ILE B C    1 
ATOM   2716 O O    . ILE A 1 388 ? 109.207 115.767 126.628 1.00 57.25  ? 388  ILE B O    1 
ATOM   2717 C CB   . ILE A 1 388 ? 109.626 116.416 123.323 1.00 55.24  ? 388  ILE B CB   1 
ATOM   2718 C CG1  . ILE A 1 388 ? 109.824 115.391 122.205 1.00 56.16  ? 388  ILE B CG1  1 
ATOM   2719 C CG2  . ILE A 1 388 ? 110.959 116.664 124.028 1.00 54.16  ? 388  ILE B CG2  1 
ATOM   2720 C CD1  . ILE A 1 388 ? 110.786 115.834 121.122 1.00 57.54  ? 388  ILE B CD1  1 
ATOM   2721 N N    . VAL A 1 389 ? 108.495 117.777 125.921 1.00 51.11  ? 389  VAL B N    1 
ATOM   2722 C CA   . VAL A 1 389 ? 108.770 118.406 127.210 1.00 50.25  ? 389  VAL B CA   1 
ATOM   2723 C C    . VAL A 1 389 ? 107.831 117.886 128.295 1.00 55.14  ? 389  VAL B C    1 
ATOM   2724 O O    . VAL A 1 389 ? 108.250 117.654 129.435 1.00 61.37  ? 389  VAL B O    1 
ATOM   2725 C CB   . VAL A 1 389 ? 108.683 119.938 127.072 1.00 48.93  ? 389  VAL B CB   1 
ATOM   2726 C CG1  . VAL A 1 389 ? 109.059 120.621 128.377 1.00 46.79  ? 389  VAL B CG1  1 
ATOM   2727 C CG2  . VAL A 1 389 ? 109.572 120.425 125.938 1.00 55.21  ? 389  VAL B CG2  1 
ATOM   2728 N N    . SER A 1 390 ? 106.552 117.700 127.963 1.00 48.23  ? 390  SER B N    1 
ATOM   2729 C CA   . SER A 1 390 ? 105.582 117.206 128.938 1.00 44.27  ? 390  SER B CA   1 
ATOM   2730 C C    . SER A 1 390 ? 105.886 115.788 129.417 1.00 53.94  ? 390  SER B C    1 
ATOM   2731 O O    . SER A 1 390 ? 105.724 115.483 130.604 1.00 57.42  ? 390  SER B O    1 
ATOM   2732 C CB   . SER A 1 390 ? 104.177 117.267 128.340 1.00 50.44  ? 390  SER B CB   1 
ATOM   2733 O OG   . SER A 1 390 ? 103.195 116.943 129.307 1.00 52.28  ? 390  SER B OG   1 
ATOM   2734 N N    . LEU A 1 391 ? 106.300 114.903 128.505 1.00 61.91  ? 391  LEU B N    1 
ATOM   2735 C CA   . LEU A 1 391 ? 106.581 113.516 128.877 1.00 57.55  ? 391  LEU B CA   1 
ATOM   2736 C C    . LEU A 1 391 ? 107.738 113.377 129.865 1.00 56.85  ? 391  LEU B C    1 
ATOM   2737 O O    . LEU A 1 391 ? 107.645 112.606 130.827 1.00 64.61  ? 391  LEU B O    1 
ATOM   2738 C CB   . LEU A 1 391 ? 106.868 112.699 127.618 1.00 54.74  ? 391  LEU B CB   1 
ATOM   2739 C CG   . LEU A 1 391 ? 106.780 111.179 127.749 1.00 58.22  ? 391  LEU B CG   1 
ATOM   2740 C CD1  . LEU A 1 391 ? 105.587 110.778 128.606 1.00 56.81  ? 391  LEU B CD1  1 
ATOM   2741 C CD2  . LEU A 1 391 ? 106.702 110.539 126.378 1.00 61.36  ? 391  LEU B CD2  1 
ATOM   2742 N N    . ILE A 1 392 ? 108.836 114.101 129.645 1.00 42.14  ? 392  ILE B N    1 
ATOM   2743 C CA   . ILE A 1 392 ? 109.979 114.024 130.557 1.00 46.71  ? 392  ILE B CA   1 
ATOM   2744 C C    . ILE A 1 392 ? 109.646 114.615 131.924 1.00 54.57  ? 392  ILE B C    1 
ATOM   2745 O O    . ILE A 1 392 ? 110.048 114.073 132.961 1.00 65.47  ? 392  ILE B O    1 
ATOM   2746 C CB   . ILE A 1 392 ? 111.227 114.684 129.938 1.00 52.93  ? 392  ILE B CB   1 
ATOM   2747 C CG1  . ILE A 1 392 ? 111.386 114.310 128.460 1.00 55.60  ? 392  ILE B CG1  1 
ATOM   2748 C CG2  . ILE A 1 392 ? 112.481 114.280 130.715 1.00 52.82  ? 392  ILE B CG2  1 
ATOM   2749 C CD1  . ILE A 1 392 ? 111.439 112.808 128.191 1.00 52.96  ? 392  ILE B CD1  1 
ATOM   2750 N N    . SER A 1 393 ? 108.927 115.738 131.950 1.00 50.37  ? 393  SER B N    1 
ATOM   2751 C CA   . SER A 1 393 ? 108.520 116.332 133.221 1.00 45.15  ? 393  SER B CA   1 
ATOM   2752 C C    . SER A 1 393 ? 107.589 115.418 134.010 1.00 48.19  ? 393  SER B C    1 
ATOM   2753 O O    . SER A 1 393 ? 107.687 115.343 135.240 1.00 56.97  ? 393  SER B O    1 
ATOM   2754 C CB   . SER A 1 393 ? 107.854 117.685 132.976 1.00 49.42  ? 393  SER B CB   1 
ATOM   2755 O OG   . SER A 1 393 ? 106.445 117.557 132.932 1.00 54.35  ? 393  SER B OG   1 
ATOM   2756 N N    . LEU A 1 394 ? 106.656 114.747 133.331 1.00 51.40  ? 394  LEU B N    1 
ATOM   2757 C CA   . LEU A 1 394 ? 105.740 113.846 134.028 1.00 56.09  ? 394  LEU B CA   1 
ATOM   2758 C C    . LEU A 1 394 ? 106.476 112.672 134.666 1.00 62.83  ? 394  LEU B C    1 
ATOM   2759 O O    . LEU A 1 394 ? 106.120 112.235 135.767 1.00 66.36  ? 394  LEU B O    1 
ATOM   2760 C CB   . LEU A 1 394 ? 104.658 113.353 133.067 1.00 55.57  ? 394  LEU B CB   1 
ATOM   2761 C CG   . LEU A 1 394 ? 103.426 114.254 132.934 1.00 57.74  ? 394  LEU B CG   1 
ATOM   2762 C CD1  . LEU A 1 394 ? 102.226 113.452 132.475 1.00 58.81  ? 394  LEU B CD1  1 
ATOM   2763 C CD2  . LEU A 1 394 ? 103.116 114.957 134.249 1.00 58.89  ? 394  LEU B CD2  1 
ATOM   2764 N N    . ILE A 1 395 ? 107.482 112.128 133.973 1.00 55.95  ? 395  ILE B N    1 
ATOM   2765 C CA   . ILE A 1 395 ? 108.243 110.989 134.490 1.00 54.46  ? 395  ILE B CA   1 
ATOM   2766 C C    . ILE A 1 395 ? 108.943 111.343 135.800 1.00 59.96  ? 395  ILE B C    1 
ATOM   2767 O O    . ILE A 1 395 ? 108.936 110.558 136.757 1.00 62.97  ? 395  ILE B O    1 
ATOM   2768 C CB   . ILE A 1 395 ? 109.238 110.494 133.422 1.00 48.13  ? 395  ILE B CB   1 
ATOM   2769 C CG1  . ILE A 1 395 ? 108.500 109.712 132.332 1.00 53.12  ? 395  ILE B CG1  1 
ATOM   2770 C CG2  . ILE A 1 395 ? 110.339 109.645 134.042 1.00 52.31  ? 395  ILE B CG2  1 
ATOM   2771 C CD1  . ILE A 1 395 ? 109.414 109.045 131.324 1.00 57.59  ? 395  ILE B CD1  1 
ATOM   2772 N N    . TRP A 1 396 ? 109.546 112.534 135.868 1.00 65.74  ? 396  TRP B N    1 
ATOM   2773 C CA   . TRP A 1 396 ? 110.224 112.979 137.085 1.00 59.88  ? 396  TRP B CA   1 
ATOM   2774 C C    . TRP A 1 396 ? 109.250 113.109 138.253 1.00 61.31  ? 396  TRP B C    1 
ATOM   2775 O O    . TRP A 1 396 ? 109.493 112.576 139.341 1.00 71.28  ? 396  TRP B O    1 
ATOM   2776 C CB   . TRP A 1 396 ? 110.936 114.308 136.829 1.00 59.84  ? 396  TRP B CB   1 
ATOM   2777 C CG   . TRP A 1 396 ? 111.604 114.876 138.043 1.00 69.38  ? 396  TRP B CG   1 
ATOM   2778 C CD1  . TRP A 1 396 ? 111.218 115.973 138.754 1.00 69.72  ? 396  TRP B CD1  1 
ATOM   2779 C CD2  . TRP A 1 396 ? 112.792 114.385 138.677 1.00 72.01  ? 396  TRP B CD2  1 
ATOM   2780 N NE1  . TRP A 1 396 ? 112.084 116.190 139.798 1.00 68.92  ? 396  TRP B NE1  1 
ATOM   2781 C CE2  . TRP A 1 396 ? 113.060 115.230 139.772 1.00 65.98  ? 396  TRP B CE2  1 
ATOM   2782 C CE3  . TRP A 1 396 ? 113.652 113.311 138.428 1.00 70.99  ? 396  TRP B CE3  1 
ATOM   2783 C CZ2  . TRP A 1 396 ? 114.151 115.034 140.615 1.00 61.10  ? 396  TRP B CZ2  1 
ATOM   2784 C CZ3  . TRP A 1 396 ? 114.733 113.118 139.266 1.00 70.44  ? 396  TRP B CZ3  1 
ATOM   2785 C CH2  . TRP A 1 396 ? 114.973 113.975 140.347 1.00 65.31  ? 396  TRP B CH2  1 
ATOM   2786 N N    . SER A 1 397 ? 108.149 113.835 138.042 1.00 51.69  ? 397  SER B N    1 
ATOM   2787 C CA   . SER A 1 397 ? 107.174 114.088 139.102 1.00 54.93  ? 397  SER B CA   1 
ATOM   2788 C C    . SER A 1 397 ? 106.538 112.798 139.610 1.00 55.08  ? 397  SER B C    1 
ATOM   2789 O O    . SER A 1 397 ? 106.348 112.624 140.819 1.00 57.96  ? 397  SER B O    1 
ATOM   2790 C CB   . SER A 1 397 ? 106.095 115.046 138.600 1.00 64.08  ? 397  SER B CB   1 
ATOM   2791 O OG   . SER A 1 397 ? 105.159 115.336 139.623 1.00 67.82  ? 397  SER B OG   1 
ATOM   2792 N N    . LEU A 1 398 ? 106.186 111.893 138.697 1.00 54.49  ? 398  LEU B N    1 
ATOM   2793 C CA   . LEU A 1 398 ? 105.578 110.620 139.078 1.00 60.96  ? 398  LEU B CA   1 
ATOM   2794 C C    . LEU A 1 398 ? 106.551 109.731 139.847 1.00 61.50  ? 398  LEU B C    1 
ATOM   2795 O O    . LEU A 1 398 ? 106.156 109.067 140.813 1.00 61.97  ? 398  LEU B O    1 
ATOM   2796 C CB   . LEU A 1 398 ? 105.064 109.901 137.831 1.00 58.11  ? 398  LEU B CB   1 
ATOM   2797 C CG   . LEU A 1 398 ? 104.549 108.470 137.996 1.00 58.26  ? 398  LEU B CG   1 
ATOM   2798 C CD1  . LEU A 1 398 ? 103.351 108.435 138.931 1.00 58.58  ? 398  LEU B CD1  1 
ATOM   2799 C CD2  . LEU A 1 398 ? 104.200 107.871 136.644 1.00 59.37  ? 398  LEU B CD2  1 
ATOM   2800 N N    . ALA A 1 399 ? 107.818 109.691 139.426 1.00 61.05  ? 399  ALA B N    1 
ATOM   2801 C CA   . ALA A 1 399 ? 108.805 108.836 140.082 1.00 59.97  ? 399  ALA B CA   1 
ATOM   2802 C C    . ALA A 1 399 ? 109.035 109.225 141.540 1.00 60.41  ? 399  ALA B C    1 
ATOM   2803 O O    . ALA A 1 399 ? 109.146 108.349 142.405 1.00 65.95  ? 399  ALA B O    1 
ATOM   2804 C CB   . ALA A 1 399 ? 110.125 108.872 139.312 1.00 59.95  ? 399  ALA B CB   1 
ATOM   2805 N N    . ILE A 1 400 ? 109.129 110.525 141.835 1.00 64.83  ? 400  ILE B N    1 
ATOM   2806 C CA   . ILE A 1 400 ? 109.331 110.955 143.219 1.00 65.56  ? 400  ILE B CA   1 
ATOM   2807 C C    . ILE A 1 400 ? 108.133 110.579 144.086 1.00 65.62  ? 400  ILE B C    1 
ATOM   2808 O O    . ILE A 1 400 ? 108.288 110.189 145.250 1.00 65.03  ? 400  ILE B O    1 
ATOM   2809 C CB   . ILE A 1 400 ? 109.611 112.470 143.267 1.00 62.24  ? 400  ILE B CB   1 
ATOM   2810 C CG1  . ILE A 1 400 ? 110.904 112.803 142.521 1.00 64.22  ? 400  ILE B CG1  1 
ATOM   2811 C CG2  . ILE A 1 400 ? 109.683 112.977 144.703 1.00 57.92  ? 400  ILE B CG2  1 
ATOM   2812 C CD1  . ILE A 1 400 ? 111.348 114.239 142.691 1.00 64.29  ? 400  ILE B CD1  1 
ATOM   2813 N N    . LEU A 1 401 ? 106.924 110.674 143.529 1.00 75.88  ? 401  LEU B N    1 
ATOM   2814 C CA   . LEU A 1 401 ? 105.722 110.308 144.276 1.00 77.21  ? 401  LEU B CA   1 
ATOM   2815 C C    . LEU A 1 401 ? 105.717 108.827 144.644 1.00 77.54  ? 401  LEU B C    1 
ATOM   2816 O O    . LEU A 1 401 ? 105.349 108.459 145.766 1.00 77.41  ? 401  LEU B O    1 
ATOM   2817 C CB   . LEU A 1 401 ? 104.477 110.678 143.471 1.00 76.25  ? 401  LEU B CB   1 
ATOM   2818 C CG   . LEU A 1 401 ? 103.962 112.104 143.694 1.00 74.08  ? 401  LEU B CG   1 
ATOM   2819 C CD1  . LEU A 1 401 ? 102.569 112.279 143.120 1.00 75.50  ? 401  LEU B CD1  1 
ATOM   2820 C CD2  . LEU A 1 401 ? 103.974 112.461 145.173 1.00 75.30  ? 401  LEU B CD2  1 
ATOM   2821 N N    . LEU A 1 402 ? 106.111 107.963 143.705 1.00 73.49  ? 402  LEU B N    1 
ATOM   2822 C CA   . LEU A 1 402 ? 106.121 106.522 143.951 1.00 74.50  ? 402  LEU B CA   1 
ATOM   2823 C C    . LEU A 1 402 ? 107.176 106.132 144.984 1.00 82.12  ? 402  LEU B C    1 
ATOM   2824 O O    . LEU A 1 402 ? 106.901 105.352 145.903 1.00 82.35  ? 402  LEU B O    1 
ATOM   2825 C CB   . LEU A 1 402 ? 106.349 105.780 142.633 1.00 72.56  ? 402  LEU B CB   1 
ATOM   2826 C CG   . LEU A 1 402 ? 106.542 104.264 142.676 1.00 76.64  ? 402  LEU B CG   1 
ATOM   2827 C CD1  . LEU A 1 402 ? 105.619 103.589 141.677 1.00 79.67  ? 402  LEU B CD1  1 
ATOM   2828 C CD2  . LEU A 1 402 ? 107.990 103.896 142.393 1.00 72.23  ? 402  LEU B CD2  1 
ATOM   2829 N N    . LEU A 1 403 ? 108.396 106.654 144.833 1.00 87.83  ? 403  LEU B N    1 
ATOM   2830 C CA   . LEU A 1 403 ? 109.494 106.319 145.739 1.00 82.60  ? 403  LEU B CA   1 
ATOM   2831 C C    . LEU A 1 403 ? 109.228 106.780 147.167 1.00 84.70  ? 403  LEU B C    1 
ATOM   2832 O O    . LEU A 1 403 ? 109.579 106.082 148.126 1.00 83.38  ? 403  LEU B O    1 
ATOM   2833 C CB   . LEU A 1 403 ? 110.805 106.919 145.229 1.00 79.43  ? 403  LEU B CB   1 
ATOM   2834 C CG   . LEU A 1 403 ? 111.348 106.399 143.898 1.00 83.39  ? 403  LEU B CG   1 
ATOM   2835 C CD1  . LEU A 1 403 ? 112.761 106.908 143.670 1.00 82.32  ? 403  LEU B CD1  1 
ATOM   2836 C CD2  . LEU A 1 403 ? 111.314 104.881 143.865 1.00 83.13  ? 403  LEU B CD2  1 
ATOM   2837 N N    . SER A 1 404 ? 108.611 107.950 147.333 1.00 94.86  ? 404  SER B N    1 
ATOM   2838 C CA   . SER A 1 404 ? 108.313 108.465 148.665 1.00 92.94  ? 404  SER B CA   1 
ATOM   2839 C C    . SER A 1 404 ? 107.240 107.689 149.421 1.00 92.92  ? 404  SER B C    1 
ATOM   2840 O O    . SER A 1 404 ? 107.060 107.963 150.613 1.00 92.11  ? 404  SER B O    1 
ATOM   2841 C CB   . SER A 1 404 ? 107.889 109.930 148.569 1.00 94.99  ? 404  SER B CB   1 
ATOM   2842 O OG   . SER A 1 404 ? 106.986 110.261 149.609 1.00 96.81  ? 404  SER B OG   1 
ATOM   2843 N N    . LYS A 1 405 ? 106.496 106.785 148.770 1.00 102.68 ? 405  LYS B N    1 
ATOM   2844 C CA   . LYS A 1 405 ? 105.473 105.939 149.396 1.00 103.64 ? 405  LYS B CA   1 
ATOM   2845 C C    . LYS A 1 405 ? 104.285 106.774 149.883 1.00 105.62 ? 405  LYS B C    1 
ATOM   2846 O O    . LYS A 1 405 ? 103.434 106.288 150.640 1.00 106.35 ? 405  LYS B O    1 
ATOM   2847 C CB   . LYS A 1 405 ? 106.086 105.067 150.513 1.00 103.85 ? 405  LYS B CB   1 
ATOM   2848 C CG   . LYS A 1 405 ? 105.227 103.943 151.113 1.00 104.59 ? 405  LYS B CG   1 
ATOM   2849 C CD   . LYS A 1 405 ? 106.031 102.671 151.333 1.00 105.25 ? 405  LYS B CD   1 
ATOM   2850 C CE   . LYS A 1 405 ? 105.214 101.436 150.984 1.00 105.26 ? 405  LYS B CE   1 
ATOM   2851 N NZ   . LYS A 1 405 ? 105.150 101.206 149.516 1.00 106.27 ? 405  LYS B NZ   1 
ATOM   2852 N N    . LYS A 1 406 ? 104.183 108.022 149.435 1.00 107.61 ? 406  LYS B N    1 
ATOM   2853 C CA   . LYS A 1 406 ? 103.079 108.905 149.779 1.00 107.82 ? 406  LYS B CA   1 
ATOM   2854 C C    . LYS A 1 406 ? 101.832 108.634 148.930 1.00 107.34 ? 406  LYS B C    1 
ATOM   2855 O O    . LYS A 1 406 ? 100.766 109.198 149.201 1.00 105.41 ? 406  LYS B O    1 
ATOM   2856 C CB   . LYS A 1 406 ? 103.665 110.318 149.650 1.00 106.10 ? 406  LYS B CB   1 
ATOM   2857 C CG   . LYS A 1 406 ? 102.844 111.568 149.626 1.00 106.56 ? 406  LYS B CG   1 
ATOM   2858 C CD   . LYS A 1 406 ? 103.442 112.457 150.723 1.00 106.39 ? 406  LYS B CD   1 
ATOM   2859 C CE   . LYS A 1 406 ? 102.837 113.833 150.769 1.00 106.95 ? 406  LYS B CE   1 
ATOM   2860 N NZ   . LYS A 1 406 ? 102.625 114.308 149.381 1.00 106.18 ? 406  LYS B NZ   1 
ATOM   2861 N N    . TYR A 1 407 ? 101.959 107.751 147.934 1.00 110.29 ? 407  TYR B N    1 
ATOM   2862 C CA   . TYR A 1 407 ? 100.910 107.291 147.019 1.00 107.97 ? 407  TYR B CA   1 
ATOM   2863 C C    . TYR A 1 407 ? 99.801  106.521 147.745 1.00 109.07 ? 407  TYR B C    1 
ATOM   2864 O O    . TYR A 1 407 ? 98.672  106.453 147.251 1.00 110.91 ? 407  TYR B O    1 
ATOM   2865 C CB   . TYR A 1 407 ? 101.499 106.469 145.863 1.00 106.10 ? 407  TYR B CB   1 
ATOM   2866 C CG   . TYR A 1 407 ? 102.106 105.133 146.214 1.00 105.65 ? 407  TYR B CG   1 
ATOM   2867 C CD1  . TYR A 1 407 ? 103.425 105.033 146.629 1.00 106.43 ? 407  TYR B CD1  1 
ATOM   2868 C CD2  . TYR A 1 407 ? 101.375 103.961 146.066 1.00 107.72 ? 407  TYR B CD2  1 
ATOM   2869 C CE1  . TYR A 1 407 ? 103.986 103.806 146.932 1.00 109.43 ? 407  TYR B CE1  1 
ATOM   2870 C CE2  . TYR A 1 407 ? 101.929 102.732 146.359 1.00 110.71 ? 407  TYR B CE2  1 
ATOM   2871 C CZ   . TYR A 1 407 ? 103.233 102.660 146.797 1.00 112.74 ? 407  TYR B CZ   1 
ATOM   2872 O OH   . TYR A 1 407 ? 103.786 101.437 147.098 1.00 113.35 ? 407  TYR B OH   1 
ATOM   2873 N N    . LYS A 1 408 ? 100.122 105.953 148.909 1.00 105.12 ? 408  LYS B N    1 
ATOM   2874 C CA   . LYS A 1 408 ? 99.324  105.119 149.809 1.00 105.14 ? 408  LYS B CA   1 
ATOM   2875 C C    . LYS A 1 408 ? 98.236  105.825 150.615 1.00 106.86 ? 408  LYS B C    1 
ATOM   2876 O O    . LYS A 1 408 ? 97.473  105.120 151.284 1.00 107.52 ? 408  LYS B O    1 
ATOM   2877 C CB   . LYS A 1 408 ? 100.240 104.374 150.782 1.00 105.10 ? 408  LYS B CB   1 
ATOM   2878 C CG   . LYS A 1 408 ? 101.131 103.355 150.112 1.00 105.73 ? 408  LYS B CG   1 
ATOM   2879 C CD   . LYS A 1 408 ? 100.275 102.342 149.365 1.00 105.43 ? 408  LYS B CD   1 
ATOM   2880 C CE   . LYS A 1 408 ? 100.793 100.925 149.535 1.00 104.85 ? 408  LYS B CE   1 
ATOM   2881 N NZ   . LYS A 1 408 ? 100.003 99.957  148.725 1.00 104.81 ? 408  LYS B NZ   1 
ATOM   2882 N N    . GLN A 1 409 ? 98.105  107.152 150.604 1.00 114.07 ? 409  GLN B N    1 
ATOM   2883 C CA   . GLN A 1 409 ? 97.114  107.697 151.530 1.00 113.66 ? 409  GLN B CA   1 
ATOM   2884 C C    . GLN A 1 409 ? 95.831  108.102 150.803 1.00 113.99 ? 409  GLN B C    1 
ATOM   2885 O O    . GLN A 1 409 ? 95.662  107.772 149.626 1.00 111.25 ? 409  GLN B O    1 
ATOM   2886 C CB   . GLN A 1 409 ? 97.694  108.895 152.284 1.00 112.41 ? 409  GLN B CB   1 
ATOM   2887 C CG   . GLN A 1 409 ? 97.347  108.936 153.766 1.00 112.95 ? 409  GLN B CG   1 
ATOM   2888 C CD   . GLN A 1 409 ? 97.925  110.153 154.463 1.00 114.37 ? 409  GLN B CD   1 
ATOM   2889 O OE1  . GLN A 1 409 ? 98.812  110.822 153.933 1.00 113.67 ? 409  GLN B OE1  1 
ATOM   2890 N NE2  . GLN A 1 409 ? 97.422  110.447 155.656 1.00 113.78 ? 409  GLN B NE2  1 
ATOM   2891 N N    . LEU A 1 410 ? 94.914  108.808 151.480 1.00 116.49 ? 410  LEU B N    1 
ATOM   2892 C CA   . LEU A 1 410 ? 93.663  109.211 150.835 1.00 116.18 ? 410  LEU B CA   1 
ATOM   2893 C C    . LEU A 1 410 ? 93.711  110.234 149.701 1.00 116.62 ? 410  LEU B C    1 
ATOM   2894 O O    . LEU A 1 410 ? 93.188  109.923 148.623 1.00 116.74 ? 410  LEU B O    1 
ATOM   2895 C CB   . LEU A 1 410 ? 92.677  109.697 151.909 1.00 115.46 ? 410  LEU B CB   1 
ATOM   2896 C CG   . LEU A 1 410 ? 91.191  109.663 151.540 1.00 115.12 ? 410  LEU B CG   1 
ATOM   2897 C CD1  . LEU A 1 410 ? 90.840  108.403 150.762 1.00 115.12 ? 410  LEU B CD1  1 
ATOM   2898 C CD2  . LEU A 1 410 ? 90.323  109.787 152.782 1.00 115.61 ? 410  LEU B CD2  1 
ATOM   2899 N N    . PRO A 1 411 ? 94.294  111.430 149.833 1.00 112.88 ? 411  PRO B N    1 
ATOM   2900 C CA   . PRO A 1 411 ? 94.153  112.365 148.705 1.00 111.53 ? 411  PRO B CA   1 
ATOM   2901 C C    . PRO A 1 411 ? 95.239  112.191 147.668 1.00 108.85 ? 411  PRO B C    1 
ATOM   2902 O O    . PRO A 1 411 ? 94.988  112.376 146.471 1.00 107.80 ? 411  PRO B O    1 
ATOM   2903 C CB   . PRO A 1 411 ? 94.236  113.745 149.378 1.00 108.97 ? 411  PRO B CB   1 
ATOM   2904 C CG   . PRO A 1 411 ? 94.427  113.472 150.872 1.00 111.34 ? 411  PRO B CG   1 
ATOM   2905 C CD   . PRO A 1 411 ? 94.967  112.087 150.966 1.00 110.46 ? 411  PRO B CD   1 
ATOM   2906 N N    . HIS A 1 412 ? 96.449  111.856 148.107 1.00 103.97 ? 412  HIS B N    1 
ATOM   2907 C CA   . HIS A 1 412 ? 97.591  111.745 147.210 1.00 103.55 ? 412  HIS B CA   1 
ATOM   2908 C C    . HIS A 1 412 ? 97.409  110.598 146.219 1.00 103.57 ? 412  HIS B C    1 
ATOM   2909 O O    . HIS A 1 412 ? 98.073  110.548 145.181 1.00 108.60 ? 412  HIS B O    1 
ATOM   2910 C CB   . HIS A 1 412 ? 98.863  111.637 148.038 1.00 104.92 ? 412  HIS B CB   1 
ATOM   2911 C CG   . HIS A 1 412 ? 99.279  112.958 148.602 1.00 105.28 ? 412  HIS B CG   1 
ATOM   2912 N ND1  . HIS A 1 412 ? 99.142  113.271 149.937 1.00 104.51 ? 412  HIS B ND1  1 
ATOM   2913 C CD2  . HIS A 1 412 ? 99.722  114.085 147.996 1.00 104.18 ? 412  HIS B CD2  1 
ATOM   2914 C CE1  . HIS A 1 412 ? 99.534  114.516 150.138 1.00 102.99 ? 412  HIS B CE1  1 
ATOM   2915 N NE2  . HIS A 1 412 ? 99.884  115.035 148.975 1.00 103.79 ? 412  HIS B NE2  1 
ATOM   2916 N N    . MET A 1 413 ? 96.650  109.575 146.605 1.00 102.32 ? 413  MET B N    1 
ATOM   2917 C CA   . MET A 1 413 ? 96.441  108.444 145.708 1.00 106.12 ? 413  MET B CA   1 
ATOM   2918 C C    . MET A 1 413 ? 95.733  108.844 144.410 1.00 106.27 ? 413  MET B C    1 
ATOM   2919 O O    . MET A 1 413 ? 96.138  108.430 143.318 1.00 102.16 ? 413  MET B O    1 
ATOM   2920 C CB   . MET A 1 413 ? 95.654  107.347 146.428 1.00 105.98 ? 413  MET B CB   1 
ATOM   2921 C CG   . MET A 1 413 ? 95.724  105.990 145.739 1.00 107.38 ? 413  MET B CG   1 
ATOM   2922 S SD   . MET A 1 413 ? 94.647  104.724 146.445 1.00 110.75 ? 413  MET B SD   1 
ATOM   2923 C CE   . MET A 1 413 ? 93.522  105.720 147.417 1.00 105.34 ? 413  MET B CE   1 
ATOM   2924 N N    . LEU A 1 414 ? 94.658  109.636 144.515 1.00 102.23 ? 414  LEU B N    1 
ATOM   2925 C CA   . LEU A 1 414 ? 93.937  110.100 143.326 1.00 99.55  ? 414  LEU B CA   1 
ATOM   2926 C C    . LEU A 1 414 ? 94.765  110.990 142.392 1.00 98.75  ? 414  LEU B C    1 
ATOM   2927 O O    . LEU A 1 414 ? 94.569  110.949 141.172 1.00 100.79 ? 414  LEU B O    1 
ATOM   2928 C CB   . LEU A 1 414 ? 92.661  110.821 143.759 1.00 100.83 ? 414  LEU B CB   1 
ATOM   2929 C CG   . LEU A 1 414 ? 91.787  110.034 144.737 1.00 98.59  ? 414  LEU B CG   1 
ATOM   2930 C CD1  . LEU A 1 414 ? 90.555  110.829 145.120 1.00 98.26  ? 414  LEU B CD1  1 
ATOM   2931 C CD2  . LEU A 1 414 ? 91.394  108.682 144.148 1.00 99.22  ? 414  LEU B CD2  1 
ATOM   2932 N N    . THR A 1 415 ? 95.674  111.818 142.928 1.00 92.82  ? 415  THR B N    1 
ATOM   2933 C CA   . THR A 1 415 ? 96.516  112.621 142.031 1.00 92.79  ? 415  THR B CA   1 
ATOM   2934 C C    . THR A 1 415 ? 97.412  111.727 141.176 1.00 94.20  ? 415  THR B C    1 
ATOM   2935 O O    . THR A 1 415 ? 97.601  111.996 139.985 1.00 99.38  ? 415  THR B O    1 
ATOM   2936 C CB   . THR A 1 415 ? 97.302  113.726 142.758 1.00 91.17  ? 415  THR B CB   1 
ATOM   2937 O OG1  . THR A 1 415 ? 98.127  114.419 141.811 1.00 89.99  ? 415  THR B OG1  1 
ATOM   2938 C CG2  . THR A 1 415 ? 98.176  113.220 143.840 1.00 93.96  ? 415  THR B CG2  1 
ATOM   2939 N N    . THR A 1 416 ? 97.978  110.675 141.776 1.00 89.19  ? 416  THR B N    1 
ATOM   2940 C CA   . THR A 1 416 ? 98.839  109.740 141.055 1.00 92.52  ? 416  THR B CA   1 
ATOM   2941 C C    . THR A 1 416 ? 98.075  109.072 139.916 1.00 94.74  ? 416  THR B C    1 
ATOM   2942 O O    . THR A 1 416 ? 98.627  108.843 138.834 1.00 93.26  ? 416  THR B O    1 
ATOM   2943 C CB   . THR A 1 416 ? 99.398  108.687 142.012 1.00 91.57  ? 416  THR B CB   1 
ATOM   2944 O OG1  . THR A 1 416 ? 98.330  108.123 142.780 1.00 90.17  ? 416  THR B OG1  1 
ATOM   2945 C CG2  . THR A 1 416 ? 100.409 109.310 142.955 1.00 90.39  ? 416  THR B CG2  1 
ATOM   2946 N N    . ASN A 1 417 ? 96.806  108.736 140.156 1.00 96.40  ? 417  ASN B N    1 
ATOM   2947 C CA   . ASN A 1 417 ? 95.936  108.220 139.100 1.00 96.28  ? 417  ASN B CA   1 
ATOM   2948 C C    . ASN A 1 417 ? 95.762  109.253 137.991 1.00 96.02  ? 417  ASN B C    1 
ATOM   2949 O O    . ASN A 1 417 ? 95.658  108.900 136.812 1.00 97.81  ? 417  ASN B O    1 
ATOM   2950 C CB   . ASN A 1 417 ? 94.583  107.816 139.684 1.00 99.18  ? 417  ASN B CB   1 
ATOM   2951 C CG   . ASN A 1 417 ? 94.651  106.512 140.453 1.00 98.29  ? 417  ASN B CG   1 
ATOM   2952 O OD1  . ASN A 1 417 ? 94.507  105.433 139.879 1.00 96.22  ? 417  ASN B OD1  1 
ATOM   2953 N ND2  . ASN A 1 417 ? 94.866  106.605 141.761 1.00 96.07  ? 417  ASN B ND2  1 
ATOM   2954 N N    . LEU A 1 418 ? 95.607  110.521 138.360 1.00 84.69  ? 418  LEU B N    1 
ATOM   2955 C CA   . LEU A 1 418 ? 95.446  111.575 137.364 1.00 80.08  ? 418  LEU B CA   1 
ATOM   2956 C C    . LEU A 1 418 ? 96.692  111.704 136.483 1.00 78.90  ? 418  LEU B C    1 
ATOM   2957 O O    . LEU A 1 418 ? 96.573  111.790 135.256 1.00 84.97  ? 418  LEU B O    1 
ATOM   2958 C CB   . LEU A 1 418 ? 95.115  112.899 138.060 1.00 80.74  ? 418  LEU B CB   1 
ATOM   2959 C CG   . LEU A 1 418 ? 94.596  114.113 137.279 1.00 78.52  ? 418  LEU B CG   1 
ATOM   2960 C CD1  . LEU A 1 418 ? 93.778  114.986 138.207 1.00 83.19  ? 418  LEU B CD1  1 
ATOM   2961 C CD2  . LEU A 1 418 ? 95.710  114.938 136.667 1.00 81.58  ? 418  LEU B CD2  1 
ATOM   2962 N N    . LEU A 1 419 ? 97.889  111.717 137.087 1.00 75.17  ? 419  LEU B N    1 
ATOM   2963 C CA   . LEU A 1 419 ? 99.136  111.884 136.333 1.00 75.17  ? 419  LEU B CA   1 
ATOM   2964 C C    . LEU A 1 419 ? 99.435  110.756 135.345 1.00 78.76  ? 419  LEU B C    1 
ATOM   2965 O O    . LEU A 1 419 ? 99.989  111.028 134.275 1.00 84.62  ? 419  LEU B O    1 
ATOM   2966 C CB   . LEU A 1 419 ? 100.322 112.013 137.290 1.00 76.32  ? 419  LEU B CB   1 
ATOM   2967 C CG   . LEU A 1 419 ? 100.271 113.002 138.448 1.00 79.02  ? 419  LEU B CG   1 
ATOM   2968 C CD1  . LEU A 1 419 ? 101.337 112.656 139.465 1.00 79.01  ? 419  LEU B CD1  1 
ATOM   2969 C CD2  . LEU A 1 419 ? 100.490 114.394 137.918 1.00 78.65  ? 419  LEU B CD2  1 
ATOM   2970 N N    . ILE A 1 420 ? 99.131  109.497 135.675 1.00 82.25  ? 420  ILE B N    1 
ATOM   2971 C CA   . ILE A 1 420 ? 99.339  108.413 134.708 1.00 84.20  ? 420  ILE B CA   1 
ATOM   2972 C C    . ILE A 1 420 ? 98.470  108.618 133.469 1.00 82.08  ? 420  ILE B C    1 
ATOM   2973 O O    . ILE A 1 420 ? 98.904  108.360 132.340 1.00 81.95  ? 420  ILE B O    1 
ATOM   2974 C CB   . ILE A 1 420 ? 99.135  107.022 135.342 1.00 87.82  ? 420  ILE B CB   1 
ATOM   2975 C CG1  . ILE A 1 420 ? 97.985  106.994 136.333 1.00 85.77  ? 420  ILE B CG1  1 
ATOM   2976 C CG2  . ILE A 1 420 ? 100.410 106.559 136.028 1.00 88.31  ? 420  ILE B CG2  1 
ATOM   2977 C CD1  . ILE A 1 420 ? 97.563  105.603 136.748 1.00 87.83  ? 420  ILE B CD1  1 
ATOM   2978 N N    . ALA A 1 421 ? 97.225  109.064 133.663 1.00 72.93  ? 421  ALA B N    1 
ATOM   2979 C CA   . ALA A 1 421 ? 96.338  109.333 132.532 1.00 72.46  ? 421  ALA B CA   1 
ATOM   2980 C C    . ALA A 1 421 ? 96.896  110.418 131.612 1.00 74.17  ? 421  ALA B C    1 
ATOM   2981 O O    . ALA A 1 421 ? 96.813  110.295 130.385 1.00 78.16  ? 421  ALA B O    1 
ATOM   2982 C CB   . ALA A 1 421 ? 94.953  109.728 133.043 1.00 76.13  ? 421  ALA B CB   1 
ATOM   2983 N N    . GLN A 1 422 ? 97.446  111.495 132.180 1.00 67.62  ? 422  GLN B N    1 
ATOM   2984 C CA   . GLN A 1 422 ? 98.067  112.534 131.357 1.00 65.13  ? 422  GLN B CA   1 
ATOM   2985 C C    . GLN A 1 422 ? 99.270  111.993 130.591 1.00 63.96  ? 422  GLN B C    1 
ATOM   2986 O O    . GLN A 1 422 ? 99.536  112.409 129.458 1.00 64.71  ? 422  GLN B O    1 
ATOM   2987 C CB   . GLN A 1 422 ? 98.491  113.724 132.217 1.00 64.64  ? 422  GLN B CB   1 
ATOM   2988 C CG   . GLN A 1 422 ? 97.360  114.570 132.762 1.00 64.11  ? 422  GLN B CG   1 
ATOM   2989 C CD   . GLN A 1 422 ? 97.857  115.636 133.720 1.00 65.64  ? 422  GLN B CD   1 
ATOM   2990 O OE1  . GLN A 1 422 ? 99.020  115.629 134.121 1.00 65.34  ? 422  GLN B OE1  1 
ATOM   2991 N NE2  . GLN A 1 422 ? 96.990  116.582 134.057 1.00 65.49  ? 422  GLN B NE2  1 
ATOM   2992 N N    . SER A 1 423 ? 100.012 111.071 131.207 1.00 64.05  ? 423  SER B N    1 
ATOM   2993 C CA   . SER A 1 423 ? 101.171 110.450 130.569 1.00 63.22  ? 423  SER B CA   1 
ATOM   2994 C C    . SER A 1 423 ? 100.790 109.662 129.320 1.00 67.62  ? 423  SER B C    1 
ATOM   2995 O O    . SER A 1 423 ? 101.517 109.682 128.320 1.00 70.42  ? 423  SER B O    1 
ATOM   2996 C CB   . SER A 1 423 ? 101.894 109.549 131.570 1.00 68.66  ? 423  SER B CB   1 
ATOM   2997 O OG   . SER A 1 423 ? 103.203 109.242 131.124 1.00 72.96  ? 423  SER B OG   1 
ATOM   2998 N N    . ILE A 1 424 ? 99.670  108.935 129.365 1.00 77.65  ? 424  ILE B N    1 
ATOM   2999 C CA   . ILE A 1 424 ? 99.249  108.149 128.204 1.00 77.22  ? 424  ILE B CA   1 
ATOM   3000 C C    . ILE A 1 424 ? 98.888  109.052 127.029 1.00 79.91  ? 424  ILE B C    1 
ATOM   3001 O O    . ILE A 1 424 ? 99.155  108.713 125.869 1.00 82.35  ? 424  ILE B O    1 
ATOM   3002 C CB   . ILE A 1 424 ? 98.076  107.225 128.587 1.00 76.58  ? 424  ILE B CB   1 
ATOM   3003 C CG1  . ILE A 1 424 ? 98.425  106.398 129.826 1.00 80.51  ? 424  ILE B CG1  1 
ATOM   3004 C CG2  . ILE A 1 424 ? 97.699  106.320 127.423 1.00 78.13  ? 424  ILE B CG2  1 
ATOM   3005 C CD1  . ILE A 1 424 ? 97.475  105.245 130.090 1.00 79.14  ? 424  ILE B CD1  1 
ATOM   3006 N N    . VAL A 1 425 ? 98.272  110.206 127.301 1.00 71.75  ? 425  VAL B N    1 
ATOM   3007 C CA   . VAL A 1 425 ? 97.908  111.137 126.230 1.00 67.36  ? 425  VAL B CA   1 
ATOM   3008 C C    . VAL A 1 425 ? 99.155  111.623 125.491 1.00 67.06  ? 425  VAL B C    1 
ATOM   3009 O O    . VAL A 1 425 ? 99.203  111.635 124.254 1.00 64.87  ? 425  VAL B O    1 
ATOM   3010 C CB   . VAL A 1 425 ? 97.085  112.306 126.802 1.00 67.08  ? 425  VAL B CB   1 
ATOM   3011 C CG1  . VAL A 1 425 ? 97.147  113.523 125.894 1.00 71.45  ? 425  VAL B CG1  1 
ATOM   3012 C CG2  . VAL A 1 425 ? 95.642  111.875 127.029 1.00 69.27  ? 425  VAL B CG2  1 
ATOM   3013 N N    . CYS A 1 426 ? 100.182 112.029 126.243 1.00 69.97  ? 426  CYS B N    1 
ATOM   3014 C CA   . CYS A 1 426 ? 101.452 112.453 125.655 1.00 68.89  ? 426  CYS B CA   1 
ATOM   3015 C C    . CYS A 1 426 ? 102.141 111.310 124.910 1.00 74.19  ? 426  CYS B C    1 
ATOM   3016 O O    . CYS A 1 426 ? 102.691 111.508 123.821 1.00 75.31  ? 426  CYS B O    1 
ATOM   3017 C CB   . CYS A 1 426 ? 102.364 113.023 126.741 1.00 66.94  ? 426  CYS B CB   1 
ATOM   3018 S SG   . CYS A 1 426 ? 101.685 114.477 127.581 1.00 68.97  ? 426  CYS B SG   1 
ATOM   3019 N N    . ALA A 1 427 ? 102.128 110.109 125.494 1.00 86.97  ? 427  ALA B N    1 
ATOM   3020 C CA   . ALA A 1 427 ? 102.725 108.933 124.859 1.00 84.04  ? 427  ALA B CA   1 
ATOM   3021 C C    . ALA A 1 427 ? 102.032 108.574 123.547 1.00 84.82  ? 427  ALA B C    1 
ATOM   3022 O O    . ALA A 1 427 ? 102.684 108.189 122.570 1.00 85.47  ? 427  ALA B O    1 
ATOM   3023 C CB   . ALA A 1 427 ? 102.692 107.748 125.824 1.00 84.52  ? 427  ALA B CB   1 
ATOM   3024 N N    . GLY A 1 428 ? 100.710 108.686 123.514 1.00 91.33  ? 428  GLY B N    1 
ATOM   3025 C CA   . GLY A 1 428 ? 99.903  108.397 122.343 1.00 93.25  ? 428  GLY B CA   1 
ATOM   3026 C C    . GLY A 1 428 ? 100.183 109.214 121.094 1.00 95.68  ? 428  GLY B C    1 
ATOM   3027 O O    . GLY A 1 428 ? 100.162 108.691 119.976 1.00 96.91  ? 428  GLY B O    1 
ATOM   3028 N N    . MET A 1 429 ? 100.448 110.503 121.280 1.00 96.35  ? 429  MET B N    1 
ATOM   3029 C CA   . MET A 1 429 ? 100.748 111.431 120.197 1.00 92.94  ? 429  MET B CA   1 
ATOM   3030 C C    . MET A 1 429 ? 102.023 111.098 119.433 1.00 90.72  ? 429  MET B C    1 
ATOM   3031 O O    . MET A 1 429 ? 102.048 111.228 118.204 1.00 95.39  ? 429  MET B O    1 
ATOM   3032 C CB   . MET A 1 429 ? 100.858 112.854 120.744 1.00 90.53  ? 429  MET B CB   1 
ATOM   3033 C CG   . MET A 1 429 ? 101.013 113.919 119.672 1.00 90.37  ? 429  MET B CG   1 
ATOM   3034 S SD   . MET A 1 429 ? 99.757  113.777 118.394 1.00 96.06  ? 429  MET B SD   1 
ATOM   3035 C CE   . MET A 1 429 ? 100.628 114.444 116.978 1.00 90.85  ? 429  MET B CE   1 
ATOM   3036 N N    . MET A 1 430 ? 103.083 110.681 120.126 1.00 85.05  ? 430  MET B N    1 
ATOM   3037 C CA   . MET A 1 430 ? 104.295 110.282 119.421 1.00 86.72  ? 430  MET B CA   1 
ATOM   3038 C C    . MET A 1 430 ? 104.096 109.085 118.497 1.00 89.72  ? 430  MET B C    1 
ATOM   3039 O O    . MET A 1 430 ? 104.571 109.111 117.360 1.00 91.28  ? 430  MET B O    1 
ATOM   3040 C CB   . MET A 1 430 ? 105.394 109.931 120.427 1.00 89.58  ? 430  MET B CB   1 
ATOM   3041 C CG   . MET A 1 430 ? 105.629 110.961 121.509 1.00 89.09  ? 430  MET B CG   1 
ATOM   3042 S SD   . MET A 1 430 ? 106.760 112.265 121.011 1.00 89.90  ? 430  MET B SD   1 
ATOM   3043 C CE   . MET A 1 430 ? 107.422 112.717 122.609 1.00 84.99  ? 430  MET B CE   1 
ATOM   3044 N N    . ILE A 1 431 ? 103.401 108.042 118.947 1.00 102.55 ? 431  ILE B N    1 
ATOM   3045 C CA   . ILE A 1 431 ? 103.067 106.921 118.070 1.00 104.41 ? 431  ILE B CA   1 
ATOM   3046 C C    . ILE A 1 431 ? 102.150 107.338 116.921 1.00 105.13 ? 431  ILE B C    1 
ATOM   3047 O O    . ILE A 1 431 ? 102.267 106.826 115.801 1.00 104.49 ? 431  ILE B O    1 
ATOM   3048 C CB   . ILE A 1 431 ? 102.423 105.790 118.901 1.00 101.92 ? 431  ILE B CB   1 
ATOM   3049 C CG1  . ILE A 1 431 ? 103.407 105.266 119.949 1.00 105.09 ? 431  ILE B CG1  1 
ATOM   3050 C CG2  . ILE A 1 431 ? 101.957 104.637 118.023 1.00 100.76 ? 431  ILE B CG2  1 
ATOM   3051 C CD1  . ILE A 1 431 ? 104.740 104.839 119.379 1.00 104.22 ? 431  ILE B CD1  1 
ATOM   3052 N N    . TRP A 1 432 ? 101.274 108.315 117.176 1.00 111.71 ? 432  TRP B N    1 
ATOM   3053 C CA   . TRP A 1 432 ? 100.278 108.715 116.182 1.00 111.02 ? 432  TRP B CA   1 
ATOM   3054 C C    . TRP A 1 432 ? 100.906 109.367 114.949 1.00 109.65 ? 432  TRP B C    1 
ATOM   3055 O O    . TRP A 1 432 ? 100.503 109.074 113.817 1.00 109.13 ? 432  TRP B O    1 
ATOM   3056 C CB   . TRP A 1 432 ? 99.239  109.622 116.847 1.00 111.86 ? 432  TRP B CB   1 
ATOM   3057 C CG   . TRP A 1 432 ? 98.412  110.452 115.919 1.00 113.22 ? 432  TRP B CG   1 
ATOM   3058 C CD1  . TRP A 1 432 ? 98.741  111.650 115.348 1.00 113.59 ? 432  TRP B CD1  1 
ATOM   3059 C CD2  . TRP A 1 432 ? 97.116  110.114 115.421 1.00 112.22 ? 432  TRP B CD2  1 
ATOM   3060 N NE1  . TRP A 1 432 ? 97.716  112.086 114.545 1.00 114.51 ? 432  TRP B NE1  1 
ATOM   3061 C CE2  . TRP A 1 432 ? 96.708  111.158 114.571 1.00 112.92 ? 432  TRP B CE2  1 
ATOM   3062 C CE3  . TRP A 1 432 ? 96.256  109.030 115.620 1.00 111.80 ? 432  TRP B CE3  1 
ATOM   3063 C CZ2  . TRP A 1 432 ? 95.479  111.149 113.918 1.00 112.14 ? 432  TRP B CZ2  1 
ATOM   3064 C CZ3  . TRP A 1 432 ? 95.037  109.023 114.974 1.00 113.01 ? 432  TRP B CZ3  1 
ATOM   3065 C CH2  . TRP A 1 432 ? 94.659  110.076 114.134 1.00 112.37 ? 432  TRP B CH2  1 
ATOM   3066 N N    . ASN A 1 433 ? 101.869 110.271 115.154 1.00 114.63 ? 433  ASN B N    1 
ATOM   3067 C CA   . ASN A 1 433 ? 102.404 111.103 114.073 1.00 115.74 ? 433  ASN B CA   1 
ATOM   3068 C C    . ASN A 1 433 ? 103.104 110.262 113.006 1.00 118.25 ? 433  ASN B C    1 
ATOM   3069 O O    . ASN A 1 433 ? 103.065 110.587 111.813 1.00 119.42 ? 433  ASN B O    1 
ATOM   3070 C CB   . ASN A 1 433 ? 103.354 112.147 114.666 1.00 114.99 ? 433  ASN B CB   1 
ATOM   3071 C CG   . ASN A 1 433 ? 103.843 113.151 113.644 1.00 117.36 ? 433  ASN B CG   1 
ATOM   3072 O OD1  . ASN A 1 433 ? 103.132 113.491 112.700 1.00 120.56 ? 433  ASN B OD1  1 
ATOM   3073 N ND2  . ASN A 1 433 ? 105.059 113.650 113.842 1.00 116.27 ? 433  ASN B ND2  1 
ATOM   3074 N N    . PHE A 1 434 ? 103.744 109.177 113.431 1.00 119.01 ? 434  PHE B N    1 
ATOM   3075 C CA   . PHE A 1 434 ? 104.557 108.257 112.644 1.00 118.16 ? 434  PHE B CA   1 
ATOM   3076 C C    . PHE A 1 434 ? 103.752 107.180 111.920 1.00 118.80 ? 434  PHE B C    1 
ATOM   3077 O O    . PHE A 1 434 ? 104.301 106.493 111.050 1.00 119.14 ? 434  PHE B O    1 
ATOM   3078 C CB   . PHE A 1 434 ? 105.629 107.624 113.527 1.00 118.67 ? 434  PHE B CB   1 
ATOM   3079 C CG   . PHE A 1 434 ? 106.695 108.588 113.940 1.00 118.69 ? 434  PHE B CG   1 
ATOM   3080 C CD1  . PHE A 1 434 ? 107.645 109.018 113.030 1.00 118.66 ? 434  PHE B CD1  1 
ATOM   3081 C CD2  . PHE A 1 434 ? 106.727 109.095 115.223 1.00 119.24 ? 434  PHE B CD2  1 
ATOM   3082 C CE1  . PHE A 1 434 ? 108.621 109.919 113.405 1.00 118.82 ? 434  PHE B CE1  1 
ATOM   3083 C CE2  . PHE A 1 434 ? 107.696 109.997 115.605 1.00 119.77 ? 434  PHE B CE2  1 
ATOM   3084 C CZ   . PHE A 1 434 ? 108.646 110.410 114.695 1.00 119.24 ? 434  PHE B CZ   1 
ATOM   3085 N N    . VAL A 1 435 ? 102.472 107.018 112.246 1.00 130.27 ? 435  VAL B N    1 
ATOM   3086 C CA   . VAL A 1 435 ? 101.710 105.843 111.840 1.00 130.89 ? 435  VAL B CA   1 
ATOM   3087 C C    . VAL A 1 435 ? 100.784 106.085 110.652 1.00 132.47 ? 435  VAL B C    1 
ATOM   3088 O O    . VAL A 1 435 ? 100.317 105.103 110.053 1.00 133.15 ? 435  VAL B O    1 
ATOM   3089 C CB   . VAL A 1 435 ? 100.896 105.285 113.025 1.00 130.21 ? 435  VAL B CB   1 
ATOM   3090 N N    . LYS A 1 436 ? 100.453 107.346 110.331 1.00 133.77 ? 436  LYS B N    1 
ATOM   3091 C CA   . LYS A 1 436 ? 99.419  107.626 109.332 1.00 133.29 ? 436  LYS B CA   1 
ATOM   3092 C C    . LYS A 1 436 ? 99.774  106.995 107.987 1.00 132.98 ? 436  LYS B C    1 
ATOM   3093 O O    . LYS A 1 436 ? 98.882  106.682 107.190 1.00 132.64 ? 436  LYS B O    1 
ATOM   3094 C CB   . LYS A 1 436 ? 99.223  109.134 109.179 1.00 132.19 ? 436  LYS B CB   1 
ATOM   3095 N N    . GLU A 1 437 ? 101.066 106.809 107.719 1.00 134.49 ? 437  GLU B N    1 
ATOM   3096 C CA   . GLU A 1 437 ? 101.559 106.320 106.443 1.00 135.23 ? 437  GLU B CA   1 
ATOM   3097 C C    . GLU A 1 437 ? 101.848 104.830 106.554 1.00 135.88 ? 437  GLU B C    1 
ATOM   3098 O O    . GLU A 1 437 ? 102.519 104.253 105.693 1.00 135.26 ? 437  GLU B O    1 
ATOM   3099 C CB   . GLU A 1 437 ? 102.813 107.085 106.016 1.00 133.65 ? 437  GLU B CB   1 
ATOM   3100 N N    . LYS A 1 438 ? 101.360 104.222 107.631 1.00 143.59 ? 438  LYS B N    1 
ATOM   3101 C CA   . LYS A 1 438 ? 101.626 102.840 108.005 1.00 143.75 ? 438  LYS B CA   1 
ATOM   3102 C C    . LYS A 1 438 ? 100.276 102.139 108.163 1.00 143.95 ? 438  LYS B C    1 
ATOM   3103 O O    . LYS A 1 438 ? 99.247  102.597 107.651 1.00 142.37 ? 438  LYS B O    1 
ATOM   3104 C CB   . LYS A 1 438 ? 102.485 102.774 109.274 1.00 142.08 ? 438  LYS B CB   1 
ATOM   3105 N N    . ASN A 1 439 ? 100.300 100.996 108.853 1.00 149.60 ? 439  ASN B N    1 
ATOM   3106 C CA   . ASN A 1 439 ? 99.175  100.066 108.935 1.00 148.81 ? 439  ASN B CA   1 
ATOM   3107 C C    . ASN A 1 439 ? 97.881  100.730 109.404 1.00 149.93 ? 439  ASN B C    1 
ATOM   3108 O O    . ASN A 1 439 ? 97.835  101.363 110.464 1.00 150.66 ? 439  ASN B O    1 
ATOM   3109 C CB   . ASN A 1 439 ? 99.532  98.912  109.872 1.00 148.52 ? 439  ASN B CB   1 
ATOM   3110 N N    . PHE A 1 440 ? 96.831  100.583 108.588 1.00 151.11 ? 440  PHE B N    1 
ATOM   3111 C CA   . PHE A 1 440 ? 95.522  101.174 108.862 1.00 151.35 ? 440  PHE B CA   1 
ATOM   3112 C C    . PHE A 1 440 ? 94.911  100.628 110.150 1.00 151.23 ? 440  PHE B C    1 
ATOM   3113 O O    . PHE A 1 440 ? 94.173  101.340 110.838 1.00 151.18 ? 440  PHE B O    1 
ATOM   3114 C CB   . PHE A 1 440 ? 94.581  100.936 107.680 1.00 151.15 ? 440  PHE B CB   1 
ATOM   3115 C CG   . PHE A 1 440 ? 93.166  101.381 107.928 1.00 150.99 ? 440  PHE B CG   1 
ATOM   3116 C CD1  . PHE A 1 440 ? 92.850  102.729 107.965 1.00 151.19 ? 440  PHE B CD1  1 
ATOM   3117 C CD2  . PHE A 1 440 ? 92.154  100.454 108.120 1.00 150.35 ? 440  PHE B CD2  1 
ATOM   3118 C CE1  . PHE A 1 440 ? 91.552  103.147 108.191 1.00 150.91 ? 440  PHE B CE1  1 
ATOM   3119 C CE2  . PHE A 1 440 ? 90.853  100.866 108.348 1.00 151.34 ? 440  PHE B CE2  1 
ATOM   3120 C CZ   . PHE A 1 440 ? 90.552  102.214 108.383 1.00 151.04 ? 440  PHE B CZ   1 
ATOM   3121 N N    . VAL A 1 441 ? 95.170  99.358  110.462 1.00 153.80 ? 441  VAL B N    1 
ATOM   3122 C CA   . VAL A 1 441 ? 94.660  98.746  111.689 1.00 153.59 ? 441  VAL B CA   1 
ATOM   3123 C C    . VAL A 1 441 ? 95.227  99.446  112.921 1.00 152.64 ? 441  VAL B C    1 
ATOM   3124 O O    . VAL A 1 441 ? 94.527  99.632  113.923 1.00 151.85 ? 441  VAL B O    1 
ATOM   3125 C CB   . VAL A 1 441 ? 94.959  97.235  111.700 1.00 152.75 ? 441  VAL B CB   1 
ATOM   3126 C CG1  . VAL A 1 441 ? 93.948  96.491  110.842 1.00 152.61 ? 441  VAL B CG1  1 
ATOM   3127 C CG2  . VAL A 1 441 ? 96.373  96.962  111.208 1.00 152.08 ? 441  VAL B CG2  1 
ATOM   3128 N N    . GLY A 1 442 ? 96.506  99.820  112.879 1.00 147.38 ? 442  GLY B N    1 
ATOM   3129 C CA   . GLY A 1 442 ? 97.099  100.578 113.973 1.00 146.80 ? 442  GLY B CA   1 
ATOM   3130 C C    . GLY A 1 442 ? 96.456  101.931 114.232 1.00 147.24 ? 442  GLY B C    1 
ATOM   3131 O O    . GLY A 1 442 ? 96.552  102.461 115.340 1.00 146.70 ? 442  GLY B O    1 
ATOM   3132 N N    . GLN A 1 443 ? 95.869  102.545 113.206 1.00 149.88 ? 443  GLN B N    1 
ATOM   3133 C CA   . GLN A 1 443 ? 95.096  103.774 113.394 1.00 149.98 ? 443  GLN B CA   1 
ATOM   3134 C C    . GLN A 1 443 ? 94.006  103.646 114.466 1.00 149.57 ? 443  GLN B C    1 
ATOM   3135 O O    . GLN A 1 443 ? 93.891  104.505 115.348 1.00 148.43 ? 443  GLN B O    1 
ATOM   3136 C CB   . GLN A 1 443 ? 94.488  104.220 112.062 1.00 149.57 ? 443  GLN B CB   1 
ATOM   3137 C CG   . GLN A 1 443 ? 93.270  105.124 112.195 1.00 148.93 ? 443  GLN B CG   1 
ATOM   3138 C CD   . GLN A 1 443 ? 92.986  105.912 110.931 1.00 148.97 ? 443  GLN B CD   1 
ATOM   3139 O OE1  . GLN A 1 443 ? 93.291  105.466 109.826 1.00 149.55 ? 443  GLN B OE1  1 
ATOM   3140 N NE2  . GLN A 1 443 ? 92.399  107.092 111.090 1.00 148.34 ? 443  GLN B NE2  1 
ATOM   3141 N N    . ILE A 1 444 ? 93.196  102.582 114.409 1.00 145.08 ? 444  ILE B N    1 
ATOM   3142 C CA   . ILE A 1 444 ? 92.042  102.471 115.307 1.00 144.71 ? 444  ILE B CA   1 
ATOM   3143 C C    . ILE A 1 444 ? 92.440  102.237 116.772 1.00 145.19 ? 444  ILE B C    1 
ATOM   3144 O O    . ILE A 1 444 ? 91.845  102.848 117.669 1.00 145.86 ? 444  ILE B O    1 
ATOM   3145 C CB   . ILE A 1 444 ? 91.039  101.416 114.781 1.00 144.60 ? 444  ILE B CB   1 
ATOM   3146 C CG1  . ILE A 1 444 ? 89.666  101.621 115.428 1.00 144.12 ? 444  ILE B CG1  1 
ATOM   3147 C CG2  . ILE A 1 444 ? 91.518  99.975  114.950 1.00 144.75 ? 444  ILE B CG2  1 
ATOM   3148 C CD1  . ILE A 1 444 ? 88.776  102.589 114.679 1.00 143.52 ? 444  ILE B CD1  1 
ATOM   3149 N N    . LEU A 1 445 ? 93.397  101.339 117.059 1.00 142.59 ? 445  LEU B N    1 
ATOM   3150 C CA   . LEU A 1 445 ? 93.734  101.055 118.461 1.00 143.21 ? 445  LEU B CA   1 
ATOM   3151 C C    . LEU A 1 445 ? 94.262  102.307 119.159 1.00 142.42 ? 445  LEU B C    1 
ATOM   3152 O O    . LEU A 1 445 ? 93.911  102.577 120.314 1.00 140.43 ? 445  LEU B O    1 
ATOM   3153 C CB   . LEU A 1 445 ? 94.703  99.875  118.622 1.00 144.72 ? 445  LEU B CB   1 
ATOM   3154 C CG   . LEU A 1 445 ? 96.231  99.872  118.753 1.00 143.67 ? 445  LEU B CG   1 
ATOM   3155 C CD1  . LEU A 1 445 ? 96.684  98.470  119.131 1.00 142.12 ? 445  LEU B CD1  1 
ATOM   3156 C CD2  . LEU A 1 445 ? 96.932  100.281 117.511 1.00 142.98 ? 445  LEU B CD2  1 
ATOM   3157 N N    . VAL A 1 446 ? 95.115  103.073 118.475 1.00 137.59 ? 446  VAL B N    1 
ATOM   3158 C CA   . VAL A 1 446 ? 95.644  104.311 119.041 1.00 136.80 ? 446  VAL B CA   1 
ATOM   3159 C C    . VAL A 1 446 ? 94.526  105.337 119.212 1.00 135.95 ? 446  VAL B C    1 
ATOM   3160 O O    . VAL A 1 446 ? 94.515  106.096 120.189 1.00 135.71 ? 446  VAL B O    1 
ATOM   3161 C CB   . VAL A 1 446 ? 96.787  104.849 118.158 1.00 136.41 ? 446  VAL B CB   1 
ATOM   3162 C CG1  . VAL A 1 446 ? 97.367  106.128 118.734 1.00 135.72 ? 446  VAL B CG1  1 
ATOM   3163 C CG2  . VAL A 1 446 ? 97.881  103.806 118.016 1.00 136.85 ? 446  VAL B CG2  1 
ATOM   3164 N N    . PHE A 1 447 ? 93.571  105.380 118.276 1.00 133.88 ? 447  PHE B N    1 
ATOM   3165 C CA   . PHE A 1 447 ? 92.453  106.318 118.386 1.00 134.01 ? 447  PHE B CA   1 
ATOM   3166 C C    . PHE A 1 447 ? 91.648  106.047 119.654 1.00 133.67 ? 447  PHE B C    1 
ATOM   3167 O O    . PHE A 1 447 ? 91.275  106.976 120.379 1.00 135.77 ? 447  PHE B O    1 
ATOM   3168 C CB   . PHE A 1 447 ? 91.565  106.240 117.142 1.00 134.13 ? 447  PHE B CB   1 
ATOM   3169 C CG   . PHE A 1 447 ? 90.305  107.064 117.238 1.00 133.21 ? 447  PHE B CG   1 
ATOM   3170 C CD1  . PHE A 1 447 ? 90.310  108.398 116.868 1.00 134.17 ? 447  PHE B CD1  1 
ATOM   3171 C CD2  . PHE A 1 447 ? 89.110  106.496 117.658 1.00 132.17 ? 447  PHE B CD2  1 
ATOM   3172 C CE1  . PHE A 1 447 ? 89.159  109.160 116.947 1.00 133.86 ? 447  PHE B CE1  1 
ATOM   3173 C CE2  . PHE A 1 447 ? 87.956  107.252 117.739 1.00 132.97 ? 447  PHE B CE2  1 
ATOM   3174 C CZ   . PHE A 1 447 ? 87.980  108.584 117.380 1.00 133.98 ? 447  PHE B CZ   1 
ATOM   3175 N N    . VAL A 1 448 ? 91.349  104.772 119.917 1.00 133.91 ? 448  VAL B N    1 
ATOM   3176 C CA   . VAL A 1 448 ? 90.567  104.386 121.091 1.00 135.55 ? 448  VAL B CA   1 
ATOM   3177 C C    . VAL A 1 448 ? 91.336  104.740 122.358 1.00 135.63 ? 448  VAL B C    1 
ATOM   3178 O O    . VAL A 1 448 ? 90.770  105.258 123.329 1.00 133.73 ? 448  VAL B O    1 
ATOM   3179 C CB   . VAL A 1 448 ? 90.213  102.888 121.031 1.00 135.69 ? 448  VAL B CB   1 
ATOM   3180 C CG1  . VAL A 1 448 ? 89.571  102.432 122.334 1.00 135.48 ? 448  VAL B CG1  1 
ATOM   3181 C CG2  . VAL A 1 448 ? 89.294  102.609 119.852 1.00 135.22 ? 448  VAL B CG2  1 
ATOM   3182 N N    . LEU A 1 449 ? 92.643  104.465 122.358 1.00 132.42 ? 449  LEU B N    1 
ATOM   3183 C CA   . LEU A 1 449 ? 93.501  104.711 123.514 1.00 132.01 ? 449  LEU B CA   1 
ATOM   3184 C C    . LEU A 1 449 ? 93.549  106.195 123.865 1.00 129.00 ? 449  LEU B C    1 
ATOM   3185 O O    . LEU A 1 449 ? 93.505  106.559 125.046 1.00 126.87 ? 449  LEU B O    1 
ATOM   3186 C CB   . LEU A 1 449 ? 94.907  104.176 123.243 1.00 131.90 ? 449  LEU B CB   1 
ATOM   3187 C CG   . LEU A 1 449 ? 95.919  104.293 124.385 1.00 129.51 ? 449  LEU B CG   1 
ATOM   3188 C CD1  . LEU A 1 449 ? 95.658  103.234 125.446 1.00 128.42 ? 449  LEU B CD1  1 
ATOM   3189 C CD2  . LEU A 1 449 ? 97.342  104.187 123.856 1.00 129.31 ? 449  LEU B CD2  1 
ATOM   3190 N N    . LEU A 1 450 ? 93.656  107.064 122.856 1.00 124.13 ? 450  LEU B N    1 
ATOM   3191 C CA   . LEU A 1 450 ? 93.847  108.492 123.101 1.00 124.33 ? 450  LEU B CA   1 
ATOM   3192 C C    . LEU A 1 450 ? 92.624  109.117 123.764 1.00 125.10 ? 450  LEU B C    1 
ATOM   3193 O O    . LEU A 1 450 ? 92.754  109.834 124.763 1.00 128.25 ? 450  LEU B O    1 
ATOM   3194 C CB   . LEU A 1 450 ? 94.159  109.219 121.791 1.00 122.48 ? 450  LEU B CB   1 
ATOM   3195 C CG   . LEU A 1 450 ? 95.615  109.461 121.391 1.00 123.35 ? 450  LEU B CG   1 
ATOM   3196 C CD1  . LEU A 1 450 ? 96.190  110.635 122.164 1.00 122.12 ? 450  LEU B CD1  1 
ATOM   3197 C CD2  . LEU A 1 450 ? 96.447  108.225 121.619 1.00 121.28 ? 450  LEU B CD2  1 
ATOM   3198 N N    . TYR A 1 451 ? 91.427  108.860 123.238 1.00 123.80 ? 451  TYR B N    1 
ATOM   3199 C CA   . TYR A 1 451 ? 90.266  109.562 123.767 1.00 124.90 ? 451  TYR B CA   1 
ATOM   3200 C C    . TYR A 1 451 ? 89.729  108.916 125.036 1.00 126.45 ? 451  TYR B C    1 
ATOM   3201 O O    . TYR A 1 451 ? 89.049  109.592 125.815 1.00 128.37 ? 451  TYR B O    1 
ATOM   3202 C CB   . TYR A 1 451 ? 89.149  109.620 122.721 1.00 123.42 ? 451  TYR B CB   1 
ATOM   3203 C CG   . TYR A 1 451 ? 89.261  110.766 121.741 1.00 126.10 ? 451  TYR B CG   1 
ATOM   3204 C CD1  . TYR A 1 451 ? 90.419  110.967 121.001 1.00 126.84 ? 451  TYR B CD1  1 
ATOM   3205 C CD2  . TYR A 1 451 ? 88.203  111.648 121.556 1.00 127.17 ? 451  TYR B CD2  1 
ATOM   3206 C CE1  . TYR A 1 451 ? 90.521  112.015 120.105 1.00 127.89 ? 451  TYR B CE1  1 
ATOM   3207 C CE2  . TYR A 1 451 ? 88.296  112.698 120.662 1.00 127.62 ? 451  TYR B CE2  1 
ATOM   3208 C CZ   . TYR A 1 451 ? 89.457  112.877 119.940 1.00 128.07 ? 451  TYR B CZ   1 
ATOM   3209 O OH   . TYR A 1 451 ? 89.551  113.920 119.048 1.00 127.63 ? 451  TYR B OH   1 
ATOM   3210 N N    . SER A 1 452 ? 90.006  107.628 125.253 1.00 128.50 ? 452  SER B N    1 
ATOM   3211 C CA   . SER A 1 452 ? 89.671  106.995 126.526 1.00 130.62 ? 452  SER B CA   1 
ATOM   3212 C C    . SER A 1 452 ? 90.443  107.624 127.681 1.00 127.85 ? 452  SER B C    1 
ATOM   3213 O O    . SER A 1 452 ? 89.876  107.894 128.746 1.00 126.31 ? 452  SER B O    1 
ATOM   3214 C CB   . SER A 1 452 ? 89.943  105.493 126.456 1.00 129.98 ? 452  SER B CB   1 
ATOM   3215 O OG   . SER A 1 452 ? 91.197  105.233 125.852 1.00 129.63 ? 452  SER B OG   1 
ATOM   3216 N N    . SER A 1 453 ? 91.741  107.865 127.486 1.00 115.77 ? 453  SER B N    1 
ATOM   3217 C CA   . SER A 1 453 ? 92.543  108.525 128.513 1.00 114.19 ? 453  SER B CA   1 
ATOM   3218 C C    . SER A 1 453 ? 92.240  110.015 128.597 1.00 113.91 ? 453  SER B C    1 
ATOM   3219 O O    . SER A 1 453 ? 92.230  110.586 129.694 1.00 117.07 ? 453  SER B O    1 
ATOM   3220 C CB   . SER A 1 453 ? 94.030  108.299 128.238 1.00 113.59 ? 453  SER B CB   1 
ATOM   3221 O OG   . SER A 1 453 ? 94.297  106.935 127.965 1.00 115.23 ? 453  SER B OG   1 
ATOM   3222 N N    . LEU A 1 454 ? 92.022  110.666 127.451 1.00 110.29 ? 454  LEU B N    1 
ATOM   3223 C CA   . LEU A 1 454 ? 91.700  112.091 127.452 1.00 113.57 ? 454  LEU B CA   1 
ATOM   3224 C C    . LEU A 1 454 ? 90.397  112.361 128.199 1.00 115.78 ? 454  LEU B C    1 
ATOM   3225 O O    . LEU A 1 454 ? 90.303  113.322 128.971 1.00 118.80 ? 454  LEU B O    1 
ATOM   3226 C CB   . LEU A 1 454 ? 91.615  112.609 126.016 1.00 113.15 ? 454  LEU B CB   1 
ATOM   3227 C CG   . LEU A 1 454 ? 91.322  114.093 125.781 1.00 110.51 ? 454  LEU B CG   1 
ATOM   3228 C CD1  . LEU A 1 454 ? 92.131  114.968 126.731 1.00 110.62 ? 454  LEU B CD1  1 
ATOM   3229 C CD2  . LEU A 1 454 ? 91.595  114.471 124.335 1.00 113.98 ? 454  LEU B CD2  1 
ATOM   3230 N N    . TYR A 1 455 ? 89.379  111.528 127.970 1.00 121.68 ? 455  TYR B N    1 
ATOM   3231 C CA   . TYR A 1 455 ? 88.124  111.657 128.706 1.00 121.39 ? 455  TYR B CA   1 
ATOM   3232 C C    . TYR A 1 455 ? 88.323  111.386 130.193 1.00 120.00 ? 455  TYR B C    1 
ATOM   3233 O O    . TYR A 1 455 ? 87.706  112.046 131.039 1.00 119.19 ? 455  TYR B O    1 
ATOM   3234 C CB   . TYR A 1 455 ? 87.076  110.707 128.128 1.00 123.46 ? 455  TYR B CB   1 
ATOM   3235 C CG   . TYR A 1 455 ? 86.489  111.155 126.806 1.00 123.77 ? 455  TYR B CG   1 
ATOM   3236 C CD1  . TYR A 1 455 ? 86.740  112.426 126.304 1.00 123.58 ? 455  TYR B CD1  1 
ATOM   3237 C CD2  . TYR A 1 455 ? 85.689  110.301 126.057 1.00 121.65 ? 455  TYR B CD2  1 
ATOM   3238 C CE1  . TYR A 1 455 ? 86.206  112.835 125.096 1.00 123.58 ? 455  TYR B CE1  1 
ATOM   3239 C CE2  . TYR A 1 455 ? 85.152  110.702 124.849 1.00 122.81 ? 455  TYR B CE2  1 
ATOM   3240 C CZ   . TYR A 1 455 ? 85.414  111.969 124.374 1.00 122.74 ? 455  TYR B CZ   1 
ATOM   3241 O OH   . TYR A 1 455 ? 84.880  112.371 123.171 1.00 122.93 ? 455  TYR B OH   1 
ATOM   3242 N N    . SER A 1 456 ? 89.165  110.403 130.527 1.00 116.89 ? 456  SER B N    1 
ATOM   3243 C CA   . SER A 1 456 ? 89.449  110.094 131.926 1.00 118.26 ? 456  SER B CA   1 
ATOM   3244 C C    . SER A 1 456 ? 90.114  111.268 132.635 1.00 114.83 ? 456  SER B C    1 
ATOM   3245 O O    . SER A 1 456 ? 89.838  111.525 133.813 1.00 116.95 ? 456  SER B O    1 
ATOM   3246 C CB   . SER A 1 456 ? 90.326  108.846 132.016 1.00 118.75 ? 456  SER B CB   1 
ATOM   3247 O OG   . SER A 1 456 ? 90.346  108.329 133.334 1.00 117.85 ? 456  SER B OG   1 
ATOM   3248 N N    . THR A 1 457 ? 91.008  111.976 131.938 1.00 96.23  ? 457  THR B N    1 
ATOM   3249 C CA   . THR A 1 457 ? 91.678  113.137 132.520 1.00 98.12  ? 457  THR B CA   1 
ATOM   3250 C C    . THR A 1 457 ? 90.671  114.216 132.911 1.00 101.24 ? 457  THR B C    1 
ATOM   3251 O O    . THR A 1 457 ? 90.784  114.828 133.981 1.00 103.63 ? 457  THR B O    1 
ATOM   3252 C CB   . THR A 1 457 ? 92.714  113.676 131.530 1.00 95.13  ? 457  THR B CB   1 
ATOM   3253 O OG1  . THR A 1 457 ? 93.914  112.898 131.624 1.00 93.97  ? 457  THR B OG1  1 
ATOM   3254 C CG2  . THR A 1 457 ? 93.044  115.128 131.810 1.00 95.66  ? 457  THR B CG2  1 
ATOM   3255 N N    . TYR A 1 458 ? 89.664  114.437 132.064 1.00 113.05 ? 458  TYR B N    1 
ATOM   3256 C CA   . TYR A 1 458 ? 88.579  115.361 132.388 1.00 113.00 ? 458  TYR B CA   1 
ATOM   3257 C C    . TYR A 1 458 ? 87.820  114.920 133.635 1.00 112.28 ? 458  TYR B C    1 
ATOM   3258 O O    . TYR A 1 458 ? 87.551  115.729 134.530 1.00 112.50 ? 458  TYR B O    1 
ATOM   3259 C CB   . TYR A 1 458 ? 87.626  115.496 131.198 1.00 114.20 ? 458  TYR B CB   1 
ATOM   3260 C CG   . TYR A 1 458 ? 88.262  116.018 129.927 1.00 113.99 ? 458  TYR B CG   1 
ATOM   3261 C CD1  . TYR A 1 458 ? 89.362  116.865 129.973 1.00 114.47 ? 458  TYR B CD1  1 
ATOM   3262 C CD2  . TYR A 1 458 ? 87.762  115.663 128.680 1.00 111.50 ? 458  TYR B CD2  1 
ATOM   3263 C CE1  . TYR A 1 458 ? 89.942  117.348 128.816 1.00 113.84 ? 458  TYR B CE1  1 
ATOM   3264 C CE2  . TYR A 1 458 ? 88.339  116.140 127.516 1.00 111.12 ? 458  TYR B CE2  1 
ATOM   3265 C CZ   . TYR A 1 458 ? 89.427  116.982 127.592 1.00 111.77 ? 458  TYR B CZ   1 
ATOM   3266 O OH   . TYR A 1 458 ? 90.008  117.463 126.441 1.00 111.61 ? 458  TYR B OH   1 
ATOM   3267 N N    . LEU A 1 459 ? 87.459  113.637 133.709 1.00 109.77 ? 459  LEU B N    1 
ATOM   3268 C CA   . LEU A 1 459 ? 86.683  113.159 134.849 1.00 109.86 ? 459  LEU B CA   1 
ATOM   3269 C C    . LEU A 1 459 ? 87.523  113.088 136.119 1.00 110.44 ? 459  LEU B C    1 
ATOM   3270 O O    . LEU A 1 459 ? 87.006  113.326 137.217 1.00 110.37 ? 459  LEU B O    1 
ATOM   3271 C CB   . LEU A 1 459 ? 86.084  111.789 134.534 1.00 111.13 ? 459  LEU B CB   1 
ATOM   3272 C CG   . LEU A 1 459 ? 84.834  111.757 133.653 1.00 111.02 ? 459  LEU B CG   1 
ATOM   3273 C CD1  . LEU A 1 459 ? 84.615  110.359 133.099 1.00 110.89 ? 459  LEU B CD1  1 
ATOM   3274 C CD2  . LEU A 1 459 ? 83.616  112.223 134.433 1.00 110.67 ? 459  LEU B CD2  1 
ATOM   3275 N N    . TRP A 1 460 ? 88.809  112.737 135.999 1.00 111.38 ? 460  TRP B N    1 
ATOM   3276 C CA   . TRP A 1 460 ? 89.664  112.662 137.182 1.00 111.08 ? 460  TRP B CA   1 
ATOM   3277 C C    . TRP A 1 460 ? 89.803  114.016 137.870 1.00 109.86 ? 460  TRP B C    1 
ATOM   3278 O O    . TRP A 1 460 ? 89.975  114.074 139.093 1.00 110.23 ? 460  TRP B O    1 
ATOM   3279 C CB   . TRP A 1 460 ? 91.044  112.118 136.808 1.00 109.97 ? 460  TRP B CB   1 
ATOM   3280 C CG   . TRP A 1 460 ? 91.149  110.623 136.893 1.00 110.90 ? 460  TRP B CG   1 
ATOM   3281 C CD1  . TRP A 1 460 ? 91.413  109.763 135.868 1.00 112.46 ? 460  TRP B CD1  1 
ATOM   3282 C CD2  . TRP A 1 460 ? 90.989  109.812 138.065 1.00 109.01 ? 460  TRP B CD2  1 
ATOM   3283 N NE1  . TRP A 1 460 ? 91.429  108.469 136.326 1.00 112.77 ? 460  TRP B NE1  1 
ATOM   3284 C CE2  . TRP A 1 460 ? 91.172  108.471 137.672 1.00 110.89 ? 460  TRP B CE2  1 
ATOM   3285 C CE3  . TRP A 1 460 ? 90.711  110.089 139.407 1.00 109.02 ? 460  TRP B CE3  1 
ATOM   3286 C CZ2  . TRP A 1 460 ? 91.086  107.412 138.571 1.00 111.66 ? 460  TRP B CZ2  1 
ATOM   3287 C CZ3  . TRP A 1 460 ? 90.625  109.035 140.297 1.00 112.30 ? 460  TRP B CZ3  1 
ATOM   3288 C CH2  . TRP A 1 460 ? 90.812  107.714 139.876 1.00 112.13 ? 460  TRP B CH2  1 
ATOM   3289 N N    . THR A 1 461 ? 89.747  115.108 137.102 1.00 110.82 ? 461  THR B N    1 
ATOM   3290 C CA   . THR A 1 461 ? 89.774  116.446 137.688 1.00 111.32 ? 461  THR B CA   1 
ATOM   3291 C C    . THR A 1 461 ? 88.561  116.690 138.577 1.00 112.05 ? 461  THR B C    1 
ATOM   3292 O O    . THR A 1 461 ? 88.686  117.255 139.671 1.00 110.41 ? 461  THR B O    1 
ATOM   3293 C CB   . THR A 1 461 ? 89.853  117.503 136.587 1.00 111.86 ? 461  THR B CB   1 
ATOM   3294 O OG1  . THR A 1 461 ? 90.954  117.209 135.718 1.00 110.48 ? 461  THR B OG1  1 
ATOM   3295 C CG2  . THR A 1 461 ? 90.045  118.888 137.189 1.00 110.49 ? 461  THR B CG2  1 
ATOM   3296 N N    . GLY A 1 462 ? 87.378  116.271 138.124 1.00 124.91 ? 462  GLY B N    1 
ATOM   3297 C CA   . GLY A 1 462 ? 86.188  116.411 138.948 1.00 124.67 ? 462  GLY B CA   1 
ATOM   3298 C C    . GLY A 1 462 ? 86.227  115.536 140.185 1.00 126.02 ? 462  GLY B C    1 
ATOM   3299 O O    . GLY A 1 462 ? 85.787  115.951 141.261 1.00 126.96 ? 462  GLY B O    1 
ATOM   3300 N N    . LEU A 1 463 ? 86.717  114.303 140.042 1.00 121.74 ? 463  LEU B N    1 
ATOM   3301 C CA   . LEU A 1 463 ? 86.795  113.399 141.185 1.00 121.93 ? 463  LEU B CA   1 
ATOM   3302 C C    . LEU A 1 463 ? 87.738  113.944 142.254 1.00 121.29 ? 463  LEU B C    1 
ATOM   3303 O O    . LEU A 1 463 ? 87.490  113.777 143.454 1.00 119.71 ? 463  LEU B O    1 
ATOM   3304 C CB   . LEU A 1 463 ? 87.234  112.011 140.718 1.00 121.19 ? 463  LEU B CB   1 
ATOM   3305 C CG   . LEU A 1 463 ? 86.205  111.262 139.862 1.00 119.25 ? 463  LEU B CG   1 
ATOM   3306 C CD1  . LEU A 1 463 ? 86.769  109.948 139.349 1.00 118.81 ? 463  LEU B CD1  1 
ATOM   3307 C CD2  . LEU A 1 463 ? 84.913  111.024 140.631 1.00 120.01 ? 463  LEU B CD2  1 
ATOM   3308 N N    . LEU A 1 464 ? 88.834  114.585 141.833 1.00 122.73 ? 464  LEU B N    1 
ATOM   3309 C CA   . LEU A 1 464 ? 89.761  115.198 142.782 1.00 121.83 ? 464  LEU B CA   1 
ATOM   3310 C C    . LEU A 1 464 ? 89.085  116.295 143.597 1.00 121.88 ? 464  LEU B C    1 
ATOM   3311 O O    . LEU A 1 464 ? 89.295  116.395 144.812 1.00 122.31 ? 464  LEU B O    1 
ATOM   3312 C CB   . LEU A 1 464 ? 90.964  115.772 142.035 1.00 121.18 ? 464  LEU B CB   1 
ATOM   3313 C CG   . LEU A 1 464 ? 92.311  115.871 142.751 1.00 120.99 ? 464  LEU B CG   1 
ATOM   3314 C CD1  . LEU A 1 464 ? 92.893  114.491 143.027 1.00 119.79 ? 464  LEU B CD1  1 
ATOM   3315 C CD2  . LEU A 1 464 ? 93.272  116.718 141.936 1.00 121.27 ? 464  LEU B CD2  1 
ATOM   3316 N N    . ALA A 1 465 ? 88.282  117.137 142.939 1.00 128.68 ? 465  ALA B N    1 
ATOM   3317 C CA   . ALA A 1 465 ? 87.597  118.226 143.630 1.00 128.99 ? 465  ALA B CA   1 
ATOM   3318 C C    . ALA A 1 465 ? 86.587  117.705 144.644 1.00 129.66 ? 465  ALA B C    1 
ATOM   3319 O O    . ALA A 1 465 ? 86.494  118.230 145.760 1.00 131.51 ? 465  ALA B O    1 
ATOM   3320 C CB   . ALA A 1 465 ? 86.915  119.145 142.618 1.00 130.80 ? 465  ALA B CB   1 
ATOM   3321 N N    . ILE A 1 466 ? 85.806  116.692 144.261 1.00 133.08 ? 466  ILE B N    1 
ATOM   3322 C CA   . ILE A 1 466 ? 84.797  116.124 145.153 1.00 134.53 ? 466  ILE B CA   1 
ATOM   3323 C C    . ILE A 1 466 ? 85.455  115.500 146.378 1.00 135.72 ? 466  ILE B C    1 
ATOM   3324 O O    . ILE A 1 466 ? 84.980  115.660 147.510 1.00 134.90 ? 466  ILE B O    1 
ATOM   3325 C CB   . ILE A 1 466 ? 83.926  115.110 144.384 1.00 134.05 ? 466  ILE B CB   1 
ATOM   3326 C CG1  . ILE A 1 466 ? 82.859  115.844 143.567 1.00 134.84 ? 466  ILE B CG1  1 
ATOM   3327 C CG2  . ILE A 1 466 ? 83.297  114.084 145.324 1.00 135.15 ? 466  ILE B CG2  1 
ATOM   3328 C CD1  . ILE A 1 466 ? 81.665  116.309 144.376 1.00 134.92 ? 466  ILE B CD1  1 
ATOM   3329 N N    . SER A 1 467 ? 86.559  114.779 146.171 1.00 139.22 ? 467  SER B N    1 
ATOM   3330 C CA   . SER A 1 467 ? 87.305  114.213 147.291 1.00 138.15 ? 467  SER B CA   1 
ATOM   3331 C C    . SER A 1 467 ? 87.859  115.295 148.213 1.00 136.50 ? 467  SER B C    1 
ATOM   3332 O O    . SER A 1 467 ? 87.880  115.117 149.437 1.00 136.77 ? 467  SER B O    1 
ATOM   3333 C CB   . SER A 1 467 ? 88.436  113.328 146.772 1.00 138.42 ? 467  SER B CB   1 
ATOM   3334 O OG   . SER A 1 467 ? 89.274  114.045 145.884 1.00 139.28 ? 467  SER B OG   1 
ATOM   3335 N N    . LEU A 1 468 ? 88.331  116.416 147.652 1.00 131.38 ? 468  LEU B N    1 
ATOM   3336 C CA   . LEU A 1 468 ? 88.718  117.538 148.505 1.00 131.36 ? 468  LEU B CA   1 
ATOM   3337 C C    . LEU A 1 468 ? 87.529  118.108 149.269 1.00 130.49 ? 468  LEU B C    1 
ATOM   3338 O O    . LEU A 1 468 ? 87.694  118.585 150.399 1.00 127.86 ? 468  LEU B O    1 
ATOM   3339 C CB   . LEU A 1 468 ? 89.376  118.628 147.659 1.00 132.63 ? 468  LEU B CB   1 
ATOM   3340 C CG   . LEU A 1 468 ? 90.876  118.830 147.869 1.00 131.63 ? 468  LEU B CG   1 
ATOM   3341 C CD1  . LEU A 1 468 ? 91.410  119.924 146.962 1.00 129.54 ? 468  LEU B CD1  1 
ATOM   3342 C CD2  . LEU A 1 468 ? 91.145  119.164 149.319 1.00 130.36 ? 468  LEU B CD2  1 
ATOM   3343 N N    . PHE A 1 469 ? 86.336  118.091 148.666 1.00 145.00 ? 469  PHE B N    1 
ATOM   3344 C CA   . PHE A 1 469 ? 85.136  118.544 149.365 1.00 145.24 ? 469  PHE B CA   1 
ATOM   3345 C C    . PHE A 1 469 ? 84.856  117.671 150.577 1.00 144.07 ? 469  PHE B C    1 
ATOM   3346 O O    . PHE A 1 469 ? 84.505  118.166 151.654 1.00 142.90 ? 469  PHE B O    1 
ATOM   3347 C CB   . PHE A 1 469 ? 83.929  118.556 148.430 1.00 146.18 ? 469  PHE B CB   1 
ATOM   3348 C CG   . PHE A 1 469 ? 82.620  118.704 149.150 1.00 145.76 ? 469  PHE B CG   1 
ATOM   3349 C CD1  . PHE A 1 469 ? 82.306  119.883 149.803 1.00 145.94 ? 469  PHE B CD1  1 
ATOM   3350 C CD2  . PHE A 1 469 ? 81.698  117.668 149.164 1.00 146.09 ? 469  PHE B CD2  1 
ATOM   3351 C CE1  . PHE A 1 469 ? 81.104  120.020 150.474 1.00 146.83 ? 469  PHE B CE1  1 
ATOM   3352 C CE2  . PHE A 1 469 ? 80.490  117.804 149.826 1.00 146.18 ? 469  PHE B CE2  1 
ATOM   3353 C CZ   . PHE A 1 469 ? 80.194  118.983 150.480 1.00 145.92 ? 469  PHE B CZ   1 
ATOM   3354 N N    . LEU A 1 470 ? 85.015  116.358 150.403 1.00 145.09 ? 470  LEU B N    1 
ATOM   3355 C CA   . LEU A 1 470 ? 84.710  115.385 151.441 1.00 144.72 ? 470  LEU B CA   1 
ATOM   3356 C C    . LEU A 1 470 ? 85.783  115.346 152.518 1.00 146.49 ? 470  LEU B C    1 
ATOM   3357 O O    . LEU A 1 470 ? 85.474  115.027 153.664 1.00 146.01 ? 470  LEU B O    1 
ATOM   3358 C CB   . LEU A 1 470 ? 84.501  114.002 150.799 1.00 145.22 ? 470  LEU B CB   1 
ATOM   3359 C CG   . LEU A 1 470 ? 84.416  112.646 151.531 1.00 145.39 ? 470  LEU B CG   1 
ATOM   3360 C CD1  . LEU A 1 470 ? 83.793  111.630 150.595 1.00 145.36 ? 470  LEU B CD1  1 
ATOM   3361 C CD2  . LEU A 1 470 ? 85.759  112.075 151.992 1.00 144.51 ? 470  LEU B CD2  1 
ATOM   3362 N N    . LEU A 1 471 ? 87.048  115.564 152.158 1.00 148.40 ? 471  LEU B N    1 
ATOM   3363 C CA   . LEU A 1 471 ? 88.146  115.354 153.101 1.00 146.58 ? 471  LEU B CA   1 
ATOM   3364 C C    . LEU A 1 471 ? 88.116  116.334 154.276 1.00 144.68 ? 471  LEU B C    1 
ATOM   3365 O O    . LEU A 1 471 ? 88.216  115.921 155.437 1.00 143.23 ? 471  LEU B O    1 
ATOM   3366 C CB   . LEU A 1 471 ? 89.483  115.450 152.368 1.00 146.62 ? 471  LEU B CB   1 
ATOM   3367 C CG   . LEU A 1 471 ? 90.726  115.387 153.258 1.00 146.08 ? 471  LEU B CG   1 
ATOM   3368 C CD1  . LEU A 1 471 ? 90.831  114.026 153.933 1.00 145.73 ? 471  LEU B CD1  1 
ATOM   3369 C CD2  . LEU A 1 471 ? 91.980  115.691 152.457 1.00 145.72 ? 471  LEU B CD2  1 
ATOM   3370 N N    . LYS A 1 472 ? 87.989  117.637 153.998 1.00 145.99 ? 472  LYS B N    1 
ATOM   3371 C CA   . LYS A 1 472 ? 88.005  118.649 155.058 1.00 147.22 ? 472  LYS B CA   1 
ATOM   3372 C C    . LYS A 1 472 ? 86.805  118.591 156.001 1.00 146.50 ? 472  LYS B C    1 
ATOM   3373 O O    . LYS A 1 472 ? 86.899  119.091 157.127 1.00 147.00 ? 472  LYS B O    1 
ATOM   3374 C CB   . LYS A 1 472 ? 88.094  120.044 154.437 1.00 147.65 ? 472  LYS B CB   1 
ATOM   3375 N N    . LYS A 1 473 ? 85.693  118.003 155.580 1.00 147.31 ? 473  LYS B N    1 
ATOM   3376 C CA   . LYS A 1 473 ? 84.504  117.866 156.417 1.00 147.09 ? 473  LYS B CA   1 
ATOM   3377 C C    . LYS A 1 473 ? 84.166  116.379 156.385 1.00 148.30 ? 473  LYS B C    1 
ATOM   3378 O O    . LYS A 1 473 ? 85.057  115.546 156.182 1.00 148.57 ? 473  LYS B O    1 
ATOM   3379 C CB   . LYS A 1 473 ? 83.365  118.767 155.925 1.00 146.99 ? 473  LYS B CB   1 
ATOM   3380 N N    . ARG A 1 474 ? 82.941  116.024 156.791 1.00 150.47 ? 474  ARG B N    1 
ATOM   3381 C CA   . ARG A 1 474 ? 82.482  114.642 156.652 1.00 149.76 ? 474  ARG B CA   1 
ATOM   3382 C C    . ARG A 1 474 ? 83.266  113.639 157.490 1.00 150.31 ? 474  ARG B C    1 
ATOM   3383 O O    . ARG A 1 474 ? 84.106  112.914 156.947 1.00 149.22 ? 474  ARG B O    1 
ATOM   3384 C CB   . ARG A 1 474 ? 82.489  114.215 155.177 1.00 148.76 ? 474  ARG B CB   1 
ATOM   3385 N N    . GLU A 1 475 ? 83.017  113.568 158.791 1.00 159.56 ? 475  GLU B N    1 
ATOM   3386 C CA   . GLU A 1 475 ? 83.662  112.510 159.549 1.00 158.05 ? 475  GLU B CA   1 
ATOM   3387 C C    . GLU A 1 475 ? 82.879  111.218 159.361 1.00 159.48 ? 475  GLU B C    1 
ATOM   3388 O O    . GLU A 1 475 ? 81.685  111.233 159.047 1.00 159.59 ? 475  GLU B O    1 
ATOM   3389 C CB   . GLU A 1 475 ? 83.745  112.874 161.032 1.00 157.12 ? 475  GLU B CB   1 
ATOM   3390 N N    . ARG A 1 476 ? 83.597  110.094 159.503 1.00 168.00 ? 476  ARG B N    1 
ATOM   3391 C CA   . ARG A 1 476 ? 83.118  108.725 159.304 1.00 168.03 ? 476  ARG B CA   1 
ATOM   3392 C C    . ARG A 1 476 ? 82.848  108.520 157.814 1.00 168.26 ? 476  ARG B C    1 
ATOM   3393 O O    . ARG A 1 476 ? 83.051  109.449 157.022 1.00 168.70 ? 476  ARG B O    1 
ATOM   3394 C CB   . ARG A 1 476 ? 81.878  108.410 160.150 1.00 167.37 ? 476  ARG B CB   1 
ATOM   3395 N N    . VAL A 1 477 ? 82.390  107.322 157.425 1.00 167.89 ? 477  VAL B N    1 
ATOM   3396 C CA   . VAL A 1 477 ? 82.006  107.009 156.046 1.00 167.65 ? 477  VAL B CA   1 
ATOM   3397 C C    . VAL A 1 477 ? 83.159  107.324 155.098 1.00 168.00 ? 477  VAL B C    1 
ATOM   3398 O O    . VAL A 1 477 ? 83.087  108.275 154.311 1.00 167.40 ? 477  VAL B O    1 
ATOM   3399 C CB   . VAL A 1 477 ? 80.727  107.760 155.631 1.00 167.68 ? 477  VAL B CB   1 
ATOM   3400 N N    . GLN A 1 478 ? 84.227  106.532 155.169 1.00 168.83 ? 478  GLN B N    1 
ATOM   3401 C CA   . GLN A 1 478 ? 85.393  106.766 154.328 1.00 169.40 ? 478  GLN B CA   1 
ATOM   3402 C C    . GLN A 1 478 ? 85.120  106.426 152.866 1.00 169.24 ? 478  GLN B C    1 
ATOM   3403 O O    . GLN A 1 478 ? 84.249  105.618 152.537 1.00 168.63 ? 478  GLN B O    1 
ATOM   3404 C CB   . GLN A 1 478 ? 86.582  105.947 154.834 1.00 168.32 ? 478  GLN B CB   1 
ATOM   3405 N N    . ILE A 1 479 ? 85.886  107.073 151.992 1.00 156.23 ? 479  ILE B N    1 
ATOM   3406 C CA   . ILE A 1 479 ? 85.738  107.009 150.540 1.00 155.13 ? 479  ILE B CA   1 
ATOM   3407 C C    . ILE A 1 479 ? 85.985  105.604 150.002 1.00 154.85 ? 479  ILE B C    1 
ATOM   3408 O O    . ILE A 1 479 ? 87.057  105.027 150.233 1.00 153.96 ? 479  ILE B O    1 
ATOM   3409 C CB   . ILE A 1 479 ? 86.674  108.015 149.852 1.00 154.18 ? 479  ILE B CB   1 
ATOM   3410 N N    . PRO A 1 480 ? 85.026  105.020 149.279 1.00 150.92 ? 480  PRO B N    1 
ATOM   3411 C CA   . PRO A 1 480 ? 85.233  103.711 148.641 1.00 149.98 ? 480  PRO B CA   1 
ATOM   3412 C C    . PRO A 1 480 ? 86.108  103.901 147.411 1.00 149.06 ? 480  PRO B C    1 
ATOM   3413 O O    . PRO A 1 480 ? 85.608  103.938 146.286 1.00 148.36 ? 480  PRO B O    1 
ATOM   3414 C CB   . PRO A 1 480 ? 83.812  103.266 148.264 1.00 149.95 ? 480  PRO B CB   1 
ATOM   3415 C CG   . PRO A 1 480 ? 82.884  104.226 148.965 1.00 149.38 ? 480  PRO B CG   1 
ATOM   3416 C CD   . PRO A 1 480 ? 83.647  105.499 149.104 1.00 150.34 ? 480  PRO B CD   1 
ATOM   3417 N N    . VAL A 1 481 ? 87.428  103.900 147.629 1.00 147.25 ? 481  VAL B N    1 
ATOM   3418 C CA   . VAL A 1 481 ? 88.423  104.147 146.583 1.00 147.79 ? 481  VAL B CA   1 
ATOM   3419 C C    . VAL A 1 481 ? 88.313  103.154 145.433 1.00 149.26 ? 481  VAL B C    1 
ATOM   3420 O O    . VAL A 1 481 ? 88.619  103.498 144.285 1.00 149.57 ? 481  VAL B O    1 
ATOM   3421 C CB   . VAL A 1 481 ? 89.838  104.162 147.199 1.00 146.93 ? 481  VAL B CB   1 
ATOM   3422 C CG1  . VAL A 1 481 ? 89.948  105.285 148.216 1.00 148.07 ? 481  VAL B CG1  1 
ATOM   3423 C CG2  . VAL A 1 481 ? 90.167  102.829 147.859 1.00 148.47 ? 481  VAL B CG2  1 
ATOM   3424 N N    . GLY A 1 482 ? 87.912  101.916 145.712 1.00 147.55 ? 482  GLY B N    1 
ATOM   3425 C CA   . GLY A 1 482 ? 87.694  100.959 144.639 1.00 145.74 ? 482  GLY B CA   1 
ATOM   3426 C C    . GLY A 1 482 ? 86.633  101.419 143.654 1.00 147.13 ? 482  GLY B C    1 
ATOM   3427 O O    . GLY A 1 482 ? 86.775  101.229 142.443 1.00 146.35 ? 482  GLY B O    1 
ATOM   3428 N N    . ILE A 1 483 ? 85.550  102.016 144.160 1.00 144.31 ? 483  ILE B N    1 
ATOM   3429 C CA   . ILE A 1 483 ? 84.499  102.557 143.294 1.00 143.37 ? 483  ILE B CA   1 
ATOM   3430 C C    . ILE A 1 483 ? 85.031  103.691 142.415 1.00 143.51 ? 483  ILE B C    1 
ATOM   3431 O O    . ILE A 1 483 ? 84.742  103.744 141.213 1.00 142.74 ? 483  ILE B O    1 
ATOM   3432 C CB   . ILE A 1 483 ? 83.298  103.014 144.141 1.00 142.18 ? 483  ILE B CB   1 
ATOM   3433 C CG1  . ILE A 1 483 ? 82.723  101.833 144.927 1.00 141.44 ? 483  ILE B CG1  1 
ATOM   3434 C CG2  . ILE A 1 483 ? 82.225  103.644 143.265 1.00 143.61 ? 483  ILE B CG2  1 
ATOM   3435 C CD1  . ILE A 1 483 ? 82.087  100.769 144.058 1.00 142.16 ? 483  ILE B CD1  1 
ATOM   3436 N N    . ILE A 1 484 ? 85.811  104.614 142.993 1.00 139.46 ? 484  ILE B N    1 
ATOM   3437 C CA   . ILE A 1 484 ? 86.379  105.717 142.206 1.00 138.90 ? 484  ILE B CA   1 
ATOM   3438 C C    . ILE A 1 484 ? 87.321  105.199 141.122 1.00 138.13 ? 484  ILE B C    1 
ATOM   3439 O O    . ILE A 1 484 ? 87.281  105.668 139.976 1.00 138.19 ? 484  ILE B O    1 
ATOM   3440 C CB   . ILE A 1 484 ? 87.067  106.785 143.092 1.00 139.35 ? 484  ILE B CB   1 
ATOM   3441 C CG1  . ILE A 1 484 ? 86.105  107.513 144.051 1.00 139.19 ? 484  ILE B CG1  1 
ATOM   3442 C CG2  . ILE A 1 484 ? 87.809  107.811 142.246 1.00 138.90 ? 484  ILE B CG2  1 
ATOM   3443 C CD1  . ILE A 1 484 ? 85.716  106.833 145.308 1.00 138.40 ? 484  ILE B CD1  1 
ATOM   3444 N N    . ILE A 1 485 ? 88.174  104.228 141.454 1.00 138.77 ? 485  ILE B N    1 
ATOM   3445 C CA   . ILE A 1 485 ? 89.060  103.640 140.449 1.00 139.42 ? 485  ILE B CA   1 
ATOM   3446 C C    . ILE A 1 485 ? 88.255  102.975 139.336 1.00 140.33 ? 485  ILE B C    1 
ATOM   3447 O O    . ILE A 1 485 ? 88.577  103.121 138.149 1.00 140.21 ? 485  ILE B O    1 
ATOM   3448 C CB   . ILE A 1 485 ? 90.034  102.649 141.115 1.00 139.90 ? 485  ILE B CB   1 
ATOM   3449 C CG1  . ILE A 1 485 ? 90.973  103.384 142.072 1.00 140.13 ? 485  ILE B CG1  1 
ATOM   3450 C CG2  . ILE A 1 485 ? 90.842  101.895 140.069 1.00 139.10 ? 485  ILE B CG2  1 
ATOM   3451 C CD1  . ILE A 1 485 ? 91.787  104.468 141.415 1.00 138.94 ? 485  ILE B CD1  1 
ATOM   3452 N N    . ILE A 1 486 ? 87.203  102.235 139.692 1.00 142.24 ? 486  ILE B N    1 
ATOM   3453 C CA   . ILE A 1 486 ? 86.323  101.656 138.677 1.00 142.94 ? 486  ILE B CA   1 
ATOM   3454 C C    . ILE A 1 486 ? 85.623  102.751 137.875 1.00 142.99 ? 486  ILE B C    1 
ATOM   3455 O O    . ILE A 1 486 ? 85.545  102.685 136.641 1.00 142.70 ? 486  ILE B O    1 
ATOM   3456 C CB   . ILE A 1 486 ? 85.312  100.698 139.337 1.00 141.24 ? 486  ILE B CB   1 
ATOM   3457 C CG1  . ILE A 1 486 ? 86.014  99.428  139.819 1.00 141.39 ? 486  ILE B CG1  1 
ATOM   3458 C CG2  . ILE A 1 486 ? 84.185  100.344 138.377 1.00 141.66 ? 486  ILE B CG2  1 
ATOM   3459 C CD1  . ILE A 1 486 ? 85.203  98.624  140.811 1.00 141.28 ? 486  ILE B CD1  1 
ATOM   3460 N N    . SER A 1 487 ? 85.115  103.780 138.561 1.00 139.43 ? 487  SER B N    1 
ATOM   3461 C CA   . SER A 1 487 ? 84.431  104.884 137.888 1.00 138.46 ? 487  SER B CA   1 
ATOM   3462 C C    . SER A 1 487 ? 85.365  105.682 136.984 1.00 138.86 ? 487  SER B C    1 
ATOM   3463 O O    . SER A 1 487 ? 84.976  106.077 135.878 1.00 139.62 ? 487  SER B O    1 
ATOM   3464 C CB   . SER A 1 487 ? 83.783  105.806 138.921 1.00 138.59 ? 487  SER B CB   1 
ATOM   3465 O OG   . SER A 1 487 ? 83.417  107.045 138.338 1.00 138.92 ? 487  SER B OG   1 
ATOM   3466 N N    . GLY A 1 488 ? 86.593  105.941 137.439 1.00 133.09 ? 488  GLY B N    1 
ATOM   3467 C CA   . GLY A 1 488 ? 87.522  106.738 136.654 1.00 132.26 ? 488  GLY B CA   1 
ATOM   3468 C C    . GLY A 1 488 ? 87.954  106.107 135.343 1.00 132.54 ? 488  GLY B C    1 
ATOM   3469 O O    . GLY A 1 488 ? 88.288  106.818 134.392 1.00 131.73 ? 488  GLY B O    1 
ATOM   3470 N N    . TRP A 1 489 ? 87.956  104.780 135.267 1.00 137.60 ? 489  TRP B N    1 
ATOM   3471 C CA   . TRP A 1 489 ? 88.387  104.080 134.061 1.00 137.93 ? 489  TRP B CA   1 
ATOM   3472 C C    . TRP A 1 489 ? 87.256  103.437 133.272 1.00 139.10 ? 489  TRP B C    1 
ATOM   3473 O O    . TRP A 1 489 ? 87.291  103.460 132.040 1.00 137.51 ? 489  TRP B O    1 
ATOM   3474 C CB   . TRP A 1 489 ? 89.423  103.010 134.422 1.00 138.55 ? 489  TRP B CB   1 
ATOM   3475 C CG   . TRP A 1 489 ? 90.746  103.584 134.831 1.00 138.40 ? 489  TRP B CG   1 
ATOM   3476 C CD1  . TRP A 1 489 ? 91.180  103.819 136.103 1.00 139.29 ? 489  TRP B CD1  1 
ATOM   3477 C CD2  . TRP A 1 489 ? 91.812  103.992 133.964 1.00 137.37 ? 489  TRP B CD2  1 
ATOM   3478 N NE1  . TRP A 1 489 ? 92.446  104.351 136.082 1.00 137.83 ? 489  TRP B NE1  1 
ATOM   3479 C CE2  . TRP A 1 489 ? 92.857  104.466 134.781 1.00 137.01 ? 489  TRP B CE2  1 
ATOM   3480 C CE3  . TRP A 1 489 ? 91.983  104.002 132.576 1.00 139.14 ? 489  TRP B CE3  1 
ATOM   3481 C CZ2  . TRP A 1 489 ? 94.055  104.946 134.256 1.00 137.77 ? 489  TRP B CZ2  1 
ATOM   3482 C CZ3  . TRP A 1 489 ? 93.174  104.478 132.058 1.00 139.34 ? 489  TRP B CZ3  1 
ATOM   3483 C CH2  . TRP A 1 489 ? 94.194  104.943 132.896 1.00 138.42 ? 489  TRP B CH2  1 
ATOM   3484 N N    . GLY A 1 490 ? 86.264  102.845 133.941 1.00 149.08 ? 490  GLY B N    1 
ATOM   3485 C CA   . GLY A 1 490 ? 85.183  102.192 133.216 1.00 149.09 ? 490  GLY B CA   1 
ATOM   3486 C C    . GLY A 1 490 ? 84.316  103.149 132.418 1.00 149.44 ? 490  GLY B C    1 
ATOM   3487 O O    . GLY A 1 490 ? 83.908  102.837 131.295 1.00 149.46 ? 490  GLY B O    1 
ATOM   3488 N N    . ILE A 1 491 ? 84.003  104.315 132.994 1.00 146.01 ? 491  ILE B N    1 
ATOM   3489 C CA   . ILE A 1 491 ? 83.135  105.280 132.308 1.00 144.90 ? 491  ILE B CA   1 
ATOM   3490 C C    . ILE A 1 491 ? 83.725  105.775 130.987 1.00 146.16 ? 491  ILE B C    1 
ATOM   3491 O O    . ILE A 1 491 ? 83.005  105.757 129.975 1.00 146.75 ? 491  ILE B O    1 
ATOM   3492 C CB   . ILE A 1 491 ? 82.742  106.417 133.269 1.00 145.30 ? 491  ILE B CB   1 
ATOM   3493 C CG1  . ILE A 1 491 ? 81.975  105.863 134.472 1.00 147.17 ? 491  ILE B CG1  1 
ATOM   3494 C CG2  . ILE A 1 491 ? 81.913  107.469 132.547 1.00 145.48 ? 491  ILE B CG2  1 
ATOM   3495 C CD1  . ILE A 1 491 ? 80.824  104.950 134.103 1.00 146.80 ? 491  ILE B CD1  1 
ATOM   3496 N N    . PRO A 1 492 ? 84.986  106.252 130.919 1.00 146.04 ? 492  PRO B N    1 
ATOM   3497 C CA   . PRO A 1 492 ? 85.528  106.662 129.607 1.00 146.04 ? 492  PRO B CA   1 
ATOM   3498 C C    . PRO A 1 492 ? 85.554  105.561 128.559 1.00 145.83 ? 492  PRO B C    1 
ATOM   3499 O O    . PRO A 1 492 ? 85.353  105.845 127.371 1.00 145.91 ? 492  PRO B O    1 
ATOM   3500 C CB   . PRO A 1 492 ? 86.948  107.129 129.948 1.00 143.13 ? 492  PRO B CB   1 
ATOM   3501 C CG   . PRO A 1 492 ? 86.884  107.541 131.344 1.00 143.32 ? 492  PRO B CG   1 
ATOM   3502 C CD   . PRO A 1 492 ? 85.938  106.593 131.999 1.00 144.92 ? 492  PRO B CD   1 
ATOM   3503 N N    . ALA A 1 493 ? 85.820  104.316 128.962 1.00 149.23 ? 493  ALA B N    1 
ATOM   3504 C CA   . ALA A 1 493 ? 85.841  103.211 128.007 1.00 149.42 ? 493  ALA B CA   1 
ATOM   3505 C C    . ALA A 1 493 ? 84.476  102.988 127.365 1.00 149.35 ? 493  ALA B C    1 
ATOM   3506 O O    . ALA A 1 493 ? 84.390  102.730 126.159 1.00 150.01 ? 493  ALA B O    1 
ATOM   3507 C CB   . ALA A 1 493 ? 86.324  101.935 128.696 1.00 149.45 ? 493  ALA B CB   1 
ATOM   3508 N N    . LEU A 1 494 ? 83.399  103.053 128.155 1.00 149.95 ? 494  LEU B N    1 
ATOM   3509 C CA   . LEU A 1 494 ? 82.062  102.885 127.590 1.00 150.91 ? 494  LEU B CA   1 
ATOM   3510 C C    . LEU A 1 494 ? 81.734  103.999 126.599 1.00 151.22 ? 494  LEU B C    1 
ATOM   3511 O O    . LEU A 1 494 ? 81.135  103.747 125.546 1.00 152.08 ? 494  LEU B O    1 
ATOM   3512 C CB   . LEU A 1 494 ? 81.020  102.838 128.709 1.00 150.77 ? 494  LEU B CB   1 
ATOM   3513 C CG   . LEU A 1 494 ? 80.570  101.457 129.198 1.00 151.29 ? 494  LEU B CG   1 
ATOM   3514 C CD1  . LEU A 1 494 ? 79.879  100.690 128.080 1.00 152.21 ? 494  LEU B CD1  1 
ATOM   3515 C CD2  . LEU A 1 494 ? 81.732  100.654 129.768 1.00 150.73 ? 494  LEU B CD2  1 
ATOM   3516 N N    . LEU A 1 495 ? 82.101  105.239 126.933 1.00 150.61 ? 495  LEU B N    1 
ATOM   3517 C CA   . LEU A 1 495 ? 81.883  106.369 126.031 1.00 150.84 ? 495  LEU B CA   1 
ATOM   3518 C C    . LEU A 1 495 ? 82.674  106.207 124.737 1.00 152.37 ? 495  LEU B C    1 
ATOM   3519 O O    . LEU A 1 495 ? 82.180  106.528 123.649 1.00 152.51 ? 495  LEU B O    1 
ATOM   3520 C CB   . LEU A 1 495 ? 82.255  107.677 126.729 1.00 150.39 ? 495  LEU B CB   1 
ATOM   3521 N N    . VAL A 1 496 ? 83.914  105.725 124.848 1.00 156.93 ? 496  VAL B N    1 
ATOM   3522 C CA   . VAL A 1 496 ? 84.769  105.483 123.687 1.00 156.33 ? 496  VAL B CA   1 
ATOM   3523 C C    . VAL A 1 496 ? 84.165  104.432 122.764 1.00 155.64 ? 496  VAL B C    1 
ATOM   3524 O O    . VAL A 1 496 ? 84.195  104.578 121.536 1.00 153.54 ? 496  VAL B O    1 
ATOM   3525 C CB   . VAL A 1 496 ? 86.184  105.084 124.145 1.00 155.74 ? 496  VAL B CB   1 
ATOM   3526 N N    . GLY A 1 497 ? 83.634  103.346 123.333 1.00 159.28 ? 497  GLY B N    1 
ATOM   3527 C CA   . GLY A 1 497 ? 83.048  102.299 122.509 1.00 158.45 ? 497  GLY B CA   1 
ATOM   3528 C C    . GLY A 1 497 ? 81.856  102.763 121.690 1.00 158.83 ? 497  GLY B C    1 
ATOM   3529 O O    . GLY A 1 497 ? 81.662  102.307 120.560 1.00 159.71 ? 497  GLY B O    1 
ATOM   3530 N N    . VAL A 1 498 ? 81.025  103.644 122.255 1.00 163.16 ? 498  VAL B N    1 
ATOM   3531 C CA   . VAL A 1 498 ? 79.885  104.168 121.502 1.00 163.59 ? 498  VAL B CA   1 
ATOM   3532 C C    . VAL A 1 498 ? 80.369  104.946 120.283 1.00 164.99 ? 498  VAL B C    1 
ATOM   3533 O O    . VAL A 1 498 ? 79.814  104.822 119.184 1.00 163.81 ? 498  VAL B O    1 
ATOM   3534 C CB   . VAL A 1 498 ? 78.995  105.035 122.411 1.00 163.40 ? 498  VAL B CB   1 
ATOM   3535 N N    . LEU A 1 499 ? 81.405  105.771 120.466 1.00 171.88 ? 499  LEU B N    1 
ATOM   3536 C CA   . LEU A 1 499 ? 81.981  106.549 119.372 1.00 171.56 ? 499  LEU B CA   1 
ATOM   3537 C C    . LEU A 1 499 ? 82.613  105.654 118.310 1.00 170.93 ? 499  LEU B C    1 
ATOM   3538 O O    . LEU A 1 499 ? 82.597  105.993 117.122 1.00 170.34 ? 499  LEU B O    1 
ATOM   3539 C CB   . LEU A 1 499 ? 83.013  107.536 119.917 1.00 170.28 ? 499  LEU B CB   1 
ATOM   3540 N N    . LEU A 1 500 ? 83.188  104.525 118.731 1.00 166.87 ? 500  LEU B N    1 
ATOM   3541 C CA   . LEU A 1 500 ? 83.827  103.588 117.810 1.00 166.23 ? 500  LEU B CA   1 
ATOM   3542 C C    . LEU A 1 500 ? 82.838  103.002 116.808 1.00 165.15 ? 500  LEU B C    1 
ATOM   3543 O O    . LEU A 1 500 ? 83.156  102.867 115.621 1.00 163.77 ? 500  LEU B O    1 
ATOM   3544 C CB   . LEU A 1 500 ? 84.512  102.471 118.597 1.00 166.13 ? 500  LEU B CB   1 
ATOM   3545 N N    . ILE A 1 501 ? 81.636  102.647 117.262 1.00 167.59 ? 501  ILE B N    1 
ATOM   3546 C CA   . ILE A 1 501 ? 80.677  101.996 116.373 1.00 167.12 ? 501  ILE B CA   1 
ATOM   3547 C C    . ILE A 1 501 ? 80.032  103.005 115.429 1.00 167.93 ? 501  ILE B C    1 
ATOM   3548 O O    . ILE A 1 501 ? 79.839  102.720 114.241 1.00 169.30 ? 501  ILE B O    1 
ATOM   3549 C CB   . ILE A 1 501 ? 79.620  101.238 117.196 1.00 167.01 ? 501  ILE B CB   1 
ATOM   3550 N N    . THR A 1 502 ? 79.690  104.188 115.924 1.00 172.08 ? 502  THR B N    1 
ATOM   3551 C CA   . THR A 1 502 ? 78.963  105.161 115.123 1.00 173.10 ? 502  THR B CA   1 
ATOM   3552 C C    . THR A 1 502 ? 79.921  106.167 114.492 1.00 174.14 ? 502  THR B C    1 
ATOM   3553 O O    . THR A 1 502 ? 80.667  106.865 115.183 1.00 174.78 ? 502  THR B O    1 
ATOM   3554 C CB   . THR A 1 502 ? 77.924  105.901 115.969 1.00 172.66 ? 502  THR B CB   1 
ATOM   3555 N N    . GLY A 1 503 ? 79.881  106.237 113.163 1.00 167.40 ? 503  GLY B N    1 
ATOM   3556 C CA   . GLY A 1 503 ? 80.777  107.084 112.397 1.00 166.58 ? 503  GLY B CA   1 
ATOM   3557 C C    . GLY A 1 503 ? 81.526  106.341 111.308 1.00 167.07 ? 503  GLY B C    1 
ATOM   3558 O O    . GLY A 1 503 ? 81.948  105.197 111.503 1.00 166.52 ? 503  GLY B O    1 
ATOM   3559 N N    . LYS A 1 504 ? 81.696  106.984 110.156 1.00 169.68 ? 504  LYS B N    1 
ATOM   3560 C CA   . LYS A 1 504 ? 82.477  106.443 109.051 1.00 169.97 ? 504  LYS B CA   1 
ATOM   3561 C C    . LYS A 1 504 ? 83.885  107.025 109.062 1.00 169.25 ? 504  LYS B C    1 
ATOM   3562 O O    . LYS A 1 504 ? 84.053  108.250 109.075 1.00 168.29 ? 504  LYS B O    1 
ATOM   3563 C CB   . LYS A 1 504 ? 81.798  106.738 107.712 1.00 168.55 ? 504  LYS B CB   1 
ATOM   3564 N N    . HIS A 1 505 ? 84.887  106.146 109.078 1.00 162.38 ? 505  HIS B N    1 
ATOM   3565 C CA   . HIS A 1 505 ? 86.277  106.581 109.148 1.00 161.91 ? 505  HIS B CA   1 
ATOM   3566 C C    . HIS A 1 505 ? 86.655  107.381 107.906 1.00 161.99 ? 505  HIS B C    1 
ATOM   3567 O O    . HIS A 1 505 ? 86.314  107.008 106.780 1.00 161.91 ? 505  HIS B O    1 
ATOM   3568 C CB   . HIS A 1 505 ? 87.203  105.374 109.300 1.00 160.84 ? 505  HIS B CB   1 
ATOM   3569 N N    . ASN A 1 506 ? 87.367  108.488 108.113 1.00 153.07 ? 506  ASN B N    1 
ATOM   3570 C CA   . ASN A 1 506 ? 87.914  109.286 107.017 1.00 152.87 ? 506  ASN B CA   1 
ATOM   3571 C C    . ASN A 1 506 ? 89.414  109.023 106.926 1.00 152.68 ? 506  ASN B C    1 
ATOM   3572 O O    . ASN A 1 506 ? 90.195  109.515 107.744 1.00 153.61 ? 506  ASN B O    1 
ATOM   3573 C CB   . ASN A 1 506 ? 87.620  110.767 107.228 1.00 151.96 ? 506  ASN B CB   1 
ATOM   3574 N N    . GLY A 1 507 ? 89.811  108.237 105.923 1.00 144.41 ? 507  GLY B N    1 
ATOM   3575 C CA   . GLY A 1 507 ? 91.201  107.843 105.777 1.00 144.36 ? 507  GLY B CA   1 
ATOM   3576 C C    . GLY A 1 507 ? 92.134  108.959 105.355 1.00 144.53 ? 507  GLY B C    1 
ATOM   3577 O O    . GLY A 1 507 ? 93.336  108.882 105.631 1.00 143.16 ? 507  GLY B O    1 
ATOM   3578 N N    . ASP A 1 508 ? 91.614  109.994 104.696 1.00 144.12 ? 508  ASP B N    1 
ATOM   3579 C CA   . ASP A 1 508 ? 92.439  111.099 104.225 1.00 142.80 ? 508  ASP B CA   1 
ATOM   3580 C C    . ASP A 1 508 ? 92.509  112.275 105.192 1.00 144.11 ? 508  ASP B C    1 
ATOM   3581 O O    . ASP A 1 508 ? 93.144  113.283 104.866 1.00 144.87 ? 508  ASP B O    1 
ATOM   3582 C CB   . ASP A 1 508 ? 91.928  111.589 102.866 1.00 142.47 ? 508  ASP B CB   1 
ATOM   3583 N N    . SER A 1 509 ? 91.885  112.182 106.364 1.00 142.89 ? 509  SER B N    1 
ATOM   3584 C CA   . SER A 1 509 ? 91.917  113.267 107.340 1.00 141.52 ? 509  SER B CA   1 
ATOM   3585 C C    . SER A 1 509 ? 93.136  113.044 108.226 1.00 141.04 ? 509  SER B C    1 
ATOM   3586 O O    . SER A 1 509 ? 93.152  112.123 109.049 1.00 141.69 ? 509  SER B O    1 
ATOM   3587 C CB   . SER A 1 509 ? 90.630  113.302 108.160 1.00 140.98 ? 509  SER B CB   1 
ATOM   3588 N N    . ILE A 1 510 ? 94.157  113.881 108.065 1.00 136.34 ? 510  ILE B N    1 
ATOM   3589 C CA   . ILE A 1 510 ? 95.375  113.757 108.880 1.00 137.87 ? 510  ILE B CA   1 
ATOM   3590 C C    . ILE A 1 510 ? 95.172  114.612 110.126 1.00 138.69 ? 510  ILE B C    1 
ATOM   3591 O O    . ILE A 1 510 ? 95.730  115.702 110.280 1.00 138.28 ? 510  ILE B O    1 
ATOM   3592 C CB   . ILE A 1 510 ? 96.633  114.144 108.097 1.00 136.89 ? 510  ILE B CB   1 
ATOM   3593 N N    . ASP A 1 511 ? 94.384  114.075 111.064 1.00 138.41 ? 511  ASP B N    1 
ATOM   3594 C CA   . ASP A 1 511 ? 94.095  114.707 112.350 1.00 136.60 ? 511  ASP B CA   1 
ATOM   3595 C C    . ASP A 1 511 ? 93.271  113.761 113.214 1.00 136.07 ? 511  ASP B C    1 
ATOM   3596 O O    . ASP A 1 511 ? 92.411  113.038 112.701 1.00 136.19 ? 511  ASP B O    1 
ATOM   3597 C CB   . ASP A 1 511 ? 93.332  116.024 112.173 1.00 136.38 ? 511  ASP B CB   1 
ATOM   3598 N N    . SER A 1 512 ? 93.527  113.753 114.524 1.00 139.58 ? 512  SER B N    1 
ATOM   3599 C CA   . SER A 1 512 ? 92.756  112.891 115.414 1.00 140.46 ? 512  SER B CA   1 
ATOM   3600 C C    . SER A 1 512 ? 91.316  113.364 115.579 1.00 141.43 ? 512  SER B C    1 
ATOM   3601 O O    . SER A 1 512 ? 90.426  112.553 115.858 1.00 141.18 ? 512  SER B O    1 
ATOM   3602 C CB   . SER A 1 512 ? 93.440  112.803 116.778 1.00 138.87 ? 512  SER B CB   1 
ATOM   3603 N N    . ALA A 1 513 ? 91.071  114.666 115.412 1.00 145.11 ? 513  ALA B N    1 
ATOM   3604 C CA   . ALA A 1 513 ? 89.748  115.230 115.654 1.00 144.77 ? 513  ALA B CA   1 
ATOM   3605 C C    . ALA A 1 513 ? 88.684  114.859 114.629 1.00 144.70 ? 513  ALA B C    1 
ATOM   3606 O O    . ALA A 1 513 ? 87.501  115.080 114.908 1.00 145.71 ? 513  ALA B O    1 
ATOM   3607 C CB   . ALA A 1 513 ? 89.849  116.754 115.738 1.00 144.88 ? 513  ALA B CB   1 
ATOM   3608 N N    . PHE A 1 514 ? 89.036  114.313 113.464 1.00 146.85 ? 514  PHE B N    1 
ATOM   3609 C CA   . PHE A 1 514 ? 87.978  114.067 112.490 1.00 148.17 ? 514  PHE B CA   1 
ATOM   3610 C C    . PHE A 1 514 ? 87.967  112.640 111.953 1.00 149.09 ? 514  PHE B C    1 
ATOM   3611 O O    . PHE A 1 514 ? 87.646  112.434 110.779 1.00 150.45 ? 514  PHE B O    1 
ATOM   3612 C CB   . PHE A 1 514 ? 88.078  115.059 111.332 1.00 148.20 ? 514  PHE B CB   1 
ATOM   3613 N N    . PHE A 1 515 ? 88.340  111.645 112.763 1.00 150.79 ? 515  PHE B N    1 
ATOM   3614 C CA   . PHE A 1 515 ? 88.281  110.273 112.267 1.00 150.95 ? 515  PHE B CA   1 
ATOM   3615 C C    . PHE A 1 515 ? 86.839  109.857 111.991 1.00 151.67 ? 515  PHE B C    1 
ATOM   3616 O O    . PHE A 1 515 ? 86.535  109.268 110.948 1.00 151.44 ? 515  PHE B O    1 
ATOM   3617 C CB   . PHE A 1 515 ? 88.936  109.322 113.270 1.00 150.25 ? 515  PHE B CB   1 
ATOM   3618 N N    . TYR A 1 516 ? 85.938  110.179 112.918 1.00 156.79 ? 516  TYR B N    1 
ATOM   3619 C CA   . TYR A 1 516 ? 84.506  109.934 112.808 1.00 157.50 ? 516  TYR B CA   1 
ATOM   3620 C C    . TYR A 1 516 ? 83.699  111.221 112.662 1.00 156.70 ? 516  TYR B C    1 
ATOM   3621 O O    . TYR A 1 516 ? 82.471  111.185 112.792 1.00 157.77 ? 516  TYR B O    1 
ATOM   3622 C CB   . TYR A 1 516 ? 84.009  109.121 114.006 1.00 156.94 ? 516  TYR B CB   1 
ATOM   3623 N N    . GLY A 1 517 ? 84.351  112.350 112.386 1.00 145.03 ? 517  GLY B N    1 
ATOM   3624 C CA   . GLY A 1 517 ? 83.604  113.580 112.148 1.00 145.12 ? 517  GLY B CA   1 
ATOM   3625 C C    . GLY A 1 517 ? 82.878  114.131 113.372 1.00 145.31 ? 517  GLY B C    1 
ATOM   3626 O O    . GLY A 1 517 ? 83.467  114.355 114.433 1.00 146.81 ? 517  GLY B O    1 
ATOM   3627 N N    . LYS A 1 518 ? 81.605  114.464 113.175 1.00 138.05 ? 518  LYS B N    1 
ATOM   3628 C CA   . LYS A 1 518 ? 80.811  115.213 114.152 1.00 137.43 ? 518  LYS B CA   1 
ATOM   3629 C C    . LYS A 1 518 ? 80.577  114.482 115.479 1.00 138.43 ? 518  LYS B C    1 
ATOM   3630 O O    . LYS A 1 518 ? 80.593  115.116 116.541 1.00 138.91 ? 518  LYS B O    1 
ATOM   3631 C CB   . LYS A 1 518 ? 79.468  115.596 113.528 1.00 136.06 ? 518  LYS B CB   1 
ATOM   3632 N N    . GLU A 1 519 ? 80.338  113.166 115.448 1.00 142.53 ? 519  GLU B N    1 
ATOM   3633 C CA   . GLU A 1 519 ? 79.995  112.431 116.674 1.00 143.44 ? 519  GLU B CA   1 
ATOM   3634 C C    . GLU A 1 519 ? 81.061  112.465 117.776 1.00 144.57 ? 519  GLU B C    1 
ATOM   3635 O O    . GLU A 1 519 ? 80.710  112.630 118.950 1.00 144.49 ? 519  GLU B O    1 
ATOM   3636 C CB   . GLU A 1 519 ? 79.671  110.981 116.316 1.00 142.35 ? 519  GLU B CB   1 
ATOM   3637 N N    . GLN A 1 520 ? 82.347  112.275 117.460 1.00 144.66 ? 520  GLN B N    1 
ATOM   3638 C CA   . GLN A 1 520 ? 83.358  112.391 118.522 1.00 143.60 ? 520  GLN B CA   1 
ATOM   3639 C C    . GLN A 1 520 ? 83.404  113.806 119.091 1.00 143.37 ? 520  GLN B C    1 
ATOM   3640 O O    . GLN A 1 520 ? 83.517  113.991 120.309 1.00 144.46 ? 520  GLN B O    1 
ATOM   3641 C CB   . GLN A 1 520 ? 84.753  111.926 118.080 1.00 143.51 ? 520  GLN B CB   1 
ATOM   3642 C CG   . GLN A 1 520 ? 85.494  112.790 117.104 1.00 143.05 ? 520  GLN B CG   1 
ATOM   3643 C CD   . GLN A 1 520 ? 85.249  112.324 115.722 1.00 144.18 ? 520  GLN B CD   1 
ATOM   3644 O OE1  . GLN A 1 520 ? 84.139  111.922 115.411 1.00 143.34 ? 520  GLN B OE1  1 
ATOM   3645 N NE2  . GLN A 1 520 ? 86.265  112.380 114.872 1.00 143.50 ? 520  GLN B NE2  1 
ATOM   3646 N N    . MET A 1 521 ? 83.344  114.812 118.217 1.00 131.60 ? 521  MET B N    1 
ATOM   3647 C CA   . MET A 1 521 ? 83.474  116.203 118.631 1.00 131.45 ? 521  MET B CA   1 
ATOM   3648 C C    . MET A 1 521 ? 82.335  116.632 119.555 1.00 131.99 ? 521  MET B C    1 
ATOM   3649 O O    . MET A 1 521 ? 82.560  117.379 120.515 1.00 133.33 ? 521  MET B O    1 
ATOM   3650 C CB   . MET A 1 521 ? 83.523  117.055 117.362 1.00 130.36 ? 521  MET B CB   1 
ATOM   3651 C CG   . MET A 1 521 ? 83.456  118.538 117.531 1.00 132.21 ? 521  MET B CG   1 
ATOM   3652 S SD   . MET A 1 521 ? 84.617  119.200 118.715 1.00 132.28 ? 521  MET B SD   1 
ATOM   3653 C CE   . MET A 1 521 ? 83.820  120.768 118.951 1.00 130.84 ? 521  MET B CE   1 
ATOM   3654 N N    . ILE A 1 522 ? 81.108  116.186 119.276 1.00 126.73 ? 522  ILE B N    1 
ATOM   3655 C CA   . ILE A 1 522 ? 79.964  116.537 120.121 1.00 127.94 ? 522  ILE B CA   1 
ATOM   3656 C C    . ILE A 1 522 ? 80.130  115.955 121.530 1.00 127.90 ? 522  ILE B C    1 
ATOM   3657 O O    . ILE A 1 522 ? 79.791  116.601 122.529 1.00 128.26 ? 522  ILE B O    1 
ATOM   3658 C CB   . ILE A 1 522 ? 78.630  116.145 119.441 1.00 128.09 ? 522  ILE B CB   1 
ATOM   3659 C CG1  . ILE A 1 522 ? 77.493  117.032 119.960 1.00 127.13 ? 522  ILE B CG1  1 
ATOM   3660 C CG2  . ILE A 1 522 ? 78.274  114.668 119.587 1.00 127.71 ? 522  ILE B CG2  1 
ATOM   3661 C CD1  . ILE A 1 522 ? 77.498  118.434 119.385 1.00 125.22 ? 522  ILE B CD1  1 
ATOM   3662 N N    . THR A 1 523 ? 80.644  114.722 121.622 1.00 126.30 ? 523  THR B N    1 
ATOM   3663 C CA   . THR A 1 523 ? 80.852  114.031 122.897 1.00 126.36 ? 523  THR B CA   1 
ATOM   3664 C C    . THR A 1 523 ? 81.830  114.761 123.813 1.00 126.18 ? 523  THR B C    1 
ATOM   3665 O O    . THR A 1 523 ? 81.636  114.787 125.034 1.00 126.88 ? 523  THR B O    1 
ATOM   3666 C CB   . THR A 1 523 ? 81.327  112.598 122.654 1.00 126.23 ? 523  THR B CB   1 
ATOM   3667 O OG1  . THR A 1 523 ? 82.453  112.603 121.769 1.00 126.50 ? 523  THR B OG1  1 
ATOM   3668 C CG2  . THR A 1 523 ? 80.209  111.757 122.056 1.00 126.77 ? 523  THR B CG2  1 
ATOM   3669 N N    . THR A 1 524 ? 82.900  115.332 123.252 1.00 124.51 ? 524  THR B N    1 
ATOM   3670 C CA   . THR A 1 524 ? 83.884  116.046 124.067 1.00 125.40 ? 524  THR B CA   1 
ATOM   3671 C C    . THR A 1 524 ? 83.261  117.237 124.791 1.00 125.55 ? 524  THR B C    1 
ATOM   3672 O O    . THR A 1 524 ? 83.570  117.482 125.963 1.00 125.80 ? 524  THR B O    1 
ATOM   3673 C CB   . THR A 1 524 ? 85.051  116.503 123.189 1.00 124.03 ? 524  THR B CB   1 
ATOM   3674 O OG1  . THR A 1 524 ? 85.637  115.365 122.544 1.00 123.30 ? 524  THR B OG1  1 
ATOM   3675 C CG2  . THR A 1 524 ? 86.118  117.201 124.022 1.00 125.45 ? 524  THR B CG2  1 
ATOM   3676 N N    . ALA A 1 525 ? 82.395  117.995 124.114 1.00 125.88 ? 525  ALA B N    1 
ATOM   3677 C CA   . ALA A 1 525 ? 81.774  119.154 124.752 1.00 125.83 ? 525  ALA B CA   1 
ATOM   3678 C C    . ALA A 1 525 ? 80.913  118.729 125.939 1.00 127.23 ? 525  ALA B C    1 
ATOM   3679 O O    . ALA A 1 525 ? 80.931  119.374 126.994 1.00 127.62 ? 525  ALA B O    1 
ATOM   3680 C CB   . ALA A 1 525 ? 80.944  119.935 123.734 1.00 126.28 ? 525  ALA B CB   1 
ATOM   3681 N N    . VAL A 1 526 ? 80.141  117.650 125.774 1.00 128.59 ? 526  VAL B N    1 
ATOM   3682 C CA   . VAL A 1 526 ? 79.289  117.130 126.844 1.00 127.62 ? 526  VAL B CA   1 
ATOM   3683 C C    . VAL A 1 526 ? 80.131  116.654 128.025 1.00 127.16 ? 526  VAL B C    1 
ATOM   3684 O O    . VAL A 1 526 ? 79.798  116.910 129.190 1.00 125.59 ? 526  VAL B O    1 
ATOM   3685 C CB   . VAL A 1 526 ? 78.385  116.007 126.300 1.00 127.42 ? 526  VAL B CB   1 
ATOM   3686 C CG1  . VAL A 1 526 ? 77.611  115.339 127.427 1.00 127.68 ? 526  VAL B CG1  1 
ATOM   3687 C CG2  . VAL A 1 526 ? 77.436  116.556 125.247 1.00 127.08 ? 526  VAL B CG2  1 
ATOM   3688 N N    . THR A 1 527 ? 81.235  115.956 127.741 1.00 126.61 ? 527  THR B N    1 
ATOM   3689 C CA   . THR A 1 527 ? 82.121  115.451 128.790 1.00 125.29 ? 527  THR B CA   1 
ATOM   3690 C C    . THR A 1 527 ? 82.731  116.584 129.611 1.00 125.23 ? 527  THR B C    1 
ATOM   3691 O O    . THR A 1 527 ? 82.809  116.492 130.843 1.00 123.70 ? 527  THR B O    1 
ATOM   3692 C CB   . THR A 1 527 ? 83.223  114.589 128.172 1.00 125.94 ? 527  THR B CB   1 
ATOM   3693 O OG1  . THR A 1 527 ? 82.636  113.594 127.325 1.00 126.67 ? 527  THR B OG1  1 
ATOM   3694 C CG2  . THR A 1 527 ? 84.036  113.898 129.258 1.00 125.66 ? 527  THR B CG2  1 
ATOM   3695 N N    . LEU A 1 528 ? 83.173  117.654 128.947 1.00 125.64 ? 528  LEU B N    1 
ATOM   3696 C CA   . LEU A 1 528 ? 83.746  118.795 129.657 1.00 124.43 ? 528  LEU B CA   1 
ATOM   3697 C C    . LEU A 1 528 ? 82.720  119.468 130.563 1.00 123.93 ? 528  LEU B C    1 
ATOM   3698 O O    . LEU A 1 528 ? 83.040  119.847 131.695 1.00 122.91 ? 528  LEU B O    1 
ATOM   3699 C CB   . LEU A 1 528 ? 84.318  119.802 128.660 1.00 124.85 ? 528  LEU B CB   1 
ATOM   3700 C CG   . LEU A 1 528 ? 85.577  119.385 127.899 1.00 123.60 ? 528  LEU B CG   1 
ATOM   3701 C CD1  . LEU A 1 528 ? 85.974  120.452 126.896 1.00 122.17 ? 528  LEU B CD1  1 
ATOM   3702 C CD2  . LEU A 1 528 ? 86.713  119.127 128.868 1.00 124.17 ? 528  LEU B CD2  1 
ATOM   3703 N N    . PHE A 1 529 ? 81.482  119.623 130.084 1.00 133.65 ? 529  PHE B N    1 
ATOM   3704 C CA   . PHE A 1 529 ? 80.445  120.287 130.873 1.00 133.26 ? 529  PHE B CA   1 
ATOM   3705 C C    . PHE A 1 529 ? 80.135  119.531 132.163 1.00 133.03 ? 529  PHE B C    1 
ATOM   3706 O O    . PHE A 1 529 ? 79.959  120.148 133.220 1.00 132.32 ? 529  PHE B O    1 
ATOM   3707 C CB   . PHE A 1 529 ? 79.176  120.448 130.037 1.00 133.81 ? 529  PHE B CB   1 
ATOM   3708 C CG   . PHE A 1 529 ? 78.050  121.121 130.770 1.00 134.37 ? 529  PHE B CG   1 
ATOM   3709 C CD1  . PHE A 1 529 ? 78.077  122.487 131.006 1.00 133.81 ? 529  PHE B CD1  1 
ATOM   3710 C CD2  . PHE A 1 529 ? 76.963  120.390 131.222 1.00 134.49 ? 529  PHE B CD2  1 
ATOM   3711 C CE1  . PHE A 1 529 ? 77.040  123.110 131.679 1.00 132.58 ? 529  PHE B CE1  1 
ATOM   3712 C CE2  . PHE A 1 529 ? 75.923  121.006 131.896 1.00 133.92 ? 529  PHE B CE2  1 
ATOM   3713 C CZ   . PHE A 1 529 ? 75.962  122.368 132.124 1.00 132.92 ? 529  PHE B CZ   1 
ATOM   3714 N N    . CYS A 1 530 ? 80.038  118.200 132.092 1.00 138.45 ? 530  CYS B N    1 
ATOM   3715 C CA   . CYS A 1 530 ? 79.773  117.410 133.294 1.00 138.65 ? 530  CYS B CA   1 
ATOM   3716 C C    . CYS A 1 530 ? 80.908  117.527 134.307 1.00 138.04 ? 530  CYS B C    1 
ATOM   3717 O O    . CYS A 1 530 ? 80.660  117.654 135.512 1.00 137.39 ? 530  CYS B O    1 
ATOM   3718 C CB   . CYS A 1 530 ? 79.540  115.947 132.919 1.00 139.59 ? 530  CYS B CB   1 
ATOM   3719 S SG   . CYS A 1 530 ? 78.184  115.676 131.751 1.00 140.77 ? 530  CYS B SG   1 
ATOM   3720 N N    . SER A 1 531 ? 82.158  117.469 133.840 1.00 130.74 ? 531  SER B N    1 
ATOM   3721 C CA   . SER A 1 531 ? 83.302  117.563 134.746 1.00 129.78 ? 531  SER B CA   1 
ATOM   3722 C C    . SER A 1 531 ? 83.383  118.930 135.421 1.00 129.40 ? 531  SER B C    1 
ATOM   3723 O O    . SER A 1 531 ? 83.670  119.016 136.620 1.00 128.64 ? 531  SER B O    1 
ATOM   3724 C CB   . SER A 1 531 ? 84.597  117.265 133.990 1.00 130.85 ? 531  SER B CB   1 
ATOM   3725 O OG   . SER A 1 531 ? 84.818  115.869 133.893 1.00 132.01 ? 531  SER B OG   1 
ATOM   3726 N N    . ILE A 1 532 ? 83.153  120.005 134.662 1.00 127.79 ? 532  ILE B N    1 
ATOM   3727 C CA   . ILE A 1 532 ? 83.242  121.360 135.210 1.00 127.36 ? 532  ILE B CA   1 
ATOM   3728 C C    . ILE A 1 532 ? 82.193  121.584 136.295 1.00 128.39 ? 532  ILE B C    1 
ATOM   3729 O O    . ILE A 1 532 ? 82.491  122.142 137.359 1.00 126.78 ? 532  ILE B O    1 
ATOM   3730 C CB   . ILE A 1 532 ? 83.123  122.402 134.080 1.00 125.95 ? 532  ILE B CB   1 
ATOM   3731 C CG1  . ILE A 1 532 ? 84.364  122.365 133.186 1.00 125.51 ? 532  ILE B CG1  1 
ATOM   3732 C CG2  . ILE A 1 532 ? 82.924  123.801 134.644 1.00 125.70 ? 532  ILE B CG2  1 
ATOM   3733 C CD1  . ILE A 1 532 ? 84.174  123.048 131.851 1.00 125.87 ? 532  ILE B CD1  1 
ATOM   3734 N N    . LEU A 1 533 ? 80.953  121.154 136.045 1.00 137.13 ? 533  LEU B N    1 
ATOM   3735 C CA   . LEU A 1 533 ? 79.898  121.296 137.045 1.00 135.40 ? 533  LEU B CA   1 
ATOM   3736 C C    . LEU A 1 533 ? 80.198  120.497 138.309 1.00 135.75 ? 533  LEU B C    1 
ATOM   3737 O O    . LEU A 1 533 ? 80.000  120.996 139.423 1.00 135.63 ? 533  LEU B O    1 
ATOM   3738 C CB   . LEU A 1 533 ? 78.557  120.868 136.447 1.00 134.26 ? 533  LEU B CB   1 
ATOM   3739 C CG   . LEU A 1 533 ? 77.438  120.476 137.415 1.00 134.39 ? 533  LEU B CG   1 
ATOM   3740 C CD1  . LEU A 1 533 ? 76.876  121.701 138.124 1.00 134.14 ? 533  LEU B CD1  1 
ATOM   3741 C CD2  . LEU A 1 533 ? 76.336  119.721 136.687 1.00 135.96 ? 533  LEU B CD2  1 
ATOM   3742 N N    . ILE A 1 534 ? 80.659  119.253 138.161 1.00 134.73 ? 534  ILE B N    1 
ATOM   3743 C CA   . ILE A 1 534 ? 80.964  118.431 139.330 1.00 133.16 ? 534  ILE B CA   1 
ATOM   3744 C C    . ILE A 1 534 ? 82.120  119.035 140.122 1.00 132.79 ? 534  ILE B C    1 
ATOM   3745 O O    . ILE A 1 534 ? 82.048  119.178 141.349 1.00 130.87 ? 534  ILE B O    1 
ATOM   3746 C CB   . ILE A 1 534 ? 81.262  116.983 138.898 1.00 133.43 ? 534  ILE B CB   1 
ATOM   3747 C CG1  . ILE A 1 534 ? 79.959  116.220 138.657 1.00 134.33 ? 534  ILE B CG1  1 
ATOM   3748 C CG2  . ILE A 1 534 ? 82.105  116.258 139.940 1.00 132.41 ? 534  ILE B CG2  1 
ATOM   3749 C CD1  . ILE A 1 534 ? 80.155  114.874 137.998 1.00 134.11 ? 534  ILE B CD1  1 
ATOM   3750 N N    . ALA A 1 535 ? 83.202  119.401 139.429 1.00 139.48 ? 535  ALA B N    1 
ATOM   3751 C CA   . ALA A 1 535 ? 84.348  120.020 140.089 1.00 139.59 ? 535  ALA B CA   1 
ATOM   3752 C C    . ALA A 1 535 ? 84.006  121.393 140.658 1.00 140.15 ? 535  ALA B C    1 
ATOM   3753 O O    . ALA A 1 535 ? 84.437  121.736 141.765 1.00 139.62 ? 535  ALA B O    1 
ATOM   3754 C CB   . ALA A 1 535 ? 85.523  120.118 139.117 1.00 136.47 ? 535  ALA B CB   1 
ATOM   3755 N N    . GLY A 1 536 ? 83.247  122.195 139.908 1.00 143.69 ? 536  GLY B N    1 
ATOM   3756 C CA   . GLY A 1 536 ? 82.913  123.537 140.361 1.00 142.52 ? 536  GLY B CA   1 
ATOM   3757 C C    . GLY A 1 536 ? 82.040  123.570 141.601 1.00 143.79 ? 536  GLY B C    1 
ATOM   3758 O O    . GLY A 1 536 ? 82.268  124.381 142.504 1.00 143.47 ? 536  GLY B O    1 
ATOM   3759 N N    . ILE A 1 537 ? 81.013  122.717 141.649 1.00 145.06 ? 537  ILE B N    1 
ATOM   3760 C CA   . ILE A 1 537 ? 80.063  122.740 142.761 1.00 143.28 ? 537  ILE B CA   1 
ATOM   3761 C C    . ILE A 1 537 ? 80.758  122.405 144.075 1.00 145.34 ? 537  ILE B C    1 
ATOM   3762 O O    . ILE A 1 537 ? 80.492  123.029 145.110 1.00 144.78 ? 537  ILE B O    1 
ATOM   3763 C CB   . ILE A 1 537 ? 78.892  121.780 142.483 1.00 142.72 ? 537  ILE B CB   1 
ATOM   3764 N N    . SER A 1 538 ? 81.644  121.405 144.060 1.00 150.88 ? 538  SER B N    1 
ATOM   3765 C CA   . SER A 1 538 ? 82.345  121.012 145.279 1.00 150.08 ? 538  SER B CA   1 
ATOM   3766 C C    . SER A 1 538 ? 83.265  122.119 145.784 1.00 150.04 ? 538  SER B C    1 
ATOM   3767 O O    . SER A 1 538 ? 83.371  122.336 146.997 1.00 148.87 ? 538  SER B O    1 
ATOM   3768 C CB   . SER A 1 538 ? 83.138  119.729 145.032 1.00 148.06 ? 538  SER B CB   1 
ATOM   3769 N N    . LEU A 1 539 ? 83.952  122.811 144.870 1.00 154.85 ? 539  LEU B N    1 
ATOM   3770 C CA   . LEU A 1 539 ? 84.942  123.809 145.270 1.00 154.67 ? 539  LEU B CA   1 
ATOM   3771 C C    . LEU A 1 539 ? 84.296  124.993 145.982 1.00 155.36 ? 539  LEU B C    1 
ATOM   3772 O O    . LEU A 1 539 ? 84.803  125.464 147.007 1.00 155.78 ? 539  LEU B O    1 
ATOM   3773 C CB   . LEU A 1 539 ? 85.730  124.281 144.048 1.00 153.55 ? 539  LEU B CB   1 
ATOM   3774 N N    . MET A 1 540 ? 83.181  125.499 145.443 1.00 157.77 ? 540  MET B N    1 
ATOM   3775 C CA   . MET A 1 540 ? 82.470  126.596 146.095 1.00 157.50 ? 540  MET B CA   1 
ATOM   3776 C C    . MET A 1 540 ? 81.893  126.184 147.443 1.00 157.43 ? 540  MET B C    1 
ATOM   3777 O O    . MET A 1 540 ? 81.736  127.028 148.333 1.00 157.58 ? 540  MET B O    1 
ATOM   3778 C CB   . MET A 1 540 ? 81.360  127.116 145.182 1.00 156.91 ? 540  MET B CB   1 
ATOM   3779 N N    . CYS A 1 541 ? 81.569  124.900 147.609 1.00 157.84 ? 541  CYS B N    1 
ATOM   3780 C CA   . CYS A 1 541 ? 81.098  124.407 148.898 1.00 158.53 ? 541  CYS B CA   1 
ATOM   3781 C C    . CYS A 1 541 ? 82.198  124.432 149.952 1.00 159.95 ? 541  CYS B C    1 
ATOM   3782 O O    . CYS A 1 541 ? 81.918  124.675 151.130 1.00 159.78 ? 541  CYS B O    1 
ATOM   3783 C CB   . CYS A 1 541 ? 80.535  122.996 148.741 1.00 157.66 ? 541  CYS B CB   1 
ATOM   3784 N N    . MET A 1 542 ? 83.445  124.174 149.547 1.00 164.46 ? 542  MET B N    1 
ATOM   3785 C CA   . MET A 1 542 ? 84.571  124.207 150.479 1.00 164.44 ? 542  MET B CA   1 
ATOM   3786 C C    . MET A 1 542 ? 84.777  125.600 151.063 1.00 164.07 ? 542  MET B C    1 
ATOM   3787 O O    . MET A 1 542 ? 85.013  125.746 152.268 1.00 162.83 ? 542  MET B O    1 
ATOM   3788 C CB   . MET A 1 542 ? 85.842  123.727 149.780 1.00 162.87 ? 542  MET B CB   1 
ATOM   3789 N N    . ASN A 1 543 ? 84.715  126.631 150.217 1.00 165.03 ? 543  ASN B N    1 
ATOM   3790 C CA   . ASN A 1 543 ? 84.888  128.004 150.684 1.00 164.93 ? 543  ASN B CA   1 
ATOM   3791 C C    . ASN A 1 543 ? 83.792  128.409 151.664 1.00 165.25 ? 543  ASN B C    1 
ATOM   3792 O O    . ASN A 1 543 ? 84.071  129.041 152.690 1.00 165.22 ? 543  ASN B O    1 
ATOM   3793 C CB   . ASN A 1 543 ? 84.921  128.962 149.493 1.00 164.30 ? 543  ASN B CB   1 
ATOM   3794 N N    . GLN A 1 544 ? 82.538  128.066 151.361 1.00 166.11 ? 544  GLN B N    1 
ATOM   3795 C CA   . GLN A 1 544 ? 81.444  128.397 152.270 1.00 166.22 ? 544  GLN B CA   1 
ATOM   3796 C C    . GLN A 1 544 ? 81.528  127.599 153.568 1.00 167.01 ? 544  GLN B C    1 
ATOM   3797 O O    . GLN A 1 544 ? 81.322  128.154 154.654 1.00 167.76 ? 544  GLN B O    1 
ATOM   3798 C CB   . GLN A 1 544 ? 80.101  128.159 151.581 1.00 164.86 ? 544  GLN B CB   1 
ATOM   3799 N N    . THR A 1 545 ? 81.810  126.301 153.479 1.00 167.04 ? 545  THR B N    1 
ATOM   3800 C CA   . THR A 1 545 ? 81.873  125.441 154.661 1.00 167.26 ? 545  THR B CA   1 
ATOM   3801 C C    . THR A 1 545 ? 83.003  125.852 155.603 1.00 166.59 ? 545  THR B C    1 
ATOM   3802 O O    . THR A 1 545 ? 82.770  126.495 156.626 1.00 166.28 ? 545  THR B O    1 
ATOM   3803 C CB   . THR A 1 545 ? 82.062  123.961 154.281 1.00 165.83 ? 545  THR B CB   1 
ATOM   3804 N N    . GLN A 1 654 ? 98.463  117.702 150.700 1.00 104.63 ? 654  GLN B N    1 
ATOM   3805 C CA   . GLN A 1 654 ? 98.337  118.936 151.466 1.00 104.14 ? 654  GLN B CA   1 
ATOM   3806 C C    . GLN A 1 654 ? 97.349  119.907 150.813 1.00 107.47 ? 654  GLN B C    1 
ATOM   3807 O O    . GLN A 1 654 ? 97.426  120.172 149.612 1.00 109.55 ? 654  GLN B O    1 
ATOM   3808 C CB   . GLN A 1 654 ? 99.717  119.590 151.647 1.00 104.56 ? 654  GLN B CB   1 
ATOM   3809 C CG   . GLN A 1 654 ? 100.466 119.901 150.355 1.00 104.56 ? 654  GLN B CG   1 
ATOM   3810 C CD   . GLN A 1 654 ? 101.971 119.776 150.503 1.00 103.53 ? 654  GLN B CD   1 
ATOM   3811 O OE1  . GLN A 1 654 ? 102.489 119.656 151.613 1.00 106.28 ? 654  GLN B OE1  1 
ATOM   3812 N NE2  . GLN A 1 654 ? 102.680 119.803 149.381 1.00 102.49 ? 654  GLN B NE2  1 
ATOM   3813 N N    . LEU A 1 655 ? 96.386  120.375 151.618 1.00 106.86 ? 655  LEU B N    1 
ATOM   3814 C CA   . LEU A 1 655 ? 95.325  121.256 151.128 1.00 107.46 ? 655  LEU B CA   1 
ATOM   3815 C C    . LEU A 1 655 ? 95.900  122.503 150.467 1.00 106.83 ? 655  LEU B C    1 
ATOM   3816 O O    . LEU A 1 655 ? 95.564  122.806 149.316 1.00 108.94 ? 655  LEU B O    1 
ATOM   3817 C CB   . LEU A 1 655 ? 94.401  121.651 152.282 1.00 106.80 ? 655  LEU B CB   1 
ATOM   3818 C CG   . LEU A 1 655 ? 93.677  120.560 153.080 1.00 106.82 ? 655  LEU B CG   1 
ATOM   3819 C CD1  . LEU A 1 655 ? 92.435  121.129 153.750 1.00 106.55 ? 655  LEU B CD1  1 
ATOM   3820 C CD2  . LEU A 1 655 ? 93.319  119.351 152.230 1.00 106.84 ? 655  LEU B CD2  1 
ATOM   3821 N N    . THR A 1 656 ? 96.716  123.249 151.225 1.00 104.23 ? 656  THR B N    1 
ATOM   3822 C CA   . THR A 1 656 ? 97.354  124.515 150.843 1.00 106.98 ? 656  THR B CA   1 
ATOM   3823 C C    . THR A 1 656 ? 97.781  124.567 149.373 1.00 105.34 ? 656  THR B C    1 
ATOM   3824 O O    . THR A 1 656 ? 97.664  125.614 148.724 1.00 103.98 ? 656  THR B O    1 
ATOM   3825 C CB   . THR A 1 656 ? 98.549  124.771 151.765 1.00 109.74 ? 656  THR B CB   1 
ATOM   3826 O OG1  . THR A 1 656 ? 98.083  124.908 153.112 1.00 108.82 ? 656  THR B OG1  1 
ATOM   3827 C CG2  . THR A 1 656 ? 99.269  126.050 151.383 1.00 107.25 ? 656  THR B CG2  1 
ATOM   3828 N N    . ARG A 1 657 ? 98.222  123.438 148.812 1.00 100.88 ? 657  ARG B N    1 
ATOM   3829 C CA   . ARG A 1 657 ? 98.617  123.412 147.407 1.00 101.20 ? 657  ARG B CA   1 
ATOM   3830 C C    . ARG A 1 657 ? 97.556  122.767 146.523 1.00 102.55 ? 657  ARG B C    1 
ATOM   3831 O O    . ARG A 1 657 ? 97.110  123.393 145.554 1.00 102.93 ? 657  ARG B O    1 
ATOM   3832 C CB   . ARG A 1 657 ? 99.953  122.683 147.254 1.00 101.68 ? 657  ARG B CB   1 
ATOM   3833 C CG   . ARG A 1 657 ? 100.966 123.005 148.335 1.00 101.23 ? 657  ARG B CG   1 
ATOM   3834 C CD   . ARG A 1 657 ? 101.866 124.149 147.905 1.00 101.23 ? 657  ARG B CD   1 
ATOM   3835 N NE   . ARG A 1 657 ? 102.850 124.486 148.926 1.00 106.16 ? 657  ARG B NE   1 
ATOM   3836 C CZ   . ARG A 1 657 ? 103.939 125.209 148.704 1.00 104.67 ? 657  ARG B CZ   1 
ATOM   3837 N NH1  . ARG A 1 657 ? 104.214 125.693 147.504 1.00 101.45 ? 657  ARG B NH1  1 
ATOM   3838 N NH2  . ARG A 1 657 ? 104.772 125.455 149.712 1.00 102.60 ? 657  ARG B NH2  1 
ATOM   3839 N N    . HIS A 1 658 ? 97.220  121.488 146.776 1.00 97.56  ? 658  HIS B N    1 
ATOM   3840 C CA   . HIS A 1 658 ? 96.191  120.710 146.069 1.00 98.43  ? 658  HIS B CA   1 
ATOM   3841 C C    . HIS A 1 658 ? 95.097  121.552 145.418 1.00 102.75 ? 658  HIS B C    1 
ATOM   3842 O O    . HIS A 1 658 ? 94.845  121.416 144.216 1.00 106.54 ? 658  HIS B O    1 
ATOM   3843 C CB   . HIS A 1 658 ? 95.521  119.722 147.029 1.00 99.27  ? 658  HIS B CB   1 
ATOM   3844 C CG   . HIS A 1 658 ? 96.144  118.361 147.041 1.00 99.86  ? 658  HIS B CG   1 
ATOM   3845 N ND1  . HIS A 1 658 ? 95.435  117.213 146.765 1.00 100.69 ? 658  HIS B ND1  1 
ATOM   3846 C CD2  . HIS A 1 658 ? 97.415  117.968 147.292 1.00 99.92  ? 658  HIS B CD2  1 
ATOM   3847 C CE1  . HIS A 1 658 ? 96.243  116.170 146.841 1.00 100.78 ? 658  HIS B CE1  1 
ATOM   3848 N NE2  . HIS A 1 658 ? 97.449  116.601 147.164 1.00 100.65 ? 658  HIS B NE2  1 
ATOM   3849 N N    . VAL A 1 659 ? 94.411  122.363 146.237 1.00 104.92 ? 659  VAL B N    1 
ATOM   3850 C CA   . VAL A 1 659 ? 93.301  123.211 145.793 1.00 105.67 ? 659  VAL B CA   1 
ATOM   3851 C C    . VAL A 1 659 ? 93.662  123.985 144.527 1.00 103.75 ? 659  VAL B C    1 
ATOM   3852 O O    . VAL A 1 659 ? 92.865  124.080 143.584 1.00 101.96 ? 659  VAL B O    1 
ATOM   3853 C CB   . VAL A 1 659 ? 92.877  124.160 146.932 1.00 106.06 ? 659  VAL B CB   1 
ATOM   3854 C CG1  . VAL A 1 659 ? 91.903  125.217 146.429 1.00 107.23 ? 659  VAL B CG1  1 
ATOM   3855 C CG2  . VAL A 1 659 ? 92.269  123.373 148.081 1.00 104.10 ? 659  VAL B CG2  1 
ATOM   3856 N N    . LEU A 1 660 ? 94.878  124.543 144.492 1.00 97.11  ? 660  LEU B N    1 
ATOM   3857 C CA   . LEU A 1 660 ? 95.318  125.365 143.366 1.00 98.02  ? 660  LEU B CA   1 
ATOM   3858 C C    . LEU A 1 660 ? 95.388  124.577 142.064 1.00 100.36 ? 660  LEU B C    1 
ATOM   3859 O O    . LEU A 1 660 ? 95.034  125.100 141.000 1.00 105.38 ? 660  LEU B O    1 
ATOM   3860 C CB   . LEU A 1 660 ? 96.678  125.991 143.675 1.00 98.95  ? 660  LEU B CB   1 
ATOM   3861 C CG   . LEU A 1 660 ? 96.755  127.517 143.764 1.00 100.58 ? 660  LEU B CG   1 
ATOM   3862 C CD1  . LEU A 1 660 ? 98.204  127.976 143.772 1.00 101.16 ? 660  LEU B CD1  1 
ATOM   3863 C CD2  . LEU A 1 660 ? 95.997  128.163 142.616 1.00 101.96 ? 660  LEU B CD2  1 
ATOM   3864 N N    . LEU A 1 661 ? 95.877  123.333 142.117 1.00 90.30  ? 661  LEU B N    1 
ATOM   3865 C CA   . LEU A 1 661 ? 95.898  122.496 140.920 1.00 92.25  ? 661  LEU B CA   1 
ATOM   3866 C C    . LEU A 1 661 ? 94.499  122.291 140.353 1.00 93.16  ? 661  LEU B C    1 
ATOM   3867 O O    . LEU A 1 661 ? 94.315  122.267 139.130 1.00 94.95  ? 661  LEU B O    1 
ATOM   3868 C CB   . LEU A 1 661 ? 96.550  121.150 141.238 1.00 89.96  ? 661  LEU B CB   1 
ATOM   3869 C CG   . LEU A 1 661 ? 96.721  120.166 140.079 1.00 87.98  ? 661  LEU B CG   1 
ATOM   3870 C CD1  . LEU A 1 661 ? 98.078  120.339 139.421 1.00 90.85  ? 661  LEU B CD1  1 
ATOM   3871 C CD2  . LEU A 1 661 ? 96.535  118.737 140.563 1.00 88.27  ? 661  LEU B CD2  1 
ATOM   3872 N N    . CYS A 1 662 ? 93.500  122.135 141.224 1.00 97.14  ? 662  CYS B N    1 
ATOM   3873 C CA   . CYS A 1 662 ? 92.115  122.102 140.766 1.00 99.31  ? 662  CYS B CA   1 
ATOM   3874 C C    . CYS A 1 662 ? 91.696  123.433 140.150 1.00 100.55 ? 662  CYS B C    1 
ATOM   3875 O O    . CYS A 1 662 ? 91.031  123.458 139.107 1.00 97.14  ? 662  CYS B O    1 
ATOM   3876 C CB   . CYS A 1 662 ? 91.191  121.732 141.925 1.00 96.57  ? 662  CYS B CB   1 
ATOM   3877 S SG   . CYS A 1 662 ? 90.901  119.958 142.106 1.00 98.27  ? 662  CYS B SG   1 
ATOM   3878 N N    . LEU A 1 663 ? 92.059  124.545 140.797 1.00 105.13 ? 663  LEU B N    1 
ATOM   3879 C CA   . LEU A 1 663 ? 91.658  125.869 140.323 1.00 103.87 ? 663  LEU B CA   1 
ATOM   3880 C C    . LEU A 1 663 ? 92.234  126.189 138.947 1.00 100.77 ? 663  LEU B C    1 
ATOM   3881 O O    . LEU A 1 663 ? 91.526  126.702 138.073 1.00 100.93 ? 663  LEU B O    1 
ATOM   3882 C CB   . LEU A 1 663 ? 92.079  126.930 141.339 1.00 102.17 ? 663  LEU B CB   1 
ATOM   3883 C CG   . LEU A 1 663 ? 91.487  128.329 141.159 1.00 102.47 ? 663  LEU B CG   1 
ATOM   3884 C CD1  . LEU A 1 663 ? 90.827  128.798 142.445 1.00 100.61 ? 663  LEU B CD1  1 
ATOM   3885 C CD2  . LEU A 1 663 ? 92.558  129.312 140.713 1.00 102.25 ? 663  LEU B CD2  1 
ATOM   3886 N N    . LEU A 1 664 ? 93.524  125.909 138.739 1.00 87.59  ? 664  LEU B N    1 
ATOM   3887 C CA   . LEU A 1 664 ? 94.129  126.178 137.437 1.00 87.28  ? 664  LEU B CA   1 
ATOM   3888 C C    . LEU A 1 664 ? 93.545  125.288 136.347 1.00 92.53  ? 664  LEU B C    1 
ATOM   3889 O O    . LEU A 1 664 ? 93.365  125.734 135.207 1.00 94.54  ? 664  LEU B O    1 
ATOM   3890 C CB   . LEU A 1 664 ? 95.645  126.004 137.511 1.00 86.97  ? 664  LEU B CB   1 
ATOM   3891 C CG   . LEU A 1 664 ? 96.428  127.163 138.130 1.00 87.10  ? 664  LEU B CG   1 
ATOM   3892 C CD1  . LEU A 1 664 ? 97.692  126.658 138.807 1.00 91.61  ? 664  LEU B CD1  1 
ATOM   3893 C CD2  . LEU A 1 664 ? 96.762  128.202 137.073 1.00 88.92  ? 664  LEU B CD2  1 
ATOM   3894 N N    . LEU A 1 665 ? 93.263  124.023 136.670 1.00 97.72  ? 665  LEU B N    1 
ATOM   3895 C CA   . LEU A 1 665 ? 92.684  123.112 135.686 1.00 98.51  ? 665  LEU B CA   1 
ATOM   3896 C C    . LEU A 1 665 ? 91.289  123.554 135.254 1.00 100.36 ? 665  LEU B C    1 
ATOM   3897 O O    . LEU A 1 665 ? 90.961  123.506 134.063 1.00 98.74  ? 665  LEU B O    1 
ATOM   3898 C CB   . LEU A 1 665 ? 92.651  121.689 136.243 1.00 96.91  ? 665  LEU B CB   1 
ATOM   3899 C CG   . LEU A 1 665 ? 93.934  120.867 136.085 1.00 98.84  ? 665  LEU B CG   1 
ATOM   3900 C CD1  . LEU A 1 665 ? 93.678  119.395 136.375 1.00 97.89  ? 665  LEU B CD1  1 
ATOM   3901 C CD2  . LEU A 1 665 ? 94.529  121.044 134.696 1.00 97.84  ? 665  LEU B CD2  1 
ATOM   3902 N N    . ILE A 1 666 ? 90.451  123.967 136.213 1.00 104.62 ? 666  ILE B N    1 
ATOM   3903 C CA   . ILE A 1 666 ? 89.093  124.416 135.903 1.00 103.52 ? 666  ILE B CA   1 
ATOM   3904 C C    . ILE A 1 666 ? 89.113  125.614 134.958 1.00 102.57 ? 666  ILE B C    1 
ATOM   3905 O O    . ILE A 1 666 ? 88.287  125.712 134.039 1.00 103.31 ? 666  ILE B O    1 
ATOM   3906 C CB   . ILE A 1 666 ? 88.335  124.718 137.212 1.00 100.85 ? 666  ILE B CB   1 
ATOM   3907 C CG1  . ILE A 1 666 ? 87.772  123.424 137.798 1.00 102.36 ? 666  ILE B CG1  1 
ATOM   3908 C CG2  . ILE A 1 666 ? 87.218  125.732 137.002 1.00 100.83 ? 666  ILE B CG2  1 
ATOM   3909 C CD1  . ILE A 1 666 ? 86.842  122.698 136.855 1.00 105.95 ? 666  ILE B CD1  1 
ATOM   3910 N N    . ILE A 1 667 ? 90.066  126.529 135.153 1.00 97.35  ? 667  ILE B N    1 
ATOM   3911 C CA   . ILE A 1 667 ? 90.254  127.640 134.222 1.00 94.98  ? 667  ILE B CA   1 
ATOM   3912 C C    . ILE A 1 667 ? 90.575  127.121 132.824 1.00 92.82  ? 667  ILE B C    1 
ATOM   3913 O O    . ILE A 1 667 ? 90.074  127.642 131.818 1.00 92.51  ? 667  ILE B O    1 
ATOM   3914 C CB   . ILE A 1 667 ? 91.347  128.590 134.754 1.00 95.54  ? 667  ILE B CB   1 
ATOM   3915 C CG1  . ILE A 1 667 ? 90.781  129.488 135.860 1.00 96.34  ? 667  ILE B CG1  1 
ATOM   3916 C CG2  . ILE A 1 667 ? 91.948  129.433 133.634 1.00 94.35  ? 667  ILE B CG2  1 
ATOM   3917 C CD1  . ILE A 1 667 ? 91.692  130.639 136.262 1.00 95.02  ? 667  ILE B CD1  1 
ATOM   3918 N N    . GLY A 1 668 ? 91.385  126.064 132.741 1.00 96.42  ? 668  GLY B N    1 
ATOM   3919 C CA   . GLY A 1 668 ? 91.715  125.489 131.448 1.00 99.65  ? 668  GLY B CA   1 
ATOM   3920 C C    . GLY A 1 668 ? 90.538  124.847 130.738 1.00 101.02 ? 668  GLY B C    1 
ATOM   3921 O O    . GLY A 1 668 ? 90.380  125.006 129.524 1.00 101.41 ? 668  GLY B O    1 
ATOM   3922 N N    . LEU A 1 669 ? 89.713  124.089 131.470 1.00 99.17  ? 669  LEU B N    1 
ATOM   3923 C CA   . LEU A 1 669 ? 88.587  123.412 130.829 1.00 97.41  ? 669  LEU B CA   1 
ATOM   3924 C C    . LEU A 1 669 ? 87.571  124.398 130.262 1.00 101.17 ? 669  LEU B C    1 
ATOM   3925 O O    . LEU A 1 669 ? 86.950  124.116 129.232 1.00 101.13 ? 669  LEU B O    1 
ATOM   3926 C CB   . LEU A 1 669 ? 87.881  122.473 131.814 1.00 95.44  ? 669  LEU B CB   1 
ATOM   3927 C CG   . LEU A 1 669 ? 88.345  121.054 132.179 1.00 98.92  ? 669  LEU B CG   1 
ATOM   3928 C CD1  . LEU A 1 669 ? 89.848  120.906 132.339 1.00 101.54 ? 669  LEU B CD1  1 
ATOM   3929 C CD2  . LEU A 1 669 ? 87.636  120.592 133.444 1.00 100.13 ? 669  LEU B CD2  1 
ATOM   3930 N N    . PHE A 1 670 ? 87.380  125.546 130.920 1.00 106.76 ? 670  PHE B N    1 
ATOM   3931 C CA   . PHE A 1 670 ? 86.460  126.553 130.397 1.00 104.58 ? 670  PHE B CA   1 
ATOM   3932 C C    . PHE A 1 670 ? 86.936  127.105 129.058 1.00 104.54 ? 670  PHE B C    1 
ATOM   3933 O O    . PHE A 1 670 ? 86.133  127.304 128.138 1.00 103.33 ? 670  PHE B O    1 
ATOM   3934 C CB   . PHE A 1 670 ? 86.289  127.681 131.411 1.00 104.93 ? 670  PHE B CB   1 
ATOM   3935 C CG   . PHE A 1 670 ? 85.005  127.607 132.184 1.00 105.73 ? 670  PHE B CG   1 
ATOM   3936 C CD1  . PHE A 1 670 ? 83.783  127.585 131.531 1.00 106.02 ? 670  PHE B CD1  1 
ATOM   3937 C CD2  . PHE A 1 670 ? 85.023  127.557 133.567 1.00 105.15 ? 670  PHE B CD2  1 
ATOM   3938 C CE1  . PHE A 1 670 ? 82.601  127.514 132.248 1.00 106.36 ? 670  PHE B CE1  1 
ATOM   3939 C CE2  . PHE A 1 670 ? 83.849  127.488 134.288 1.00 103.58 ? 670  PHE B CE2  1 
ATOM   3940 C CZ   . PHE A 1 670 ? 82.635  127.466 133.628 1.00 104.92 ? 670  PHE B CZ   1 
ATOM   3941 N N    . ALA A 1 671 ? 88.240  127.376 128.940 1.00 106.95 ? 671  ALA B N    1 
ATOM   3942 C CA   . ALA A 1 671 ? 88.794  127.881 127.688 1.00 105.66 ? 671  ALA B CA   1 
ATOM   3943 C C    . ALA A 1 671 ? 88.640  126.868 126.562 1.00 105.62 ? 671  ALA B C    1 
ATOM   3944 O O    . ALA A 1 671 ? 88.302  127.232 125.430 1.00 107.02 ? 671  ALA B O    1 
ATOM   3945 C CB   . ALA A 1 671 ? 90.264  128.252 127.876 1.00 104.80 ? 671  ALA B CB   1 
ATOM   3946 N N    . ASN A 1 672 ? 88.906  125.593 126.854 1.00 109.21 ? 672  ASN B N    1 
ATOM   3947 C CA   . ASN A 1 672 ? 88.741  124.544 125.853 1.00 109.06 ? 672  ASN B CA   1 
ATOM   3948 C C    . ASN A 1 672 ? 87.284  124.415 125.423 1.00 111.11 ? 672  ASN B C    1 
ATOM   3949 O O    . ASN A 1 672 ? 86.996  124.290 124.228 1.00 109.67 ? 672  ASN B O    1 
ATOM   3950 C CB   . ASN A 1 672 ? 89.261  123.216 126.408 1.00 108.56 ? 672  ASN B CB   1 
ATOM   3951 C CG   . ASN A 1 672 ? 89.698  122.244 125.320 1.00 108.13 ? 672  ASN B CG   1 
ATOM   3952 O OD1  . ASN A 1 672 ? 90.543  121.382 125.559 1.00 109.82 ? 672  ASN B OD1  1 
ATOM   3953 N ND2  . ASN A 1 672 ? 89.132  122.377 124.126 1.00 106.89 ? 672  ASN B ND2  1 
ATOM   3954 N N    . LEU A 1 673 ? 86.355  124.475 126.383 1.00 115.45 ? 673  LEU B N    1 
ATOM   3955 C CA   . LEU A 1 673 ? 84.935  124.299 126.085 1.00 113.41 ? 673  LEU B CA   1 
ATOM   3956 C C    . LEU A 1 673 ? 84.412  125.365 125.128 1.00 116.79 ? 673  LEU B C    1 
ATOM   3957 O O    . LEU A 1 673 ? 83.644  125.055 124.210 1.00 116.04 ? 673  LEU B O    1 
ATOM   3958 C CB   . LEU A 1 673 ? 84.127  124.303 127.384 1.00 111.66 ? 673  LEU B CB   1 
ATOM   3959 C CG   . LEU A 1 673 ? 82.604  124.246 127.252 1.00 112.74 ? 673  LEU B CG   1 
ATOM   3960 C CD1  . LEU A 1 673 ? 82.172  122.976 126.536 1.00 114.78 ? 673  LEU B CD1  1 
ATOM   3961 C CD2  . LEU A 1 673 ? 81.939  124.348 128.616 1.00 113.60 ? 673  LEU B CD2  1 
ATOM   3962 N N    . SER A 1 674 ? 84.795  126.628 125.340 1.00 119.17 ? 674  SER B N    1 
ATOM   3963 C CA   . SER A 1 674 ? 84.376  127.692 124.430 1.00 116.13 ? 674  SER B CA   1 
ATOM   3964 C C    . SER A 1 674 ? 84.891  127.458 123.013 1.00 116.15 ? 674  SER B C    1 
ATOM   3965 O O    . SER A 1 674 ? 84.213  127.802 122.037 1.00 115.62 ? 674  SER B O    1 
ATOM   3966 C CB   . SER A 1 674 ? 84.851  129.046 124.956 1.00 115.57 ? 674  SER B CB   1 
ATOM   3967 O OG   . SER A 1 674 ? 85.090  129.950 123.893 1.00 118.29 ? 674  SER B OG   1 
ATOM   3968 N N    . SER A 1 675 ? 86.095  126.895 122.879 1.00 118.54 ? 675  SER B N    1 
ATOM   3969 C CA   . SER A 1 675 ? 86.609  126.542 121.557 1.00 117.16 ? 675  SER B CA   1 
ATOM   3970 C C    . SER A 1 675 ? 85.737  125.482 120.894 1.00 117.14 ? 675  SER B C    1 
ATOM   3971 O O    . SER A 1 675 ? 85.460  125.554 119.691 1.00 118.89 ? 675  SER B O    1 
ATOM   3972 C CB   . SER A 1 675 ? 88.055  126.061 121.666 1.00 119.36 ? 675  SER B CB   1 
ATOM   3973 O OG   . SER A 1 675 ? 88.941  127.151 121.855 1.00 118.38 ? 675  SER B OG   1 
ATOM   3974 N N    . CYS A 1 676 ? 85.311  124.481 121.668 1.00 122.67 ? 676  CYS B N    1 
ATOM   3975 C CA   . CYS A 1 676 ? 84.398  123.460 121.164 1.00 124.45 ? 676  CYS B CA   1 
ATOM   3976 C C    . CYS A 1 676 ? 83.052  124.042 120.750 1.00 126.13 ? 676  CYS B C    1 
ATOM   3977 O O    . CYS A 1 676 ? 82.516  123.692 119.693 1.00 127.91 ? 676  CYS B O    1 
ATOM   3978 C CB   . CYS A 1 676 ? 84.194  122.347 122.196 1.00 125.35 ? 676  CYS B CB   1 
ATOM   3979 S SG   . CYS A 1 676 ? 85.668  121.785 123.066 1.00 128.64 ? 676  CYS B SG   1 
ATOM   3980 N N    . LEU A 1 677 ? 82.499  124.940 121.566 1.00 125.03 ? 677  LEU B N    1 
ATOM   3981 C CA   . LEU A 1 677 ? 81.186  125.515 121.286 1.00 125.62 ? 677  LEU B CA   1 
ATOM   3982 C C    . LEU A 1 677 ? 81.168  126.350 120.009 1.00 127.30 ? 677  LEU B C    1 
ATOM   3983 O O    . LEU A 1 677 ? 80.179  126.323 119.266 1.00 125.07 ? 677  LEU B O    1 
ATOM   3984 C CB   . LEU A 1 677 ? 80.762  126.360 122.489 1.00 124.62 ? 677  LEU B CB   1 
ATOM   3985 C CG   . LEU A 1 677 ? 79.303  126.678 122.797 1.00 123.72 ? 677  LEU B CG   1 
ATOM   3986 C CD1  . LEU A 1 677 ? 79.084  126.692 124.296 1.00 125.71 ? 677  LEU B CD1  1 
ATOM   3987 C CD2  . LEU A 1 677 ? 78.956  128.037 122.218 1.00 124.75 ? 677  LEU B CD2  1 
ATOM   3988 N N    . TRP A 1 678 ? 82.229  127.117 119.747 1.00 129.11 ? 678  TRP B N    1 
ATOM   3989 C CA   . TRP A 1 678 ? 82.243  127.987 118.571 1.00 125.45 ? 678  TRP B CA   1 
ATOM   3990 C C    . TRP A 1 678 ? 82.144  127.211 117.257 1.00 124.60 ? 678  TRP B C    1 
ATOM   3991 O O    . TRP A 1 678 ? 81.405  127.610 116.349 1.00 127.10 ? 678  TRP B O    1 
ATOM   3992 C CB   . TRP A 1 678 ? 83.512  128.840 118.578 1.00 124.53 ? 678  TRP B CB   1 
ATOM   3993 C CG   . TRP A 1 678 ? 83.403  130.117 117.799 1.00 125.53 ? 678  TRP B CG   1 
ATOM   3994 C CD1  . TRP A 1 678 ? 84.131  130.467 116.699 1.00 125.50 ? 678  TRP B CD1  1 
ATOM   3995 C CD2  . TRP A 1 678 ? 82.531  131.222 118.070 1.00 126.08 ? 678  TRP B CD2  1 
ATOM   3996 N NE1  . TRP A 1 678 ? 83.760  131.714 116.262 1.00 125.17 ? 678  TRP B NE1  1 
ATOM   3997 C CE2  . TRP A 1 678 ? 82.780  132.200 117.087 1.00 125.78 ? 678  TRP B CE2  1 
ATOM   3998 C CE3  . TRP A 1 678 ? 81.563  131.478 119.046 1.00 125.85 ? 678  TRP B CE3  1 
ATOM   3999 C CZ2  . TRP A 1 678 ? 82.096  133.413 117.050 1.00 125.93 ? 678  TRP B CZ2  1 
ATOM   4000 C CZ3  . TRP A 1 678 ? 80.884  132.683 119.007 1.00 126.27 ? 678  TRP B CZ3  1 
ATOM   4001 C CH2  . TRP A 1 678 ? 81.154  133.635 118.017 1.00 126.65 ? 678  TRP B CH2  1 
ATOM   4002 N N    . TRP A 1 679 ? 82.889  126.108 117.134 1.00 124.02 ? 679  TRP B N    1 
ATOM   4003 C CA   . TRP A 1 679 ? 82.903  125.334 115.892 1.00 124.56 ? 679  TRP B CA   1 
ATOM   4004 C C    . TRP A 1 679 ? 81.560  124.669 115.582 1.00 127.34 ? 679  TRP B C    1 
ATOM   4005 O O    . TRP A 1 679 ? 81.112  124.682 114.430 1.00 129.56 ? 679  TRP B O    1 
ATOM   4006 C CB   . TRP A 1 679 ? 84.024  124.293 115.946 1.00 123.33 ? 679  TRP B CB   1 
ATOM   4007 C CG   . TRP A 1 679 ? 84.118  123.412 114.728 1.00 125.99 ? 679  TRP B CG   1 
ATOM   4008 C CD1  . TRP A 1 679 ? 84.903  123.625 113.631 1.00 126.89 ? 679  TRP B CD1  1 
ATOM   4009 C CD2  . TRP A 1 679 ? 83.433  122.174 114.492 1.00 128.31 ? 679  TRP B CD2  1 
ATOM   4010 N NE1  . TRP A 1 679 ? 84.738  122.610 112.723 1.00 127.07 ? 679  TRP B NE1  1 
ATOM   4011 C CE2  . TRP A 1 679 ? 83.842  121.705 113.227 1.00 127.71 ? 679  TRP B CE2  1 
ATOM   4012 C CE3  . TRP A 1 679 ? 82.509  121.421 115.223 1.00 128.06 ? 679  TRP B CE3  1 
ATOM   4013 C CZ2  . TRP A 1 679 ? 83.360  120.520 112.679 1.00 126.93 ? 679  TRP B CZ2  1 
ATOM   4014 C CZ3  . TRP A 1 679 ? 82.030  120.245 114.675 1.00 126.75 ? 679  TRP B CZ3  1 
ATOM   4015 C CH2  . TRP A 1 679 ? 82.457  119.806 113.417 1.00 126.81 ? 679  TRP B CH2  1 
ATOM   4016 N N    . LEU A 1 680 ? 80.910  124.076 116.589 1.00 133.61 ? 680  LEU B N    1 
ATOM   4017 C CA   . LEU A 1 680 ? 79.689  123.300 116.351 1.00 134.42 ? 680  LEU B CA   1 
ATOM   4018 C C    . LEU A 1 680 ? 78.495  124.159 115.933 1.00 135.82 ? 680  LEU B C    1 
ATOM   4019 O O    . LEU A 1 680 ? 77.647  123.692 115.164 1.00 135.09 ? 680  LEU B O    1 
ATOM   4020 C CB   . LEU A 1 680 ? 79.358  122.441 117.575 1.00 135.48 ? 680  LEU B CB   1 
ATOM   4021 C CG   . LEU A 1 680 ? 78.901  123.013 118.911 1.00 137.90 ? 680  LEU B CG   1 
ATOM   4022 C CD1  . LEU A 1 680 ? 77.417  122.793 119.021 1.00 137.06 ? 680  LEU B CD1  1 
ATOM   4023 C CD2  . LEU A 1 680 ? 79.613  122.323 120.057 1.00 135.96 ? 680  LEU B CD2  1 
ATOM   4024 N N    . PHE A 1 681 ? 78.402  125.399 116.412 1.00 136.64 ? 681  PHE B N    1 
ATOM   4025 C CA   . PHE A 1 681 ? 77.231  126.240 116.169 1.00 137.06 ? 681  PHE B CA   1 
ATOM   4026 C C    . PHE A 1 681 ? 77.331  127.129 114.937 1.00 137.06 ? 681  PHE B C    1 
ATOM   4027 O O    . PHE A 1 681 ? 76.287  127.530 114.410 1.00 138.16 ? 681  PHE B O    1 
ATOM   4028 C CB   . PHE A 1 681 ? 76.897  127.122 117.378 1.00 135.99 ? 681  PHE B CB   1 
ATOM   4029 C CG   . PHE A 1 681 ? 76.364  126.370 118.564 1.00 137.44 ? 681  PHE B CG   1 
ATOM   4030 C CD1  . PHE A 1 681 ? 75.204  125.619 118.443 1.00 138.33 ? 681  PHE B CD1  1 
ATOM   4031 C CD2  . PHE A 1 681 ? 76.980  126.443 119.797 1.00 137.45 ? 681  PHE B CD2  1 
ATOM   4032 C CE1  . PHE A 1 681 ? 74.679  124.941 119.527 1.00 138.87 ? 681  PHE B CE1  1 
ATOM   4033 C CE2  . PHE A 1 681 ? 76.462  125.761 120.886 1.00 137.03 ? 681  PHE B CE2  1 
ATOM   4034 C CZ   . PHE A 1 681 ? 75.311  125.010 120.751 1.00 138.42 ? 681  PHE B CZ   1 
ATOM   4035 N N    . ASN A 1 682 ? 78.525  127.455 114.452 1.00 131.22 ? 682  ASN B N    1 
ATOM   4036 C CA   . ASN A 1 682 ? 78.635  128.326 113.285 1.00 131.22 ? 682  ASN B CA   1 
ATOM   4037 C C    . ASN A 1 682 ? 79.173  127.518 112.107 1.00 131.76 ? 682  ASN B C    1 
ATOM   4038 O O    . ASN A 1 682 ? 80.365  127.532 111.794 1.00 131.17 ? 682  ASN B O    1 
ATOM   4039 C CB   . ASN A 1 682 ? 79.527  129.531 113.596 1.00 133.00 ? 682  ASN B CB   1 
ATOM   4040 C CG   . ASN A 1 682 ? 78.924  130.447 114.641 1.00 132.56 ? 682  ASN B CG   1 
ATOM   4041 O OD1  . ASN A 1 682 ? 77.718  130.694 114.644 1.00 132.76 ? 682  ASN B OD1  1 
ATOM   4042 N ND2  . ASN A 1 682 ? 79.762  130.960 115.534 1.00 131.42 ? 682  ASN B ND2  1 
ATOM   4043 N N    . GLN A 1 683 ? 78.242  126.830 111.437 1.00 138.25 ? 683  GLN B N    1 
ATOM   4044 C CA   . GLN A 1 683 ? 78.431  125.966 110.274 1.00 139.70 ? 683  GLN B CA   1 
ATOM   4045 C C    . GLN A 1 683 ? 79.686  125.101 110.296 1.00 140.53 ? 683  GLN B C    1 
ATOM   4046 O O    . GLN A 1 683 ? 80.061  124.541 111.331 1.00 140.36 ? 683  GLN B O    1 
ATOM   4047 C CB   . GLN A 1 683 ? 78.432  126.820 109.003 1.00 138.29 ? 683  GLN B CB   1 
ATOM   4048 N N    . GLU A 1 684 ? 80.327  125.000 109.143 1.00 142.37 ? 684  GLU B N    1 
ATOM   4049 C CA   . GLU A 1 684 ? 81.535  124.266 108.817 1.00 142.18 ? 684  GLU B CA   1 
ATOM   4050 C C    . GLU A 1 684 ? 82.723  125.211 108.777 1.00 142.90 ? 684  GLU B C    1 
ATOM   4051 O O    . GLU A 1 684 ? 82.710  126.193 108.027 1.00 142.28 ? 684  GLU B O    1 
ATOM   4052 C CB   . GLU A 1 684 ? 81.385  123.560 107.465 1.00 139.23 ? 684  GLU B CB   1 
ATOM   4053 N N    . PRO A 1 685 ? 83.738  124.969 109.660 1.00 145.07 ? 685  PRO B N    1 
ATOM   4054 C CA   . PRO A 1 685 ? 84.994  125.751 109.673 1.00 143.38 ? 685  PRO B CA   1 
ATOM   4055 C C    . PRO A 1 685 ? 84.810  127.227 110.003 1.00 143.31 ? 685  PRO B C    1 
ATOM   4056 O O    . PRO A 1 685 ? 84.323  128.024 109.196 1.00 143.05 ? 685  PRO B O    1 
ATOM   4057 C CB   . PRO A 1 685 ? 85.590  125.528 108.272 1.00 141.73 ? 685  PRO B CB   1 
ATOM   4058 N N    . GLY A 1 686 ? 85.253  127.597 111.198 1.00 142.94 ? 686  GLY B N    1 
ATOM   4059 C CA   . GLY A 1 686 ? 85.119  128.948 111.693 1.00 142.24 ? 686  GLY B CA   1 
ATOM   4060 C C    . GLY A 1 686 ? 86.104  129.883 111.020 1.00 142.67 ? 686  GLY B C    1 
ATOM   4061 O O    . GLY A 1 686 ? 86.890  129.500 110.153 1.00 142.88 ? 686  GLY B O    1 
ATOM   4062 N N    . ARG A 1 687 ? 86.037  131.158 111.421 1.00 139.34 ? 687  ARG B N    1 
ATOM   4063 C CA   . ARG A 1 687 ? 86.932  132.156 110.843 1.00 138.68 ? 687  ARG B CA   1 
ATOM   4064 C C    . ARG A 1 687 ? 88.394  131.844 111.135 1.00 139.26 ? 687  ARG B C    1 
ATOM   4065 O O    . ARG A 1 687 ? 89.276  132.248 110.369 1.00 138.48 ? 687  ARG B O    1 
ATOM   4066 C CB   . ARG A 1 687 ? 86.572  133.547 111.367 1.00 138.46 ? 687  ARG B CB   1 
ATOM   4067 N N    . LEU A 1 688 ? 88.678  131.131 112.233 1.00 132.28 ? 688  LEU B N    1 
ATOM   4068 C CA   . LEU A 1 688 ? 90.043  130.701 112.529 1.00 131.69 ? 688  LEU B CA   1 
ATOM   4069 C C    . LEU A 1 688 ? 89.949  129.251 113.012 1.00 131.30 ? 688  LEU B C    1 
ATOM   4070 O O    . LEU A 1 688 ? 89.978  128.970 114.213 1.00 130.40 ? 688  LEU B O    1 
ATOM   4071 C CB   . LEU A 1 688 ? 90.705  131.612 113.560 1.00 128.53 ? 688  LEU B CB   1 
ATOM   4072 N N    . TYR A 1 689 ? 89.825  128.321 112.060 1.00 118.88 ? 689  TYR B N    1 
ATOM   4073 C CA   . TYR A 1 689 ? 89.856  126.902 112.404 1.00 116.51 ? 689  TYR B CA   1 
ATOM   4074 C C    . TYR A 1 689 ? 91.226  126.481 112.921 1.00 115.27 ? 689  TYR B C    1 
ATOM   4075 O O    . TYR A 1 689 ? 91.325  125.689 113.866 1.00 115.87 ? 689  TYR B O    1 
ATOM   4076 C CB   . TYR A 1 689 ? 89.459  126.061 111.191 1.00 114.54 ? 689  TYR B CB   1 
ATOM   4077 N N    . VAL A 1 690 ? 92.290  126.989 112.294 1.00 97.63  ? 690  VAL B N    1 
ATOM   4078 C CA   . VAL A 1 690 ? 93.654  126.662 112.703 1.00 95.33  ? 690  VAL B CA   1 
ATOM   4079 C C    . VAL A 1 690 ? 93.935  127.148 114.119 1.00 96.36  ? 690  VAL B C    1 
ATOM   4080 O O    . VAL A 1 690 ? 94.537  126.432 114.929 1.00 97.90  ? 690  VAL B O    1 
ATOM   4081 C CB   . VAL A 1 690 ? 94.661  127.241 111.693 1.00 97.01  ? 690  VAL B CB   1 
ATOM   4082 C CG1  . VAL A 1 690 ? 96.081  126.875 112.087 1.00 96.80  ? 690  VAL B CG1  1 
ATOM   4083 C CG2  . VAL A 1 690 ? 94.347  126.741 110.292 1.00 97.56  ? 690  VAL B CG2  1 
ATOM   4084 N N    . GLU A 1 691 ? 93.506  128.372 114.437 1.00 99.01  ? 691  GLU B N    1 
ATOM   4085 C CA   . GLU A 1 691 ? 93.655  128.903 115.790 1.00 101.46 ? 691  GLU B CA   1 
ATOM   4086 C C    . GLU A 1 691 ? 92.891  128.083 116.822 1.00 102.75 ? 691  GLU B C    1 
ATOM   4087 O O    . GLU A 1 691 ? 93.401  127.840 117.923 1.00 102.34 ? 691  GLU B O    1 
ATOM   4088 C CB   . GLU A 1 691 ? 93.213  130.365 115.834 1.00 100.36 ? 691  GLU B CB   1 
ATOM   4089 C CG   . GLU A 1 691 ? 94.295  131.362 115.438 1.00 101.49 ? 691  GLU B CG   1 
ATOM   4090 C CD   . GLU A 1 691 ? 94.710  131.246 113.983 1.00 103.15 ? 691  GLU B CD   1 
ATOM   4091 O OE1  . GLU A 1 691 ? 93.879  130.829 113.150 1.00 103.42 ? 691  GLU B OE1  1 
ATOM   4092 O OE2  . GLU A 1 691 ? 95.874  131.574 113.673 1.00 102.81 ? 691  GLU B OE2  1 
ATOM   4093 N N    . LEU A 1 692 ? 91.657  127.676 116.507 1.00 101.16 ? 692  LEU B N    1 
ATOM   4094 C CA   . LEU A 1 692 ? 90.890  126.883 117.463 1.00 101.11 ? 692  LEU B CA   1 
ATOM   4095 C C    . LEU A 1 692 ? 91.559  125.538 117.721 1.00 99.14  ? 692  LEU B C    1 
ATOM   4096 O O    . LEU A 1 692 ? 91.723  125.130 118.876 1.00 98.53  ? 692  LEU B O    1 
ATOM   4097 C CB   . LEU A 1 692 ? 89.464  126.684 116.951 1.00 99.70  ? 692  LEU B CB   1 
ATOM   4098 C CG   . LEU A 1 692 ? 88.525  127.886 117.056 1.00 101.57 ? 692  LEU B CG   1 
ATOM   4099 C CD1  . LEU A 1 692 ? 87.130  127.515 116.579 1.00 103.34 ? 692  LEU B CD1  1 
ATOM   4100 C CD2  . LEU A 1 692 ? 88.486  128.412 118.482 1.00 101.08 ? 692  LEU B CD2  1 
ATOM   4101 N N    . GLN A 1 693 ? 91.945  124.834 116.652 1.00 86.35  ? 693  GLN B N    1 
ATOM   4102 C CA   . GLN A 1 693 ? 92.579  123.526 116.802 1.00 86.12  ? 693  GLN B CA   1 
ATOM   4103 C C    . GLN A 1 693 ? 93.892  123.632 117.569 1.00 84.81  ? 693  GLN B C    1 
ATOM   4104 O O    . GLN A 1 693 ? 94.216  122.767 118.392 1.00 85.45  ? 693  GLN B O    1 
ATOM   4105 C CB   . GLN A 1 693 ? 92.812  122.885 115.434 1.00 88.05  ? 693  GLN B CB   1 
ATOM   4106 C CG   . GLN A 1 693 ? 91.645  122.054 114.928 1.00 85.99  ? 693  GLN B CG   1 
ATOM   4107 C CD   . GLN A 1 693 ? 91.716  121.797 113.436 1.00 85.88  ? 693  GLN B CD   1 
ATOM   4108 O OE1  . GLN A 1 693 ? 92.762  121.415 112.909 1.00 86.45  ? 693  GLN B OE1  1 
ATOM   4109 N NE2  . GLN A 1 693 ? 90.601  122.003 112.745 1.00 86.89  ? 693  GLN B NE2  1 
ATOM   4110 N N    . PHE A 1 694 ? 94.667  124.683 117.288 1.00 76.15  ? 694  PHE B N    1 
ATOM   4111 C CA   . PHE A 1 694 ? 95.907  124.949 118.011 1.00 77.54  ? 694  PHE B CA   1 
ATOM   4112 C C    . PHE A 1 694 ? 95.682  125.129 119.509 1.00 80.14  ? 694  PHE B C    1 
ATOM   4113 O O    . PHE A 1 694 ? 96.529  124.730 120.316 1.00 85.91  ? 694  PHE B O    1 
ATOM   4114 C CB   . PHE A 1 694 ? 96.576  126.191 117.419 1.00 79.20  ? 694  PHE B CB   1 
ATOM   4115 C CG   . PHE A 1 694 ? 97.911  126.522 118.022 1.00 77.54  ? 694  PHE B CG   1 
ATOM   4116 C CD1  . PHE A 1 694 ? 99.067  125.946 117.528 1.00 72.59  ? 694  PHE B CD1  1 
ATOM   4117 C CD2  . PHE A 1 694 ? 98.013  127.429 119.064 1.00 76.73  ? 694  PHE B CD2  1 
ATOM   4118 C CE1  . PHE A 1 694 ? 100.295 126.258 118.071 1.00 72.16  ? 694  PHE B CE1  1 
ATOM   4119 C CE2  . PHE A 1 694 ? 99.239  127.738 119.614 1.00 76.18  ? 694  PHE B CE2  1 
ATOM   4120 C CZ   . PHE A 1 694 ? 100.382 127.151 119.117 1.00 76.18  ? 694  PHE B CZ   1 
ATOM   4121 N N    . PHE A 1 695 ? 94.561  125.740 119.906 1.00 84.98  ? 695  PHE B N    1 
ATOM   4122 C CA   . PHE A 1 695 ? 94.284  125.878 121.335 1.00 87.69  ? 695  PHE B CA   1 
ATOM   4123 C C    . PHE A 1 695 ? 94.055  124.529 122.009 1.00 87.90  ? 695  PHE B C    1 
ATOM   4124 O O    . PHE A 1 695 ? 94.519  124.313 123.135 1.00 86.96  ? 695  PHE B O    1 
ATOM   4125 C CB   . PHE A 1 695 ? 93.081  126.796 121.553 1.00 86.89  ? 695  PHE B CB   1 
ATOM   4126 C CG   . PHE A 1 695 ? 93.431  128.258 121.603 1.00 86.05  ? 695  PHE B CG   1 
ATOM   4127 C CD1  . PHE A 1 695 ? 94.564  128.742 120.969 1.00 84.73  ? 695  PHE B CD1  1 
ATOM   4128 C CD2  . PHE A 1 695 ? 92.624  129.149 122.293 1.00 87.65  ? 695  PHE B CD2  1 
ATOM   4129 C CE1  . PHE A 1 695 ? 94.885  130.086 121.018 1.00 88.95  ? 695  PHE B CE1  1 
ATOM   4130 C CE2  . PHE A 1 695 ? 92.939  130.495 122.346 1.00 89.44  ? 695  PHE B CE2  1 
ATOM   4131 C CZ   . PHE A 1 695 ? 94.071  130.964 121.707 1.00 89.92  ? 695  PHE B CZ   1 
ATOM   4132 N N    . CYS A 1 696 ? 93.326  123.620 121.355 1.00 85.23  ? 696  CYS B N    1 
ATOM   4133 C CA   . CYS A 1 696 ? 93.097  122.302 121.941 1.00 84.68  ? 696  CYS B CA   1 
ATOM   4134 C C    . CYS A 1 696 ? 94.399  121.529 122.105 1.00 82.39  ? 696  CYS B C    1 
ATOM   4135 O O    . CYS A 1 696 ? 94.619  120.882 123.133 1.00 85.82  ? 696  CYS B O    1 
ATOM   4136 C CB   . CYS A 1 696 ? 92.104  121.498 121.099 1.00 87.65  ? 696  CYS B CB   1 
ATOM   4137 S SG   . CYS A 1 696 ? 90.838  122.459 120.250 1.00 90.73  ? 696  CYS B SG   1 
ATOM   4138 N N    . ALA A 1 697 ? 95.275  121.600 121.101 1.00 68.42  ? 697  ALA B N    1 
ATOM   4139 C CA   . ALA A 1 697 ? 96.562  120.910 121.149 1.00 67.48  ? 697  ALA B CA   1 
ATOM   4140 C C    . ALA A 1 697 ? 97.445  121.379 122.302 1.00 68.62  ? 697  ALA B C    1 
ATOM   4141 O O    . ALA A 1 697 ? 98.093  120.558 122.961 1.00 75.10  ? 697  ALA B O    1 
ATOM   4142 C CB   . ALA A 1 697 ? 97.294  121.087 119.820 1.00 68.99  ? 697  ALA B CB   1 
ATOM   4143 N N    . VAL A 1 698 ? 97.503  122.689 122.551 1.00 65.60  ? 698  VAL B N    1 
ATOM   4144 C CA   . VAL A 1 698 ? 98.289  123.191 123.677 1.00 65.84  ? 698  VAL B CA   1 
ATOM   4145 C C    . VAL A 1 698 ? 97.696  122.752 125.015 1.00 72.26  ? 698  VAL B C    1 
ATOM   4146 O O    . VAL A 1 698 ? 98.423  122.305 125.910 1.00 73.09  ? 698  VAL B O    1 
ATOM   4147 C CB   . VAL A 1 698 ? 98.420  124.722 123.587 1.00 64.50  ? 698  VAL B CB   1 
ATOM   4148 C CG1  . VAL A 1 698 ? 99.131  125.274 124.808 1.00 68.98  ? 698  VAL B CG1  1 
ATOM   4149 C CG2  . VAL A 1 698 ? 99.170  125.105 122.320 1.00 63.90  ? 698  VAL B CG2  1 
ATOM   4150 N N    . PHE A 1 699 ? 96.374  122.854 125.176 1.00 78.82  ? 699  PHE B N    1 
ATOM   4151 C CA   . PHE A 1 699 ? 95.791  122.515 126.471 1.00 74.53  ? 699  PHE B CA   1 
ATOM   4152 C C    . PHE A 1 699 ? 95.645  121.011 126.680 1.00 70.42  ? 699  PHE B C    1 
ATOM   4153 O O    . PHE A 1 699 ? 95.526  120.563 127.825 1.00 70.92  ? 699  PHE B O    1 
ATOM   4154 C CB   . PHE A 1 699 ? 94.433  123.199 126.659 1.00 78.69  ? 699  PHE B CB   1 
ATOM   4155 C CG   . PHE A 1 699 ? 93.770  122.860 127.964 1.00 79.23  ? 699  PHE B CG   1 
ATOM   4156 C CD1  . PHE A 1 699 ? 94.396  123.154 129.166 1.00 81.13  ? 699  PHE B CD1  1 
ATOM   4157 C CD2  . PHE A 1 699 ? 92.548  122.213 127.993 1.00 79.07  ? 699  PHE B CD2  1 
ATOM   4158 C CE1  . PHE A 1 699 ? 93.805  122.823 130.372 1.00 83.25  ? 699  PHE B CE1  1 
ATOM   4159 C CE2  . PHE A 1 699 ? 91.950  121.886 129.197 1.00 79.78  ? 699  PHE B CE2  1 
ATOM   4160 C CZ   . PHE A 1 699 ? 92.581  122.189 130.386 1.00 81.15  ? 699  PHE B CZ   1 
ATOM   4161 N N    . ASN A 1 700 ? 95.732  120.215 125.621 1.00 68.93  ? 700  ASN B N    1 
ATOM   4162 C CA   . ASN A 1 700 ? 95.654  118.770 125.788 1.00 69.77  ? 700  ASN B CA   1 
ATOM   4163 C C    . ASN A 1 700 ? 97.007  118.152 126.096 1.00 66.62  ? 700  ASN B C    1 
ATOM   4164 O O    . ASN A 1 700 ? 97.105  117.310 126.994 1.00 68.29  ? 700  ASN B O    1 
ATOM   4165 C CB   . ASN A 1 700 ? 95.058  118.113 124.541 1.00 65.66  ? 700  ASN B CB   1 
ATOM   4166 C CG   . ASN A 1 700 ? 93.548  118.220 124.494 1.00 66.25  ? 700  ASN B CG   1 
ATOM   4167 O OD1  . ASN A 1 700 ? 92.901  118.468 125.510 1.00 72.38  ? 700  ASN B OD1  1 
ATOM   4168 N ND2  . ASN A 1 700 ? 92.979  118.037 123.309 1.00 63.89  ? 700  ASN B ND2  1 
ATOM   4169 N N    . PHE A 1 701 ? 98.057  118.539 125.376 1.00 54.58  ? 701  PHE B N    1 
ATOM   4170 C CA   . PHE A 1 701 ? 99.344  117.902 125.592 1.00 52.76  ? 701  PHE B CA   1 
ATOM   4171 C C    . PHE A 1 701 ? 100.242 118.672 126.551 1.00 60.53  ? 701  PHE B C    1 
ATOM   4172 O O    . PHE A 1 701 ? 101.297 118.153 126.928 1.00 67.52  ? 701  PHE B O    1 
ATOM   4173 C CB   . PHE A 1 701 ? 100.069 117.732 124.249 1.00 54.97  ? 701  PHE B CB   1 
ATOM   4174 C CG   . PHE A 1 701 ? 99.313  116.901 123.241 1.00 60.72  ? 701  PHE B CG   1 
ATOM   4175 C CD1  . PHE A 1 701 ? 98.332  116.007 123.636 1.00 62.33  ? 701  PHE B CD1  1 
ATOM   4176 C CD2  . PHE A 1 701 ? 99.570  117.042 121.890 1.00 66.84  ? 701  PHE B CD2  1 
ATOM   4177 C CE1  . PHE A 1 701 ? 97.637  115.258 122.705 1.00 65.08  ? 701  PHE B CE1  1 
ATOM   4178 C CE2  . PHE A 1 701 ? 98.873  116.300 120.957 1.00 68.43  ? 701  PHE B CE2  1 
ATOM   4179 C CZ   . PHE A 1 701 ? 97.910  115.403 121.364 1.00 64.13  ? 701  PHE B CZ   1 
ATOM   4180 N N    . GLY A 1 702 ? 99.864  119.884 126.956 1.00 59.17  ? 702  GLY B N    1 
ATOM   4181 C CA   . GLY A 1 702 ? 100.683 120.643 127.876 1.00 56.80  ? 702  GLY B CA   1 
ATOM   4182 C C    . GLY A 1 702 ? 100.233 120.589 129.320 1.00 62.57  ? 702  GLY B C    1 
ATOM   4183 O O    . GLY A 1 702 ? 100.848 121.239 130.171 1.00 67.94  ? 702  GLY B O    1 
ATOM   4184 N N    . GLN A 1 703 ? 99.164  119.843 129.614 1.00 59.09  ? 703  GLN B N    1 
ATOM   4185 C CA   . GLN A 1 703 ? 98.627  119.743 130.970 1.00 49.62  ? 703  GLN B CA   1 
ATOM   4186 C C    . GLN A 1 703 ? 99.631  119.144 131.950 1.00 52.41  ? 703  GLN B C    1 
ATOM   4187 O O    . GLN A 1 703 ? 99.643  119.513 133.130 1.00 61.95  ? 703  GLN B O    1 
ATOM   4188 C CB   . GLN A 1 703 ? 97.312  118.966 130.952 1.00 51.02  ? 703  GLN B CB   1 
ATOM   4189 C CG   . GLN A 1 703 ? 97.382  117.549 130.437 1.00 52.92  ? 703  GLN B CG   1 
ATOM   4190 C CD   . GLN A 1 703 ? 96.022  116.894 130.453 1.00 58.57  ? 703  GLN B CD   1 
ATOM   4191 O OE1  . GLN A 1 703 ? 95.068  117.453 130.992 1.00 60.45  ? 703  GLN B OE1  1 
ATOM   4192 N NE2  . GLN A 1 703 ? 95.919  115.713 129.859 1.00 60.27  ? 703  GLN B NE2  1 
ATOM   4193 N N    . GLY A 1 704 ? 100.457 118.208 131.480 1.00 51.99  ? 704  GLY B N    1 
ATOM   4194 C CA   . GLY A 1 704 ? 101.494 117.625 132.320 1.00 54.04  ? 704  GLY B CA   1 
ATOM   4195 C C    . GLY A 1 704 ? 102.490 118.636 132.855 1.00 50.98  ? 704  GLY B C    1 
ATOM   4196 O O    . GLY A 1 704 ? 102.962 118.513 133.988 1.00 55.60  ? 704  GLY B O    1 
ATOM   4197 N N    . PHE A 1 705 ? 102.843 119.631 132.039 1.00 47.64  ? 705  PHE B N    1 
ATOM   4198 C CA   . PHE A 1 705 ? 103.768 120.676 132.473 1.00 52.15  ? 705  PHE B CA   1 
ATOM   4199 C C    . PHE A 1 705 ? 103.225 121.449 133.674 1.00 52.02  ? 705  PHE B C    1 
ATOM   4200 O O    . PHE A 1 705 ? 103.976 121.762 134.605 1.00 54.51  ? 705  PHE B O    1 
ATOM   4201 C CB   . PHE A 1 705 ? 104.052 121.622 131.308 1.00 51.33  ? 705  PHE B CB   1 
ATOM   4202 C CG   . PHE A 1 705 ? 105.375 122.318 131.400 1.00 52.91  ? 705  PHE B CG   1 
ATOM   4203 C CD1  . PHE A 1 705 ? 106.451 121.708 132.023 1.00 50.84  ? 705  PHE B CD1  1 
ATOM   4204 C CD2  . PHE A 1 705 ? 105.547 123.581 130.859 1.00 59.14  ? 705  PHE B CD2  1 
ATOM   4205 C CE1  . PHE A 1 705 ? 107.673 122.345 132.105 1.00 54.86  ? 705  PHE B CE1  1 
ATOM   4206 C CE2  . PHE A 1 705 ? 106.767 124.224 130.940 1.00 55.12  ? 705  PHE B CE2  1 
ATOM   4207 C CZ   . PHE A 1 705 ? 107.830 123.605 131.564 1.00 55.24  ? 705  PHE B CZ   1 
ATOM   4208 N N    . ILE A 1 706 ? 101.933 121.785 133.659 1.00 50.20  ? 706  ILE B N    1 
ATOM   4209 C CA   . ILE A 1 706 ? 101.323 122.525 134.765 1.00 51.24  ? 706  ILE B CA   1 
ATOM   4210 C C    . ILE A 1 706 ? 101.357 121.699 136.050 1.00 52.80  ? 706  ILE B C    1 
ATOM   4211 O O    . ILE A 1 706 ? 101.687 122.210 137.128 1.00 56.62  ? 706  ILE B O    1 
ATOM   4212 C CB   . ILE A 1 706 ? 99.888  122.946 134.388 1.00 49.77  ? 706  ILE B CB   1 
ATOM   4213 C CG1  . ILE A 1 706 ? 99.907  124.252 133.592 1.00 48.59  ? 706  ILE B CG1  1 
ATOM   4214 C CG2  . ILE A 1 706 ? 99.009  123.102 135.623 1.00 49.60  ? 706  ILE B CG2  1 
ATOM   4215 C CD1  . ILE A 1 706 ? 98.687  124.450 132.719 1.00 49.52  ? 706  ILE B CD1  1 
ATOM   4216 N N    . SER A 1 707 ? 101.025 120.411 135.950 1.00 53.79  ? 707  SER B N    1 
ATOM   4217 C CA   . SER A 1 707 ? 101.023 119.515 137.106 1.00 52.54  ? 707  SER B CA   1 
ATOM   4218 C C    . SER A 1 707 ? 102.417 119.357 137.710 1.00 57.05  ? 707  SER B C    1 
ATOM   4219 O O    . SER A 1 707 ? 102.567 119.322 138.937 1.00 60.75  ? 707  SER B O    1 
ATOM   4220 C CB   . SER A 1 707 ? 100.448 118.157 136.715 1.00 49.09  ? 707  SER B CB   1 
ATOM   4221 O OG   . SER A 1 707 ? 99.889  117.520 137.847 1.00 51.57  ? 707  SER B OG   1 
ATOM   4222 N N    . PHE A 1 708 ? 103.440 119.230 136.860 1.00 51.02  ? 708  PHE B N    1 
ATOM   4223 C CA   . PHE A 1 708 ? 104.815 119.014 137.314 1.00 43.46  ? 708  PHE B CA   1 
ATOM   4224 C C    . PHE A 1 708 ? 105.297 120.171 138.184 1.00 50.22  ? 708  PHE B C    1 
ATOM   4225 O O    . PHE A 1 708 ? 105.937 119.949 139.218 1.00 58.91  ? 708  PHE B O    1 
ATOM   4226 C CB   . PHE A 1 708 ? 105.722 118.827 136.089 1.00 46.03  ? 708  PHE B CB   1 
ATOM   4227 C CG   . PHE A 1 708 ? 107.152 119.301 136.270 1.00 47.37  ? 708  PHE B CG   1 
ATOM   4228 C CD1  . PHE A 1 708 ? 107.982 118.766 137.253 1.00 54.25  ? 708  PHE B CD1  1 
ATOM   4229 C CD2  . PHE A 1 708 ? 107.656 120.306 135.461 1.00 49.74  ? 708  PHE B CD2  1 
ATOM   4230 C CE1  . PHE A 1 708 ? 109.279 119.214 137.405 1.00 53.00  ? 708  PHE B CE1  1 
ATOM   4231 C CE2  . PHE A 1 708 ? 108.953 120.758 135.612 1.00 50.03  ? 708  PHE B CE2  1 
ATOM   4232 C CZ   . PHE A 1 708 ? 109.765 120.211 136.584 1.00 49.07  ? 708  PHE B CZ   1 
ATOM   4233 N N    . GLY A 1 709 ? 105.004 121.408 137.777 1.00 61.47  ? 709  GLY B N    1 
ATOM   4234 C CA   . GLY A 1 709 ? 105.477 122.574 138.513 1.00 62.79  ? 709  GLY B CA   1 
ATOM   4235 C C    . GLY A 1 709 ? 105.049 122.600 139.971 1.00 60.42  ? 709  GLY B C    1 
ATOM   4236 O O    . GLY A 1 709 ? 105.841 122.950 140.849 1.00 58.79  ? 709  GLY B O    1 
ATOM   4237 N N    . ILE A 1 710 ? 103.803 122.227 140.254 1.00 63.11  ? 710  ILE B N    1 
ATOM   4238 C CA   . ILE A 1 710 ? 103.321 122.252 141.634 1.00 64.81  ? 710  ILE B CA   1 
ATOM   4239 C C    . ILE A 1 710 ? 103.822 121.040 142.414 1.00 65.43  ? 710  ILE B C    1 
ATOM   4240 O O    . ILE A 1 710 ? 104.436 121.183 143.477 1.00 69.13  ? 710  ILE B O    1 
ATOM   4241 C CB   . ILE A 1 710 ? 101.783 122.338 141.665 1.00 67.93  ? 710  ILE B CB   1 
ATOM   4242 C CG1  . ILE A 1 710 ? 101.268 123.262 140.559 1.00 69.12  ? 710  ILE B CG1  1 
ATOM   4243 C CG2  . ILE A 1 710 ? 101.299 122.793 143.036 1.00 70.70  ? 710  ILE B CG2  1 
ATOM   4244 C CD1  . ILE A 1 710 ? 101.657 124.712 140.738 1.00 68.17  ? 710  ILE B CD1  1 
ATOM   4245 N N    . PHE A 1 711 ? 103.574 119.834 141.906 1.00 70.14  ? 711  PHE B N    1 
ATOM   4246 C CA   . PHE A 1 711 ? 103.845 118.606 142.652 1.00 71.50  ? 711  PHE B CA   1 
ATOM   4247 C C    . PHE A 1 711 ? 105.288 118.123 142.529 1.00 71.24  ? 711  PHE B C    1 
ATOM   4248 O O    . PHE A 1 711 ? 105.900 117.753 143.536 1.00 72.50  ? 711  PHE B O    1 
ATOM   4249 C CB   . PHE A 1 711 ? 102.879 117.494 142.235 1.00 72.00  ? 711  PHE B CB   1 
ATOM   4250 C CG   . PHE A 1 711 ? 101.574 117.523 142.977 1.00 75.46  ? 711  PHE B CG   1 
ATOM   4251 C CD1  . PHE A 1 711 ? 100.982 118.728 143.319 1.00 72.94  ? 711  PHE B CD1  1 
ATOM   4252 C CD2  . PHE A 1 711 ? 100.965 116.346 143.375 1.00 77.15  ? 711  PHE B CD2  1 
ATOM   4253 C CE1  . PHE A 1 711 ? 99.793  118.758 144.016 1.00 75.04  ? 711  PHE B CE1  1 
ATOM   4254 C CE2  . PHE A 1 711 ? 99.775  116.372 144.076 1.00 75.77  ? 711  PHE B CE2  1 
ATOM   4255 C CZ   . PHE A 1 711 ? 99.190  117.580 144.393 1.00 76.42  ? 711  PHE B CZ   1 
ATOM   4256 N N    . GLY A 1 712 ? 105.838 118.105 141.313 1.00 58.65  ? 712  GLY B N    1 
ATOM   4257 C CA   . GLY A 1 712 ? 107.146 117.501 141.108 1.00 58.68  ? 712  GLY B CA   1 
ATOM   4258 C C    . GLY A 1 712 ? 108.265 118.268 141.784 1.00 61.15  ? 712  GLY B C    1 
ATOM   4259 O O    . GLY A 1 712 ? 109.132 117.672 142.430 1.00 61.90  ? 712  GLY B O    1 
ATOM   4260 N N    . LEU A 1 713 ? 108.272 119.592 141.647 1.00 59.61  ? 713  LEU B N    1 
ATOM   4261 C CA   . LEU A 1 713 ? 109.346 120.406 142.211 1.00 58.92  ? 713  LEU B CA   1 
ATOM   4262 C C    . LEU A 1 713 ? 109.034 120.724 143.675 1.00 63.45  ? 713  LEU B C    1 
ATOM   4263 O O    . LEU A 1 713 ? 108.848 121.871 144.077 1.00 63.30  ? 713  LEU B O    1 
ATOM   4264 C CB   . LEU A 1 713 ? 109.512 121.678 141.393 1.00 55.28  ? 713  LEU B CB   1 
ATOM   4265 C CG   . LEU A 1 713 ? 110.467 121.603 140.208 1.00 58.24  ? 713  LEU B CG   1 
ATOM   4266 C CD1  . LEU A 1 713 ? 110.448 122.925 139.480 1.00 53.45  ? 713  LEU B CD1  1 
ATOM   4267 C CD2  . LEU A 1 713 ? 111.867 121.247 140.668 1.00 61.75  ? 713  LEU B CD2  1 
ATOM   4268 N N    . ASP A 1 714 ? 108.981 119.660 144.475 1.00 76.03  ? 714  ASP B N    1 
ATOM   4269 C CA   . ASP A 1 714 ? 108.710 119.732 145.904 1.00 74.17  ? 714  ASP B CA   1 
ATOM   4270 C C    . ASP A 1 714 ? 109.716 118.875 146.657 1.00 76.57  ? 714  ASP B C    1 
ATOM   4271 O O    . ASP A 1 714 ? 110.195 117.859 146.145 1.00 76.61  ? 714  ASP B O    1 
ATOM   4272 C CB   . ASP A 1 714 ? 107.276 119.271 146.231 1.00 71.13  ? 714  ASP B CB   1 
ATOM   4273 C CG   . ASP A 1 714 ? 106.792 119.761 147.593 1.00 74.29  ? 714  ASP B CG   1 
ATOM   4274 O OD1  . ASP A 1 714 ? 107.541 119.654 148.587 1.00 73.21  ? 714  ASP B OD1  1 
ATOM   4275 O OD2  . ASP A 1 714 ? 105.652 120.265 147.666 1.00 79.44  ? 714  ASP B OD2  1 
ATOM   4276 N N    . LYS A 1 715 ? 110.030 119.293 147.880 1.00 81.22  ? 715  LYS B N    1 
ATOM   4277 C CA   . LYS A 1 715 ? 110.985 118.566 148.704 1.00 78.96  ? 715  LYS B CA   1 
ATOM   4278 C C    . LYS A 1 715 ? 110.269 117.435 149.429 1.00 79.48  ? 715  LYS B C    1 
ATOM   4279 O O    . LYS A 1 715 ? 109.309 117.669 150.171 1.00 78.26  ? 715  LYS B O    1 
ATOM   4280 C CB   . LYS A 1 715 ? 111.658 119.493 149.715 1.00 78.75  ? 715  LYS B CB   1 
ATOM   4281 C CG   . LYS A 1 715 ? 112.186 120.791 149.137 1.00 80.97  ? 715  LYS B CG   1 
ATOM   4282 C CD   . LYS A 1 715 ? 113.289 121.364 150.014 1.00 80.54  ? 715  LYS B CD   1 
ATOM   4283 C CE   . LYS A 1 715 ? 113.269 122.882 150.009 1.00 80.40  ? 715  LYS B CE   1 
ATOM   4284 N NZ   . LYS A 1 715 ? 113.939 123.446 148.804 1.00 77.81  ? 715  LYS B NZ   1 
ATOM   4285 N N    . HIS A 1 716 ? 110.738 116.210 149.212 1.00 93.22  ? 716  HIS B N    1 
ATOM   4286 C CA   . HIS A 1 716 ? 110.174 115.039 149.872 1.00 93.97  ? 716  HIS B CA   1 
ATOM   4287 C C    . HIS A 1 716 ? 111.301 114.068 150.177 1.00 93.73  ? 716  HIS B C    1 
ATOM   4288 O O    . HIS A 1 716 ? 111.950 113.569 149.252 1.00 96.45  ? 716  HIS B O    1 
ATOM   4289 C CB   . HIS A 1 716 ? 109.114 114.366 148.998 1.00 92.21  ? 716  HIS B CB   1 
ATOM   4290 C CG   . HIS A 1 716 ? 107.736 114.921 149.177 1.00 93.07  ? 716  HIS B CG   1 
ATOM   4291 N ND1  . HIS A 1 716 ? 107.280 115.397 150.387 1.00 92.96  ? 716  HIS B ND1  1 
ATOM   4292 C CD2  . HIS A 1 716 ? 106.718 115.084 148.300 1.00 94.02  ? 716  HIS B CD2  1 
ATOM   4293 C CE1  . HIS A 1 716 ? 106.039 115.828 150.248 1.00 93.41  ? 716  HIS B CE1  1 
ATOM   4294 N NE2  . HIS A 1 716 ? 105.674 115.649 148.991 1.00 93.88  ? 716  HIS B NE2  1 
ATOM   4295 N N    . LEU A 1 717 ? 111.545 113.841 151.468 1.00 91.76  ? 717  LEU B N    1 
ATOM   4296 C CA   . LEU A 1 717 ? 112.603 112.940 151.910 1.00 93.48  ? 717  LEU B CA   1 
ATOM   4297 C C    . LEU A 1 717 ? 112.402 111.539 151.339 1.00 95.95  ? 717  LEU B C    1 
ATOM   4298 O O    . LEU A 1 717 ? 111.304 110.978 151.398 1.00 94.86  ? 717  LEU B O    1 
ATOM   4299 C CB   . LEU A 1 717 ? 112.662 112.900 153.443 1.00 95.28  ? 717  LEU B CB   1 
ATOM   4300 C CG   . LEU A 1 717 ? 111.572 112.237 154.300 1.00 95.66  ? 717  LEU B CG   1 
ATOM   4301 C CD1  . LEU A 1 717 ? 112.112 111.890 155.677 1.00 93.84  ? 717  LEU B CD1  1 
ATOM   4302 C CD2  . LEU A 1 717 ? 110.333 113.114 154.441 1.00 92.29  ? 717  LEU B CD2  1 
ATOM   4303 N N    . ILE A 1 718 ? 113.464 110.989 150.760 1.00 95.04  ? 718  ILE B N    1 
ATOM   4304 C CA   . ILE A 1 718 ? 113.410 109.659 150.169 1.00 95.13  ? 718  ILE B CA   1 
ATOM   4305 C C    . ILE A 1 718 ? 113.523 108.599 151.257 1.00 96.33  ? 718  ILE B C    1 
ATOM   4306 O O    . ILE A 1 718 ? 112.541 108.271 151.922 1.00 94.96  ? 718  ILE B O    1 
ATOM   4307 C CB   . ILE A 1 718 ? 114.510 109.473 149.112 1.00 91.29  ? 718  ILE B CB   1 
ATOM   4308 C CG1  . ILE A 1 718 ? 114.571 110.687 148.181 1.00 91.20  ? 718  ILE B CG1  1 
ATOM   4309 C CG2  . ILE A 1 718 ? 114.273 108.200 148.315 1.00 91.47  ? 718  ILE B CG2  1 
ATOM   4310 C CD1  . ILE A 1 718 ? 113.298 110.927 147.397 1.00 92.26  ? 718  ILE B CD1  1 
ATOM   4311 N N    . SER B 1 36  ? 153.390 128.881 106.130 1.00 65.33  ? 36   SER A N    1 
ATOM   4312 C CA   . SER B 1 36  ? 153.802 128.273 107.388 1.00 65.08  ? 36   SER A CA   1 
ATOM   4313 C C    . SER B 1 36  ? 153.192 129.005 108.580 1.00 60.44  ? 36   SER A C    1 
ATOM   4314 O O    . SER B 1 36  ? 152.024 129.390 108.558 1.00 60.46  ? 36   SER A O    1 
ATOM   4315 C CB   . SER B 1 36  ? 155.329 128.267 107.505 1.00 66.19  ? 36   SER A CB   1 
ATOM   4316 O OG   . SER B 1 36  ? 155.907 127.284 106.664 1.00 74.64  ? 36   SER A OG   1 
ATOM   4317 N N    . MET B 1 37  ? 154.001 129.178 109.621 1.00 53.32  ? 37   MET A N    1 
ATOM   4318 C CA   . MET B 1 37  ? 153.600 129.897 110.823 1.00 58.65  ? 37   MET A CA   1 
ATOM   4319 C C    . MET B 1 37  ? 153.205 131.332 110.468 1.00 58.16  ? 37   MET A C    1 
ATOM   4320 O O    . MET B 1 37  ? 153.992 132.070 109.866 1.00 61.22  ? 37   MET A O    1 
ATOM   4321 C CB   . MET B 1 37  ? 154.720 129.855 111.861 1.00 62.06  ? 37   MET A CB   1 
ATOM   4322 C CG   . MET B 1 37  ? 155.125 128.449 112.297 1.00 63.13  ? 37   MET A CG   1 
ATOM   4323 S SD   . MET B 1 37  ? 156.699 128.420 113.177 1.00 71.15  ? 37   MET A SD   1 
ATOM   4324 C CE   . MET B 1 37  ? 156.167 127.793 114.768 1.00 51.15  ? 37   MET A CE   1 
ATOM   4325 N N    . SER B 1 38  ? 151.956 131.692 110.773 1.00 43.78  ? 38   SER A N    1 
ATOM   4326 C CA   . SER B 1 38  ? 151.438 133.059 110.651 1.00 43.33  ? 38   SER A CA   1 
ATOM   4327 C C    . SER B 1 38  ? 151.754 133.889 111.900 1.00 46.27  ? 38   SER A C    1 
ATOM   4328 O O    . SER B 1 38  ? 150.871 134.417 112.577 1.00 50.84  ? 38   SER A O    1 
ATOM   4329 C CB   . SER B 1 38  ? 149.940 133.032 110.373 1.00 46.81  ? 38   SER A CB   1 
ATOM   4330 O OG   . SER B 1 38  ? 149.677 132.967 108.982 1.00 46.57  ? 38   SER A OG   1 
ATOM   4331 N N    . ILE B 1 39  ? 153.056 134.000 112.190 1.00 40.53  ? 39   ILE A N    1 
ATOM   4332 C CA   . ILE B 1 39  ? 153.544 134.627 113.419 1.00 44.86  ? 39   ILE A CA   1 
ATOM   4333 C C    . ILE B 1 39  ? 153.191 136.107 113.491 1.00 41.57  ? 39   ILE A C    1 
ATOM   4334 O O    . ILE B 1 39  ? 153.247 136.698 114.576 1.00 46.77  ? 39   ILE A O    1 
ATOM   4335 C CB   . ILE B 1 39  ? 155.076 134.472 113.573 1.00 41.88  ? 39   ILE A CB   1 
ATOM   4336 C CG1  . ILE B 1 39  ? 155.567 133.117 113.109 1.00 43.92  ? 39   ILE A CG1  1 
ATOM   4337 C CG2  . ILE B 1 39  ? 155.480 134.538 115.012 1.00 42.67  ? 39   ILE A CG2  1 
ATOM   4338 C CD1  . ILE B 1 39  ? 156.205 133.202 111.784 1.00 38.66  ? 39   ILE A CD1  1 
ATOM   4339 N N    . THR B 1 40  ? 152.823 136.727 112.363 1.00 41.33  ? 40   THR A N    1 
ATOM   4340 C CA   . THR B 1 40  ? 152.355 138.110 112.401 1.00 40.63  ? 40   THR A CA   1 
ATOM   4341 C C    . THR B 1 40  ? 151.149 138.263 113.320 1.00 46.52  ? 40   THR A C    1 
ATOM   4342 O O    . THR B 1 40  ? 150.949 139.335 113.902 1.00 53.76  ? 40   THR A O    1 
ATOM   4343 C CB   . THR B 1 40  ? 152.025 138.603 110.991 1.00 40.16  ? 40   THR A CB   1 
ATOM   4344 O OG1  . THR B 1 40  ? 150.772 138.053 110.569 1.00 43.78  ? 40   THR A OG1  1 
ATOM   4345 C CG2  . THR B 1 40  ? 153.116 138.196 110.009 1.00 48.07  ? 40   THR A CG2  1 
ATOM   4346 N N    . ARG B 1 41  ? 150.345 137.209 113.482 1.00 41.20  ? 41   ARG A N    1 
ATOM   4347 C CA   . ARG B 1 41  ? 149.154 137.278 114.318 1.00 42.61  ? 41   ARG A CA   1 
ATOM   4348 C C    . ARG B 1 41  ? 149.288 136.386 115.549 1.00 46.11  ? 41   ARG A C    1 
ATOM   4349 O O    . ARG B 1 41  ? 148.328 135.727 115.955 1.00 53.66  ? 41   ARG A O    1 
ATOM   4350 C CB   . ARG B 1 41  ? 147.910 136.885 113.522 1.00 42.79  ? 41   ARG A CB   1 
ATOM   4351 C CG   . ARG B 1 41  ? 148.003 137.146 112.032 1.00 45.89  ? 41   ARG A CG   1 
ATOM   4352 C CD   . ARG B 1 41  ? 146.718 136.750 111.317 1.00 47.15  ? 41   ARG A CD   1 
ATOM   4353 N NE   . ARG B 1 41  ? 146.634 135.311 111.095 1.00 48.53  ? 41   ARG A NE   1 
ATOM   4354 C CZ   . ARG B 1 41  ? 145.621 134.548 111.484 1.00 50.90  ? 41   ARG A CZ   1 
ATOM   4355 N NH1  . ARG B 1 41  ? 144.578 135.054 112.121 1.00 47.19  ? 41   ARG A NH1  1 
ATOM   4356 N NH2  . ARG B 1 41  ? 145.656 133.243 111.228 1.00 47.04  ? 41   ARG A NH2  1 
ATOM   4357 N N    . LEU B 1 42  ? 150.478 136.360 116.152 1.00 38.73  ? 42   LEU A N    1 
ATOM   4358 C CA   . LEU B 1 42  ? 150.735 135.626 117.386 1.00 37.38  ? 42   LEU A CA   1 
ATOM   4359 C C    . LEU B 1 42  ? 150.734 136.523 118.617 1.00 51.13  ? 42   LEU A C    1 
ATOM   4360 O O    . LEU B 1 42  ? 150.295 136.093 119.689 1.00 56.83  ? 42   LEU A O    1 
ATOM   4361 C CB   . LEU B 1 42  ? 152.080 134.887 117.297 1.00 27.30  ? 42   LEU A CB   1 
ATOM   4362 C CG   . LEU B 1 42  ? 152.747 134.319 118.560 1.00 26.58  ? 42   LEU A CG   1 
ATOM   4363 C CD1  . LEU B 1 42  ? 151.841 133.322 119.276 1.00 32.76  ? 42   LEU A CD1  1 
ATOM   4364 C CD2  . LEU B 1 42  ? 154.085 133.678 118.250 1.00 29.47  ? 42   LEU A CD2  1 
ATOM   4365 N N    . PHE B 1 43  ? 151.184 137.771 118.468 1.00 37.85  ? 43   PHE A N    1 
ATOM   4366 C CA   . PHE B 1 43  ? 151.190 138.716 119.585 1.00 20.53  ? 43   PHE A CA   1 
ATOM   4367 C C    . PHE B 1 43  ? 149.797 139.037 120.126 1.00 22.27  ? 43   PHE A C    1 
ATOM   4368 O O    . PHE B 1 43  ? 149.649 139.062 121.360 1.00 28.56  ? 43   PHE A O    1 
ATOM   4369 C CB   . PHE B 1 43  ? 151.985 139.966 119.181 1.00 24.32  ? 43   PHE A CB   1 
ATOM   4370 C CG   . PHE B 1 43  ? 152.294 140.889 120.323 1.00 33.94  ? 43   PHE A CG   1 
ATOM   4371 C CD1  . PHE B 1 43  ? 152.867 140.404 121.485 1.00 35.57  ? 43   PHE A CD1  1 
ATOM   4372 C CD2  . PHE B 1 43  ? 152.033 142.245 120.227 1.00 36.59  ? 43   PHE A CD2  1 
ATOM   4373 C CE1  . PHE B 1 43  ? 153.161 141.252 122.535 1.00 34.91  ? 43   PHE A CE1  1 
ATOM   4374 C CE2  . PHE B 1 43  ? 152.325 143.097 121.274 1.00 27.96  ? 43   PHE A CE2  1 
ATOM   4375 C CZ   . PHE B 1 43  ? 152.890 142.600 122.429 1.00 28.77  ? 43   PHE A CZ   1 
ATOM   4376 N N    . PRO B 1 44  ? 148.773 139.366 119.316 1.00 21.34  ? 44   PRO A N    1 
ATOM   4377 C CA   . PRO B 1 44  ? 147.432 139.574 119.905 1.00 37.51  ? 44   PRO A CA   1 
ATOM   4378 C C    . PRO B 1 44  ? 146.912 138.379 120.696 1.00 39.07  ? 44   PRO A C    1 
ATOM   4379 O O    . PRO B 1 44  ? 146.257 138.555 121.739 1.00 49.34  ? 44   PRO A O    1 
ATOM   4380 C CB   . PRO B 1 44  ? 146.545 139.842 118.683 1.00 40.78  ? 44   PRO A CB   1 
ATOM   4381 C CG   . PRO B 1 44  ? 147.436 140.353 117.651 1.00 32.69  ? 44   PRO A CG   1 
ATOM   4382 C CD   . PRO B 1 44  ? 148.816 139.841 117.916 1.00 23.84  ? 44   PRO A CD   1 
ATOM   4383 N N    . ALA B 1 45  ? 147.234 137.162 120.252 1.00 20.60  ? 45   ALA A N    1 
ATOM   4384 C CA   . ALA B 1 45  ? 146.861 135.973 121.001 1.00 21.68  ? 45   ALA A CA   1 
ATOM   4385 C C    . ALA B 1 45  ? 147.625 135.845 122.307 1.00 20.12  ? 45   ALA A C    1 
ATOM   4386 O O    . ALA B 1 45  ? 147.149 135.160 123.215 1.00 32.10  ? 45   ALA A O    1 
ATOM   4387 C CB   . ALA B 1 45  ? 147.082 134.724 120.148 1.00 23.30  ? 45   ALA A CB   1 
ATOM   4388 N N    . LEU B 1 46  ? 148.791 136.475 122.433 1.00 11.86  ? 46   LEU A N    1 
ATOM   4389 C CA   . LEU B 1 46  ? 149.465 136.468 123.722 1.00 22.26  ? 46   LEU A CA   1 
ATOM   4390 C C    . LEU B 1 46  ? 149.090 137.672 124.572 1.00 28.04  ? 46   LEU A C    1 
ATOM   4391 O O    . LEU B 1 46  ? 149.342 137.665 125.781 1.00 31.62  ? 46   LEU A O    1 
ATOM   4392 C CB   . LEU B 1 46  ? 150.984 136.440 123.526 1.00 22.49  ? 46   LEU A CB   1 
ATOM   4393 C CG   . LEU B 1 46  ? 151.628 135.083 123.248 1.00 25.82  ? 46   LEU A CG   1 
ATOM   4394 C CD1  . LEU B 1 46  ? 152.951 135.265 122.528 1.00 25.72  ? 46   LEU A CD1  1 
ATOM   4395 C CD2  . LEU B 1 46  ? 151.820 134.307 124.537 1.00 32.37  ? 46   LEU A CD2  1 
ATOM   4396 N N    . LEU B 1 47  ? 148.496 138.701 123.964 1.00 23.42  ? 47   LEU A N    1 
ATOM   4397 C CA   . LEU B 1 47  ? 147.955 139.832 124.705 1.00 20.27  ? 47   LEU A CA   1 
ATOM   4398 C C    . LEU B 1 47  ? 146.578 139.549 125.285 1.00 28.25  ? 47   LEU A C    1 
ATOM   4399 O O    . LEU B 1 47  ? 146.284 140.031 126.378 1.00 39.01  ? 47   LEU A O    1 
ATOM   4400 C CB   . LEU B 1 47  ? 147.881 141.071 123.811 1.00 17.26  ? 47   LEU A CB   1 
ATOM   4401 C CG   . LEU B 1 47  ? 149.188 141.817 123.542 1.00 17.47  ? 47   LEU A CG   1 
ATOM   4402 C CD1  . LEU B 1 47  ? 148.944 142.988 122.609 1.00 17.43  ? 47   LEU A CD1  1 
ATOM   4403 C CD2  . LEU B 1 47  ? 149.813 142.286 124.842 1.00 30.85  ? 47   LEU A CD2  1 
ATOM   4404 N N    . GLU B 1 48  ? 145.858 138.575 124.734 1.00 23.37  ? 48   GLU A N    1 
ATOM   4405 C CA   . GLU B 1 48  ? 144.537 138.233 125.266 1.00 27.83  ? 48   GLU A CA   1 
ATOM   4406 C C    . GLU B 1 48  ? 144.642 137.259 126.431 1.00 34.17  ? 48   GLU A C    1 
ATOM   4407 O O    . GLU B 1 48  ? 144.050 137.483 127.500 1.00 39.09  ? 48   GLU A O    1 
ATOM   4408 C CB   . GLU B 1 48  ? 143.675 137.625 124.160 1.00 31.89  ? 48   GLU A CB   1 
ATOM   4409 C CG   . GLU B 1 48  ? 142.424 136.928 124.665 1.00 36.10  ? 48   GLU A CG   1 
ATOM   4410 C CD   . GLU B 1 48  ? 141.929 135.861 123.709 1.00 45.10  ? 48   GLU A CD   1 
ATOM   4411 O OE1  . GLU B 1 48  ? 142.543 135.698 122.634 1.00 43.21  ? 48   GLU A OE1  1 
ATOM   4412 O OE2  . GLU B 1 48  ? 140.933 135.182 124.034 1.00 43.84  ? 48   GLU A OE2  1 
ATOM   4413 N N    . CYS B 1 49  ? 145.395 136.179 126.231 1.00 26.65  ? 49   CYS A N    1 
ATOM   4414 C CA   . CYS B 1 49  ? 145.541 135.126 127.228 1.00 19.91  ? 49   CYS A CA   1 
ATOM   4415 C C    . CYS B 1 49  ? 146.071 135.680 128.543 1.00 16.16  ? 49   CYS A C    1 
ATOM   4416 O O    . CYS B 1 49  ? 145.592 135.304 129.617 1.00 19.70  ? 49   CYS A O    1 
ATOM   4417 C CB   . CYS B 1 49  ? 146.440 134.012 126.700 1.00 23.71  ? 49   CYS A CB   1 
ATOM   4418 S SG   . CYS B 1 49  ? 145.816 133.181 125.224 1.00 23.22  ? 49   CYS A SG   1 
ATOM   4419 N N    . PHE B 1 50  ? 147.055 136.573 128.485 1.00 18.09  ? 50   PHE A N    1 
ATOM   4420 C CA   . PHE B 1 50  ? 147.577 137.163 129.709 1.00 24.26  ? 50   PHE A CA   1 
ATOM   4421 C C    . PHE B 1 50  ? 146.935 138.500 130.070 1.00 29.69  ? 50   PHE A C    1 
ATOM   4422 O O    . PHE B 1 50  ? 147.040 138.909 131.230 1.00 28.08  ? 50   PHE A O    1 
ATOM   4423 C CB   . PHE B 1 50  ? 149.094 137.345 129.593 1.00 17.21  ? 50   PHE A CB   1 
ATOM   4424 C CG   . PHE B 1 50  ? 149.855 136.052 129.505 1.00 18.53  ? 50   PHE A CG   1 
ATOM   4425 C CD1  . PHE B 1 50  ? 150.066 135.439 128.280 1.00 20.30  ? 50   PHE A CD1  1 
ATOM   4426 C CD2  . PHE B 1 50  ? 150.356 135.448 130.644 1.00 21.60  ? 50   PHE A CD2  1 
ATOM   4427 C CE1  . PHE B 1 50  ? 150.761 134.250 128.194 1.00 16.56  ? 50   PHE A CE1  1 
ATOM   4428 C CE2  . PHE B 1 50  ? 151.053 134.257 130.564 1.00 24.71  ? 50   PHE A CE2  1 
ATOM   4429 C CZ   . PHE B 1 50  ? 151.256 133.659 129.336 1.00 17.63  ? 50   PHE A CZ   1 
ATOM   4430 N N    . GLY B 1 51  ? 146.192 139.147 129.165 1.00 29.38  ? 51   GLY A N    1 
ATOM   4431 C CA   . GLY B 1 51  ? 145.395 140.289 129.574 1.00 21.25  ? 51   GLY A CA   1 
ATOM   4432 C C    . GLY B 1 51  ? 144.256 139.889 130.490 1.00 25.22  ? 51   GLY A C    1 
ATOM   4433 O O    . GLY B 1 51  ? 143.992 140.553 131.500 1.00 27.31  ? 51   GLY A O    1 
ATOM   4434 N N    . ILE B 1 52  ? 143.602 138.764 130.189 1.00 23.12  ? 52   ILE A N    1 
ATOM   4435 C CA   . ILE B 1 52  ? 142.536 138.315 131.080 1.00 20.26  ? 52   ILE A CA   1 
ATOM   4436 C C    . ILE B 1 52  ? 143.116 137.790 132.392 1.00 24.67  ? 52   ILE A C    1 
ATOM   4437 O O    . ILE B 1 52  ? 142.508 137.957 133.457 1.00 32.91  ? 52   ILE A O    1 
ATOM   4438 C CB   . ILE B 1 52  ? 141.668 137.256 130.375 1.00 6.70   ? 52   ILE A CB   1 
ATOM   4439 C CG1  . ILE B 1 52  ? 141.168 137.784 129.032 1.00 9.56   ? 52   ILE A CG1  1 
ATOM   4440 C CG2  . ILE B 1 52  ? 140.485 136.858 131.236 1.00 12.77  ? 52   ILE A CG2  1 
ATOM   4441 C CD1  . ILE B 1 52  ? 140.705 136.701 128.092 1.00 15.59  ? 52   ILE A CD1  1 
ATOM   4442 N N    . VAL B 1 53  ? 144.279 137.132 132.346 1.00 16.20  ? 53   VAL A N    1 
ATOM   4443 C CA   . VAL B 1 53  ? 144.912 136.694 133.590 1.00 10.62  ? 53   VAL A CA   1 
ATOM   4444 C C    . VAL B 1 53  ? 145.289 137.895 134.458 1.00 23.04  ? 53   VAL A C    1 
ATOM   4445 O O    . VAL B 1 53  ? 145.133 137.862 135.688 1.00 27.17  ? 53   VAL A O    1 
ATOM   4446 C CB   . VAL B 1 53  ? 146.130 135.799 133.277 1.00 15.46  ? 53   VAL A CB   1 
ATOM   4447 C CG1  . VAL B 1 53  ? 146.994 135.597 134.508 1.00 16.98  ? 53   VAL A CG1  1 
ATOM   4448 C CG2  . VAL B 1 53  ? 145.671 134.456 132.746 1.00 13.46  ? 53   VAL A CG2  1 
ATOM   4449 N N    . LEU B 1 54  ? 145.735 138.992 133.831 1.00 22.34  ? 54   LEU A N    1 
ATOM   4450 C CA   . LEU B 1 54  ? 145.998 140.225 134.568 1.00 26.70  ? 54   LEU A CA   1 
ATOM   4451 C C    . LEU B 1 54  ? 144.726 140.792 135.186 1.00 27.32  ? 54   LEU A C    1 
ATOM   4452 O O    . LEU B 1 54  ? 144.752 141.291 136.318 1.00 28.32  ? 54   LEU A O    1 
ATOM   4453 C CB   . LEU B 1 54  ? 146.654 141.252 133.648 1.00 24.75  ? 54   LEU A CB   1 
ATOM   4454 C CG   . LEU B 1 54  ? 147.107 142.556 134.302 1.00 20.77  ? 54   LEU A CG   1 
ATOM   4455 C CD1  . LEU B 1 54  ? 148.456 142.370 134.973 1.00 24.80  ? 54   LEU A CD1  1 
ATOM   4456 C CD2  . LEU B 1 54  ? 147.167 143.672 133.275 1.00 26.01  ? 54   LEU A CD2  1 
ATOM   4457 N N    . CYS B 1 55  ? 143.615 140.760 134.444 1.00 25.36  ? 55   CYS A N    1 
ATOM   4458 C CA   . CYS B 1 55  ? 142.346 141.241 134.991 1.00 23.80  ? 55   CYS A CA   1 
ATOM   4459 C C    . CYS B 1 55  ? 141.921 140.407 136.195 1.00 20.15  ? 55   CYS A C    1 
ATOM   4460 O O    . CYS B 1 55  ? 141.455 140.940 137.209 1.00 32.68  ? 55   CYS A O    1 
ATOM   4461 C CB   . CYS B 1 55  ? 141.262 141.222 133.913 1.00 16.39  ? 55   CYS A CB   1 
ATOM   4462 S SG   . CYS B 1 55  ? 141.533 142.382 132.556 1.00 47.02  ? 55   CYS A SG   1 
ATOM   4463 N N    . GLY B 1 56  ? 142.100 139.088 136.096 1.00 15.94  ? 56   GLY A N    1 
ATOM   4464 C CA   . GLY B 1 56  ? 141.805 138.204 137.214 1.00 7.80   ? 56   GLY A CA   1 
ATOM   4465 C C    . GLY B 1 56  ? 142.663 138.484 138.432 1.00 10.10  ? 56   GLY A C    1 
ATOM   4466 O O    . GLY B 1 56  ? 142.171 138.489 139.563 1.00 23.89  ? 56   GLY A O    1 
ATOM   4467 N N    . TYR B 1 57  ? 143.934 138.822 138.207 1.00 15.81  ? 57   TYR A N    1 
ATOM   4468 C CA   . TYR B 1 57  ? 144.824 139.134 139.322 1.00 21.26  ? 57   TYR A CA   1 
ATOM   4469 C C    . TYR B 1 57  ? 144.411 140.442 139.978 1.00 29.01  ? 57   TYR A C    1 
ATOM   4470 O O    . TYR B 1 57  ? 144.351 140.545 141.212 1.00 29.91  ? 57   TYR A O    1 
ATOM   4471 C CB   . TYR B 1 57  ? 146.269 139.235 138.835 1.00 21.41  ? 57   TYR A CB   1 
ATOM   4472 C CG   . TYR B 1 57  ? 147.260 139.470 139.949 1.00 24.42  ? 57   TYR A CG   1 
ATOM   4473 C CD1  . TYR B 1 57  ? 147.449 138.523 140.944 1.00 15.23  ? 57   TYR A CD1  1 
ATOM   4474 C CD2  . TYR B 1 57  ? 147.952 140.670 140.049 1.00 33.32  ? 57   TYR A CD2  1 
ATOM   4475 C CE1  . TYR B 1 57  ? 148.341 138.738 141.976 1.00 9.99   ? 57   TYR A CE1  1 
ATOM   4476 C CE2  . TYR B 1 57  ? 148.847 140.894 141.079 1.00 26.50  ? 57   TYR A CE2  1 
ATOM   4477 C CZ   . TYR B 1 57  ? 149.034 139.925 142.040 1.00 14.99  ? 57   TYR A CZ   1 
ATOM   4478 O OH   . TYR B 1 57  ? 149.921 140.140 143.068 1.00 14.63  ? 57   TYR A OH   1 
ATOM   4479 N N    . ILE B 1 58  ? 144.151 141.465 139.159 1.00 16.15  ? 58   ILE A N    1 
ATOM   4480 C CA   . ILE B 1 58  ? 143.810 142.786 139.680 1.00 3.56   ? 58   ILE A CA   1 
ATOM   4481 C C    . ILE B 1 58  ? 142.523 142.690 140.490 1.00 21.39  ? 58   ILE A C    1 
ATOM   4482 O O    . ILE B 1 58  ? 142.427 143.214 141.604 1.00 29.33  ? 58   ILE A O    1 
ATOM   4483 C CB   . ILE B 1 58  ? 143.698 143.805 138.531 1.00 10.18  ? 58   ILE A CB   1 
ATOM   4484 C CG1  . ILE B 1 58  ? 145.079 144.356 138.182 1.00 20.54  ? 58   ILE A CG1  1 
ATOM   4485 C CG2  . ILE B 1 58  ? 142.769 144.947 138.900 1.00 24.53  ? 58   ILE A CG2  1 
ATOM   4486 C CD1  . ILE B 1 58  ? 145.131 145.075 136.853 1.00 27.12  ? 58   ILE A CD1  1 
ATOM   4487 N N    . ALA B 1 59  ? 141.521 141.996 139.939 1.00 24.48  ? 59   ALA A N    1 
ATOM   4488 C CA   . ALA B 1 59  ? 140.239 141.823 140.617 1.00 6.55   ? 59   ALA A CA   1 
ATOM   4489 C C    . ALA B 1 59  ? 140.413 141.063 141.926 1.00 10.69  ? 59   ALA A C    1 
ATOM   4490 O O    . ALA B 1 59  ? 139.815 141.414 142.948 1.00 15.97  ? 59   ALA A O    1 
ATOM   4491 C CB   . ALA B 1 59  ? 139.260 141.092 139.703 1.00 8.46   ? 59   ALA A CB   1 
ATOM   4492 N N    . GLY B 1 60  ? 141.215 139.995 141.900 1.00 32.39  ? 60   GLY A N    1 
ATOM   4493 C CA   . GLY B 1 60  ? 141.425 139.197 143.096 1.00 24.78  ? 60   GLY A CA   1 
ATOM   4494 C C    . GLY B 1 60  ? 142.090 139.966 144.221 1.00 21.93  ? 60   GLY A C    1 
ATOM   4495 O O    . GLY B 1 60  ? 141.666 139.881 145.375 1.00 22.94  ? 60   GLY A O    1 
ATOM   4496 N N    . ARG B 1 61  ? 143.154 140.713 143.909 1.00 29.98  ? 61   ARG A N    1 
ATOM   4497 C CA   . ARG B 1 61  ? 143.861 141.424 144.972 1.00 40.42  ? 61   ARG A CA   1 
ATOM   4498 C C    . ARG B 1 61  ? 143.094 142.662 145.431 1.00 41.85  ? 61   ARG A C    1 
ATOM   4499 O O    . ARG B 1 61  ? 143.190 143.057 146.599 1.00 35.41  ? 61   ARG A O    1 
ATOM   4500 C CB   . ARG B 1 61  ? 145.254 141.802 144.475 1.00 34.98  ? 61   ARG A CB   1 
ATOM   4501 C CG   . ARG B 1 61  ? 146.383 141.585 145.457 1.00 32.85  ? 61   ARG A CG   1 
ATOM   4502 C CD   . ARG B 1 61  ? 147.691 141.989 144.809 1.00 37.91  ? 61   ARG A CD   1 
ATOM   4503 N NE   . ARG B 1 61  ? 148.677 142.488 145.757 1.00 41.45  ? 61   ARG A NE   1 
ATOM   4504 C CZ   . ARG B 1 61  ? 149.599 143.392 145.457 1.00 39.35  ? 61   ARG A CZ   1 
ATOM   4505 N NH1  . ARG B 1 61  ? 149.688 143.910 144.244 1.00 37.10  ? 61   ARG A NH1  1 
ATOM   4506 N NH2  . ARG B 1 61  ? 150.448 143.789 146.397 1.00 40.67  ? 61   ARG A NH2  1 
ATOM   4507 N N    . ALA B 1 62  ? 142.348 143.304 144.522 1.00 39.60  ? 62   ALA A N    1 
ATOM   4508 C CA   . ALA B 1 62  ? 141.477 144.427 144.886 1.00 29.92  ? 62   ALA A CA   1 
ATOM   4509 C C    . ALA B 1 62  ? 140.412 144.039 145.915 1.00 34.19  ? 62   ALA A C    1 
ATOM   4510 O O    . ALA B 1 62  ? 139.669 144.905 146.393 1.00 38.87  ? 62   ALA A O    1 
ATOM   4511 C CB   . ALA B 1 62  ? 140.821 145.020 143.642 1.00 30.01  ? 62   ALA A CB   1 
ATOM   4512 N N    . ASN B 1 63  ? 140.270 142.734 146.193 1.00 39.57  ? 63   ASN A N    1 
ATOM   4513 C CA   . ASN B 1 63  ? 139.508 142.122 147.284 1.00 32.17  ? 63   ASN A CA   1 
ATOM   4514 C C    . ASN B 1 63  ? 138.035 142.041 146.900 1.00 25.02  ? 63   ASN A C    1 
ATOM   4515 O O    . ASN B 1 63  ? 137.179 141.748 147.741 1.00 29.84  ? 63   ASN A O    1 
ATOM   4516 C CB   . ASN B 1 63  ? 139.690 142.864 148.613 1.00 27.62  ? 63   ASN A CB   1 
ATOM   4517 C CG   . ASN B 1 63  ? 140.077 141.939 149.746 1.00 38.93  ? 63   ASN A CG   1 
ATOM   4518 O OD1  . ASN B 1 63  ? 139.338 141.017 150.086 1.00 37.23  ? 63   ASN A OD1  1 
ATOM   4519 N ND2  . ASN B 1 63  ? 141.236 142.187 150.345 1.00 41.41  ? 63   ASN A ND2  1 
ATOM   4520 N N    . VAL B 1 64  ? 137.742 142.333 145.631 1.00 20.99  ? 64   VAL A N    1 
ATOM   4521 C CA   . VAL B 1 64  ? 136.374 142.336 145.118 1.00 22.31  ? 64   VAL A CA   1 
ATOM   4522 C C    . VAL B 1 64  ? 135.741 140.951 145.217 1.00 31.87  ? 64   VAL A C    1 
ATOM   4523 O O    . VAL B 1 64  ? 134.596 140.808 145.660 1.00 46.94  ? 64   VAL A O    1 
ATOM   4524 C CB   . VAL B 1 64  ? 136.344 142.862 143.670 1.00 20.50  ? 64   VAL A CB   1 
ATOM   4525 C CG1  . VAL B 1 64  ? 134.951 143.335 143.306 1.00 22.21  ? 64   VAL A CG1  1 
ATOM   4526 C CG2  . VAL B 1 64  ? 137.327 143.996 143.506 1.00 30.07  ? 64   VAL A CG2  1 
ATOM   4527 N N    . ILE B 1 65  ? 136.473 139.914 144.810 1.00 18.30  ? 65   ILE A N    1 
ATOM   4528 C CA   . ILE B 1 65  ? 136.002 138.529 144.844 1.00 19.21  ? 65   ILE A CA   1 
ATOM   4529 C C    . ILE B 1 65  ? 136.997 137.693 145.639 1.00 30.79  ? 65   ILE A C    1 
ATOM   4530 O O    . ILE B 1 65  ? 138.016 137.244 145.100 1.00 44.43  ? 65   ILE A O    1 
ATOM   4531 C CB   . ILE B 1 65  ? 135.812 137.947 143.437 1.00 11.53  ? 65   ILE A CB   1 
ATOM   4532 C CG1  . ILE B 1 65  ? 135.354 139.019 142.447 1.00 16.55  ? 65   ILE A CG1  1 
ATOM   4533 C CG2  . ILE B 1 65  ? 134.844 136.782 143.466 1.00 23.29  ? 65   ILE A CG2  1 
ATOM   4534 C CD1  . ILE B 1 65  ? 135.501 138.610 141.003 1.00 24.04  ? 65   ILE A CD1  1 
ATOM   4535 N N    . THR B 1 66  ? 136.712 137.493 146.924 1.00 24.99  ? 66   THR A N    1 
ATOM   4536 C CA   . THR B 1 66  ? 137.624 136.816 147.836 1.00 22.20  ? 66   THR A CA   1 
ATOM   4537 C C    . THR B 1 66  ? 137.779 135.334 147.465 1.00 29.76  ? 66   THR A C    1 
ATOM   4538 O O    . THR B 1 66  ? 137.175 134.826 146.516 1.00 45.35  ? 66   THR A O    1 
ATOM   4539 C CB   . THR B 1 66  ? 137.139 136.970 149.276 1.00 29.08  ? 66   THR A CB   1 
ATOM   4540 O OG1  . THR B 1 66  ? 138.169 136.544 150.177 1.00 41.17  ? 66   THR A OG1  1 
ATOM   4541 C CG2  . THR B 1 66  ? 135.888 136.142 149.515 1.00 30.52  ? 66   THR A CG2  1 
ATOM   4542 N N    . SER B 1 67  ? 138.613 134.639 148.247 1.00 28.48  ? 67   SER A N    1 
ATOM   4543 C CA   . SER B 1 67  ? 138.938 133.235 147.992 1.00 38.33  ? 67   SER A CA   1 
ATOM   4544 C C    . SER B 1 67  ? 137.720 132.317 148.086 1.00 36.25  ? 67   SER A C    1 
ATOM   4545 O O    . SER B 1 67  ? 137.519 131.449 147.221 1.00 31.16  ? 67   SER A O    1 
ATOM   4546 C CB   . SER B 1 67  ? 140.020 132.774 148.967 1.00 37.32  ? 67   SER A CB   1 
ATOM   4547 O OG   . SER B 1 67  ? 141.035 133.752 149.101 1.00 39.86  ? 67   SER A OG   1 
ATOM   4548 N N    . THR B 1 68  ? 136.866 132.532 149.093 1.00 34.32  ? 68   THR A N    1 
ATOM   4549 C CA   . THR B 1 68  ? 135.682 131.692 149.253 1.00 32.34  ? 68   THR A CA   1 
ATOM   4550 C C    . THR B 1 68  ? 134.731 131.858 148.081 1.00 33.79  ? 68   THR A C    1 
ATOM   4551 O O    . THR B 1 68  ? 134.196 130.869 147.567 1.00 41.30  ? 68   THR A O    1 
ATOM   4552 C CB   . THR B 1 68  ? 134.974 132.027 150.566 1.00 30.01  ? 68   THR A CB   1 
ATOM   4553 O OG1  . THR B 1 68  ? 135.912 131.959 151.647 1.00 38.82  ? 68   THR A OG1  1 
ATOM   4554 C CG2  . THR B 1 68  ? 133.841 131.048 150.826 1.00 29.53  ? 68   THR A CG2  1 
ATOM   4555 N N    . GLN B 1 69  ? 134.485 133.097 147.661 1.00 29.98  ? 69   GLN A N    1 
ATOM   4556 C CA   . GLN B 1 69  ? 133.619 133.311 146.510 1.00 23.16  ? 69   GLN A CA   1 
ATOM   4557 C C    . GLN B 1 69  ? 134.248 132.713 145.253 1.00 25.38  ? 69   GLN A C    1 
ATOM   4558 O O    . GLN B 1 69  ? 133.544 132.187 144.383 1.00 38.29  ? 69   GLN A O    1 
ATOM   4559 C CB   . GLN B 1 69  ? 133.343 134.804 146.343 1.00 22.86  ? 69   GLN A CB   1 
ATOM   4560 C CG   . GLN B 1 69  ? 132.419 135.381 147.402 1.00 31.64  ? 69   GLN A CG   1 
ATOM   4561 C CD   . GLN B 1 69  ? 132.570 136.881 147.562 1.00 38.31  ? 69   GLN A CD   1 
ATOM   4562 O OE1  . GLN B 1 69  ? 132.981 137.366 148.614 1.00 41.41  ? 69   GLN A OE1  1 
ATOM   4563 N NE2  . GLN B 1 69  ? 132.229 137.624 146.517 1.00 28.99  ? 69   GLN A NE2  1 
ATOM   4564 N N    . ALA B 1 70  ? 135.578 132.804 145.143 1.00 18.09  ? 70   ALA A N    1 
ATOM   4565 C CA   . ALA B 1 70  ? 136.323 132.239 144.018 1.00 17.06  ? 70   ALA A CA   1 
ATOM   4566 C C    . ALA B 1 70  ? 136.165 130.726 143.899 1.00 17.57  ? 70   ALA A C    1 
ATOM   4567 O O    . ALA B 1 70  ? 136.251 130.179 142.786 1.00 25.69  ? 70   ALA A O    1 
ATOM   4568 C CB   . ALA B 1 70  ? 137.802 132.592 144.141 1.00 14.22  ? 70   ALA A CB   1 
ATOM   4569 N N    . LYS B 1 71  ? 135.964 130.028 145.025 1.00 12.03  ? 71   LYS A N    1 
ATOM   4570 C CA   . LYS B 1 71  ? 135.772 128.579 144.942 1.00 20.44  ? 71   LYS A CA   1 
ATOM   4571 C C    . LYS B 1 71  ? 134.542 128.200 144.124 1.00 19.34  ? 71   LYS A C    1 
ATOM   4572 O O    . LYS B 1 71  ? 134.546 127.159 143.455 1.00 29.74  ? 71   LYS A O    1 
ATOM   4573 C CB   . LYS B 1 71  ? 135.652 127.960 146.336 1.00 22.93  ? 71   LYS A CB   1 
ATOM   4574 C CG   . LYS B 1 71  ? 136.669 128.431 147.346 1.00 26.38  ? 71   LYS A CG   1 
ATOM   4575 C CD   . LYS B 1 71  ? 137.880 127.520 147.382 1.00 24.84  ? 71   LYS A CD   1 
ATOM   4576 C CE   . LYS B 1 71  ? 139.037 128.177 148.116 1.00 29.59  ? 71   LYS A CE   1 
ATOM   4577 N NZ   . LYS B 1 71  ? 139.676 129.246 147.300 1.00 32.02  ? 71   LYS A NZ   1 
ATOM   4578 N N    . GLY B 1 72  ? 133.493 129.023 144.140 1.00 11.24  ? 72   GLY A N    1 
ATOM   4579 C CA   . GLY B 1 72  ? 132.328 128.702 143.332 1.00 12.33  ? 72   GLY A CA   1 
ATOM   4580 C C    . GLY B 1 72  ? 132.592 128.808 141.843 1.00 17.40  ? 72   GLY A C    1 
ATOM   4581 O O    . GLY B 1 72  ? 132.143 127.961 141.062 1.00 27.20  ? 72   GLY A O    1 
ATOM   4582 N N    . LEU B 1 73  ? 133.332 129.841 141.424 1.00 8.65   ? 73   LEU A N    1 
ATOM   4583 C CA   . LEU B 1 73  ? 133.697 129.937 140.017 1.00 12.76  ? 73   LEU A CA   1 
ATOM   4584 C C    . LEU B 1 73  ? 134.653 128.830 139.600 1.00 15.54  ? 73   LEU A C    1 
ATOM   4585 O O    . LEU B 1 73  ? 134.569 128.337 138.464 1.00 10.03  ? 73   LEU A O    1 
ATOM   4586 C CB   . LEU B 1 73  ? 134.331 131.301 139.744 1.00 9.84   ? 73   LEU A CB   1 
ATOM   4587 C CG   . LEU B 1 73  ? 134.735 131.660 138.315 1.00 0.00   ? 73   LEU A CG   1 
ATOM   4588 C CD1  . LEU B 1 73  ? 133.563 131.549 137.379 1.00 11.51  ? 73   LEU A CD1  1 
ATOM   4589 C CD2  . LEU B 1 73  ? 135.323 133.059 138.271 1.00 8.71   ? 73   LEU A CD2  1 
ATOM   4590 N N    . GLY B 1 74  ? 135.472 128.333 140.532 1.00 14.04  ? 74   GLY A N    1 
ATOM   4591 C CA   . GLY B 1 74  ? 136.293 127.184 140.194 1.00 8.99   ? 74   GLY A CA   1 
ATOM   4592 C C    . GLY B 1 74  ? 135.471 125.924 140.022 1.00 14.37  ? 74   GLY A C    1 
ATOM   4593 O O    . GLY B 1 74  ? 135.700 125.146 139.088 1.00 24.33  ? 74   GLY A O    1 
ATOM   4594 N N    . ASN B 1 75  ? 134.485 125.720 140.902 1.00 8.27   ? 75   ASN A N    1 
ATOM   4595 C CA   . ASN B 1 75  ? 133.650 124.527 140.813 1.00 3.14   ? 75   ASN A CA   1 
ATOM   4596 C C    . ASN B 1 75  ? 132.828 124.532 139.534 1.00 15.85  ? 75   ASN A C    1 
ATOM   4597 O O    . ASN B 1 75  ? 132.754 123.514 138.830 1.00 21.68  ? 75   ASN A O    1 
ATOM   4598 C CB   . ASN B 1 75  ? 132.728 124.428 142.028 1.00 3.66   ? 75   ASN A CB   1 
ATOM   4599 C CG   . ASN B 1 75  ? 133.417 123.845 143.239 1.00 22.13  ? 75   ASN A CG   1 
ATOM   4600 O OD1  . ASN B 1 75  ? 134.382 123.093 143.115 1.00 36.87  ? 75   ASN A OD1  1 
ATOM   4601 N ND2  . ASN B 1 75  ? 132.917 124.180 144.422 1.00 14.92  ? 75   ASN A ND2  1 
ATOM   4602 N N    . PHE B 1 76  ? 132.340 125.716 139.146 1.00 8.77   ? 76   PHE A N    1 
ATOM   4603 C CA   . PHE B 1 76  ? 131.579 125.850 137.909 1.00 0.00   ? 76   PHE A CA   1 
ATOM   4604 C C    . PHE B 1 76  ? 132.437 125.553 136.691 1.00 9.34   ? 76   PHE A C    1 
ATOM   4605 O O    . PHE B 1 76  ? 132.062 124.716 135.862 1.00 15.90  ? 76   PHE A O    1 
ATOM   4606 C CB   . PHE B 1 76  ? 130.976 127.253 137.807 1.00 11.25  ? 76   PHE A CB   1 
ATOM   4607 C CG   . PHE B 1 76  ? 130.699 127.703 136.391 1.00 19.86  ? 76   PHE A CG   1 
ATOM   4608 C CD1  . PHE B 1 76  ? 129.751 127.059 135.608 1.00 12.13  ? 76   PHE A CD1  1 
ATOM   4609 C CD2  . PHE B 1 76  ? 131.386 128.774 135.846 1.00 18.38  ? 76   PHE A CD2  1 
ATOM   4610 C CE1  . PHE B 1 76  ? 129.501 127.473 134.313 1.00 4.08   ? 76   PHE A CE1  1 
ATOM   4611 C CE2  . PHE B 1 76  ? 131.137 129.190 134.551 1.00 3.72   ? 76   PHE A CE2  1 
ATOM   4612 C CZ   . PHE B 1 76  ? 130.195 128.539 133.786 1.00 4.25   ? 76   PHE A CZ   1 
ATOM   4613 N N    . VAL B 1 77  ? 133.639 126.130 136.617 1.00 22.21  ? 77   VAL A N    1 
ATOM   4614 C CA   . VAL B 1 77  ? 134.429 125.953 135.402 1.00 16.43  ? 77   VAL A CA   1 
ATOM   4615 C C    . VAL B 1 77  ? 134.907 124.516 135.285 1.00 21.46  ? 77   VAL A C    1 
ATOM   4616 O O    . VAL B 1 77  ? 134.575 123.834 134.303 1.00 24.66  ? 77   VAL A O    1 
ATOM   4617 C CB   . VAL B 1 77  ? 135.614 126.931 135.386 1.00 7.59   ? 77   VAL A CB   1 
ATOM   4618 C CG1  . VAL B 1 77  ? 136.567 126.586 134.259 1.00 9.36   ? 77   VAL A CG1  1 
ATOM   4619 C CG2  . VAL B 1 77  ? 135.118 128.331 135.239 1.00 11.04  ? 77   VAL A CG2  1 
ATOM   4620 N N    . SER B 1 78  ? 135.425 123.973 136.390 1.00 9.36   ? 78   SER A N    1 
ATOM   4621 C CA   . SER B 1 78  ? 136.098 122.684 136.463 1.00 0.00   ? 78   SER A CA   1 
ATOM   4622 C C    . SER B 1 78  ? 135.133 121.514 136.374 1.00 18.19  ? 78   SER A C    1 
ATOM   4623 O O    . SER B 1 78  ? 135.545 120.400 136.036 1.00 39.79  ? 78   SER A O    1 
ATOM   4624 C CB   . SER B 1 78  ? 136.908 122.590 137.756 1.00 12.82  ? 78   SER A CB   1 
ATOM   4625 O OG   . SER B 1 78  ? 137.960 123.538 137.765 1.00 27.84  ? 78   SER A OG   1 
ATOM   4626 N N    . ARG B 1 79  ? 133.853 121.737 136.670 1.00 12.30  ? 79   ARG A N    1 
ATOM   4627 C CA   . ARG B 1 79  ? 132.930 120.614 136.692 1.00 9.68   ? 79   ARG A CA   1 
ATOM   4628 C C    . ARG B 1 79  ? 131.871 120.730 135.604 1.00 13.48  ? 79   ARG A C    1 
ATOM   4629 O O    . ARG B 1 79  ? 131.222 119.730 135.282 1.00 19.95  ? 79   ARG A O    1 
ATOM   4630 C CB   . ARG B 1 79  ? 132.301 120.505 138.080 1.00 2.79   ? 79   ARG A CB   1 
ATOM   4631 C CG   . ARG B 1 79  ? 133.335 120.156 139.145 1.00 16.60  ? 79   ARG A CG   1 
ATOM   4632 C CD   . ARG B 1 79  ? 132.868 120.483 140.556 1.00 22.36  ? 79   ARG A CD   1 
ATOM   4633 N NE   . ARG B 1 79  ? 132.534 119.290 141.326 1.00 27.99  ? 79   ARG A NE   1 
ATOM   4634 C CZ   . ARG B 1 79  ? 133.424 118.445 141.831 1.00 34.98  ? 79   ARG A CZ   1 
ATOM   4635 N NH1  . ARG B 1 79  ? 134.724 118.627 141.666 1.00 29.16  ? 79   ARG A NH1  1 
ATOM   4636 N NH2  . ARG B 1 79  ? 132.999 117.393 142.523 1.00 32.08  ? 79   ARG A NH2  1 
ATOM   4637 N N    . PHE B 1 80  ? 131.673 121.920 135.037 1.00 19.03  ? 80   PHE A N    1 
ATOM   4638 C CA   . PHE B 1 80  ? 130.651 122.164 134.032 1.00 12.59  ? 80   PHE A CA   1 
ATOM   4639 C C    . PHE B 1 80  ? 131.189 122.537 132.657 1.00 8.63   ? 80   PHE A C    1 
ATOM   4640 O O    . PHE B 1 80  ? 130.808 121.899 131.669 1.00 15.12  ? 80   PHE A O    1 
ATOM   4641 C CB   . PHE B 1 80  ? 129.668 123.224 134.547 1.00 14.02  ? 80   PHE A CB   1 
ATOM   4642 C CG   . PHE B 1 80  ? 128.717 122.691 135.582 1.00 7.06   ? 80   PHE A CG   1 
ATOM   4643 C CD1  . PHE B 1 80  ? 127.751 121.762 135.231 1.00 5.35   ? 80   PHE A CD1  1 
ATOM   4644 C CD2  . PHE B 1 80  ? 128.814 123.078 136.907 1.00 14.24  ? 80   PHE A CD2  1 
ATOM   4645 C CE1  . PHE B 1 80  ? 126.882 121.254 136.173 1.00 15.60  ? 80   PHE A CE1  1 
ATOM   4646 C CE2  . PHE B 1 80  ? 127.947 122.568 137.856 1.00 15.14  ? 80   PHE A CE2  1 
ATOM   4647 C CZ   . PHE B 1 80  ? 126.980 121.656 137.486 1.00 19.78  ? 80   PHE A CZ   1 
ATOM   4648 N N    . ALA B 1 81  ? 132.052 123.556 132.541 1.00 2.30   ? 81   ALA A N    1 
ATOM   4649 C CA   . ALA B 1 81  ? 132.451 124.004 131.205 1.00 10.45  ? 81   ALA A CA   1 
ATOM   4650 C C    . ALA B 1 81  ? 133.379 123.028 130.484 1.00 19.17  ? 81   ALA A C    1 
ATOM   4651 O O    . ALA B 1 81  ? 133.178 122.755 129.295 1.00 24.63  ? 81   ALA A O    1 
ATOM   4652 C CB   . ALA B 1 81  ? 133.106 125.379 131.303 1.00 14.07  ? 81   ALA A CB   1 
ATOM   4653 N N    . LEU B 1 82  ? 134.402 122.513 131.157 1.00 15.87  ? 82   LEU A N    1 
ATOM   4654 C CA   . LEU B 1 82  ? 135.357 121.619 130.498 1.00 15.72  ? 82   LEU A CA   1 
ATOM   4655 C C    . LEU B 1 82  ? 134.753 120.308 129.978 1.00 25.60  ? 82   LEU A C    1 
ATOM   4656 O O    . LEU B 1 82  ? 135.053 119.939 128.824 1.00 29.94  ? 82   LEU A O    1 
ATOM   4657 C CB   . LEU B 1 82  ? 136.547 121.372 131.436 1.00 25.04  ? 82   LEU A CB   1 
ATOM   4658 C CG   . LEU B 1 82  ? 137.637 120.407 130.970 1.00 30.78  ? 82   LEU A CG   1 
ATOM   4659 C CD1  . LEU B 1 82  ? 138.230 120.876 129.652 1.00 22.34  ? 82   LEU A CD1  1 
ATOM   4660 C CD2  . LEU B 1 82  ? 138.718 120.263 132.029 1.00 28.99  ? 82   LEU A CD2  1 
ATOM   4661 N N    . PRO B 1 83  ? 133.948 119.548 130.748 1.00 26.26  ? 83   PRO A N    1 
ATOM   4662 C CA   . PRO B 1 83  ? 133.376 118.305 130.191 1.00 17.92  ? 83   PRO A CA   1 
ATOM   4663 C C    . PRO B 1 83  ? 132.529 118.468 128.938 1.00 19.14  ? 83   PRO A C    1 
ATOM   4664 O O    . PRO B 1 83  ? 132.587 117.591 128.068 1.00 28.30  ? 83   PRO A O    1 
ATOM   4665 C CB   . PRO B 1 83  ? 132.517 117.784 131.347 1.00 18.71  ? 83   PRO A CB   1 
ATOM   4666 C CG   . PRO B 1 83  ? 133.204 118.252 132.540 1.00 24.68  ? 83   PRO A CG   1 
ATOM   4667 C CD   . PRO B 1 83  ? 133.667 119.633 132.196 1.00 21.49  ? 83   PRO A CD   1 
ATOM   4668 N N    . ALA B 1 84  ? 131.830 119.590 128.754 1.00 19.99  ? 84   ALA A N    1 
ATOM   4669 C CA   . ALA B 1 84  ? 131.038 119.726 127.536 1.00 23.42  ? 84   ALA A CA   1 
ATOM   4670 C C    . ALA B 1 84  ? 131.918 120.037 126.337 1.00 22.68  ? 84   ALA A C    1 
ATOM   4671 O O    . ALA B 1 84  ? 131.642 119.560 125.227 1.00 30.61  ? 84   ALA A O    1 
ATOM   4672 C CB   . ALA B 1 84  ? 129.979 120.813 127.710 1.00 30.22  ? 84   ALA A CB   1 
ATOM   4673 N N    . LEU B 1 85  ? 133.038 120.719 126.572 1.00 22.25  ? 85   LEU A N    1 
ATOM   4674 C CA   . LEU B 1 85  ? 133.959 121.041 125.492 1.00 25.31  ? 85   LEU A CA   1 
ATOM   4675 C C    . LEU B 1 85  ? 134.632 119.766 125.009 1.00 29.76  ? 85   LEU A C    1 
ATOM   4676 O O    . LEU B 1 85  ? 134.678 119.487 123.797 1.00 24.78  ? 85   LEU A O    1 
ATOM   4677 C CB   . LEU B 1 85  ? 134.993 122.060 125.972 1.00 20.34  ? 85   LEU A CB   1 
ATOM   4678 C CG   . LEU B 1 85  ? 136.082 122.498 124.994 1.00 20.84  ? 85   LEU A CG   1 
ATOM   4679 C CD1  . LEU B 1 85  ? 135.463 123.242 123.825 1.00 21.85  ? 85   LEU A CD1  1 
ATOM   4680 C CD2  . LEU B 1 85  ? 137.124 123.354 125.689 1.00 25.88  ? 85   LEU A CD2  1 
ATOM   4681 N N    . LEU B 1 86  ? 135.131 118.960 125.957 1.00 27.90  ? 86   LEU A N    1 
ATOM   4682 C CA   . LEU B 1 86  ? 135.773 117.711 125.568 1.00 18.18  ? 86   LEU A CA   1 
ATOM   4683 C C    . LEU B 1 86  ? 134.768 116.772 124.915 1.00 31.38  ? 86   LEU A C    1 
ATOM   4684 O O    . LEU B 1 86  ? 135.102 116.099 123.933 1.00 37.91  ? 86   LEU A O    1 
ATOM   4685 C CB   . LEU B 1 86  ? 136.429 117.043 126.774 1.00 9.50   ? 86   LEU A CB   1 
ATOM   4686 C CG   . LEU B 1 86  ? 137.402 117.896 127.584 1.00 21.52  ? 86   LEU A CG   1 
ATOM   4687 C CD1  . LEU B 1 86  ? 138.065 117.058 128.658 1.00 35.31  ? 86   LEU A CD1  1 
ATOM   4688 C CD2  . LEU B 1 86  ? 138.446 118.513 126.672 1.00 17.90  ? 86   LEU A CD2  1 
ATOM   4689 N N    . PHE B 1 87  ? 133.538 116.698 125.449 1.00 34.16  ? 87   PHE A N    1 
ATOM   4690 C CA   . PHE B 1 87  ? 132.572 115.746 124.913 1.00 27.79  ? 87   PHE A CA   1 
ATOM   4691 C C    . PHE B 1 87  ? 132.212 116.101 123.477 1.00 26.44  ? 87   PHE A C    1 
ATOM   4692 O O    . PHE B 1 87  ? 132.211 115.228 122.599 1.00 33.14  ? 87   PHE A O    1 
ATOM   4693 C CB   . PHE B 1 87  ? 131.322 115.733 125.792 1.00 34.65  ? 87   PHE A CB   1 
ATOM   4694 C CG   . PHE B 1 87  ? 130.194 114.913 125.238 1.00 33.47  ? 87   PHE A CG   1 
ATOM   4695 C CD1  . PHE B 1 87  ? 130.287 113.537 125.168 1.00 36.24  ? 87   PHE A CD1  1 
ATOM   4696 C CD2  . PHE B 1 87  ? 129.040 115.525 124.778 1.00 32.88  ? 87   PHE A CD2  1 
ATOM   4697 C CE1  . PHE B 1 87  ? 129.249 112.782 124.655 1.00 39.40  ? 87   PHE A CE1  1 
ATOM   4698 C CE2  . PHE B 1 87  ? 127.999 114.776 124.263 1.00 35.64  ? 87   PHE A CE2  1 
ATOM   4699 C CZ   . PHE B 1 87  ? 128.104 113.403 124.202 1.00 39.58  ? 87   PHE A CZ   1 
ATOM   4700 N N    . LYS B 1 88  ? 132.011 117.397 123.203 1.00 21.92  ? 88   LYS A N    1 
ATOM   4701 C CA   . LYS B 1 88  ? 131.676 117.835 121.852 1.00 17.72  ? 88   LYS A CA   1 
ATOM   4702 C C    . LYS B 1 88  ? 132.814 117.528 120.888 1.00 29.87  ? 88   LYS A C    1 
ATOM   4703 O O    . LYS B 1 88  ? 132.606 116.915 119.827 1.00 30.81  ? 88   LYS A O    1 
ATOM   4704 C CB   . LYS B 1 88  ? 131.338 119.325 121.848 1.00 24.15  ? 88   LYS A CB   1 
ATOM   4705 C CG   . LYS B 1 88  ? 131.009 119.880 120.470 1.00 29.28  ? 88   LYS A CG   1 
ATOM   4706 C CD   . LYS B 1 88  ? 130.945 121.401 120.469 1.00 31.94  ? 88   LYS A CD   1 
ATOM   4707 C CE   . LYS B 1 88  ? 132.116 122.020 121.213 1.00 28.68  ? 88   LYS A CE   1 
ATOM   4708 N NZ   . LYS B 1 88  ? 132.048 123.506 121.223 1.00 28.40  ? 88   LYS A NZ   1 
ATOM   4709 N N    . ASN B 1 89  ? 134.038 117.934 121.254 1.00 33.13  ? 89   ASN A N    1 
ATOM   4710 C CA   . ASN B 1 89  ? 135.156 117.763 120.335 1.00 25.23  ? 89   ASN A CA   1 
ATOM   4711 C C    . ASN B 1 89  ? 135.433 116.288 120.078 1.00 27.57  ? 89   ASN A C    1 
ATOM   4712 O O    . ASN B 1 89  ? 135.684 115.895 118.936 1.00 25.80  ? 89   ASN A O    1 
ATOM   4713 C CB   . ASN B 1 89  ? 136.395 118.466 120.879 1.00 21.56  ? 89   ASN A CB   1 
ATOM   4714 C CG   . ASN B 1 89  ? 136.303 119.968 120.756 1.00 24.45  ? 89   ASN A CG   1 
ATOM   4715 O OD1  . ASN B 1 89  ? 136.458 120.525 119.670 1.00 22.57  ? 89   ASN A OD1  1 
ATOM   4716 N ND2  . ASN B 1 89  ? 136.035 120.633 121.868 1.00 28.39  ? 89   ASN A ND2  1 
ATOM   4717 N N    . MET B 1 90  ? 135.344 115.448 121.116 1.00 22.75  ? 90   MET A N    1 
ATOM   4718 C CA   . MET B 1 90  ? 135.544 114.016 120.921 1.00 23.50  ? 90   MET A CA   1 
ATOM   4719 C C    . MET B 1 90  ? 134.462 113.422 120.025 1.00 35.25  ? 90   MET A C    1 
ATOM   4720 O O    . MET B 1 90  ? 134.725 112.469 119.282 1.00 31.08  ? 90   MET A O    1 
ATOM   4721 C CB   . MET B 1 90  ? 135.579 113.303 122.270 1.00 22.42  ? 90   MET A CB   1 
ATOM   4722 C CG   . MET B 1 90  ? 136.713 112.309 122.405 1.00 34.44  ? 90   MET A CG   1 
ATOM   4723 S SD   . MET B 1 90  ? 138.337 113.065 122.203 1.00 30.60  ? 90   MET A SD   1 
ATOM   4724 C CE   . MET B 1 90  ? 138.267 114.361 123.435 1.00 24.23  ? 90   MET A CE   1 
ATOM   4725 N N    . VAL B 1 91  ? 133.242 113.965 120.088 1.00 44.70  ? 91   VAL A N    1 
ATOM   4726 C CA   . VAL B 1 91  ? 132.175 113.513 119.197 1.00 36.73  ? 91   VAL A CA   1 
ATOM   4727 C C    . VAL B 1 91  ? 132.503 113.831 117.741 1.00 32.56  ? 91   VAL A C    1 
ATOM   4728 O O    . VAL B 1 91  ? 132.280 113.002 116.850 1.00 34.97  ? 91   VAL A O    1 
ATOM   4729 C CB   . VAL B 1 91  ? 130.813 114.096 119.623 1.00 39.69  ? 91   VAL A CB   1 
ATOM   4730 C CG1  . VAL B 1 91  ? 129.766 113.849 118.556 1.00 38.26  ? 91   VAL A CG1  1 
ATOM   4731 C CG2  . VAL B 1 91  ? 130.338 113.411 120.884 1.00 36.36  ? 91   VAL A CG2  1 
ATOM   4732 N N    . VAL B 1 92  ? 133.086 115.008 117.469 1.00 39.15  ? 92   VAL A N    1 
ATOM   4733 C CA   . VAL B 1 92  ? 133.249 115.395 116.061 1.00 39.23  ? 92   VAL A CA   1 
ATOM   4734 C C    . VAL B 1 92  ? 134.555 114.919 115.401 1.00 46.74  ? 92   VAL A C    1 
ATOM   4735 O O    . VAL B 1 92  ? 134.696 115.054 114.174 1.00 47.08  ? 92   VAL A O    1 
ATOM   4736 C CB   . VAL B 1 92  ? 133.073 116.932 115.988 1.00 39.42  ? 92   VAL A CB   1 
ATOM   4737 C CG1  . VAL B 1 92  ? 132.932 117.457 114.557 1.00 40.41  ? 92   VAL A CG1  1 
ATOM   4738 C CG2  . VAL B 1 92  ? 131.854 117.351 116.777 1.00 43.29  ? 92   VAL A CG2  1 
ATOM   4739 N N    . LEU B 1 93  ? 135.491 114.318 116.145 1.00 53.03  ? 93   LEU A N    1 
ATOM   4740 C CA   . LEU B 1 93  ? 136.765 113.910 115.542 1.00 49.76  ? 93   LEU A CA   1 
ATOM   4741 C C    . LEU B 1 93  ? 136.567 112.846 114.462 1.00 50.95  ? 93   LEU A C    1 
ATOM   4742 O O    . LEU B 1 93  ? 135.773 111.916 114.622 1.00 54.38  ? 93   LEU A O    1 
ATOM   4743 C CB   . LEU B 1 93  ? 137.728 113.374 116.604 1.00 46.74  ? 93   LEU A CB   1 
ATOM   4744 C CG   . LEU B 1 93  ? 138.883 114.202 117.177 1.00 44.22  ? 93   LEU A CG   1 
ATOM   4745 C CD1  . LEU B 1 93  ? 138.488 115.580 117.639 1.00 46.37  ? 93   LEU A CD1  1 
ATOM   4746 C CD2  . LEU B 1 93  ? 139.486 113.419 118.333 1.00 45.14  ? 93   LEU A CD2  1 
ATOM   4747 N N    . ASN B 1 94  ? 137.295 112.995 113.350 1.00 62.63  ? 94   ASN A N    1 
ATOM   4748 C CA   . ASN B 1 94  ? 137.250 112.063 112.220 1.00 69.09  ? 94   ASN A CA   1 
ATOM   4749 C C    . ASN B 1 94  ? 138.536 111.227 112.233 1.00 69.48  ? 94   ASN A C    1 
ATOM   4750 O O    . ASN B 1 94  ? 139.603 111.707 111.842 1.00 67.42  ? 94   ASN A O    1 
ATOM   4751 C CB   . ASN B 1 94  ? 137.012 112.840 110.916 1.00 71.09  ? 94   ASN A CB   1 
ATOM   4752 C CG   . ASN B 1 94  ? 137.541 112.139 109.664 1.00 71.06  ? 94   ASN A CG   1 
ATOM   4753 O OD1  . ASN B 1 94  ? 138.732 112.169 109.354 1.00 67.05  ? 94   ASN A OD1  1 
ATOM   4754 N ND2  . ASN B 1 94  ? 136.634 111.501 108.934 1.00 70.01  ? 94   ASN A ND2  1 
ATOM   4755 N N    . PHE B 1 95  ? 138.459 110.016 112.787 1.00 67.34  ? 95   PHE A N    1 
ATOM   4756 C CA   . PHE B 1 95  ? 139.638 109.160 112.918 1.00 63.68  ? 95   PHE A CA   1 
ATOM   4757 C C    . PHE B 1 95  ? 140.184 108.596 111.607 1.00 69.21  ? 95   PHE A C    1 
ATOM   4758 O O    . PHE B 1 95  ? 140.283 107.373 111.466 1.00 68.45  ? 95   PHE A O    1 
ATOM   4759 C CB   . PHE B 1 95  ? 139.345 107.992 113.863 1.00 60.62  ? 95   PHE A CB   1 
ATOM   4760 C CG   . PHE B 1 95  ? 139.176 108.394 115.295 1.00 61.14  ? 95   PHE A CG   1 
ATOM   4761 C CD1  . PHE B 1 95  ? 140.276 108.769 116.047 1.00 63.15  ? 95   PHE A CD1  1 
ATOM   4762 C CD2  . PHE B 1 95  ? 137.932 108.377 115.897 1.00 68.85  ? 95   PHE A CD2  1 
ATOM   4763 C CE1  . PHE B 1 95  ? 140.137 109.132 117.371 1.00 68.12  ? 95   PHE A CE1  1 
ATOM   4764 C CE2  . PHE B 1 95  ? 137.786 108.739 117.223 1.00 69.35  ? 95   PHE A CE2  1 
ATOM   4765 C CZ   . PHE B 1 95  ? 138.890 109.117 117.960 1.00 69.32  ? 95   PHE A CZ   1 
ATOM   4766 N N    . SER B 1 96  ? 140.534 109.444 110.639 1.00 72.20  ? 96   SER A N    1 
ATOM   4767 C CA   . SER B 1 96  ? 141.102 108.938 109.387 1.00 69.29  ? 96   SER A CA   1 
ATOM   4768 C C    . SER B 1 96  ? 142.266 109.754 108.841 1.00 70.42  ? 96   SER A C    1 
ATOM   4769 O O    . SER B 1 96  ? 143.053 109.214 108.057 1.00 72.53  ? 96   SER A O    1 
ATOM   4770 C CB   . SER B 1 96  ? 140.021 108.832 108.304 1.00 68.98  ? 96   SER A CB   1 
ATOM   4771 O OG   . SER B 1 96  ? 139.217 109.995 108.253 1.00 70.18  ? 96   SER A OG   1 
ATOM   4772 N N    . ASN B 1 97  ? 142.403 111.025 109.206 1.00 67.41  ? 97   ASN A N    1 
ATOM   4773 C CA   . ASN B 1 97  ? 143.412 111.927 108.666 1.00 67.90  ? 97   ASN A CA   1 
ATOM   4774 C C    . ASN B 1 97  ? 144.495 112.250 109.687 1.00 70.94  ? 97   ASN A C    1 
ATOM   4775 O O    . ASN B 1 97  ? 145.329 113.123 109.437 1.00 70.67  ? 97   ASN A O    1 
ATOM   4776 C CB   . ASN B 1 97  ? 142.748 113.212 108.162 1.00 68.46  ? 97   ASN A CB   1 
ATOM   4777 C CG   . ASN B 1 97  ? 142.060 113.979 109.270 1.00 66.58  ? 97   ASN A CG   1 
ATOM   4778 O OD1  . ASN B 1 97  ? 141.306 113.406 110.058 1.00 65.55  ? 97   ASN A OD1  1 
ATOM   4779 N ND2  . ASN B 1 97  ? 142.315 115.279 109.339 1.00 64.86  ? 97   ASN A ND2  1 
ATOM   4780 N N    . VAL B 1 98  ? 144.501 111.569 110.828 1.00 68.63  ? 98   VAL A N    1 
ATOM   4781 C CA   . VAL B 1 98  ? 145.458 111.846 111.895 1.00 67.53  ? 98   VAL A CA   1 
ATOM   4782 C C    . VAL B 1 98  ? 146.795 111.156 111.653 1.00 68.83  ? 98   VAL A C    1 
ATOM   4783 O O    . VAL B 1 98  ? 146.869 109.945 111.410 1.00 70.69  ? 98   VAL A O    1 
ATOM   4784 C CB   . VAL B 1 98  ? 144.876 111.464 113.266 1.00 63.05  ? 98   VAL A CB   1 
ATOM   4785 C CG1  . VAL B 1 98  ? 143.761 112.410 113.626 1.00 64.62  ? 98   VAL A CG1  1 
ATOM   4786 C CG2  . VAL B 1 98  ? 144.338 110.041 113.247 1.00 58.90  ? 98   VAL A CG2  1 
ATOM   4787 N N    . ASP B 1 99  ? 147.854 111.960 111.652 1.00 63.92  ? 99   ASP A N    1 
ATOM   4788 C CA   . ASP B 1 99  ? 149.224 111.478 111.519 1.00 64.20  ? 99   ASP A CA   1 
ATOM   4789 C C    . ASP B 1 99  ? 149.641 110.950 112.889 1.00 67.24  ? 99   ASP A C    1 
ATOM   4790 O O    . ASP B 1 99  ? 149.958 111.721 113.801 1.00 74.23  ? 99   ASP A O    1 
ATOM   4791 C CB   . ASP B 1 99  ? 150.144 112.592 111.040 1.00 62.15  ? 99   ASP A CB   1 
ATOM   4792 C CG   . ASP B 1 99  ? 149.685 113.200 109.734 1.00 62.09  ? 99   ASP A CG   1 
ATOM   4793 O OD1  . ASP B 1 99  ? 148.893 112.550 109.019 1.00 64.43  ? 99   ASP A OD1  1 
ATOM   4794 O OD2  . ASP B 1 99  ? 150.076 114.348 109.441 1.00 63.70  ? 99   ASP A OD2  1 
ATOM   4795 N N    . TRP B 1 100 ? 149.678 109.622 113.011 1.00 62.56  ? 100  TRP A N    1 
ATOM   4796 C CA   . TRP B 1 100 ? 149.953 108.927 114.268 1.00 61.57  ? 100  TRP A CA   1 
ATOM   4797 C C    . TRP B 1 100 ? 151.412 108.995 114.720 1.00 65.01  ? 100  TRP A C    1 
ATOM   4798 O O    . TRP B 1 100 ? 151.663 108.923 115.929 1.00 68.17  ? 100  TRP A O    1 
ATOM   4799 C CB   . TRP B 1 100 ? 149.563 107.454 114.117 1.00 63.39  ? 100  TRP A CB   1 
ATOM   4800 C CG   . TRP B 1 100 ? 148.079 107.193 113.933 1.00 69.54  ? 100  TRP A CG   1 
ATOM   4801 C CD1  . TRP B 1 100 ? 147.424 107.021 112.744 1.00 70.66  ? 100  TRP A CD1  1 
ATOM   4802 C CD2  . TRP B 1 100 ? 147.095 107.021 114.955 1.00 70.09  ? 100  TRP A CD2  1 
ATOM   4803 N NE1  . TRP B 1 100 ? 146.095 106.776 112.963 1.00 69.63  ? 100  TRP A NE1  1 
ATOM   4804 C CE2  . TRP B 1 100 ? 145.865 106.770 114.312 1.00 67.16  ? 100  TRP A CE2  1 
ATOM   4805 C CE3  . TRP B 1 100 ? 147.128 107.065 116.348 1.00 68.23  ? 100  TRP A CE3  1 
ATOM   4806 C CZ2  . TRP B 1 100 ? 144.684 106.566 115.017 1.00 66.18  ? 100  TRP A CZ2  1 
ATOM   4807 C CZ3  . TRP B 1 100 ? 145.953 106.863 117.045 1.00 65.17  ? 100  TRP A CZ3  1 
ATOM   4808 C CH2  . TRP B 1 100 ? 144.750 106.617 116.381 1.00 66.32  ? 100  TRP A CH2  1 
ATOM   4809 N N    . SER B 1 101 ? 152.351 109.276 113.808 1.00 58.98  ? 101  SER A N    1 
ATOM   4810 C CA   . SER B 1 101 ? 153.771 109.414 114.166 1.00 65.36  ? 101  SER A CA   1 
ATOM   4811 C C    . SER B 1 101 ? 154.005 110.521 115.188 1.00 68.62  ? 101  SER A C    1 
ATOM   4812 O O    . SER B 1 101 ? 154.781 110.351 116.145 1.00 67.14  ? 101  SER A O    1 
ATOM   4813 C CB   . SER B 1 101 ? 154.607 109.694 112.914 1.00 59.46  ? 101  SER A CB   1 
ATOM   4814 O OG   . SER B 1 101 ? 155.959 109.312 113.108 1.00 63.22  ? 101  SER A OG   1 
ATOM   4815 N N    . PHE B 1 102 ? 153.311 111.643 115.023 1.00 50.79  ? 102  PHE A N    1 
ATOM   4816 C CA   . PHE B 1 102 ? 153.407 112.733 115.981 1.00 48.28  ? 102  PHE A CA   1 
ATOM   4817 C C    . PHE B 1 102 ? 152.895 112.259 117.343 1.00 47.68  ? 102  PHE A C    1 
ATOM   4818 O O    . PHE B 1 102 ? 153.520 112.522 118.381 1.00 47.77  ? 102  PHE A O    1 
ATOM   4819 C CB   . PHE B 1 102 ? 152.590 113.906 115.423 1.00 38.85  ? 102  PHE A CB   1 
ATOM   4820 C CG   . PHE B 1 102 ? 152.584 115.148 116.264 1.00 43.34  ? 102  PHE A CG   1 
ATOM   4821 C CD1  . PHE B 1 102 ? 153.659 116.023 116.232 1.00 46.12  ? 102  PHE A CD1  1 
ATOM   4822 C CD2  . PHE B 1 102 ? 151.482 115.478 117.036 1.00 46.14  ? 102  PHE A CD2  1 
ATOM   4823 C CE1  . PHE B 1 102 ? 153.639 117.192 116.979 1.00 53.16  ? 102  PHE A CE1  1 
ATOM   4824 C CE2  . PHE B 1 102 ? 151.466 116.637 117.792 1.00 41.77  ? 102  PHE A CE2  1 
ATOM   4825 C CZ   . PHE B 1 102 ? 152.543 117.493 117.762 1.00 44.46  ? 102  PHE A CZ   1 
ATOM   4826 N N    . LEU B 1 103 ? 151.813 111.470 117.343 1.00 40.85  ? 103  LEU A N    1 
ATOM   4827 C CA   . LEU B 1 103 ? 151.214 110.989 118.586 1.00 41.94  ? 103  LEU A CA   1 
ATOM   4828 C C    . LEU B 1 103 ? 152.174 110.076 119.346 1.00 47.18  ? 103  LEU A C    1 
ATOM   4829 O O    . LEU B 1 103 ? 152.357 110.235 120.563 1.00 58.24  ? 103  LEU A O    1 
ATOM   4830 C CB   . LEU B 1 103 ? 149.902 110.264 118.293 1.00 38.97  ? 103  LEU A CB   1 
ATOM   4831 C CG   . LEU B 1 103 ? 148.912 110.141 119.446 1.00 39.17  ? 103  LEU A CG   1 
ATOM   4832 C CD1  . LEU B 1 103 ? 148.461 111.522 119.861 1.00 39.24  ? 103  LEU A CD1  1 
ATOM   4833 C CD2  . LEU B 1 103 ? 147.720 109.299 119.068 1.00 49.10  ? 103  LEU A CD2  1 
ATOM   4834 N N    . TYR B 1 104 ? 152.830 109.134 118.645 1.00 51.18  ? 104  TYR A N    1 
ATOM   4835 C CA   . TYR B 1 104 ? 153.781 108.272 119.349 1.00 56.68  ? 104  TYR A CA   1 
ATOM   4836 C C    . TYR B 1 104 ? 154.993 109.048 119.841 1.00 57.47  ? 104  TYR A C    1 
ATOM   4837 O O    . TYR B 1 104 ? 155.500 108.774 120.940 1.00 56.88  ? 104  TYR A O    1 
ATOM   4838 C CB   . TYR B 1 104 ? 154.299 107.128 118.457 1.00 57.98  ? 104  TYR A CB   1 
ATOM   4839 C CG   . TYR B 1 104 ? 153.350 106.095 117.879 1.00 58.99  ? 104  TYR A CG   1 
ATOM   4840 C CD1  . TYR B 1 104 ? 152.673 106.322 116.695 1.00 53.08  ? 104  TYR A CD1  1 
ATOM   4841 C CD2  . TYR B 1 104 ? 153.251 104.828 118.475 1.00 64.76  ? 104  TYR A CD2  1 
ATOM   4842 C CE1  . TYR B 1 104 ? 151.841 105.372 116.152 1.00 53.85  ? 104  TYR A CE1  1 
ATOM   4843 C CE2  . TYR B 1 104 ? 152.433 103.840 117.948 1.00 63.20  ? 104  TYR A CE2  1 
ATOM   4844 C CZ   . TYR B 1 104 ? 151.722 104.119 116.782 1.00 58.76  ? 104  TYR A CZ   1 
ATOM   4845 O OH   . TYR B 1 104 ? 150.883 103.179 116.217 1.00 58.41  ? 104  TYR A OH   1 
ATOM   4846 N N    . SER B 1 105 ? 155.454 110.043 119.072 1.00 38.34  ? 105  SER A N    1 
ATOM   4847 C CA   . SER B 1 105 ? 156.616 110.805 119.530 1.00 39.49  ? 105  SER A CA   1 
ATOM   4848 C C    . SER B 1 105 ? 156.337 111.576 120.816 1.00 47.24  ? 105  SER A C    1 
ATOM   4849 O O    . SER B 1 105 ? 157.122 111.505 121.770 1.00 51.40  ? 105  SER A O    1 
ATOM   4850 C CB   . SER B 1 105 ? 157.083 111.744 118.425 1.00 33.68  ? 105  SER A CB   1 
ATOM   4851 O OG   . SER B 1 105 ? 157.509 111.021 117.284 1.00 34.25  ? 105  SER A OG   1 
ATOM   4852 N N    . ILE B 1 106 ? 155.198 112.273 120.890 1.00 30.66  ? 106  ILE A N    1 
ATOM   4853 C CA   . ILE B 1 106 ? 154.893 112.993 122.133 1.00 25.18  ? 106  ILE A CA   1 
ATOM   4854 C C    . ILE B 1 106 ? 154.646 112.042 123.302 1.00 27.13  ? 106  ILE A C    1 
ATOM   4855 O O    . ILE B 1 106 ? 155.128 112.291 124.416 1.00 27.07  ? 106  ILE A O    1 
ATOM   4856 C CB   . ILE B 1 106 ? 153.779 114.049 121.974 1.00 17.19  ? 106  ILE A CB   1 
ATOM   4857 C CG1  . ILE B 1 106 ? 154.249 115.241 121.132 1.00 22.89  ? 106  ILE A CG1  1 
ATOM   4858 C CG2  . ILE B 1 106 ? 153.339 114.576 123.314 1.00 33.94  ? 106  ILE A CG2  1 
ATOM   4859 C CD1  . ILE B 1 106 ? 154.189 115.129 119.704 1.00 29.49  ? 106  ILE A CD1  1 
ATOM   4860 N N    . LEU B 1 107 ? 153.893 110.954 123.093 1.00 32.18  ? 107  LEU A N    1 
ATOM   4861 C CA   . LEU B 1 107 ? 153.644 110.065 124.226 1.00 32.89  ? 107  LEU A CA   1 
ATOM   4862 C C    . LEU B 1 107 ? 154.927 109.420 124.754 1.00 31.32  ? 107  LEU A C    1 
ATOM   4863 O O    . LEU B 1 107 ? 155.127 109.341 125.976 1.00 25.38  ? 107  LEU A O    1 
ATOM   4864 C CB   . LEU B 1 107 ? 152.644 108.986 123.818 1.00 39.71  ? 107  LEU A CB   1 
ATOM   4865 C CG   . LEU B 1 107 ? 151.182 109.397 123.648 1.00 42.73  ? 107  LEU A CG   1 
ATOM   4866 C CD1  . LEU B 1 107 ? 150.374 108.201 123.185 1.00 38.26  ? 107  LEU A CD1  1 
ATOM   4867 C CD2  . LEU B 1 107 ? 150.619 109.966 124.942 1.00 31.27  ? 107  LEU A CD2  1 
ATOM   4868 N N    . ILE B 1 108 ? 155.830 109.000 123.861 1.00 39.53  ? 108  ILE A N    1 
ATOM   4869 C CA   . ILE B 1 108 ? 157.102 108.426 124.302 1.00 41.40  ? 108  ILE A CA   1 
ATOM   4870 C C    . ILE B 1 108 ? 157.952 109.464 125.043 1.00 47.95  ? 108  ILE A C    1 
ATOM   4871 O O    . ILE B 1 108 ? 158.564 109.163 126.080 1.00 48.96  ? 108  ILE A O    1 
ATOM   4872 C CB   . ILE B 1 108 ? 157.844 107.807 123.104 1.00 35.56  ? 108  ILE A CB   1 
ATOM   4873 C CG1  . ILE B 1 108 ? 157.157 106.517 122.673 1.00 44.53  ? 108  ILE A CG1  1 
ATOM   4874 C CG2  . ILE B 1 108 ? 159.229 107.366 123.513 1.00 38.03  ? 108  ILE A CG2  1 
ATOM   4875 C CD1  . ILE B 1 108 ? 157.618 106.013 121.323 1.00 39.45  ? 108  ILE A CD1  1 
ATOM   4876 N N    . ALA B 1 109 ? 157.995 110.704 124.528 1.00 36.79  ? 109  ALA A N    1 
ATOM   4877 C CA   . ALA B 1 109 ? 158.752 111.776 125.179 1.00 30.59  ? 109  ALA A CA   1 
ATOM   4878 C C    . ALA B 1 109 ? 158.233 112.076 126.579 1.00 35.39  ? 109  ALA A C    1 
ATOM   4879 O O    . ALA B 1 109 ? 159.021 112.233 127.527 1.00 29.30  ? 109  ALA A O    1 
ATOM   4880 C CB   . ALA B 1 109 ? 158.710 113.040 124.321 1.00 18.02  ? 109  ALA A CB   1 
ATOM   4881 N N    . LYS B 1 110 ? 156.909 112.149 126.729 1.00 34.47  ? 110  LYS A N    1 
ATOM   4882 C CA   . LYS B 1 110 ? 156.324 112.398 128.041 1.00 18.98  ? 110  LYS A CA   1 
ATOM   4883 C C    . LYS B 1 110 ? 156.628 111.249 128.992 1.00 25.17  ? 110  LYS A C    1 
ATOM   4884 O O    . LYS B 1 110 ? 156.892 111.472 130.182 1.00 16.89  ? 110  LYS A O    1 
ATOM   4885 C CB   . LYS B 1 110 ? 154.819 112.615 127.897 1.00 22.55  ? 110  LYS A CB   1 
ATOM   4886 C CG   . LYS B 1 110 ? 154.454 114.042 127.516 1.00 24.79  ? 110  LYS A CG   1 
ATOM   4887 C CD   . LYS B 1 110 ? 152.982 114.324 127.719 1.00 23.06  ? 110  LYS A CD   1 
ATOM   4888 C CE   . LYS B 1 110 ? 152.668 115.786 127.479 1.00 23.82  ? 110  LYS A CE   1 
ATOM   4889 N NZ   . LYS B 1 110 ? 151.278 115.965 126.990 1.00 24.90  ? 110  LYS A NZ   1 
ATOM   4890 N N    . ALA B 1 111 ? 156.615 110.012 128.480 1.00 42.26  ? 111  ALA A N    1 
ATOM   4891 C CA   . ALA B 1 111 ? 156.934 108.867 129.329 1.00 42.38  ? 111  ALA A CA   1 
ATOM   4892 C C    . ALA B 1 111 ? 158.370 108.956 129.837 1.00 30.71  ? 111  ALA A C    1 
ATOM   4893 O O    . ALA B 1 111 ? 158.635 108.714 131.021 1.00 33.82  ? 111  ALA A O    1 
ATOM   4894 C CB   . ALA B 1 111 ? 156.712 107.564 128.563 1.00 46.81  ? 111  ALA A CB   1 
ATOM   4895 N N    . SER B 1 112 ? 159.308 109.305 128.949 1.00 22.88  ? 112  SER A N    1 
ATOM   4896 C CA   . SER B 1 112 ? 160.715 109.402 129.340 1.00 34.39  ? 112  SER A CA   1 
ATOM   4897 C C    . SER B 1 112 ? 160.925 110.492 130.389 1.00 47.28  ? 112  SER A C    1 
ATOM   4898 O O    . SER B 1 112 ? 161.671 110.301 131.367 1.00 48.65  ? 112  SER A O    1 
ATOM   4899 C CB   . SER B 1 112 ? 161.583 109.662 128.111 1.00 26.28  ? 112  SER A CB   1 
ATOM   4900 O OG   . SER B 1 112 ? 161.444 108.617 127.166 1.00 32.41  ? 112  SER A OG   1 
ATOM   4901 N N    . VAL B 1 113 ? 160.291 111.654 130.182 1.00 45.43  ? 113  VAL A N    1 
ATOM   4902 C CA   . VAL B 1 113 ? 160.406 112.757 131.136 1.00 35.69  ? 113  VAL A CA   1 
ATOM   4903 C C    . VAL B 1 113 ? 159.858 112.337 132.497 1.00 32.01  ? 113  VAL A C    1 
ATOM   4904 O O    . VAL B 1 113 ? 160.453 112.633 133.540 1.00 21.08  ? 113  VAL A O    1 
ATOM   4905 C CB   . VAL B 1 113 ? 159.703 114.014 130.586 1.00 29.28  ? 113  VAL A CB   1 
ATOM   4906 C CG1  . VAL B 1 113 ? 159.338 114.976 131.705 1.00 22.60  ? 113  VAL A CG1  1 
ATOM   4907 C CG2  . VAL B 1 113 ? 160.594 114.705 129.572 1.00 17.77  ? 113  VAL A CG2  1 
ATOM   4908 N N    . PHE B 1 114 ? 158.731 111.617 132.503 1.00 41.17  ? 114  PHE A N    1 
ATOM   4909 C CA   . PHE B 1 114 ? 158.152 111.118 133.750 1.00 37.69  ? 114  PHE A CA   1 
ATOM   4910 C C    . PHE B 1 114 ? 159.116 110.155 134.441 1.00 37.62  ? 114  PHE A C    1 
ATOM   4911 O O    . PHE B 1 114 ? 159.313 110.218 135.667 1.00 38.60  ? 114  PHE A O    1 
ATOM   4912 C CB   . PHE B 1 114 ? 156.824 110.424 133.416 1.00 45.48  ? 114  PHE A CB   1 
ATOM   4913 C CG   . PHE B 1 114 ? 155.998 109.998 134.608 1.00 45.83  ? 114  PHE A CG   1 
ATOM   4914 C CD1  . PHE B 1 114 ? 156.277 108.829 135.300 1.00 41.88  ? 114  PHE A CD1  1 
ATOM   4915 C CD2  . PHE B 1 114 ? 154.869 110.721 134.961 1.00 39.79  ? 114  PHE A CD2  1 
ATOM   4916 C CE1  . PHE B 1 114 ? 155.492 108.433 136.366 1.00 44.29  ? 114  PHE A CE1  1 
ATOM   4917 C CE2  . PHE B 1 114 ? 154.071 110.320 136.017 1.00 37.94  ? 114  PHE A CE2  1 
ATOM   4918 C CZ   . PHE B 1 114 ? 154.389 109.179 136.724 1.00 44.21  ? 114  PHE A CZ   1 
ATOM   4919 N N    . PHE B 1 115 ? 159.778 109.305 133.648 1.00 52.92  ? 115  PHE A N    1 
ATOM   4920 C CA   . PHE B 1 115 ? 160.642 108.257 134.184 1.00 54.90  ? 115  PHE A CA   1 
ATOM   4921 C C    . PHE B 1 115 ? 161.872 108.830 134.875 1.00 50.54  ? 115  PHE A C    1 
ATOM   4922 O O    . PHE B 1 115 ? 162.205 108.416 135.995 1.00 51.74  ? 115  PHE A O    1 
ATOM   4923 C CB   . PHE B 1 115 ? 161.085 107.318 133.058 1.00 48.18  ? 115  PHE A CB   1 
ATOM   4924 C CG   . PHE B 1 115 ? 160.130 106.190 132.774 1.00 47.83  ? 115  PHE A CG   1 
ATOM   4925 C CD1  . PHE B 1 115 ? 160.606 104.975 132.308 1.00 49.87  ? 115  PHE A CD1  1 
ATOM   4926 C CD2  . PHE B 1 115 ? 158.766 106.335 132.972 1.00 51.18  ? 115  PHE A CD2  1 
ATOM   4927 C CE1  . PHE B 1 115 ? 159.742 103.931 132.039 1.00 51.95  ? 115  PHE A CE1  1 
ATOM   4928 C CE2  . PHE B 1 115 ? 157.896 105.295 132.704 1.00 49.42  ? 115  PHE A CE2  1 
ATOM   4929 C CZ   . PHE B 1 115 ? 158.386 104.091 132.239 1.00 48.60  ? 115  PHE A CZ   1 
ATOM   4930 N N    . ILE B 1 116 ? 162.528 109.816 134.256 1.00 38.60  ? 116  ILE A N    1 
ATOM   4931 C CA   . ILE B 1 116 ? 163.773 110.319 134.843 1.00 48.27  ? 116  ILE A CA   1 
ATOM   4932 C C    . ILE B 1 116 ? 163.494 111.079 136.138 1.00 56.09  ? 116  ILE A C    1 
ATOM   4933 O O    . ILE B 1 116 ? 164.216 110.921 137.139 1.00 58.52  ? 116  ILE A O    1 
ATOM   4934 C CB   . ILE B 1 116 ? 164.534 111.192 133.828 1.00 50.95  ? 116  ILE A CB   1 
ATOM   4935 C CG1  . ILE B 1 116 ? 164.705 110.453 132.500 1.00 51.87  ? 116  ILE A CG1  1 
ATOM   4936 C CG2  . ILE B 1 116 ? 165.889 111.595 134.384 1.00 52.22  ? 116  ILE A CG2  1 
ATOM   4937 C CD1  . ILE B 1 116 ? 165.470 109.155 132.616 1.00 51.99  ? 116  ILE A CD1  1 
ATOM   4938 N N    . VAL B 1 117 ? 162.396 111.839 136.171 1.00 57.11  ? 117  VAL A N    1 
ATOM   4939 C CA   . VAL B 1 117 ? 162.068 112.620 137.359 1.00 49.82  ? 117  VAL A CA   1 
ATOM   4940 C C    . VAL B 1 117 ? 161.682 111.692 138.501 1.00 46.66  ? 117  VAL A C    1 
ATOM   4941 O O    . VAL B 1 117 ? 162.121 111.887 139.643 1.00 44.19  ? 117  VAL A O    1 
ATOM   4942 C CB   . VAL B 1 117 ? 160.971 113.656 137.058 1.00 49.02  ? 117  VAL A CB   1 
ATOM   4943 C CG1  . VAL B 1 117 ? 160.704 114.507 138.286 1.00 39.89  ? 117  VAL A CG1  1 
ATOM   4944 C CG2  . VAL B 1 117 ? 161.407 114.552 135.914 1.00 49.70  ? 117  VAL A CG2  1 
ATOM   4945 N N    . CYS B 1 118 ? 160.896 110.645 138.212 1.00 61.26  ? 118  CYS A N    1 
ATOM   4946 C CA   . CYS B 1 118 ? 160.509 109.730 139.282 1.00 61.21  ? 118  CYS A CA   1 
ATOM   4947 C C    . CYS B 1 118 ? 161.726 108.988 139.821 1.00 60.00  ? 118  CYS A C    1 
ATOM   4948 O O    . CYS B 1 118 ? 161.846 108.787 141.039 1.00 52.22  ? 118  CYS A O    1 
ATOM   4949 C CB   . CYS B 1 118 ? 159.455 108.741 138.786 1.00 60.49  ? 118  CYS A CB   1 
ATOM   4950 S SG   . CYS B 1 118 ? 158.361 108.110 140.081 1.00 55.76  ? 118  CYS A SG   1 
ATOM   4951 N N    . VAL B 1 119 ? 162.639 108.575 138.932 1.00 65.99  ? 119  VAL A N    1 
ATOM   4952 C CA   . VAL B 1 119 ? 163.793 107.789 139.364 1.00 65.80  ? 119  VAL A CA   1 
ATOM   4953 C C    . VAL B 1 119 ? 164.663 108.615 140.307 1.00 62.61  ? 119  VAL A C    1 
ATOM   4954 O O    . VAL B 1 119 ? 165.004 108.174 141.417 1.00 63.22  ? 119  VAL A O    1 
ATOM   4955 C CB   . VAL B 1 119 ? 164.589 107.280 138.149 1.00 62.40  ? 119  VAL A CB   1 
ATOM   4956 C CG1  . VAL B 1 119 ? 165.994 106.877 138.561 1.00 64.44  ? 119  VAL A CG1  1 
ATOM   4957 C CG2  . VAL B 1 119 ? 163.877 106.097 137.514 1.00 59.59  ? 119  VAL A CG2  1 
ATOM   4958 N N    . LEU B 1 120 ? 165.009 109.845 139.900 1.00 66.23  ? 120  LEU A N    1 
ATOM   4959 C CA   . LEU B 1 120 ? 165.875 110.624 140.783 1.00 68.26  ? 120  LEU A CA   1 
ATOM   4960 C C    . LEU B 1 120 ? 165.136 111.082 142.035 1.00 73.32  ? 120  LEU A C    1 
ATOM   4961 O O    . LEU B 1 120 ? 165.766 111.244 143.091 1.00 79.51  ? 120  LEU A O    1 
ATOM   4962 C CB   . LEU B 1 120 ? 166.491 111.819 140.053 1.00 70.84  ? 120  LEU A CB   1 
ATOM   4963 C CG   . LEU B 1 120 ? 166.950 111.621 138.610 1.00 75.80  ? 120  LEU A CG   1 
ATOM   4964 C CD1  . LEU B 1 120 ? 166.915 112.931 137.852 1.00 74.22  ? 120  LEU A CD1  1 
ATOM   4965 C CD2  . LEU B 1 120 ? 168.344 111.019 138.578 1.00 75.63  ? 120  LEU A CD2  1 
ATOM   4966 N N    . THR B 1 121 ? 163.810 111.272 141.958 1.00 67.40  ? 121  THR A N    1 
ATOM   4967 C CA   . THR B 1 121 ? 163.065 111.628 143.161 1.00 65.11  ? 121  THR A CA   1 
ATOM   4968 C C    . THR B 1 121 ? 163.147 110.502 144.180 1.00 65.38  ? 121  THR A C    1 
ATOM   4969 O O    . THR B 1 121 ? 163.312 110.749 145.381 1.00 61.67  ? 121  THR A O    1 
ATOM   4970 C CB   . THR B 1 121 ? 161.614 111.952 142.819 1.00 65.08  ? 121  THR A CB   1 
ATOM   4971 O OG1  . THR B 1 121 ? 161.582 112.970 141.812 1.00 69.23  ? 121  THR A OG1  1 
ATOM   4972 C CG2  . THR B 1 121 ? 160.908 112.481 144.051 1.00 60.34  ? 121  THR A CG2  1 
ATOM   4973 N N    . LEU B 1 122 ? 163.024 109.251 143.717 1.00 73.70  ? 122  LEU A N    1 
ATOM   4974 C CA   . LEU B 1 122 ? 163.128 108.128 144.642 1.00 75.50  ? 122  LEU A CA   1 
ATOM   4975 C C    . LEU B 1 122 ? 164.542 108.025 145.191 1.00 74.06  ? 122  LEU A C    1 
ATOM   4976 O O    . LEU B 1 122 ? 164.736 107.628 146.346 1.00 72.73  ? 122  LEU A O    1 
ATOM   4977 C CB   . LEU B 1 122 ? 162.736 106.817 143.958 1.00 72.67  ? 122  LEU A CB   1 
ATOM   4978 C CG   . LEU B 1 122 ? 161.297 106.610 143.493 1.00 70.73  ? 122  LEU A CG   1 
ATOM   4979 C CD1  . LEU B 1 122 ? 161.256 105.663 142.309 1.00 69.64  ? 122  LEU A CD1  1 
ATOM   4980 C CD2  . LEU B 1 122 ? 160.477 106.050 144.642 1.00 69.61  ? 122  LEU A CD2  1 
ATOM   4981 N N    . LEU B 1 123 ? 165.536 108.380 144.373 1.00 74.49  ? 123  LEU A N    1 
ATOM   4982 C CA   . LEU B 1 123 ? 166.929 108.208 144.768 1.00 72.28  ? 123  LEU A CA   1 
ATOM   4983 C C    . LEU B 1 123 ? 167.405 109.258 145.770 1.00 72.85  ? 123  LEU A C    1 
ATOM   4984 O O    . LEU B 1 123 ? 168.308 108.974 146.564 1.00 78.21  ? 123  LEU A O    1 
ATOM   4985 C CB   . LEU B 1 123 ? 167.834 108.222 143.535 1.00 75.63  ? 123  LEU A CB   1 
ATOM   4986 C CG   . LEU B 1 123 ? 168.370 106.858 143.088 1.00 78.09  ? 123  LEU A CG   1 
ATOM   4987 C CD1  . LEU B 1 123 ? 167.238 105.861 142.877 1.00 74.70  ? 123  LEU A CD1  1 
ATOM   4988 C CD2  . LEU B 1 123 ? 169.215 106.993 141.831 1.00 77.39  ? 123  LEU A CD2  1 
ATOM   4989 N N    . VAL B 1 124 ? 166.827 110.461 145.763 1.00 76.09  ? 124  VAL A N    1 
ATOM   4990 C CA   . VAL B 1 124 ? 167.381 111.571 146.529 1.00 79.85  ? 124  VAL A CA   1 
ATOM   4991 C C    . VAL B 1 124 ? 166.530 111.985 147.735 1.00 81.04  ? 124  VAL A C    1 
ATOM   4992 O O    . VAL B 1 124 ? 167.098 112.348 148.773 1.00 78.70  ? 124  VAL A O    1 
ATOM   4993 C CB   . VAL B 1 124 ? 167.640 112.778 145.600 1.00 77.27  ? 124  VAL A CB   1 
ATOM   4994 C CG1  . VAL B 1 124 ? 168.332 113.910 146.345 1.00 78.24  ? 124  VAL A CG1  1 
ATOM   4995 C CG2  . VAL B 1 124 ? 168.488 112.355 144.413 1.00 76.70  ? 124  VAL A CG2  1 
ATOM   4996 N N    . ALA B 1 125 ? 165.200 111.921 147.645 1.00 89.64  ? 125  ALA A N    1 
ATOM   4997 C CA   . ALA B 1 125 ? 164.321 112.423 148.702 1.00 89.54  ? 125  ALA A CA   1 
ATOM   4998 C C    . ALA B 1 125 ? 164.559 111.748 150.054 1.00 89.47  ? 125  ALA A C    1 
ATOM   4999 O O    . ALA B 1 125 ? 165.010 110.603 150.138 1.00 86.63  ? 125  ALA A O    1 
ATOM   5000 C CB   . ALA B 1 125 ? 162.858 112.244 148.297 1.00 88.41  ? 125  ALA A CB   1 
ATOM   5001 N N    . SER B 1 126 ? 164.260 112.499 151.120 1.00 102.08 ? 126  SER A N    1 
ATOM   5002 C CA   . SER B 1 126 ? 164.458 112.039 152.489 1.00 104.77 ? 126  SER A CA   1 
ATOM   5003 C C    . SER B 1 126 ? 163.546 110.848 152.787 1.00 102.41 ? 126  SER A C    1 
ATOM   5004 O O    . SER B 1 126 ? 162.442 110.757 152.244 1.00 99.88  ? 126  SER A O    1 
ATOM   5005 C CB   . SER B 1 126 ? 164.171 113.183 153.464 1.00 102.09 ? 126  SER A CB   1 
ATOM   5006 O OG   . SER B 1 126 ? 164.276 112.777 154.817 1.00 102.40 ? 126  SER A OG   1 
ATOM   5007 N N    . PRO B 1 127 ? 163.993 109.910 153.636 1.00 98.02  ? 127  PRO A N    1 
ATOM   5008 C CA   . PRO B 1 127 ? 163.165 108.717 153.899 1.00 98.04  ? 127  PRO A CA   1 
ATOM   5009 C C    . PRO B 1 127 ? 161.779 108.974 154.475 1.00 100.70 ? 127  PRO A C    1 
ATOM   5010 O O    . PRO B 1 127 ? 160.848 108.244 154.114 1.00 99.59  ? 127  PRO A O    1 
ATOM   5011 C CB   . PRO B 1 127 ? 164.032 107.908 154.877 1.00 99.14  ? 127  PRO A CB   1 
ATOM   5012 C CG   . PRO B 1 127 ? 165.422 108.381 154.639 1.00 98.30  ? 127  PRO A CG   1 
ATOM   5013 C CD   . PRO B 1 127 ? 165.305 109.829 154.301 1.00 96.50  ? 127  PRO A CD   1 
ATOM   5014 N N    . ASP B 1 128 ? 161.598 109.954 155.368 1.00 107.36 ? 128  ASP A N    1 
ATOM   5015 C CA   . ASP B 1 128 ? 160.255 110.135 155.915 1.00 106.68 ? 128  ASP A CA   1 
ATOM   5016 C C    . ASP B 1 128 ? 159.287 110.694 154.878 1.00 106.84 ? 128  ASP A C    1 
ATOM   5017 O O    . ASP B 1 128 ? 158.082 110.427 154.949 1.00 105.70 ? 128  ASP A O    1 
ATOM   5018 C CB   . ASP B 1 128 ? 160.301 111.045 157.143 1.00 106.83 ? 128  ASP A CB   1 
ATOM   5019 C CG   . ASP B 1 128 ? 159.235 110.695 158.165 1.00 107.37 ? 128  ASP A CG   1 
ATOM   5020 O OD1  . ASP B 1 128 ? 158.573 109.649 157.998 1.00 103.75 ? 128  ASP A OD1  1 
ATOM   5021 O OD2  . ASP B 1 128 ? 159.058 111.465 159.132 1.00 109.96 ? 128  ASP A OD2  1 
ATOM   5022 N N    . SER B 1 129 ? 159.793 111.469 153.920 1.00 105.55 ? 129  SER A N    1 
ATOM   5023 C CA   . SER B 1 129 ? 158.960 112.082 152.887 1.00 104.76 ? 129  SER A CA   1 
ATOM   5024 C C    . SER B 1 129 ? 159.575 111.761 151.531 1.00 102.75 ? 129  SER A C    1 
ATOM   5025 O O    . SER B 1 129 ? 160.299 112.595 150.979 1.00 102.36 ? 129  SER A O    1 
ATOM   5026 C CB   . SER B 1 129 ? 158.834 113.585 153.111 1.00 104.18 ? 129  SER A CB   1 
ATOM   5027 O OG   . SER B 1 129 ? 160.092 114.229 153.000 1.00 104.60 ? 129  SER A OG   1 
ATOM   5028 N N    . ARG B 1 130 ? 159.291 110.580 150.986 1.00 88.01  ? 130  ARG A N    1 
ATOM   5029 C CA   . ARG B 1 130 ? 159.866 110.196 149.698 1.00 89.25  ? 130  ARG A CA   1 
ATOM   5030 C C    . ARG B 1 130 ? 158.816 109.705 148.708 1.00 86.90  ? 130  ARG A C    1 
ATOM   5031 O O    . ARG B 1 130 ? 158.892 110.007 147.511 1.00 85.74  ? 130  ARG A O    1 
ATOM   5032 C CB   . ARG B 1 130 ? 160.976 109.157 149.868 1.00 89.81  ? 130  ARG A CB   1 
ATOM   5033 C CG   . ARG B 1 130 ? 160.733 108.034 150.855 1.00 87.63  ? 130  ARG A CG   1 
ATOM   5034 C CD   . ARG B 1 130 ? 161.958 107.122 150.860 1.00 87.88  ? 130  ARG A CD   1 
ATOM   5035 N NE   . ARG B 1 130 ? 161.973 106.182 151.974 1.00 89.34  ? 130  ARG A NE   1 
ATOM   5036 C CZ   . ARG B 1 130 ? 161.709 104.887 151.866 1.00 89.43  ? 130  ARG A CZ   1 
ATOM   5037 N NH1  . ARG B 1 130 ? 161.409 104.338 150.701 1.00 89.11  ? 130  ARG A NH1  1 
ATOM   5038 N NH2  . ARG B 1 130 ? 161.748 104.125 152.955 1.00 89.21  ? 130  ARG A NH2  1 
ATOM   5039 N N    . PHE B 1 131 ? 157.811 108.979 149.199 1.00 84.92  ? 131  PHE A N    1 
ATOM   5040 C CA   . PHE B 1 131 ? 156.814 108.418 148.295 1.00 86.96  ? 131  PHE A CA   1 
ATOM   5041 C C    . PHE B 1 131 ? 155.862 109.500 147.795 1.00 87.83  ? 131  PHE A C    1 
ATOM   5042 O O    . PHE B 1 131 ? 155.442 109.466 146.632 1.00 85.85  ? 131  PHE A O    1 
ATOM   5043 C CB   . PHE B 1 131 ? 156.005 107.317 148.986 1.00 84.67  ? 131  PHE A CB   1 
ATOM   5044 C CG   . PHE B 1 131 ? 156.805 106.125 149.455 1.00 84.45  ? 131  PHE A CG   1 
ATOM   5045 C CD1  . PHE B 1 131 ? 156.675 104.905 148.812 1.00 82.65  ? 131  PHE A CD1  1 
ATOM   5046 C CD2  . PHE B 1 131 ? 157.594 106.190 150.594 1.00 84.67  ? 131  PHE A CD2  1 
ATOM   5047 C CE1  . PHE B 1 131 ? 157.375 103.793 149.247 1.00 85.75  ? 131  PHE A CE1  1 
ATOM   5048 C CE2  . PHE B 1 131 ? 158.295 105.079 151.037 1.00 83.69  ? 131  PHE A CE2  1 
ATOM   5049 C CZ   . PHE B 1 131 ? 158.184 103.880 150.363 1.00 84.78  ? 131  PHE A CZ   1 
ATOM   5050 N N    . SER B 1 132 ? 155.511 110.465 148.651 1.00 84.40  ? 132  SER A N    1 
ATOM   5051 C CA   . SER B 1 132 ? 154.656 111.571 148.218 1.00 80.35  ? 132  SER A CA   1 
ATOM   5052 C C    . SER B 1 132 ? 155.326 112.372 147.107 1.00 77.08  ? 132  SER A C    1 
ATOM   5053 O O    . SER B 1 132 ? 154.690 112.714 146.097 1.00 71.39  ? 132  SER A O    1 
ATOM   5054 C CB   . SER B 1 132 ? 154.324 112.472 149.404 1.00 80.98  ? 132  SER A CB   1 
ATOM   5055 O OG   . SER B 1 132 ? 154.145 111.703 150.579 1.00 83.81  ? 132  SER A OG   1 
ATOM   5056 N N    . LYS B 1 133 ? 156.634 112.617 147.240 1.00 67.77  ? 133  LYS A N    1 
ATOM   5057 C CA   . LYS B 1 133 ? 157.332 113.375 146.210 1.00 68.21  ? 133  LYS A CA   1 
ATOM   5058 C C    . LYS B 1 133 ? 157.461 112.553 144.941 1.00 63.77  ? 133  LYS A C    1 
ATOM   5059 O O    . LYS B 1 133 ? 157.268 113.082 143.839 1.00 67.21  ? 133  LYS A O    1 
ATOM   5060 C CB   . LYS B 1 133 ? 158.708 113.843 146.686 1.00 70.65  ? 133  LYS A CB   1 
ATOM   5061 C CG   . LYS B 1 133 ? 158.705 114.862 147.814 1.00 66.19  ? 133  LYS A CG   1 
ATOM   5062 C CD   . LYS B 1 133 ? 160.110 115.052 148.364 1.00 68.00  ? 133  LYS A CD   1 
ATOM   5063 C CE   . LYS B 1 133 ? 160.146 116.107 149.454 1.00 66.78  ? 133  LYS A CE   1 
ATOM   5064 N NZ   . LYS B 1 133 ? 159.618 115.619 150.745 1.00 68.63  ? 133  LYS A NZ   1 
ATOM   5065 N N    . ALA B 1 134 ? 157.802 111.267 145.063 1.00 55.87  ? 134  ALA A N    1 
ATOM   5066 C CA   . ALA B 1 134 ? 157.917 110.459 143.858 1.00 60.59  ? 134  ALA A CA   1 
ATOM   5067 C C    . ALA B 1 134 ? 156.572 110.299 143.161 1.00 55.26  ? 134  ALA A C    1 
ATOM   5068 O O    . ALA B 1 134 ? 156.538 110.064 141.950 1.00 45.45  ? 134  ALA A O    1 
ATOM   5069 C CB   . ALA B 1 134 ? 158.489 109.089 144.201 1.00 67.55  ? 134  ALA A CB   1 
ATOM   5070 N N    . GLY B 1 135 ? 155.473 110.422 143.901 1.00 60.99  ? 135  GLY A N    1 
ATOM   5071 C CA   . GLY B 1 135 ? 154.147 110.302 143.339 1.00 65.87  ? 135  GLY A CA   1 
ATOM   5072 C C    . GLY B 1 135 ? 153.600 111.593 142.757 1.00 66.68  ? 135  GLY A C    1 
ATOM   5073 O O    . GLY B 1 135 ? 152.675 111.555 141.942 1.00 60.70  ? 135  GLY A O    1 
ATOM   5074 N N    . LEU B 1 136 ? 154.179 112.738 143.128 1.00 63.66  ? 136  LEU A N    1 
ATOM   5075 C CA   . LEU B 1 136 ? 153.650 114.030 142.682 1.00 56.54  ? 136  LEU A CA   1 
ATOM   5076 C C    . LEU B 1 136 ? 154.557 114.825 141.752 1.00 58.54  ? 136  LEU A C    1 
ATOM   5077 O O    . LEU B 1 136 ? 154.048 115.553 140.898 1.00 61.26  ? 136  LEU A O    1 
ATOM   5078 C CB   . LEU B 1 136 ? 153.290 114.896 143.895 1.00 54.54  ? 136  LEU A CB   1 
ATOM   5079 C CG   . LEU B 1 136 ? 152.126 114.314 144.698 1.00 57.59  ? 136  LEU A CG   1 
ATOM   5080 C CD1  . LEU B 1 136 ? 151.878 115.091 145.969 1.00 53.63  ? 136  LEU A CD1  1 
ATOM   5081 C CD2  . LEU B 1 136 ? 150.874 114.291 143.843 1.00 58.83  ? 136  LEU A CD2  1 
ATOM   5082 N N    . PHE B 1 137 ? 155.879 114.762 141.916 1.00 50.36  ? 137  PHE A N    1 
ATOM   5083 C CA   . PHE B 1 137 ? 156.785 115.521 141.052 1.00 41.27  ? 137  PHE A CA   1 
ATOM   5084 C C    . PHE B 1 137 ? 156.665 115.120 139.575 1.00 41.88  ? 137  PHE A C    1 
ATOM   5085 O O    . PHE B 1 137 ? 156.594 116.027 138.723 1.00 44.76  ? 137  PHE A O    1 
ATOM   5086 C CB   . PHE B 1 137 ? 158.222 115.464 141.598 1.00 41.93  ? 137  PHE A CB   1 
ATOM   5087 C CG   . PHE B 1 137 ? 158.472 116.354 142.781 1.00 46.06  ? 137  PHE A CG   1 
ATOM   5088 C CD1  . PHE B 1 137 ? 157.461 117.132 143.314 1.00 44.19  ? 137  PHE A CD1  1 
ATOM   5089 C CD2  . PHE B 1 137 ? 159.728 116.401 143.366 1.00 47.26  ? 137  PHE A CD2  1 
ATOM   5090 C CE1  . PHE B 1 137 ? 157.702 117.948 144.400 1.00 47.26  ? 137  PHE A CE1  1 
ATOM   5091 C CE2  . PHE B 1 137 ? 159.968 117.212 144.456 1.00 44.42  ? 137  PHE A CE2  1 
ATOM   5092 C CZ   . PHE B 1 137 ? 158.954 117.983 144.973 1.00 46.53  ? 137  PHE A CZ   1 
ATOM   5093 N N    . PRO B 1 138 ? 156.695 113.830 139.187 1.00 31.16  ? 138  PRO A N    1 
ATOM   5094 C CA   . PRO B 1 138 ? 156.511 113.510 137.768 1.00 29.81  ? 138  PRO A CA   1 
ATOM   5095 C C    . PRO B 1 138 ? 155.214 114.005 137.140 1.00 38.41  ? 138  PRO A C    1 
ATOM   5096 O O    . PRO B 1 138 ? 155.218 114.299 135.938 1.00 39.12  ? 138  PRO A O    1 
ATOM   5097 C CB   . PRO B 1 138 ? 156.492 111.975 137.795 1.00 41.26  ? 138  PRO A CB   1 
ATOM   5098 C CG   . PRO B 1 138 ? 157.088 111.599 139.145 1.00 47.85  ? 138  PRO A CG   1 
ATOM   5099 C CD   . PRO B 1 138 ? 157.670 112.829 139.669 1.00 40.71  ? 138  PRO A CD   1 
ATOM   5100 N N    . ILE B 1 139 ? 154.098 114.073 137.875 1.00 44.44  ? 139  ILE A N    1 
ATOM   5101 C CA   . ILE B 1 139 ? 152.905 114.715 137.317 1.00 40.87  ? 139  ILE A CA   1 
ATOM   5102 C C    . ILE B 1 139 ? 153.135 116.208 137.122 1.00 36.87  ? 139  ILE A C    1 
ATOM   5103 O O    . ILE B 1 139 ? 152.612 116.807 136.176 1.00 33.54  ? 139  ILE A O    1 
ATOM   5104 C CB   . ILE B 1 139 ? 151.653 114.443 138.171 1.00 39.07  ? 139  ILE A CB   1 
ATOM   5105 C CG1  . ILE B 1 139 ? 151.690 113.052 138.804 1.00 43.63  ? 139  ILE A CG1  1 
ATOM   5106 C CG2  . ILE B 1 139 ? 150.396 114.642 137.342 1.00 31.39  ? 139  ILE A CG2  1 
ATOM   5107 C CD1  . ILE B 1 139 ? 150.605 112.842 139.841 1.00 39.06  ? 139  ILE A CD1  1 
ATOM   5108 N N    . PHE B 1 140 ? 153.889 116.838 138.028 1.00 31.54  ? 140  PHE A N    1 
ATOM   5109 C CA   . PHE B 1 140 ? 154.175 118.263 137.888 1.00 23.66  ? 140  PHE A CA   1 
ATOM   5110 C C    . PHE B 1 140 ? 154.990 118.546 136.636 1.00 25.08  ? 140  PHE A C    1 
ATOM   5111 O O    . PHE B 1 140 ? 154.771 119.557 135.959 1.00 42.37  ? 140  PHE A O    1 
ATOM   5112 C CB   . PHE B 1 140 ? 154.911 118.792 139.116 1.00 28.84  ? 140  PHE A CB   1 
ATOM   5113 C CG   . PHE B 1 140 ? 155.204 120.262 139.045 1.00 27.97  ? 140  PHE A CG   1 
ATOM   5114 C CD1  . PHE B 1 140 ? 154.182 121.191 139.025 1.00 32.33  ? 140  PHE A CD1  1 
ATOM   5115 C CD2  . PHE B 1 140 ? 156.511 120.711 138.966 1.00 24.37  ? 140  PHE A CD2  1 
ATOM   5116 C CE1  . PHE B 1 140 ? 154.459 122.537 138.942 1.00 38.12  ? 140  PHE A CE1  1 
ATOM   5117 C CE2  . PHE B 1 140 ? 156.792 122.056 138.884 1.00 20.62  ? 140  PHE A CE2  1 
ATOM   5118 C CZ   . PHE B 1 140 ? 155.766 122.968 138.869 1.00 24.68  ? 140  PHE A CZ   1 
ATOM   5119 N N    . ALA B 1 141 ? 155.939 117.678 136.315 1.00 14.67  ? 141  ALA A N    1 
ATOM   5120 C CA   . ALA B 1 141 ? 156.868 117.970 135.234 1.00 12.56  ? 141  ALA A CA   1 
ATOM   5121 C C    . ALA B 1 141 ? 156.365 117.507 133.871 1.00 12.64  ? 141  ALA A C    1 
ATOM   5122 O O    . ALA B 1 141 ? 157.124 117.561 132.901 1.00 24.59  ? 141  ALA A O    1 
ATOM   5123 C CB   . ALA B 1 141 ? 158.231 117.336 135.521 1.00 20.54  ? 141  ALA A CB   1 
ATOM   5124 N N    . THR B 1 142 ? 155.115 117.039 133.769 1.00 21.13  ? 142  THR A N    1 
ATOM   5125 C CA   . THR B 1 142 ? 154.619 116.563 132.480 1.00 19.76  ? 142  THR A CA   1 
ATOM   5126 C C    . THR B 1 142 ? 153.209 117.018 132.085 1.00 30.27  ? 142  THR A C    1 
ATOM   5127 O O    . THR B 1 142 ? 152.824 116.786 130.935 1.00 29.37  ? 142  THR A O    1 
ATOM   5128 C CB   . THR B 1 142 ? 154.668 115.022 132.479 1.00 25.53  ? 142  THR A CB   1 
ATOM   5129 O OG1  . THR B 1 142 ? 155.813 114.590 133.221 1.00 35.88  ? 142  THR A OG1  1 
ATOM   5130 C CG2  . THR B 1 142 ? 154.832 114.473 131.077 1.00 23.09  ? 142  THR A CG2  1 
ATOM   5131 N N    . GLN B 1 143 ? 152.441 117.694 132.943 1.00 16.10  ? 143  GLN A N    1 
ATOM   5132 C CA   . GLN B 1 143 ? 151.046 118.018 132.623 1.00 3.21   ? 143  GLN A CA   1 
ATOM   5133 C C    . GLN B 1 143 ? 150.894 119.463 132.152 1.00 8.10   ? 143  GLN A C    1 
ATOM   5134 O O    . GLN B 1 143 ? 150.755 120.383 132.960 1.00 17.17  ? 143  GLN A O    1 
ATOM   5135 C CB   . GLN B 1 143 ? 150.140 117.745 133.819 1.00 17.63  ? 143  GLN A CB   1 
ATOM   5136 C CG   . GLN B 1 143 ? 148.684 117.503 133.431 1.00 20.85  ? 143  GLN A CG   1 
ATOM   5137 C CD   . GLN B 1 143 ? 147.864 116.881 134.545 1.00 26.87  ? 143  GLN A CD   1 
ATOM   5138 O OE1  . GLN B 1 143 ? 148.252 115.870 135.127 1.00 31.98  ? 143  GLN A OE1  1 
ATOM   5139 N NE2  . GLN B 1 143 ? 146.718 117.482 134.843 1.00 25.17  ? 143  GLN A NE2  1 
ATOM   5140 N N    . SER B 1 144 ? 150.911 119.649 130.835 1.00 20.28  ? 144  SER A N    1 
ATOM   5141 C CA   . SER B 1 144 ? 150.859 120.964 130.212 1.00 13.58  ? 144  SER A CA   1 
ATOM   5142 C C    . SER B 1 144 ? 149.458 121.571 130.335 1.00 14.02  ? 144  SER A C    1 
ATOM   5143 O O    . SER B 1 144 ? 148.461 120.878 130.552 1.00 31.81  ? 144  SER A O    1 
ATOM   5144 C CB   . SER B 1 144 ? 151.277 120.873 128.746 1.00 14.93  ? 144  SER A CB   1 
ATOM   5145 O OG   . SER B 1 144 ? 152.633 120.486 128.624 1.00 23.71  ? 144  SER A OG   1 
ATOM   5146 N N    . ASN B 1 145 ? 149.393 122.897 130.204 1.00 15.76  ? 145  ASN A N    1 
ATOM   5147 C CA   . ASN B 1 145 ? 148.144 123.651 130.138 1.00 21.69  ? 145  ASN A CA   1 
ATOM   5148 C C    . ASN B 1 145 ? 147.667 123.785 128.693 1.00 15.59  ? 145  ASN A C    1 
ATOM   5149 O O    . ASN B 1 145 ? 147.660 124.884 128.135 1.00 2.51   ? 145  ASN A O    1 
ATOM   5150 C CB   . ASN B 1 145 ? 148.321 125.028 130.773 1.00 10.59  ? 145  ASN A CB   1 
ATOM   5151 C CG   . ASN B 1 145 ? 147.005 125.692 131.111 1.00 12.65  ? 145  ASN A CG   1 
ATOM   5152 O OD1  . ASN B 1 145 ? 146.972 126.800 131.641 1.00 35.46  ? 145  ASN A OD1  1 
ATOM   5153 N ND2  . ASN B 1 145 ? 145.908 125.014 130.801 1.00 2.35   ? 145  ASN A ND2  1 
ATOM   5154 N N    . ASP B 1 146 ? 147.267 122.671 128.078 1.00 15.67  ? 146  ASP A N    1 
ATOM   5155 C CA   . ASP B 1 146 ? 146.981 122.637 126.648 1.00 12.41  ? 146  ASP A CA   1 
ATOM   5156 C C    . ASP B 1 146 ? 145.664 123.236 126.167 1.00 22.90  ? 146  ASP A C    1 
ATOM   5157 O O    . ASP B 1 146 ? 145.657 123.917 125.140 1.00 24.02  ? 146  ASP A O    1 
ATOM   5158 C CB   . ASP B 1 146 ? 147.025 121.187 126.157 1.00 14.82  ? 146  ASP A CB   1 
ATOM   5159 C CG   . ASP B 1 146 ? 148.181 120.409 126.736 1.00 28.19  ? 146  ASP A CG   1 
ATOM   5160 O OD1  . ASP B 1 146 ? 148.064 119.945 127.888 1.00 19.79  ? 146  ASP A OD1  1 
ATOM   5161 O OD2  . ASP B 1 146 ? 149.208 120.261 126.045 1.00 33.83  ? 146  ASP A OD2  1 
ATOM   5162 N N    . PHE B 1 147 ? 144.564 123.076 126.901 1.00 22.12  ? 147  PHE A N    1 
ATOM   5163 C CA   . PHE B 1 147 ? 143.315 123.572 126.331 1.00 11.00  ? 147  PHE A CA   1 
ATOM   5164 C C    . PHE B 1 147 ? 143.136 125.081 126.410 1.00 19.88  ? 147  PHE A C    1 
ATOM   5165 O O    . PHE B 1 147 ? 143.141 125.727 125.354 1.00 31.34  ? 147  PHE A O    1 
ATOM   5166 C CB   . PHE B 1 147 ? 142.126 122.908 127.031 1.00 9.96   ? 147  PHE A CB   1 
ATOM   5167 C CG   . PHE B 1 147 ? 142.178 121.410 127.029 1.00 12.42  ? 147  PHE A CG   1 
ATOM   5168 C CD1  . PHE B 1 147 ? 142.152 120.701 125.841 1.00 19.74  ? 147  PHE A CD1  1 
ATOM   5169 C CD2  . PHE B 1 147 ? 142.244 120.709 128.221 1.00 17.88  ? 147  PHE A CD2  1 
ATOM   5170 C CE1  . PHE B 1 147 ? 142.201 119.321 125.843 1.00 25.42  ? 147  PHE A CE1  1 
ATOM   5171 C CE2  . PHE B 1 147 ? 142.292 119.330 128.228 1.00 18.00  ? 147  PHE A CE2  1 
ATOM   5172 C CZ   . PHE B 1 147 ? 142.270 118.636 127.037 1.00 20.31  ? 147  PHE A CZ   1 
ATOM   5173 N N    . ALA B 1 148 ? 143.392 125.639 127.593 1.00 16.37  ? 148  ALA A N    1 
ATOM   5174 C CA   . ALA B 1 148 ? 143.179 127.044 127.932 1.00 9.60   ? 148  ALA A CA   1 
ATOM   5175 C C    . ALA B 1 148 ? 144.148 127.941 127.189 1.00 13.47  ? 148  ALA A C    1 
ATOM   5176 O O    . ALA B 1 148 ? 143.748 128.964 126.626 1.00 15.18  ? 148  ALA A O    1 
ATOM   5177 C CB   . ALA B 1 148 ? 143.310 127.257 129.440 1.00 14.76  ? 148  ALA A CB   1 
ATOM   5178 N N    . LEU B 1 149 ? 145.420 127.572 127.180 1.00 12.86  ? 149  LEU A N    1 
ATOM   5179 C CA   . LEU B 1 149 ? 146.414 128.428 126.562 1.00 15.24  ? 149  LEU A CA   1 
ATOM   5180 C C    . LEU B 1 149 ? 146.828 127.840 125.226 1.00 20.51  ? 149  LEU A C    1 
ATOM   5181 O O    . LEU B 1 149 ? 147.086 128.585 124.275 1.00 30.18  ? 149  LEU A O    1 
ATOM   5182 C CB   . LEU B 1 149 ? 147.618 128.582 127.490 1.00 11.31  ? 149  LEU A CB   1 
ATOM   5183 C CG   . LEU B 1 149 ? 147.590 129.743 128.481 1.00 14.28  ? 149  LEU A CG   1 
ATOM   5184 C CD1  . LEU B 1 149 ? 148.514 129.475 129.644 1.00 19.33  ? 149  LEU A CD1  1 
ATOM   5185 C CD2  . LEU B 1 149 ? 148.018 131.000 127.779 1.00 19.61  ? 149  LEU A CD2  1 
ATOM   5186 N N    . GLY B 1 150 ? 146.930 126.513 125.147 1.00 12.17  ? 150  GLY A N    1 
ATOM   5187 C CA   . GLY B 1 150 ? 147.382 125.892 123.921 1.00 4.90   ? 150  GLY A CA   1 
ATOM   5188 C C    . GLY B 1 150 ? 146.434 126.085 122.749 1.00 9.45   ? 150  GLY A C    1 
ATOM   5189 O O    . GLY B 1 150 ? 146.881 126.409 121.646 1.00 25.58  ? 150  GLY A O    1 
ATOM   5190 N N    . TYR B 1 151 ? 145.101 125.873 122.952 1.00 11.07  ? 151  TYR A N    1 
ATOM   5191 C CA   . TYR B 1 151 ? 144.215 125.970 121.788 1.00 19.64  ? 151  TYR A CA   1 
ATOM   5192 C C    . TYR B 1 151 ? 144.147 127.362 121.141 1.00 21.93  ? 151  TYR A C    1 
ATOM   5193 O O    . TYR B 1 151 ? 144.261 127.449 119.907 1.00 25.33  ? 151  TYR A O    1 
ATOM   5194 C CB   . TYR B 1 151 ? 142.811 125.459 122.135 1.00 20.57  ? 151  TYR A CB   1 
ATOM   5195 C CG   . TYR B 1 151 ? 141.873 125.430 120.947 1.00 18.39  ? 151  TYR A CG   1 
ATOM   5196 C CD1  . TYR B 1 151 ? 141.887 124.356 120.066 1.00 19.85  ? 151  TYR A CD1  1 
ATOM   5197 C CD2  . TYR B 1 151 ? 140.969 126.458 120.713 1.00 23.19  ? 151  TYR A CD2  1 
ATOM   5198 C CE1  . TYR B 1 151 ? 141.039 124.312 118.979 1.00 23.65  ? 151  TYR A CE1  1 
ATOM   5199 C CE2  . TYR B 1 151 ? 140.116 126.422 119.625 1.00 30.06  ? 151  TYR A CE2  1 
ATOM   5200 C CZ   . TYR B 1 151 ? 140.155 125.346 118.764 1.00 30.84  ? 151  TYR A CZ   1 
ATOM   5201 O OH   . TYR B 1 151 ? 139.309 125.303 117.680 1.00 29.80  ? 151  TYR A OH   1 
ATOM   5202 N N    . PRO B 1 152 ? 143.948 128.464 121.895 1.00 12.29  ? 152  PRO A N    1 
ATOM   5203 C CA   . PRO B 1 152 ? 143.911 129.788 121.243 1.00 8.24   ? 152  PRO A CA   1 
ATOM   5204 C C    . PRO B 1 152 ? 145.170 130.164 120.484 1.00 7.82   ? 152  PRO A C    1 
ATOM   5205 O O    . PRO B 1 152 ? 145.070 130.799 119.427 1.00 20.49  ? 152  PRO A O    1 
ATOM   5206 C CB   . PRO B 1 152 ? 143.667 130.751 122.411 1.00 17.41  ? 152  PRO A CB   1 
ATOM   5207 C CG   . PRO B 1 152 ? 143.036 129.944 123.446 1.00 17.04  ? 152  PRO A CG   1 
ATOM   5208 C CD   . PRO B 1 152 ? 143.648 128.594 123.336 1.00 15.51  ? 152  PRO A CD   1 
ATOM   5209 N N    . ILE B 1 153 ? 146.354 129.804 120.981 1.00 7.34   ? 153  ILE A N    1 
ATOM   5210 C CA   . ILE B 1 153 ? 147.589 130.135 120.278 1.00 12.24  ? 153  ILE A CA   1 
ATOM   5211 C C    . ILE B 1 153 ? 147.787 129.290 119.027 1.00 18.21  ? 153  ILE A C    1 
ATOM   5212 O O    . ILE B 1 153 ? 148.187 129.837 117.985 1.00 28.09  ? 153  ILE A O    1 
ATOM   5213 C CB   . ILE B 1 153 ? 148.803 129.995 121.223 1.00 9.79   ? 153  ILE A CB   1 
ATOM   5214 C CG1  . ILE B 1 153 ? 148.749 131.070 122.308 1.00 13.29  ? 153  ILE A CG1  1 
ATOM   5215 C CG2  . ILE B 1 153 ? 150.114 130.106 120.466 1.00 10.06  ? 153  ILE A CG2  1 
ATOM   5216 C CD1  . ILE B 1 153 ? 149.826 130.939 123.350 1.00 20.78  ? 153  ILE A CD1  1 
ATOM   5217 N N    . VAL B 1 154 ? 147.503 127.989 119.083 1.00 24.77  ? 154  VAL A N    1 
ATOM   5218 C CA   . VAL B 1 154 ? 147.635 127.139 117.901 1.00 19.31  ? 154  VAL A CA   1 
ATOM   5219 C C    . VAL B 1 154 ? 146.644 127.564 116.822 1.00 23.63  ? 154  VAL A C    1 
ATOM   5220 O O    . VAL B 1 154 ? 146.964 127.561 115.627 1.00 28.37  ? 154  VAL A O    1 
ATOM   5221 C CB   . VAL B 1 154 ? 147.464 125.657 118.285 1.00 18.81  ? 154  VAL A CB   1 
ATOM   5222 C CG1  . VAL B 1 154 ? 147.444 124.774 117.052 1.00 20.58  ? 154  VAL A CG1  1 
ATOM   5223 C CG2  . VAL B 1 154 ? 148.597 125.228 119.193 1.00 28.81  ? 154  VAL A CG2  1 
ATOM   5224 N N    . GLU B 1 155 ? 145.438 127.968 117.233 1.00 19.11  ? 155  GLU A N    1 
ATOM   5225 C CA   . GLU B 1 155 ? 144.419 128.410 116.287 1.00 15.07  ? 155  GLU A CA   1 
ATOM   5226 C C    . GLU B 1 155 ? 144.858 129.663 115.534 1.00 25.11  ? 155  GLU A C    1 
ATOM   5227 O O    . GLU B 1 155 ? 144.655 129.761 114.321 1.00 32.38  ? 155  GLU A O    1 
ATOM   5228 C CB   . GLU B 1 155 ? 143.084 128.639 117.005 1.00 12.51  ? 155  GLU A CB   1 
ATOM   5229 C CG   . GLU B 1 155 ? 142.282 129.831 116.512 1.00 24.75  ? 155  GLU A CG   1 
ATOM   5230 C CD   . GLU B 1 155 ? 140.886 129.877 117.092 1.00 35.37  ? 155  GLU A CD   1 
ATOM   5231 O OE1  . GLU B 1 155 ? 140.110 128.930 116.848 1.00 33.19  ? 155  GLU A OE1  1 
ATOM   5232 O OE2  . GLU B 1 155 ? 140.557 130.865 117.785 1.00 35.28  ? 155  GLU A OE2  1 
ATOM   5233 N N    . ALA B 1 156 ? 145.471 130.617 116.242 1.00 30.42  ? 156  ALA A N    1 
ATOM   5234 C CA   . ALA B 1 156 ? 145.889 131.870 115.616 1.00 25.07  ? 156  ALA A CA   1 
ATOM   5235 C C    . ALA B 1 156 ? 146.938 131.627 114.539 1.00 19.13  ? 156  ALA A C    1 
ATOM   5236 O O    . ALA B 1 156 ? 146.874 132.210 113.451 1.00 31.90  ? 156  ALA A O    1 
ATOM   5237 C CB   . ALA B 1 156 ? 146.420 132.835 116.674 1.00 18.80  ? 156  ALA A CB   1 
ATOM   5238 N N    . LEU B 1 157 ? 147.907 130.764 114.828 1.00 16.27  ? 157  LEU A N    1 
ATOM   5239 C CA   . LEU B 1 157 ? 149.013 130.494 113.919 1.00 27.50  ? 157  LEU A CA   1 
ATOM   5240 C C    . LEU B 1 157 ? 148.609 129.580 112.771 1.00 33.06  ? 157  LEU A C    1 
ATOM   5241 O O    . LEU B 1 157 ? 149.114 129.738 111.655 1.00 33.17  ? 157  LEU A O    1 
ATOM   5242 C CB   . LEU B 1 157 ? 150.177 129.862 114.684 1.00 28.09  ? 157  LEU A CB   1 
ATOM   5243 C CG   . LEU B 1 157 ? 150.952 130.713 115.689 1.00 28.86  ? 157  LEU A CG   1 
ATOM   5244 C CD1  . LEU B 1 157 ? 151.835 129.828 116.547 1.00 19.55  ? 157  LEU A CD1  1 
ATOM   5245 C CD2  . LEU B 1 157 ? 151.788 131.743 114.966 1.00 37.10  ? 157  LEU A CD2  1 
ATOM   5246 N N    . TYR B 1 158 ? 147.714 128.624 113.021 1.00 33.27  ? 158  TYR A N    1 
ATOM   5247 C CA   . TYR B 1 158 ? 147.486 127.500 112.120 1.00 24.88  ? 158  TYR A CA   1 
ATOM   5248 C C    . TYR B 1 158 ? 146.076 127.401 111.548 1.00 28.04  ? 158  TYR A C    1 
ATOM   5249 O O    . TYR B 1 158 ? 145.771 126.390 110.905 1.00 32.09  ? 158  TYR A O    1 
ATOM   5250 C CB   . TYR B 1 158 ? 147.843 126.188 112.824 1.00 28.65  ? 158  TYR A CB   1 
ATOM   5251 C CG   . TYR B 1 158 ? 149.329 125.938 112.929 1.00 31.85  ? 158  TYR A CG   1 
ATOM   5252 C CD1  . TYR B 1 158 ? 150.104 125.785 111.788 1.00 36.34  ? 158  TYR A CD1  1 
ATOM   5253 C CD2  . TYR B 1 158 ? 149.956 125.857 114.162 1.00 30.65  ? 158  TYR A CD2  1 
ATOM   5254 C CE1  . TYR B 1 158 ? 151.461 125.556 111.872 1.00 33.09  ? 158  TYR A CE1  1 
ATOM   5255 C CE2  . TYR B 1 158 ? 151.315 125.630 114.256 1.00 28.97  ? 158  TYR A CE2  1 
ATOM   5256 C CZ   . TYR B 1 158 ? 152.061 125.480 113.107 1.00 27.66  ? 158  TYR A CZ   1 
ATOM   5257 O OH   . TYR B 1 158 ? 153.413 125.254 113.193 1.00 27.17  ? 158  TYR A OH   1 
ATOM   5258 N N    . GLN B 1 159 ? 145.183 128.371 111.786 1.00 46.37  ? 159  GLN A N    1 
ATOM   5259 C CA   . GLN B 1 159 ? 143.846 128.214 111.215 1.00 37.42  ? 159  GLN A CA   1 
ATOM   5260 C C    . GLN B 1 159 ? 143.877 128.305 109.695 1.00 42.04  ? 159  GLN A C    1 
ATOM   5261 O O    . GLN B 1 159 ? 143.201 127.522 109.018 1.00 38.12  ? 159  GLN A O    1 
ATOM   5262 C CB   . GLN B 1 159 ? 142.895 129.271 111.779 1.00 36.93  ? 159  GLN A CB   1 
ATOM   5263 C CG   . GLN B 1 159 ? 141.414 129.205 111.345 1.00 41.94  ? 159  GLN A CG   1 
ATOM   5264 C CD   . GLN B 1 159 ? 140.769 127.824 111.432 1.00 50.04  ? 159  GLN A CD   1 
ATOM   5265 O OE1  . GLN B 1 159 ? 139.974 127.567 112.336 1.00 53.80  ? 159  GLN A OE1  1 
ATOM   5266 N NE2  . GLN B 1 159 ? 141.030 126.968 110.447 1.00 47.06  ? 159  GLN A NE2  1 
ATOM   5267 N N    . THR B 1 160 ? 144.643 129.237 109.127 1.00 58.12  ? 160  THR A N    1 
ATOM   5268 C CA   . THR B 1 160 ? 144.537 129.378 107.683 1.00 54.46  ? 160  THR A CA   1 
ATOM   5269 C C    . THR B 1 160 ? 145.596 128.550 106.977 1.00 49.68  ? 160  THR A C    1 
ATOM   5270 O O    . THR B 1 160 ? 145.473 128.286 105.776 1.00 50.85  ? 160  THR A O    1 
ATOM   5271 C CB   . THR B 1 160 ? 144.673 130.846 107.269 1.00 48.21  ? 160  THR A CB   1 
ATOM   5272 O OG1  . THR B 1 160 ? 145.866 131.397 107.842 1.00 46.84  ? 160  THR A OG1  1 
ATOM   5273 C CG2  . THR B 1 160 ? 143.472 131.646 107.745 1.00 47.57  ? 160  THR A CG2  1 
ATOM   5274 N N    . THR B 1 161 ? 146.631 128.148 107.712 1.00 52.52  ? 161  THR A N    1 
ATOM   5275 C CA   . THR B 1 161 ? 147.757 127.376 107.203 1.00 53.48  ? 161  THR A CA   1 
ATOM   5276 C C    . THR B 1 161 ? 147.681 125.995 107.839 1.00 57.93  ? 161  THR A C    1 
ATOM   5277 O O    . THR B 1 161 ? 147.802 125.882 109.064 1.00 58.15  ? 161  THR A O    1 
ATOM   5278 C CB   . THR B 1 161 ? 149.091 128.051 107.509 1.00 56.20  ? 161  THR A CB   1 
ATOM   5279 O OG1  . THR B 1 161 ? 149.230 129.224 106.699 1.00 55.99  ? 161  THR A OG1  1 
ATOM   5280 C CG2  . THR B 1 161 ? 150.233 127.097 107.195 1.00 54.92  ? 161  THR A CG2  1 
ATOM   5281 N N    . TYR B 1 162 ? 147.496 124.954 107.022 1.00 51.38  ? 162  TYR A N    1 
ATOM   5282 C CA   . TYR B 1 162 ? 147.473 123.567 107.487 1.00 45.38  ? 162  TYR A CA   1 
ATOM   5283 C C    . TYR B 1 162 ? 146.399 123.373 108.560 1.00 42.32  ? 162  TYR A C    1 
ATOM   5284 O O    . TYR B 1 162 ? 146.715 123.299 109.754 1.00 47.61  ? 162  TYR A O    1 
ATOM   5285 C CB   . TYR B 1 162 ? 148.852 123.181 108.025 1.00 47.74  ? 162  TYR A CB   1 
ATOM   5286 C CG   . TYR B 1 162 ? 149.948 123.114 106.984 1.00 49.46  ? 162  TYR A CG   1 
ATOM   5287 C CD1  . TYR B 1 162 ? 149.655 122.994 105.633 1.00 50.31  ? 162  TYR A CD1  1 
ATOM   5288 C CD2  . TYR B 1 162 ? 151.283 123.198 107.357 1.00 49.53  ? 162  TYR A CD2  1 
ATOM   5289 C CE1  . TYR B 1 162 ? 150.662 122.945 104.687 1.00 51.59  ? 162  TYR A CE1  1 
ATOM   5290 C CE2  . TYR B 1 162 ? 152.294 123.148 106.419 1.00 52.14  ? 162  TYR A CE2  1 
ATOM   5291 C CZ   . TYR B 1 162 ? 151.978 123.019 105.086 1.00 52.20  ? 162  TYR A CZ   1 
ATOM   5292 O OH   . TYR B 1 162 ? 152.981 122.972 104.146 1.00 54.52  ? 162  TYR A OH   1 
ATOM   5293 N N    . PRO B 1 163 ? 145.126 123.296 108.167 1.00 38.08  ? 163  PRO A N    1 
ATOM   5294 C CA   . PRO B 1 163 ? 144.028 123.153 109.147 1.00 39.23  ? 163  PRO A CA   1 
ATOM   5295 C C    . PRO B 1 163 ? 144.047 121.897 110.019 1.00 37.28  ? 163  PRO A C    1 
ATOM   5296 O O    . PRO B 1 163 ? 143.441 121.915 111.097 1.00 33.28  ? 163  PRO A O    1 
ATOM   5297 C CB   . PRO B 1 163 ? 142.773 123.185 108.264 1.00 42.01  ? 163  PRO A CB   1 
ATOM   5298 C CG   . PRO B 1 163 ? 143.245 122.760 106.915 1.00 45.47  ? 163  PRO A CG   1 
ATOM   5299 C CD   . PRO B 1 163 ? 144.628 123.312 106.782 1.00 44.03  ? 163  PRO A CD   1 
ATOM   5300 N N    . GLU B 1 164 ? 144.708 120.816 109.605 1.00 48.43  ? 164  GLU A N    1 
ATOM   5301 C CA   . GLU B 1 164 ? 144.733 119.583 110.392 1.00 48.11  ? 164  GLU A CA   1 
ATOM   5302 C C    . GLU B 1 164 ? 145.551 119.643 111.681 1.00 45.45  ? 164  GLU A C    1 
ATOM   5303 O O    . GLU B 1 164 ? 145.471 118.694 112.467 1.00 53.04  ? 164  GLU A O    1 
ATOM   5304 C CB   . GLU B 1 164 ? 145.281 118.434 109.543 1.00 45.16  ? 164  GLU A CB   1 
ATOM   5305 C CG   . GLU B 1 164 ? 146.484 118.808 108.691 1.00 48.05  ? 164  GLU A CG   1 
ATOM   5306 C CD   . GLU B 1 164 ? 146.144 118.976 107.227 1.00 55.77  ? 164  GLU A CD   1 
ATOM   5307 O OE1  . GLU B 1 164 ? 147.070 118.907 106.391 1.00 54.27  ? 164  GLU A OE1  1 
ATOM   5308 O OE2  . GLU B 1 164 ? 144.953 119.175 106.910 1.00 52.46  ? 164  GLU A OE2  1 
ATOM   5309 N N    . TYR B 1 165 ? 146.326 120.697 111.937 1.00 33.09  ? 165  TYR A N    1 
ATOM   5310 C CA   . TYR B 1 165 ? 147.087 120.727 113.185 1.00 33.70  ? 165  TYR A CA   1 
ATOM   5311 C C    . TYR B 1 165 ? 146.251 121.040 114.422 1.00 35.49  ? 165  TYR A C    1 
ATOM   5312 O O    . TYR B 1 165 ? 146.680 120.703 115.531 1.00 47.96  ? 165  TYR A O    1 
ATOM   5313 C CB   . TYR B 1 165 ? 148.239 121.723 113.087 1.00 41.62  ? 165  TYR A CB   1 
ATOM   5314 C CG   . TYR B 1 165 ? 149.383 121.218 112.248 1.00 43.92  ? 165  TYR A CG   1 
ATOM   5315 C CD1  . TYR B 1 165 ? 150.100 120.095 112.631 1.00 39.33  ? 165  TYR A CD1  1 
ATOM   5316 C CD2  . TYR B 1 165 ? 149.757 121.865 111.086 1.00 44.31  ? 165  TYR A CD2  1 
ATOM   5317 C CE1  . TYR B 1 165 ? 151.148 119.628 111.872 1.00 43.75  ? 165  TYR A CE1  1 
ATOM   5318 C CE2  . TYR B 1 165 ? 150.807 121.404 110.320 1.00 41.95  ? 165  TYR A CE2  1 
ATOM   5319 C CZ   . TYR B 1 165 ? 151.498 120.287 110.716 1.00 44.81  ? 165  TYR A CZ   1 
ATOM   5320 O OH   . TYR B 1 165 ? 152.544 119.827 109.951 1.00 48.73  ? 165  TYR A OH   1 
ATOM   5321 N N    . LEU B 1 166 ? 145.093 121.690 114.278 1.00 26.73  ? 166  LEU A N    1 
ATOM   5322 C CA   . LEU B 1 166 ? 144.295 122.039 115.454 1.00 30.53  ? 166  LEU A CA   1 
ATOM   5323 C C    . LEU B 1 166 ? 143.763 120.799 116.170 1.00 33.26  ? 166  LEU A C    1 
ATOM   5324 O O    . LEU B 1 166 ? 143.690 120.772 117.404 1.00 34.65  ? 166  LEU A O    1 
ATOM   5325 C CB   . LEU B 1 166 ? 143.135 122.956 115.060 1.00 33.97  ? 166  LEU A CB   1 
ATOM   5326 C CG   . LEU B 1 166 ? 143.391 124.435 114.749 1.00 32.83  ? 166  LEU A CG   1 
ATOM   5327 C CD1  . LEU B 1 166 ? 143.997 124.641 113.370 1.00 28.32  ? 166  LEU A CD1  1 
ATOM   5328 C CD2  . LEU B 1 166 ? 142.101 125.225 114.887 1.00 35.06  ? 166  LEU A CD2  1 
ATOM   5329 N N    . GLN B 1 167 ? 143.376 119.773 115.410 1.00 38.92  ? 167  GLN A N    1 
ATOM   5330 C CA   . GLN B 1 167 ? 142.739 118.577 115.958 1.00 37.27  ? 167  GLN A CA   1 
ATOM   5331 C C    . GLN B 1 167 ? 143.660 117.733 116.842 1.00 42.57  ? 167  GLN A C    1 
ATOM   5332 O O    . GLN B 1 167 ? 143.163 116.999 117.701 1.00 47.57  ? 167  GLN A O    1 
ATOM   5333 C CB   . GLN B 1 167 ? 142.209 117.741 114.785 1.00 38.32  ? 167  GLN A CB   1 
ATOM   5334 C CG   . GLN B 1 167 ? 141.470 116.460 115.133 1.00 41.56  ? 167  GLN A CG   1 
ATOM   5335 C CD   . GLN B 1 167 ? 140.914 115.766 113.905 1.00 50.86  ? 167  GLN A CD   1 
ATOM   5336 O OE1  . GLN B 1 167 ? 139.715 115.506 113.813 1.00 53.02  ? 167  GLN A OE1  1 
ATOM   5337 N NE2  . GLN B 1 167 ? 141.786 115.472 112.947 1.00 47.49  ? 167  GLN A NE2  1 
ATOM   5338 N N    . TYR B 1 168 ? 144.980 117.892 116.726 1.00 31.91  ? 168  TYR A N    1 
ATOM   5339 C CA   . TYR B 1 168 ? 145.937 117.116 117.516 1.00 19.08  ? 168  TYR A CA   1 
ATOM   5340 C C    . TYR B 1 168 ? 145.905 117.439 119.007 1.00 16.25  ? 168  TYR A C    1 
ATOM   5341 O O    . TYR B 1 168 ? 146.337 116.608 119.822 1.00 33.61  ? 168  TYR A O    1 
ATOM   5342 C CB   . TYR B 1 168 ? 147.341 117.340 116.961 1.00 22.13  ? 168  TYR A CB   1 
ATOM   5343 C CG   . TYR B 1 168 ? 147.551 116.674 115.622 1.00 25.08  ? 168  TYR A CG   1 
ATOM   5344 C CD1  . TYR B 1 168 ? 146.829 115.544 115.265 1.00 25.65  ? 168  TYR A CD1  1 
ATOM   5345 C CD2  . TYR B 1 168 ? 148.445 117.195 114.700 1.00 35.64  ? 168  TYR A CD2  1 
ATOM   5346 C CE1  . TYR B 1 168 ? 147.005 114.944 114.036 1.00 25.37  ? 168  TYR A CE1  1 
ATOM   5347 C CE2  . TYR B 1 168 ? 148.630 116.601 113.470 1.00 36.61  ? 168  TYR A CE2  1 
ATOM   5348 C CZ   . TYR B 1 168 ? 147.907 115.478 113.144 1.00 34.53  ? 168  TYR A CZ   1 
ATOM   5349 O OH   . TYR B 1 168 ? 148.090 114.887 111.917 1.00 37.29  ? 168  TYR A OH   1 
ATOM   5350 N N    . ILE B 1 169 ? 145.399 118.617 119.375 1.00 14.07  ? 169  ILE A N    1 
ATOM   5351 C CA   . ILE B 1 169 ? 145.321 119.021 120.777 1.00 26.82  ? 169  ILE A CA   1 
ATOM   5352 C C    . ILE B 1 169 ? 144.380 118.108 121.556 1.00 34.60  ? 169  ILE A C    1 
ATOM   5353 O O    . ILE B 1 169 ? 144.676 117.717 122.692 1.00 38.13  ? 169  ILE A O    1 
ATOM   5354 C CB   . ILE B 1 169 ? 144.898 120.500 120.866 1.00 27.69  ? 169  ILE A CB   1 
ATOM   5355 C CG1  . ILE B 1 169 ? 146.047 121.406 120.419 1.00 36.08  ? 169  ILE A CG1  1 
ATOM   5356 C CG2  . ILE B 1 169 ? 144.441 120.862 122.271 1.00 24.34  ? 169  ILE A CG2  1 
ATOM   5357 C CD1  . ILE B 1 169 ? 147.150 121.558 121.442 1.00 32.43  ? 169  ILE A CD1  1 
ATOM   5358 N N    . TYR B 1 170 ? 143.256 117.723 120.955 1.00 35.04  ? 170  TYR A N    1 
ATOM   5359 C CA   . TYR B 1 170 ? 142.287 116.885 121.650 1.00 24.89  ? 170  TYR A CA   1 
ATOM   5360 C C    . TYR B 1 170 ? 142.661 115.408 121.637 1.00 28.84  ? 170  TYR A C    1 
ATOM   5361 O O    . TYR B 1 170 ? 141.995 114.615 122.308 1.00 38.39  ? 170  TYR A O    1 
ATOM   5362 C CB   . TYR B 1 170 ? 140.894 117.085 121.054 1.00 13.35  ? 170  TYR A CB   1 
ATOM   5363 C CG   . TYR B 1 170 ? 140.420 118.514 121.155 1.00 19.25  ? 170  TYR A CG   1 
ATOM   5364 C CD1  . TYR B 1 170 ? 140.125 119.076 122.390 1.00 20.25  ? 170  TYR A CD1  1 
ATOM   5365 C CD2  . TYR B 1 170 ? 140.278 119.304 120.024 1.00 22.59  ? 170  TYR A CD2  1 
ATOM   5366 C CE1  . TYR B 1 170 ? 139.698 120.381 122.497 1.00 19.91  ? 170  TYR A CE1  1 
ATOM   5367 C CE2  . TYR B 1 170 ? 139.848 120.613 120.121 1.00 24.95  ? 170  TYR A CE2  1 
ATOM   5368 C CZ   . TYR B 1 170 ? 139.560 121.145 121.361 1.00 26.16  ? 170  TYR A CZ   1 
ATOM   5369 O OH   . TYR B 1 170 ? 139.133 122.447 121.469 1.00 32.96  ? 170  TYR A OH   1 
ATOM   5370 N N    . LEU B 1 171 ? 143.693 115.022 120.889 1.00 28.77  ? 171  LEU A N    1 
ATOM   5371 C CA   . LEU B 1 171 ? 144.185 113.650 120.896 1.00 32.86  ? 171  LEU A CA   1 
ATOM   5372 C C    . LEU B 1 171 ? 145.360 113.453 121.846 1.00 38.15  ? 171  LEU A C    1 
ATOM   5373 O O    . LEU B 1 171 ? 145.390 112.466 122.589 1.00 32.76  ? 171  LEU A O    1 
ATOM   5374 C CB   . LEU B 1 171 ? 144.615 113.192 119.497 1.00 20.14  ? 171  LEU A CB   1 
ATOM   5375 C CG   . LEU B 1 171 ? 143.603 112.721 118.453 1.00 18.05  ? 171  LEU A CG   1 
ATOM   5376 C CD1  . LEU B 1 171 ? 143.020 113.868 117.685 1.00 31.46  ? 171  LEU A CD1  1 
ATOM   5377 C CD2  . LEU B 1 171 ? 144.256 111.730 117.506 1.00 21.67  ? 171  LEU A CD2  1 
ATOM   5378 N N    . VAL B 1 172 ? 146.337 114.364 121.832 1.00 46.92  ? 172  VAL A N    1 
ATOM   5379 C CA   . VAL B 1 172 ? 147.539 114.159 122.640 1.00 32.91  ? 172  VAL A CA   1 
ATOM   5380 C C    . VAL B 1 172 ? 147.265 114.270 124.142 1.00 39.85  ? 172  VAL A C    1 
ATOM   5381 O O    . VAL B 1 172 ? 147.773 113.467 124.935 1.00 47.93  ? 172  VAL A O    1 
ATOM   5382 C CB   . VAL B 1 172 ? 148.612 115.173 122.204 1.00 26.84  ? 172  VAL A CB   1 
ATOM   5383 C CG1  . VAL B 1 172 ? 149.822 115.068 123.083 1.00 39.59  ? 172  VAL A CG1  1 
ATOM   5384 C CG2  . VAL B 1 172 ? 148.990 114.972 120.750 1.00 31.08  ? 172  VAL A CG2  1 
ATOM   5385 N N    . ALA B 1 173 ? 146.454 115.241 124.556 1.00 45.68  ? 173  ALA A N    1 
ATOM   5386 C CA   . ALA B 1 173 ? 146.203 115.464 125.983 1.00 51.94  ? 173  ALA A CA   1 
ATOM   5387 C C    . ALA B 1 173 ? 145.496 114.330 126.737 1.00 56.74  ? 173  ALA A C    1 
ATOM   5388 O O    . ALA B 1 173 ? 146.040 113.875 127.766 1.00 55.96  ? 173  ALA A O    1 
ATOM   5389 C CB   . ALA B 1 173 ? 145.479 116.807 126.163 1.00 49.23  ? 173  ALA A CB   1 
ATOM   5390 N N    . PRO B 1 174 ? 144.322 113.822 126.307 1.00 58.06  ? 174  PRO A N    1 
ATOM   5391 C CA   . PRO B 1 174 ? 143.668 112.758 127.098 1.00 56.18  ? 174  PRO A CA   1 
ATOM   5392 C C    . PRO B 1 174 ? 144.437 111.460 127.233 1.00 56.15  ? 174  PRO A C    1 
ATOM   5393 O O    . PRO B 1 174 ? 144.407 110.864 128.317 1.00 55.91  ? 174  PRO A O    1 
ATOM   5394 C CB   . PRO B 1 174 ? 142.356 112.521 126.339 1.00 55.48  ? 174  PRO A CB   1 
ATOM   5395 C CG   . PRO B 1 174 ? 142.114 113.751 125.577 1.00 56.62  ? 174  PRO A CG   1 
ATOM   5396 C CD   . PRO B 1 174 ? 143.468 114.229 125.174 1.00 49.04  ? 174  PRO A CD   1 
ATOM   5397 N N    . ILE B 1 175 ? 145.123 110.997 126.188 1.00 51.79  ? 175  ILE A N    1 
ATOM   5398 C CA   . ILE B 1 175 ? 145.833 109.728 126.305 1.00 56.43  ? 175  ILE A CA   1 
ATOM   5399 C C    . ILE B 1 175 ? 146.961 109.841 127.329 1.00 55.63  ? 175  ILE A C    1 
ATOM   5400 O O    . ILE B 1 175 ? 147.155 108.944 128.165 1.00 60.51  ? 175  ILE A O    1 
ATOM   5401 C CB   . ILE B 1 175 ? 146.332 109.286 124.917 1.00 58.84  ? 175  ILE A CB   1 
ATOM   5402 C CG1  . ILE B 1 175 ? 145.147 108.964 124.006 1.00 51.74  ? 175  ILE A CG1  1 
ATOM   5403 C CG2  . ILE B 1 175 ? 147.189 108.070 125.012 1.00 58.57  ? 175  ILE A CG2  1 
ATOM   5404 C CD1  . ILE B 1 175 ? 145.528 108.790 122.554 1.00 50.71  ? 175  ILE A CD1  1 
ATOM   5405 N N    . SER B 1 176 ? 147.709 110.949 127.293 1.00 48.52  ? 176  SER A N    1 
ATOM   5406 C CA   . SER B 1 176 ? 148.781 111.150 128.262 1.00 57.01  ? 176  SER A CA   1 
ATOM   5407 C C    . SER B 1 176 ? 148.235 111.241 129.682 1.00 57.91  ? 176  SER A C    1 
ATOM   5408 O O    . SER B 1 176 ? 148.810 110.657 130.614 1.00 63.06  ? 176  SER A O    1 
ATOM   5409 C CB   . SER B 1 176 ? 149.575 112.408 127.921 1.00 65.43  ? 176  SER A CB   1 
ATOM   5410 O OG   . SER B 1 176 ? 150.507 112.697 128.947 1.00 69.29  ? 176  SER A OG   1 
ATOM   5411 N N    . LEU B 1 177 ? 147.105 111.944 129.860 1.00 50.70  ? 177  LEU A N    1 
ATOM   5412 C CA   . LEU B 1 177 ? 146.515 112.058 131.194 1.00 57.46  ? 177  LEU A CA   1 
ATOM   5413 C C    . LEU B 1 177 ? 146.087 110.692 131.716 1.00 61.76  ? 177  LEU A C    1 
ATOM   5414 O O    . LEU B 1 177 ? 146.428 110.317 132.852 1.00 65.25  ? 177  LEU A O    1 
ATOM   5415 C CB   . LEU B 1 177 ? 145.326 113.022 131.143 1.00 56.12  ? 177  LEU A CB   1 
ATOM   5416 C CG   . LEU B 1 177 ? 144.167 112.958 132.145 1.00 50.57  ? 177  LEU A CG   1 
ATOM   5417 C CD1  . LEU B 1 177 ? 144.619 113.191 133.575 1.00 56.00  ? 177  LEU A CD1  1 
ATOM   5418 C CD2  . LEU B 1 177 ? 143.087 113.958 131.760 1.00 50.93  ? 177  LEU A CD2  1 
ATOM   5419 N N    . MET B 1 178 ? 145.523 109.870 130.819 1.00 67.57  ? 178  MET A N    1 
ATOM   5420 C CA   . MET B 1 178 ? 144.981 108.561 131.166 1.00 66.40  ? 178  MET A CA   1 
ATOM   5421 C C    . MET B 1 178 ? 146.092 107.601 131.535 1.00 69.42  ? 178  MET A C    1 
ATOM   5422 O O    . MET B 1 178 ? 145.909 106.741 132.404 1.00 70.62  ? 178  MET A O    1 
ATOM   5423 C CB   . MET B 1 178 ? 144.170 108.001 130.000 1.00 61.43  ? 178  MET A CB   1 
ATOM   5424 C CG   . MET B 1 178 ? 142.787 108.594 129.851 1.00 65.92  ? 178  MET A CG   1 
ATOM   5425 S SD   . MET B 1 178 ? 141.614 107.367 129.261 1.00 74.13  ? 178  MET A SD   1 
ATOM   5426 C CE   . MET B 1 178 ? 141.926 107.410 127.497 1.00 68.02  ? 178  MET A CE   1 
ATOM   5427 N N    . MET B 1 179 ? 147.239 107.722 130.880 1.00 58.78  ? 179  MET A N    1 
ATOM   5428 C CA   . MET B 1 179 ? 148.291 106.736 131.040 1.00 53.63  ? 179  MET A CA   1 
ATOM   5429 C C    . MET B 1 179 ? 149.268 107.132 132.133 1.00 53.53  ? 179  MET A C    1 
ATOM   5430 O O    . MET B 1 179 ? 149.980 106.262 132.647 1.00 62.93  ? 179  MET A O    1 
ATOM   5431 C CB   . MET B 1 179 ? 149.048 106.491 129.733 1.00 54.08  ? 179  MET A CB   1 
ATOM   5432 C CG   . MET B 1 179 ? 148.218 105.800 128.673 1.00 56.59  ? 179  MET A CG   1 
ATOM   5433 S SD   . MET B 1 179 ? 148.975 105.906 127.047 1.00 70.13  ? 179  MET A SD   1 
ATOM   5434 C CE   . MET B 1 179 ? 148.543 104.308 126.368 1.00 58.34  ? 179  MET A CE   1 
ATOM   5435 N N    . LEU B 1 180 ? 149.339 108.413 132.496 1.00 45.06  ? 180  LEU A N    1 
ATOM   5436 C CA   . LEU B 1 180 ? 150.335 108.833 133.471 1.00 56.03  ? 180  LEU A CA   1 
ATOM   5437 C C    . LEU B 1 180 ? 149.777 109.185 134.848 1.00 58.29  ? 180  LEU A C    1 
ATOM   5438 O O    . LEU B 1 180 ? 150.421 108.848 135.844 1.00 59.16  ? 180  LEU A O    1 
ATOM   5439 C CB   . LEU B 1 180 ? 151.128 110.030 132.930 1.00 59.10  ? 180  LEU A CB   1 
ATOM   5440 C CG   . LEU B 1 180 ? 152.324 109.702 132.024 1.00 53.69  ? 180  LEU A CG   1 
ATOM   5441 C CD1  . LEU B 1 180 ? 153.216 108.644 132.659 1.00 53.47  ? 180  LEU A CD1  1 
ATOM   5442 C CD2  . LEU B 1 180 ? 151.904 109.289 130.617 1.00 52.03  ? 180  LEU A CD2  1 
ATOM   5443 N N    . ASN B 1 181 ? 148.635 109.878 134.969 1.00 49.43  ? 181  ASN A N    1 
ATOM   5444 C CA   . ASN B 1 181 ? 148.119 110.198 136.307 1.00 49.03  ? 181  ASN A CA   1 
ATOM   5445 C C    . ASN B 1 181 ? 147.832 108.997 137.228 1.00 58.32  ? 181  ASN A C    1 
ATOM   5446 O O    . ASN B 1 181 ? 148.128 109.106 138.438 1.00 56.96  ? 181  ASN A O    1 
ATOM   5447 C CB   . ASN B 1 181 ? 146.889 111.103 136.167 1.00 49.59  ? 181  ASN A CB   1 
ATOM   5448 C CG   . ASN B 1 181 ? 147.265 112.536 135.855 1.00 50.51  ? 181  ASN A CG   1 
ATOM   5449 O OD1  . ASN B 1 181 ? 147.631 112.860 134.727 1.00 46.94  ? 181  ASN A OD1  1 
ATOM   5450 N ND2  . ASN B 1 181 ? 147.174 113.404 136.855 1.00 55.30  ? 181  ASN A ND2  1 
ATOM   5451 N N    . PRO B 1 182 ? 147.242 107.876 136.765 1.00 65.28  ? 182  PRO A N    1 
ATOM   5452 C CA   . PRO B 1 182 ? 146.998 106.743 137.683 1.00 59.56  ? 182  PRO A CA   1 
ATOM   5453 C C    . PRO B 1 182 ? 148.232 106.222 138.397 1.00 56.84  ? 182  PRO A C    1 
ATOM   5454 O O    . PRO B 1 182 ? 148.130 105.831 139.564 1.00 56.50  ? 182  PRO A O    1 
ATOM   5455 C CB   . PRO B 1 182 ? 146.399 105.664 136.772 1.00 54.93  ? 182  PRO A CB   1 
ATOM   5456 C CG   . PRO B 1 182 ? 145.833 106.371 135.639 1.00 53.50  ? 182  PRO A CG   1 
ATOM   5457 C CD   . PRO B 1 182 ? 146.518 107.688 135.490 1.00 59.89  ? 182  PRO A CD   1 
ATOM   5458 N N    . ILE B 1 183 ? 149.397 106.244 137.749 1.00 54.73  ? 183  ILE A N    1 
ATOM   5459 C CA   . ILE B 1 183 ? 150.633 105.804 138.394 1.00 58.31  ? 183  ILE A CA   1 
ATOM   5460 C C    . ILE B 1 183 ? 150.973 106.695 139.583 1.00 61.73  ? 183  ILE A C    1 
ATOM   5461 O O    . ILE B 1 183 ? 151.328 106.199 140.665 1.00 73.47  ? 183  ILE A O    1 
ATOM   5462 C CB   . ILE B 1 183 ? 151.779 105.759 137.368 1.00 58.31  ? 183  ILE A CB   1 
ATOM   5463 C CG1  . ILE B 1 183 ? 151.382 104.902 136.166 1.00 57.19  ? 183  ILE A CG1  1 
ATOM   5464 C CG2  . ILE B 1 183 ? 153.040 105.217 138.002 1.00 61.29  ? 183  ILE A CG2  1 
ATOM   5465 C CD1  . ILE B 1 183 ? 152.392 104.923 135.047 1.00 58.38  ? 183  ILE A CD1  1 
ATOM   5466 N N    . GLY B 1 184 ? 150.849 108.013 139.423 1.00 57.52  ? 184  GLY A N    1 
ATOM   5467 C CA   . GLY B 1 184 ? 151.137 108.889 140.544 1.00 61.67  ? 184  GLY A CA   1 
ATOM   5468 C C    . GLY B 1 184 ? 150.162 108.667 141.684 1.00 62.18  ? 184  GLY A C    1 
ATOM   5469 O O    . GLY B 1 184 ? 150.558 108.673 142.859 1.00 59.19  ? 184  GLY A O    1 
ATOM   5470 N N    . PHE B 1 185 ? 148.867 108.518 141.365 1.00 63.45  ? 185  PHE A N    1 
ATOM   5471 C CA   . PHE B 1 185 ? 147.938 108.287 142.472 1.00 64.72  ? 185  PHE A CA   1 
ATOM   5472 C C    . PHE B 1 185 ? 148.206 106.941 143.145 1.00 67.22  ? 185  PHE A C    1 
ATOM   5473 O O    . PHE B 1 185 ? 147.994 106.807 144.359 1.00 65.56  ? 185  PHE A O    1 
ATOM   5474 C CB   . PHE B 1 185 ? 146.479 108.393 142.017 1.00 65.27  ? 185  PHE A CB   1 
ATOM   5475 C CG   . PHE B 1 185 ? 146.022 109.803 141.722 1.00 63.91  ? 185  PHE A CG   1 
ATOM   5476 C CD1  . PHE B 1 185 ? 144.673 110.079 141.590 1.00 67.56  ? 185  PHE A CD1  1 
ATOM   5477 C CD2  . PHE B 1 185 ? 146.922 110.856 141.632 1.00 65.21  ? 185  PHE A CD2  1 
ATOM   5478 C CE1  . PHE B 1 185 ? 144.233 111.361 141.339 1.00 69.74  ? 185  PHE A CE1  1 
ATOM   5479 C CE2  . PHE B 1 185 ? 146.489 112.138 141.380 1.00 67.78  ? 185  PHE A CE2  1 
ATOM   5480 C CZ   . PHE B 1 185 ? 145.142 112.391 141.235 1.00 66.29  ? 185  PHE A CZ   1 
ATOM   5481 N N    . ILE B 1 186 ? 148.745 105.965 142.393 1.00 70.55  ? 186  ILE A N    1 
ATOM   5482 C CA   . ILE B 1 186 ? 149.110 104.678 142.987 1.00 67.69  ? 186  ILE A CA   1 
ATOM   5483 C C    . ILE B 1 186 ? 150.220 104.886 144.002 1.00 65.53  ? 186  ILE A C    1 
ATOM   5484 O O    . ILE B 1 186 ? 150.164 104.364 145.123 1.00 64.51  ? 186  ILE A O    1 
ATOM   5485 C CB   . ILE B 1 186 ? 149.511 103.659 141.901 1.00 63.71  ? 186  ILE A CB   1 
ATOM   5486 C CG1  . ILE B 1 186 ? 148.284 103.153 141.143 1.00 62.62  ? 186  ILE A CG1  1 
ATOM   5487 C CG2  . ILE B 1 186 ? 150.279 102.490 142.500 1.00 65.74  ? 186  ILE A CG2  1 
ATOM   5488 C CD1  . ILE B 1 186 ? 148.622 102.452 139.847 1.00 61.98  ? 186  ILE A CD1  1 
ATOM   5489 N N    . PHE B 1 187 ? 151.226 105.688 143.637 1.00 65.58  ? 187  PHE A N    1 
ATOM   5490 C CA   . PHE B 1 187 ? 152.361 105.886 144.536 1.00 64.85  ? 187  PHE A CA   1 
ATOM   5491 C C    . PHE B 1 187 ? 151.912 106.616 145.793 1.00 69.62  ? 187  PHE A C    1 
ATOM   5492 O O    . PHE B 1 187 ? 152.338 106.276 146.905 1.00 76.02  ? 187  PHE A O    1 
ATOM   5493 C CB   . PHE B 1 187 ? 153.516 106.618 143.851 1.00 64.71  ? 187  PHE A CB   1 
ATOM   5494 C CG   . PHE B 1 187 ? 154.383 105.731 142.999 1.00 65.29  ? 187  PHE A CG   1 
ATOM   5495 C CD1  . PHE B 1 187 ? 153.950 105.244 141.783 1.00 64.48  ? 187  PHE A CD1  1 
ATOM   5496 C CD2  . PHE B 1 187 ? 155.652 105.385 143.435 1.00 66.02  ? 187  PHE A CD2  1 
ATOM   5497 C CE1  . PHE B 1 187 ? 154.761 104.428 141.017 1.00 65.09  ? 187  PHE A CE1  1 
ATOM   5498 C CE2  . PHE B 1 187 ? 156.468 104.572 142.675 1.00 68.41  ? 187  PHE A CE2  1 
ATOM   5499 C CZ   . PHE B 1 187 ? 156.021 104.093 141.463 1.00 68.56  ? 187  PHE A CZ   1 
ATOM   5500 N N    . CYS B 1 188 ? 151.113 107.674 145.631 1.00 76.73  ? 188  CYS A N    1 
ATOM   5501 C CA   . CYS B 1 188 ? 150.684 108.425 146.806 1.00 79.50  ? 188  CYS A CA   1 
ATOM   5502 C C    . CYS B 1 188 ? 149.833 107.553 147.734 1.00 78.85  ? 188  CYS A C    1 
ATOM   5503 O O    . CYS B 1 188 ? 149.948 107.647 148.965 1.00 80.94  ? 188  CYS A O    1 
ATOM   5504 C CB   . CYS B 1 188 ? 149.933 109.687 146.391 1.00 78.74  ? 188  CYS A CB   1 
ATOM   5505 S SG   . CYS B 1 188 ? 150.123 111.021 147.590 1.00 75.09  ? 188  CYS A SG   1 
ATOM   5506 N N    . GLU B 1 189 ? 148.946 106.720 147.167 1.00 79.68  ? 189  GLU A N    1 
ATOM   5507 C CA   . GLU B 1 189 ? 148.189 105.788 148.004 1.00 80.72  ? 189  GLU A CA   1 
ATOM   5508 C C    . GLU B 1 189 ? 149.112 104.804 148.718 1.00 79.98  ? 189  GLU A C    1 
ATOM   5509 O O    . GLU B 1 189 ? 148.844 104.407 149.859 1.00 79.38  ? 189  GLU A O    1 
ATOM   5510 C CB   . GLU B 1 189 ? 147.149 105.042 147.166 1.00 81.13  ? 189  GLU A CB   1 
ATOM   5511 C CG   . GLU B 1 189 ? 145.859 105.821 146.894 1.00 82.68  ? 189  GLU A CG   1 
ATOM   5512 C CD   . GLU B 1 189 ? 145.051 106.153 148.148 1.00 84.15  ? 189  GLU A CD   1 
ATOM   5513 O OE1  . GLU B 1 189 ? 145.329 105.606 149.237 1.00 82.70  ? 189  GLU A OE1  1 
ATOM   5514 O OE2  . GLU B 1 189 ? 144.124 106.982 148.041 1.00 84.86  ? 189  GLU A OE2  1 
ATOM   5515 N N    . ILE B 1 190 ? 150.187 104.377 148.047 1.00 75.59  ? 190  ILE A N    1 
ATOM   5516 C CA   . ILE B 1 190 ? 151.191 103.529 148.690 1.00 72.71  ? 190  ILE A CA   1 
ATOM   5517 C C    . ILE B 1 190 ? 151.820 104.252 149.875 1.00 76.62  ? 190  ILE A C    1 
ATOM   5518 O O    . ILE B 1 190 ? 152.084 103.647 150.920 1.00 80.32  ? 190  ILE A O    1 
ATOM   5519 C CB   . ILE B 1 190 ? 152.248 103.056 147.671 1.00 76.35  ? 190  ILE A CB   1 
ATOM   5520 C CG1  . ILE B 1 190 ? 151.629 102.075 146.675 1.00 77.67  ? 190  ILE A CG1  1 
ATOM   5521 C CG2  . ILE B 1 190 ? 153.436 102.402 148.360 1.00 78.33  ? 190  ILE A CG2  1 
ATOM   5522 C CD1  . ILE B 1 190 ? 152.478 101.833 145.449 1.00 79.84  ? 190  ILE A CD1  1 
ATOM   5523 N N    . GLN B 1 191 ? 152.073 105.556 149.728 1.00 87.46  ? 191  GLN A N    1 
ATOM   5524 C CA   . GLN B 1 191 ? 152.577 106.336 150.858 1.00 88.70  ? 191  GLN A CA   1 
ATOM   5525 C C    . GLN B 1 191 ? 151.582 106.371 152.009 1.00 86.23  ? 191  GLN A C    1 
ATOM   5526 O O    . GLN B 1 191 ? 151.971 106.256 153.180 1.00 87.28  ? 191  GLN A O    1 
ATOM   5527 C CB   . GLN B 1 191 ? 152.881 107.765 150.407 1.00 91.16  ? 191  GLN A CB   1 
ATOM   5528 C CG   . GLN B 1 191 ? 152.830 108.818 151.510 1.00 88.87  ? 191  GLN A CG   1 
ATOM   5529 C CD   . GLN B 1 191 ? 154.112 108.887 152.315 1.00 88.30  ? 191  GLN A CD   1 
ATOM   5530 O OE1  . GLN B 1 191 ? 154.371 108.036 153.167 1.00 88.89  ? 191  GLN A OE1  1 
ATOM   5531 N NE2  . GLN B 1 191 ? 154.923 109.905 152.052 1.00 86.10  ? 191  GLN A NE2  1 
ATOM   5532 N N    . LYS B 1 192 ? 150.294 106.534 151.697 1.00 89.30  ? 192  LYS A N    1 
ATOM   5533 C CA   . LYS B 1 192 ? 149.285 106.531 152.755 1.00 93.29  ? 192  LYS A CA   1 
ATOM   5534 C C    . LYS B 1 192 ? 149.239 105.186 153.473 1.00 95.67  ? 192  LYS A C    1 
ATOM   5535 O O    . LYS B 1 192 ? 149.148 105.130 154.708 1.00 93.79  ? 192  LYS A O    1 
ATOM   5536 C CB   . LYS B 1 192 ? 147.913 106.886 152.185 1.00 95.86  ? 192  LYS A CB   1 
ATOM   5537 C CG   . LYS B 1 192 ? 146.965 107.486 153.214 1.00 96.00  ? 192  LYS A CG   1 
ATOM   5538 C CD   . LYS B 1 192 ? 145.768 108.147 152.556 1.00 93.96  ? 192  LYS A CD   1 
ATOM   5539 C CE   . LYS B 1 192 ? 146.198 109.290 151.653 1.00 93.91  ? 192  LYS A CE   1 
ATOM   5540 N NZ   . LYS B 1 192 ? 146.292 110.576 152.397 1.00 95.07  ? 192  LYS A NZ   1 
ATOM   5541 N N    . TRP B 1 193 ? 149.343 104.093 152.712 1.00 100.19 ? 193  TRP A N    1 
ATOM   5542 C CA   . TRP B 1 193 ? 149.392 102.758 153.304 1.00 98.53  ? 193  TRP A CA   1 
ATOM   5543 C C    . TRP B 1 193 ? 150.632 102.574 154.171 1.00 96.34  ? 193  TRP A C    1 
ATOM   5544 O O    . TRP B 1 193 ? 150.556 101.980 155.254 1.00 94.81  ? 193  TRP A O    1 
ATOM   5545 C CB   . TRP B 1 193 ? 149.343 101.697 152.205 1.00 97.95  ? 193  TRP A CB   1 
ATOM   5546 N N    . LYS B 1 194 ? 151.789 103.048 153.696 1.00 104.10 ? 194  LYS A N    1 
ATOM   5547 C CA   . LYS B 1 194 ? 153.017 102.900 154.470 1.00 104.11 ? 194  LYS A CA   1 
ATOM   5548 C C    . LYS B 1 194 ? 152.920 103.662 155.782 1.00 104.34 ? 194  LYS A C    1 
ATOM   5549 O O    . LYS B 1 194 ? 153.297 103.144 156.840 1.00 103.36 ? 194  LYS A O    1 
ATOM   5550 C CB   . LYS B 1 194 ? 154.217 103.381 153.654 1.00 104.88 ? 194  LYS A CB   1 
ATOM   5551 N N    . ASP B 1 195 ? 152.429 104.904 155.729 1.00 113.82 ? 195  ASP A N    1 
ATOM   5552 C CA   . ASP B 1 195 ? 152.325 105.702 156.945 1.00 115.48 ? 195  ASP A CA   1 
ATOM   5553 C C    . ASP B 1 195 ? 151.253 105.136 157.866 1.00 116.96 ? 195  ASP A C    1 
ATOM   5554 O O    . ASP B 1 195 ? 151.258 105.391 159.076 1.00 117.40 ? 195  ASP A O    1 
ATOM   5555 C CB   . ASP B 1 195 ? 152.026 107.160 156.597 1.00 112.97 ? 195  ASP A CB   1 
ATOM   5556 N N    . THR B 1 196 ? 150.324 104.357 157.303 1.00 117.72 ? 196  THR A N    1 
ATOM   5557 C CA   . THR B 1 196 ? 149.260 103.723 158.069 1.00 117.94 ? 196  THR A CA   1 
ATOM   5558 C C    . THR B 1 196 ? 149.701 102.460 158.799 1.00 118.35 ? 196  THR A C    1 
ATOM   5559 O O    . THR B 1 196 ? 148.832 101.774 159.352 1.00 117.75 ? 196  THR A O    1 
ATOM   5560 C CB   . THR B 1 196 ? 148.082 103.389 157.151 1.00 117.29 ? 196  THR A CB   1 
ATOM   5561 N N    . GLN B 1 197 ? 150.997 102.111 158.767 1.00 122.17 ? 197  GLN A N    1 
ATOM   5562 C CA   . GLN B 1 197 ? 151.539 100.960 159.491 1.00 121.02 ? 197  GLN A CA   1 
ATOM   5563 C C    . GLN B 1 197 ? 150.959 99.683  158.894 1.00 122.86 ? 197  GLN A C    1 
ATOM   5564 O O    . GLN B 1 197 ? 150.155 98.999  159.536 1.00 121.51 ? 197  GLN A O    1 
ATOM   5565 C CB   . GLN B 1 197 ? 151.278 101.047 161.001 1.00 120.76 ? 197  GLN A CB   1 
ATOM   5566 N N    . ASN B 1 198 ? 151.361 99.354  157.669 1.00 133.44 ? 198  ASN A N    1 
ATOM   5567 C CA   . ASN B 1 198 ? 150.810 98.203  156.967 1.00 132.59 ? 198  ASN A CA   1 
ATOM   5568 C C    . ASN B 1 198 ? 151.930 97.434  156.280 1.00 132.81 ? 198  ASN A C    1 
ATOM   5569 O O    . ASN B 1 198 ? 153.108 97.566  156.620 1.00 133.53 ? 198  ASN A O    1 
ATOM   5570 C CB   . ASN B 1 198 ? 149.745 98.631  155.952 1.00 130.69 ? 198  ASN A CB   1 
ATOM   5571 N N    . ALA B 1 199 ? 151.535 96.622  155.301 1.00 136.59 ? 199  ALA A N    1 
ATOM   5572 C CA   . ALA B 1 199 ? 152.446 95.766  154.553 1.00 137.07 ? 199  ALA A CA   1 
ATOM   5573 C C    . ALA B 1 199 ? 152.006 95.643  153.100 1.00 137.37 ? 199  ALA A C    1 
ATOM   5574 O O    . ALA B 1 199 ? 151.330 96.532  152.573 1.00 137.72 ? 199  ALA A O    1 
ATOM   5575 C CB   . ALA B 1 199 ? 152.538 94.383  155.200 1.00 136.54 ? 199  ALA A CB   1 
ATOM   5576 N N    . SER B 1 200 ? 152.382 94.546  152.445 1.00 130.28 ? 200  SER A N    1 
ATOM   5577 C CA   . SER B 1 200 ? 151.911 94.283  151.086 1.00 128.81 ? 200  SER A CA   1 
ATOM   5578 C C    . SER B 1 200 ? 150.542 93.624  151.037 1.00 130.57 ? 200  SER A C    1 
ATOM   5579 O O    . SER B 1 200 ? 150.226 92.917  150.070 1.00 130.54 ? 200  SER A O    1 
ATOM   5580 C CB   . SER B 1 200 ? 152.926 93.414  150.343 1.00 129.48 ? 200  SER A CB   1 
ATOM   5581 N N    . GLN B 1 201 ? 149.731 93.852  152.067 1.00 132.69 ? 201  GLN A N    1 
ATOM   5582 C CA   . GLN B 1 201 ? 148.451 93.174  152.185 1.00 131.54 ? 201  GLN A CA   1 
ATOM   5583 C C    . GLN B 1 201 ? 147.419 93.949  151.380 1.00 130.70 ? 201  GLN A C    1 
ATOM   5584 O O    . GLN B 1 201 ? 147.406 95.184  151.403 1.00 130.27 ? 201  GLN A O    1 
ATOM   5585 C CB   . GLN B 1 201 ? 148.025 93.073  153.650 1.00 130.21 ? 201  GLN A CB   1 
ATOM   5586 N N    . ASN B 1 202 ? 146.588 93.216  150.637 1.00 122.80 ? 202  ASN A N    1 
ATOM   5587 C CA   . ASN B 1 202 ? 145.536 93.783  149.792 1.00 122.01 ? 202  ASN A CA   1 
ATOM   5588 C C    . ASN B 1 202 ? 146.143 94.632  148.677 1.00 122.20 ? 202  ASN A C    1 
ATOM   5589 O O    . ASN B 1 202 ? 145.857 95.823  148.533 1.00 121.76 ? 202  ASN A O    1 
ATOM   5590 C CB   . ASN B 1 202 ? 144.512 94.578  150.607 1.00 122.77 ? 202  ASN A CB   1 
ATOM   5591 N N    . LYS B 1 203 ? 147.009 93.990  147.886 1.00 123.03 ? 203  LYS A N    1 
ATOM   5592 C CA   . LYS B 1 203 ? 147.701 94.644  146.778 1.00 123.11 ? 203  LYS A CA   1 
ATOM   5593 C C    . LYS B 1 203 ? 146.700 95.089  145.716 1.00 122.36 ? 203  LYS A C    1 
ATOM   5594 O O    . LYS B 1 203 ? 146.963 95.998  144.922 1.00 121.01 ? 203  LYS A O    1 
ATOM   5595 C CB   . LYS B 1 203 ? 148.750 93.700  146.188 1.00 121.00 ? 203  LYS A CB   1 
ATOM   5596 N N    . ILE B 1 204 ? 145.541 94.431  145.703 1.00 123.83 ? 204  ILE A N    1 
ATOM   5597 C CA   . ILE B 1 204 ? 144.450 94.744  144.782 1.00 124.80 ? 204  ILE A CA   1 
ATOM   5598 C C    . ILE B 1 204 ? 143.868 96.117  145.101 1.00 123.96 ? 204  ILE A C    1 
ATOM   5599 O O    . ILE B 1 204 ? 143.592 96.924  144.205 1.00 124.66 ? 204  ILE A O    1 
ATOM   5600 C CB   . ILE B 1 204 ? 143.371 93.648  144.840 1.00 124.13 ? 204  ILE A CB   1 
ATOM   5601 C CG1  . ILE B 1 204 ? 143.959 92.294  144.435 1.00 124.05 ? 204  ILE A CG1  1 
ATOM   5602 C CG2  . ILE B 1 204 ? 142.201 93.992  143.935 1.00 123.16 ? 204  ILE A CG2  1 
ATOM   5603 C CD1  . ILE B 1 204 ? 144.694 92.315  143.101 1.00 124.68 ? 204  ILE A CD1  1 
ATOM   5604 N N    . LYS B 1 205 ? 143.683 96.401  146.388 1.00 115.12 ? 205  LYS A N    1 
ATOM   5605 C CA   . LYS B 1 205 ? 143.000 97.606  146.841 1.00 115.30 ? 205  LYS A CA   1 
ATOM   5606 C C    . LYS B 1 205 ? 143.733 98.925  146.605 1.00 115.11 ? 205  LYS A C    1 
ATOM   5607 O O    . LYS B 1 205 ? 143.081 99.928  146.301 1.00 113.18 ? 205  LYS A O    1 
ATOM   5608 C CB   . LYS B 1 205 ? 142.725 97.440  148.341 1.00 117.79 ? 205  LYS A CB   1 
ATOM   5609 C CG   . LYS B 1 205 ? 142.608 98.731  149.140 1.00 119.76 ? 205  LYS A CG   1 
ATOM   5610 C CD   . LYS B 1 205 ? 142.245 98.482  150.594 1.00 117.46 ? 205  LYS A CD   1 
ATOM   5611 C CE   . LYS B 1 205 ? 140.924 97.745  150.712 1.00 116.38 ? 205  LYS A CE   1 
ATOM   5612 N NZ   . LYS B 1 205 ? 140.355 97.899  152.076 1.00 115.23 ? 205  LYS A NZ   1 
ATOM   5613 N N    . ILE B 1 206 ? 145.064 98.954  146.685 1.00 109.01 ? 206  ILE A N    1 
ATOM   5614 C CA   . ILE B 1 206 ? 145.766 100.194 146.353 1.00 109.81 ? 206  ILE A CA   1 
ATOM   5615 C C    . ILE B 1 206 ? 145.552 100.564 144.882 1.00 109.19 ? 206  ILE A C    1 
ATOM   5616 O O    . ILE B 1 206 ? 145.238 101.723 144.545 1.00 108.66 ? 206  ILE A O    1 
ATOM   5617 C CB   . ILE B 1 206 ? 147.264 100.094 146.723 1.00 109.08 ? 206  ILE A CB   1 
ATOM   5618 C CG1  . ILE B 1 206 ? 147.988 98.967  145.970 1.00 107.91 ? 206  ILE A CG1  1 
ATOM   5619 C CG2  . ILE B 1 206 ? 147.418 99.917  148.231 1.00 109.73 ? 206  ILE A CG2  1 
ATOM   5620 C CD1  . ILE B 1 206 ? 149.496 99.051  146.068 1.00 108.43 ? 206  ILE A CD1  1 
ATOM   5621 N N    . VAL B 1 207 ? 145.653 99.571  143.997 1.00 102.29 ? 207  VAL A N    1 
ATOM   5622 C CA   . VAL B 1 207 ? 145.373 99.763  142.580 1.00 100.76 ? 207  VAL A CA   1 
ATOM   5623 C C    . VAL B 1 207 ? 143.923 100.172 142.351 1.00 102.07 ? 207  VAL A C    1 
ATOM   5624 O O    . VAL B 1 207 ? 143.644 101.091 141.568 1.00 104.83 ? 207  VAL A O    1 
ATOM   5625 C CB   . VAL B 1 207 ? 145.734 98.486  141.796 1.00 99.54  ? 207  VAL A CB   1 
ATOM   5626 C CG1  . VAL B 1 207 ? 145.266 98.579  140.355 1.00 101.45 ? 207  VAL A CG1  1 
ATOM   5627 C CG2  . VAL B 1 207 ? 147.235 98.224  141.859 1.00 100.19 ? 207  VAL A CG2  1 
ATOM   5628 N N    . GLY B 1 208 ? 142.972 99.498  143.012 1.00 105.43 ? 208  GLY A N    1 
ATOM   5629 C CA   . GLY B 1 208 ? 141.589 99.898  142.820 1.00 107.66 ? 208  GLY A CA   1 
ATOM   5630 C C    . GLY B 1 208 ? 141.271 101.299 143.310 1.00 105.60 ? 208  GLY A C    1 
ATOM   5631 O O    . GLY B 1 208 ? 140.513 102.015 142.657 1.00 106.83 ? 208  GLY A O    1 
ATOM   5632 N N    . LEU B 1 209 ? 141.833 101.721 144.454 1.00 98.45  ? 209  LEU A N    1 
ATOM   5633 C CA   . LEU B 1 209 ? 141.547 103.092 144.883 1.00 100.94 ? 209  LEU A CA   1 
ATOM   5634 C C    . LEU B 1 209 ? 142.140 104.107 143.917 1.00 101.58 ? 209  LEU A C    1 
ATOM   5635 O O    . LEU B 1 209 ? 141.498 105.121 143.612 1.00 102.47 ? 209  LEU A O    1 
ATOM   5636 C CB   . LEU B 1 209 ? 141.936 103.398 146.335 1.00 102.60 ? 209  LEU A CB   1 
ATOM   5637 C CG   . LEU B 1 209 ? 141.159 102.851 147.557 1.00 102.71 ? 209  LEU A CG   1 
ATOM   5638 C CD1  . LEU B 1 209 ? 140.657 101.400 147.542 1.00 102.13 ? 209  LEU A CD1  1 
ATOM   5639 C CD2  . LEU B 1 209 ? 141.934 103.143 148.846 1.00 100.18 ? 209  LEU A CD2  1 
ATOM   5640 N N    . GLY B 1 210 ? 143.360 103.861 143.422 1.00 97.07  ? 210  GLY A N    1 
ATOM   5641 C CA   . GLY B 1 210 ? 143.921 104.797 142.461 1.00 97.86  ? 210  GLY A CA   1 
ATOM   5642 C C    . GLY B 1 210 ? 143.119 104.868 141.173 1.00 97.42  ? 210  GLY A C    1 
ATOM   5643 O O    . GLY B 1 210 ? 142.843 105.964 140.660 1.00 99.16  ? 210  GLY A O    1 
ATOM   5644 N N    . LEU B 1 211 ? 142.703 103.707 140.648 1.00 86.96  ? 211  LEU A N    1 
ATOM   5645 C CA   . LEU B 1 211 ? 141.919 103.720 139.417 1.00 87.86  ? 211  LEU A CA   1 
ATOM   5646 C C    . LEU B 1 211 ? 140.580 104.403 139.639 1.00 89.57  ? 211  LEU A C    1 
ATOM   5647 O O    . LEU B 1 211 ? 140.109 105.148 138.770 1.00 93.77  ? 211  LEU A O    1 
ATOM   5648 C CB   . LEU B 1 211 ? 141.724 102.303 138.869 1.00 87.79  ? 211  LEU A CB   1 
ATOM   5649 C CG   . LEU B 1 211 ? 142.763 101.736 137.889 1.00 86.26  ? 211  LEU A CG   1 
ATOM   5650 C CD1  . LEU B 1 211 ? 144.175 101.759 138.442 1.00 86.84  ? 211  LEU A CD1  1 
ATOM   5651 C CD2  . LEU B 1 211 ? 142.389 100.324 137.465 1.00 85.84  ? 211  LEU A CD2  1 
ATOM   5652 N N    . LEU B 1 212 ? 139.932 104.125 140.779 1.00 85.31  ? 212  LEU A N    1 
ATOM   5653 C CA   . LEU B 1 212 ? 138.631 104.721 141.049 1.00 84.78  ? 212  LEU A CA   1 
ATOM   5654 C C    . LEU B 1 212 ? 138.735 106.233 141.185 1.00 86.23  ? 212  LEU A C    1 
ATOM   5655 O O    . LEU B 1 212 ? 137.855 106.966 140.717 1.00 88.62  ? 212  LEU A O    1 
ATOM   5656 C CB   . LEU B 1 212 ? 138.041 104.101 142.314 1.00 86.81  ? 212  LEU A CB   1 
ATOM   5657 C CG   . LEU B 1 212 ? 136.609 104.474 142.686 1.00 85.95  ? 212  LEU A CG   1 
ATOM   5658 C CD1  . LEU B 1 212 ? 135.626 103.496 142.066 1.00 84.09  ? 212  LEU A CD1  1 
ATOM   5659 C CD2  . LEU B 1 212 ? 136.454 104.512 144.198 1.00 89.00  ? 212  LEU A CD2  1 
ATOM   5660 N N    . ARG B 1 213 ? 139.797 106.720 141.843 1.00 85.93  ? 213  ARG A N    1 
ATOM   5661 C CA   . ARG B 1 213 ? 139.946 108.162 141.991 1.00 88.18  ? 213  ARG A CA   1 
ATOM   5662 C C    . ARG B 1 213 ? 140.214 108.831 140.653 1.00 88.22  ? 213  ARG A C    1 
ATOM   5663 O O    . ARG B 1 213 ? 139.773 109.963 140.427 1.00 89.04  ? 213  ARG A O    1 
ATOM   5664 C CB   . ARG B 1 213 ? 141.058 108.490 142.989 1.00 86.36  ? 213  ARG A CB   1 
ATOM   5665 C CG   . ARG B 1 213 ? 140.964 109.901 143.555 1.00 87.93  ? 213  ARG A CG   1 
ATOM   5666 C CD   . ARG B 1 213 ? 142.178 110.265 144.394 1.00 88.28  ? 213  ARG A CD   1 
ATOM   5667 N NE   . ARG B 1 213 ? 142.465 109.258 145.408 1.00 90.25  ? 213  ARG A NE   1 
ATOM   5668 C CZ   . ARG B 1 213 ? 141.971 109.280 146.638 1.00 89.43  ? 213  ARG A CZ   1 
ATOM   5669 N NH1  . ARG B 1 213 ? 141.163 110.247 147.041 1.00 87.64  ? 213  ARG A NH1  1 
ATOM   5670 N NH2  . ARG B 1 213 ? 142.297 108.310 147.486 1.00 90.29  ? 213  ARG A NH2  1 
ATOM   5671 N N    . VAL B 1 214 ? 140.943 108.152 139.764 1.00 82.94  ? 214  VAL A N    1 
ATOM   5672 C CA   . VAL B 1 214 ? 141.179 108.704 138.433 1.00 84.96  ? 214  VAL A CA   1 
ATOM   5673 C C    . VAL B 1 214 ? 139.892 108.741 137.612 1.00 87.10  ? 214  VAL A C    1 
ATOM   5674 O O    . VAL B 1 214 ? 139.584 109.741 136.950 1.00 88.83  ? 214  VAL A O    1 
ATOM   5675 C CB   . VAL B 1 214 ? 142.285 107.898 137.729 1.00 83.78  ? 214  VAL A CB   1 
ATOM   5676 C CG1  . VAL B 1 214 ? 142.305 108.187 136.239 1.00 87.23  ? 214  VAL A CG1  1 
ATOM   5677 C CG2  . VAL B 1 214 ? 143.634 108.206 138.354 1.00 84.13  ? 214  VAL A CG2  1 
ATOM   5678 N N    . LEU B 1 215 ? 139.120 107.652 137.655 1.00 80.64  ? 215  LEU A N    1 
ATOM   5679 C CA   . LEU B 1 215 ? 137.867 107.558 136.907 1.00 78.73  ? 215  LEU A CA   1 
ATOM   5680 C C    . LEU B 1 215 ? 136.798 108.544 137.382 1.00 79.95  ? 215  LEU A C    1 
ATOM   5681 O O    . LEU B 1 215 ? 136.062 109.102 136.559 1.00 83.41  ? 215  LEU A O    1 
ATOM   5682 C CB   . LEU B 1 215 ? 137.351 106.115 136.970 1.00 80.29  ? 215  LEU A CB   1 
ATOM   5683 C CG   . LEU B 1 215 ? 136.393 105.547 135.910 1.00 83.22  ? 215  LEU A CG   1 
ATOM   5684 C CD1  . LEU B 1 215 ? 136.397 104.027 135.985 1.00 79.86  ? 215  LEU A CD1  1 
ATOM   5685 C CD2  . LEU B 1 215 ? 134.960 106.054 136.040 1.00 82.14  ? 215  LEU A CD2  1 
ATOM   5686 N N    . GLN B 1 216 ? 136.690 108.781 138.691 1.00 71.59  ? 216  GLN A N    1 
ATOM   5687 C CA   . GLN B 1 216 ? 135.657 109.710 139.145 1.00 71.10  ? 216  GLN A CA   1 
ATOM   5688 C C    . GLN B 1 216 ? 135.904 111.180 138.814 1.00 67.00  ? 216  GLN A C    1 
ATOM   5689 O O    . GLN B 1 216 ? 134.994 111.981 139.038 1.00 65.04  ? 216  GLN A O    1 
ATOM   5690 C CB   . GLN B 1 216 ? 135.455 109.568 140.655 1.00 73.49  ? 216  GLN A CB   1 
ATOM   5691 C CG   . GLN B 1 216 ? 134.769 108.280 141.082 1.00 75.99  ? 216  GLN A CG   1 
ATOM   5692 C CD   . GLN B 1 216 ? 134.622 108.184 142.586 1.00 77.75  ? 216  GLN A CD   1 
ATOM   5693 O OE1  . GLN B 1 216 ? 134.692 109.190 143.290 1.00 75.43  ? 216  GLN A OE1  1 
ATOM   5694 N NE2  . GLN B 1 216 ? 134.391 106.976 143.084 1.00 76.47  ? 216  GLN A NE2  1 
ATOM   5695 N N    . ASN B 1 217 ? 137.081 111.566 138.328 1.00 67.42  ? 217  ASN A N    1 
ATOM   5696 C CA   . ASN B 1 217 ? 137.297 112.956 137.903 1.00 70.69  ? 217  ASN A CA   1 
ATOM   5697 C C    . ASN B 1 217 ? 136.425 113.310 136.700 1.00 68.46  ? 217  ASN A C    1 
ATOM   5698 O O    . ASN B 1 217 ? 136.399 112.554 135.724 1.00 65.88  ? 217  ASN A O    1 
ATOM   5699 C CB   . ASN B 1 217 ? 138.765 113.204 137.565 1.00 67.34  ? 217  ASN A CB   1 
ATOM   5700 C CG   . ASN B 1 217 ? 139.166 114.652 137.770 1.00 66.34  ? 217  ASN A CG   1 
ATOM   5701 O OD1  . ASN B 1 217 ? 138.386 115.453 138.279 1.00 66.59  ? 217  ASN A OD1  1 
ATOM   5702 N ND2  . ASN B 1 217 ? 140.390 114.994 137.378 1.00 69.14  ? 217  ASN A ND2  1 
ATOM   5703 N N    . PRO B 1 218 ? 135.689 114.443 136.724 1.00 66.12  ? 218  PRO A N    1 
ATOM   5704 C CA   . PRO B 1 218 ? 134.814 114.779 135.587 1.00 61.62  ? 218  PRO A CA   1 
ATOM   5705 C C    . PRO B 1 218 ? 135.539 115.034 134.266 1.00 67.18  ? 218  PRO A C    1 
ATOM   5706 O O    . PRO B 1 218 ? 135.212 116.011 133.590 1.00 70.09  ? 218  PRO A O    1 
ATOM   5707 C CB   . PRO B 1 218 ? 134.159 116.094 136.055 1.00 62.86  ? 218  PRO A CB   1 
ATOM   5708 C CG   . PRO B 1 218 ? 134.508 116.220 137.554 1.00 65.83  ? 218  PRO A CG   1 
ATOM   5709 C CD   . PRO B 1 218 ? 135.011 114.878 137.943 1.00 68.90  ? 218  PRO A CD   1 
ATOM   5710 N N    . ILE B 1 219 ? 136.514 114.213 133.877 1.00 65.55  ? 219  ILE A N    1 
ATOM   5711 C CA   . ILE B 1 219 ? 137.205 114.385 132.600 1.00 60.55  ? 219  ILE A CA   1 
ATOM   5712 C C    . ILE B 1 219 ? 137.234 113.054 131.862 1.00 68.12  ? 219  ILE A C    1 
ATOM   5713 O O    . ILE B 1 219 ? 136.879 112.964 130.678 1.00 66.31  ? 219  ILE A O    1 
ATOM   5714 C CB   . ILE B 1 219 ? 138.624 114.946 132.795 1.00 56.58  ? 219  ILE A CB   1 
ATOM   5715 C CG1  . ILE B 1 219 ? 138.568 116.353 133.401 1.00 58.92  ? 219  ILE A CG1  1 
ATOM   5716 C CG2  . ILE B 1 219 ? 139.374 114.962 131.476 1.00 55.43  ? 219  ILE A CG2  1 
ATOM   5717 C CD1  . ILE B 1 219 ? 139.916 116.916 133.783 1.00 64.69  ? 219  ILE A CD1  1 
ATOM   5718 N N    . VAL B 1 220 ? 137.587 112.002 132.601 1.00 80.98  ? 220  VAL A N    1 
ATOM   5719 C CA   . VAL B 1 220 ? 137.724 110.670 132.030 1.00 78.18  ? 220  VAL A CA   1 
ATOM   5720 C C    . VAL B 1 220 ? 136.360 110.134 131.634 1.00 73.26  ? 220  VAL A C    1 
ATOM   5721 O O    . VAL B 1 220 ? 136.207 109.505 130.578 1.00 71.28  ? 220  VAL A O    1 
ATOM   5722 C CB   . VAL B 1 220 ? 138.443 109.744 133.026 1.00 73.55  ? 220  VAL A CB   1 
ATOM   5723 C CG1  . VAL B 1 220 ? 138.704 108.385 132.400 1.00 72.58  ? 220  VAL A CG1  1 
ATOM   5724 C CG2  . VAL B 1 220 ? 139.740 110.380 133.496 1.00 67.04  ? 220  VAL A CG2  1 
ATOM   5725 N N    . PHE B 1 221 ? 135.357 110.328 132.491 1.00 68.83  ? 221  PHE A N    1 
ATOM   5726 C CA   . PHE B 1 221 ? 134.048 109.768 132.198 1.00 69.20  ? 221  PHE A CA   1 
ATOM   5727 C C    . PHE B 1 221 ? 133.470 110.409 130.943 1.00 76.93  ? 221  PHE A C    1 
ATOM   5728 O O    . PHE B 1 221 ? 132.914 109.712 130.083 1.00 81.21  ? 221  PHE A O    1 
ATOM   5729 C CB   . PHE B 1 221 ? 133.120 109.971 133.395 1.00 67.10  ? 221  PHE A CB   1 
ATOM   5730 C CG   . PHE B 1 221 ? 131.765 109.349 133.230 1.00 77.47  ? 221  PHE A CG   1 
ATOM   5731 C CD1  . PHE B 1 221 ? 131.619 107.972 133.205 1.00 80.29  ? 221  PHE A CD1  1 
ATOM   5732 C CD2  . PHE B 1 221 ? 130.636 110.142 133.109 1.00 78.57  ? 221  PHE A CD2  1 
ATOM   5733 C CE1  . PHE B 1 221 ? 130.371 107.395 133.056 1.00 77.59  ? 221  PHE A CE1  1 
ATOM   5734 C CE2  . PHE B 1 221 ? 129.385 109.572 132.960 1.00 79.71  ? 221  PHE A CE2  1 
ATOM   5735 C CZ   . PHE B 1 221 ? 129.252 108.197 132.933 1.00 78.78  ? 221  PHE A CZ   1 
ATOM   5736 N N    . MET B 1 222 ? 133.656 111.725 130.775 1.00 58.94  ? 222  MET A N    1 
ATOM   5737 C CA   . MET B 1 222 ? 133.079 112.345 129.592 1.00 56.55  ? 222  MET A CA   1 
ATOM   5738 C C    . MET B 1 222 ? 133.936 112.127 128.352 1.00 53.08  ? 222  MET A C    1 
ATOM   5739 O O    . MET B 1 222 ? 133.393 112.143 127.241 1.00 52.36  ? 222  MET A O    1 
ATOM   5740 C CB   . MET B 1 222 ? 132.880 113.844 129.823 1.00 50.92  ? 222  MET A CB   1 
ATOM   5741 C CG   . MET B 1 222 ? 131.981 114.174 131.000 1.00 56.67  ? 222  MET A CG   1 
ATOM   5742 S SD   . MET B 1 222 ? 130.371 113.375 130.893 1.00 65.51  ? 222  MET A SD   1 
ATOM   5743 C CE   . MET B 1 222 ? 129.510 114.505 129.803 1.00 61.59  ? 222  MET A CE   1 
ATOM   5744 N N    . VAL B 1 223 ? 135.213 111.762 128.512 1.00 51.54  ? 223  VAL A N    1 
ATOM   5745 C CA   . VAL B 1 223 ? 135.998 111.416 127.330 1.00 54.78  ? 223  VAL A CA   1 
ATOM   5746 C C    . VAL B 1 223 ? 135.580 110.032 126.842 1.00 52.67  ? 223  VAL A C    1 
ATOM   5747 O O    . VAL B 1 223 ? 135.435 109.803 125.633 1.00 52.50  ? 223  VAL A O    1 
ATOM   5748 C CB   . VAL B 1 223 ? 137.523 111.565 127.563 1.00 56.42  ? 223  VAL A CB   1 
ATOM   5749 C CG1  . VAL B 1 223 ? 138.161 110.407 128.316 1.00 53.39  ? 223  VAL A CG1  1 
ATOM   5750 C CG2  . VAL B 1 223 ? 138.238 111.786 126.235 1.00 54.18  ? 223  VAL A CG2  1 
ATOM   5751 N N    . PHE B 1 224 ? 135.370 109.096 127.779 1.00 50.63  ? 224  PHE A N    1 
ATOM   5752 C CA   . PHE B 1 224 ? 134.901 107.762 127.422 1.00 47.80  ? 224  PHE A CA   1 
ATOM   5753 C C    . PHE B 1 224 ? 133.527 107.828 126.772 1.00 52.96  ? 224  PHE A C    1 
ATOM   5754 O O    . PHE B 1 224 ? 133.277 107.155 125.763 1.00 55.26  ? 224  PHE A O    1 
ATOM   5755 C CB   . PHE B 1 224 ? 134.835 106.870 128.663 1.00 50.88  ? 224  PHE A CB   1 
ATOM   5756 C CG   . PHE B 1 224 ? 136.110 106.147 128.970 1.00 53.76  ? 224  PHE A CG   1 
ATOM   5757 C CD1  . PHE B 1 224 ? 137.260 106.840 129.294 1.00 56.66  ? 224  PHE A CD1  1 
ATOM   5758 C CD2  . PHE B 1 224 ? 136.151 104.763 128.946 1.00 55.76  ? 224  PHE A CD2  1 
ATOM   5759 C CE1  . PHE B 1 224 ? 138.426 106.166 129.583 1.00 59.42  ? 224  PHE A CE1  1 
ATOM   5760 C CE2  . PHE B 1 224 ? 137.317 104.085 129.232 1.00 55.25  ? 224  PHE A CE2  1 
ATOM   5761 C CZ   . PHE B 1 224 ? 138.457 104.788 129.551 1.00 56.53  ? 224  PHE A CZ   1 
ATOM   5762 N N    . ILE B 1 225 ? 132.623 108.636 127.338 1.00 60.80  ? 225  ILE A N    1 
ATOM   5763 C CA   . ILE B 1 225 ? 131.291 108.768 126.756 1.00 61.11  ? 225  ILE A CA   1 
ATOM   5764 C C    . ILE B 1 225 ? 131.371 109.374 125.358 1.00 58.75  ? 225  ILE A C    1 
ATOM   5765 O O    . ILE B 1 225 ? 130.680 108.921 124.435 1.00 60.96  ? 225  ILE A O    1 
ATOM   5766 C CB   . ILE B 1 225 ? 130.386 109.595 127.691 1.00 54.26  ? 225  ILE A CB   1 
ATOM   5767 C CG1  . ILE B 1 225 ? 130.036 108.791 128.944 1.00 51.87  ? 225  ILE A CG1  1 
ATOM   5768 C CG2  . ILE B 1 225 ? 129.113 110.029 126.987 1.00 53.58  ? 225  ILE A CG2  1 
ATOM   5769 C CD1  . ILE B 1 225 ? 129.536 107.393 128.658 1.00 56.66  ? 225  ILE A CD1  1 
ATOM   5770 N N    . GLY B 1 226 ? 132.193 110.417 125.178 1.00 56.35  ? 226  GLY A N    1 
ATOM   5771 C CA   . GLY B 1 226 ? 132.324 111.009 123.855 1.00 55.11  ? 226  GLY A CA   1 
ATOM   5772 C C    . GLY B 1 226 ? 132.875 110.050 122.815 1.00 57.84  ? 226  GLY A C    1 
ATOM   5773 O O    . GLY B 1 226 ? 132.384 110.000 121.683 1.00 61.58  ? 226  GLY A O    1 
ATOM   5774 N N    . ILE B 1 227 ? 133.862 109.233 123.201 1.00 58.60  ? 227  ILE A N    1 
ATOM   5775 C CA   . ILE B 1 227 ? 134.405 108.258 122.258 1.00 57.80  ? 227  ILE A CA   1 
ATOM   5776 C C    . ILE B 1 227 ? 133.366 107.194 121.920 1.00 56.86  ? 227  ILE A C    1 
ATOM   5777 O O    . ILE B 1 227 ? 133.231 106.789 120.757 1.00 55.70  ? 227  ILE A O    1 
ATOM   5778 C CB   . ILE B 1 227 ? 135.697 107.637 122.825 1.00 56.19  ? 227  ILE A CB   1 
ATOM   5779 C CG1  . ILE B 1 227 ? 136.815 108.677 122.870 1.00 51.60  ? 227  ILE A CG1  1 
ATOM   5780 C CG2  . ILE B 1 227 ? 136.144 106.442 121.997 1.00 57.87  ? 227  ILE A CG2  1 
ATOM   5781 C CD1  . ILE B 1 227 ? 137.998 108.260 123.714 1.00 51.59  ? 227  ILE A CD1  1 
ATOM   5782 N N    . ALA B 1 228 ? 132.617 106.726 122.924 1.00 58.78  ? 228  ALA A N    1 
ATOM   5783 C CA   . ALA B 1 228 ? 131.588 105.718 122.681 1.00 56.42  ? 228  ALA A CA   1 
ATOM   5784 C C    . ALA B 1 228 ? 130.501 106.241 121.748 1.00 58.38  ? 228  ALA A C    1 
ATOM   5785 O O    . ALA B 1 228 ? 130.120 105.580 120.769 1.00 63.89  ? 228  ALA A O    1 
ATOM   5786 C CB   . ALA B 1 228 ? 130.985 105.258 124.008 1.00 58.05  ? 228  ALA A CB   1 
ATOM   5787 N N    . PHE B 1 229 ? 130.037 107.469 121.997 1.00 67.79  ? 229  PHE A N    1 
ATOM   5788 C CA   . PHE B 1 229 ? 129.006 108.031 121.140 1.00 73.05  ? 229  PHE A CA   1 
ATOM   5789 C C    . PHE B 1 229 ? 129.532 108.446 119.777 1.00 76.54  ? 229  PHE A C    1 
ATOM   5790 O O    . PHE B 1 229 ? 128.721 108.689 118.877 1.00 80.05  ? 229  PHE A O    1 
ATOM   5791 C CB   . PHE B 1 229 ? 128.356 109.231 121.831 1.00 73.55  ? 229  PHE A CB   1 
ATOM   5792 C CG   . PHE B 1 229 ? 127.214 108.864 122.735 1.00 78.40  ? 229  PHE A CG   1 
ATOM   5793 C CD1  . PHE B 1 229 ? 127.443 108.177 123.916 1.00 78.49  ? 229  PHE A CD1  1 
ATOM   5794 C CD2  . PHE B 1 229 ? 125.915 109.217 122.411 1.00 77.39  ? 229  PHE A CD2  1 
ATOM   5795 C CE1  . PHE B 1 229 ? 126.396 107.839 124.753 1.00 74.23  ? 229  PHE A CE1  1 
ATOM   5796 C CE2  . PHE B 1 229 ? 124.863 108.884 123.245 1.00 77.12  ? 229  PHE A CE2  1 
ATOM   5797 C CZ   . PHE B 1 229 ? 125.105 108.194 124.417 1.00 75.71  ? 229  PHE A CZ   1 
ATOM   5798 N N    . ASN B 1 230 ? 130.853 108.571 119.604 1.00 70.14  ? 230  ASN A N    1 
ATOM   5799 C CA   . ASN B 1 230 ? 131.343 108.883 118.267 1.00 68.38  ? 230  ASN A CA   1 
ATOM   5800 C C    . ASN B 1 230 ? 131.027 107.744 117.305 1.00 66.78  ? 230  ASN A C    1 
ATOM   5801 O O    . ASN B 1 230 ? 130.582 107.979 116.176 1.00 65.66  ? 230  ASN A O    1 
ATOM   5802 C CB   . ASN B 1 230 ? 132.844 109.161 118.295 1.00 70.60  ? 230  ASN A CB   1 
ATOM   5803 C CG   . ASN B 1 230 ? 133.369 109.613 116.950 1.00 73.49  ? 230  ASN A CG   1 
ATOM   5804 O OD1  . ASN B 1 230 ? 132.615 110.118 116.121 1.00 78.44  ? 230  ASN A OD1  1 
ATOM   5805 N ND2  . ASN B 1 230 ? 134.663 109.432 116.724 1.00 69.63  ? 230  ASN A ND2  1 
ATOM   5806 N N    . PHE B 1 231 ? 131.257 106.502 117.739 1.00 76.08  ? 231  PHE A N    1 
ATOM   5807 C CA   . PHE B 1 231 ? 130.958 105.352 116.898 1.00 75.69  ? 231  PHE A CA   1 
ATOM   5808 C C    . PHE B 1 231 ? 129.479 105.002 116.919 1.00 77.68  ? 231  PHE A C    1 
ATOM   5809 O O    . PHE B 1 231 ? 128.940 104.554 115.901 1.00 77.11  ? 231  PHE A O    1 
ATOM   5810 C CB   . PHE B 1 231 ? 131.777 104.135 117.334 1.00 78.16  ? 231  PHE A CB   1 
ATOM   5811 C CG   . PHE B 1 231 ? 133.260 104.310 117.178 1.00 81.61  ? 231  PHE A CG   1 
ATOM   5812 C CD1  . PHE B 1 231 ? 133.826 104.469 115.923 1.00 79.57  ? 231  PHE A CD1  1 
ATOM   5813 C CD2  . PHE B 1 231 ? 134.091 104.297 118.287 1.00 79.69  ? 231  PHE A CD2  1 
ATOM   5814 C CE1  . PHE B 1 231 ? 135.193 104.625 115.779 1.00 79.78  ? 231  PHE A CE1  1 
ATOM   5815 C CE2  . PHE B 1 231 ? 135.457 104.452 118.149 1.00 76.84  ? 231  PHE A CE2  1 
ATOM   5816 C CZ   . PHE B 1 231 ? 136.008 104.615 116.894 1.00 78.40  ? 231  PHE A CZ   1 
ATOM   5817 N N    . ILE B 1 232 ? 128.811 105.188 118.063 1.00 83.12  ? 232  ILE A N    1 
ATOM   5818 C CA   . ILE B 1 232 ? 127.411 104.781 118.165 1.00 81.00  ? 232  ILE A CA   1 
ATOM   5819 C C    . ILE B 1 232 ? 126.514 105.664 117.303 1.00 80.29  ? 232  ILE A C    1 
ATOM   5820 O O    . ILE B 1 232 ? 125.668 105.167 116.550 1.00 84.55  ? 232  ILE A O    1 
ATOM   5821 C CB   . ILE B 1 232 ? 126.955 104.770 119.636 1.00 77.57  ? 232  ILE A CB   1 
ATOM   5822 C CG1  . ILE B 1 232 ? 127.648 103.634 120.394 1.00 81.81  ? 232  ILE A CG1  1 
ATOM   5823 C CG2  . ILE B 1 232 ? 125.438 104.658 119.731 1.00 79.10  ? 232  ILE A CG2  1 
ATOM   5824 C CD1  . ILE B 1 232 ? 126.993 103.269 121.708 1.00 82.79  ? 232  ILE A CD1  1 
ATOM   5825 N N    . LEU B 1 233 ? 126.697 106.980 117.377 1.00 75.33  ? 233  LEU A N    1 
ATOM   5826 C CA   . LEU B 1 233 ? 125.798 107.906 116.701 1.00 78.82  ? 233  LEU A CA   1 
ATOM   5827 C C    . LEU B 1 233 ? 126.263 108.269 115.282 1.00 77.54  ? 233  LEU A C    1 
ATOM   5828 O O    . LEU B 1 233 ? 125.562 109.001 114.576 1.00 77.78  ? 233  LEU A O    1 
ATOM   5829 C CB   . LEU B 1 233 ? 125.607 109.124 117.618 1.00 80.36  ? 233  LEU A CB   1 
ATOM   5830 C CG   . LEU B 1 233 ? 125.289 110.577 117.314 1.00 78.93  ? 233  LEU A CG   1 
ATOM   5831 C CD1  . LEU B 1 233 ? 123.905 110.664 116.671 1.00 79.29  ? 233  LEU A CD1  1 
ATOM   5832 C CD2  . LEU B 1 233 ? 125.353 111.405 118.581 1.00 75.44  ? 233  LEU A CD2  1 
ATOM   5833 N N    . ASP B 1 234 ? 127.400 107.724 114.841 1.00 78.41  ? 234  ASP A N    1 
ATOM   5834 C CA   . ASP B 1 234 ? 128.029 107.944 113.529 1.00 84.34  ? 234  ASP A CA   1 
ATOM   5835 C C    . ASP B 1 234 ? 128.336 109.437 113.300 1.00 83.79  ? 234  ASP A C    1 
ATOM   5836 O O    . ASP B 1 234 ? 127.656 110.157 112.564 1.00 81.88  ? 234  ASP A O    1 
ATOM   5837 C CB   . ASP B 1 234 ? 127.148 107.268 112.446 1.00 82.00  ? 234  ASP A CB   1 
ATOM   5838 C CG   . ASP B 1 234 ? 127.391 107.732 110.975 1.00 82.61  ? 234  ASP A CG   1 
ATOM   5839 O OD1  . ASP B 1 234 ? 128.286 108.529 110.622 1.00 79.28  ? 234  ASP A OD1  1 
ATOM   5840 O OD2  . ASP B 1 234 ? 126.615 107.252 110.123 1.00 84.53  ? 234  ASP A OD2  1 
ATOM   5841 N N    . ARG B 1 235 ? 129.275 109.920 114.118 1.00 77.55  ? 235  ARG A N    1 
ATOM   5842 C CA   . ARG B 1 235 ? 129.972 111.212 113.960 1.00 73.02  ? 235  ARG A CA   1 
ATOM   5843 C C    . ARG B 1 235 ? 129.089 112.447 113.734 1.00 73.76  ? 235  ARG A C    1 
ATOM   5844 O O    . ARG B 1 235 ? 129.582 113.455 113.221 1.00 77.47  ? 235  ARG A O    1 
ATOM   5845 C CB   . ARG B 1 235 ? 130.996 111.129 112.820 1.00 70.91  ? 235  ARG A CB   1 
ATOM   5846 C CG   . ARG B 1 235 ? 132.419 111.471 113.228 1.00 69.34  ? 235  ARG A CG   1 
ATOM   5847 C CD   . ARG B 1 235 ? 133.321 111.678 112.022 1.00 70.98  ? 235  ARG A CD   1 
ATOM   5848 N NE   . ARG B 1 235 ? 133.004 110.777 110.921 1.00 77.97  ? 235  ARG A NE   1 
ATOM   5849 C CZ   . ARG B 1 235 ? 133.539 109.575 110.759 1.00 79.25  ? 235  ARG A CZ   1 
ATOM   5850 N NH1  . ARG B 1 235 ? 134.414 109.086 111.623 1.00 76.42  ? 235  ARG A NH1  1 
ATOM   5851 N NH2  . ARG B 1 235 ? 133.188 108.845 109.705 1.00 78.22  ? 235  ARG A NH2  1 
ATOM   5852 N N    . LYS B 1 236 ? 127.805 112.454 114.078 1.00 78.00  ? 236  LYS A N    1 
ATOM   5853 C CA   . LYS B 1 236 ? 126.988 113.638 113.816 1.00 80.40  ? 236  LYS A CA   1 
ATOM   5854 C C    . LYS B 1 236 ? 126.227 113.981 115.085 1.00 81.45  ? 236  LYS A C    1 
ATOM   5855 O O    . LYS B 1 236 ? 125.464 113.157 115.586 1.00 84.15  ? 236  LYS A O    1 
ATOM   5856 C CB   . LYS B 1 236 ? 126.027 113.402 112.648 1.00 82.23  ? 236  LYS A CB   1 
ATOM   5857 C CG   . LYS B 1 236 ? 125.384 114.672 112.101 1.00 79.93  ? 236  LYS A CG   1 
ATOM   5858 C CD   . LYS B 1 236 ? 125.317 114.680 110.572 1.00 82.35  ? 236  LYS A CD   1 
ATOM   5859 C CE   . LYS B 1 236 ? 125.201 113.279 109.982 1.00 82.16  ? 236  LYS A CE   1 
ATOM   5860 N NZ   . LYS B 1 236 ? 125.141 113.310 108.495 1.00 81.02  ? 236  LYS A NZ   1 
ATOM   5861 N N    . VAL B 1 237 ? 126.379 115.211 115.565 1.00 72.41  ? 237  VAL A N    1 
ATOM   5862 C CA   . VAL B 1 237 ? 125.663 115.643 116.765 1.00 72.62  ? 237  VAL A CA   1 
ATOM   5863 C C    . VAL B 1 237 ? 124.189 115.935 116.486 1.00 76.14  ? 237  VAL A C    1 
ATOM   5864 O O    . VAL B 1 237 ? 123.841 116.449 115.410 1.00 77.42  ? 237  VAL A O    1 
ATOM   5865 C CB   . VAL B 1 237 ? 126.390 116.853 117.393 1.00 69.51  ? 237  VAL A CB   1 
ATOM   5866 C CG1  . VAL B 1 237 ? 126.047 118.168 116.698 1.00 74.07  ? 237  VAL A CG1  1 
ATOM   5867 C CG2  . VAL B 1 237 ? 126.144 116.955 118.895 1.00 66.12  ? 237  VAL A CG2  1 
ATOM   5868 N N    . PRO B 1 238 ? 123.286 115.530 117.384 1.00 74.87  ? 238  PRO A N    1 
ATOM   5869 C CA   . PRO B 1 238 ? 121.860 115.840 117.212 1.00 71.11  ? 238  PRO A CA   1 
ATOM   5870 C C    . PRO B 1 238 ? 121.596 117.341 117.204 1.00 69.77  ? 238  PRO A C    1 
ATOM   5871 O O    . PRO B 1 238 ? 122.285 118.115 117.872 1.00 71.96  ? 238  PRO A O    1 
ATOM   5872 C CB   . PRO B 1 238 ? 121.194 115.145 118.406 1.00 67.78  ? 238  PRO A CB   1 
ATOM   5873 C CG   . PRO B 1 238 ? 122.155 114.077 118.794 1.00 65.89  ? 238  PRO A CG   1 
ATOM   5874 C CD   . PRO B 1 238 ? 123.513 114.626 118.524 1.00 69.60  ? 238  PRO A CD   1 
ATOM   5875 N N    . VAL B 1 239 ? 120.595 117.745 116.417 1.00 61.69  ? 239  VAL A N    1 
ATOM   5876 C CA   . VAL B 1 239 ? 120.295 119.165 116.230 1.00 65.86  ? 239  VAL A CA   1 
ATOM   5877 C C    . VAL B 1 239 ? 119.878 119.824 117.545 1.00 69.51  ? 239  VAL A C    1 
ATOM   5878 O O    . VAL B 1 239 ? 120.273 120.958 117.838 1.00 65.08  ? 239  VAL A O    1 
ATOM   5879 C CB   . VAL B 1 239 ? 119.216 119.339 115.144 1.00 66.71  ? 239  VAL A CB   1 
ATOM   5880 C CG1  . VAL B 1 239 ? 118.947 120.814 114.884 1.00 63.43  ? 239  VAL A CG1  1 
ATOM   5881 C CG2  . VAL B 1 239 ? 119.634 118.632 113.865 1.00 65.64  ? 239  VAL A CG2  1 
ATOM   5882 N N    . TYR B 1 240 ? 119.034 119.153 118.332 1.00 71.69  ? 240  TYR A N    1 
ATOM   5883 C CA   . TYR B 1 240 ? 118.573 119.732 119.595 1.00 71.06  ? 240  TYR A CA   1 
ATOM   5884 C C    . TYR B 1 240 ? 119.692 119.955 120.612 1.00 70.32  ? 240  TYR A C    1 
ATOM   5885 O O    . TYR B 1 240 ? 119.563 120.828 121.478 1.00 66.68  ? 240  TYR A O    1 
ATOM   5886 C CB   . TYR B 1 240 ? 117.457 118.883 120.211 1.00 71.65  ? 240  TYR A CB   1 
ATOM   5887 C CG   . TYR B 1 240 ? 116.229 118.706 119.341 1.00 67.20  ? 240  TYR A CG   1 
ATOM   5888 C CD1  . TYR B 1 240 ? 115.320 117.687 119.592 1.00 68.59  ? 240  TYR A CD1  1 
ATOM   5889 C CD2  . TYR B 1 240 ? 115.938 119.602 118.318 1.00 64.57  ? 240  TYR A CD2  1 
ATOM   5890 C CE1  . TYR B 1 240 ? 114.185 117.535 118.816 1.00 73.77  ? 240  TYR A CE1  1 
ATOM   5891 C CE2  . TYR B 1 240 ? 114.808 119.457 117.538 1.00 68.99  ? 240  TYR A CE2  1 
ATOM   5892 C CZ   . TYR B 1 240 ? 113.934 118.424 117.792 1.00 73.66  ? 240  TYR A CZ   1 
ATOM   5893 O OH   . TYR B 1 240 ? 112.807 118.278 117.018 1.00 72.62  ? 240  TYR A OH   1 
ATOM   5894 N N    . VAL B 1 241 ? 120.788 119.194 120.544 1.00 57.13  ? 241  VAL A N    1 
ATOM   5895 C CA   . VAL B 1 241 ? 121.826 119.305 121.571 1.00 54.79  ? 241  VAL A CA   1 
ATOM   5896 C C    . VAL B 1 241 ? 123.073 120.065 121.128 1.00 51.88  ? 241  VAL A C    1 
ATOM   5897 O O    . VAL B 1 241 ? 123.929 120.357 121.983 1.00 48.36  ? 241  VAL A O    1 
ATOM   5898 C CB   . VAL B 1 241 ? 122.241 117.914 122.093 1.00 53.36  ? 241  VAL A CB   1 
ATOM   5899 C CG1  . VAL B 1 241 ? 121.022 117.137 122.565 1.00 52.40  ? 241  VAL A CG1  1 
ATOM   5900 C CG2  . VAL B 1 241 ? 122.996 117.157 121.029 1.00 55.63  ? 241  VAL A CG2  1 
ATOM   5901 N N    . GLU B 1 242 ? 123.200 120.415 119.843 1.00 47.04  ? 242  GLU A N    1 
ATOM   5902 C CA   . GLU B 1 242 ? 124.410 121.098 119.382 1.00 47.27  ? 242  GLU A CA   1 
ATOM   5903 C C    . GLU B 1 242 ? 124.557 122.450 120.072 1.00 45.68  ? 242  GLU A C    1 
ATOM   5904 O O    . GLU B 1 242 ? 125.623 122.771 120.612 1.00 58.26  ? 242  GLU A O    1 
ATOM   5905 C CB   . GLU B 1 242 ? 124.430 121.242 117.855 1.00 51.24  ? 242  GLU A CB   1 
ATOM   5906 C CG   . GLU B 1 242 ? 123.183 121.788 117.193 1.00 53.47  ? 242  GLU A CG   1 
ATOM   5907 C CD   . GLU B 1 242 ? 123.253 123.283 116.940 1.00 56.27  ? 242  GLU A CD   1 
ATOM   5908 O OE1  . GLU B 1 242 ? 124.374 123.834 116.928 1.00 59.98  ? 242  GLU A OE1  1 
ATOM   5909 O OE2  . GLU B 1 242 ? 122.187 123.907 116.755 1.00 53.16  ? 242  GLU A OE2  1 
ATOM   5910 N N    . ASN B 1 243 ? 123.500 123.266 120.048 1.00 31.62  ? 243  ASN A N    1 
ATOM   5911 C CA   . ASN B 1 243 ? 123.603 124.604 120.610 1.00 43.69  ? 243  ASN A CA   1 
ATOM   5912 C C    . ASN B 1 243 ? 123.734 124.540 122.126 1.00 38.61  ? 243  ASN A C    1 
ATOM   5913 O O    . ASN B 1 243 ? 124.402 125.392 122.726 1.00 33.23  ? 243  ASN A O    1 
ATOM   5914 C CB   . ASN B 1 243 ? 122.381 125.430 120.208 1.00 43.35  ? 243  ASN A CB   1 
ATOM   5915 C CG   . ASN B 1 243 ? 122.662 126.918 120.185 1.00 45.41  ? 243  ASN A CG   1 
ATOM   5916 O OD1  . ASN B 1 243 ? 123.563 127.404 120.869 1.00 36.17  ? 243  ASN A OD1  1 
ATOM   5917 N ND2  . ASN B 1 243 ? 121.882 127.653 119.401 1.00 49.96  ? 243  ASN A ND2  1 
ATOM   5918 N N    . PHE B 1 244 ? 123.125 123.528 122.756 1.00 29.51  ? 244  PHE A N    1 
ATOM   5919 C CA   . PHE B 1 244 ? 123.275 123.362 124.198 1.00 25.94  ? 244  PHE A CA   1 
ATOM   5920 C C    . PHE B 1 244 ? 124.721 123.054 124.560 1.00 37.27  ? 244  PHE A C    1 
ATOM   5921 O O    . PHE B 1 244 ? 125.234 123.549 125.571 1.00 48.36  ? 244  PHE A O    1 
ATOM   5922 C CB   . PHE B 1 244 ? 122.345 122.256 124.698 1.00 31.79  ? 244  PHE A CB   1 
ATOM   5923 C CG   . PHE B 1 244 ? 122.612 121.828 126.113 1.00 25.72  ? 244  PHE A CG   1 
ATOM   5924 C CD1  . PHE B 1 244 ? 122.206 122.611 127.177 1.00 19.10  ? 244  PHE A CD1  1 
ATOM   5925 C CD2  . PHE B 1 244 ? 123.253 120.628 126.376 1.00 19.69  ? 244  PHE A CD2  1 
ATOM   5926 C CE1  . PHE B 1 244 ? 122.449 122.215 128.478 1.00 15.12  ? 244  PHE A CE1  1 
ATOM   5927 C CE2  . PHE B 1 244 ? 123.498 120.227 127.673 1.00 23.44  ? 244  PHE A CE2  1 
ATOM   5928 C CZ   . PHE B 1 244 ? 123.096 121.021 128.725 1.00 21.61  ? 244  PHE A CZ   1 
ATOM   5929 N N    . LEU B 1 245 ? 125.396 122.237 123.746 1.00 38.26  ? 245  LEU A N    1 
ATOM   5930 C CA   . LEU B 1 245 ? 126.802 121.945 124.011 1.00 24.78  ? 245  LEU A CA   1 
ATOM   5931 C C    . LEU B 1 245 ? 127.684 123.152 123.719 1.00 19.33  ? 245  LEU A C    1 
ATOM   5932 O O    . LEU B 1 245 ? 128.656 123.397 124.439 1.00 26.14  ? 245  LEU A O    1 
ATOM   5933 C CB   . LEU B 1 245 ? 127.269 120.731 123.209 1.00 21.52  ? 245  LEU A CB   1 
ATOM   5934 C CG   . LEU B 1 245 ? 126.592 119.401 123.537 1.00 30.47  ? 245  LEU A CG   1 
ATOM   5935 C CD1  . LEU B 1 245 ? 127.093 118.302 122.618 1.00 31.18  ? 245  LEU A CD1  1 
ATOM   5936 C CD2  . LEU B 1 245 ? 126.828 119.034 124.993 1.00 29.58  ? 245  LEU A CD2  1 
ATOM   5937 N N    . ASP B 1 246 ? 127.336 123.930 122.690 1.00 19.61  ? 246  ASP A N    1 
ATOM   5938 C CA   . ASP B 1 246 ? 128.144 125.084 122.299 1.00 30.68  ? 246  ASP A CA   1 
ATOM   5939 C C    . ASP B 1 246 ? 128.051 126.217 123.316 1.00 31.21  ? 246  ASP A C    1 
ATOM   5940 O O    . ASP B 1 246 ? 129.045 126.918 123.562 1.00 29.67  ? 246  ASP A O    1 
ATOM   5941 C CB   . ASP B 1 246 ? 127.713 125.574 120.917 1.00 29.35  ? 246  ASP A CB   1 
ATOM   5942 C CG   . ASP B 1 246 ? 128.207 124.677 119.801 1.00 35.12  ? 246  ASP A CG   1 
ATOM   5943 O OD1  . ASP B 1 246 ? 128.358 123.461 120.037 1.00 32.27  ? 246  ASP A OD1  1 
ATOM   5944 O OD2  . ASP B 1 246 ? 128.442 125.187 118.686 1.00 33.01  ? 246  ASP A OD2  1 
ATOM   5945 N N    . GLY B 1 247 ? 126.879 126.392 123.932 1.00 23.26  ? 247  GLY A N    1 
ATOM   5946 C CA   . GLY B 1 247 ? 126.732 127.408 124.965 1.00 17.08  ? 247  GLY A CA   1 
ATOM   5947 C C    . GLY B 1 247 ? 127.639 127.178 126.159 1.00 20.77  ? 247  GLY A C    1 
ATOM   5948 O O    . GLY B 1 247 ? 128.239 128.120 126.682 1.00 35.70  ? 247  GLY A O    1 
ATOM   5949 N N    . LEU B 1 248 ? 127.748 125.931 126.613 1.00 14.65  ? 248  LEU A N    1 
ATOM   5950 C CA   . LEU B 1 248 ? 128.661 125.630 127.710 1.00 23.06  ? 248  LEU A CA   1 
ATOM   5951 C C    . LEU B 1 248 ? 130.111 125.582 127.242 1.00 27.75  ? 248  LEU A C    1 
ATOM   5952 O O    . LEU B 1 248 ? 131.015 125.942 128.004 1.00 15.43  ? 248  LEU A O    1 
ATOM   5953 C CB   . LEU B 1 248 ? 128.284 124.300 128.367 1.00 20.56  ? 248  LEU A CB   1 
ATOM   5954 C CG   . LEU B 1 248 ? 126.993 124.227 129.183 1.00 6.80   ? 248  LEU A CG   1 
ATOM   5955 C CD1  . LEU B 1 248 ? 127.059 123.073 130.163 1.00 10.61  ? 248  LEU A CD1  1 
ATOM   5956 C CD2  . LEU B 1 248 ? 126.756 125.529 129.923 1.00 12.43  ? 248  LEU A CD2  1 
ATOM   5957 N N    . GLY B 1 249 ? 130.350 125.133 126.009 1.00 28.70  ? 249  GLY A N    1 
ATOM   5958 C CA   . GLY B 1 249 ? 131.708 125.019 125.507 1.00 15.44  ? 249  GLY A CA   1 
ATOM   5959 C C    . GLY B 1 249 ? 132.424 126.345 125.324 1.00 23.03  ? 249  GLY A C    1 
ATOM   5960 O O    . GLY B 1 249 ? 133.597 126.476 125.681 1.00 36.76  ? 249  GLY A O    1 
ATOM   5961 N N    . ASN B 1 250 ? 131.737 127.346 124.765 1.00 15.99  ? 250  ASN A N    1 
ATOM   5962 C CA   . ASN B 1 250 ? 132.405 128.618 124.498 1.00 27.25  ? 250  ASN A CA   1 
ATOM   5963 C C    . ASN B 1 250 ? 132.657 129.462 125.746 1.00 33.54  ? 250  ASN A C    1 
ATOM   5964 O O    . ASN B 1 250 ? 133.492 130.371 125.698 1.00 40.16  ? 250  ASN A O    1 
ATOM   5965 C CB   . ASN B 1 250 ? 131.581 129.431 123.500 1.00 28.05  ? 250  ASN A CB   1 
ATOM   5966 C CG   . ASN B 1 250 ? 131.542 128.799 122.125 1.00 36.27  ? 250  ASN A CG   1 
ATOM   5967 O OD1  . ASN B 1 250 ? 132.390 127.975 121.783 1.00 45.83  ? 250  ASN A OD1  1 
ATOM   5968 N ND2  . ASN B 1 250 ? 130.555 129.183 121.325 1.00 37.43  ? 250  ASN A ND2  1 
ATOM   5969 N N    . SER B 1 251 ? 131.966 129.194 126.849 1.00 18.42  ? 251  SER A N    1 
ATOM   5970 C CA   . SER B 1 251 ? 132.157 129.926 128.098 1.00 16.50  ? 251  SER A CA   1 
ATOM   5971 C C    . SER B 1 251 ? 133.377 129.485 128.906 1.00 22.82  ? 251  SER A C    1 
ATOM   5972 O O    . SER B 1 251 ? 133.680 130.118 129.922 1.00 35.19  ? 251  SER A O    1 
ATOM   5973 C CB   . SER B 1 251 ? 130.906 129.801 128.970 1.00 6.63   ? 251  SER A CB   1 
ATOM   5974 O OG   . SER B 1 251 ? 130.752 128.478 129.451 1.00 18.47  ? 251  SER A OG   1 
ATOM   5975 N N    . PHE B 1 252 ? 134.076 128.427 128.493 1.00 8.25   ? 252  PHE A N    1 
ATOM   5976 C CA   . PHE B 1 252 ? 135.204 127.920 129.276 1.00 7.07   ? 252  PHE A CA   1 
ATOM   5977 C C    . PHE B 1 252 ? 136.458 128.790 129.203 1.00 26.42  ? 252  PHE A C    1 
ATOM   5978 O O    . PHE B 1 252 ? 137.103 129.017 130.230 1.00 39.90  ? 252  PHE A O    1 
ATOM   5979 C CB   . PHE B 1 252 ? 135.540 126.503 128.812 1.00 12.11  ? 252  PHE A CB   1 
ATOM   5980 C CG   . PHE B 1 252 ? 136.800 125.948 129.413 1.00 16.41  ? 252  PHE A CG   1 
ATOM   5981 C CD1  . PHE B 1 252 ? 136.863 125.629 130.757 1.00 17.44  ? 252  PHE A CD1  1 
ATOM   5982 C CD2  . PHE B 1 252 ? 137.923 125.745 128.629 1.00 16.52  ? 252  PHE A CD2  1 
ATOM   5983 C CE1  . PHE B 1 252 ? 138.021 125.116 131.307 1.00 8.57   ? 252  PHE A CE1  1 
ATOM   5984 C CE2  . PHE B 1 252 ? 139.082 125.235 129.175 1.00 15.72  ? 252  PHE A CE2  1 
ATOM   5985 C CZ   . PHE B 1 252 ? 139.131 124.920 130.515 1.00 13.93  ? 252  PHE A CZ   1 
ATOM   5986 N N    . SER B 1 253 ? 136.849 129.247 128.010 1.00 22.75  ? 253  SER A N    1 
ATOM   5987 C CA   . SER B 1 253 ? 138.155 129.894 127.841 1.00 17.35  ? 253  SER A CA   1 
ATOM   5988 C C    . SER B 1 253 ? 138.328 131.170 128.672 1.00 17.50  ? 253  SER A C    1 
ATOM   5989 O O    . SER B 1 253 ? 139.267 131.274 129.478 1.00 25.09  ? 253  SER A O    1 
ATOM   5990 C CB   . SER B 1 253 ? 138.383 130.197 126.360 1.00 19.99  ? 253  SER A CB   1 
ATOM   5991 O OG   . SER B 1 253 ? 139.669 130.750 126.150 1.00 38.26  ? 253  SER A OG   1 
ATOM   5992 N N    . GLY B 1 254 ? 137.374 132.099 128.575 1.00 12.76  ? 254  GLY A N    1 
ATOM   5993 C CA   . GLY B 1 254 ? 137.482 133.346 129.322 1.00 6.85   ? 254  GLY A CA   1 
ATOM   5994 C C    . GLY B 1 254 ? 137.386 133.177 130.824 1.00 12.06  ? 254  GLY A C    1 
ATOM   5995 O O    . GLY B 1 254 ? 138.169 133.770 131.577 1.00 15.26  ? 254  GLY A O    1 
ATOM   5996 N N    . SER B 1 255 ? 136.495 132.307 131.281 1.00 9.15   ? 255  SER A N    1 
ATOM   5997 C CA   . SER B 1 255 ? 136.295 132.204 132.715 1.00 9.50   ? 255  SER A CA   1 
ATOM   5998 C C    . SER B 1 255 ? 137.404 131.373 133.335 1.00 13.44  ? 255  SER A C    1 
ATOM   5999 O O    . SER B 1 255 ? 137.797 131.625 134.479 1.00 30.23  ? 255  SER A O    1 
ATOM   6000 C CB   . SER B 1 255 ? 134.919 131.618 133.015 1.00 8.97   ? 255  SER A CB   1 
ATOM   6001 O OG   . SER B 1 255 ? 134.803 131.312 134.385 1.00 31.19  ? 255  SER A OG   1 
ATOM   6002 N N    . ALA B 1 256 ? 137.917 130.388 132.594 1.00 1.72   ? 256  ALA A N    1 
ATOM   6003 C CA   . ALA B 1 256 ? 139.036 129.589 133.075 1.00 7.51   ? 256  ALA A CA   1 
ATOM   6004 C C    . ALA B 1 256 ? 140.280 130.455 133.222 1.00 15.02  ? 256  ALA A C    1 
ATOM   6005 O O    . ALA B 1 256 ? 140.995 130.357 134.226 1.00 10.89  ? 256  ALA A O    1 
ATOM   6006 C CB   . ALA B 1 256 ? 139.300 128.422 132.125 1.00 15.29  ? 256  ALA A CB   1 
ATOM   6007 N N    . LEU B 1 257 ? 140.542 131.330 132.240 1.00 18.63  ? 257  LEU A N    1 
ATOM   6008 C CA   . LEU B 1 257 ? 141.677 132.245 132.361 1.00 1.84   ? 257  LEU A CA   1 
ATOM   6009 C C    . LEU B 1 257 ? 141.486 133.209 133.529 1.00 5.65   ? 257  LEU A C    1 
ATOM   6010 O O    . LEU B 1 257 ? 142.438 133.487 134.274 1.00 23.38  ? 257  LEU A O    1 
ATOM   6011 C CB   . LEU B 1 257 ? 141.899 133.012 131.059 1.00 5.35   ? 257  LEU A CB   1 
ATOM   6012 C CG   . LEU B 1 257 ? 142.333 132.191 129.844 1.00 3.56   ? 257  LEU A CG   1 
ATOM   6013 C CD1  . LEU B 1 257 ? 142.174 132.995 128.567 1.00 4.21   ? 257  LEU A CD1  1 
ATOM   6014 C CD2  . LEU B 1 257 ? 143.767 131.728 130.009 1.00 1.10   ? 257  LEU A CD2  1 
ATOM   6015 N N    . PHE B 1 258 ? 140.272 133.749 133.692 1.00 10.82  ? 258  PHE A N    1 
ATOM   6016 C CA   . PHE B 1 258 ? 140.023 134.678 134.792 1.00 5.56   ? 258  PHE A CA   1 
ATOM   6017 C C    . PHE B 1 258 ? 140.236 134.003 136.146 1.00 8.39   ? 258  PHE A C    1 
ATOM   6018 O O    . PHE B 1 258 ? 140.878 134.572 137.039 1.00 18.16  ? 258  PHE A O    1 
ATOM   6019 C CB   . PHE B 1 258 ? 138.600 135.234 134.672 1.00 9.28   ? 258  PHE A CB   1 
ATOM   6020 C CG   . PHE B 1 258 ? 138.301 136.390 135.590 1.00 16.98  ? 258  PHE A CG   1 
ATOM   6021 C CD1  . PHE B 1 258 ? 137.902 136.175 136.901 1.00 16.95  ? 258  PHE A CD1  1 
ATOM   6022 C CD2  . PHE B 1 258 ? 138.411 137.693 135.137 1.00 20.90  ? 258  PHE A CD2  1 
ATOM   6023 C CE1  . PHE B 1 258 ? 137.622 137.234 137.740 1.00 14.21  ? 258  PHE A CE1  1 
ATOM   6024 C CE2  . PHE B 1 258 ? 138.133 138.756 135.974 1.00 22.68  ? 258  PHE A CE2  1 
ATOM   6025 C CZ   . PHE B 1 258 ? 137.739 138.525 137.277 1.00 16.97  ? 258  PHE A CZ   1 
ATOM   6026 N N    . TYR B 1 259 ? 139.698 132.791 136.326 1.00 8.86   ? 259  TYR A N    1 
ATOM   6027 C CA   . TYR B 1 259 ? 139.906 132.102 137.596 1.00 3.00   ? 259  TYR A CA   1 
ATOM   6028 C C    . TYR B 1 259 ? 141.363 131.708 137.795 1.00 20.37  ? 259  TYR A C    1 
ATOM   6029 O O    . TYR B 1 259 ? 141.848 131.692 138.936 1.00 26.98  ? 259  TYR A O    1 
ATOM   6030 C CB   . TYR B 1 259 ? 139.017 130.863 137.675 1.00 5.21   ? 259  TYR A CB   1 
ATOM   6031 C CG   . TYR B 1 259 ? 139.280 130.003 138.889 1.00 7.21   ? 259  TYR A CG   1 
ATOM   6032 C CD1  . TYR B 1 259 ? 139.120 130.510 140.170 1.00 4.46   ? 259  TYR A CD1  1 
ATOM   6033 C CD2  . TYR B 1 259 ? 139.700 128.687 138.754 1.00 22.53  ? 259  TYR A CD2  1 
ATOM   6034 C CE1  . TYR B 1 259 ? 139.362 129.729 141.283 1.00 11.98  ? 259  TYR A CE1  1 
ATOM   6035 C CE2  . TYR B 1 259 ? 139.945 127.899 139.861 1.00 17.99  ? 259  TYR A CE2  1 
ATOM   6036 C CZ   . TYR B 1 259 ? 139.774 128.425 141.123 1.00 11.33  ? 259  TYR A CZ   1 
ATOM   6037 O OH   . TYR B 1 259 ? 140.016 127.645 142.229 1.00 7.34   ? 259  TYR A OH   1 
ATOM   6038 N N    . LEU B 1 260 ? 142.091 131.433 136.703 1.00 24.92  ? 260  LEU A N    1 
ATOM   6039 C CA   . LEU B 1 260 ? 143.515 131.155 136.838 1.00 17.58  ? 260  LEU A CA   1 
ATOM   6040 C C    . LEU B 1 260 ? 144.247 132.373 137.371 1.00 3.94   ? 260  LEU A C    1 
ATOM   6041 O O    . LEU B 1 260 ? 145.136 132.251 138.220 1.00 6.07   ? 260  LEU A O    1 
ATOM   6042 C CB   . LEU B 1 260 ? 144.099 130.717 135.495 1.00 21.40  ? 260  LEU A CB   1 
ATOM   6043 C CG   . LEU B 1 260 ? 145.612 130.488 135.441 1.00 8.58   ? 260  LEU A CG   1 
ATOM   6044 C CD1  . LEU B 1 260 ? 146.040 129.451 136.463 1.00 12.26  ? 260  LEU A CD1  1 
ATOM   6045 C CD2  . LEU B 1 260 ? 146.043 130.073 134.044 1.00 11.82  ? 260  LEU A CD2  1 
ATOM   6046 N N    . GLY B 1 261 ? 143.914 133.555 136.852 1.00 17.52  ? 261  GLY A N    1 
ATOM   6047 C CA   . GLY B 1 261 ? 144.527 134.759 137.384 1.00 26.91  ? 261  GLY A CA   1 
ATOM   6048 C C    . GLY B 1 261 ? 144.160 134.997 138.837 1.00 28.23  ? 261  GLY A C    1 
ATOM   6049 O O    . GLY B 1 261 ? 145.001 135.394 139.646 1.00 29.36  ? 261  GLY A O    1 
ATOM   6050 N N    . LEU B 1 262 ? 142.891 134.756 139.184 1.00 34.33  ? 262  LEU A N    1 
ATOM   6051 C CA   . LEU B 1 262 ? 142.416 134.980 140.547 1.00 27.76  ? 262  LEU A CA   1 
ATOM   6052 C C    . LEU B 1 262 ? 143.010 134.002 141.561 1.00 23.06  ? 262  LEU A C    1 
ATOM   6053 O O    . LEU B 1 262 ? 143.060 134.319 142.754 1.00 20.32  ? 262  LEU A O    1 
ATOM   6054 C CB   . LEU B 1 262 ? 140.884 134.904 140.549 1.00 19.43  ? 262  LEU A CB   1 
ATOM   6055 C CG   . LEU B 1 262 ? 139.987 135.665 141.535 1.00 8.46   ? 262  LEU A CG   1 
ATOM   6056 C CD1  . LEU B 1 262 ? 138.555 135.607 141.037 1.00 18.77  ? 262  LEU A CD1  1 
ATOM   6057 C CD2  . LEU B 1 262 ? 140.050 135.168 142.961 1.00 12.73  ? 262  LEU A CD2  1 
ATOM   6058 N N    . THR B 1 263 ? 143.510 132.849 141.113 1.00 20.22  ? 263  THR A N    1 
ATOM   6059 C CA   . THR B 1 263 ? 144.017 131.828 142.028 1.00 27.34  ? 263  THR A CA   1 
ATOM   6060 C C    . THR B 1 263 ? 145.474 132.025 142.437 1.00 31.98  ? 263  THR A C    1 
ATOM   6061 O O    . THR B 1 263 ? 145.930 131.367 143.378 1.00 28.02  ? 263  THR A O    1 
ATOM   6062 C CB   . THR B 1 263 ? 143.837 130.425 141.425 1.00 25.27  ? 263  THR A CB   1 
ATOM   6063 O OG1  . THR B 1 263 ? 143.752 129.462 142.481 1.00 29.99  ? 263  THR A OG1  1 
ATOM   6064 C CG2  . THR B 1 263 ? 145.005 130.053 140.533 1.00 27.96  ? 263  THR A CG2  1 
ATOM   6065 N N    . MET B 1 264 ? 146.208 132.909 141.770 1.00 26.28  ? 264  MET A N    1 
ATOM   6066 C CA   . MET B 1 264 ? 147.618 133.141 142.054 1.00 17.93  ? 264  MET A CA   1 
ATOM   6067 C C    . MET B 1 264 ? 147.872 134.166 143.155 1.00 20.28  ? 264  MET A C    1 
ATOM   6068 O O    . MET B 1 264 ? 149.029 134.354 143.542 1.00 23.78  ? 264  MET A O    1 
ATOM   6069 C CB   . MET B 1 264 ? 148.311 133.570 140.759 1.00 11.96  ? 264  MET A CB   1 
ATOM   6070 C CG   . MET B 1 264 ? 148.503 132.403 139.808 1.00 25.50  ? 264  MET A CG   1 
ATOM   6071 S SD   . MET B 1 264 ? 148.591 132.816 138.056 1.00 41.34  ? 264  MET A SD   1 
ATOM   6072 C CE   . MET B 1 264 ? 149.728 134.188 138.054 1.00 24.43  ? 264  MET A CE   1 
ATOM   6073 N N    . VAL B 1 265 ? 146.832 134.827 143.657 1.00 40.63  ? 265  VAL A N    1 
ATOM   6074 C CA   . VAL B 1 265 ? 146.950 135.975 144.556 1.00 42.76  ? 265  VAL A CA   1 
ATOM   6075 C C    . VAL B 1 265 ? 147.530 135.515 145.897 1.00 40.74  ? 265  VAL A C    1 
ATOM   6076 O O    . VAL B 1 265 ? 146.890 134.757 146.633 1.00 42.30  ? 265  VAL A O    1 
ATOM   6077 C CB   . VAL B 1 265 ? 145.598 136.678 144.746 1.00 39.87  ? 265  VAL A CB   1 
ATOM   6078 C CG1  . VAL B 1 265 ? 145.540 137.458 146.066 1.00 37.02  ? 265  VAL A CG1  1 
ATOM   6079 C CG2  . VAL B 1 265 ? 145.289 137.582 143.566 1.00 38.50  ? 265  VAL A CG2  1 
ATOM   6080 N N    . GLY B 1 266 ? 148.779 135.895 146.175 1.00 44.71  ? 266  GLY A N    1 
ATOM   6081 C CA   . GLY B 1 266 ? 149.387 135.639 147.471 1.00 44.51  ? 266  GLY A CA   1 
ATOM   6082 C C    . GLY B 1 266 ? 149.882 134.236 147.741 1.00 49.44  ? 266  GLY A C    1 
ATOM   6083 O O    . GLY B 1 266 ? 150.233 133.936 148.887 1.00 46.86  ? 266  GLY A O    1 
ATOM   6084 N N    . LYS B 1 267 ? 149.932 133.369 146.733 1.00 57.65  ? 267  LYS A N    1 
ATOM   6085 C CA   . LYS B 1 267 ? 150.283 131.971 146.949 1.00 53.14  ? 267  LYS A CA   1 
ATOM   6086 C C    . LYS B 1 267 ? 151.786 131.709 146.965 1.00 51.98  ? 267  LYS A C    1 
ATOM   6087 O O    . LYS B 1 267 ? 152.205 130.678 147.503 1.00 47.86  ? 267  LYS A O    1 
ATOM   6088 C CB   . LYS B 1 267 ? 149.615 131.099 145.887 1.00 45.93  ? 267  LYS A CB   1 
ATOM   6089 C CG   . LYS B 1 267 ? 148.109 131.274 145.836 1.00 52.83  ? 267  LYS A CG   1 
ATOM   6090 C CD   . LYS B 1 267 ? 147.376 129.984 146.146 1.00 54.27  ? 267  LYS A CD   1 
ATOM   6091 C CE   . LYS B 1 267 ? 146.005 130.268 146.732 1.00 56.79  ? 267  LYS A CE   1 
ATOM   6092 N NZ   . LYS B 1 267 ? 146.089 131.130 147.944 1.00 56.92  ? 267  LYS A NZ   1 
ATOM   6093 N N    . ILE B 1 268 ? 152.596 132.593 146.373 1.00 58.88  ? 268  ILE A N    1 
ATOM   6094 C CA   . ILE B 1 268 ? 154.036 132.351 146.255 1.00 60.53  ? 268  ILE A CA   1 
ATOM   6095 C C    . ILE B 1 268 ? 154.706 132.234 147.628 1.00 62.02  ? 268  ILE A C    1 
ATOM   6096 O O    . ILE B 1 268 ? 155.609 131.407 147.807 1.00 60.28  ? 268  ILE A O    1 
ATOM   6097 C CB   . ILE B 1 268 ? 154.701 133.409 145.344 1.00 56.74  ? 268  ILE A CB   1 
ATOM   6098 C CG1  . ILE B 1 268 ? 155.938 132.818 144.665 1.00 61.46  ? 268  ILE A CG1  1 
ATOM   6099 C CG2  . ILE B 1 268 ? 155.073 134.691 146.076 1.00 55.44  ? 268  ILE A CG2  1 
ATOM   6100 C CD1  . ILE B 1 268 ? 156.435 133.626 143.490 1.00 59.33  ? 268  ILE A CD1  1 
ATOM   6101 N N    . LYS B 1 269 ? 154.289 133.053 148.610 1.00 78.63  ? 269  LYS A N    1 
ATOM   6102 C CA   . LYS B 1 269 ? 154.712 132.918 150.009 1.00 79.15  ? 269  LYS A CA   1 
ATOM   6103 C C    . LYS B 1 269 ? 156.219 133.091 150.192 1.00 79.43  ? 269  LYS A C    1 
ATOM   6104 O O    . LYS B 1 269 ? 156.937 133.408 149.238 1.00 82.28  ? 269  LYS A O    1 
ATOM   6105 C CB   . LYS B 1 269 ? 154.254 131.577 150.594 1.00 75.91  ? 269  LYS A CB   1 
ATOM   6106 C CG   . LYS B 1 269 ? 152.843 131.603 151.162 1.00 77.68  ? 269  LYS A CG   1 
ATOM   6107 C CD   . LYS B 1 269 ? 152.615 132.839 152.022 1.00 76.12  ? 269  LYS A CD   1 
ATOM   6108 C CE   . LYS B 1 269 ? 151.382 132.691 152.897 1.00 77.28  ? 269  LYS A CE   1 
ATOM   6109 N NZ   . LYS B 1 269 ? 151.109 131.270 153.240 1.00 77.23  ? 269  LYS A NZ   1 
ATOM   6110 N N    . ARG B 1 270 ? 156.709 132.933 151.422 1.00 86.91  ? 270  ARG A N    1 
ATOM   6111 C CA   . ARG B 1 270 ? 158.150 132.930 151.619 1.00 89.86  ? 270  ARG A CA   1 
ATOM   6112 C C    . ARG B 1 270 ? 158.675 131.528 151.294 1.00 89.32  ? 270  ARG A C    1 
ATOM   6113 O O    . ARG B 1 270 ? 157.908 130.627 150.944 1.00 87.73  ? 270  ARG A O    1 
ATOM   6114 C CB   . ARG B 1 270 ? 158.472 133.391 153.045 1.00 89.60  ? 270  ARG A CB   1 
ATOM   6115 C CG   . ARG B 1 270 ? 159.927 133.782 153.334 1.00 88.75  ? 270  ARG A CG   1 
ATOM   6116 C CD   . ARG B 1 270 ? 160.358 134.955 152.463 1.00 91.64  ? 270  ARG A CD   1 
ATOM   6117 N NE   . ARG B 1 270 ? 160.990 134.525 151.220 1.00 92.36  ? 270  ARG A NE   1 
ATOM   6118 C CZ   . ARG B 1 270 ? 161.645 135.331 150.396 1.00 92.89  ? 270  ARG A CZ   1 
ATOM   6119 N NH1  . ARG B 1 270 ? 161.779 136.620 150.654 1.00 91.64  ? 270  ARG A NH1  1 
ATOM   6120 N NH2  . ARG B 1 270 ? 162.176 134.830 149.285 1.00 92.70  ? 270  ARG A NH2  1 
ATOM   6121 N N    . LEU B 1 271 ? 159.983 131.311 151.421 1.00 93.50  ? 271  LEU A N    1 
ATOM   6122 C CA   . LEU B 1 271 ? 160.533 129.998 151.113 1.00 95.41  ? 271  LEU A CA   1 
ATOM   6123 C C    . LEU B 1 271 ? 161.758 129.702 151.975 1.00 96.61  ? 271  LEU A C    1 
ATOM   6124 O O    . LEU B 1 271 ? 162.020 130.361 152.985 1.00 98.51  ? 271  LEU A O    1 
ATOM   6125 C CB   . LEU B 1 271 ? 160.864 129.898 149.618 1.00 94.94  ? 271  LEU A CB   1 
ATOM   6126 C CG   . LEU B 1 271 ? 159.821 129.196 148.745 1.00 96.22  ? 271  LEU A CG   1 
ATOM   6127 C CD1  . LEU B 1 271 ? 160.241 129.197 147.285 1.00 95.07  ? 271  LEU A CD1  1 
ATOM   6128 C CD2  . LEU B 1 271 ? 159.549 127.784 149.237 1.00 93.84  ? 271  LEU A CD2  1 
ATOM   6129 N N    . LYS B 1 272 ? 162.496 128.682 151.540 1.00 95.96  ? 272  LYS A N    1 
ATOM   6130 C CA   . LYS B 1 272 ? 163.644 128.054 152.174 1.00 93.49  ? 272  LYS A CA   1 
ATOM   6131 C C    . LYS B 1 272 ? 164.585 127.690 151.032 1.00 96.45  ? 272  LYS A C    1 
ATOM   6132 O O    . LYS B 1 272 ? 164.178 127.703 149.868 1.00 99.85  ? 272  LYS A O    1 
ATOM   6133 C CB   . LYS B 1 272 ? 163.259 126.854 153.054 1.00 93.23  ? 272  LYS A CB   1 
ATOM   6134 C CG   . LYS B 1 272 ? 162.916 125.581 152.330 1.00 94.63  ? 272  LYS A CG   1 
ATOM   6135 C CD   . LYS B 1 272 ? 163.119 124.375 153.237 1.00 94.85  ? 272  LYS A CD   1 
ATOM   6136 C CE   . LYS B 1 272 ? 164.560 124.255 153.700 1.00 94.82  ? 272  LYS A CE   1 
ATOM   6137 N NZ   . LYS B 1 272 ? 164.704 123.261 154.801 1.00 95.56  ? 272  LYS A NZ   1 
ATOM   6138 N N    . LYS B 1 273 ? 165.851 127.406 151.355 1.00 81.52  ? 273  LYS A N    1 
ATOM   6139 C CA   . LYS B 1 273 ? 166.785 126.927 150.334 1.00 79.20  ? 273  LYS A CA   1 
ATOM   6140 C C    . LYS B 1 273 ? 166.293 125.681 149.603 1.00 76.02  ? 273  LYS A C    1 
ATOM   6141 O O    . LYS B 1 273 ? 166.124 125.749 148.375 1.00 74.62  ? 273  LYS A O    1 
ATOM   6142 C CB   . LYS B 1 273 ? 168.144 126.637 150.975 1.00 79.04  ? 273  LYS A CB   1 
ATOM   6143 C CG   . LYS B 1 273 ? 169.027 127.859 151.165 1.00 78.69  ? 273  LYS A CG   1 
ATOM   6144 C CD   . LYS B 1 273 ? 169.148 128.660 149.882 1.00 79.60  ? 273  LYS A CD   1 
ATOM   6145 C CE   . LYS B 1 273 ? 170.170 128.033 148.948 1.00 79.40  ? 273  LYS A CE   1 
ATOM   6146 N NZ   . LYS B 1 273 ? 170.580 128.963 147.863 1.00 79.93  ? 273  LYS A NZ   1 
ATOM   6147 N N    . SER B 1 274 ? 166.103 124.547 150.294 1.00 71.88  ? 274  SER A N    1 
ATOM   6148 C CA   . SER B 1 274 ? 166.102 123.263 149.593 1.00 75.00  ? 274  SER A CA   1 
ATOM   6149 C C    . SER B 1 274 ? 164.919 123.212 148.637 1.00 76.87  ? 274  SER A C    1 
ATOM   6150 O O    . SER B 1 274 ? 165.074 122.837 147.471 1.00 80.77  ? 274  SER A O    1 
ATOM   6151 C CB   . SER B 1 274 ? 166.046 122.106 150.588 1.00 74.76  ? 274  SER A CB   1 
ATOM   6152 O OG   . SER B 1 274 ? 164.707 121.802 150.934 1.00 74.54  ? 274  SER A OG   1 
ATOM   6153 N N    . ALA B 1 275 ? 163.754 123.639 149.139 1.00 68.38  ? 275  ALA A N    1 
ATOM   6154 C CA   . ALA B 1 275 ? 162.524 123.853 148.375 1.00 68.47  ? 275  ALA A CA   1 
ATOM   6155 C C    . ALA B 1 275 ? 162.804 124.540 147.047 1.00 70.95  ? 275  ALA A C    1 
ATOM   6156 O O    . ALA B 1 275 ? 162.516 123.997 145.975 1.00 74.06  ? 275  ALA A O    1 
ATOM   6157 C CB   . ALA B 1 275 ? 161.521 124.662 149.193 1.00 68.60  ? 275  ALA A CB   1 
ATOM   6158 N N    . PHE B 1 276 ? 163.256 125.790 147.124 1.00 53.71  ? 276  PHE A N    1 
ATOM   6159 C CA   . PHE B 1 276 ? 163.646 126.582 145.962 1.00 54.66  ? 276  PHE A CA   1 
ATOM   6160 C C    . PHE B 1 276 ? 164.567 125.839 144.993 1.00 54.65  ? 276  PHE A C    1 
ATOM   6161 O O    . PHE B 1 276 ? 164.340 125.899 143.782 1.00 55.47  ? 276  PHE A O    1 
ATOM   6162 C CB   . PHE B 1 276 ? 164.327 127.863 146.450 1.00 52.97  ? 276  PHE A CB   1 
ATOM   6163 C CG   . PHE B 1 276 ? 164.521 128.902 145.385 1.00 53.19  ? 276  PHE A CG   1 
ATOM   6164 C CD1  . PHE B 1 276 ? 163.467 129.308 144.588 1.00 52.82  ? 276  PHE A CD1  1 
ATOM   6165 C CD2  . PHE B 1 276 ? 165.766 129.477 145.189 1.00 54.15  ? 276  PHE A CD2  1 
ATOM   6166 C CE1  . PHE B 1 276 ? 163.652 130.267 143.612 1.00 55.95  ? 276  PHE A CE1  1 
ATOM   6167 C CE2  . PHE B 1 276 ? 165.958 130.436 144.216 1.00 53.46  ? 276  PHE A CE2  1 
ATOM   6168 C CZ   . PHE B 1 276 ? 164.900 130.832 143.426 1.00 55.48  ? 276  PHE A CZ   1 
ATOM   6169 N N    . VAL B 1 277 ? 165.672 125.248 145.464 1.00 46.72  ? 277  VAL A N    1 
ATOM   6170 C CA   . VAL B 1 277 ? 166.523 124.488 144.532 1.00 42.59  ? 277  VAL A CA   1 
ATOM   6171 C C    . VAL B 1 277 ? 165.743 123.378 143.809 1.00 49.72  ? 277  VAL A C    1 
ATOM   6172 O O    . VAL B 1 277 ? 165.906 123.169 142.593 1.00 48.91  ? 277  VAL A O    1 
ATOM   6173 C CB   . VAL B 1 277 ? 167.742 123.914 145.277 1.00 46.05  ? 277  VAL A CB   1 
ATOM   6174 C CG1  . VAL B 1 277 ? 168.690 123.236 144.302 1.00 48.85  ? 277  VAL A CG1  1 
ATOM   6175 C CG2  . VAL B 1 277 ? 168.459 125.012 146.041 1.00 53.10  ? 277  VAL A CG2  1 
ATOM   6176 N N    . VAL B 1 278 ? 164.839 122.695 144.527 1.00 53.45  ? 278  VAL A N    1 
ATOM   6177 C CA   . VAL B 1 278 ? 163.946 121.720 143.883 1.00 43.96  ? 278  VAL A CA   1 
ATOM   6178 C C    . VAL B 1 278 ? 163.090 122.378 142.811 1.00 44.04  ? 278  VAL A C    1 
ATOM   6179 O O    . VAL B 1 278 ? 162.908 121.831 141.717 1.00 54.89  ? 278  VAL A O    1 
ATOM   6180 C CB   . VAL B 1 278 ? 163.076 120.950 144.894 1.00 38.71  ? 278  VAL A CB   1 
ATOM   6181 C CG1  . VAL B 1 278 ? 162.557 119.704 144.233 1.00 51.87  ? 278  VAL A CG1  1 
ATOM   6182 C CG2  . VAL B 1 278 ? 163.900 120.464 146.036 1.00 38.08  ? 278  VAL A CG2  1 
ATOM   6183 N N    . LEU B 1 279 ? 162.518 123.537 143.131 1.00 27.28  ? 279  LEU A N    1 
ATOM   6184 C CA   . LEU B 1 279 ? 161.675 124.254 142.181 1.00 29.43  ? 279  LEU A CA   1 
ATOM   6185 C C    . LEU B 1 279 ? 162.466 124.666 140.947 1.00 35.68  ? 279  LEU A C    1 
ATOM   6186 O O    . LEU B 1 279 ? 161.962 124.593 139.814 1.00 43.62  ? 279  LEU A O    1 
ATOM   6187 C CB   . LEU B 1 279 ? 161.083 125.482 142.873 1.00 30.67  ? 279  LEU A CB   1 
ATOM   6188 C CG   . LEU B 1 279 ? 159.866 126.104 142.212 1.00 30.25  ? 279  LEU A CG   1 
ATOM   6189 C CD1  . LEU B 1 279 ? 158.977 124.977 141.761 1.00 32.45  ? 279  LEU A CD1  1 
ATOM   6190 C CD2  . LEU B 1 279 ? 159.134 127.024 143.171 1.00 39.21  ? 279  LEU A CD2  1 
ATOM   6191 N N    . ILE B 1 280 ? 163.733 125.036 141.150 1.00 35.63  ? 280  ILE A N    1 
ATOM   6192 C CA   . ILE B 1 280 ? 164.598 125.481 140.061 1.00 35.73  ? 280  ILE A CA   1 
ATOM   6193 C C    . ILE B 1 280 ? 164.783 124.333 139.085 1.00 36.48  ? 280  ILE A C    1 
ATOM   6194 O O    . ILE B 1 280 ? 164.590 124.474 137.867 1.00 29.96  ? 280  ILE A O    1 
ATOM   6195 C CB   . ILE B 1 280 ? 165.958 125.948 140.612 1.00 36.92  ? 280  ILE A CB   1 
ATOM   6196 C CG1  . ILE B 1 280 ? 165.865 127.332 141.254 1.00 43.53  ? 280  ILE A CG1  1 
ATOM   6197 C CG2  . ILE B 1 280 ? 167.007 125.957 139.512 1.00 27.80  ? 280  ILE A CG2  1 
ATOM   6198 C CD1  . ILE B 1 280 ? 165.322 128.383 140.353 1.00 36.63  ? 280  ILE A CD1  1 
ATOM   6199 N N    . LEU B 1 281 ? 165.041 123.147 139.639 1.00 42.51  ? 281  LEU A N    1 
ATOM   6200 C CA   . LEU B 1 281 ? 165.303 121.995 138.791 1.00 37.95  ? 281  LEU A CA   1 
ATOM   6201 C C    . LEU B 1 281 ? 164.017 121.562 138.101 1.00 38.95  ? 281  LEU A C    1 
ATOM   6202 O O    . LEU B 1 281 ? 164.044 121.180 136.933 1.00 42.92  ? 281  LEU A O    1 
ATOM   6203 C CB   . LEU B 1 281 ? 165.882 120.838 139.607 1.00 37.40  ? 281  LEU A CB   1 
ATOM   6204 C CG   . LEU B 1 281 ? 167.189 121.095 140.354 1.00 37.82  ? 281  LEU A CG   1 
ATOM   6205 C CD1  . LEU B 1 281 ? 167.384 120.066 141.449 1.00 35.43  ? 281  LEU A CD1  1 
ATOM   6206 C CD2  . LEU B 1 281 ? 168.363 121.081 139.392 1.00 40.73  ? 281  LEU A CD2  1 
ATOM   6207 N N    . LEU B 1 282 ? 162.909 121.508 138.837 1.00 36.16  ? 282  LEU A N    1 
ATOM   6208 C CA   . LEU B 1 282 ? 161.664 121.018 138.255 1.00 31.87  ? 282  LEU A CA   1 
ATOM   6209 C C    . LEU B 1 282 ? 161.177 121.871 137.080 1.00 37.02  ? 282  LEU A C    1 
ATOM   6210 O O    . LEU B 1 282 ? 160.828 121.346 136.010 1.00 42.69  ? 282  LEU A O    1 
ATOM   6211 C CB   . LEU B 1 282 ? 160.585 120.951 139.335 1.00 18.29  ? 282  LEU A CB   1 
ATOM   6212 C CG   . LEU B 1 282 ? 160.576 119.721 140.240 1.00 23.85  ? 282  LEU A CG   1 
ATOM   6213 C CD1  . LEU B 1 282 ? 159.293 119.674 141.049 1.00 31.00  ? 282  LEU A CD1  1 
ATOM   6214 C CD2  . LEU B 1 282 ? 160.737 118.458 139.418 1.00 28.69  ? 282  LEU A CD2  1 
ATOM   6215 N N    . ILE B 1 283 ? 161.171 123.201 137.253 1.00 25.60  ? 283  ILE A N    1 
ATOM   6216 C CA   . ILE B 1 283 ? 160.821 124.096 136.146 1.00 13.11  ? 283  ILE A CA   1 
ATOM   6217 C C    . ILE B 1 283 ? 161.825 124.042 134.993 1.00 23.06  ? 283  ILE A C    1 
ATOM   6218 O O    . ILE B 1 283 ? 161.427 124.047 133.813 1.00 26.06  ? 283  ILE A O    1 
ATOM   6219 C CB   . ILE B 1 283 ? 160.643 125.530 136.680 1.00 7.31   ? 283  ILE A CB   1 
ATOM   6220 C CG1  . ILE B 1 283 ? 159.358 125.631 137.496 1.00 18.61  ? 283  ILE A CG1  1 
ATOM   6221 C CG2  . ILE B 1 283 ? 160.615 126.543 135.566 1.00 16.96  ? 283  ILE A CG2  1 
ATOM   6222 C CD1  . ILE B 1 283 ? 159.400 126.705 138.542 1.00 35.55  ? 283  ILE A CD1  1 
ATOM   6223 N N    . THR B 1 284 ? 163.127 123.906 135.292 1.00 32.08  ? 284  THR A N    1 
ATOM   6224 C CA   . THR B 1 284 ? 164.088 123.763 134.196 1.00 38.07  ? 284  THR A CA   1 
ATOM   6225 C C    . THR B 1 284 ? 163.866 122.463 133.426 1.00 32.70  ? 284  THR A C    1 
ATOM   6226 O O    . THR B 1 284 ? 163.886 122.456 132.192 1.00 22.74  ? 284  THR A O    1 
ATOM   6227 C CB   . THR B 1 284 ? 165.541 123.940 134.682 1.00 35.35  ? 284  THR A CB   1 
ATOM   6228 O OG1  . THR B 1 284 ? 166.354 124.338 133.571 1.00 41.69  ? 284  THR A OG1  1 
ATOM   6229 C CG2  . THR B 1 284 ? 166.157 122.689 135.263 1.00 26.70  ? 284  THR A CG2  1 
ATOM   6230 N N    . ALA B 1 285 ? 163.537 121.383 134.137 1.00 35.96  ? 285  ALA A N    1 
ATOM   6231 C CA   . ALA B 1 285 ? 163.271 120.084 133.539 1.00 33.15  ? 285  ALA A CA   1 
ATOM   6232 C C    . ALA B 1 285 ? 162.084 120.152 132.599 1.00 22.45  ? 285  ALA A C    1 
ATOM   6233 O O    . ALA B 1 285 ? 162.239 119.866 131.409 1.00 32.72  ? 285  ALA A O    1 
ATOM   6234 C CB   . ALA B 1 285 ? 163.020 119.033 134.622 1.00 29.59  ? 285  ALA A CB   1 
ATOM   6235 N N    . LYS B 1 286 ? 160.982 120.742 133.054 1.00 5.99   ? 286  LYS A N    1 
ATOM   6236 C CA   . LYS B 1 286 ? 159.792 120.799 132.213 1.00 8.33   ? 286  LYS A CA   1 
ATOM   6237 C C    . LYS B 1 286 ? 160.011 121.655 130.973 1.00 26.53  ? 286  LYS A C    1 
ATOM   6238 O O    . LYS B 1 286 ? 160.153 121.086 129.871 1.00 34.32  ? 286  LYS A O    1 
ATOM   6239 C CB   . LYS B 1 286 ? 158.604 121.336 133.014 1.00 11.46  ? 286  LYS A CB   1 
ATOM   6240 C CG   . LYS B 1 286 ? 157.413 121.763 132.166 1.00 10.87  ? 286  LYS A CG   1 
ATOM   6241 C CD   . LYS B 1 286 ? 156.105 121.237 132.717 1.00 15.96  ? 286  LYS A CD   1 
ATOM   6242 C CE   . LYS B 1 286 ? 155.017 121.258 131.657 1.00 16.52  ? 286  LYS A CE   1 
ATOM   6243 N NZ   . LYS B 1 286 ? 155.513 120.826 130.325 1.00 11.61  ? 286  LYS A NZ   1 
ATOM   6244 N N    . LEU B 1 287 ? 160.340 122.935 131.171 1.00 31.72  ? 287  LEU A N    1 
ATOM   6245 C CA   . LEU B 1 287 ? 160.394 123.907 130.080 1.00 16.94  ? 287  LEU A CA   1 
ATOM   6246 C C    . LEU B 1 287 ? 161.541 123.607 129.129 1.00 19.48  ? 287  LEU A C    1 
ATOM   6247 O O    . LEU B 1 287 ? 161.417 123.853 127.926 1.00 18.33  ? 287  LEU A O    1 
ATOM   6248 C CB   . LEU B 1 287 ? 160.468 125.348 130.587 1.00 12.64  ? 287  LEU A CB   1 
ATOM   6249 C CG   . LEU B 1 287 ? 159.217 125.835 131.322 1.00 15.44  ? 287  LEU A CG   1 
ATOM   6250 C CD1  . LEU B 1 287 ? 159.529 127.032 132.188 1.00 30.35  ? 287  LEU A CD1  1 
ATOM   6251 C CD2  . LEU B 1 287 ? 158.104 126.163 130.342 1.00 10.04  ? 287  LEU A CD2  1 
ATOM   6252 N N    . LEU B 1 288 ? 162.661 123.095 129.629 1.00 31.07  ? 288  LEU A N    1 
ATOM   6253 C CA   . LEU B 1 288 ? 163.830 122.935 128.786 1.00 29.13  ? 288  LEU A CA   1 
ATOM   6254 C C    . LEU B 1 288 ? 163.852 121.534 128.182 1.00 34.85  ? 288  LEU A C    1 
ATOM   6255 O O    . LEU B 1 288 ? 163.842 121.389 126.954 1.00 33.83  ? 288  LEU A O    1 
ATOM   6256 C CB   . LEU B 1 288 ? 165.100 123.201 129.598 1.00 33.04  ? 288  LEU A CB   1 
ATOM   6257 C CG   . LEU B 1 288 ? 166.484 122.920 129.000 1.00 36.73  ? 288  LEU A CG   1 
ATOM   6258 C CD1  . LEU B 1 288 ? 166.602 123.403 127.553 1.00 34.92  ? 288  LEU A CD1  1 
ATOM   6259 C CD2  . LEU B 1 288 ? 167.576 123.532 129.863 1.00 37.94  ? 288  LEU A CD2  1 
ATOM   6260 N N    . VAL B 1 289 ? 163.895 120.484 129.008 1.00 34.23  ? 289  VAL A N    1 
ATOM   6261 C CA   . VAL B 1 289 ? 164.190 119.177 128.432 1.00 32.61  ? 289  VAL A CA   1 
ATOM   6262 C C    . VAL B 1 289 ? 162.962 118.534 127.779 1.00 29.59  ? 289  VAL A C    1 
ATOM   6263 O O    . VAL B 1 289 ? 163.128 117.624 126.961 1.00 35.36  ? 289  VAL A O    1 
ATOM   6264 C CB   . VAL B 1 289 ? 164.832 118.231 129.470 1.00 27.58  ? 289  VAL A CB   1 
ATOM   6265 C CG1  . VAL B 1 289 ? 165.890 118.957 130.301 1.00 39.49  ? 289  VAL A CG1  1 
ATOM   6266 C CG2  . VAL B 1 289 ? 163.806 117.471 130.302 1.00 16.70  ? 289  VAL A CG2  1 
ATOM   6267 N N    . LEU B 1 290 ? 161.716 118.944 128.100 1.00 16.13  ? 290  LEU A N    1 
ATOM   6268 C CA   . LEU B 1 290 ? 160.628 118.318 127.343 1.00 13.48  ? 290  LEU A CA   1 
ATOM   6269 C C    . LEU B 1 290 ? 160.620 118.667 125.846 1.00 31.81  ? 290  LEU A C    1 
ATOM   6270 O O    . LEU B 1 290 ? 160.581 117.730 125.021 1.00 30.57  ? 290  LEU A O    1 
ATOM   6271 C CB   . LEU B 1 290 ? 159.287 118.626 128.026 1.00 9.95   ? 290  LEU A CB   1 
ATOM   6272 C CG   . LEU B 1 290 ? 158.010 118.249 127.275 1.00 14.83  ? 290  LEU A CG   1 
ATOM   6273 C CD1  . LEU B 1 290 ? 157.711 116.773 127.447 1.00 10.76  ? 290  LEU A CD1  1 
ATOM   6274 C CD2  . LEU B 1 290 ? 156.836 119.083 127.756 1.00 13.26  ? 290  LEU A CD2  1 
ATOM   6275 N N    . PRO B 1 291 ? 160.661 119.945 125.417 1.00 28.12  ? 291  PRO A N    1 
ATOM   6276 C CA   . PRO B 1 291 ? 160.635 120.226 123.963 1.00 17.41  ? 291  PRO A CA   1 
ATOM   6277 C C    . PRO B 1 291 ? 161.784 119.664 123.129 1.00 21.64  ? 291  PRO A C    1 
ATOM   6278 O O    . PRO B 1 291 ? 161.570 119.296 121.966 1.00 20.74  ? 291  PRO A O    1 
ATOM   6279 C CB   . PRO B 1 291 ? 160.623 121.761 123.921 1.00 18.06  ? 291  PRO A CB   1 
ATOM   6280 C CG   . PRO B 1 291 ? 160.047 122.166 125.214 1.00 26.49  ? 291  PRO A CG   1 
ATOM   6281 C CD   . PRO B 1 291 ? 160.649 121.209 126.178 1.00 18.26  ? 291  PRO A CD   1 
ATOM   6282 N N    . LEU B 1 292 ? 162.999 119.602 123.682 1.00 33.97  ? 292  LEU A N    1 
ATOM   6283 C CA   . LEU B 1 292 ? 164.130 119.022 122.956 1.00 35.70  ? 292  LEU A CA   1 
ATOM   6284 C C    . LEU B 1 292 ? 163.924 117.542 122.645 1.00 30.78  ? 292  LEU A C    1 
ATOM   6285 O O    . LEU B 1 292 ? 164.182 117.095 121.519 1.00 25.30  ? 292  LEU A O    1 
ATOM   6286 C CB   . LEU B 1 292 ? 165.416 119.238 123.751 1.00 37.66  ? 292  LEU A CB   1 
ATOM   6287 C CG   . LEU B 1 292 ? 165.948 120.673 123.708 1.00 29.40  ? 292  LEU A CG   1 
ATOM   6288 C CD1  . LEU B 1 292 ? 166.983 120.904 124.795 1.00 32.22  ? 292  LEU A CD1  1 
ATOM   6289 C CD2  . LEU B 1 292 ? 166.520 120.999 122.337 1.00 28.23  ? 292  LEU A CD2  1 
ATOM   6290 N N    . LEU B 1 293 ? 163.436 116.770 123.620 1.00 27.16  ? 293  LEU A N    1 
ATOM   6291 C CA   . LEU B 1 293 ? 163.112 115.370 123.353 1.00 31.18  ? 293  LEU A CA   1 
ATOM   6292 C C    . LEU B 1 293 ? 161.985 115.258 122.340 1.00 41.49  ? 293  LEU A C    1 
ATOM   6293 O O    . LEU B 1 293 ? 162.030 114.403 121.443 1.00 47.54  ? 293  LEU A O    1 
ATOM   6294 C CB   . LEU B 1 293 ? 162.781 114.613 124.642 1.00 19.91  ? 293  LEU A CB   1 
ATOM   6295 C CG   . LEU B 1 293 ? 163.915 114.109 125.553 1.00 24.84  ? 293  LEU A CG   1 
ATOM   6296 C CD1  . LEU B 1 293 ? 164.874 115.171 126.065 1.00 32.12  ? 293  LEU A CD1  1 
ATOM   6297 C CD2  . LEU B 1 293 ? 163.327 113.321 126.718 1.00 26.78  ? 293  LEU A CD2  1 
ATOM   6298 N N    . CYS B 1 294 ? 160.966 116.118 122.460 1.00 35.47  ? 294  CYS A N    1 
ATOM   6299 C CA   . CYS B 1 294 ? 159.845 116.038 121.527 1.00 26.58  ? 294  CYS A CA   1 
ATOM   6300 C C    . CYS B 1 294 ? 160.311 116.284 120.094 1.00 26.35  ? 294  CYS A C    1 
ATOM   6301 O O    . CYS B 1 294 ? 159.995 115.501 119.189 1.00 27.00  ? 294  CYS A O    1 
ATOM   6302 C CB   . CYS B 1 294 ? 158.758 117.038 121.920 1.00 24.74  ? 294  CYS A CB   1 
ATOM   6303 S SG   . CYS B 1 294 ? 157.748 116.535 123.331 1.00 50.68  ? 294  CYS A SG   1 
ATOM   6304 N N    . ARG B 1 295 ? 161.167 117.290 119.891 1.00 33.73  ? 295  ARG A N    1 
ATOM   6305 C CA   . ARG B 1 295 ? 161.657 117.561 118.540 1.00 32.33  ? 295  ARG A CA   1 
ATOM   6306 C C    . ARG B 1 295 ? 162.577 116.465 118.034 1.00 38.19  ? 295  ARG A C    1 
ATOM   6307 O O    . ARG B 1 295 ? 162.484 116.079 116.863 1.00 40.49  ? 295  ARG A O    1 
ATOM   6308 C CB   . ARG B 1 295 ? 162.408 118.884 118.456 1.00 39.03  ? 295  ARG A CB   1 
ATOM   6309 C CG   . ARG B 1 295 ? 162.051 119.696 117.229 1.00 38.75  ? 295  ARG A CG   1 
ATOM   6310 C CD   . ARG B 1 295 ? 162.535 121.113 117.355 1.00 34.96  ? 295  ARG A CD   1 
ATOM   6311 N NE   . ARG B 1 295 ? 163.985 121.161 117.487 1.00 35.00  ? 295  ARG A NE   1 
ATOM   6312 C CZ   . ARG B 1 295 ? 164.826 121.257 116.467 1.00 41.54  ? 295  ARG A CZ   1 
ATOM   6313 N NH1  . ARG B 1 295 ? 164.393 121.321 115.218 1.00 44.44  ? 295  ARG A NH1  1 
ATOM   6314 N NH2  . ARG B 1 295 ? 166.134 121.300 116.705 1.00 37.56  ? 295  ARG A NH2  1 
ATOM   6315 N N    . GLU B 1 296 ? 163.507 115.986 118.869 1.00 49.31  ? 296  GLU A N    1 
ATOM   6316 C CA   . GLU B 1 296 ? 164.442 114.977 118.384 1.00 52.17  ? 296  GLU A CA   1 
ATOM   6317 C C    . GLU B 1 296 ? 163.711 113.705 117.977 1.00 53.91  ? 296  GLU A C    1 
ATOM   6318 O O    . GLU B 1 296 ? 163.978 113.140 116.909 1.00 53.41  ? 296  GLU A O    1 
ATOM   6319 C CB   . GLU B 1 296 ? 165.479 114.679 119.468 1.00 47.63  ? 296  GLU A CB   1 
ATOM   6320 C CG   . GLU B 1 296 ? 166.533 113.659 119.088 1.00 52.07  ? 296  GLU A CG   1 
ATOM   6321 C CD   . GLU B 1 296 ? 166.826 112.697 120.228 1.00 58.24  ? 296  GLU A CD   1 
ATOM   6322 O OE1  . GLU B 1 296 ? 166.053 111.733 120.406 1.00 57.93  ? 296  GLU A OE1  1 
ATOM   6323 O OE2  . GLU B 1 296 ? 167.821 112.907 120.953 1.00 56.08  ? 296  GLU A OE2  1 
ATOM   6324 N N    . MET B 1 297 ? 162.775 113.245 118.805 1.00 42.81  ? 297  MET A N    1 
ATOM   6325 C CA   . MET B 1 297 ? 161.994 112.070 118.442 1.00 38.58  ? 297  MET A CA   1 
ATOM   6326 C C    . MET B 1 297 ? 161.133 112.292 117.201 1.00 31.83  ? 297  MET A C    1 
ATOM   6327 O O    . MET B 1 297 ? 161.011 111.379 116.376 1.00 37.76  ? 297  MET A O    1 
ATOM   6328 C CB   . MET B 1 297 ? 161.216 111.602 119.654 1.00 38.60  ? 297  MET A CB   1 
ATOM   6329 C CG   . MET B 1 297 ? 162.212 111.185 120.730 1.00 39.64  ? 297  MET A CG   1 
ATOM   6330 S SD   . MET B 1 297 ? 161.626 109.801 121.681 1.00 54.19  ? 297  MET A SD   1 
ATOM   6331 C CE   . MET B 1 297 ? 160.030 110.484 121.998 1.00 34.28  ? 297  MET A CE   1 
ATOM   6332 N N    . VAL B 1 298 ? 160.503 113.467 117.063 1.00 31.39  ? 298  VAL A N    1 
ATOM   6333 C CA   . VAL B 1 298 ? 159.708 113.737 115.865 1.00 34.61  ? 298  VAL A CA   1 
ATOM   6334 C C    . VAL B 1 298 ? 160.591 113.711 114.623 1.00 40.82  ? 298  VAL A C    1 
ATOM   6335 O O    . VAL B 1 298 ? 160.214 113.149 113.594 1.00 40.53  ? 298  VAL A O    1 
ATOM   6336 C CB   . VAL B 1 298 ? 158.937 115.063 115.993 1.00 37.25  ? 298  VAL A CB   1 
ATOM   6337 C CG1  . VAL B 1 298 ? 158.278 115.405 114.681 1.00 31.35  ? 298  VAL A CG1  1 
ATOM   6338 C CG2  . VAL B 1 298 ? 157.852 114.923 117.021 1.00 43.94  ? 298  VAL A CG2  1 
ATOM   6339 N N    . GLU B 1 299 ? 161.818 114.220 114.738 1.00 62.51  ? 299  GLU A N    1 
ATOM   6340 C CA   . GLU B 1 299 ? 162.779 114.182 113.637 1.00 63.04  ? 299  GLU A CA   1 
ATOM   6341 C C    . GLU B 1 299 ? 163.280 112.767 113.378 1.00 58.49  ? 299  GLU A C    1 
ATOM   6342 O O    . GLU B 1 299 ? 163.754 112.456 112.279 1.00 56.18  ? 299  GLU A O    1 
ATOM   6343 C CB   . GLU B 1 299 ? 163.958 115.110 113.934 1.00 60.20  ? 299  GLU A CB   1 
ATOM   6344 C CG   . GLU B 1 299 ? 163.647 116.595 113.883 1.00 60.44  ? 299  GLU A CG   1 
ATOM   6345 C CD   . GLU B 1 299 ? 163.597 117.119 112.464 1.00 64.23  ? 299  GLU A CD   1 
ATOM   6346 O OE1  . GLU B 1 299 ? 164.049 116.400 111.549 1.00 62.92  ? 299  GLU A OE1  1 
ATOM   6347 O OE2  . GLU B 1 299 ? 163.130 118.258 112.259 1.00 61.61  ? 299  GLU A OE2  1 
ATOM   6348 N N    . LEU B 1 300 ? 163.184 111.896 114.379 1.00 55.43  ? 300  LEU A N    1 
ATOM   6349 C CA   . LEU B 1 300 ? 163.706 110.543 114.231 1.00 55.49  ? 300  LEU A CA   1 
ATOM   6350 C C    . LEU B 1 300 ? 162.670 109.590 113.635 1.00 63.34  ? 300  LEU A C    1 
ATOM   6351 O O    . LEU B 1 300 ? 163.026 108.685 112.871 1.00 63.40  ? 300  LEU A O    1 
ATOM   6352 C CB   . LEU B 1 300 ? 164.194 110.042 115.597 1.00 55.20  ? 300  LEU A CB   1 
ATOM   6353 C CG   . LEU B 1 300 ? 165.097 108.820 115.814 1.00 58.48  ? 300  LEU A CG   1 
ATOM   6354 C CD1  . LEU B 1 300 ? 165.647 108.869 117.228 1.00 62.48  ? 300  LEU A CD1  1 
ATOM   6355 C CD2  . LEU B 1 300 ? 164.388 107.489 115.606 1.00 56.91  ? 300  LEU A CD2  1 
ATOM   6356 N N    . LEU B 1 301 ? 161.387 109.776 113.947 1.00 70.86  ? 301  LEU A N    1 
ATOM   6357 C CA   . LEU B 1 301 ? 160.390 108.795 113.510 1.00 63.81  ? 301  LEU A CA   1 
ATOM   6358 C C    . LEU B 1 301 ? 159.617 109.144 112.232 1.00 64.78  ? 301  LEU A C    1 
ATOM   6359 O O    . LEU B 1 301 ? 159.277 108.242 111.460 1.00 70.36  ? 301  LEU A O    1 
ATOM   6360 C CB   . LEU B 1 301 ? 159.389 108.541 114.643 1.00 56.97  ? 301  LEU A CB   1 
ATOM   6361 C CG   . LEU B 1 301 ? 159.931 107.933 115.936 1.00 60.95  ? 301  LEU A CG   1 
ATOM   6362 C CD1  . LEU B 1 301 ? 158.844 107.895 116.993 1.00 64.61  ? 301  LEU A CD1  1 
ATOM   6363 C CD2  . LEU B 1 301 ? 160.483 106.541 115.686 1.00 62.56  ? 301  LEU A CD2  1 
ATOM   6364 N N    . ASP B 1 302 ? 159.325 110.420 111.983 1.00 69.69  ? 302  ASP A N    1 
ATOM   6365 C CA   . ASP B 1 302 ? 158.631 110.769 110.740 1.00 69.77  ? 302  ASP A CA   1 
ATOM   6366 C C    . ASP B 1 302 ? 159.516 110.675 109.492 1.00 72.53  ? 302  ASP A C    1 
ATOM   6367 O O    . ASP B 1 302 ? 160.612 111.235 109.431 1.00 72.73  ? 302  ASP A O    1 
ATOM   6368 C CB   . ASP B 1 302 ? 157.931 112.142 110.852 1.00 68.52  ? 302  ASP A CB   1 
ATOM   6369 C CG   . ASP B 1 302 ? 158.872 113.348 110.932 1.00 70.24  ? 302  ASP A CG   1 
ATOM   6370 O OD1  . ASP B 1 302 ? 160.110 113.239 110.956 1.00 68.31  ? 302  ASP A OD1  1 
ATOM   6371 O OD2  . ASP B 1 302 ? 158.329 114.471 110.983 1.00 74.31  ? 302  ASP A OD2  1 
ATOM   6372 N N    . LYS B 1 303 ? 159.086 109.849 108.542 1.00 81.87  ? 303  LYS A N    1 
ATOM   6373 C CA   . LYS B 1 303 ? 159.795 109.641 107.281 1.00 83.15  ? 303  LYS A CA   1 
ATOM   6374 C C    . LYS B 1 303 ? 158.816 109.973 106.157 1.00 82.45  ? 303  LYS A C    1 
ATOM   6375 O O    . LYS B 1 303 ? 158.111 109.094 105.656 1.00 82.88  ? 303  LYS A O    1 
ATOM   6376 C CB   . LYS B 1 303 ? 160.326 108.213 107.165 1.00 82.73  ? 303  LYS A CB   1 
ATOM   6377 C CG   . LYS B 1 303 ? 161.432 107.875 108.150 1.00 80.26  ? 303  LYS A CG   1 
ATOM   6378 C CD   . LYS B 1 303 ? 161.039 106.711 109.044 1.00 79.91  ? 303  LYS A CD   1 
ATOM   6379 C CE   . LYS B 1 303 ? 162.151 106.365 110.019 1.00 79.29  ? 303  LYS A CE   1 
ATOM   6380 N NZ   . LYS B 1 303 ? 161.777 105.221 110.896 1.00 80.70  ? 303  LYS A NZ   1 
ATOM   6381 N N    . GLY B 1 304 ? 158.773 111.243 105.761 1.00 93.82  ? 304  GLY A N    1 
ATOM   6382 C CA   . GLY B 1 304 ? 157.898 111.688 104.693 1.00 93.86  ? 304  GLY A CA   1 
ATOM   6383 C C    . GLY B 1 304 ? 158.649 112.425 103.600 1.00 93.87  ? 304  GLY A C    1 
ATOM   6384 O O    . GLY B 1 304 ? 159.702 113.018 103.838 1.00 95.28  ? 304  GLY A O    1 
ATOM   6385 N N    . ASP B 1 305 ? 158.088 112.381 102.390 1.00 93.24  ? 305  ASP A N    1 
ATOM   6386 C CA   . ASP B 1 305 ? 158.681 113.004 101.213 1.00 94.63  ? 305  ASP A CA   1 
ATOM   6387 C C    . ASP B 1 305 ? 158.411 114.503 101.110 1.00 95.10  ? 305  ASP A C    1 
ATOM   6388 O O    . ASP B 1 305 ? 158.982 115.157 100.231 1.00 94.46  ? 305  ASP A O    1 
ATOM   6389 C CB   . ASP B 1 305 ? 158.165 112.304 99.950  1.00 93.08  ? 305  ASP A CB   1 
ATOM   6390 C CG   . ASP B 1 305 ? 159.064 112.521 98.748  1.00 96.07  ? 305  ASP A CG   1 
ATOM   6391 O OD1  . ASP B 1 305 ? 160.289 112.671 98.939  1.00 97.31  ? 305  ASP A OD1  1 
ATOM   6392 O OD2  . ASP B 1 305 ? 158.544 112.544 97.613  1.00 97.97  ? 305  ASP A OD2  1 
ATOM   6393 N N    . SER B 1 306 ? 157.578 115.068 101.980 1.00 88.56  ? 306  SER A N    1 
ATOM   6394 C CA   . SER B 1 306 ? 157.264 116.494 101.954 1.00 85.18  ? 306  SER A CA   1 
ATOM   6395 C C    . SER B 1 306 ? 158.154 117.240 102.939 1.00 88.06  ? 306  SER A C    1 
ATOM   6396 O O    . SER B 1 306 ? 157.991 117.106 104.157 1.00 90.66  ? 306  SER A O    1 
ATOM   6397 C CB   . SER B 1 306 ? 155.793 116.719 102.282 1.00 84.67  ? 306  SER A CB   1 
ATOM   6398 O OG   . SER B 1 306 ? 155.480 118.101 102.294 1.00 83.76  ? 306  SER A OG   1 
ATOM   6399 N N    . VAL B 1 307 ? 159.103 118.015 102.410 1.00 87.83  ? 307  VAL A N    1 
ATOM   6400 C CA   . VAL B 1 307 ? 160.017 118.756 103.273 1.00 88.96  ? 307  VAL A CA   1 
ATOM   6401 C C    . VAL B 1 307 ? 159.284 119.856 104.038 1.00 84.83  ? 307  VAL A C    1 
ATOM   6402 O O    . VAL B 1 307 ? 159.566 120.094 105.218 1.00 83.47  ? 307  VAL A O    1 
ATOM   6403 C CB   . VAL B 1 307 ? 161.186 119.322 102.445 1.00 85.28  ? 307  VAL A CB   1 
ATOM   6404 C CG1  . VAL B 1 307 ? 162.247 118.255 102.234 1.00 84.36  ? 307  VAL A CG1  1 
ATOM   6405 C CG2  . VAL B 1 307 ? 160.689 119.846 101.105 1.00 81.16  ? 307  VAL A CG2  1 
ATOM   6406 N N    . VAL B 1 308 ? 158.367 120.570 103.373 1.00 73.41  ? 308  VAL A N    1 
ATOM   6407 C CA   . VAL B 1 308 ? 157.638 121.655 104.032 1.00 74.45  ? 308  VAL A CA   1 
ATOM   6408 C C    . VAL B 1 308 ? 156.790 121.122 105.183 1.00 74.67  ? 308  VAL A C    1 
ATOM   6409 O O    . VAL B 1 308 ? 156.763 121.697 106.281 1.00 74.76  ? 308  VAL A O    1 
ATOM   6410 C CB   . VAL B 1 308 ? 156.781 122.421 103.009 1.00 78.61  ? 308  VAL A CB   1 
ATOM   6411 C CG1  . VAL B 1 308 ? 156.324 123.751 103.588 1.00 78.08  ? 308  VAL A CG1  1 
ATOM   6412 C CG2  . VAL B 1 308 ? 157.559 122.632 101.720 1.00 75.29  ? 308  VAL A CG2  1 
ATOM   6413 N N    . ASN B 1 309 ? 156.086 120.009 104.946 1.00 76.04  ? 309  ASN A N    1 
ATOM   6414 C CA   . ASN B 1 309 ? 155.319 119.371 106.011 1.00 79.97  ? 309  ASN A CA   1 
ATOM   6415 C C    . ASN B 1 309 ? 156.226 118.863 107.126 1.00 79.35  ? 309  ASN A C    1 
ATOM   6416 O O    . ASN B 1 309 ? 155.868 118.947 108.306 1.00 78.60  ? 309  ASN A O    1 
ATOM   6417 C CB   . ASN B 1 309 ? 154.430 118.257 105.445 1.00 79.60  ? 309  ASN A CB   1 
ATOM   6418 C CG   . ASN B 1 309 ? 153.254 118.802 104.626 1.00 79.56  ? 309  ASN A CG   1 
ATOM   6419 O OD1  . ASN B 1 309 ? 153.098 120.016 104.490 1.00 74.66  ? 309  ASN A OD1  1 
ATOM   6420 N ND2  . ASN B 1 309 ? 152.414 117.891 104.100 1.00 83.51  ? 309  ASN A ND2  1 
ATOM   6421 N N    . HIS B 1 310 ? 157.408 118.345 106.774 1.00 74.02  ? 310  HIS A N    1 
ATOM   6422 C CA   . HIS B 1 310 ? 158.355 117.885 107.788 1.00 72.86  ? 310  HIS A CA   1 
ATOM   6423 C C    . HIS B 1 310 ? 158.810 119.036 108.679 1.00 74.95  ? 310  HIS A C    1 
ATOM   6424 O O    . HIS B 1 310 ? 158.836 118.914 109.913 1.00 71.28  ? 310  HIS A O    1 
ATOM   6425 C CB   . HIS B 1 310 ? 159.558 117.246 107.093 1.00 69.37  ? 310  HIS A CB   1 
ATOM   6426 C CG   . HIS B 1 310 ? 160.385 116.370 107.979 1.00 76.87  ? 310  HIS A CG   1 
ATOM   6427 N ND1  . HIS B 1 310 ? 161.684 116.674 108.322 1.00 79.45  ? 310  HIS A ND1  1 
ATOM   6428 C CD2  . HIS B 1 310 ? 160.110 115.181 108.561 1.00 76.01  ? 310  HIS A CD2  1 
ATOM   6429 C CE1  . HIS B 1 310 ? 162.167 115.720 109.097 1.00 74.07  ? 310  HIS A CE1  1 
ATOM   6430 N NE2  . HIS B 1 310 ? 161.231 114.801 109.258 1.00 74.81  ? 310  HIS A NE2  1 
ATOM   6431 N N    . THR B 1 311 ? 159.108 120.183 108.065 1.00 63.73  ? 311  THR A N    1 
ATOM   6432 C CA   . THR B 1 311 ? 159.562 121.362 108.795 1.00 57.80  ? 311  THR A CA   1 
ATOM   6433 C C    . THR B 1 311 ? 158.469 121.890 109.712 1.00 64.96  ? 311  THR A C    1 
ATOM   6434 O O    . THR B 1 311 ? 158.712 122.172 110.895 1.00 69.41  ? 311  THR A O    1 
ATOM   6435 C CB   . THR B 1 311 ? 160.017 122.444 107.816 1.00 62.62  ? 311  THR A CB   1 
ATOM   6436 O OG1  . THR B 1 311 ? 160.970 121.891 106.900 1.00 69.42  ? 311  THR A OG1  1 
ATOM   6437 C CG2  . THR B 1 311 ? 160.658 123.601 108.566 1.00 61.77  ? 311  THR A CG2  1 
ATOM   6438 N N    . SER B 1 312 ? 157.256 122.038 109.173 1.00 60.69  ? 312  SER A N    1 
ATOM   6439 C CA   . SER B 1 312 ? 156.138 122.529 109.972 1.00 59.00  ? 312  SER A CA   1 
ATOM   6440 C C    . SER B 1 312 ? 155.801 121.581 111.118 1.00 57.67  ? 312  SER A C    1 
ATOM   6441 O O    . SER B 1 312 ? 155.519 122.035 112.233 1.00 59.30  ? 312  SER A O    1 
ATOM   6442 C CB   . SER B 1 312 ? 154.918 122.748 109.080 1.00 54.55  ? 312  SER A CB   1 
ATOM   6443 O OG   . SER B 1 312 ? 154.892 124.072 108.575 1.00 55.14  ? 312  SER A OG   1 
ATOM   6444 N N    . LEU B 1 313 ? 155.795 120.267 110.868 1.00 47.06  ? 313  LEU A N    1 
ATOM   6445 C CA   . LEU B 1 313 ? 155.506 119.327 111.946 1.00 43.10  ? 313  LEU A CA   1 
ATOM   6446 C C    . LEU B 1 313 ? 156.569 119.368 113.036 1.00 46.30  ? 313  LEU A C    1 
ATOM   6447 O O    . LEU B 1 313 ? 156.240 119.321 114.227 1.00 57.56  ? 313  LEU A O    1 
ATOM   6448 C CB   . LEU B 1 313 ? 155.389 117.912 111.379 1.00 49.78  ? 313  LEU A CB   1 
ATOM   6449 C CG   . LEU B 1 313 ? 154.832 116.813 112.285 1.00 52.33  ? 313  LEU A CG   1 
ATOM   6450 C CD1  . LEU B 1 313 ? 153.475 117.187 112.841 1.00 44.78  ? 313  LEU A CD1  1 
ATOM   6451 C CD2  . LEU B 1 313 ? 154.756 115.495 111.533 1.00 55.12  ? 313  LEU A CD2  1 
ATOM   6452 N N    . SER B 1 314 ? 157.846 119.490 112.657 1.00 35.83  ? 314  SER A N    1 
ATOM   6453 C CA   . SER B 1 314 ? 158.900 119.598 113.665 1.00 43.19  ? 314  SER A CA   1 
ATOM   6454 C C    . SER B 1 314 ? 158.768 120.870 114.499 1.00 40.51  ? 314  SER A C    1 
ATOM   6455 O O    . SER B 1 314 ? 158.903 120.835 115.734 1.00 31.06  ? 314  SER A O    1 
ATOM   6456 C CB   . SER B 1 314 ? 160.272 119.531 112.999 1.00 44.14  ? 314  SER A CB   1 
ATOM   6457 O OG   . SER B 1 314 ? 160.246 120.131 111.719 1.00 48.66  ? 314  SER A OG   1 
ATOM   6458 N N    . ASN B 1 315 ? 158.472 122.000 113.847 1.00 32.92  ? 315  ASN A N    1 
ATOM   6459 C CA   . ASN B 1 315 ? 158.293 123.241 114.595 1.00 31.74  ? 315  ASN A CA   1 
ATOM   6460 C C    . ASN B 1 315 ? 157.077 123.177 115.512 1.00 42.79  ? 315  ASN A C    1 
ATOM   6461 O O    . ASN B 1 315 ? 157.130 123.668 116.650 1.00 51.58  ? 315  ASN A O    1 
ATOM   6462 C CB   . ASN B 1 315 ? 158.179 124.416 113.627 1.00 29.90  ? 315  ASN A CB   1 
ATOM   6463 C CG   . ASN B 1 315 ? 159.476 124.687 112.891 1.00 34.91  ? 315  ASN A CG   1 
ATOM   6464 O OD1  . ASN B 1 315 ? 160.552 124.303 113.348 1.00 36.78  ? 315  ASN A OD1  1 
ATOM   6465 N ND2  . ASN B 1 315 ? 159.380 125.349 111.745 1.00 42.25  ? 315  ASN A ND2  1 
ATOM   6466 N N    . TYR B 1 316 ? 155.963 122.613 115.032 1.00 29.53  ? 316  TYR A N    1 
ATOM   6467 C CA   . TYR B 1 316 ? 154.782 122.513 115.882 1.00 25.65  ? 316  TYR A CA   1 
ATOM   6468 C C    . TYR B 1 316 ? 155.060 121.603 117.070 1.00 23.31  ? 316  TYR A C    1 
ATOM   6469 O O    . TYR B 1 316 ? 154.584 121.853 118.186 1.00 33.62  ? 316  TYR A O    1 
ATOM   6470 C CB   . TYR B 1 316 ? 153.593 122.004 115.068 1.00 28.54  ? 316  TYR A CB   1 
ATOM   6471 C CG   . TYR B 1 316 ? 152.346 121.754 115.881 1.00 28.37  ? 316  TYR A CG   1 
ATOM   6472 C CD1  . TYR B 1 316 ? 151.799 122.753 116.673 1.00 20.11  ? 316  TYR A CD1  1 
ATOM   6473 C CD2  . TYR B 1 316 ? 151.709 120.522 115.849 1.00 32.68  ? 316  TYR A CD2  1 
ATOM   6474 C CE1  . TYR B 1 316 ? 150.658 122.530 117.414 1.00 20.49  ? 316  TYR A CE1  1 
ATOM   6475 C CE2  . TYR B 1 316 ? 150.567 120.290 116.587 1.00 28.84  ? 316  TYR A CE2  1 
ATOM   6476 C CZ   . TYR B 1 316 ? 150.047 121.297 117.367 1.00 27.22  ? 316  TYR A CZ   1 
ATOM   6477 O OH   . TYR B 1 316 ? 148.909 121.070 118.104 1.00 35.90  ? 316  TYR A OH   1 
ATOM   6478 N N    . ALA B 1 317 ? 155.858 120.551 116.847 1.00 12.19  ? 317  ALA A N    1 
ATOM   6479 C CA   . ALA B 1 317 ? 156.214 119.643 117.928 1.00 8.16   ? 317  ALA A CA   1 
ATOM   6480 C C    . ALA B 1 317 ? 157.023 120.365 118.990 1.00 20.17  ? 317  ALA A C    1 
ATOM   6481 O O    . ALA B 1 317 ? 156.841 120.127 120.190 1.00 35.61  ? 317  ALA A O    1 
ATOM   6482 C CB   . ALA B 1 317 ? 156.995 118.454 117.377 1.00 25.87  ? 317  ALA A CB   1 
ATOM   6483 N N    . PHE B 1 318 ? 157.944 121.233 118.562 1.00 19.42  ? 318  PHE A N    1 
ATOM   6484 C CA   . PHE B 1 318 ? 158.727 122.006 119.524 1.00 19.20  ? 318  PHE A CA   1 
ATOM   6485 C C    . PHE B 1 318 ? 157.833 122.950 120.316 1.00 19.03  ? 318  PHE A C    1 
ATOM   6486 O O    . PHE B 1 318 ? 157.908 123.014 121.548 1.00 25.66  ? 318  PHE A O    1 
ATOM   6487 C CB   . PHE B 1 318 ? 159.829 122.791 118.812 1.00 18.75  ? 318  PHE A CB   1 
ATOM   6488 C CG   . PHE B 1 318 ? 160.714 123.584 119.742 1.00 16.70  ? 318  PHE A CG   1 
ATOM   6489 C CD1  . PHE B 1 318 ? 160.414 124.894 120.080 1.00 18.36  ? 318  PHE A CD1  1 
ATOM   6490 C CD2  . PHE B 1 318 ? 161.853 123.009 120.280 1.00 26.46  ? 318  PHE A CD2  1 
ATOM   6491 C CE1  . PHE B 1 318 ? 161.229 125.606 120.937 1.00 27.80  ? 318  PHE A CE1  1 
ATOM   6492 C CE2  . PHE B 1 318 ? 162.673 123.720 121.135 1.00 28.49  ? 318  PHE A CE2  1 
ATOM   6493 C CZ   . PHE B 1 318 ? 162.360 125.020 121.463 1.00 27.28  ? 318  PHE A CZ   1 
ATOM   6494 N N    . LEU B 1 319 ? 156.994 123.712 119.609 1.00 23.67  ? 319  LEU A N    1 
ATOM   6495 C CA   . LEU B 1 319 ? 156.132 124.701 120.252 1.00 21.90  ? 319  LEU A CA   1 
ATOM   6496 C C    . LEU B 1 319 ? 155.127 124.072 121.214 1.00 18.13  ? 319  LEU A C    1 
ATOM   6497 O O    . LEU B 1 319 ? 154.700 124.726 122.173 1.00 18.61  ? 319  LEU A O    1 
ATOM   6498 C CB   . LEU B 1 319 ? 155.407 125.517 119.179 1.00 15.04  ? 319  LEU A CB   1 
ATOM   6499 C CG   . LEU B 1 319 ? 154.454 126.632 119.611 1.00 22.64  ? 319  LEU A CG   1 
ATOM   6500 C CD1  . LEU B 1 319 ? 155.228 127.793 120.213 1.00 27.23  ? 319  LEU A CD1  1 
ATOM   6501 C CD2  . LEU B 1 319 ? 153.609 127.094 118.437 1.00 26.03  ? 319  LEU A CD2  1 
ATOM   6502 N N    . TYR B 1 320 ? 154.738 122.815 120.982 1.00 22.89  ? 320  TYR A N    1 
ATOM   6503 C CA   . TYR B 1 320 ? 153.745 122.172 121.843 1.00 13.46  ? 320  TYR A CA   1 
ATOM   6504 C C    . TYR B 1 320 ? 154.227 121.999 123.284 1.00 11.65  ? 320  TYR A C    1 
ATOM   6505 O O    . TYR B 1 320 ? 153.455 122.213 124.225 1.00 31.65  ? 320  TYR A O    1 
ATOM   6506 C CB   . TYR B 1 320 ? 153.335 120.816 121.264 1.00 27.13  ? 320  TYR A CB   1 
ATOM   6507 C CG   . TYR B 1 320 ? 152.716 119.890 122.290 1.00 21.15  ? 320  TYR A CG   1 
ATOM   6508 C CD1  . TYR B 1 320 ? 151.374 120.007 122.623 1.00 22.59  ? 320  TYR A CD1  1 
ATOM   6509 C CD2  . TYR B 1 320 ? 153.462 118.897 122.920 1.00 19.20  ? 320  TYR A CD2  1 
ATOM   6510 C CE1  . TYR B 1 320 ? 150.794 119.178 123.555 1.00 25.40  ? 320  TYR A CE1  1 
ATOM   6511 C CE2  . TYR B 1 320 ? 152.889 118.068 123.863 1.00 23.18  ? 320  TYR A CE2  1 
ATOM   6512 C CZ   . TYR B 1 320 ? 151.554 118.211 124.172 1.00 23.34  ? 320  TYR A CZ   1 
ATOM   6513 O OH   . TYR B 1 320 ? 150.971 117.387 125.104 1.00 29.57  ? 320  TYR A OH   1 
ATOM   6514 N N    . GLY B 1 321 ? 155.490 121.617 123.485 1.00 6.49   ? 321  GLY A N    1 
ATOM   6515 C CA   . GLY B 1 321 ? 155.974 121.310 124.826 1.00 24.50  ? 321  GLY A CA   1 
ATOM   6516 C C    . GLY B 1 321 ? 156.225 122.498 125.735 1.00 27.10  ? 321  GLY A C    1 
ATOM   6517 O O    . GLY B 1 321 ? 156.316 122.317 126.954 1.00 32.89  ? 321  GLY A O    1 
ATOM   6518 N N    . VAL B 1 322 ? 156.350 123.702 125.179 1.00 14.20  ? 322  VAL A N    1 
ATOM   6519 C CA   . VAL B 1 322 ? 156.655 124.895 125.966 1.00 0.00   ? 322  VAL A CA   1 
ATOM   6520 C C    . VAL B 1 322 ? 155.514 125.324 126.892 1.00 8.63   ? 322  VAL A C    1 
ATOM   6521 O O    . VAL B 1 322 ? 155.744 126.113 127.817 1.00 26.78  ? 322  VAL A O    1 
ATOM   6522 C CB   . VAL B 1 322 ? 157.088 125.973 124.944 1.00 7.31   ? 322  VAL A CB   1 
ATOM   6523 C CG1  . VAL B 1 322 ? 157.315 127.333 125.567 1.00 21.17  ? 322  VAL A CG1  1 
ATOM   6524 C CG2  . VAL B 1 322 ? 158.345 125.523 124.218 1.00 16.73  ? 322  VAL A CG2  1 
ATOM   6525 N N    . PHE B 1 323 ? 154.317 124.761 126.726 1.00 0.77   ? 323  PHE A N    1 
ATOM   6526 C CA   . PHE B 1 323 ? 153.148 125.190 127.493 1.00 3.96   ? 323  PHE A CA   1 
ATOM   6527 C C    . PHE B 1 323 ? 153.345 125.026 129.003 1.00 9.01   ? 323  PHE A C    1 
ATOM   6528 O O    . PHE B 1 323 ? 153.984 124.067 129.451 1.00 13.30  ? 323  PHE A O    1 
ATOM   6529 C CB   . PHE B 1 323 ? 151.921 124.388 127.050 1.00 6.17   ? 323  PHE A CB   1 
ATOM   6530 C CG   . PHE B 1 323 ? 151.508 124.632 125.624 1.00 14.93  ? 323  PHE A CG   1 
ATOM   6531 C CD1  . PHE B 1 323 ? 151.874 125.793 124.962 1.00 15.82  ? 323  PHE A CD1  1 
ATOM   6532 C CD2  . PHE B 1 323 ? 150.760 123.689 124.940 1.00 21.93  ? 323  PHE A CD2  1 
ATOM   6533 C CE1  . PHE B 1 323 ? 151.497 126.008 123.651 1.00 14.69  ? 323  PHE A CE1  1 
ATOM   6534 C CE2  . PHE B 1 323 ? 150.383 123.898 123.629 1.00 17.81  ? 323  PHE A CE2  1 
ATOM   6535 C CZ   . PHE B 1 323 ? 150.751 125.060 122.985 1.00 12.20  ? 323  PHE A CZ   1 
ATOM   6536 N N    . PRO B 1 324 ? 152.816 125.952 129.807 1.00 1.08   ? 324  PRO A N    1 
ATOM   6537 C CA   . PRO B 1 324 ? 152.985 125.896 131.268 1.00 4.60   ? 324  PRO A CA   1 
ATOM   6538 C C    . PRO B 1 324 ? 152.238 124.739 131.923 1.00 14.02  ? 324  PRO A C    1 
ATOM   6539 O O    . PRO B 1 324 ? 151.404 124.062 131.321 1.00 30.85  ? 324  PRO A O    1 
ATOM   6540 C CB   . PRO B 1 324 ? 152.441 127.246 131.738 1.00 6.88   ? 324  PRO A CB   1 
ATOM   6541 C CG   . PRO B 1 324 ? 151.500 127.658 130.688 1.00 12.85  ? 324  PRO A CG   1 
ATOM   6542 C CD   . PRO B 1 324 ? 152.042 127.134 129.392 1.00 14.82  ? 324  PRO A CD   1 
ATOM   6543 N N    . VAL B 1 325 ? 152.582 124.519 133.197 1.00 10.17  ? 325  VAL A N    1 
ATOM   6544 C CA   . VAL B 1 325 ? 151.982 123.455 133.998 1.00 14.28  ? 325  VAL A CA   1 
ATOM   6545 C C    . VAL B 1 325 ? 150.488 123.702 134.188 1.00 30.21  ? 325  VAL A C    1 
ATOM   6546 O O    . VAL B 1 325 ? 150.055 124.825 134.479 1.00 32.84  ? 325  VAL A O    1 
ATOM   6547 C CB   . VAL B 1 325 ? 152.696 123.359 135.357 1.00 5.07   ? 325  VAL A CB   1 
ATOM   6548 C CG1  . VAL B 1 325 ? 152.109 122.241 136.206 1.00 0.00   ? 325  VAL A CG1  1 
ATOM   6549 C CG2  . VAL B 1 325 ? 154.185 123.166 135.164 1.00 10.77  ? 325  VAL A CG2  1 
ATOM   6550 N N    . ALA B 1 326 ? 149.693 122.645 134.007 1.00 30.79  ? 326  ALA A N    1 
ATOM   6551 C CA   . ALA B 1 326 ? 148.241 122.750 134.103 1.00 14.92  ? 326  ALA A CA   1 
ATOM   6552 C C    . ALA B 1 326 ? 147.809 123.083 135.532 1.00 22.84  ? 326  ALA A C    1 
ATOM   6553 O O    . ALA B 1 326 ? 148.377 122.554 136.492 1.00 25.10  ? 326  ALA A O    1 
ATOM   6554 C CB   . ALA B 1 326 ? 147.588 121.441 133.659 1.00 10.50  ? 326  ALA A CB   1 
ATOM   6555 N N    . PRO B 1 327 ? 146.820 123.969 135.703 1.00 24.05  ? 327  PRO A N    1 
ATOM   6556 C CA   . PRO B 1 327 ? 146.361 124.324 137.058 1.00 17.54  ? 327  PRO A CA   1 
ATOM   6557 C C    . PRO B 1 327 ? 145.727 123.190 137.854 1.00 21.08  ? 327  PRO A C    1 
ATOM   6558 O O    . PRO B 1 327 ? 145.622 123.312 139.080 1.00 31.61  ? 327  PRO A O    1 
ATOM   6559 C CB   . PRO B 1 327 ? 145.354 125.457 136.799 1.00 13.21  ? 327  PRO A CB   1 
ATOM   6560 C CG   . PRO B 1 327 ? 145.370 125.690 135.298 1.00 23.54  ? 327  PRO A CG   1 
ATOM   6561 C CD   . PRO B 1 327 ? 145.869 124.441 134.686 1.00 25.52  ? 327  PRO A CD   1 
ATOM   6562 N N    . GLY B 1 328 ? 145.292 122.103 137.212 1.00 17.58  ? 328  GLY A N    1 
ATOM   6563 C CA   . GLY B 1 328 ? 144.686 120.997 137.939 1.00 18.52  ? 328  GLY A CA   1 
ATOM   6564 C C    . GLY B 1 328 ? 145.611 120.295 138.914 1.00 20.54  ? 328  GLY A C    1 
ATOM   6565 O O    . GLY B 1 328 ? 145.134 119.651 139.858 1.00 29.68  ? 328  GLY A O    1 
ATOM   6566 N N    . VAL B 1 329 ? 146.923 120.393 138.700 1.00 21.76  ? 329  VAL A N    1 
ATOM   6567 C CA   . VAL B 1 329 ? 147.883 119.770 139.605 1.00 25.54  ? 329  VAL A CA   1 
ATOM   6568 C C    . VAL B 1 329 ? 147.787 120.377 141.001 1.00 31.99  ? 329  VAL A C    1 
ATOM   6569 O O    . VAL B 1 329 ? 147.840 119.661 142.008 1.00 41.88  ? 329  VAL A O    1 
ATOM   6570 C CB   . VAL B 1 329 ? 149.307 119.875 139.031 1.00 24.34  ? 329  VAL A CB   1 
ATOM   6571 C CG1  . VAL B 1 329 ? 150.264 119.025 139.842 1.00 17.32  ? 329  VAL A CG1  1 
ATOM   6572 C CG2  . VAL B 1 329 ? 149.320 119.446 137.577 1.00 24.89  ? 329  VAL A CG2  1 
ATOM   6573 N N    . ALA B 1 330 ? 147.683 121.708 141.089 1.00 33.16  ? 330  ALA A N    1 
ATOM   6574 C CA   . ALA B 1 330 ? 147.464 122.338 142.389 1.00 31.75  ? 330  ALA A CA   1 
ATOM   6575 C C    . ALA B 1 330 ? 146.139 121.930 143.028 1.00 39.66  ? 330  ALA A C    1 
ATOM   6576 O O    . ALA B 1 330 ? 146.057 121.837 144.257 1.00 41.74  ? 330  ALA A O    1 
ATOM   6577 C CB   . ALA B 1 330 ? 147.531 123.858 142.248 1.00 32.12  ? 330  ALA A CB   1 
ATOM   6578 N N    . ILE B 1 331 ? 145.093 121.696 142.229 1.00 40.66  ? 331  ILE A N    1 
ATOM   6579 C CA   . ILE B 1 331 ? 143.837 121.177 142.774 1.00 35.28  ? 331  ILE A CA   1 
ATOM   6580 C C    . ILE B 1 331 ? 144.052 119.799 143.392 1.00 31.16  ? 331  ILE A C    1 
ATOM   6581 O O    . ILE B 1 331 ? 143.543 119.495 144.481 1.00 39.15  ? 331  ILE A O    1 
ATOM   6582 C CB   . ILE B 1 331 ? 142.744 121.162 141.688 1.00 41.91  ? 331  ILE A CB   1 
ATOM   6583 C CG1  . ILE B 1 331 ? 142.417 122.593 141.254 1.00 32.72  ? 331  ILE A CG1  1 
ATOM   6584 C CG2  . ILE B 1 331 ? 141.489 120.473 142.192 1.00 41.09  ? 331  ILE A CG2  1 
ATOM   6585 C CD1  . ILE B 1 331 ? 141.585 122.680 139.995 1.00 34.86  ? 331  ILE A CD1  1 
ATOM   6586 N N    . PHE B 1 332 ? 144.821 118.952 142.703 1.00 35.15  ? 332  PHE A N    1 
ATOM   6587 C CA   . PHE B 1 332 ? 145.147 117.623 143.222 1.00 40.83  ? 332  PHE A CA   1 
ATOM   6588 C C    . PHE B 1 332 ? 145.958 117.721 144.509 1.00 43.26  ? 332  PHE A C    1 
ATOM   6589 O O    . PHE B 1 332 ? 145.750 116.944 145.449 1.00 41.31  ? 332  PHE A O    1 
ATOM   6590 C CB   . PHE B 1 332 ? 145.916 116.802 142.178 1.00 37.20  ? 332  PHE A CB   1 
ATOM   6591 C CG   . PHE B 1 332 ? 145.121 116.429 140.939 1.00 40.43  ? 332  PHE A CG   1 
ATOM   6592 C CD1  . PHE B 1 332 ? 145.652 115.523 140.036 1.00 32.83  ? 332  PHE A CD1  1 
ATOM   6593 C CD2  . PHE B 1 332 ? 143.838 116.909 140.709 1.00 51.97  ? 332  PHE A CD2  1 
ATOM   6594 C CE1  . PHE B 1 332 ? 144.952 115.148 138.907 1.00 38.66  ? 332  PHE A CE1  1 
ATOM   6595 C CE2  . PHE B 1 332 ? 143.133 116.538 139.580 1.00 51.54  ? 332  PHE A CE2  1 
ATOM   6596 C CZ   . PHE B 1 332 ? 143.690 115.653 138.680 1.00 45.92  ? 332  PHE A CZ   1 
ATOM   6597 N N    . ALA B 1 333 ? 146.899 118.662 144.560 1.00 52.40  ? 333  ALA A N    1 
ATOM   6598 C CA   . ALA B 1 333 ? 147.675 118.869 145.778 1.00 46.40  ? 333  ALA A CA   1 
ATOM   6599 C C    . ALA B 1 333 ? 146.794 119.347 146.926 1.00 50.98  ? 333  ALA A C    1 
ATOM   6600 O O    . ALA B 1 333 ? 146.972 118.911 148.068 1.00 55.70  ? 333  ALA A O    1 
ATOM   6601 C CB   . ALA B 1 333 ? 148.804 119.865 145.519 1.00 45.00  ? 333  ALA A CB   1 
ATOM   6602 N N    . THR B 1 334 ? 145.859 120.263 146.651 1.00 57.76  ? 334  THR A N    1 
ATOM   6603 C CA   . THR B 1 334 ? 144.970 120.755 147.701 1.00 58.64  ? 334  THR A CA   1 
ATOM   6604 C C    . THR B 1 334 ? 144.081 119.645 148.241 1.00 52.98  ? 334  THR A C    1 
ATOM   6605 O O    . THR B 1 334 ? 143.915 119.510 149.460 1.00 45.54  ? 334  THR A O    1 
ATOM   6606 C CB   . THR B 1 334 ? 144.132 121.920 147.164 1.00 58.82  ? 334  THR A CB   1 
ATOM   6607 O OG1  . THR B 1 334 ? 144.908 123.123 147.211 1.00 54.39  ? 334  THR A OG1  1 
ATOM   6608 C CG2  . THR B 1 334 ? 142.858 122.115 147.981 1.00 56.72  ? 334  THR A CG2  1 
ATOM   6609 N N    . GLN B 1 335 ? 143.512 118.832 147.351 1.00 66.61  ? 335  GLN A N    1 
ATOM   6610 C CA   . GLN B 1 335 ? 142.695 117.700 147.776 1.00 69.37  ? 335  GLN A CA   1 
ATOM   6611 C C    . GLN B 1 335 ? 143.519 116.694 148.583 1.00 71.33  ? 335  GLN A C    1 
ATOM   6612 O O    . GLN B 1 335 ? 143.044 116.168 149.594 1.00 74.58  ? 335  GLN A O    1 
ATOM   6613 C CB   . GLN B 1 335 ? 141.967 117.059 146.579 1.00 69.84  ? 335  GLN A CB   1 
ATOM   6614 C CG   . GLN B 1 335 ? 142.737 116.113 145.678 1.00 69.38  ? 335  GLN A CG   1 
ATOM   6615 C CD   . GLN B 1 335 ? 141.815 115.210 144.878 1.00 75.09  ? 335  GLN A CD   1 
ATOM   6616 O OE1  . GLN B 1 335 ? 142.018 113.999 144.805 1.00 75.83  ? 335  GLN A OE1  1 
ATOM   6617 N NE2  . GLN B 1 335 ? 140.796 115.803 144.266 1.00 73.26  ? 335  GLN A NE2  1 
ATOM   6618 N N    . PHE B 1 336 ? 144.754 116.405 148.151 1.00 74.40  ? 336  PHE A N    1 
ATOM   6619 C CA   . PHE B 1 336 ? 145.562 115.474 148.932 1.00 75.37  ? 336  PHE A CA   1 
ATOM   6620 C C    . PHE B 1 336 ? 146.210 116.115 150.167 1.00 73.07  ? 336  PHE A C    1 
ATOM   6621 O O    . PHE B 1 336 ? 146.710 115.381 151.028 1.00 68.55  ? 336  PHE A O    1 
ATOM   6622 C CB   . PHE B 1 336 ? 146.615 114.859 148.011 1.00 73.27  ? 336  PHE A CB   1 
ATOM   6623 C CG   . PHE B 1 336 ? 146.231 113.510 147.473 1.00 70.11  ? 336  PHE A CG   1 
ATOM   6624 C CD1  . PHE B 1 336 ? 145.082 113.363 146.709 1.00 70.55  ? 336  PHE A CD1  1 
ATOM   6625 C CD2  . PHE B 1 336 ? 147.004 112.396 147.724 1.00 70.78  ? 336  PHE A CD2  1 
ATOM   6626 C CE1  . PHE B 1 336 ? 144.715 112.128 146.204 1.00 74.47  ? 336  PHE A CE1  1 
ATOM   6627 C CE2  . PHE B 1 336 ? 146.643 111.156 147.222 1.00 73.24  ? 336  PHE A CE2  1 
ATOM   6628 C CZ   . PHE B 1 336 ? 145.499 111.022 146.463 1.00 76.26  ? 336  PHE A CZ   1 
ATOM   6629 N N    . ASN B 1 337 ? 146.286 117.452 150.230 1.00 77.69  ? 337  ASN A N    1 
ATOM   6630 C CA   . ASN B 1 337 ? 146.902 118.262 151.314 1.00 78.15  ? 337  ASN A CA   1 
ATOM   6631 C C    . ASN B 1 337 ? 148.308 117.798 151.730 1.00 78.62  ? 337  ASN A C    1 
ATOM   6632 O O    . ASN B 1 337 ? 148.504 117.339 152.857 1.00 79.27  ? 337  ASN A O    1 
ATOM   6633 C CB   . ASN B 1 337 ? 146.045 118.535 152.584 1.00 79.58  ? 337  ASN A CB   1 
ATOM   6634 C CG   . ASN B 1 337 ? 145.172 117.378 153.126 1.00 81.13  ? 337  ASN A CG   1 
ATOM   6635 O OD1  . ASN B 1 337 ? 144.736 116.458 152.457 1.00 80.44  ? 337  ASN A OD1  1 
ATOM   6636 N ND2  . ASN B 1 337 ? 144.931 117.464 154.428 1.00 78.70  ? 337  ASN A ND2  1 
ATOM   6637 N N    . MET B 1 338 ? 149.298 117.889 150.839 1.00 71.75  ? 338  MET A N    1 
ATOM   6638 C CA   . MET B 1 338 ? 150.638 117.430 151.204 1.00 73.55  ? 338  MET A CA   1 
ATOM   6639 C C    . MET B 1 338 ? 151.766 118.206 150.527 1.00 75.61  ? 338  MET A C    1 
ATOM   6640 O O    . MET B 1 338 ? 152.850 118.327 151.100 1.00 78.73  ? 338  MET A O    1 
ATOM   6641 C CB   . MET B 1 338 ? 150.702 115.931 150.870 1.00 70.84  ? 338  MET A CB   1 
ATOM   6642 C CG   . MET B 1 338 ? 152.047 115.197 150.923 1.00 71.42  ? 338  MET A CG   1 
ATOM   6643 S SD   . MET B 1 338 ? 153.130 115.556 152.325 1.00 76.97  ? 338  MET A SD   1 
ATOM   6644 C CE   . MET B 1 338 ? 154.757 115.505 151.572 1.00 72.30  ? 338  MET A CE   1 
ATOM   6645 N N    . GLU B 1 339 ? 151.544 118.807 149.359 1.00 64.56  ? 339  GLU A N    1 
ATOM   6646 C CA   . GLU B 1 339 ? 152.576 119.611 148.680 1.00 59.75  ? 339  GLU A CA   1 
ATOM   6647 C C    . GLU B 1 339 ? 151.990 120.859 148.027 1.00 60.43  ? 339  GLU A C    1 
ATOM   6648 O O    . GLU B 1 339 ? 152.410 121.262 146.943 1.00 56.90  ? 339  GLU A O    1 
ATOM   6649 C CB   . GLU B 1 339 ? 153.380 118.823 147.643 1.00 57.96  ? 339  GLU A CB   1 
ATOM   6650 C CG   . GLU B 1 339 ? 153.743 117.398 148.018 1.00 64.41  ? 339  GLU A CG   1 
ATOM   6651 C CD   . GLU B 1 339 ? 155.191 117.082 147.716 1.00 65.58  ? 339  GLU A CD   1 
ATOM   6652 O OE1  . GLU B 1 339 ? 155.686 117.514 146.658 1.00 66.29  ? 339  GLU A OE1  1 
ATOM   6653 O OE2  . GLU B 1 339 ? 155.841 116.421 148.551 1.00 67.25  ? 339  GLU A OE2  1 
ATOM   6654 N N    . VAL B 1 340 ? 151.021 121.502 148.679 1.00 54.29  ? 340  VAL A N    1 
ATOM   6655 C CA   . VAL B 1 340 ? 150.358 122.665 148.082 1.00 52.00  ? 340  VAL A CA   1 
ATOM   6656 C C    . VAL B 1 340 ? 151.318 123.832 147.851 1.00 47.38  ? 340  VAL A C    1 
ATOM   6657 O O    . VAL B 1 340 ? 151.273 124.484 146.801 1.00 48.56  ? 340  VAL A O    1 
ATOM   6658 C CB   . VAL B 1 340 ? 149.178 123.106 148.963 1.00 52.50  ? 340  VAL A CB   1 
ATOM   6659 C CG1  . VAL B 1 340 ? 148.001 122.226 148.715 1.00 53.20  ? 340  VAL A CG1  1 
ATOM   6660 C CG2  . VAL B 1 340 ? 149.563 123.050 150.437 1.00 51.97  ? 340  VAL A CG2  1 
ATOM   6661 N N    . GLU B 1 341 ? 152.198 124.119 148.815 1.00 46.84  ? 341  GLU A N    1 
ATOM   6662 C CA   . GLU B 1 341 ? 153.087 125.274 148.677 1.00 52.89  ? 341  GLU A CA   1 
ATOM   6663 C C    . GLU B 1 341 ? 154.056 125.150 147.497 1.00 55.88  ? 341  GLU A C    1 
ATOM   6664 O O    . GLU B 1 341 ? 154.158 126.062 146.661 1.00 54.75  ? 341  GLU A O    1 
ATOM   6665 C CB   . GLU B 1 341 ? 153.846 125.512 149.991 1.00 51.32  ? 341  GLU A CB   1 
ATOM   6666 C CG   . GLU B 1 341 ? 154.669 124.341 150.527 1.00 52.01  ? 341  GLU A CG   1 
ATOM   6667 C CD   . GLU B 1 341 ? 153.857 123.390 151.382 1.00 58.90  ? 341  GLU A CD   1 
ATOM   6668 O OE1  . GLU B 1 341 ? 152.757 123.780 151.824 1.00 60.92  ? 341  GLU A OE1  1 
ATOM   6669 O OE2  . GLU B 1 341 ? 154.321 122.254 151.612 1.00 60.03  ? 341  GLU A OE2  1 
ATOM   6670 N N    . ILE B 1 342 ? 154.680 123.978 147.342 1.00 49.97  ? 342  ILE A N    1 
ATOM   6671 C CA   . ILE B 1 342 ? 155.665 123.789 146.276 1.00 40.08  ? 342  ILE A CA   1 
ATOM   6672 C C    . ILE B 1 342 ? 154.991 123.766 144.911 1.00 41.29  ? 342  ILE A C    1 
ATOM   6673 O O    . ILE B 1 342 ? 155.440 124.432 143.972 1.00 46.60  ? 342  ILE A O    1 
ATOM   6674 C CB   . ILE B 1 342 ? 156.489 122.513 146.524 1.00 40.00  ? 342  ILE A CB   1 
ATOM   6675 C CG1  . ILE B 1 342 ? 157.099 122.540 147.926 1.00 38.86  ? 342  ILE A CG1  1 
ATOM   6676 C CG2  . ILE B 1 342 ? 157.582 122.375 145.481 1.00 41.69  ? 342  ILE A CG2  1 
ATOM   6677 C CD1  . ILE B 1 342 ? 156.726 121.350 148.778 1.00 43.14  ? 342  ILE A CD1  1 
ATOM   6678 N N    . ILE B 1 343 ? 153.908 123.000 144.779 1.00 29.93  ? 343  ILE A N    1 
ATOM   6679 C CA   . ILE B 1 343 ? 153.246 122.862 143.484 1.00 31.79  ? 343  ILE A CA   1 
ATOM   6680 C C    . ILE B 1 343 ? 152.607 124.179 143.055 1.00 31.45  ? 343  ILE A C    1 
ATOM   6681 O O    . ILE B 1 343 ? 152.664 124.552 141.877 1.00 28.13  ? 343  ILE A O    1 
ATOM   6682 C CB   . ILE B 1 343 ? 152.227 121.709 143.511 1.00 34.99  ? 343  ILE A CB   1 
ATOM   6683 C CG1  . ILE B 1 343 ? 152.898 120.419 143.987 1.00 36.16  ? 343  ILE A CG1  1 
ATOM   6684 C CG2  . ILE B 1 343 ? 151.604 121.517 142.147 1.00 36.70  ? 343  ILE A CG2  1 
ATOM   6685 C CD1  . ILE B 1 343 ? 153.871 119.834 142.994 1.00 33.33  ? 343  ILE A CD1  1 
ATOM   6686 N N    . THR B 1 344 ? 151.953 124.882 143.984 1.00 30.12  ? 344  THR A N    1 
ATOM   6687 C CA   . THR B 1 344 ? 151.387 126.186 143.649 1.00 37.31  ? 344  THR A CA   1 
ATOM   6688 C C    . THR B 1 344 ? 152.455 127.199 143.235 1.00 45.14  ? 344  THR A C    1 
ATOM   6689 O O    . THR B 1 344 ? 152.287 127.895 142.220 1.00 54.02  ? 344  THR A O    1 
ATOM   6690 C CB   . THR B 1 344 ? 150.574 126.723 144.821 1.00 39.34  ? 344  THR A CB   1 
ATOM   6691 O OG1  . THR B 1 344 ? 149.853 125.648 145.433 1.00 42.25  ? 344  THR A OG1  1 
ATOM   6692 C CG2  . THR B 1 344 ? 149.587 127.755 144.323 1.00 39.91  ? 344  THR A CG2  1 
ATOM   6693 N N    . SER B 1 345 ? 153.592 127.245 143.947 1.00 35.47  ? 345  SER A N    1 
ATOM   6694 C CA   . SER B 1 345 ? 154.674 128.137 143.534 1.00 30.63  ? 345  SER A CA   1 
ATOM   6695 C C    . SER B 1 345 ? 155.200 127.742 142.161 1.00 39.79  ? 345  SER A C    1 
ATOM   6696 O O    . SER B 1 345 ? 155.501 128.602 141.318 1.00 44.01  ? 345  SER A O    1 
ATOM   6697 C CB   . SER B 1 345 ? 155.795 128.115 144.571 1.00 28.59  ? 345  SER A CB   1 
ATOM   6698 O OG   . SER B 1 345 ? 155.313 128.483 145.851 1.00 38.23  ? 345  SER A OG   1 
ATOM   6699 N N    . GLY B 1 346 ? 155.289 126.435 141.917 1.00 29.24  ? 346  GLY A N    1 
ATOM   6700 C CA   . GLY B 1 346 ? 155.793 125.948 140.649 1.00 14.07  ? 346  GLY A CA   1 
ATOM   6701 C C    . GLY B 1 346 ? 154.897 126.340 139.496 1.00 22.54  ? 346  GLY A C    1 
ATOM   6702 O O    . GLY B 1 346 ? 155.374 126.761 138.445 1.00 38.22  ? 346  GLY A O    1 
ATOM   6703 N N    . MET B 1 347 ? 153.584 126.179 139.672 1.00 2.75   ? 347  MET A N    1 
ATOM   6704 C CA   . MET B 1 347 ? 152.648 126.507 138.603 1.00 13.68  ? 347  MET A CA   1 
ATOM   6705 C C    . MET B 1 347 ? 152.654 128.002 138.311 1.00 25.73  ? 347  MET A C    1 
ATOM   6706 O O    . MET B 1 347 ? 152.624 128.412 137.142 1.00 22.99  ? 347  MET A O    1 
ATOM   6707 C CB   . MET B 1 347 ? 151.242 126.043 138.983 1.00 19.38  ? 347  MET A CB   1 
ATOM   6708 C CG   . MET B 1 347 ? 150.129 126.627 138.127 1.00 21.11  ? 347  MET A CG   1 
ATOM   6709 S SD   . MET B 1 347 ? 148.541 126.681 138.976 1.00 44.81  ? 347  MET A SD   1 
ATOM   6710 C CE   . MET B 1 347 ? 148.523 128.378 139.544 1.00 22.72  ? 347  MET A CE   1 
ATOM   6711 N N    . VAL B 1 348 ? 152.778 128.832 139.353 1.00 23.88  ? 348  VAL A N    1 
ATOM   6712 C CA   . VAL B 1 348 ? 152.795 130.280 139.138 1.00 14.88  ? 348  VAL A CA   1 
ATOM   6713 C C    . VAL B 1 348 ? 154.046 130.699 138.367 1.00 30.40  ? 348  VAL A C    1 
ATOM   6714 O O    . VAL B 1 348 ? 153.970 131.409 137.346 1.00 44.27  ? 348  VAL A O    1 
ATOM   6715 C CB   . VAL B 1 348 ? 152.682 131.017 140.483 1.00 4.33   ? 348  VAL A CB   1 
ATOM   6716 C CG1  . VAL B 1 348 ? 152.742 132.495 140.270 1.00 20.69  ? 348  VAL A CG1  1 
ATOM   6717 C CG2  . VAL B 1 348 ? 151.371 130.680 141.150 1.00 12.46  ? 348  VAL A CG2  1 
ATOM   6718 N N    . ILE B 1 349 ? 155.213 130.215 138.806 1.00 20.18  ? 349  ILE A N    1 
ATOM   6719 C CA   . ILE B 1 349 ? 156.449 130.581 138.121 1.00 10.08  ? 349  ILE A CA   1 
ATOM   6720 C C    . ILE B 1 349 ? 156.475 129.987 136.716 1.00 13.55  ? 349  ILE A C    1 
ATOM   6721 O O    . ILE B 1 349 ? 157.000 130.608 135.778 1.00 23.22  ? 349  ILE A O    1 
ATOM   6722 C CB   . ILE B 1 349 ? 157.657 130.142 138.971 1.00 13.92  ? 349  ILE A CB   1 
ATOM   6723 C CG1  . ILE B 1 349 ? 157.685 130.932 140.280 1.00 14.39  ? 349  ILE A CG1  1 
ATOM   6724 C CG2  . ILE B 1 349 ? 158.946 130.373 138.229 1.00 24.59  ? 349  ILE A CG2  1 
ATOM   6725 C CD1  . ILE B 1 349 ? 158.551 130.312 141.350 1.00 24.94  ? 349  ILE A CD1  1 
ATOM   6726 N N    . SER B 1 350 ? 155.921 128.780 136.546 1.00 2.76   ? 350  SER A N    1 
ATOM   6727 C CA   . SER B 1 350 ? 155.916 128.140 135.240 1.00 0.00   ? 350  SER A CA   1 
ATOM   6728 C C    . SER B 1 350 ? 155.089 128.959 134.270 1.00 4.22   ? 350  SER A C    1 
ATOM   6729 O O    . SER B 1 350 ? 155.443 129.070 133.091 1.00 27.75  ? 350  SER A O    1 
ATOM   6730 C CB   . SER B 1 350 ? 155.370 126.719 135.345 1.00 11.43  ? 350  SER A CB   1 
ATOM   6731 O OG   . SER B 1 350 ? 156.281 125.876 136.026 1.00 29.09  ? 350  SER A OG   1 
ATOM   6732 N N    . THR B 1 351 ? 153.966 129.507 134.747 1.00 3.25   ? 351  THR A N    1 
ATOM   6733 C CA   . THR B 1 351 ? 153.131 130.335 133.893 1.00 17.34  ? 351  THR A CA   1 
ATOM   6734 C C    . THR B 1 351 ? 153.881 131.584 133.465 1.00 20.12  ? 351  THR A C    1 
ATOM   6735 O O    . THR B 1 351 ? 153.850 131.939 132.283 1.00 25.73  ? 351  THR A O    1 
ATOM   6736 C CB   . THR B 1 351 ? 151.836 130.718 134.611 1.00 6.83   ? 351  THR A CB   1 
ATOM   6737 O OG1  . THR B 1 351 ? 151.140 129.531 135.011 1.00 19.94  ? 351  THR A OG1  1 
ATOM   6738 C CG2  . THR B 1 351 ? 150.939 131.533 133.696 1.00 0.00   ? 351  THR A CG2  1 
ATOM   6739 N N    . PHE B 1 352 ? 154.551 132.258 134.406 1.00 20.89  ? 352  PHE A N    1 
ATOM   6740 C CA   . PHE B 1 352 ? 155.285 133.475 134.055 1.00 19.56  ? 352  PHE A CA   1 
ATOM   6741 C C    . PHE B 1 352 ? 156.442 133.264 133.085 1.00 24.10  ? 352  PHE A C    1 
ATOM   6742 O O    . PHE B 1 352 ? 156.578 134.023 132.120 1.00 26.48  ? 352  PHE A O    1 
ATOM   6743 C CB   . PHE B 1 352 ? 155.814 134.172 135.302 1.00 23.84  ? 352  PHE A CB   1 
ATOM   6744 C CG   . PHE B 1 352 ? 154.750 134.799 136.105 1.00 31.96  ? 352  PHE A CG   1 
ATOM   6745 C CD1  . PHE B 1 352 ? 153.922 135.734 135.523 1.00 36.35  ? 352  PHE A CD1  1 
ATOM   6746 C CD2  . PHE B 1 352 ? 154.571 134.474 137.430 1.00 36.37  ? 352  PHE A CD2  1 
ATOM   6747 C CE1  . PHE B 1 352 ? 152.932 136.322 136.239 1.00 45.18  ? 352  PHE A CE1  1 
ATOM   6748 C CE2  . PHE B 1 352 ? 153.579 135.070 138.153 1.00 37.56  ? 352  PHE A CE2  1 
ATOM   6749 C CZ   . PHE B 1 352 ? 152.758 135.992 137.557 1.00 43.81  ? 352  PHE A CZ   1 
ATOM   6750 N N    . VAL B 1 353 ? 157.292 132.264 133.330 1.00 34.06  ? 353  VAL A N    1 
ATOM   6751 C CA   . VAL B 1 353 ? 158.467 132.055 132.483 1.00 28.03  ? 353  VAL A CA   1 
ATOM   6752 C C    . VAL B 1 353 ? 158.085 131.649 131.060 1.00 23.24  ? 353  VAL A C    1 
ATOM   6753 O O    . VAL B 1 353 ? 158.813 131.945 130.104 1.00 31.61  ? 353  VAL A O    1 
ATOM   6754 C CB   . VAL B 1 353 ? 159.391 131.014 133.158 1.00 23.54  ? 353  VAL A CB   1 
ATOM   6755 C CG1  . VAL B 1 353 ? 160.586 130.655 132.288 1.00 25.89  ? 353  VAL A CG1  1 
ATOM   6756 C CG2  . VAL B 1 353 ? 159.866 131.533 134.503 1.00 26.46  ? 353  VAL A CG2  1 
ATOM   6757 N N    . SER B 1 354 ? 156.927 131.011 130.884 1.00 19.71  ? 354  SER A N    1 
ATOM   6758 C CA   . SER B 1 354 ? 156.536 130.522 129.563 1.00 16.01  ? 354  SER A CA   1 
ATOM   6759 C C    . SER B 1 354 ? 156.243 131.631 128.551 1.00 34.08  ? 354  SER A C    1 
ATOM   6760 O O    . SER B 1 354 ? 156.408 131.408 127.346 1.00 45.20  ? 354  SER A O    1 
ATOM   6761 C CB   . SER B 1 354 ? 155.315 129.615 129.693 1.00 21.15  ? 354  SER A CB   1 
ATOM   6762 O OG   . SER B 1 354 ? 154.120 130.352 129.519 1.00 25.57  ? 354  SER A OG   1 
ATOM   6763 N N    . ALA B 1 355 ? 155.783 132.806 128.997 1.00 20.34  ? 355  ALA A N    1 
ATOM   6764 C CA   . ALA B 1 355 ? 155.415 133.869 128.056 1.00 13.33  ? 355  ALA A CA   1 
ATOM   6765 C C    . ALA B 1 355 ? 156.543 134.354 127.139 1.00 19.84  ? 355  ALA A C    1 
ATOM   6766 O O    . ALA B 1 355 ? 156.327 134.386 125.916 1.00 26.78  ? 355  ALA A O    1 
ATOM   6767 C CB   . ALA B 1 355 ? 154.765 135.028 128.824 1.00 19.61  ? 355  ALA A CB   1 
ATOM   6768 N N    . PRO B 1 356 ? 157.735 134.749 127.622 1.00 16.48  ? 356  PRO A N    1 
ATOM   6769 C CA   . PRO B 1 356 ? 158.789 135.153 126.670 1.00 15.72  ? 356  PRO A CA   1 
ATOM   6770 C C    . PRO B 1 356 ? 159.358 134.004 125.854 1.00 22.12  ? 356  PRO A C    1 
ATOM   6771 O O    . PRO B 1 356 ? 159.842 134.226 124.733 1.00 32.07  ? 356  PRO A O    1 
ATOM   6772 C CB   . PRO B 1 356 ? 159.857 135.782 127.573 1.00 15.73  ? 356  PRO A CB   1 
ATOM   6773 C CG   . PRO B 1 356 ? 159.676 135.119 128.863 1.00 21.28  ? 356  PRO A CG   1 
ATOM   6774 C CD   . PRO B 1 356 ? 158.202 134.922 129.012 1.00 20.28  ? 356  PRO A CD   1 
ATOM   6775 N N    . ILE B 1 357 ? 159.301 132.784 126.388 1.00 21.41  ? 357  ILE A N    1 
ATOM   6776 C CA   . ILE B 1 357 ? 159.914 131.630 125.740 1.00 14.85  ? 357  ILE A CA   1 
ATOM   6777 C C    . ILE B 1 357 ? 159.194 131.286 124.441 1.00 15.39  ? 357  ILE A C    1 
ATOM   6778 O O    . ILE B 1 357 ? 159.839 130.980 123.433 1.00 28.78  ? 357  ILE A O    1 
ATOM   6779 C CB   . ILE B 1 357 ? 159.956 130.440 126.716 1.00 18.30  ? 357  ILE A CB   1 
ATOM   6780 C CG1  . ILE B 1 357 ? 160.962 130.720 127.832 1.00 27.27  ? 357  ILE A CG1  1 
ATOM   6781 C CG2  . ILE B 1 357 ? 160.393 129.179 125.999 1.00 20.13  ? 357  ILE A CG2  1 
ATOM   6782 C CD1  . ILE B 1 357 ? 161.228 129.538 128.739 1.00 18.97  ? 357  ILE A CD1  1 
ATOM   6783 N N    . MET B 1 358 ? 157.859 131.341 124.431 1.00 12.17  ? 358  MET A N    1 
ATOM   6784 C CA   . MET B 1 358 ? 157.115 131.013 123.216 1.00 23.18  ? 358  MET A CA   1 
ATOM   6785 C C    . MET B 1 358 ? 157.430 131.997 122.094 1.00 37.94  ? 358  MET A C    1 
ATOM   6786 O O    . MET B 1 358 ? 157.661 131.597 120.948 1.00 42.54  ? 358  MET A O    1 
ATOM   6787 C CB   . MET B 1 358 ? 155.611 131.021 123.499 1.00 20.35  ? 358  MET A CB   1 
ATOM   6788 C CG   . MET B 1 358 ? 155.137 130.053 124.561 1.00 26.02  ? 358  MET A CG   1 
ATOM   6789 S SD   . MET B 1 358 ? 153.348 129.831 124.501 1.00 51.97  ? 358  MET A SD   1 
ATOM   6790 C CE   . MET B 1 358 ? 152.955 129.717 126.244 1.00 27.15  ? 358  MET A CE   1 
ATOM   6791 N N    . TYR B 1 359 ? 157.532 133.282 122.426 1.00 25.44  ? 359  TYR A N    1 
ATOM   6792 C CA   . TYR B 1 359 ? 157.834 134.323 121.449 1.00 16.26  ? 359  TYR A CA   1 
ATOM   6793 C C    . TYR B 1 359 ? 159.242 134.193 120.884 1.00 30.58  ? 359  TYR A C    1 
ATOM   6794 O O    . TYR B 1 359 ? 159.437 134.181 119.654 1.00 42.05  ? 359  TYR A O    1 
ATOM   6795 C CB   . TYR B 1 359 ? 157.668 135.701 122.093 1.00 17.61  ? 359  TYR A CB   1 
ATOM   6796 C CG   . TYR B 1 359 ? 157.347 136.814 121.126 1.00 25.48  ? 359  TYR A CG   1 
ATOM   6797 C CD1  . TYR B 1 359 ? 156.140 136.850 120.446 1.00 27.65  ? 359  TYR A CD1  1 
ATOM   6798 C CD2  . TYR B 1 359 ? 158.259 137.836 120.898 1.00 28.80  ? 359  TYR A CD2  1 
ATOM   6799 C CE1  . TYR B 1 359 ? 155.852 137.873 119.562 1.00 35.67  ? 359  TYR A CE1  1 
ATOM   6800 C CE2  . TYR B 1 359 ? 157.981 138.860 120.019 1.00 30.61  ? 359  TYR A CE2  1 
ATOM   6801 C CZ   . TYR B 1 359 ? 156.777 138.875 119.353 1.00 35.27  ? 359  TYR A CZ   1 
ATOM   6802 O OH   . TYR B 1 359 ? 156.499 139.896 118.475 1.00 36.16  ? 359  TYR A OH   1 
ATOM   6803 N N    . VAL B 1 360 ? 160.219 134.012 121.778 1.00 25.62  ? 360  VAL A N    1 
ATOM   6804 C CA   . VAL B 1 360 ? 161.606 133.899 121.335 1.00 25.44  ? 360  VAL A CA   1 
ATOM   6805 C C    . VAL B 1 360 ? 161.800 132.630 120.517 1.00 27.91  ? 360  VAL A C    1 
ATOM   6806 O O    . VAL B 1 360 ? 162.429 132.656 119.453 1.00 30.30  ? 360  VAL A O    1 
ATOM   6807 C CB   . VAL B 1 360 ? 162.560 133.949 122.541 1.00 33.47  ? 360  VAL A CB   1 
ATOM   6808 C CG1  . VAL B 1 360 ? 163.975 133.579 122.124 1.00 37.02  ? 360  VAL A CG1  1 
ATOM   6809 C CG2  . VAL B 1 360 ? 162.537 135.329 123.174 1.00 33.24  ? 360  VAL A CG2  1 
ATOM   6810 N N    . SER B 1 361 ? 161.262 131.501 120.990 1.00 34.75  ? 361  SER A N    1 
ATOM   6811 C CA   . SER B 1 361 ? 161.422 130.256 120.251 1.00 35.06  ? 361  SER A CA   1 
ATOM   6812 C C    . SER B 1 361 ? 160.737 130.324 118.890 1.00 31.15  ? 361  SER A C    1 
ATOM   6813 O O    . SER B 1 361 ? 161.276 129.837 117.892 1.00 37.01  ? 361  SER A O    1 
ATOM   6814 C CB   . SER B 1 361 ? 160.870 129.095 121.077 1.00 31.76  ? 361  SER A CB   1 
ATOM   6815 O OG   . SER B 1 361 ? 161.165 129.266 122.452 1.00 35.61  ? 361  SER A OG   1 
ATOM   6816 N N    . ALA B 1 362 ? 159.545 130.934 118.829 1.00 30.41  ? 362  ALA A N    1 
ATOM   6817 C CA   . ALA B 1 362 ? 158.802 130.970 117.574 1.00 32.51  ? 362  ALA A CA   1 
ATOM   6818 C C    . ALA B 1 362 ? 159.567 131.763 116.526 1.00 40.44  ? 362  ALA A C    1 
ATOM   6819 O O    . ALA B 1 362 ? 159.739 131.320 115.377 1.00 50.62  ? 362  ALA A O    1 
ATOM   6820 C CB   . ALA B 1 362 ? 157.413 131.567 117.799 1.00 29.68  ? 362  ALA A CB   1 
ATOM   6821 N N    . TRP B 1 363 ? 160.133 132.901 116.942 1.00 30.62  ? 363  TRP A N    1 
ATOM   6822 C CA   . TRP B 1 363 ? 160.824 133.713 115.953 1.00 26.28  ? 363  TRP A CA   1 
ATOM   6823 C C    . TRP B 1 363 ? 162.224 133.177 115.708 1.00 33.24  ? 363  TRP A C    1 
ATOM   6824 O O    . TRP B 1 363 ? 162.856 133.519 114.705 1.00 36.21  ? 363  TRP A O    1 
ATOM   6825 C CB   . TRP B 1 363 ? 160.893 135.175 116.390 1.00 29.83  ? 363  TRP A CB   1 
ATOM   6826 C CG   . TRP B 1 363 ? 159.616 135.921 116.211 1.00 30.36  ? 363  TRP A CG   1 
ATOM   6827 C CD1  . TRP B 1 363 ? 158.486 135.791 116.959 1.00 34.46  ? 363  TRP A CD1  1 
ATOM   6828 C CD2  . TRP B 1 363 ? 159.299 136.844 115.164 1.00 32.59  ? 363  TRP A CD2  1 
ATOM   6829 N NE1  . TRP B 1 363 ? 157.506 136.624 116.484 1.00 31.65  ? 363  TRP A NE1  1 
ATOM   6830 C CE2  . TRP B 1 363 ? 157.975 137.272 115.373 1.00 33.04  ? 363  TRP A CE2  1 
ATOM   6831 C CE3  . TRP B 1 363 ? 160.013 137.366 114.083 1.00 34.41  ? 363  TRP A CE3  1 
ATOM   6832 C CZ2  . TRP B 1 363 ? 157.350 138.195 114.541 1.00 41.02  ? 363  TRP A CZ2  1 
ATOM   6833 C CZ3  . TRP B 1 363 ? 159.389 138.282 113.259 1.00 33.40  ? 363  TRP A CZ3  1 
ATOM   6834 C CH2  . TRP B 1 363 ? 158.072 138.688 113.492 1.00 41.52  ? 363  TRP A CH2  1 
ATOM   6835 N N    . LEU B 1 364 ? 162.727 132.324 116.604 1.00 40.53  ? 364  LEU A N    1 
ATOM   6836 C CA   . LEU B 1 364 ? 164.010 131.694 116.332 1.00 40.00  ? 364  LEU A CA   1 
ATOM   6837 C C    . LEU B 1 364 ? 163.872 130.565 115.320 1.00 42.12  ? 364  LEU A C    1 
ATOM   6838 O O    . LEU B 1 364 ? 164.768 130.349 114.497 1.00 35.29  ? 364  LEU A O    1 
ATOM   6839 C CB   . LEU B 1 364 ? 164.603 131.170 117.639 1.00 37.79  ? 364  LEU A CB   1 
ATOM   6840 C CG   . LEU B 1 364 ? 165.916 131.798 118.089 1.00 42.44  ? 364  LEU A CG   1 
ATOM   6841 C CD1  . LEU B 1 364 ? 166.585 130.947 119.154 1.00 44.62  ? 364  LEU A CD1  1 
ATOM   6842 C CD2  . LEU B 1 364 ? 166.810 131.964 116.898 1.00 41.78  ? 364  LEU A CD2  1 
ATOM   6843 N N    . LEU B 1 365 ? 162.755 129.831 115.361 1.00 45.65  ? 365  LEU A N    1 
ATOM   6844 C CA   . LEU B 1 365 ? 162.558 128.780 114.365 1.00 37.51  ? 365  LEU A CA   1 
ATOM   6845 C C    . LEU B 1 365 ? 162.149 129.350 113.013 1.00 38.34  ? 365  LEU A C    1 
ATOM   6846 O O    . LEU B 1 365 ? 162.389 128.718 111.979 1.00 45.77  ? 365  LEU A O    1 
ATOM   6847 C CB   . LEU B 1 365 ? 161.548 127.726 114.830 1.00 29.77  ? 365  LEU A CB   1 
ATOM   6848 C CG   . LEU B 1 365 ? 161.520 127.212 116.267 1.00 28.70  ? 365  LEU A CG   1 
ATOM   6849 C CD1  . LEU B 1 365 ? 160.499 126.102 116.413 1.00 36.78  ? 365  LEU A CD1  1 
ATOM   6850 C CD2  . LEU B 1 365 ? 162.896 126.720 116.679 1.00 29.93  ? 365  LEU A CD2  1 
ATOM   6851 N N    . THR B 1 366 ? 161.503 130.522 112.988 1.00 41.99  ? 366  THR A N    1 
ATOM   6852 C CA   . THR B 1 366 ? 161.141 131.066 111.678 1.00 43.29  ? 366  THR A CA   1 
ATOM   6853 C C    . THR B 1 366 ? 162.249 131.954 111.090 1.00 50.34  ? 366  THR A C    1 
ATOM   6854 O O    . THR B 1 366 ? 162.126 132.440 109.959 1.00 51.65  ? 366  THR A O    1 
ATOM   6855 C CB   . THR B 1 366 ? 159.804 131.810 111.793 1.00 40.19  ? 366  THR A CB   1 
ATOM   6856 O OG1  . THR B 1 366 ? 158.859 130.957 112.448 1.00 40.45  ? 366  THR A OG1  1 
ATOM   6857 C CG2  . THR B 1 366 ? 159.211 132.077 110.411 1.00 41.04  ? 366  THR A CG2  1 
ATOM   6858 N N    . PHE B 1 367 ? 163.382 132.107 111.777 1.00 68.01  ? 367  PHE A N    1 
ATOM   6859 C CA   . PHE B 1 367 ? 164.421 132.918 111.139 1.00 68.35  ? 367  PHE A CA   1 
ATOM   6860 C C    . PHE B 1 367 ? 165.232 132.297 109.996 1.00 66.66  ? 367  PHE A C    1 
ATOM   6861 O O    . PHE B 1 367 ? 165.619 133.047 109.090 1.00 67.12  ? 367  PHE A O    1 
ATOM   6862 C CB   . PHE B 1 367 ? 165.407 133.429 112.192 1.00 67.40  ? 367  PHE A CB   1 
ATOM   6863 C CG   . PHE B 1 367 ? 164.952 134.681 112.889 1.00 65.71  ? 367  PHE A CG   1 
ATOM   6864 C CD1  . PHE B 1 367 ? 163.880 135.408 112.397 1.00 64.05  ? 367  PHE A CD1  1 
ATOM   6865 C CD2  . PHE B 1 367 ? 165.601 135.140 114.022 1.00 65.27  ? 367  PHE A CD2  1 
ATOM   6866 C CE1  . PHE B 1 367 ? 163.456 136.561 113.028 1.00 64.12  ? 367  PHE A CE1  1 
ATOM   6867 C CE2  . PHE B 1 367 ? 165.181 136.297 114.657 1.00 65.73  ? 367  PHE A CE2  1 
ATOM   6868 C CZ   . PHE B 1 367 ? 164.107 137.007 114.158 1.00 65.60  ? 367  PHE A CZ   1 
ATOM   6869 N N    . PRO B 1 368 ? 165.538 130.990 109.966 1.00 71.83  ? 368  PRO A N    1 
ATOM   6870 C CA   . PRO B 1 368 ? 166.590 130.554 109.034 1.00 71.97  ? 368  PRO A CA   1 
ATOM   6871 C C    . PRO B 1 368 ? 166.262 130.619 107.533 1.00 74.51  ? 368  PRO A C    1 
ATOM   6872 O O    . PRO B 1 368 ? 167.199 130.610 106.726 1.00 77.75  ? 368  PRO A O    1 
ATOM   6873 C CB   . PRO B 1 368 ? 166.903 129.148 109.568 1.00 72.30  ? 368  PRO A CB   1 
ATOM   6874 C CG   . PRO B 1 368 ? 165.541 128.675 110.180 1.00 73.14  ? 368  PRO A CG   1 
ATOM   6875 C CD   . PRO B 1 368 ? 164.599 129.851 109.977 1.00 73.40  ? 368  PRO A CD   1 
ATOM   6876 N N    . THR B 1 369 ? 164.993 130.684 107.124 1.00 80.75  ? 369  THR A N    1 
ATOM   6877 C CA   . THR B 1 369 ? 164.551 130.362 105.767 1.00 86.16  ? 369  THR A CA   1 
ATOM   6878 C C    . THR B 1 369 ? 163.636 131.507 105.345 1.00 87.03  ? 369  THR A C    1 
ATOM   6879 O O    . THR B 1 369 ? 162.411 131.373 105.378 1.00 88.03  ? 369  THR A O    1 
ATOM   6880 C CB   . THR B 1 369 ? 163.814 128.985 105.683 1.00 87.91  ? 369  THR A CB   1 
ATOM   6881 O OG1  . THR B 1 369 ? 162.471 129.127 106.162 1.00 86.66  ? 369  THR A OG1  1 
ATOM   6882 C CG2  . THR B 1 369 ? 164.531 127.909 106.490 1.00 83.56  ? 369  THR A CG2  1 
ATOM   6883 N N    . MET B 1 370 ? 164.240 132.608 104.907 1.00 93.03  ? 370  MET A N    1 
ATOM   6884 C CA   . MET B 1 370 ? 163.538 133.800 104.432 1.00 94.14  ? 370  MET A CA   1 
ATOM   6885 C C    . MET B 1 370 ? 164.548 134.699 103.730 1.00 97.28  ? 370  MET A C    1 
ATOM   6886 O O    . MET B 1 370 ? 165.689 134.300 103.473 1.00 96.04  ? 370  MET A O    1 
ATOM   6887 C CB   . MET B 1 370 ? 162.852 134.554 105.580 1.00 92.41  ? 370  MET A CB   1 
ATOM   6888 C CG   . MET B 1 370 ? 161.364 134.289 105.749 1.00 96.31  ? 370  MET A CG   1 
ATOM   6889 S SD   . MET B 1 370 ? 160.593 135.440 106.901 1.00 102.41 ? 370  MET A SD   1 
ATOM   6890 C CE   . MET B 1 370 ? 161.722 135.337 108.287 1.00 92.90  ? 370  MET A CE   1 
ATOM   6891 N N    . ASP B 1 371 ? 164.124 135.915 103.421 1.00 109.24 ? 371  ASP A N    1 
ATOM   6892 C CA   . ASP B 1 371 ? 164.919 136.868 102.661 1.00 108.14 ? 371  ASP A CA   1 
ATOM   6893 C C    . ASP B 1 371 ? 165.850 137.603 103.615 1.00 108.95 ? 371  ASP A C    1 
ATOM   6894 O O    . ASP B 1 371 ? 165.742 137.467 104.835 1.00 111.13 ? 371  ASP A O    1 
ATOM   6895 C CB   . ASP B 1 371 ? 163.976 137.816 101.920 1.00 107.30 ? 371  ASP A CB   1 
ATOM   6896 C CG   . ASP B 1 371 ? 164.522 138.288 100.583 1.00 108.86 ? 371  ASP A CG   1 
ATOM   6897 O OD1  . ASP B 1 371 ? 165.342 139.228 100.557 1.00 110.37 ? 371  ASP A OD1  1 
ATOM   6898 O OD2  . ASP B 1 371 ? 164.124 137.713 99.548  1.00 107.48 ? 371  ASP A OD2  1 
ATOM   6899 N N    . PRO B 1 372 ? 166.785 138.404 103.104 1.00 105.78 ? 372  PRO A N    1 
ATOM   6900 C CA   . PRO B 1 372 ? 167.414 139.428 103.953 1.00 105.78 ? 372  PRO A CA   1 
ATOM   6901 C C    . PRO B 1 372 ? 166.485 140.506 104.501 1.00 105.17 ? 372  PRO A C    1 
ATOM   6902 O O    . PRO B 1 372 ? 166.430 140.723 105.722 1.00 104.54 ? 372  PRO A O    1 
ATOM   6903 C CB   . PRO B 1 372 ? 168.459 140.049 103.019 1.00 103.49 ? 372  PRO A CB   1 
ATOM   6904 C CG   . PRO B 1 372 ? 168.763 138.992 101.995 1.00 104.69 ? 372  PRO A CG   1 
ATOM   6905 C CD   . PRO B 1 372 ? 167.714 137.914 102.071 1.00 104.39 ? 372  PRO A CD   1 
ATOM   6906 N N    . LYS B 1 373 ? 165.769 141.211 103.627 1.00 103.62 ? 373  LYS A N    1 
ATOM   6907 C CA   . LYS B 1 373 ? 165.161 142.432 104.138 1.00 104.80 ? 373  LYS A CA   1 
ATOM   6908 C C    . LYS B 1 373 ? 163.923 142.108 104.978 1.00 105.27 ? 373  LYS A C    1 
ATOM   6909 O O    . LYS B 1 373 ? 163.700 142.791 105.991 1.00 105.13 ? 373  LYS A O    1 
ATOM   6910 C CB   . LYS B 1 373 ? 164.839 143.402 102.994 1.00 103.75 ? 373  LYS A CB   1 
ATOM   6911 C CG   . LYS B 1 373 ? 165.778 143.290 101.802 1.00 105.22 ? 373  LYS A CG   1 
ATOM   6912 C CD   . LYS B 1 373 ? 165.256 144.079 100.611 1.00 105.14 ? 373  LYS A CD   1 
ATOM   6913 C CE   . LYS B 1 373 ? 165.979 143.691 99.331  1.00 103.84 ? 373  LYS A CE   1 
ATOM   6914 N NZ   . LYS B 1 373 ? 166.101 144.838 98.390  1.00 102.54 ? 373  LYS A NZ   1 
ATOM   6915 N N    . PRO B 1 374 ? 163.025 141.197 104.564 1.00 102.57 ? 374  PRO A N    1 
ATOM   6916 C CA   . PRO B 1 374 ? 162.069 140.675 105.550 1.00 103.51 ? 374  PRO A CA   1 
ATOM   6917 C C    . PRO B 1 374 ? 162.675 140.207 106.873 1.00 100.67 ? 374  PRO A C    1 
ATOM   6918 O O    . PRO B 1 374 ? 162.009 140.367 107.907 1.00 99.36  ? 374  PRO A O    1 
ATOM   6919 C CB   . PRO B 1 374 ? 161.411 139.516 104.796 1.00 100.51 ? 374  PRO A CB   1 
ATOM   6920 C CG   . PRO B 1 374 ? 161.358 139.999 103.409 1.00 99.14  ? 374  PRO A CG   1 
ATOM   6921 C CD   . PRO B 1 374 ? 162.609 140.820 103.197 1.00 98.52  ? 374  PRO A CD   1 
ATOM   6922 N N    . LEU B 1 375 ? 163.923 139.693 106.914 1.00 93.43  ? 375  LEU A N    1 
ATOM   6923 C CA   . LEU B 1 375 ? 164.515 139.500 108.236 1.00 94.20  ? 375  LEU A CA   1 
ATOM   6924 C C    . LEU B 1 375 ? 164.748 140.828 108.935 1.00 95.18  ? 375  LEU A C    1 
ATOM   6925 O O    . LEU B 1 375 ? 164.679 140.898 110.174 1.00 92.08  ? 375  LEU A O    1 
ATOM   6926 C CB   . LEU B 1 375 ? 165.831 138.729 108.123 1.00 92.36  ? 375  LEU A CB   1 
ATOM   6927 C CG   . LEU B 1 375 ? 165.785 137.202 108.092 1.00 94.71  ? 375  LEU A CG   1 
ATOM   6928 C CD1  . LEU B 1 375 ? 167.155 136.638 107.748 1.00 93.69  ? 375  LEU A CD1  1 
ATOM   6929 C CD2  . LEU B 1 375 ? 165.300 136.654 109.414 1.00 94.45  ? 375  LEU A CD2  1 
ATOM   6930 N N    . ALA B 1 376 ? 165.066 141.880 108.163 1.00 92.77  ? 376  ALA A N    1 
ATOM   6931 C CA   . ALA B 1 376 ? 165.374 143.144 108.821 1.00 90.49  ? 376  ALA A CA   1 
ATOM   6932 C C    . ALA B 1 376 ? 164.118 143.637 109.516 1.00 88.31  ? 376  ALA A C    1 
ATOM   6933 O O    . ALA B 1 376 ? 164.142 144.090 110.672 1.00 88.15  ? 376  ALA A O    1 
ATOM   6934 C CB   . ALA B 1 376 ? 165.903 144.171 107.820 1.00 87.63  ? 376  ALA A CB   1 
ATOM   6935 N N    . TYR B 1 377 ? 163.002 143.516 108.788 1.00 80.20  ? 377  TYR A N    1 
ATOM   6936 C CA   . TYR B 1 377 ? 161.689 143.865 109.310 1.00 83.45  ? 377  TYR A CA   1 
ATOM   6937 C C    . TYR B 1 377 ? 161.326 142.996 110.503 1.00 84.76  ? 377  TYR A C    1 
ATOM   6938 O O    . TYR B 1 377 ? 160.648 143.456 111.423 1.00 88.47  ? 377  TYR A O    1 
ATOM   6939 C CB   . TYR B 1 377 ? 160.635 143.717 108.209 1.00 81.95  ? 377  TYR A CB   1 
ATOM   6940 C CG   . TYR B 1 377 ? 160.546 144.878 107.235 1.00 81.17  ? 377  TYR A CG   1 
ATOM   6941 C CD1  . TYR B 1 377 ? 161.638 145.705 106.996 1.00 81.97  ? 377  TYR A CD1  1 
ATOM   6942 C CD2  . TYR B 1 377 ? 159.370 145.134 106.541 1.00 83.64  ? 377  TYR A CD2  1 
ATOM   6943 C CE1  . TYR B 1 377 ? 161.559 146.757 106.102 1.00 84.36  ? 377  TYR A CE1  1 
ATOM   6944 C CE2  . TYR B 1 377 ? 159.281 146.184 105.645 1.00 87.45  ? 377  TYR A CE2  1 
ATOM   6945 C CZ   . TYR B 1 377 ? 160.378 146.992 105.431 1.00 87.79  ? 377  TYR A CZ   1 
ATOM   6946 O OH   . TYR B 1 377 ? 160.293 148.039 104.541 1.00 84.68  ? 377  TYR A OH   1 
ATOM   6947 N N    . ALA B 1 378 ? 161.773 141.735 110.495 1.00 75.47  ? 378  ALA A N    1 
ATOM   6948 C CA   . ALA B 1 378 ? 161.536 140.828 111.615 1.00 75.15  ? 378  ALA A CA   1 
ATOM   6949 C C    . ALA B 1 378 ? 162.182 141.329 112.902 1.00 76.35  ? 378  ALA A C    1 
ATOM   6950 O O    . ALA B 1 378 ? 161.535 141.393 113.958 1.00 78.17  ? 378  ALA A O    1 
ATOM   6951 C CB   . ALA B 1 378 ? 162.043 139.429 111.266 1.00 77.09  ? 378  ALA A CB   1 
ATOM   6952 N N    . ILE B 1 379 ? 163.463 141.704 112.824 1.00 77.98  ? 379  ILE A N    1 
ATOM   6953 C CA   . ILE B 1 379 ? 164.153 142.246 113.999 1.00 79.63  ? 379  ILE A CA   1 
ATOM   6954 C C    . ILE B 1 379 ? 163.532 143.565 114.449 1.00 76.86  ? 379  ILE A C    1 
ATOM   6955 O O    . ILE B 1 379 ? 163.329 143.791 115.655 1.00 72.75  ? 379  ILE A O    1 
ATOM   6956 C CB   . ILE B 1 379 ? 165.663 142.397 113.731 1.00 76.17  ? 379  ILE A CB   1 
ATOM   6957 C CG1  . ILE B 1 379 ? 166.217 141.175 113.000 1.00 72.82  ? 379  ILE A CG1  1 
ATOM   6958 C CG2  . ILE B 1 379 ? 166.415 142.612 115.035 1.00 76.09  ? 379  ILE A CG2  1 
ATOM   6959 C CD1  . ILE B 1 379 ? 167.286 141.510 111.984 1.00 76.61  ? 379  ILE A CD1  1 
ATOM   6960 N N    . GLN B 1 380 ? 163.177 144.435 113.495 1.00 70.58  ? 380  GLN A N    1 
ATOM   6961 C CA   . GLN B 1 380 ? 162.545 145.700 113.869 1.00 67.42  ? 380  GLN A CA   1 
ATOM   6962 C C    . GLN B 1 380 ? 161.211 145.461 114.567 1.00 69.38  ? 380  GLN A C    1 
ATOM   6963 O O    . GLN B 1 380 ? 160.917 146.087 115.593 1.00 76.34  ? 380  GLN A O    1 
ATOM   6964 C CB   . GLN B 1 380 ? 162.360 146.581 112.634 1.00 65.81  ? 380  GLN A CB   1 
ATOM   6965 C CG   . GLN B 1 380 ? 163.660 147.073 112.009 1.00 69.39  ? 380  GLN A CG   1 
ATOM   6966 C CD   . GLN B 1 380 ? 164.715 147.433 113.039 1.00 73.51  ? 380  GLN A CD   1 
ATOM   6967 O OE1  . GLN B 1 380 ? 165.616 146.642 113.327 1.00 73.65  ? 380  GLN A OE1  1 
ATOM   6968 N NE2  . GLN B 1 380 ? 164.612 148.633 113.596 1.00 74.97  ? 380  GLN A NE2  1 
ATOM   6969 N N    . ASN B 1 381 ? 160.402 144.545 114.033 1.00 65.26  ? 381  ASN A N    1 
ATOM   6970 C CA   . ASN B 1 381 ? 159.081 144.276 114.586 1.00 67.25  ? 381  ASN A CA   1 
ATOM   6971 C C    . ASN B 1 381 ? 159.178 143.680 115.985 1.00 70.20  ? 381  ASN A C    1 
ATOM   6972 O O    . ASN B 1 381 ? 158.395 144.039 116.872 1.00 79.58  ? 381  ASN A O    1 
ATOM   6973 C CB   . ASN B 1 381 ? 158.301 143.349 113.656 1.00 66.87  ? 381  ASN A CB   1 
ATOM   6974 C CG   . ASN B 1 381 ? 157.732 144.075 112.453 1.00 69.64  ? 381  ASN A CG   1 
ATOM   6975 O OD1  . ASN B 1 381 ? 158.125 145.202 112.151 1.00 69.92  ? 381  ASN A OD1  1 
ATOM   6976 N ND2  . ASN B 1 381 ? 156.801 143.431 111.758 1.00 72.58  ? 381  ASN A ND2  1 
ATOM   6977 N N    . VAL B 1 382 ? 160.101 142.733 116.187 1.00 52.74  ? 382  VAL A N    1 
ATOM   6978 C CA   . VAL B 1 382 ? 160.264 142.129 117.509 1.00 52.20  ? 382  VAL A CA   1 
ATOM   6979 C C    . VAL B 1 382 ? 160.703 143.165 118.542 1.00 61.36  ? 382  VAL A C    1 
ATOM   6980 O O    . VAL B 1 382 ? 160.172 143.206 119.665 1.00 63.70  ? 382  VAL A O    1 
ATOM   6981 C CB   . VAL B 1 382 ? 161.258 140.955 117.428 1.00 55.86  ? 382  VAL A CB   1 
ATOM   6982 C CG1  . VAL B 1 382 ? 161.812 140.626 118.800 1.00 61.19  ? 382  VAL A CG1  1 
ATOM   6983 C CG2  . VAL B 1 382 ? 160.587 139.743 116.815 1.00 59.53  ? 382  VAL A CG2  1 
ATOM   6984 N N    . SER B 1 383 ? 161.661 144.032 118.180 1.00 60.56  ? 383  SER A N    1 
ATOM   6985 C CA   . SER B 1 383 ? 162.079 145.080 119.112 1.00 58.99  ? 383  SER A CA   1 
ATOM   6986 C C    . SER B 1 383 ? 160.930 146.034 119.424 1.00 56.58  ? 383  SER A C    1 
ATOM   6987 O O    . SER B 1 383 ? 160.728 146.430 120.585 1.00 61.91  ? 383  SER A O    1 
ATOM   6988 C CB   . SER B 1 383 ? 163.271 145.844 118.540 1.00 59.49  ? 383  SER A CB   1 
ATOM   6989 O OG   . SER B 1 383 ? 164.367 144.981 118.299 1.00 57.48  ? 383  SER A OG   1 
ATOM   6990 N N    . PHE B 1 384 ? 160.119 146.340 118.407 1.00 53.08  ? 384  PHE A N    1 
ATOM   6991 C CA   . PHE B 1 384 ? 158.964 147.211 118.589 1.00 50.93  ? 384  PHE A CA   1 
ATOM   6992 C C    . PHE B 1 384 ? 157.961 146.596 119.556 1.00 54.28  ? 384  PHE A C    1 
ATOM   6993 O O    . PHE B 1 384 ? 157.443 147.280 120.446 1.00 61.29  ? 384  PHE A O    1 
ATOM   6994 C CB   . PHE B 1 384 ? 158.325 147.479 117.225 1.00 55.05  ? 384  PHE A CB   1 
ATOM   6995 C CG   . PHE B 1 384 ? 157.079 148.313 117.278 1.00 56.92  ? 384  PHE A CG   1 
ATOM   6996 C CD1  . PHE B 1 384 ? 157.155 149.692 117.349 1.00 60.04  ? 384  PHE A CD1  1 
ATOM   6997 C CD2  . PHE B 1 384 ? 155.830 147.717 117.228 1.00 62.47  ? 384  PHE A CD2  1 
ATOM   6998 C CE1  . PHE B 1 384 ? 156.009 150.461 117.384 1.00 61.76  ? 384  PHE A CE1  1 
ATOM   6999 C CE2  . PHE B 1 384 ? 154.679 148.481 117.267 1.00 65.85  ? 384  PHE A CE2  1 
ATOM   7000 C CZ   . PHE B 1 384 ? 154.770 149.855 117.345 1.00 63.74  ? 384  PHE A CZ   1 
ATOM   7001 N N    . ASP B 1 385 ? 157.652 145.310 119.378 1.00 50.08  ? 385  ASP A N    1 
ATOM   7002 C CA   . ASP B 1 385 ? 156.666 144.671 120.243 1.00 46.78  ? 385  ASP A CA   1 
ATOM   7003 C C    . ASP B 1 385 ? 157.154 144.584 121.686 1.00 52.38  ? 385  ASP A C    1 
ATOM   7004 O O    . ASP B 1 385 ? 156.381 144.830 122.619 1.00 58.12  ? 385  ASP A O    1 
ATOM   7005 C CB   . ASP B 1 385 ? 156.316 143.284 119.708 1.00 53.81  ? 385  ASP A CB   1 
ATOM   7006 C CG   . ASP B 1 385 ? 155.668 143.336 118.339 1.00 64.50  ? 385  ASP A CG   1 
ATOM   7007 O OD1  . ASP B 1 385 ? 155.873 142.394 117.546 1.00 65.71  ? 385  ASP A OD1  1 
ATOM   7008 O OD2  . ASP B 1 385 ? 154.953 144.321 118.057 1.00 62.25  ? 385  ASP A OD2  1 
ATOM   7009 N N    . ILE B 1 386 ? 158.423 144.216 121.894 1.00 51.41  ? 386  ILE A N    1 
ATOM   7010 C CA   . ILE B 1 386 ? 158.934 144.087 123.261 1.00 52.91  ? 386  ILE A CA   1 
ATOM   7011 C C    . ILE B 1 386 ? 158.983 145.430 124.001 1.00 56.33  ? 386  ILE A C    1 
ATOM   7012 O O    . ILE B 1 386 ? 158.697 145.494 125.217 1.00 53.59  ? 386  ILE A O    1 
ATOM   7013 C CB   . ILE B 1 386 ? 160.316 143.399 123.225 1.00 48.40  ? 386  ILE A CB   1 
ATOM   7014 C CG1  . ILE B 1 386 ? 160.154 141.884 123.134 1.00 50.63  ? 386  ILE A CG1  1 
ATOM   7015 C CG2  . ILE B 1 386 ? 161.169 143.752 124.436 1.00 56.20  ? 386  ILE A CG2  1 
ATOM   7016 C CD1  . ILE B 1 386 ? 161.263 141.212 122.379 1.00 53.60  ? 386  ILE A CD1  1 
ATOM   7017 N N    . SER B 1 387 ? 159.289 146.524 123.284 1.00 57.76  ? 387  SER A N    1 
ATOM   7018 C CA   . SER B 1 387 ? 159.389 147.829 123.939 1.00 52.52  ? 387  SER A CA   1 
ATOM   7019 C C    . SER B 1 387 ? 158.080 148.307 124.568 1.00 53.26  ? 387  SER A C    1 
ATOM   7020 O O    . SER B 1 387 ? 158.115 148.956 125.619 1.00 57.96  ? 387  SER A O    1 
ATOM   7021 C CB   . SER B 1 387 ? 159.889 148.871 122.937 1.00 56.45  ? 387  SER A CB   1 
ATOM   7022 O OG   . SER B 1 387 ? 160.835 148.315 122.041 1.00 56.29  ? 387  SER A OG   1 
ATOM   7023 N N    . ILE B 1 388 ? 156.928 147.967 123.982 1.00 42.27  ? 388  ILE A N    1 
ATOM   7024 C CA   . ILE B 1 388 ? 155.639 148.400 124.533 1.00 39.34  ? 388  ILE A CA   1 
ATOM   7025 C C    . ILE B 1 388 ? 155.409 147.810 125.922 1.00 42.78  ? 388  ILE A C    1 
ATOM   7026 O O    . ILE B 1 388 ? 155.088 148.528 126.885 1.00 51.96  ? 388  ILE A O    1 
ATOM   7027 C CB   . ILE B 1 388 ? 154.498 148.036 123.564 1.00 44.60  ? 388  ILE A CB   1 
ATOM   7028 C CG1  . ILE B 1 388 ? 154.344 149.119 122.496 1.00 45.84  ? 388  ILE A CG1  1 
ATOM   7029 C CG2  . ILE B 1 388 ? 153.177 147.853 124.305 1.00 47.19  ? 388  ILE A CG2  1 
ATOM   7030 C CD1  . ILE B 1 388 ? 153.316 148.790 121.436 1.00 49.15  ? 388  ILE A CD1  1 
ATOM   7031 N N    . VAL B 1 389 ? 155.626 146.500 126.059 1.00 42.43  ? 389  VAL A N    1 
ATOM   7032 C CA   . VAL B 1 389 ? 155.362 145.836 127.329 1.00 43.46  ? 389  VAL A CA   1 
ATOM   7033 C C    . VAL B 1 389 ? 156.378 146.277 128.368 1.00 47.26  ? 389  VAL A C    1 
ATOM   7034 O O    . VAL B 1 389 ? 156.029 146.511 129.538 1.00 55.65  ? 389  VAL A O    1 
ATOM   7035 C CB   . VAL B 1 389 ? 155.362 144.309 127.143 1.00 41.28  ? 389  VAL A CB   1 
ATOM   7036 C CG1  . VAL B 1 389 ? 154.991 143.614 128.441 1.00 38.56  ? 389  VAL A CG1  1 
ATOM   7037 C CG2  . VAL B 1 389 ? 154.412 143.909 126.026 1.00 47.56  ? 389  VAL A CG2  1 
ATOM   7038 N N    . SER B 1 390 ? 157.647 146.414 127.961 1.00 41.12  ? 390  SER A N    1 
ATOM   7039 C CA   . SER B 1 390 ? 158.651 146.853 128.922 1.00 40.57  ? 390  SER A CA   1 
ATOM   7040 C C    . SER B 1 390 ? 158.350 148.262 129.421 1.00 50.68  ? 390  SER A C    1 
ATOM   7041 O O    . SER B 1 390 ? 158.486 148.546 130.617 1.00 51.44  ? 390  SER A O    1 
ATOM   7042 C CB   . SER B 1 390 ? 160.042 146.790 128.295 1.00 47.67  ? 390  SER A CB   1 
ATOM   7043 O OG   . SER B 1 390 ? 161.046 147.062 129.256 1.00 49.79  ? 390  SER A OG   1 
ATOM   7044 N N    . LEU B 1 391 ? 157.927 149.155 128.518 1.00 59.43  ? 391  LEU A N    1 
ATOM   7045 C CA   . LEU B 1 391 ? 157.622 150.528 128.907 1.00 52.64  ? 391  LEU A CA   1 
ATOM   7046 C C    . LEU B 1 391 ? 156.452 150.609 129.883 1.00 53.21  ? 391  LEU A C    1 
ATOM   7047 O O    . LEU B 1 391 ? 156.523 151.336 130.884 1.00 63.20  ? 391  LEU A O    1 
ATOM   7048 C CB   . LEU B 1 391 ? 157.332 151.366 127.663 1.00 49.89  ? 391  LEU A CB   1 
ATOM   7049 C CG   . LEU B 1 391 ? 157.397 152.884 127.834 1.00 55.74  ? 391  LEU A CG   1 
ATOM   7050 C CD1  . LEU B 1 391 ? 158.579 153.281 128.712 1.00 53.36  ? 391  LEU A CD1  1 
ATOM   7051 C CD2  . LEU B 1 391 ? 157.474 153.559 126.481 1.00 60.03  ? 391  LEU A CD2  1 
ATOM   7052 N N    . ILE B 1 392 ? 155.375 149.855 129.630 1.00 36.06  ? 392  ILE A N    1 
ATOM   7053 C CA   . ILE B 1 392 ? 154.229 149.903 130.548 1.00 38.35  ? 392  ILE A CA   1 
ATOM   7054 C C    . ILE B 1 392 ? 154.578 149.314 131.916 1.00 46.06  ? 392  ILE A C    1 
ATOM   7055 O O    . ILE B 1 392 ? 154.216 149.883 132.963 1.00 56.62  ? 392  ILE A O    1 
ATOM   7056 C CB   . ILE B 1 392 ? 152.979 149.222 129.946 1.00 46.97  ? 392  ILE A CB   1 
ATOM   7057 C CG1  . ILE B 1 392 ? 152.652 149.656 128.502 1.00 51.45  ? 392  ILE A CG1  1 
ATOM   7058 C CG2  . ILE B 1 392 ? 151.759 149.469 130.832 1.00 48.38  ? 392  ILE A CG2  1 
ATOM   7059 C CD1  . ILE B 1 392 ? 152.933 151.115 128.127 1.00 46.64  ? 392  ILE A CD1  1 
ATOM   7060 N N    . SER B 1 393 ? 155.318 148.197 131.942 1.00 44.73  ? 393  SER A N    1 
ATOM   7061 C CA   . SER B 1 393 ? 155.720 147.638 133.231 1.00 39.16  ? 393  SER A CA   1 
ATOM   7062 C C    . SER B 1 393 ? 156.629 148.590 133.999 1.00 45.53  ? 393  SER A C    1 
ATOM   7063 O O    . SER B 1 393 ? 156.493 148.740 135.224 1.00 52.17  ? 393  SER A O    1 
ATOM   7064 C CB   . SER B 1 393 ? 156.410 146.293 133.022 1.00 43.87  ? 393  SER A CB   1 
ATOM   7065 O OG   . SER B 1 393 ? 157.816 146.443 132.970 1.00 54.08  ? 393  SER A OG   1 
ATOM   7066 N N    . LEU B 1 394 ? 157.559 149.247 133.298 1.00 53.21  ? 394  LEU A N    1 
ATOM   7067 C CA   . LEU B 1 394 ? 158.446 150.189 133.966 1.00 53.85  ? 394  LEU A CA   1 
ATOM   7068 C C    . LEU B 1 394 ? 157.671 151.370 134.526 1.00 58.18  ? 394  LEU A C    1 
ATOM   7069 O O    . LEU B 1 394 ? 157.980 151.856 135.619 1.00 59.38  ? 394  LEU A O    1 
ATOM   7070 C CB   . LEU B 1 394 ? 159.527 150.659 133.000 1.00 51.82  ? 394  LEU A CB   1 
ATOM   7071 C CG   . LEU B 1 394 ? 160.759 149.762 132.938 1.00 54.02  ? 394  LEU A CG   1 
ATOM   7072 C CD1  . LEU B 1 394 ? 161.914 150.581 132.463 1.00 58.73  ? 394  LEU A CD1  1 
ATOM   7073 C CD2  . LEU B 1 394 ? 161.072 149.165 134.304 1.00 56.48  ? 394  LEU A CD2  1 
ATOM   7074 N N    . ILE B 1 395 ? 156.679 151.863 133.776 1.00 52.31  ? 395  ILE A N    1 
ATOM   7075 C CA   . ILE B 1 395 ? 155.884 152.996 134.243 1.00 50.04  ? 395  ILE A CA   1 
ATOM   7076 C C    . ILE B 1 395 ? 155.154 152.637 135.531 1.00 55.79  ? 395  ILE A C    1 
ATOM   7077 O O    . ILE B 1 395 ? 155.153 153.410 136.499 1.00 59.04  ? 395  ILE A O    1 
ATOM   7078 C CB   . ILE B 1 395 ? 154.914 153.464 133.141 1.00 46.75  ? 395  ILE A CB   1 
ATOM   7079 C CG1  . ILE B 1 395 ? 155.675 154.244 132.064 1.00 50.96  ? 395  ILE A CG1  1 
ATOM   7080 C CG2  . ILE B 1 395 ? 153.784 154.299 133.725 1.00 51.06  ? 395  ILE A CG2  1 
ATOM   7081 C CD1  . ILE B 1 395 ? 154.783 154.950 131.063 1.00 54.94  ? 395  ILE A CD1  1 
ATOM   7082 N N    . TRP B 1 396 ? 154.574 151.430 135.583 1.00 67.02  ? 396  TRP A N    1 
ATOM   7083 C CA   . TRP B 1 396 ? 153.874 150.991 136.792 1.00 61.27  ? 396  TRP A CA   1 
ATOM   7084 C C    . TRP B 1 396 ? 154.825 150.894 137.984 1.00 61.53  ? 396  TRP A C    1 
ATOM   7085 O O    . TRP B 1 396 ? 154.552 151.443 139.064 1.00 68.84  ? 396  TRP A O    1 
ATOM   7086 C CB   . TRP B 1 396 ? 153.187 149.649 136.551 1.00 59.71  ? 396  TRP A CB   1 
ATOM   7087 C CG   . TRP B 1 396 ? 152.503 149.106 137.770 1.00 66.52  ? 396  TRP A CG   1 
ATOM   7088 C CD1  . TRP B 1 396 ? 152.884 148.032 138.519 1.00 68.75  ? 396  TRP A CD1  1 
ATOM   7089 C CD2  . TRP B 1 396 ? 151.297 149.602 138.364 1.00 71.89  ? 396  TRP A CD2  1 
ATOM   7090 N NE1  . TRP B 1 396 ? 151.997 147.837 139.551 1.00 69.27  ? 396  TRP A NE1  1 
ATOM   7091 C CE2  . TRP B 1 396 ? 151.011 148.786 139.475 1.00 67.73  ? 396  TRP A CE2  1 
ATOM   7092 C CE3  . TRP B 1 396 ? 150.433 150.660 138.064 1.00 70.88  ? 396  TRP A CE3  1 
ATOM   7093 C CZ2  . TRP B 1 396 ? 149.898 148.995 140.288 1.00 61.34  ? 396  TRP A CZ2  1 
ATOM   7094 C CZ3  . TRP B 1 396 ? 149.331 150.866 138.873 1.00 70.02  ? 396  TRP A CZ3  1 
ATOM   7095 C CH2  . TRP B 1 396 ? 149.074 150.039 139.972 1.00 66.18  ? 396  TRP A CH2  1 
ATOM   7096 N N    . SER B 1 397 ? 155.946 150.183 137.804 1.00 58.61  ? 397  SER A N    1 
ATOM   7097 C CA   . SER B 1 397 ? 156.892 149.970 138.899 1.00 59.45  ? 397  SER A CA   1 
ATOM   7098 C C    . SER B 1 397 ? 157.480 151.286 139.398 1.00 57.51  ? 397  SER A C    1 
ATOM   7099 O O    . SER B 1 397 ? 157.577 151.513 140.613 1.00 58.51  ? 397  SER A O    1 
ATOM   7100 C CB   . SER B 1 397 ? 158.002 149.018 138.459 1.00 68.80  ? 397  SER A CB   1 
ATOM   7101 O OG   . SER B 1 397 ? 158.883 148.736 139.532 1.00 72.49  ? 397  SER A OG   1 
ATOM   7102 N N    . LEU B 1 398 ? 157.840 152.183 138.476 1.00 56.96  ? 398  LEU A N    1 
ATOM   7103 C CA   . LEU B 1 398 ? 158.400 153.473 138.860 1.00 62.06  ? 398  LEU A CA   1 
ATOM   7104 C C    . LEU B 1 398 ? 157.368 154.325 139.585 1.00 62.70  ? 398  LEU A C    1 
ATOM   7105 O O    . LEU B 1 398 ? 157.707 155.018 140.552 1.00 63.38  ? 398  LEU A O    1 
ATOM   7106 C CB   . LEU B 1 398 ? 158.923 154.199 137.622 1.00 59.99  ? 398  LEU A CB   1 
ATOM   7107 C CG   . LEU B 1 398 ? 159.390 155.643 137.793 1.00 60.60  ? 398  LEU A CG   1 
ATOM   7108 C CD1  . LEU B 1 398 ? 160.553 155.718 138.771 1.00 60.32  ? 398  LEU A CD1  1 
ATOM   7109 C CD2  . LEU B 1 398 ? 159.767 156.241 136.449 1.00 62.88  ? 398  LEU A CD2  1 
ATOM   7110 N N    . ALA B 1 399 ? 156.115 154.322 139.115 1.00 64.08  ? 399  ALA A N    1 
ATOM   7111 C CA   . ALA B 1 399 ? 155.096 155.130 139.772 1.00 61.87  ? 399  ALA A CA   1 
ATOM   7112 C C    . ALA B 1 399 ? 154.869 154.649 141.200 1.00 60.70  ? 399  ALA A C    1 
ATOM   7113 O O    . ALA B 1 399 ? 154.764 155.465 142.127 1.00 64.33  ? 399  ALA A O    1 
ATOM   7114 C CB   . ALA B 1 399 ? 153.793 155.092 138.975 1.00 64.01  ? 399  ALA A CB   1 
ATOM   7115 N N    . ILE B 1 400 ? 154.806 153.325 141.401 1.00 68.30  ? 400  ILE A N    1 
ATOM   7116 C CA   . ILE B 1 400 ? 154.621 152.811 142.759 1.00 68.03  ? 400  ILE A CA   1 
ATOM   7117 C C    . ILE B 1 400 ? 155.823 153.154 143.635 1.00 67.99  ? 400  ILE A C    1 
ATOM   7118 O O    . ILE B 1 400 ? 155.669 153.499 144.814 1.00 64.98  ? 400  ILE A O    1 
ATOM   7119 C CB   . ILE B 1 400 ? 154.351 151.293 142.728 1.00 67.69  ? 400  ILE A CB   1 
ATOM   7120 C CG1  . ILE B 1 400 ? 152.857 151.015 142.602 1.00 67.91  ? 400  ILE A CG1  1 
ATOM   7121 C CG2  . ILE B 1 400 ? 154.913 150.577 143.953 1.00 61.83  ? 400  ILE A CG2  1 
ATOM   7122 C CD1  . ILE B 1 400 ? 152.554 149.553 142.487 1.00 67.78  ? 400  ILE A CD1  1 
ATOM   7123 N N    . LEU B 1 401 ? 157.034 153.096 143.069 1.00 80.14  ? 401  LEU A N    1 
ATOM   7124 C CA   . LEU B 1 401 ? 158.226 153.451 143.842 1.00 80.30  ? 401  LEU A CA   1 
ATOM   7125 C C    . LEU B 1 401 ? 158.211 154.918 144.262 1.00 79.70  ? 401  LEU A C    1 
ATOM   7126 O O    . LEU B 1 401 ? 158.565 155.252 145.399 1.00 80.22  ? 401  LEU A O    1 
ATOM   7127 C CB   . LEU B 1 401 ? 159.496 153.120 143.059 1.00 79.71  ? 401  LEU A CB   1 
ATOM   7128 C CG   . LEU B 1 401 ? 160.018 151.696 143.267 1.00 78.59  ? 401  LEU A CG   1 
ATOM   7129 C CD1  . LEU B 1 401 ? 161.425 151.555 142.729 1.00 80.48  ? 401  LEU A CD1  1 
ATOM   7130 C CD2  . LEU B 1 401 ? 159.981 151.321 144.740 1.00 76.19  ? 401  LEU A CD2  1 
ATOM   7131 N N    . LEU B 1 402 ? 157.811 155.805 143.349 1.00 75.99  ? 402  LEU A N    1 
ATOM   7132 C CA   . LEU B 1 402 ? 157.783 157.239 143.629 1.00 75.75  ? 402  LEU A CA   1 
ATOM   7133 C C    . LEU B 1 402 ? 156.725 157.593 144.671 1.00 83.92  ? 402  LEU A C    1 
ATOM   7134 O O    . LEU B 1 402 ? 156.992 158.359 145.605 1.00 84.18  ? 402  LEU A O    1 
ATOM   7135 C CB   . LEU B 1 402 ? 157.548 158.013 142.331 1.00 75.71  ? 402  LEU A CB   1 
ATOM   7136 C CG   . LEU B 1 402 ? 157.380 159.529 142.430 1.00 77.14  ? 402  LEU A CG   1 
ATOM   7137 C CD1  . LEU B 1 402 ? 158.321 160.225 141.460 1.00 80.75  ? 402  LEU A CD1  1 
ATOM   7138 C CD2  . LEU B 1 402 ? 155.940 159.938 142.164 1.00 73.77  ? 402  LEU A CD2  1 
ATOM   7139 N N    . LEU B 1 403 ? 155.513 157.053 144.517 1.00 92.92  ? 403  LEU A N    1 
ATOM   7140 C CA   . LEU B 1 403 ? 154.417 157.361 145.436 1.00 88.00  ? 403  LEU A CA   1 
ATOM   7141 C C    . LEU B 1 403 ? 154.698 156.900 146.864 1.00 88.41  ? 403  LEU A C    1 
ATOM   7142 O O    . LEU B 1 403 ? 154.318 157.580 147.824 1.00 87.46  ? 403  LEU A O    1 
ATOM   7143 C CB   . LEU B 1 403 ? 153.105 156.758 144.935 1.00 85.67  ? 403  LEU A CB   1 
ATOM   7144 C CG   . LEU B 1 403 ? 152.558 157.311 143.619 1.00 88.97  ? 403  LEU A CG   1 
ATOM   7145 C CD1  . LEU B 1 403 ? 151.145 156.808 143.380 1.00 87.32  ? 403  LEU A CD1  1 
ATOM   7146 C CD2  . LEU B 1 403 ? 152.593 158.832 143.628 1.00 88.02  ? 403  LEU A CD2  1 
ATOM   7147 N N    . SER B 1 404 ? 155.353 155.750 147.032 1.00 97.46  ? 404  SER A N    1 
ATOM   7148 C CA   . SER B 1 404 ? 155.643 155.255 148.375 1.00 96.28  ? 404  SER A CA   1 
ATOM   7149 C C    . SER B 1 404 ? 156.663 156.075 149.163 1.00 95.38  ? 404  SER A C    1 
ATOM   7150 O O    . SER B 1 404 ? 156.821 155.797 150.357 1.00 95.05  ? 404  SER A O    1 
ATOM   7151 C CB   . SER B 1 404 ? 156.130 153.808 148.292 1.00 99.76  ? 404  SER A CB   1 
ATOM   7152 O OG   . SER B 1 404 ? 156.997 153.505 149.370 1.00 101.62 ? 404  SER A OG   1 
ATOM   7153 N N    . LYS B 1 405 ? 157.390 157.013 148.540 1.00 103.13 ? 405  LYS A N    1 
ATOM   7154 C CA   . LYS B 1 405 ? 158.351 157.908 149.201 1.00 105.18 ? 405  LYS A CA   1 
ATOM   7155 C C    . LYS B 1 405 ? 159.558 157.126 149.736 1.00 106.77 ? 405  LYS A C    1 
ATOM   7156 O O    . LYS B 1 405 ? 160.379 157.655 150.494 1.00 107.35 ? 405  LYS A O    1 
ATOM   7157 C CB   . LYS B 1 405 ? 157.607 158.724 150.288 1.00 105.27 ? 405  LYS A CB   1 
ATOM   7158 C CG   . LYS B 1 405 ? 158.301 159.695 151.269 1.00 105.31 ? 405  LYS A CG   1 
ATOM   7159 C CD   . LYS B 1 405 ? 159.357 160.594 150.652 1.00 104.46 ? 405  LYS A CD   1 
ATOM   7160 C CE   . LYS B 1 405 ? 159.277 161.989 151.267 1.00 106.25 ? 405  LYS A CE   1 
ATOM   7161 N NZ   . LYS B 1 405 ? 160.227 162.954 150.652 1.00 105.63 ? 405  LYS A NZ   1 
ATOM   7162 N N    . LYS B 1 406 ? 159.719 155.876 149.310 1.00 109.17 ? 406  LYS A N    1 
ATOM   7163 C CA   . LYS B 1 406 ? 160.840 155.022 149.681 1.00 109.87 ? 406  LYS A CA   1 
ATOM   7164 C C    . LYS B 1 406 ? 162.098 155.295 148.845 1.00 109.19 ? 406  LYS A C    1 
ATOM   7165 O O    . LYS B 1 406 ? 163.163 154.744 149.142 1.00 108.17 ? 406  LYS A O    1 
ATOM   7166 C CB   . LYS B 1 406 ? 160.271 153.596 149.599 1.00 108.74 ? 406  LYS A CB   1 
ATOM   7167 C CG   . LYS B 1 406 ? 161.077 152.332 149.592 1.00 108.98 ? 406  LYS A CG   1 
ATOM   7168 C CD   . LYS B 1 406 ? 160.443 151.499 150.723 1.00 108.55 ? 406  LYS A CD   1 
ATOM   7169 C CE   . LYS B 1 406 ? 161.012 150.110 150.907 1.00 109.38 ? 406  LYS A CE   1 
ATOM   7170 N NZ   . LYS B 1 406 ? 161.323 149.513 149.589 1.00 108.59 ? 406  LYS A NZ   1 
ATOM   7171 N N    . TYR B 1 407 ? 161.980 156.157 147.827 1.00 111.71 ? 407  TYR A N    1 
ATOM   7172 C CA   . TYR B 1 407 ? 163.039 156.606 146.914 1.00 110.46 ? 407  TYR A CA   1 
ATOM   7173 C C    . TYR B 1 407 ? 164.147 157.402 147.614 1.00 111.78 ? 407  TYR A C    1 
ATOM   7174 O O    . TYR B 1 407 ? 165.281 157.442 147.124 1.00 113.48 ? 407  TYR A O    1 
ATOM   7175 C CB   . TYR B 1 407 ? 162.448 157.402 145.741 1.00 109.29 ? 407  TYR A CB   1 
ATOM   7176 C CG   . TYR B 1 407 ? 161.835 158.734 146.085 1.00 108.75 ? 407  TYR A CG   1 
ATOM   7177 C CD1  . TYR B 1 407 ? 160.518 158.828 146.503 1.00 110.16 ? 407  TYR A CD1  1 
ATOM   7178 C CD2  . TYR B 1 407 ? 162.564 159.907 145.946 1.00 109.84 ? 407  TYR A CD2  1 
ATOM   7179 C CE1  . TYR B 1 407 ? 159.952 160.050 146.807 1.00 112.53 ? 407  TYR A CE1  1 
ATOM   7180 C CE2  . TYR B 1 407 ? 162.010 161.132 146.243 1.00 112.43 ? 407  TYR A CE2  1 
ATOM   7181 C CZ   . TYR B 1 407 ? 160.703 161.199 146.676 1.00 114.49 ? 407  TYR A CZ   1 
ATOM   7182 O OH   . TYR B 1 407 ? 160.145 162.420 146.978 1.00 114.74 ? 407  TYR A OH   1 
ATOM   7183 N N    . LYS B 1 408 ? 163.829 158.013 148.755 1.00 108.83 ? 408  LYS A N    1 
ATOM   7184 C CA   . LYS B 1 408 ? 164.645 158.873 149.615 1.00 109.06 ? 408  LYS A CA   1 
ATOM   7185 C C    . LYS B 1 408 ? 165.729 158.183 150.437 1.00 110.82 ? 408  LYS A C    1 
ATOM   7186 O O    . LYS B 1 408 ? 166.503 158.899 151.082 1.00 111.43 ? 408  LYS A O    1 
ATOM   7187 C CB   . LYS B 1 408 ? 163.760 159.700 150.546 1.00 109.29 ? 408  LYS A CB   1 
ATOM   7188 C CG   . LYS B 1 408 ? 162.901 160.687 149.798 1.00 109.22 ? 408  LYS A CG   1 
ATOM   7189 C CD   . LYS B 1 408 ? 163.813 161.754 149.203 1.00 108.53 ? 408  LYS A CD   1 
ATOM   7190 C CE   . LYS B 1 408 ? 163.127 163.100 149.073 1.00 108.16 ? 408  LYS A CE   1 
ATOM   7191 N NZ   . LYS B 1 408 ? 163.981 164.081 148.345 1.00 109.83 ? 408  LYS A NZ   1 
ATOM   7192 N N    . GLN B 1 409 ? 165.843 156.857 150.461 1.00 119.84 ? 409  GLN A N    1 
ATOM   7193 C CA   . GLN B 1 409 ? 166.826 156.313 151.394 1.00 119.88 ? 409  GLN A CA   1 
ATOM   7194 C C    . GLN B 1 409 ? 168.093 155.896 150.644 1.00 120.06 ? 409  GLN A C    1 
ATOM   7195 O O    . GLN B 1 409 ? 168.261 156.271 149.479 1.00 117.75 ? 409  GLN A O    1 
ATOM   7196 C CB   . GLN B 1 409 ? 166.233 155.132 152.167 1.00 118.81 ? 409  GLN A CB   1 
ATOM   7197 C CG   . GLN B 1 409 ? 166.671 155.043 153.625 1.00 119.19 ? 409  GLN A CG   1 
ATOM   7198 C CD   . GLN B 1 409 ? 166.108 153.820 154.325 1.00 120.37 ? 409  GLN A CD   1 
ATOM   7199 O OE1  . GLN B 1 409 ? 165.274 153.106 153.771 1.00 118.86 ? 409  GLN A OE1  1 
ATOM   7200 N NE2  . GLN B 1 409 ? 166.562 153.574 155.549 1.00 120.02 ? 409  GLN A NE2  1 
ATOM   7201 N N    . LEU B 1 410 ? 168.995 155.137 151.275 1.00 119.41 ? 410  LEU A N    1 
ATOM   7202 C CA   . LEU B 1 410 ? 170.224 154.747 150.579 1.00 118.72 ? 410  LEU A CA   1 
ATOM   7203 C C    . LEU B 1 410 ? 170.144 153.798 149.383 1.00 119.22 ? 410  LEU A C    1 
ATOM   7204 O O    . LEU B 1 410 ? 170.633 154.181 148.313 1.00 119.54 ? 410  LEU A O    1 
ATOM   7205 C CB   . LEU B 1 410 ? 171.214 154.175 151.606 1.00 118.26 ? 410  LEU A CB   1 
ATOM   7206 C CG   . LEU B 1 410 ? 172.704 154.238 151.259 1.00 118.07 ? 410  LEU A CG   1 
ATOM   7207 C CD1  . LEU B 1 410 ? 173.053 155.533 150.541 1.00 117.87 ? 410  LEU A CD1  1 
ATOM   7208 C CD2  . LEU B 1 410 ? 173.555 154.071 152.507 1.00 118.25 ? 410  LEU A CD2  1 
ATOM   7209 N N    . PRO B 1 411 ? 169.571 152.594 149.453 1.00 115.95 ? 411  PRO A N    1 
ATOM   7210 C CA   . PRO B 1 411 ? 169.762 151.691 148.305 1.00 114.54 ? 411  PRO A CA   1 
ATOM   7211 C C    . PRO B 1 411 ? 168.715 151.866 147.220 1.00 112.13 ? 411  PRO A C    1 
ATOM   7212 O O    . PRO B 1 411 ? 169.014 151.661 146.037 1.00 112.62 ? 411  PRO A O    1 
ATOM   7213 C CB   . PRO B 1 411 ? 169.679 150.293 148.943 1.00 111.42 ? 411  PRO A CB   1 
ATOM   7214 C CG   . PRO B 1 411 ? 169.410 150.532 150.438 1.00 113.52 ? 411  PRO A CG   1 
ATOM   7215 C CD   . PRO B 1 411 ? 168.845 151.905 150.533 1.00 113.89 ? 411  PRO A CD   1 
ATOM   7216 N N    . HIS B 1 412 ? 167.493 152.227 147.601 1.00 104.52 ? 412  HIS A N    1 
ATOM   7217 C CA   . HIS B 1 412 ? 166.382 152.331 146.662 1.00 105.31 ? 412  HIS A CA   1 
ATOM   7218 C C    . HIS B 1 412 ? 166.603 153.444 145.639 1.00 107.75 ? 412  HIS A C    1 
ATOM   7219 O O    . HIS B 1 412 ? 166.027 153.430 144.542 1.00 111.16 ? 412  HIS A O    1 
ATOM   7220 C CB   . HIS B 1 412 ? 165.099 152.495 147.459 1.00 106.26 ? 412  HIS A CB   1 
ATOM   7221 C CG   . HIS B 1 412 ? 164.648 151.204 148.061 1.00 106.75 ? 412  HIS A CG   1 
ATOM   7222 N ND1  . HIS B 1 412 ? 164.752 150.943 149.410 1.00 105.70 ? 412  HIS A ND1  1 
ATOM   7223 C CD2  . HIS B 1 412 ? 164.188 150.067 147.490 1.00 106.10 ? 412  HIS A CD2  1 
ATOM   7224 C CE1  . HIS B 1 412 ? 164.334 149.713 149.650 1.00 104.23 ? 412  HIS A CE1  1 
ATOM   7225 N NE2  . HIS B 1 412 ? 163.985 149.160 148.502 1.00 105.27 ? 412  HIS A NE2  1 
ATOM   7226 N N    . MET B 1 413 ? 167.357 154.471 146.016 1.00 108.96 ? 413  MET A N    1 
ATOM   7227 C CA   . MET B 1 413 ? 167.593 155.572 145.092 1.00 110.93 ? 413  MET A CA   1 
ATOM   7228 C C    . MET B 1 413 ? 168.311 155.103 143.827 1.00 109.64 ? 413  MET A C    1 
ATOM   7229 O O    . MET B 1 413 ? 167.934 155.477 142.707 1.00 106.80 ? 413  MET A O    1 
ATOM   7230 C CB   . MET B 1 413 ? 168.402 156.666 145.790 1.00 110.17 ? 413  MET A CB   1 
ATOM   7231 C CG   . MET B 1 413 ? 168.275 158.041 145.156 1.00 111.54 ? 413  MET A CG   1 
ATOM   7232 S SD   . MET B 1 413 ? 168.785 159.390 146.244 1.00 116.93 ? 413  MET A SD   1 
ATOM   7233 C CE   . MET B 1 413 ? 169.943 158.554 147.326 1.00 109.61 ? 413  MET A CE   1 
ATOM   7234 N N    . LEU B 1 414 ? 169.365 154.295 143.988 1.00 104.17 ? 414  LEU A N    1 
ATOM   7235 C CA   . LEU B 1 414 ? 170.069 153.771 142.821 1.00 103.69 ? 414  LEU A CA   1 
ATOM   7236 C C    . LEU B 1 414 ? 169.199 152.860 141.951 1.00 102.79 ? 414  LEU A C    1 
ATOM   7237 O O    . LEU B 1 414 ? 169.332 152.865 140.721 1.00 105.65 ? 414  LEU A O    1 
ATOM   7238 C CB   . LEU B 1 414 ? 171.318 153.027 143.292 1.00 104.80 ? 414  LEU A CB   1 
ATOM   7239 C CG   . LEU B 1 414 ? 172.204 153.820 144.262 1.00 102.93 ? 414  LEU A CG   1 
ATOM   7240 C CD1  . LEU B 1 414 ? 173.412 153.008 144.682 1.00 102.31 ? 414  LEU A CD1  1 
ATOM   7241 C CD2  . LEU B 1 414 ? 172.619 155.180 143.728 1.00 103.45 ? 414  LEU A CD2  1 
ATOM   7242 N N    . THR B 1 415 ? 168.299 152.066 142.557 1.00 93.24  ? 415  THR A N    1 
ATOM   7243 C CA   . THR B 1 415 ? 167.411 151.256 141.717 1.00 93.38  ? 415  THR A CA   1 
ATOM   7244 C C    . THR B 1 415 ? 166.490 152.153 140.898 1.00 95.04  ? 415  THR A C    1 
ATOM   7245 O O    . THR B 1 415 ? 166.227 151.864 139.725 1.00 99.84  ? 415  THR A O    1 
ATOM   7246 C CB   . THR B 1 415 ? 166.653 150.156 142.487 1.00 92.35  ? 415  THR A CB   1 
ATOM   7247 O OG1  . THR B 1 415 ? 165.888 149.383 141.553 1.00 92.49  ? 415  THR A OG1  1 
ATOM   7248 C CG2  . THR B 1 415 ? 165.703 150.670 143.497 1.00 94.34  ? 415  THR A CG2  1 
ATOM   7249 N N    . THR B 1 416 ? 165.957 153.213 141.519 1.00 89.90  ? 416  THR A N    1 
ATOM   7250 C CA   . THR B 1 416 ? 165.085 154.147 140.807 1.00 94.55  ? 416  THR A CA   1 
ATOM   7251 C C    . THR B 1 416 ? 165.831 154.807 139.652 1.00 95.60  ? 416  THR A C    1 
ATOM   7252 O O    . THR B 1 416 ? 165.285 154.974 138.551 1.00 94.87  ? 416  THR A O    1 
ATOM   7253 C CB   . THR B 1 416 ? 164.537 155.207 141.764 1.00 92.90  ? 416  THR A CB   1 
ATOM   7254 O OG1  . THR B 1 416 ? 165.616 155.802 142.492 1.00 91.69  ? 416  THR A OG1  1 
ATOM   7255 C CG2  . THR B 1 416 ? 163.548 154.594 142.738 1.00 91.48  ? 416  THR A CG2  1 
ATOM   7256 N N    . ASN B 1 417 ? 167.103 155.149 139.880 1.00 94.51  ? 417  ASN A N    1 
ATOM   7257 C CA   . ASN B 1 417 ? 167.949 155.672 138.807 1.00 94.13  ? 417  ASN A CA   1 
ATOM   7258 C C    . ASN B 1 417 ? 168.111 154.651 137.684 1.00 94.77  ? 417  ASN A C    1 
ATOM   7259 O O    . ASN B 1 417 ? 168.089 155.014 136.502 1.00 96.28  ? 417  ASN A O    1 
ATOM   7260 C CB   . ASN B 1 417 ? 169.312 156.080 139.365 1.00 98.11  ? 417  ASN A CB   1 
ATOM   7261 C CG   . ASN B 1 417 ? 169.258 157.379 140.145 1.00 97.49  ? 417  ASN A CG   1 
ATOM   7262 O OD1  . ASN B 1 417 ? 169.386 158.463 139.576 1.00 95.06  ? 417  ASN A OD1  1 
ATOM   7263 N ND2  . ASN B 1 417 ? 169.069 157.276 141.455 1.00 96.02  ? 417  ASN A ND2  1 
ATOM   7264 N N    . LEU B 1 418 ? 168.299 153.376 138.033 1.00 80.73  ? 418  LEU A N    1 
ATOM   7265 C CA   . LEU B 1 418 ? 168.453 152.334 137.017 1.00 76.49  ? 418  LEU A CA   1 
ATOM   7266 C C    . LEU B 1 418 ? 167.183 152.209 136.176 1.00 76.67  ? 418  LEU A C    1 
ATOM   7267 O O    . LEU B 1 418 ? 167.253 152.115 134.939 1.00 83.41  ? 418  LEU A O    1 
ATOM   7268 C CB   . LEU B 1 418 ? 168.807 151.000 137.676 1.00 75.66  ? 418  LEU A CB   1 
ATOM   7269 C CG   . LEU B 1 418 ? 168.791 149.752 136.793 1.00 76.01  ? 418  LEU A CG   1 
ATOM   7270 C CD1  . LEU B 1 418 ? 170.090 148.983 136.945 1.00 74.73  ? 418  LEU A CD1  1 
ATOM   7271 C CD2  . LEU B 1 418 ? 167.607 148.862 137.130 1.00 81.51  ? 418  LEU A CD2  1 
ATOM   7272 N N    . LEU B 1 419 ? 166.020 152.178 136.836 1.00 71.54  ? 419  LEU A N    1 
ATOM   7273 C CA   . LEU B 1 419 ? 164.750 152.044 136.128 1.00 70.66  ? 419  LEU A CA   1 
ATOM   7274 C C    . LEU B 1 419 ? 164.488 153.232 135.215 1.00 75.67  ? 419  LEU A C    1 
ATOM   7275 O O    . LEU B 1 419 ? 163.920 153.057 134.131 1.00 80.44  ? 419  LEU A O    1 
ATOM   7276 C CB   . LEU B 1 419 ? 163.577 151.908 137.100 1.00 71.17  ? 419  LEU A CB   1 
ATOM   7277 C CG   . LEU B 1 419 ? 163.582 150.907 138.246 1.00 74.47  ? 419  LEU A CG   1 
ATOM   7278 C CD1  . LEU B 1 419 ? 162.522 151.285 139.252 1.00 75.33  ? 419  LEU A CD1  1 
ATOM   7279 C CD2  . LEU B 1 419 ? 163.295 149.541 137.695 1.00 75.73  ? 419  LEU A CD2  1 
ATOM   7280 N N    . ILE B 1 420 ? 164.875 154.441 135.632 1.00 81.39  ? 420  ILE A N    1 
ATOM   7281 C CA   . ILE B 1 420 ? 164.715 155.601 134.754 1.00 82.90  ? 420  ILE A CA   1 
ATOM   7282 C C    . ILE B 1 420 ? 165.540 155.433 133.478 1.00 80.08  ? 420  ILE A C    1 
ATOM   7283 O O    . ILE B 1 420 ? 165.062 155.712 132.371 1.00 78.37  ? 420  ILE A O    1 
ATOM   7284 C CB   . ILE B 1 420 ? 165.091 156.892 135.505 1.00 85.04  ? 420  ILE A CB   1 
ATOM   7285 C CG1  . ILE B 1 420 ? 164.066 157.192 136.600 1.00 86.74  ? 420  ILE A CG1  1 
ATOM   7286 C CG2  . ILE B 1 420 ? 165.197 158.071 134.548 1.00 83.63  ? 420  ILE A CG2  1 
ATOM   7287 C CD1  . ILE B 1 420 ? 164.532 158.223 137.602 1.00 84.31  ? 420  ILE A CD1  1 
ATOM   7288 N N    . ALA B 1 421 ? 166.774 154.934 133.608 1.00 74.21  ? 421  ALA A N    1 
ATOM   7289 C CA   . ALA B 1 421 ? 167.615 154.689 132.435 1.00 74.08  ? 421  ALA A CA   1 
ATOM   7290 C C    . ALA B 1 421 ? 167.003 153.645 131.504 1.00 74.99  ? 421  ALA A C    1 
ATOM   7291 O O    . ALA B 1 421 ? 167.007 153.814 130.274 1.00 79.29  ? 421  ALA A O    1 
ATOM   7292 C CB   . ALA B 1 421 ? 169.012 154.258 132.877 1.00 76.63  ? 421  ALA A CB   1 
ATOM   7293 N N    . GLN B 1 422 ? 166.469 152.560 132.072 1.00 68.48  ? 422  GLN A N    1 
ATOM   7294 C CA   . GLN B 1 422 ? 165.811 151.550 131.243 1.00 66.45  ? 422  GLN A CA   1 
ATOM   7295 C C    . GLN B 1 422 ? 164.582 152.130 130.541 1.00 63.04  ? 422  GLN A C    1 
ATOM   7296 O O    . GLN B 1 422 ? 164.290 151.791 129.381 1.00 63.68  ? 422  GLN A O    1 
ATOM   7297 C CB   . GLN B 1 422 ? 165.429 150.352 132.109 1.00 66.13  ? 422  GLN A CB   1 
ATOM   7298 C CG   . GLN B 1 422 ? 166.599 149.514 132.584 1.00 64.25  ? 422  GLN A CG   1 
ATOM   7299 C CD   . GLN B 1 422 ? 166.173 148.432 133.559 1.00 65.58  ? 422  GLN A CD   1 
ATOM   7300 O OE1  . GLN B 1 422 ? 165.034 148.417 134.026 1.00 65.92  ? 422  GLN A OE1  1 
ATOM   7301 N NE2  . GLN B 1 422 ? 167.090 147.528 133.880 1.00 66.04  ? 422  GLN A NE2  1 
ATOM   7302 N N    . SER B 1 423 ? 163.864 153.024 131.229 1.00 64.09  ? 423  SER A N    1 
ATOM   7303 C CA   . SER B 1 423 ? 162.706 153.685 130.637 1.00 64.22  ? 423  SER A CA   1 
ATOM   7304 C C    . SER B 1 423 ? 163.125 154.533 129.445 1.00 68.36  ? 423  SER A C    1 
ATOM   7305 O O    . SER B 1 423 ? 162.441 154.562 128.414 1.00 67.74  ? 423  SER A O    1 
ATOM   7306 C CB   . SER B 1 423 ? 161.990 154.536 131.683 1.00 69.33  ? 423  SER A CB   1 
ATOM   7307 O OG   . SER B 1 423 ? 160.755 155.018 131.181 1.00 74.45  ? 423  SER A OG   1 
ATOM   7308 N N    . ILE B 1 424 ? 164.252 155.240 129.577 1.00 79.23  ? 424  ILE A N    1 
ATOM   7309 C CA   . ILE B 1 424 ? 164.728 156.066 128.470 1.00 76.89  ? 424  ILE A CA   1 
ATOM   7310 C C    . ILE B 1 424 ? 165.131 155.185 127.296 1.00 79.54  ? 424  ILE A C    1 
ATOM   7311 O O    . ILE B 1 424 ? 164.916 155.548 126.137 1.00 82.88  ? 424  ILE A O    1 
ATOM   7312 C CB   . ILE B 1 424 ? 165.887 156.985 128.910 1.00 76.49  ? 424  ILE A CB   1 
ATOM   7313 C CG1  . ILE B 1 424 ? 165.512 157.799 130.148 1.00 80.96  ? 424  ILE A CG1  1 
ATOM   7314 C CG2  . ILE B 1 424 ? 166.315 157.906 127.772 1.00 78.39  ? 424  ILE A CG2  1 
ATOM   7315 C CD1  . ILE B 1 424 ? 166.483 158.919 130.471 1.00 80.51  ? 424  ILE A CD1  1 
ATOM   7316 N N    . VAL B 1 425 ? 165.723 154.020 127.574 1.00 74.47  ? 425  VAL A N    1 
ATOM   7317 C CA   . VAL B 1 425 ? 166.116 153.110 126.493 1.00 70.30  ? 425  VAL A CA   1 
ATOM   7318 C C    . VAL B 1 425 ? 164.892 152.648 125.696 1.00 70.02  ? 425  VAL A C    1 
ATOM   7319 O O    . VAL B 1 425 ? 164.876 152.692 124.456 1.00 66.69  ? 425  VAL A O    1 
ATOM   7320 C CB   . VAL B 1 425 ? 166.908 151.916 127.058 1.00 69.30  ? 425  VAL A CB   1 
ATOM   7321 C CG1  . VAL B 1 425 ? 166.859 150.724 126.108 1.00 71.47  ? 425  VAL A CG1  1 
ATOM   7322 C CG2  . VAL B 1 425 ? 168.348 152.316 127.335 1.00 72.47  ? 425  VAL A CG2  1 
ATOM   7323 N N    . CYS B 1 426 ? 163.835 152.229 126.404 1.00 77.07  ? 426  CYS A N    1 
ATOM   7324 C CA   . CYS B 1 426 ? 162.597 151.815 125.732 1.00 75.03  ? 426  CYS A CA   1 
ATOM   7325 C C    . CYS B 1 426 ? 161.936 152.962 124.961 1.00 78.59  ? 426  CYS A C    1 
ATOM   7326 O O    . CYS B 1 426 ? 161.489 152.782 123.815 1.00 78.08  ? 426  CYS A O    1 
ATOM   7327 C CB   . CYS B 1 426 ? 161.628 151.222 126.755 1.00 71.54  ? 426  CYS A CB   1 
ATOM   7328 S SG   . CYS B 1 426 ? 162.256 149.751 127.603 1.00 74.82  ? 426  CYS A SG   1 
ATOM   7329 N N    . ALA B 1 427 ? 161.883 154.156 125.563 1.00 89.16  ? 427  ALA A N    1 
ATOM   7330 C CA   . ALA B 1 427 ? 161.304 155.309 124.875 1.00 86.57  ? 427  ALA A CA   1 
ATOM   7331 C C    . ALA B 1 427 ? 162.107 155.663 123.632 1.00 87.18  ? 427  ALA A C    1 
ATOM   7332 O O    . ALA B 1 427 ? 161.544 156.028 122.591 1.00 88.35  ? 427  ALA A O    1 
ATOM   7333 C CB   . ALA B 1 427 ? 161.223 156.503 125.825 1.00 87.83  ? 427  ALA A CB   1 
ATOM   7334 N N    . GLY B 1 428 ? 163.429 155.594 123.740 1.00 93.73  ? 428  GLY A N    1 
ATOM   7335 C CA   . GLY B 1 428 ? 164.316 155.867 122.640 1.00 95.18  ? 428  GLY A CA   1 
ATOM   7336 C C    . GLY B 1 428 ? 164.083 154.909 121.496 1.00 96.91  ? 428  GLY A C    1 
ATOM   7337 O O    . GLY B 1 428 ? 164.104 155.318 120.339 1.00 98.47  ? 428  GLY A O    1 
ATOM   7338 N N    . MET B 1 429 ? 163.864 153.632 121.806 1.00 97.03  ? 429  MET A N    1 
ATOM   7339 C CA   . MET B 1 429 ? 163.587 152.643 120.767 1.00 97.10  ? 429  MET A CA   1 
ATOM   7340 C C    . MET B 1 429 ? 162.273 152.933 120.050 1.00 93.70  ? 429  MET A C    1 
ATOM   7341 O O    . MET B 1 429 ? 162.178 152.813 118.814 1.00 92.68  ? 429  MET A O    1 
ATOM   7342 C CB   . MET B 1 429 ? 163.533 151.237 121.354 1.00 95.01  ? 429  MET A CB   1 
ATOM   7343 C CG   . MET B 1 429 ? 163.405 150.153 120.299 1.00 90.72  ? 429  MET A CG   1 
ATOM   7344 S SD   . MET B 1 429 ? 164.644 150.317 119.003 1.00 92.47  ? 429  MET A SD   1 
ATOM   7345 C CE   . MET B 1 429 ? 163.788 149.599 117.604 1.00 92.56  ? 429  MET A CE   1 
ATOM   7346 N N    . MET B 1 430 ? 161.260 153.323 120.828 1.00 90.62  ? 430  MET A N    1 
ATOM   7347 C CA   . MET B 1 430 ? 159.987 153.705 120.227 1.00 89.24  ? 430  MET A CA   1 
ATOM   7348 C C    . MET B 1 430 ? 160.098 154.919 119.312 1.00 91.69  ? 430  MET A C    1 
ATOM   7349 O O    . MET B 1 430 ? 159.529 154.914 118.216 1.00 91.62  ? 430  MET A O    1 
ATOM   7350 C CB   . MET B 1 430 ? 158.964 153.999 121.335 1.00 91.67  ? 430  MET A CB   1 
ATOM   7351 C CG   . MET B 1 430 ? 158.362 152.779 122.027 1.00 90.30  ? 430  MET A CG   1 
ATOM   7352 S SD   . MET B 1 430 ? 157.226 151.745 121.070 1.00 91.58  ? 430  MET A SD   1 
ATOM   7353 C CE   . MET B 1 430 ? 156.582 152.899 119.853 1.00 91.92  ? 430  MET A CE   1 
ATOM   7354 N N    . ILE B 1 431 ? 160.807 155.963 119.740 1.00 105.53 ? 431  ILE A N    1 
ATOM   7355 C CA   . ILE B 1 431 ? 161.070 157.103 118.862 1.00 106.40 ? 431  ILE A CA   1 
ATOM   7356 C C    . ILE B 1 431 ? 161.928 156.703 117.660 1.00 106.97 ? 431  ILE A C    1 
ATOM   7357 O O    . ILE B 1 431 ? 161.748 157.217 116.549 1.00 106.83 ? 431  ILE A O    1 
ATOM   7358 C CB   . ILE B 1 431 ? 161.737 158.238 119.666 1.00 105.80 ? 431  ILE A CB   1 
ATOM   7359 C CG1  . ILE B 1 431 ? 160.802 158.726 120.775 1.00 108.31 ? 431  ILE A CG1  1 
ATOM   7360 C CG2  . ILE B 1 431 ? 162.121 159.411 118.774 1.00 104.05 ? 431  ILE A CG2  1 
ATOM   7361 C CD1  . ILE B 1 431 ? 159.436 159.148 120.282 1.00 107.38 ? 431  ILE A CD1  1 
ATOM   7362 N N    . TRP B 1 432 ? 162.830 155.742 117.875 1.00 113.85 ? 432  TRP A N    1 
ATOM   7363 C CA   . TRP B 1 432 ? 163.790 155.326 116.855 1.00 113.18 ? 432  TRP A CA   1 
ATOM   7364 C C    . TRP B 1 432 ? 163.139 154.636 115.665 1.00 112.08 ? 432  TRP A C    1 
ATOM   7365 O O    . TRP B 1 432 ? 163.537 154.877 114.520 1.00 108.77 ? 432  TRP A O    1 
ATOM   7366 C CB   . TRP B 1 432 ? 164.876 154.439 117.474 1.00 114.27 ? 432  TRP A CB   1 
ATOM   7367 C CG   . TRP B 1 432 ? 165.651 153.601 116.474 1.00 115.90 ? 432  TRP A CG   1 
ATOM   7368 C CD1  . TRP B 1 432 ? 165.286 152.394 115.934 1.00 115.88 ? 432  TRP A CD1  1 
ATOM   7369 C CD2  . TRP B 1 432 ? 166.884 153.961 115.840 1.00 115.10 ? 432  TRP A CD2  1 
ATOM   7370 N NE1  . TRP B 1 432 ? 166.236 151.969 115.039 1.00 116.28 ? 432  TRP A NE1  1 
ATOM   7371 C CE2  . TRP B 1 432 ? 167.225 152.913 114.961 1.00 114.44 ? 432  TRP A CE2  1 
ATOM   7372 C CE3  . TRP B 1 432 ? 167.743 155.059 115.946 1.00 114.38 ? 432  TRP A CE3  1 
ATOM   7373 C CZ2  . TRP B 1 432 ? 168.386 152.934 114.192 1.00 113.13 ? 432  TRP A CZ2  1 
ATOM   7374 C CZ3  . TRP B 1 432 ? 168.895 155.076 115.182 1.00 115.54 ? 432  TRP A CZ3  1 
ATOM   7375 C CH2  . TRP B 1 432 ? 169.206 154.021 114.318 1.00 114.27 ? 432  TRP A CH2  1 
ATOM   7376 N N    . ASN B 1 433 ? 162.183 153.732 115.914 1.00 117.69 ? 433  ASN A N    1 
ATOM   7377 C CA   . ASN B 1 433 ? 161.702 152.880 114.822 1.00 116.55 ? 433  ASN A CA   1 
ATOM   7378 C C    . ASN B 1 433 ? 161.039 153.677 113.698 1.00 117.72 ? 433  ASN A C    1 
ATOM   7379 O O    . ASN B 1 433 ? 161.171 153.322 112.521 1.00 119.15 ? 433  ASN A O    1 
ATOM   7380 C CB   . ASN B 1 433 ? 160.729 151.834 115.367 1.00 117.03 ? 433  ASN A CB   1 
ATOM   7381 C CG   . ASN B 1 433 ? 160.275 150.852 114.305 1.00 116.77 ? 433  ASN A CG   1 
ATOM   7382 O OD1  . ASN B 1 433 ? 161.022 150.529 113.382 1.00 118.97 ? 433  ASN A OD1  1 
ATOM   7383 N ND2  . ASN B 1 433 ? 159.043 150.371 114.431 1.00 114.95 ? 433  ASN A ND2  1 
ATOM   7384 N N    . PHE B 1 434 ? 160.330 154.753 114.028 1.00 121.32 ? 434  PHE A N    1 
ATOM   7385 C CA   . PHE B 1 434 ? 159.612 155.535 113.028 1.00 120.80 ? 434  PHE A CA   1 
ATOM   7386 C C    . PHE B 1 434 ? 160.486 156.592 112.348 1.00 120.73 ? 434  PHE A C    1 
ATOM   7387 O O    . PHE B 1 434 ? 159.948 157.543 111.768 1.00 119.34 ? 434  PHE A O    1 
ATOM   7388 C CB   . PHE B 1 434 ? 158.367 156.173 113.644 1.00 120.70 ? 434  PHE A CB   1 
ATOM   7389 C CG   . PHE B 1 434 ? 157.292 155.180 113.976 1.00 120.71 ? 434  PHE A CG   1 
ATOM   7390 C CD1  . PHE B 1 434 ? 156.537 154.603 112.967 1.00 120.53 ? 434  PHE A CD1  1 
ATOM   7391 C CD2  . PHE B 1 434 ? 157.041 154.812 115.287 1.00 120.99 ? 434  PHE A CD2  1 
ATOM   7392 C CE1  . PHE B 1 434 ? 155.547 153.683 113.258 1.00 120.54 ? 434  PHE A CE1  1 
ATOM   7393 C CE2  . PHE B 1 434 ? 156.052 153.892 115.585 1.00 121.80 ? 434  PHE A CE2  1 
ATOM   7394 C CZ   . PHE B 1 434 ? 155.305 153.327 114.569 1.00 120.48 ? 434  PHE A CZ   1 
ATOM   7395 N N    . VAL B 1 435 ? 161.811 156.452 112.401 1.00 129.31 ? 435  VAL A N    1 
ATOM   7396 C CA   . VAL B 1 435 ? 162.702 157.547 112.026 1.00 129.15 ? 435  VAL A CA   1 
ATOM   7397 C C    . VAL B 1 435 ? 163.378 157.393 110.664 1.00 129.58 ? 435  VAL A C    1 
ATOM   7398 O O    . VAL B 1 435 ? 163.867 158.398 110.126 1.00 129.89 ? 435  VAL A O    1 
ATOM   7399 C CB   . VAL B 1 435 ? 163.778 157.765 113.109 1.00 128.34 ? 435  VAL A CB   1 
ATOM   7400 N N    . LYS B 1 436 ? 163.461 156.171 110.114 1.00 126.75 ? 436  LYS A N    1 
ATOM   7401 C CA   . LYS B 1 436 ? 164.286 155.942 108.924 1.00 125.97 ? 436  LYS A CA   1 
ATOM   7402 C C    . LYS B 1 436 ? 163.850 156.801 107.740 1.00 126.97 ? 436  LYS A C    1 
ATOM   7403 O O    . LYS B 1 436 ? 164.675 157.139 106.884 1.00 127.22 ? 436  LYS A O    1 
ATOM   7404 C CB   . LYS B 1 436 ? 164.252 154.463 108.542 1.00 125.71 ? 436  LYS A CB   1 
ATOM   7405 N N    . GLU B 1 437 ? 162.570 157.161 107.672 1.00 131.24 ? 437  GLU A N    1 
ATOM   7406 C CA   . GLU B 1 437 ? 162.015 157.871 106.529 1.00 131.38 ? 437  GLU A CA   1 
ATOM   7407 C C    . GLU B 1 437 ? 161.898 159.361 106.813 1.00 131.81 ? 437  GLU A C    1 
ATOM   7408 O O    . GLU B 1 437 ? 161.233 160.082 106.061 1.00 131.06 ? 437  GLU A O    1 
ATOM   7409 C CB   . GLU B 1 437 ? 160.651 157.292 106.151 1.00 128.98 ? 437  GLU A CB   1 
ATOM   7410 N N    . LYS B 1 438 ? 162.532 159.828 107.882 1.00 141.84 ? 438  LYS A N    1 
ATOM   7411 C CA   . LYS B 1 438 ? 162.390 161.197 108.361 1.00 141.81 ? 438  LYS A CA   1 
ATOM   7412 C C    . LYS B 1 438 ? 163.760 161.865 108.460 1.00 141.95 ? 438  LYS A C    1 
ATOM   7413 O O    . LYS B 1 438 ? 164.753 161.411 107.877 1.00 140.66 ? 438  LYS A O    1 
ATOM   7414 C CB   . LYS B 1 438 ? 161.641 161.209 109.700 1.00 141.30 ? 438  LYS A CB   1 
ATOM   7415 N N    . ASN B 1 439 ? 163.791 162.981 109.191 1.00 147.59 ? 439  ASN A N    1 
ATOM   7416 C CA   . ASN B 1 439 ? 164.926 163.895 109.247 1.00 147.23 ? 439  ASN A CA   1 
ATOM   7417 C C    . ASN B 1 439 ? 166.219 163.206 109.678 1.00 148.32 ? 439  ASN A C    1 
ATOM   7418 O O    . ASN B 1 439 ? 166.277 162.557 110.727 1.00 148.71 ? 439  ASN A O    1 
ATOM   7419 C CB   . ASN B 1 439 ? 164.611 165.049 110.200 1.00 146.98 ? 439  ASN A CB   1 
ATOM   7420 N N    . PHE B 1 440 ? 167.249 163.345 108.839 1.00 149.53 ? 440  PHE A N    1 
ATOM   7421 C CA   . PHE B 1 440 ? 168.554 162.731 109.079 1.00 148.92 ? 440  PHE A CA   1 
ATOM   7422 C C    . PHE B 1 440 ? 169.194 163.255 110.361 1.00 149.35 ? 440  PHE A C    1 
ATOM   7423 O O    . PHE B 1 440 ? 169.925 162.522 111.036 1.00 149.87 ? 440  PHE A O    1 
ATOM   7424 C CB   . PHE B 1 440 ? 169.471 162.978 107.880 1.00 148.43 ? 440  PHE A CB   1 
ATOM   7425 C CG   . PHE B 1 440 ? 170.885 162.516 108.087 1.00 148.90 ? 440  PHE A CG   1 
ATOM   7426 C CD1  . PHE B 1 440 ? 171.192 161.166 108.094 1.00 149.54 ? 440  PHE A CD1  1 
ATOM   7427 C CD2  . PHE B 1 440 ? 171.907 163.434 108.268 1.00 148.74 ? 440  PHE A CD2  1 
ATOM   7428 C CE1  . PHE B 1 440 ? 172.494 160.738 108.283 1.00 149.83 ? 440  PHE A CE1  1 
ATOM   7429 C CE2  . PHE B 1 440 ? 173.210 163.013 108.458 1.00 149.93 ? 440  PHE A CE2  1 
ATOM   7430 C CZ   . PHE B 1 440 ? 173.503 161.663 108.465 1.00 149.60 ? 440  PHE A CZ   1 
ATOM   7431 N N    . VAL B 1 441 ? 168.956 164.525 110.687 1.00 149.20 ? 441  VAL A N    1 
ATOM   7432 C CA   . VAL B 1 441 ? 169.490 165.133 111.906 1.00 148.83 ? 441  VAL A CA   1 
ATOM   7433 C C    . VAL B 1 441 ? 168.938 164.439 113.150 1.00 147.91 ? 441  VAL A C    1 
ATOM   7434 O O    . VAL B 1 441 ? 169.654 164.251 114.140 1.00 146.84 ? 441  VAL A O    1 
ATOM   7435 C CB   . VAL B 1 441 ? 169.199 166.646 111.919 1.00 148.13 ? 441  VAL A CB   1 
ATOM   7436 C CG1  . VAL B 1 441 ? 170.195 167.380 111.037 1.00 148.26 ? 441  VAL A CG1  1 
ATOM   7437 C CG2  . VAL B 1 441 ? 167.776 166.923 111.451 1.00 146.74 ? 441  VAL A CG2  1 
ATOM   7438 N N    . GLY B 1 442 ? 167.656 164.071 113.129 1.00 143.93 ? 442  GLY A N    1 
ATOM   7439 C CA   . GLY B 1 442 ? 167.069 163.324 114.234 1.00 143.34 ? 442  GLY A CA   1 
ATOM   7440 C C    . GLY B 1 442 ? 167.701 161.968 114.509 1.00 143.01 ? 442  GLY A C    1 
ATOM   7441 O O    . GLY B 1 442 ? 167.604 161.454 115.624 1.00 142.36 ? 442  GLY A O    1 
ATOM   7442 N N    . GLN B 1 443 ? 168.280 161.336 113.491 1.00 145.43 ? 443  GLN A N    1 
ATOM   7443 C CA   . GLN B 1 443 ? 169.037 160.098 113.693 1.00 145.37 ? 443  GLN A CA   1 
ATOM   7444 C C    . GLN B 1 443 ? 170.128 160.209 114.769 1.00 145.41 ? 443  GLN A C    1 
ATOM   7445 O O    . GLN B 1 443 ? 170.204 159.368 115.675 1.00 144.73 ? 443  GLN A O    1 
ATOM   7446 C CB   . GLN B 1 443 ? 169.642 159.642 112.363 1.00 145.93 ? 443  GLN A CB   1 
ATOM   7447 C CG   . GLN B 1 443 ? 170.842 158.717 112.494 1.00 145.52 ? 443  GLN A CG   1 
ATOM   7448 C CD   . GLN B 1 443 ? 171.147 157.976 111.206 1.00 145.39 ? 443  GLN A CD   1 
ATOM   7449 O OE1  . GLN B 1 443 ? 170.876 158.471 110.112 1.00 145.87 ? 443  GLN A OE1  1 
ATOM   7450 N NE2  . GLN B 1 443 ? 171.712 156.781 111.331 1.00 144.82 ? 443  GLN A NE2  1 
ATOM   7451 N N    . ILE B 1 444 ? 170.957 161.259 114.710 1.00 142.61 ? 444  ILE A N    1 
ATOM   7452 C CA   . ILE B 1 444 ? 172.114 161.351 115.607 1.00 142.65 ? 444  ILE A CA   1 
ATOM   7453 C C    . ILE B 1 444 ? 171.718 161.584 117.072 1.00 143.09 ? 444  ILE A C    1 
ATOM   7454 O O    . ILE B 1 444 ? 172.315 160.973 117.969 1.00 143.20 ? 444  ILE A O    1 
ATOM   7455 C CB   . ILE B 1 444 ? 173.124 162.399 115.082 1.00 142.59 ? 444  ILE A CB   1 
ATOM   7456 C CG1  . ILE B 1 444 ? 174.498 162.187 115.725 1.00 141.92 ? 444  ILE A CG1  1 
ATOM   7457 C CG2  . ILE B 1 444 ? 172.645 163.845 115.236 1.00 142.29 ? 444  ILE A CG2  1 
ATOM   7458 C CD1  . ILE B 1 444 ? 175.395 161.251 114.948 1.00 141.59 ? 444  ILE A CD1  1 
ATOM   7459 N N    . LEU B 1 445 ? 170.776 162.496 117.358 1.00 140.29 ? 445  LEU A N    1 
ATOM   7460 C CA   . LEU B 1 445 ? 170.438 162.768 118.759 1.00 140.32 ? 445  LEU A CA   1 
ATOM   7461 C C    . LEU B 1 445 ? 169.885 161.509 119.422 1.00 140.05 ? 445  LEU A C    1 
ATOM   7462 O O    . LEU B 1 445 ? 170.243 161.188 120.563 1.00 138.39 ? 445  LEU A O    1 
ATOM   7463 C CB   . LEU B 1 445 ? 169.487 163.962 118.933 1.00 140.88 ? 445  LEU A CB   1 
ATOM   7464 C CG   . LEU B 1 445 ? 167.957 163.994 119.039 1.00 139.98 ? 445  LEU A CG   1 
ATOM   7465 C CD1  . LEU B 1 445 ? 167.531 165.390 119.472 1.00 139.46 ? 445  LEU A CD1  1 
ATOM   7466 C CD2  . LEU B 1 445 ? 167.269 163.663 117.766 1.00 140.06 ? 445  LEU A CD2  1 
ATOM   7467 N N    . VAL B 1 446 ? 169.024 160.778 118.709 1.00 138.86 ? 446  VAL A N    1 
ATOM   7468 C CA   . VAL B 1 446 ? 168.470 159.536 119.238 1.00 138.12 ? 446  VAL A CA   1 
ATOM   7469 C C    . VAL B 1 446 ? 169.568 158.487 119.393 1.00 137.05 ? 446  VAL A C    1 
ATOM   7470 O O    . VAL B 1 446 ? 169.560 157.716 120.358 1.00 136.81 ? 446  VAL A O    1 
ATOM   7471 C CB   . VAL B 1 446 ? 167.322 159.043 118.334 1.00 137.66 ? 446  VAL A CB   1 
ATOM   7472 C CG1  . VAL B 1 446 ? 166.717 157.760 118.870 1.00 136.74 ? 446  VAL A CG1  1 
ATOM   7473 C CG2  . VAL B 1 446 ? 166.243 160.107 118.226 1.00 137.32 ? 446  VAL A CG2  1 
ATOM   7474 N N    . PHE B 1 447 ? 170.531 158.437 118.464 1.00 135.43 ? 447  PHE A N    1 
ATOM   7475 C CA   . PHE B 1 447 ? 171.627 157.472 118.590 1.00 136.20 ? 447  PHE A CA   1 
ATOM   7476 C C    . PHE B 1 447 ? 172.420 157.734 119.871 1.00 136.38 ? 447  PHE A C    1 
ATOM   7477 O O    . PHE B 1 447 ? 172.731 156.805 120.639 1.00 137.49 ? 447  PHE A O    1 
ATOM   7478 C CB   . PHE B 1 447 ? 172.531 157.536 117.356 1.00 135.71 ? 447  PHE A CB   1 
ATOM   7479 C CG   . PHE B 1 447 ? 173.774 156.691 117.459 1.00 135.41 ? 447  PHE A CG   1 
ATOM   7480 C CD1  . PHE B 1 447 ? 173.751 155.359 117.085 1.00 135.89 ? 447  PHE A CD1  1 
ATOM   7481 C CD2  . PHE B 1 447 ? 174.975 157.241 117.887 1.00 134.37 ? 447  PHE A CD2  1 
ATOM   7482 C CE1  . PHE B 1 447 ? 174.891 154.580 117.169 1.00 135.64 ? 447  PHE A CE1  1 
ATOM   7483 C CE2  . PHE B 1 447 ? 176.117 156.468 117.973 1.00 134.86 ? 447  PHE A CE2  1 
ATOM   7484 C CZ   . PHE B 1 447 ? 176.075 155.137 117.612 1.00 135.84 ? 447  PHE A CZ   1 
ATOM   7485 N N    . VAL B 1 448 ? 172.736 159.011 120.116 1.00 134.72 ? 448  VAL A N    1 
ATOM   7486 C CA   . VAL B 1 448 ? 173.509 159.401 121.293 1.00 135.82 ? 448  VAL A CA   1 
ATOM   7487 C C    . VAL B 1 448 ? 172.718 159.072 122.550 1.00 135.68 ? 448  VAL A C    1 
ATOM   7488 O O    . VAL B 1 448 ? 173.261 158.523 123.519 1.00 134.69 ? 448  VAL A O    1 
ATOM   7489 C CB   . VAL B 1 448 ? 173.885 160.894 121.223 1.00 135.85 ? 448  VAL A CB   1 
ATOM   7490 C CG1  . VAL B 1 448 ? 174.516 161.349 122.530 1.00 135.97 ? 448  VAL A CG1  1 
ATOM   7491 C CG2  . VAL B 1 448 ? 174.834 161.146 120.062 1.00 135.54 ? 448  VAL A CG2  1 
ATOM   7492 N N    . LEU B 1 449 ? 171.412 159.367 122.534 1.00 132.95 ? 449  LEU A N    1 
ATOM   7493 C CA   . LEU B 1 449 ? 170.556 159.122 123.691 1.00 132.50 ? 449  LEU A CA   1 
ATOM   7494 C C    . LEU B 1 449 ? 170.521 157.632 124.001 1.00 130.21 ? 449  LEU A C    1 
ATOM   7495 O O    . LEU B 1 449 ? 170.662 157.223 125.164 1.00 129.21 ? 449  LEU A O    1 
ATOM   7496 C CB   . LEU B 1 449 ? 169.150 159.662 123.431 1.00 132.05 ? 449  LEU A CB   1 
ATOM   7497 C CG   . LEU B 1 449 ? 168.137 159.549 124.571 1.00 130.94 ? 449  LEU A CG   1 
ATOM   7498 C CD1  . LEU B 1 449 ? 168.406 160.606 125.632 1.00 130.62 ? 449  LEU A CD1  1 
ATOM   7499 C CD2  . LEU B 1 449 ? 166.717 159.667 124.039 1.00 130.23 ? 449  LEU A CD2  1 
ATOM   7500 N N    . LEU B 1 450 ? 170.405 156.806 122.956 1.00 126.54 ? 450  LEU A N    1 
ATOM   7501 C CA   . LEU B 1 450 ? 170.243 155.369 123.130 1.00 127.34 ? 450  LEU A CA   1 
ATOM   7502 C C    . LEU B 1 450 ? 171.500 154.772 123.732 1.00 127.63 ? 450  LEU A C    1 
ATOM   7503 O O    . LEU B 1 450 ? 171.430 154.025 124.717 1.00 129.60 ? 450  LEU A O    1 
ATOM   7504 C CB   . LEU B 1 450 ? 169.945 154.690 121.791 1.00 126.27 ? 450  LEU A CB   1 
ATOM   7505 C CG   . LEU B 1 450 ? 168.511 154.393 121.364 1.00 126.67 ? 450  LEU A CG   1 
ATOM   7506 C CD1  . LEU B 1 450 ? 167.991 153.156 122.076 1.00 125.29 ? 450  LEU A CD1  1 
ATOM   7507 C CD2  . LEU B 1 450 ? 167.640 155.568 121.663 1.00 124.38 ? 450  LEU A CD2  1 
ATOM   7508 N N    . TYR B 1 451 ? 172.669 155.106 123.183 1.00 128.38 ? 451  TYR A N    1 
ATOM   7509 C CA   . TYR B 1 451 ? 173.827 154.397 123.704 1.00 130.14 ? 451  TYR A CA   1 
ATOM   7510 C C    . TYR B 1 451 ? 174.328 155.012 125.004 1.00 131.74 ? 451  TYR A C    1 
ATOM   7511 O O    . TYR B 1 451 ? 174.887 154.284 125.834 1.00 133.17 ? 451  TYR A O    1 
ATOM   7512 C CB   . TYR B 1 451 ? 174.957 154.379 122.672 1.00 128.52 ? 451  TYR A CB   1 
ATOM   7513 C CG   . TYR B 1 451 ? 174.853 153.260 121.659 1.00 130.67 ? 451  TYR A CG   1 
ATOM   7514 C CD1  . TYR B 1 451 ? 173.703 153.086 120.899 1.00 131.46 ? 451  TYR A CD1  1 
ATOM   7515 C CD2  . TYR B 1 451 ? 175.905 152.373 121.466 1.00 131.44 ? 451  TYR A CD2  1 
ATOM   7516 C CE1  . TYR B 1 451 ? 173.604 152.064 119.974 1.00 132.73 ? 451  TYR A CE1  1 
ATOM   7517 C CE2  . TYR B 1 451 ? 175.815 151.348 120.543 1.00 132.61 ? 451  TYR A CE2  1 
ATOM   7518 C CZ   . TYR B 1 451 ? 174.663 151.198 119.801 1.00 133.07 ? 451  TYR A CZ   1 
ATOM   7519 O OH   . TYR B 1 451 ? 174.570 150.180 118.880 1.00 131.59 ? 451  TYR A OH   1 
ATOM   7520 N N    . SER B 1 452 ? 174.044 156.297 125.249 1.00 130.36 ? 452  SER A N    1 
ATOM   7521 C CA   . SER B 1 452 ? 174.333 156.905 126.544 1.00 130.71 ? 452  SER A CA   1 
ATOM   7522 C C    . SER B 1 452 ? 173.516 156.262 127.660 1.00 127.92 ? 452  SER A C    1 
ATOM   7523 O O    . SER B 1 452 ? 174.060 155.903 128.712 1.00 126.05 ? 452  SER A O    1 
ATOM   7524 C CB   . SER B 1 452 ? 174.079 158.411 126.494 1.00 130.76 ? 452  SER A CB   1 
ATOM   7525 O OG   . SER B 1 452 ? 172.831 158.698 125.899 1.00 131.92 ? 452  SER A OG   1 
ATOM   7526 N N    . SER B 1 453 ? 172.224 156.020 127.412 1.00 116.98 ? 453  SER A N    1 
ATOM   7527 C CA   . SER B 1 453 ? 171.403 155.366 128.427 1.00 116.00 ? 453  SER A CA   1 
ATOM   7528 C C    . SER B 1 453 ? 171.728 153.884 128.567 1.00 115.95 ? 453  SER A C    1 
ATOM   7529 O O    . SER B 1 453 ? 171.691 153.350 129.682 1.00 118.23 ? 453  SER A O    1 
ATOM   7530 C CB   . SER B 1 453 ? 169.923 155.559 128.099 1.00 114.47 ? 453  SER A CB   1 
ATOM   7531 O OG   . SER B 1 453 ? 169.637 156.914 127.802 1.00 113.78 ? 453  SER A OG   1 
ATOM   7532 N N    . LEU B 1 454 ? 171.999 153.187 127.462 1.00 112.95 ? 454  LEU A N    1 
ATOM   7533 C CA   . LEU B 1 454 ? 172.350 151.772 127.564 1.00 116.07 ? 454  LEU A CA   1 
ATOM   7534 C C    . LEU B 1 454 ? 173.640 151.592 128.373 1.00 118.39 ? 454  LEU A C    1 
ATOM   7535 O O    . LEU B 1 454 ? 173.724 150.725 129.262 1.00 121.38 ? 454  LEU A O    1 
ATOM   7536 C CB   . LEU B 1 454 ? 172.488 151.175 126.164 1.00 114.54 ? 454  LEU A CB   1 
ATOM   7537 C CG   . LEU B 1 454 ? 172.804 149.687 126.032 1.00 112.78 ? 454  LEU A CG   1 
ATOM   7538 C CD1  . LEU B 1 454 ? 171.946 148.907 127.020 1.00 113.80 ? 454  LEU A CD1  1 
ATOM   7539 C CD2  . LEU B 1 454 ? 172.570 149.207 124.612 1.00 115.26 ? 454  LEU A CD2  1 
ATOM   7540 N N    . TYR B 1 455 ? 174.638 152.445 128.110 1.00 125.67 ? 455  TYR A N    1 
ATOM   7541 C CA   . TYR B 1 455 ? 175.877 152.416 128.879 1.00 126.30 ? 455  TYR A CA   1 
ATOM   7542 C C    . TYR B 1 455 ? 175.623 152.773 130.336 1.00 125.27 ? 455  TYR A C    1 
ATOM   7543 O O    . TYR B 1 455 ? 176.252 152.205 131.242 1.00 123.77 ? 455  TYR A O    1 
ATOM   7544 C CB   . TYR B 1 455 ? 176.892 153.377 128.261 1.00 127.81 ? 455  TYR A CB   1 
ATOM   7545 C CG   . TYR B 1 455 ? 177.524 152.879 126.979 1.00 127.43 ? 455  TYR A CG   1 
ATOM   7546 C CD1  . TYR B 1 455 ? 177.342 151.570 126.550 1.00 126.90 ? 455  TYR A CD1  1 
ATOM   7547 C CD2  . TYR B 1 455 ? 178.292 153.726 126.189 1.00 125.84 ? 455  TYR A CD2  1 
ATOM   7548 C CE1  . TYR B 1 455 ? 177.915 151.116 125.376 1.00 127.64 ? 455  TYR A CE1  1 
ATOM   7549 C CE2  . TYR B 1 455 ? 178.868 153.281 125.014 1.00 126.85 ? 455  TYR A CE2  1 
ATOM   7550 C CZ   . TYR B 1 455 ? 178.676 151.976 124.613 1.00 127.00 ? 455  TYR A CZ   1 
ATOM   7551 O OH   . TYR B 1 455 ? 179.248 151.529 123.444 1.00 127.10 ? 455  TYR A OH   1 
ATOM   7552 N N    . SER B 1 456 ? 174.731 153.740 130.585 1.00 120.64 ? 456  SER A N    1 
ATOM   7553 C CA   . SER B 1 456 ? 174.413 154.085 131.964 1.00 120.99 ? 456  SER A CA   1 
ATOM   7554 C C    . SER B 1 456 ? 173.782 152.905 132.689 1.00 117.69 ? 456  SER A C    1 
ATOM   7555 O O    . SER B 1 456 ? 174.043 152.695 133.872 1.00 119.46 ? 456  SER A O    1 
ATOM   7556 C CB   . SER B 1 456 ? 173.488 155.300 132.003 1.00 121.19 ? 456  SER A CB   1 
ATOM   7557 O OG   . SER B 1 456 ? 173.410 155.839 133.311 1.00 120.57 ? 456  SER A OG   1 
ATOM   7558 N N    . THR B 1 457 ? 172.915 152.149 132.006 1.00 100.02 ? 457  THR A N    1 
ATOM   7559 C CA   . THR B 1 457 ? 172.300 150.969 132.616 1.00 101.93 ? 457  THR A CA   1 
ATOM   7560 C C    . THR B 1 457 ? 173.355 149.929 132.990 1.00 104.21 ? 457  THR A C    1 
ATOM   7561 O O    . THR B 1 457 ? 173.346 149.378 134.109 1.00 106.53 ? 457  THR A O    1 
ATOM   7562 C CB   . THR B 1 457 ? 171.261 150.377 131.661 1.00 99.27  ? 457  THR A CB   1 
ATOM   7563 O OG1  . THR B 1 457 ? 170.034 151.110 131.776 1.00 97.84  ? 457  THR A OG1  1 
ATOM   7564 C CG2  . THR B 1 457 ? 170.996 148.915 131.976 1.00 101.06 ? 457  THR A CG2  1 
ATOM   7565 N N    . TYR B 1 458 ? 174.338 149.738 132.099 1.00 115.10 ? 458  TYR A N    1 
ATOM   7566 C CA   . TYR B 1 458 ? 175.461 148.845 132.394 1.00 115.54 ? 458  TYR A CA   1 
ATOM   7567 C C    . TYR B 1 458 ? 176.242 149.300 133.619 1.00 114.59 ? 458  TYR A C    1 
ATOM   7568 O O    . TYR B 1 458 ? 176.563 148.489 134.495 1.00 113.75 ? 458  TYR A O    1 
ATOM   7569 C CB   . TYR B 1 458 ? 176.399 148.713 131.191 1.00 117.61 ? 458  TYR A CB   1 
ATOM   7570 C CG   . TYR B 1 458 ? 175.786 148.148 129.931 1.00 117.43 ? 458  TYR A CG   1 
ATOM   7571 C CD1  . TYR B 1 458 ? 174.716 147.265 129.992 1.00 117.47 ? 458  TYR A CD1  1 
ATOM   7572 C CD2  . TYR B 1 458 ? 176.312 148.456 128.683 1.00 114.39 ? 458  TYR A CD2  1 
ATOM   7573 C CE1  . TYR B 1 458 ? 174.168 146.728 128.844 1.00 116.48 ? 458  TYR A CE1  1 
ATOM   7574 C CE2  . TYR B 1 458 ? 175.770 147.924 127.529 1.00 114.42 ? 458  TYR A CE2  1 
ATOM   7575 C CZ   . TYR B 1 458 ? 174.703 147.057 127.617 1.00 114.59 ? 458  TYR A CZ   1 
ATOM   7576 O OH   . TYR B 1 458 ? 174.156 146.525 126.472 1.00 114.39 ? 458  TYR A OH   1 
ATOM   7577 N N    . LEU B 1 459 ? 176.570 150.588 133.698 1.00 115.40 ? 459  LEU A N    1 
ATOM   7578 C CA   . LEU B 1 459 ? 177.361 151.040 134.838 1.00 116.41 ? 459  LEU A CA   1 
ATOM   7579 C C    . LEU B 1 459 ? 176.533 151.053 136.120 1.00 116.54 ? 459  LEU A C    1 
ATOM   7580 O O    . LEU B 1 459 ? 177.063 150.796 137.210 1.00 116.17 ? 459  LEU A O    1 
ATOM   7581 C CB   . LEU B 1 459 ? 177.936 152.429 134.560 1.00 116.90 ? 459  LEU A CB   1 
ATOM   7582 C CG   . LEU B 1 459 ? 179.165 152.489 133.653 1.00 116.32 ? 459  LEU A CG   1 
ATOM   7583 C CD1  . LEU B 1 459 ? 179.368 153.899 133.123 1.00 116.06 ? 459  LEU A CD1  1 
ATOM   7584 C CD2  . LEU B 1 459 ? 180.402 152.009 134.395 1.00 115.10 ? 459  LEU A CD2  1 
ATOM   7585 N N    . TRP B 1 460 ? 175.242 151.386 136.016 1.00 115.66 ? 460  TRP A N    1 
ATOM   7586 C CA   . TRP B 1 460 ? 174.372 151.413 137.184 1.00 114.81 ? 460  TRP A CA   1 
ATOM   7587 C C    . TRP B 1 460 ? 174.228 150.041 137.824 1.00 113.75 ? 460  TRP A C    1 
ATOM   7588 O O    . TRP B 1 460 ? 174.072 149.950 139.046 1.00 113.51 ? 460  TRP A O    1 
ATOM   7589 C CB   . TRP B 1 460 ? 172.991 151.956 136.809 1.00 113.64 ? 460  TRP A CB   1 
ATOM   7590 C CG   . TRP B 1 460 ? 172.874 153.443 136.939 1.00 114.33 ? 460  TRP A CG   1 
ATOM   7591 C CD1  . TRP B 1 460 ? 172.611 154.335 135.940 1.00 115.38 ? 460  TRP A CD1  1 
ATOM   7592 C CD2  . TRP B 1 460 ? 173.073 154.219 138.124 1.00 113.30 ? 460  TRP A CD2  1 
ATOM   7593 N NE1  . TRP B 1 460 ? 172.603 155.614 136.436 1.00 115.46 ? 460  TRP A NE1  1 
ATOM   7594 C CE2  . TRP B 1 460 ? 172.888 155.571 137.774 1.00 114.45 ? 460  TRP A CE2  1 
ATOM   7595 C CE3  . TRP B 1 460 ? 173.377 153.902 139.450 1.00 113.18 ? 460  TRP A CE3  1 
ATOM   7596 C CZ2  . TRP B 1 460 ? 172.998 156.600 138.701 1.00 115.16 ? 460  TRP A CZ2  1 
ATOM   7597 C CZ3  . TRP B 1 460 ? 173.488 154.922 140.362 1.00 116.10 ? 460  TRP A CZ3  1 
ATOM   7598 C CH2  . TRP B 1 460 ? 173.298 156.255 139.988 1.00 115.73 ? 460  TRP A CH2  1 
ATOM   7599 N N    . THR B 1 461 ? 174.291 148.966 137.028 1.00 115.69 ? 461  THR A N    1 
ATOM   7600 C CA   . THR B 1 461 ? 174.249 147.630 137.630 1.00 114.85 ? 461  THR A CA   1 
ATOM   7601 C C    . THR B 1 461 ? 175.452 147.387 138.544 1.00 115.73 ? 461  THR A C    1 
ATOM   7602 O O    . THR B 1 461 ? 175.303 146.905 139.681 1.00 113.90 ? 461  THR A O    1 
ATOM   7603 C CB   . THR B 1 461 ? 174.184 146.559 136.542 1.00 115.83 ? 461  THR A CB   1 
ATOM   7604 O OG1  . THR B 1 461 ? 173.098 146.845 135.652 1.00 115.08 ? 461  THR A OG1  1 
ATOM   7605 C CG2  . THR B 1 461 ? 173.979 145.184 137.160 1.00 114.12 ? 461  THR A CG2  1 
ATOM   7606 N N    . GLY B 1 462 ? 176.642 147.787 138.092 1.00 130.46 ? 462  GLY A N    1 
ATOM   7607 C CA   . GLY B 1 462 ? 177.823 147.652 138.928 1.00 130.50 ? 462  GLY A CA   1 
ATOM   7608 C C    . GLY B 1 462 ? 177.773 148.555 140.142 1.00 131.36 ? 462  GLY A C    1 
ATOM   7609 O O    . GLY B 1 462 ? 178.210 148.167 141.231 1.00 132.21 ? 462  GLY A O    1 
ATOM   7610 N N    . LEU B 1 463 ? 177.291 149.789 139.963 1.00 125.73 ? 463  LEU A N    1 
ATOM   7611 C CA   . LEU B 1 463 ? 177.208 150.703 141.097 1.00 126.00 ? 463  LEU A CA   1 
ATOM   7612 C C    . LEU B 1 463 ? 176.244 150.165 142.149 1.00 125.53 ? 463  LEU A C    1 
ATOM   7613 O O    . LEU B 1 463 ? 176.497 150.285 143.355 1.00 123.17 ? 463  LEU A O    1 
ATOM   7614 C CB   . LEU B 1 463 ? 176.774 152.086 140.613 1.00 124.27 ? 463  LEU A CB   1 
ATOM   7615 C CG   . LEU B 1 463 ? 177.807 152.824 139.758 1.00 122.82 ? 463  LEU A CG   1 
ATOM   7616 C CD1  . LEU B 1 463 ? 177.246 154.132 139.225 1.00 122.35 ? 463  LEU A CD1  1 
ATOM   7617 C CD2  . LEU B 1 463 ? 179.081 153.069 140.551 1.00 124.30 ? 463  LEU A CD2  1 
ATOM   7618 N N    . LEU B 1 464 ? 175.141 149.547 141.704 1.00 126.85 ? 464  LEU A N    1 
ATOM   7619 C CA   . LEU B 1 464 ? 174.195 148.926 142.626 1.00 125.17 ? 464  LEU A CA   1 
ATOM   7620 C C    . LEU B 1 464 ? 174.859 147.797 143.401 1.00 125.22 ? 464  LEU A C    1 
ATOM   7621 O O    . LEU B 1 464 ? 174.662 147.662 144.616 1.00 126.15 ? 464  LEU A O    1 
ATOM   7622 C CB   . LEU B 1 464 ? 172.972 148.415 141.867 1.00 124.88 ? 464  LEU A CB   1 
ATOM   7623 C CG   . LEU B 1 464 ? 171.800 147.966 142.742 1.00 124.57 ? 464  LEU A CG   1 
ATOM   7624 C CD1  . LEU B 1 464 ? 171.173 149.160 143.442 1.00 124.02 ? 464  LEU A CD1  1 
ATOM   7625 C CD2  . LEU B 1 464 ? 170.763 147.218 141.920 1.00 125.58 ? 464  LEU A CD2  1 
ATOM   7626 N N    . ALA B 1 465 ? 175.653 146.974 142.705 1.00 131.78 ? 465  ALA A N    1 
ATOM   7627 C CA   . ALA B 1 465 ? 176.326 145.863 143.374 1.00 132.24 ? 465  ALA A CA   1 
ATOM   7628 C C    . ALA B 1 465 ? 177.328 146.369 144.407 1.00 133.10 ? 465  ALA A C    1 
ATOM   7629 O O    . ALA B 1 465 ? 177.414 145.830 145.518 1.00 134.44 ? 465  ALA A O    1 
ATOM   7630 C CB   . ALA B 1 465 ? 177.014 144.967 142.347 1.00 133.34 ? 465  ALA A CB   1 
ATOM   7631 N N    . ILE B 1 466 ? 178.107 147.392 144.047 1.00 135.61 ? 466  ILE A N    1 
ATOM   7632 C CA   . ILE B 1 466 ? 179.102 147.950 144.962 1.00 136.12 ? 466  ILE A CA   1 
ATOM   7633 C C    . ILE B 1 466 ? 178.424 148.554 146.190 1.00 137.00 ? 466  ILE A C    1 
ATOM   7634 O O    . ILE B 1 466 ? 178.893 148.389 147.326 1.00 136.54 ? 466  ILE A O    1 
ATOM   7635 C CB   . ILE B 1 466 ? 179.982 148.978 144.222 1.00 136.18 ? 466  ILE A CB   1 
ATOM   7636 C CG1  . ILE B 1 466 ? 181.064 148.261 143.412 1.00 137.23 ? 466  ILE A CG1  1 
ATOM   7637 C CG2  . ILE B 1 466 ? 180.602 149.988 145.185 1.00 137.17 ? 466  ILE A CG2  1 
ATOM   7638 C CD1  . ILE B 1 466 ? 182.231 147.761 144.241 1.00 137.24 ? 466  ILE A CD1  1 
ATOM   7639 N N    . SER B 1 467 ? 177.320 149.275 145.980 1.00 140.89 ? 467  SER A N    1 
ATOM   7640 C CA   . SER B 1 467 ? 176.563 149.818 147.105 1.00 140.83 ? 467  SER A CA   1 
ATOM   7641 C C    . SER B 1 467 ? 176.000 148.722 148.006 1.00 139.09 ? 467  SER A C    1 
ATOM   7642 O O    . SER B 1 467 ? 175.978 148.880 149.233 1.00 137.94 ? 467  SER A O    1 
ATOM   7643 C CB   . SER B 1 467 ? 175.436 150.713 146.597 1.00 140.81 ? 467  SER A CB   1 
ATOM   7644 O OG   . SER B 1 467 ? 174.592 150.009 145.705 1.00 141.73 ? 467  SER A OG   1 
ATOM   7645 N N    . LEU B 1 468 ? 175.525 147.610 147.427 1.00 135.30 ? 468  LEU A N    1 
ATOM   7646 C CA   . LEU B 1 468 ? 175.131 146.484 148.273 1.00 134.62 ? 468  LEU A CA   1 
ATOM   7647 C C    . LEU B 1 468 ? 176.316 145.907 149.037 1.00 133.23 ? 468  LEU A C    1 
ATOM   7648 O O    . LEU B 1 468 ? 176.151 145.428 150.166 1.00 130.85 ? 468  LEU A O    1 
ATOM   7649 C CB   . LEU B 1 468 ? 174.471 145.398 147.423 1.00 135.52 ? 468  LEU A CB   1 
ATOM   7650 C CG   . LEU B 1 468 ? 172.970 145.203 147.633 1.00 134.46 ? 468  LEU A CG   1 
ATOM   7651 C CD1  . LEU B 1 468 ? 172.441 144.074 146.765 1.00 132.59 ? 468  LEU A CD1  1 
ATOM   7652 C CD2  . LEU B 1 468 ? 172.686 144.931 149.096 1.00 133.16 ? 468  LEU A CD2  1 
ATOM   7653 N N    . PHE B 1 469 ? 177.506 145.921 148.432 1.00 147.92 ? 469  PHE A N    1 
ATOM   7654 C CA   . PHE B 1 469 ? 178.707 145.464 149.127 1.00 149.04 ? 469  PHE A CA   1 
ATOM   7655 C C    . PHE B 1 469 ? 179.000 146.334 150.338 1.00 148.73 ? 469  PHE A C    1 
ATOM   7656 O O    . PHE B 1 469 ? 179.355 145.837 151.413 1.00 147.46 ? 469  PHE A O    1 
ATOM   7657 C CB   . PHE B 1 469 ? 179.915 145.451 148.195 1.00 150.23 ? 469  PHE A CB   1 
ATOM   7658 C CG   . PHE B 1 469 ? 181.223 145.302 148.921 1.00 149.90 ? 469  PHE A CG   1 
ATOM   7659 C CD1  . PHE B 1 469 ? 181.537 144.125 149.576 1.00 149.65 ? 469  PHE A CD1  1 
ATOM   7660 C CD2  . PHE B 1 469 ? 182.142 146.342 148.943 1.00 149.76 ? 469  PHE A CD2  1 
ATOM   7661 C CE1  . PHE B 1 469 ? 182.736 143.993 150.256 1.00 150.36 ? 469  PHE A CE1  1 
ATOM   7662 C CE2  . PHE B 1 469 ? 183.347 146.210 149.612 1.00 149.81 ? 469  PHE A CE2  1 
ATOM   7663 C CZ   . PHE B 1 469 ? 183.643 145.033 150.267 1.00 149.67 ? 469  PHE A CZ   1 
ATOM   7664 N N    . LEU B 1 470 ? 178.846 147.645 150.164 1.00 148.97 ? 470  LEU A N    1 
ATOM   7665 C CA   . LEU B 1 470 ? 179.175 148.611 151.205 1.00 147.61 ? 470  LEU A CA   1 
ATOM   7666 C C    . LEU B 1 470 ? 178.122 148.654 152.303 1.00 149.09 ? 470  LEU A C    1 
ATOM   7667 O O    . LEU B 1 470 ? 178.458 148.949 153.450 1.00 148.36 ? 470  LEU A O    1 
ATOM   7668 C CB   . LEU B 1 470 ? 179.387 149.997 150.568 1.00 147.74 ? 470  LEU A CB   1 
ATOM   7669 C CG   . LEU B 1 470 ? 179.532 151.368 151.268 1.00 147.95 ? 470  LEU A CG   1 
ATOM   7670 C CD1  . LEU B 1 470 ? 179.984 152.383 150.235 1.00 148.20 ? 470  LEU A CD1  1 
ATOM   7671 C CD2  . LEU B 1 470 ? 178.270 151.929 151.928 1.00 147.54 ? 470  LEU A CD2  1 
ATOM   7672 N N    . LEU B 1 471 ? 176.847 148.446 151.971 1.00 151.54 ? 471  LEU A N    1 
ATOM   7673 C CA   . LEU B 1 471 ? 175.772 148.664 152.939 1.00 149.68 ? 471  LEU A CA   1 
ATOM   7674 C C    . LEU B 1 471 ? 175.817 147.685 154.114 1.00 147.67 ? 471  LEU A C    1 
ATOM   7675 O O    . LEU B 1 471 ? 175.739 148.101 155.276 1.00 146.20 ? 471  LEU A O    1 
ATOM   7676 C CB   . LEU B 1 471 ? 174.417 148.585 152.235 1.00 149.32 ? 471  LEU A CB   1 
ATOM   7677 C CG   . LEU B 1 471 ? 173.190 148.657 153.146 1.00 148.71 ? 471  LEU A CG   1 
ATOM   7678 C CD1  . LEU B 1 471 ? 173.127 150.004 153.853 1.00 148.39 ? 471  LEU A CD1  1 
ATOM   7679 C CD2  . LEU B 1 471 ? 171.917 148.408 152.354 1.00 148.95 ? 471  LEU A CD2  1 
ATOM   7680 N N    . LYS B 1 472 ? 175.932 146.381 153.838 1.00 150.23 ? 472  LYS A N    1 
ATOM   7681 C CA   . LYS B 1 472 ? 175.928 145.374 154.902 1.00 151.47 ? 472  LYS A CA   1 
ATOM   7682 C C    . LYS B 1 472 ? 177.138 145.432 155.833 1.00 150.81 ? 472  LYS A C    1 
ATOM   7683 O O    . LYS B 1 472 ? 177.052 144.934 156.961 1.00 151.22 ? 472  LYS A O    1 
ATOM   7684 C CB   . LYS B 1 472 ? 175.831 143.977 154.289 1.00 152.13 ? 472  LYS A CB   1 
ATOM   7685 N N    . LYS B 1 473 ? 178.249 146.016 155.404 1.00 153.73 ? 473  LYS A N    1 
ATOM   7686 C CA   . LYS B 1 473 ? 179.440 146.148 156.238 1.00 153.86 ? 473  LYS A CA   1 
ATOM   7687 C C    . LYS B 1 473 ? 179.787 147.633 156.219 1.00 155.05 ? 473  LYS A C    1 
ATOM   7688 O O    . LYS B 1 473 ? 178.909 148.473 155.994 1.00 155.15 ? 473  LYS A O    1 
ATOM   7689 C CB   . LYS B 1 473 ? 180.575 145.247 155.736 1.00 153.89 ? 473  LYS A CB   1 
ATOM   7690 N N    . ARG B 1 474 ? 181.011 147.977 156.641 1.00 156.53 ? 474  ARG A N    1 
ATOM   7691 C CA   . ARG B 1 474 ? 181.485 149.356 156.521 1.00 155.85 ? 474  ARG A CA   1 
ATOM   7692 C C    . ARG B 1 474 ? 180.698 150.352 157.365 1.00 156.25 ? 474  ARG A C    1 
ATOM   7693 O O    . ARG B 1 474 ? 179.864 151.086 156.826 1.00 154.85 ? 474  ARG A O    1 
ATOM   7694 C CB   . ARG B 1 474 ? 181.497 149.802 155.052 1.00 155.04 ? 474  ARG A CB   1 
ATOM   7695 N N    . GLU B 1 475 ? 180.940 150.406 158.669 1.00 164.40 ? 475  GLU A N    1 
ATOM   7696 C CA   . GLU B 1 475 ? 180.292 151.454 159.439 1.00 163.27 ? 475  GLU A CA   1 
ATOM   7697 C C    . GLU B 1 475 ? 181.076 152.749 159.273 1.00 164.43 ? 475  GLU A C    1 
ATOM   7698 O O    . GLU B 1 475 ? 182.273 152.738 158.967 1.00 164.14 ? 475  GLU A O    1 
ATOM   7699 C CB   . GLU B 1 475 ? 180.201 151.070 160.916 1.00 162.42 ? 475  GLU A CB   1 
ATOM   7700 N N    . ARG B 1 476 ? 180.357 153.870 159.427 1.00 171.16 ? 476  ARG A N    1 
ATOM   7701 C CA   . ARG B 1 476 ? 180.832 155.244 159.251 1.00 170.97 ? 476  ARG A CA   1 
ATOM   7702 C C    . ARG B 1 476 ? 181.092 155.473 157.762 1.00 171.19 ? 476  ARG A C    1 
ATOM   7703 O O    . ARG B 1 476 ? 180.886 154.556 156.958 1.00 171.78 ? 476  ARG A O    1 
ATOM   7704 C CB   . ARG B 1 476 ? 182.077 155.547 160.095 1.00 170.27 ? 476  ARG A CB   1 
ATOM   7705 N N    . VAL B 1 477 ? 181.541 156.679 157.389 1.00 168.36 ? 477  VAL A N    1 
ATOM   7706 C CA   . VAL B 1 477 ? 181.914 157.016 156.013 1.00 168.32 ? 477  VAL A CA   1 
ATOM   7707 C C    . VAL B 1 477 ? 180.754 156.718 155.067 1.00 168.71 ? 477  VAL A C    1 
ATOM   7708 O O    . VAL B 1 477 ? 180.810 155.766 154.281 1.00 168.50 ? 477  VAL A O    1 
ATOM   7709 C CB   . VAL B 1 477 ? 183.191 156.273 155.575 1.00 168.22 ? 477  VAL A CB   1 
ATOM   7710 N N    . GLN B 1 478 ? 179.699 157.527 155.138 1.00 163.47 ? 478  GLN A N    1 
ATOM   7711 C CA   . GLN B 1 478 ? 178.527 157.315 154.300 1.00 163.50 ? 478  GLN A CA   1 
ATOM   7712 C C    . GLN B 1 478 ? 178.803 157.652 152.837 1.00 163.58 ? 478  GLN A C    1 
ATOM   7713 O O    . GLN B 1 478 ? 179.644 158.494 152.510 1.00 163.04 ? 478  GLN A O    1 
ATOM   7714 C CB   . GLN B 1 478 ? 177.354 158.152 154.808 1.00 162.57 ? 478  GLN A CB   1 
ATOM   7715 N N    . ILE B 1 479 ? 178.076 156.965 151.960 1.00 154.79 ? 479  ILE A N    1 
ATOM   7716 C CA   . ILE B 1 479 ? 178.241 157.025 150.509 1.00 154.00 ? 479  ILE A CA   1 
ATOM   7717 C C    . ILE B 1 479 ? 177.940 158.413 149.951 1.00 153.81 ? 479  ILE A C    1 
ATOM   7718 O O    . ILE B 1 479 ? 176.839 158.944 150.159 1.00 153.10 ? 479  ILE A O    1 
ATOM   7719 C CB   . ILE B 1 479 ? 177.362 155.972 149.817 1.00 153.12 ? 479  ILE A CB   1 
ATOM   7720 N N    . PRO B 1 480 ? 178.884 159.029 149.237 1.00 146.83 ? 480  PRO A N    1 
ATOM   7721 C CA   . PRO B 1 480 ? 178.641 160.322 148.576 1.00 145.53 ? 480  PRO A CA   1 
ATOM   7722 C C    . PRO B 1 480 ? 177.802 160.091 147.327 1.00 144.51 ? 480  PRO A C    1 
ATOM   7723 O O    . PRO B 1 480 ? 178.334 160.061 146.217 1.00 144.05 ? 480  PRO A O    1 
ATOM   7724 C CB   . PRO B 1 480 ? 180.052 160.817 148.228 1.00 145.41 ? 480  PRO A CB   1 
ATOM   7725 C CG   . PRO B 1 480 ? 180.996 159.924 148.991 1.00 145.08 ? 480  PRO A CG   1 
ATOM   7726 C CD   . PRO B 1 480 ? 180.290 158.616 149.119 1.00 145.86 ? 480  PRO A CD   1 
ATOM   7727 N N    . VAL B 1 481 ? 176.476 160.050 147.507 1.00 144.91 ? 481  VAL A N    1 
ATOM   7728 C CA   . VAL B 1 481 ? 175.527 159.757 146.428 1.00 146.05 ? 481  VAL A CA   1 
ATOM   7729 C C    . VAL B 1 481 ? 175.645 160.740 145.268 1.00 147.92 ? 481  VAL A C    1 
ATOM   7730 O O    . VAL B 1 481 ? 175.397 160.370 144.112 1.00 147.94 ? 481  VAL A O    1 
ATOM   7731 C CB   . VAL B 1 481 ? 174.089 159.703 146.990 1.00 144.78 ? 481  VAL A CB   1 
ATOM   7732 C CG1  . VAL B 1 481 ? 173.975 158.601 148.030 1.00 145.32 ? 481  VAL A CG1  1 
ATOM   7733 C CG2  . VAL B 1 481 ? 173.684 161.038 147.604 1.00 146.30 ? 481  VAL A CG2  1 
ATOM   7734 N N    . GLY B 1 482 ? 175.994 161.996 145.545 1.00 146.08 ? 482  GLY A N    1 
ATOM   7735 C CA   . GLY B 1 482 ? 176.219 162.944 144.465 1.00 143.48 ? 482  GLY A CA   1 
ATOM   7736 C C    . GLY B 1 482 ? 177.336 162.501 143.536 1.00 145.10 ? 482  GLY A C    1 
ATOM   7737 O O    . GLY B 1 482 ? 177.230 162.635 142.314 1.00 144.49 ? 482  GLY A O    1 
ATOM   7738 N N    . ILE B 1 483 ? 178.414 161.951 144.104 1.00 141.82 ? 483  ILE A N    1 
ATOM   7739 C CA   . ILE B 1 483 ? 179.518 161.423 143.300 1.00 140.96 ? 483  ILE A CA   1 
ATOM   7740 C C    . ILE B 1 483 ? 179.052 160.257 142.427 1.00 140.86 ? 483  ILE A C    1 
ATOM   7741 O O    . ILE B 1 483 ? 179.421 160.165 141.251 1.00 140.35 ? 483  ILE A O    1 
ATOM   7742 C CB   . ILE B 1 483 ? 180.695 161.019 144.207 1.00 139.64 ? 483  ILE A CB   1 
ATOM   7743 C CG1  . ILE B 1 483 ? 181.200 162.233 144.989 1.00 138.57 ? 483  ILE A CG1  1 
ATOM   7744 C CG2  . ILE B 1 483 ? 181.823 160.405 143.392 1.00 140.36 ? 483  ILE A CG2  1 
ATOM   7745 C CD1  . ILE B 1 483 ? 181.848 163.294 144.126 1.00 138.23 ? 483  ILE A CD1  1 
ATOM   7746 N N    . ILE B 1 484 ? 178.265 159.333 142.991 1.00 134.29 ? 484  ILE A N    1 
ATOM   7747 C CA   . ILE B 1 484 ? 177.760 158.207 142.197 1.00 133.62 ? 484  ILE A CA   1 
ATOM   7748 C C    . ILE B 1 484 ? 176.857 158.686 141.062 1.00 132.47 ? 484  ILE A C    1 
ATOM   7749 O O    . ILE B 1 484 ? 176.967 158.202 139.931 1.00 132.76 ? 484  ILE A O    1 
ATOM   7750 C CB   . ILE B 1 484 ? 177.059 157.134 143.068 1.00 134.50 ? 484  ILE A CB   1 
ATOM   7751 C CG1  . ILE B 1 484 ? 177.991 156.448 144.084 1.00 134.22 ? 484  ILE A CG1  1 
ATOM   7752 C CG2  . ILE B 1 484 ? 176.376 156.082 142.213 1.00 134.59 ? 484  ILE A CG2  1 
ATOM   7753 C CD1  . ILE B 1 484 ? 178.290 157.146 145.343 1.00 133.62 ? 484  ILE A CD1  1 
ATOM   7754 N N    . ILE B 1 485 ? 175.963 159.639 141.333 1.00 132.61 ? 485  ILE A N    1 
ATOM   7755 C CA   . ILE B 1 485 ? 175.106 160.192 140.278 1.00 134.44 ? 485  ILE A CA   1 
ATOM   7756 C C    . ILE B 1 485 ? 175.925 160.882 139.184 1.00 135.73 ? 485  ILE A C    1 
ATOM   7757 O O    . ILE B 1 485 ? 175.695 160.663 137.980 1.00 136.56 ? 485  ILE A O    1 
ATOM   7758 C CB   . ILE B 1 485 ? 174.079 161.164 140.892 1.00 133.99 ? 485  ILE A CB   1 
ATOM   7759 C CG1  . ILE B 1 485 ? 173.105 160.433 141.819 1.00 134.20 ? 485  ILE A CG1  1 
ATOM   7760 C CG2  . ILE B 1 485 ? 173.310 161.896 139.802 1.00 133.44 ? 485  ILE A CG2  1 
ATOM   7761 C CD1  . ILE B 1 485 ? 172.245 159.415 141.123 1.00 133.45 ? 485  ILE A CD1  1 
ATOM   7762 N N    . ILE B 1 486 ? 176.936 161.664 139.580 1.00 137.39 ? 486  ILE A N    1 
ATOM   7763 C CA   . ILE B 1 486 ? 177.811 162.306 138.601 1.00 137.90 ? 486  ILE A CA   1 
ATOM   7764 C C    . ILE B 1 486 ? 178.575 161.280 137.771 1.00 138.52 ? 486  ILE A C    1 
ATOM   7765 O O    . ILE B 1 486 ? 178.674 161.419 136.550 1.00 137.73 ? 486  ILE A O    1 
ATOM   7766 C CB   . ILE B 1 486 ? 178.765 163.287 139.312 1.00 136.00 ? 486  ILE A CB   1 
ATOM   7767 C CG1  . ILE B 1 486 ? 177.996 164.514 139.807 1.00 136.60 ? 486  ILE A CG1  1 
ATOM   7768 C CG2  . ILE B 1 486 ? 179.901 163.718 138.395 1.00 136.53 ? 486  ILE A CG2  1 
ATOM   7769 C CD1  . ILE B 1 486 ? 178.745 165.326 140.839 1.00 137.04 ? 486  ILE A CD1  1 
ATOM   7770 N N    . SER B 1 487 ? 179.124 160.242 138.401 1.00 136.41 ? 487  SER A N    1 
ATOM   7771 C CA   . SER B 1 487 ? 179.846 159.233 137.627 1.00 135.45 ? 487  SER A CA   1 
ATOM   7772 C C    . SER B 1 487 ? 178.910 158.479 136.687 1.00 135.61 ? 487  SER A C    1 
ATOM   7773 O O    . SER B 1 487 ? 179.182 158.382 135.478 1.00 136.23 ? 487  SER A O    1 
ATOM   7774 C CB   . SER B 1 487 ? 180.557 158.262 138.569 1.00 135.33 ? 487  SER A CB   1 
ATOM   7775 O OG   . SER B 1 487 ? 180.939 157.079 137.889 1.00 134.23 ? 487  SER A OG   1 
ATOM   7776 N N    . GLY B 1 488 ? 177.717 158.139 137.194 1.00 130.99 ? 488  GLY A N    1 
ATOM   7777 C CA   . GLY B 1 488 ? 176.735 157.370 136.449 1.00 129.84 ? 488  GLY A CA   1 
ATOM   7778 C C    . GLY B 1 488 ? 176.211 158.084 135.229 1.00 129.81 ? 488  GLY A C    1 
ATOM   7779 O O    . GLY B 1 488 ? 175.773 157.441 134.272 1.00 128.93 ? 488  GLY A O    1 
ATOM   7780 N N    . TRP B 1 489 ? 176.226 159.409 135.240 1.00 134.96 ? 489  TRP A N    1 
ATOM   7781 C CA   . TRP B 1 489 ? 175.714 160.115 134.076 1.00 135.40 ? 489  TRP A CA   1 
ATOM   7782 C C    . TRP B 1 489 ? 176.824 160.726 133.236 1.00 136.39 ? 489  TRP A C    1 
ATOM   7783 O O    . TRP B 1 489 ? 176.729 160.710 132.007 1.00 134.72 ? 489  TRP A O    1 
ATOM   7784 C CB   . TRP B 1 489 ? 174.710 161.194 134.495 1.00 136.46 ? 489  TRP A CB   1 
ATOM   7785 C CG   . TRP B 1 489 ? 173.418 160.609 134.985 1.00 136.04 ? 489  TRP A CG   1 
ATOM   7786 C CD1  . TRP B 1 489 ? 173.061 160.374 136.281 1.00 136.64 ? 489  TRP A CD1  1 
ATOM   7787 C CD2  . TRP B 1 489 ? 172.318 160.164 134.180 1.00 134.23 ? 489  TRP A CD2  1 
ATOM   7788 N NE1  . TRP B 1 489 ? 171.805 159.820 136.334 1.00 135.66 ? 489  TRP A NE1  1 
ATOM   7789 C CE2  . TRP B 1 489 ? 171.327 159.680 135.057 1.00 134.38 ? 489  TRP A CE2  1 
ATOM   7790 C CE3  . TRP B 1 489 ? 172.074 160.133 132.804 1.00 135.03 ? 489  TRP A CE3  1 
ATOM   7791 C CZ2  . TRP B 1 489 ? 170.112 159.172 134.603 1.00 134.54 ? 489  TRP A CZ2  1 
ATOM   7792 C CZ3  . TRP B 1 489 ? 170.866 159.627 132.355 1.00 135.30 ? 489  TRP A CZ3  1 
ATOM   7793 C CH2  . TRP B 1 489 ? 169.901 159.154 133.252 1.00 133.99 ? 489  TRP A CH2  1 
ATOM   7794 N N    . GLY B 1 490 ? 177.868 161.281 133.855 1.00 146.16 ? 490  GLY A N    1 
ATOM   7795 C CA   . GLY B 1 490 ? 178.942 161.882 133.086 1.00 146.96 ? 490  GLY A CA   1 
ATOM   7796 C C    . GLY B 1 490 ? 179.745 160.880 132.271 1.00 147.61 ? 490  GLY A C    1 
ATOM   7797 O O    . GLY B 1 490 ? 180.115 161.169 131.129 1.00 147.38 ? 490  GLY A O    1 
ATOM   7798 N N    . ILE B 1 491 ? 180.052 159.698 132.845 1.00 144.10 ? 491  ILE A N    1 
ATOM   7799 C CA   . ILE B 1 491 ? 180.867 158.715 132.115 1.00 142.92 ? 491  ILE A CA   1 
ATOM   7800 C C    . ILE B 1 491 ? 180.201 158.241 130.822 1.00 143.72 ? 491  ILE A C    1 
ATOM   7801 O O    . ILE B 1 491 ? 180.866 158.260 129.769 1.00 144.45 ? 491  ILE A O    1 
ATOM   7802 C CB   . ILE B 1 491 ? 181.284 157.566 133.051 1.00 142.75 ? 491  ILE A CB   1 
ATOM   7803 C CG1  . ILE B 1 491 ? 182.124 158.097 134.216 1.00 144.70 ? 491  ILE A CG1  1 
ATOM   7804 C CG2  . ILE B 1 491 ? 182.051 156.500 132.285 1.00 142.88 ? 491  ILE A CG2  1 
ATOM   7805 C CD1  . ILE B 1 491 ? 183.270 158.993 133.793 1.00 144.28 ? 491  ILE A CD1  1 
ATOM   7806 N N    . PRO B 1 492 ? 178.928 157.791 130.817 1.00 144.46 ? 492  PRO A N    1 
ATOM   7807 C CA   . PRO B 1 492 ? 178.310 157.404 129.536 1.00 144.55 ? 492  PRO A CA   1 
ATOM   7808 C C    . PRO B 1 492 ? 178.265 158.526 128.517 1.00 145.34 ? 492  PRO A C    1 
ATOM   7809 O O    . PRO B 1 492 ? 178.396 158.258 127.320 1.00 145.76 ? 492  PRO A O    1 
ATOM   7810 C CB   . PRO B 1 492 ? 176.899 156.967 129.944 1.00 142.17 ? 492  PRO A CB   1 
ATOM   7811 C CG   . PRO B 1 492 ? 177.027 156.542 131.330 1.00 142.45 ? 492  PRO A CG   1 
ATOM   7812 C CD   . PRO B 1 492 ? 178.026 157.463 131.941 1.00 144.04 ? 492  PRO A CD   1 
ATOM   7813 N N    . ALA B 1 493 ? 178.050 159.770 128.952 1.00 148.40 ? 493  ALA A N    1 
ATOM   7814 C CA   . ALA B 1 493 ? 178.032 160.883 128.008 1.00 148.22 ? 493  ALA A CA   1 
ATOM   7815 C C    . ALA B 1 493 ? 179.390 161.063 127.338 1.00 148.06 ? 493  ALA A C    1 
ATOM   7816 O O    . ALA B 1 493 ? 179.461 161.312 126.128 1.00 148.86 ? 493  ALA A O    1 
ATOM   7817 C CB   . ALA B 1 493 ? 177.608 162.167 128.718 1.00 147.46 ? 493  ALA A CB   1 
ATOM   7818 N N    . LEU B 1 494 ? 180.479 160.964 128.108 1.00 146.15 ? 494  LEU A N    1 
ATOM   7819 C CA   . LEU B 1 494 ? 181.810 161.080 127.517 1.00 147.09 ? 494  LEU A CA   1 
ATOM   7820 C C    . LEU B 1 494 ? 182.080 159.942 126.538 1.00 147.13 ? 494  LEU A C    1 
ATOM   7821 O O    . LEU B 1 494 ? 182.637 160.163 125.451 1.00 147.93 ? 494  LEU A O    1 
ATOM   7822 C CB   . LEU B 1 494 ? 182.875 161.110 128.615 1.00 147.16 ? 494  LEU A CB   1 
ATOM   7823 C CG   . LEU B 1 494 ? 183.365 162.478 129.102 1.00 147.64 ? 494  LEU A CG   1 
ATOM   7824 C CD1  . LEU B 1 494 ? 184.040 163.240 127.970 1.00 147.80 ? 494  LEU A CD1  1 
ATOM   7825 C CD2  . LEU B 1 494 ? 182.239 163.302 129.711 1.00 146.88 ? 494  LEU A CD2  1 
ATOM   7826 N N    . LEU B 1 495 ? 181.680 158.717 126.902 1.00 148.14 ? 495  LEU A N    1 
ATOM   7827 C CA   . LEU B 1 495 ? 181.857 157.582 125.996 1.00 148.57 ? 495  LEU A CA   1 
ATOM   7828 C C    . LEU B 1 495 ? 181.046 157.765 124.716 1.00 149.78 ? 495  LEU A C    1 
ATOM   7829 O O    . LEU B 1 495 ? 181.525 157.470 123.610 1.00 149.67 ? 495  LEU A O    1 
ATOM   7830 C CB   . LEU B 1 495 ? 181.468 156.282 126.700 1.00 148.32 ? 495  LEU A CB   1 
ATOM   7831 N N    . VAL B 1 496 ? 179.818 158.272 124.854 1.00 152.63 ? 496  VAL A N    1 
ATOM   7832 C CA   . VAL B 1 496 ? 178.963 158.537 123.702 1.00 151.66 ? 496  VAL A CA   1 
ATOM   7833 C C    . VAL B 1 496 ? 179.595 159.585 122.803 1.00 152.04 ? 496  VAL A C    1 
ATOM   7834 O O    . VAL B 1 496 ? 179.557 159.462 121.576 1.00 150.70 ? 496  VAL A O    1 
ATOM   7835 C CB   . VAL B 1 496 ? 177.557 158.961 124.165 1.00 150.89 ? 496  VAL A CB   1 
ATOM   7836 N N    . GLY B 1 497 ? 180.131 160.660 123.388 1.00 153.70 ? 497  GLY A N    1 
ATOM   7837 C CA   . GLY B 1 497 ? 180.766 161.684 122.572 1.00 152.45 ? 497  GLY A CA   1 
ATOM   7838 C C    . GLY B 1 497 ? 181.980 161.153 121.832 1.00 152.61 ? 497  GLY A C    1 
ATOM   7839 O O    . GLY B 1 497 ? 182.230 161.524 120.676 1.00 153.27 ? 497  GLY A O    1 
ATOM   7840 N N    . VAL B 1 498 ? 182.753 160.277 122.489 1.00 158.07 ? 498  VAL A N    1 
ATOM   7841 C CA   . VAL B 1 498 ? 183.910 159.683 121.824 1.00 158.67 ? 498  VAL A CA   1 
ATOM   7842 C C    . VAL B 1 498 ? 183.455 158.853 120.632 1.00 159.85 ? 498  VAL A C    1 
ATOM   7843 O O    . VAL B 1 498 ? 184.057 158.904 119.552 1.00 158.87 ? 498  VAL A O    1 
ATOM   7844 C CB   . VAL B 1 498 ? 184.732 158.845 122.821 1.00 158.45 ? 498  VAL A CB   1 
ATOM   7845 N N    . LEU B 1 499 ? 182.393 158.057 120.816 1.00 165.41 ? 499  LEU A N    1 
ATOM   7846 C CA   . LEU B 1 499 ? 181.861 157.260 119.712 1.00 164.96 ? 499  LEU A CA   1 
ATOM   7847 C C    . LEU B 1 499 ? 181.290 158.151 118.612 1.00 164.64 ? 499  LEU A C    1 
ATOM   7848 O O    . LEU B 1 499 ? 181.374 157.818 117.425 1.00 164.14 ? 499  LEU A O    1 
ATOM   7849 C CB   . LEU B 1 499 ? 180.796 156.292 120.226 1.00 163.58 ? 499  LEU A CB   1 
ATOM   7850 N N    . LEU B 1 500 ? 180.699 159.279 119.012 1.00 163.06 ? 500  LEU A N    1 
ATOM   7851 C CA   . LEU B 1 500 ? 180.104 160.249 118.099 1.00 162.96 ? 500  LEU A CA   1 
ATOM   7852 C C    . LEU B 1 500 ? 181.139 160.867 117.172 1.00 162.24 ? 500  LEU A C    1 
ATOM   7853 O O    . LEU B 1 500 ? 180.880 161.055 115.978 1.00 160.78 ? 500  LEU A O    1 
ATOM   7854 C CB   . LEU B 1 500 ? 179.384 161.339 118.894 1.00 162.65 ? 500  LEU A CB   1 
ATOM   7855 N N    . ILE B 1 501 ? 182.317 161.191 117.703 1.00 163.11 ? 501  ILE A N    1 
ATOM   7856 C CA   . ILE B 1 501 ? 183.309 161.880 116.882 1.00 162.19 ? 501  ILE A CA   1 
ATOM   7857 C C    . ILE B 1 501 ? 183.978 160.917 115.906 1.00 161.87 ? 501  ILE A C    1 
ATOM   7858 O O    . ILE B 1 501 ? 184.211 161.265 114.743 1.00 162.68 ? 501  ILE A O    1 
ATOM   7859 C CB   . ILE B 1 501 ? 184.344 162.585 117.777 1.00 162.80 ? 501  ILE A CB   1 
ATOM   7860 N N    . THR B 1 502 ? 184.295 159.704 116.343 1.00 164.93 ? 502  THR A N    1 
ATOM   7861 C CA   . THR B 1 502 ? 185.035 158.775 115.501 1.00 166.41 ? 502  THR A CA   1 
ATOM   7862 C C    . THR B 1 502 ? 184.085 157.815 114.791 1.00 167.34 ? 502  THR A C    1 
ATOM   7863 O O    . THR B 1 502 ? 183.316 157.088 115.425 1.00 168.27 ? 502  THR A O    1 
ATOM   7864 C CB   . THR B 1 502 ? 186.051 157.980 116.324 1.00 166.16 ? 502  THR A CB   1 
ATOM   7865 N N    . GLY B 1 503 ? 184.153 157.813 113.458 1.00 162.56 ? 503  GLY A N    1 
ATOM   7866 C CA   . GLY B 1 503 ? 183.261 157.008 112.641 1.00 162.06 ? 503  GLY A CA   1 
ATOM   7867 C C    . GLY B 1 503 ? 182.523 157.759 111.549 1.00 162.71 ? 503  GLY A C    1 
ATOM   7868 O O    . GLY B 1 503 ? 182.089 158.898 111.746 1.00 162.49 ? 503  GLY A O    1 
ATOM   7869 N N    . LYS B 1 504 ? 182.377 157.122 110.388 1.00 166.16 ? 504  LYS A N    1 
ATOM   7870 C CA   . LYS B 1 504 ? 181.609 157.657 109.268 1.00 166.63 ? 504  LYS A CA   1 
ATOM   7871 C C    . LYS B 1 504 ? 180.207 157.058 109.246 1.00 165.94 ? 504  LYS A C    1 
ATOM   7872 O O    . LYS B 1 504 ? 180.053 155.832 109.248 1.00 164.59 ? 504  LYS A O    1 
ATOM   7873 C CB   . LYS B 1 504 ? 182.319 157.376 107.943 1.00 164.84 ? 504  LYS A CB   1 
ATOM   7874 N N    . HIS B 1 505 ? 179.194 157.926 109.243 1.00 159.46 ? 505  HIS A N    1 
ATOM   7875 C CA   . HIS B 1 505 ? 177.806 157.477 109.282 1.00 158.44 ? 505  HIS A CA   1 
ATOM   7876 C C    . HIS B 1 505 ? 177.455 156.676 108.032 1.00 159.01 ? 505  HIS A C    1 
ATOM   7877 O O    . HIS B 1 505 ? 177.813 157.051 106.912 1.00 159.19 ? 505  HIS A O    1 
ATOM   7878 C CB   . HIS B 1 505 ? 176.868 158.676 109.418 1.00 157.84 ? 505  HIS A CB   1 
ATOM   7879 N N    . ASN B 1 506 ? 176.746 155.563 108.227 1.00 150.61 ? 506  ASN A N    1 
ATOM   7880 C CA   . ASN B 1 506 ? 176.219 154.760 107.124 1.00 150.48 ? 506  ASN A CA   1 
ATOM   7881 C C    . ASN B 1 506 ? 174.718 155.011 107.010 1.00 149.84 ? 506  ASN A C    1 
ATOM   7882 O O    . ASN B 1 506 ? 173.929 154.511 107.817 1.00 150.40 ? 506  ASN A O    1 
ATOM   7883 C CB   . ASN B 1 506 ? 176.522 153.281 107.339 1.00 149.29 ? 506  ASN A CB   1 
ATOM   7884 N N    . GLY B 1 507 ? 174.328 155.792 106.002 1.00 141.03 ? 507  GLY A N    1 
ATOM   7885 C CA   . GLY B 1 507 ? 172.938 156.180 105.832 1.00 141.13 ? 507  GLY A CA   1 
ATOM   7886 C C    . GLY B 1 507 ? 172.011 155.062 105.396 1.00 141.95 ? 507  GLY A C    1 
ATOM   7887 O O    . GLY B 1 507 ? 170.805 155.141 105.654 1.00 140.87 ? 507  GLY A O    1 
ATOM   7888 N N    . ASP B 1 508 ? 172.539 154.026 104.746 1.00 141.73 ? 508  ASP A N    1 
ATOM   7889 C CA   . ASP B 1 508 ? 171.715 152.924 104.262 1.00 140.35 ? 508  ASP A CA   1 
ATOM   7890 C C    . ASP B 1 508 ? 171.622 151.748 105.226 1.00 141.56 ? 508  ASP A C    1 
ATOM   7891 O O    . ASP B 1 508 ? 170.986 150.744 104.887 1.00 142.44 ? 508  ASP A O    1 
ATOM   7892 C CB   . ASP B 1 508 ? 172.245 152.431 102.911 1.00 139.84 ? 508  ASP A CB   1 
ATOM   7893 N N    . SER B 1 509 ? 172.225 151.834 106.409 1.00 141.48 ? 509  SER A N    1 
ATOM   7894 C CA   . SER B 1 509 ? 172.170 150.747 107.381 1.00 140.26 ? 509  SER A CA   1 
ATOM   7895 C C    . SER B 1 509 ? 170.937 150.972 108.247 1.00 140.36 ? 509  SER A C    1 
ATOM   7896 O O    . SER B 1 509 ? 170.911 151.891 109.072 1.00 141.31 ? 509  SER A O    1 
ATOM   7897 C CB   . SER B 1 509 ? 173.442 150.702 108.223 1.00 140.03 ? 509  SER A CB   1 
ATOM   7898 N N    . ILE B 1 510 ? 169.915 150.140 108.067 1.00 135.72 ? 510  ILE A N    1 
ATOM   7899 C CA   . ILE B 1 510 ? 168.684 150.267 108.862 1.00 136.95 ? 510  ILE A CA   1 
ATOM   7900 C C    . ILE B 1 510 ? 168.866 149.410 110.109 1.00 136.98 ? 510  ILE A C    1 
ATOM   7901 O O    . ILE B 1 510 ? 168.301 148.323 110.255 1.00 135.67 ? 510  ILE A O    1 
ATOM   7902 C CB   . ILE B 1 510 ? 167.438 149.885 108.059 1.00 135.80 ? 510  ILE A CB   1 
ATOM   7903 N N    . ASP B 1 511 ? 169.643 149.943 111.058 1.00 139.65 ? 511  ASP A N    1 
ATOM   7904 C CA   . ASP B 1 511 ? 169.916 149.314 112.349 1.00 138.30 ? 511  ASP A CA   1 
ATOM   7905 C C    . ASP B 1 511 ? 170.736 150.261 113.213 1.00 138.24 ? 511  ASP A C    1 
ATOM   7906 O O    . ASP B 1 511 ? 171.602 150.979 112.702 1.00 138.01 ? 511  ASP A O    1 
ATOM   7907 C CB   . ASP B 1 511 ? 170.674 147.991 112.183 1.00 137.67 ? 511  ASP A CB   1 
ATOM   7908 N N    . SER B 1 512 ? 170.471 150.278 114.522 1.00 141.98 ? 512  SER A N    1 
ATOM   7909 C CA   . SER B 1 512 ? 171.239 151.144 115.409 1.00 141.89 ? 512  SER A CA   1 
ATOM   7910 C C    . SER B 1 512 ? 172.677 150.668 115.585 1.00 143.21 ? 512  SER A C    1 
ATOM   7911 O O    . SER B 1 512 ? 173.567 151.478 115.866 1.00 143.25 ? 512  SER A O    1 
ATOM   7912 C CB   . SER B 1 512 ? 170.548 151.243 116.769 1.00 139.75 ? 512  SER A CB   1 
ATOM   7913 N N    . ALA B 1 513 ? 172.919 149.364 115.426 1.00 150.13 ? 513  ALA A N    1 
ATOM   7914 C CA   . ALA B 1 513 ? 174.240 148.798 115.678 1.00 149.82 ? 513  ALA A CA   1 
ATOM   7915 C C    . ALA B 1 513 ? 175.310 149.159 114.656 1.00 150.11 ? 513  ALA A C    1 
ATOM   7916 O O    . ALA B 1 513 ? 176.491 148.934 114.943 1.00 150.83 ? 513  ALA A O    1 
ATOM   7917 C CB   . ALA B 1 513 ? 174.133 147.274 115.768 1.00 150.34 ? 513  ALA A CB   1 
ATOM   7918 N N    . PHE B 1 514 ? 174.967 149.700 113.486 1.00 149.35 ? 514  PHE A N    1 
ATOM   7919 C CA   . PHE B 1 514 ? 176.030 149.937 112.516 1.00 149.80 ? 514  PHE A CA   1 
ATOM   7920 C C    . PHE B 1 514 ? 176.048 151.361 111.973 1.00 150.49 ? 514  PHE A C    1 
ATOM   7921 O O    . PHE B 1 514 ? 176.373 151.563 110.799 1.00 151.48 ? 514  PHE A O    1 
ATOM   7922 C CB   . PHE B 1 514 ? 175.930 148.941 111.361 1.00 149.50 ? 514  PHE A CB   1 
ATOM   7923 N N    . PHE B 1 515 ? 175.676 152.360 112.779 1.00 151.14 ? 515  PHE A N    1 
ATOM   7924 C CA   . PHE B 1 515 ? 175.742 153.731 112.280 1.00 151.42 ? 515  PHE A CA   1 
ATOM   7925 C C    . PHE B 1 515 ? 177.185 154.142 112.005 1.00 151.80 ? 515  PHE A C    1 
ATOM   7926 O O    . PHE B 1 515 ? 177.492 154.727 110.961 1.00 151.26 ? 515  PHE A O    1 
ATOM   7927 C CB   . PHE B 1 515 ? 175.088 154.686 113.279 1.00 150.76 ? 515  PHE A CB   1 
ATOM   7928 N N    . TYR B 1 516 ? 178.085 153.819 112.934 1.00 155.16 ? 516  TYR A N    1 
ATOM   7929 C CA   . TYR B 1 516 ? 179.518 154.060 112.824 1.00 155.78 ? 516  TYR A CA   1 
ATOM   7930 C C    . TYR B 1 516 ? 180.322 152.772 112.681 1.00 155.34 ? 516  TYR A C    1 
ATOM   7931 O O    . TYR B 1 516 ? 181.551 152.807 112.812 1.00 155.77 ? 516  TYR A O    1 
ATOM   7932 C CB   . TYR B 1 516 ? 180.015 154.875 114.020 1.00 155.67 ? 516  TYR A CB   1 
ATOM   7933 N N    . GLY B 1 517 ? 179.670 151.644 112.406 1.00 146.66 ? 517  GLY A N    1 
ATOM   7934 C CA   . GLY B 1 517 ? 180.416 150.414 112.168 1.00 146.34 ? 517  GLY A CA   1 
ATOM   7935 C C    . GLY B 1 517 ? 181.141 149.862 113.394 1.00 145.66 ? 517  GLY A C    1 
ATOM   7936 O O    . GLY B 1 517 ? 180.552 149.639 114.455 1.00 146.01 ? 517  GLY A O    1 
ATOM   7937 N N    . LYS B 1 518 ? 182.414 149.527 113.196 1.00 138.61 ? 518  LYS A N    1 
ATOM   7938 C CA   . LYS B 1 518 ? 183.208 148.779 114.174 1.00 137.60 ? 518  LYS A CA   1 
ATOM   7939 C C    . LYS B 1 518 ? 183.442 149.512 115.500 1.00 138.60 ? 518  LYS A C    1 
ATOM   7940 O O    . LYS B 1 518 ? 183.426 148.879 116.563 1.00 139.91 ? 518  LYS A O    1 
ATOM   7941 C CB   . LYS B 1 518 ? 184.551 148.395 113.550 1.00 136.78 ? 518  LYS A CB   1 
ATOM   7942 N N    . GLU B 1 519 ? 183.682 150.828 115.468 1.00 142.29 ? 519  GLU A N    1 
ATOM   7943 C CA   . GLU B 1 519 ? 184.026 151.562 116.693 1.00 143.52 ? 519  GLU A CA   1 
ATOM   7944 C C    . GLU B 1 519 ? 182.959 151.531 117.796 1.00 144.22 ? 519  GLU A C    1 
ATOM   7945 O O    . GLU B 1 519 ? 183.310 151.366 118.969 1.00 143.83 ? 519  GLU A O    1 
ATOM   7946 C CB   . GLU B 1 519 ? 184.353 153.012 116.335 1.00 142.90 ? 519  GLU A CB   1 
ATOM   7947 N N    . GLN B 1 520 ? 181.674 151.722 117.479 1.00 145.01 ? 520  GLN A N    1 
ATOM   7948 C CA   . GLN B 1 520 ? 180.662 151.608 118.540 1.00 144.49 ? 520  GLN A CA   1 
ATOM   7949 C C    . GLN B 1 520 ? 180.615 150.193 119.109 1.00 144.07 ? 520  GLN A C    1 
ATOM   7950 O O    . GLN B 1 520 ? 180.503 150.008 120.327 1.00 144.20 ? 520  GLN A O    1 
ATOM   7951 C CB   . GLN B 1 520 ? 179.268 152.075 118.098 1.00 144.20 ? 520  GLN A CB   1 
ATOM   7952 C CG   . GLN B 1 520 ? 178.527 151.211 117.123 1.00 143.12 ? 520  GLN A CG   1 
ATOM   7953 C CD   . GLN B 1 520 ? 178.773 151.676 115.741 1.00 143.96 ? 520  GLN A CD   1 
ATOM   7954 O OE1  . GLN B 1 520 ? 179.885 152.074 115.429 1.00 143.36 ? 520  GLN A OE1  1 
ATOM   7955 N NE2  . GLN B 1 520 ? 177.757 151.623 114.890 1.00 143.58 ? 520  GLN A NE2  1 
ATOM   7956 N N    . MET B 1 521 ? 180.673 149.188 118.235 1.00 134.43 ? 521  MET A N    1 
ATOM   7957 C CA   . MET B 1 521 ? 180.542 147.797 118.648 1.00 133.81 ? 521  MET A CA   1 
ATOM   7958 C C    . MET B 1 521 ? 181.680 147.365 119.571 1.00 133.59 ? 521  MET A C    1 
ATOM   7959 O O    . MET B 1 521 ? 181.454 146.618 120.531 1.00 135.14 ? 521  MET A O    1 
ATOM   7960 C CB   . MET B 1 521 ? 180.491 146.945 117.378 1.00 133.08 ? 521  MET A CB   1 
ATOM   7961 C CG   . MET B 1 521 ? 180.557 145.462 117.545 1.00 134.16 ? 521  MET A CG   1 
ATOM   7962 S SD   . MET B 1 521 ? 179.396 144.797 118.728 1.00 133.38 ? 521  MET A SD   1 
ATOM   7963 C CE   . MET B 1 521 ? 180.191 143.227 118.960 1.00 132.67 ? 521  MET A CE   1 
ATOM   7964 N N    . ILE B 1 522 ? 182.908 147.810 119.292 1.00 128.35 ? 522  ILE A N    1 
ATOM   7965 C CA   . ILE B 1 522 ? 184.052 147.456 120.135 1.00 129.75 ? 522  ILE A CA   1 
ATOM   7966 C C    . ILE B 1 522 ? 183.889 148.038 121.544 1.00 129.62 ? 522  ILE A C    1 
ATOM   7967 O O    . ILE B 1 522 ? 184.228 147.392 122.543 1.00 129.67 ? 522  ILE A O    1 
ATOM   7968 C CB   . ILE B 1 522 ? 185.386 147.846 119.454 1.00 130.93 ? 522  ILE A CB   1 
ATOM   7969 C CG1  . ILE B 1 522 ? 186.522 146.957 119.971 1.00 130.38 ? 522  ILE A CG1  1 
ATOM   7970 C CG2  . ILE B 1 522 ? 185.745 149.323 119.599 1.00 129.82 ? 522  ILE A CG2  1 
ATOM   7971 C CD1  . ILE B 1 522 ? 186.511 145.554 119.399 1.00 127.84 ? 522  ILE A CD1  1 
ATOM   7972 N N    . THR B 1 523 ? 183.376 149.272 121.638 1.00 130.33 ? 523  THR A N    1 
ATOM   7973 C CA   . THR B 1 523 ? 183.172 149.963 122.913 1.00 130.99 ? 523  THR A CA   1 
ATOM   7974 C C    . THR B 1 523 ? 182.192 149.234 123.829 1.00 130.66 ? 523  THR A C    1 
ATOM   7975 O O    . THR B 1 523 ? 182.386 149.209 125.050 1.00 131.60 ? 523  THR A O    1 
ATOM   7976 C CB   . THR B 1 523 ? 182.699 151.397 122.670 1.00 130.86 ? 523  THR A CB   1 
ATOM   7977 O OG1  . THR B 1 523 ? 181.574 151.394 121.785 1.00 131.33 ? 523  THR A OG1  1 
ATOM   7978 C CG2  . THR B 1 523 ? 183.819 152.236 122.074 1.00 130.95 ? 523  THR A CG2  1 
ATOM   7979 N N    . THR B 1 524 ? 181.122 148.664 123.268 1.00 129.41 ? 524  THR A N    1 
ATOM   7980 C CA   . THR B 1 524 ? 180.138 147.951 124.083 1.00 130.75 ? 524  THR A CA   1 
ATOM   7981 C C    . THR B 1 524 ? 180.761 146.760 124.807 1.00 131.28 ? 524  THR A C    1 
ATOM   7982 O O    . THR B 1 524 ? 180.453 146.516 125.980 1.00 131.50 ? 524  THR A O    1 
ATOM   7983 C CB   . THR B 1 524 ? 178.970 147.496 123.206 1.00 129.49 ? 524  THR A CB   1 
ATOM   7984 O OG1  . THR B 1 524 ? 178.385 148.634 122.562 1.00 128.32 ? 524  THR A OG1  1 
ATOM   7985 C CG2  . THR B 1 524 ? 177.903 146.798 124.040 1.00 130.19 ? 524  THR A CG2  1 
ATOM   7986 N N    . ALA B 1 525 ? 181.625 146.001 124.129 1.00 130.75 ? 525  ALA A N    1 
ATOM   7987 C CA   . ALA B 1 525 ? 182.245 144.841 124.767 1.00 129.67 ? 525  ALA A CA   1 
ATOM   7988 C C    . ALA B 1 525 ? 183.107 145.266 125.954 1.00 131.45 ? 525  ALA A C    1 
ATOM   7989 O O    . ALA B 1 525 ? 183.087 144.622 127.010 1.00 131.69 ? 525  ALA A O    1 
ATOM   7990 C CB   . ALA B 1 525 ? 183.075 144.059 123.749 1.00 130.17 ? 525  ALA A CB   1 
ATOM   7991 N N    . VAL B 1 526 ? 183.880 146.343 125.788 1.00 134.09 ? 526  VAL A N    1 
ATOM   7992 C CA   . VAL B 1 526 ? 184.732 146.863 126.858 1.00 133.44 ? 526  VAL A CA   1 
ATOM   7993 C C    . VAL B 1 526 ? 183.890 147.342 128.038 1.00 132.30 ? 526  VAL A C    1 
ATOM   7994 O O    . VAL B 1 526 ? 184.221 147.087 129.203 1.00 131.08 ? 526  VAL A O    1 
ATOM   7995 C CB   . VAL B 1 526 ? 185.641 147.982 126.314 1.00 133.41 ? 526  VAL A CB   1 
ATOM   7996 C CG1  . VAL B 1 526 ? 186.415 148.649 127.442 1.00 133.64 ? 526  VAL A CG1  1 
ATOM   7997 C CG2  . VAL B 1 526 ? 186.590 147.429 125.264 1.00 133.20 ? 526  VAL A CG2  1 
ATOM   7998 N N    . THR B 1 527 ? 182.789 148.042 127.751 1.00 130.61 ? 527  THR A N    1 
ATOM   7999 C CA   . THR B 1 527 ? 181.903 148.550 128.799 1.00 129.63 ? 527  THR A CA   1 
ATOM   8000 C C    . THR B 1 527 ? 181.288 147.420 129.618 1.00 130.19 ? 527  THR A C    1 
ATOM   8001 O O    . THR B 1 527 ? 181.207 147.511 130.849 1.00 128.81 ? 527  THR A O    1 
ATOM   8002 C CB   . THR B 1 527 ? 180.805 149.417 128.180 1.00 130.88 ? 527  THR A CB   1 
ATOM   8003 O OG1  . THR B 1 527 ? 181.398 150.410 127.334 1.00 131.76 ? 527  THR A OG1  1 
ATOM   8004 C CG2  . THR B 1 527 ? 179.994 150.111 129.264 1.00 130.20 ? 527  THR A CG2  1 
ATOM   8005 N N    . LEU B 1 528 ? 180.843 146.352 128.952 1.00 129.66 ? 528  LEU A N    1 
ATOM   8006 C CA   . LEU B 1 528 ? 180.266 145.212 129.660 1.00 128.32 ? 528  LEU A CA   1 
ATOM   8007 C C    . LEU B 1 528 ? 181.291 144.535 130.564 1.00 127.94 ? 528  LEU A C    1 
ATOM   8008 O O    . LEU B 1 528 ? 180.969 144.153 131.695 1.00 126.71 ? 528  LEU A O    1 
ATOM   8009 C CB   . LEU B 1 528 ? 179.690 144.208 128.662 1.00 129.33 ? 528  LEU A CB   1 
ATOM   8010 C CG   . LEU B 1 528 ? 178.433 144.643 127.908 1.00 127.55 ? 528  LEU A CG   1 
ATOM   8011 C CD1  . LEU B 1 528 ? 178.019 143.585 126.901 1.00 126.14 ? 528  LEU A CD1  1 
ATOM   8012 C CD2  . LEU B 1 528 ? 177.307 144.925 128.880 1.00 127.70 ? 528  LEU A CD2  1 
ATOM   8013 N N    . PHE B 1 529 ? 182.528 144.378 130.085 1.00 137.17 ? 529  PHE A N    1 
ATOM   8014 C CA   . PHE B 1 529 ? 183.563 143.710 130.873 1.00 136.55 ? 529  PHE A CA   1 
ATOM   8015 C C    . PHE B 1 529 ? 183.874 144.464 132.163 1.00 136.02 ? 529  PHE A C    1 
ATOM   8016 O O    . PHE B 1 529 ? 184.050 143.845 133.219 1.00 135.17 ? 529  PHE A O    1 
ATOM   8017 C CB   . PHE B 1 529 ? 184.833 143.547 130.038 1.00 136.91 ? 529  PHE A CB   1 
ATOM   8018 C CG   . PHE B 1 529 ? 185.956 142.872 130.772 1.00 137.16 ? 529  PHE A CG   1 
ATOM   8019 C CD1  . PHE B 1 529 ? 185.927 141.506 131.008 1.00 136.53 ? 529  PHE A CD1  1 
ATOM   8020 C CD2  . PHE B 1 529 ? 187.042 143.602 131.228 1.00 137.44 ? 529  PHE A CD2  1 
ATOM   8021 C CE1  . PHE B 1 529 ? 186.961 140.882 131.683 1.00 135.18 ? 529  PHE A CE1  1 
ATOM   8022 C CE2  . PHE B 1 529 ? 188.079 142.985 131.904 1.00 137.14 ? 529  PHE A CE2  1 
ATOM   8023 C CZ   . PHE B 1 529 ? 188.039 141.623 132.131 1.00 136.03 ? 529  PHE A CZ   1 
ATOM   8024 N N    . CYS B 1 530 ? 183.973 145.795 132.095 1.00 141.06 ? 530  CYS A N    1 
ATOM   8025 C CA   . CYS B 1 530 ? 184.238 146.580 133.298 1.00 140.61 ? 530  CYS A CA   1 
ATOM   8026 C C    . CYS B 1 530 ? 183.103 146.459 134.310 1.00 139.69 ? 530  CYS A C    1 
ATOM   8027 O O    . CYS B 1 530 ? 183.351 146.329 135.515 1.00 138.83 ? 530  CYS A O    1 
ATOM   8028 C CB   . CYS B 1 530 ? 184.471 148.045 132.929 1.00 141.72 ? 530  CYS A CB   1 
ATOM   8029 S SG   . CYS B 1 530 ? 185.828 148.321 131.765 1.00 143.56 ? 530  CYS A SG   1 
ATOM   8030 N N    . SER B 1 531 ? 181.852 146.518 133.843 1.00 135.39 ? 531  SER A N    1 
ATOM   8031 C CA   . SER B 1 531 ? 180.711 146.417 134.751 1.00 135.86 ? 531  SER A CA   1 
ATOM   8032 C C    . SER B 1 531 ? 180.635 145.046 135.417 1.00 135.48 ? 531  SER A C    1 
ATOM   8033 O O    . SER B 1 531 ? 180.355 144.952 136.617 1.00 134.03 ? 531  SER A O    1 
ATOM   8034 C CB   . SER B 1 531 ? 179.414 146.718 133.999 1.00 136.52 ? 531  SER A CB   1 
ATOM   8035 O OG   . SER B 1 531 ? 179.185 148.114 133.919 1.00 136.29 ? 531  SER A OG   1 
ATOM   8036 N N    . ILE B 1 532 ? 180.864 143.976 134.650 1.00 132.53 ? 532  ILE A N    1 
ATOM   8037 C CA   . ILE B 1 532 ? 180.779 142.618 135.189 1.00 131.70 ? 532  ILE A CA   1 
ATOM   8038 C C    . ILE B 1 532 ? 181.834 142.388 136.266 1.00 132.19 ? 532  ILE A C    1 
ATOM   8039 O O    . ILE B 1 532 ? 181.542 141.824 137.329 1.00 130.74 ? 532  ILE A O    1 
ATOM   8040 C CB   . ILE B 1 532 ? 180.890 141.583 134.052 1.00 130.08 ? 532  ILE A CB   1 
ATOM   8041 C CG1  . ILE B 1 532 ? 179.642 141.625 133.168 1.00 129.50 ? 532  ILE A CG1  1 
ATOM   8042 C CG2  . ILE B 1 532 ? 181.096 140.180 134.605 1.00 129.29 ? 532  ILE A CG2  1 
ATOM   8043 C CD1  . ILE B 1 532 ? 179.821 140.951 131.826 1.00 130.36 ? 532  ILE A CD1  1 
ATOM   8044 N N    . LEU B 1 533 ? 183.073 142.818 136.012 1.00 142.13 ? 533  LEU A N    1 
ATOM   8045 C CA   . LEU B 1 533 ? 184.133 142.671 137.007 1.00 140.64 ? 533  LEU A CA   1 
ATOM   8046 C C    . LEU B 1 533 ? 183.835 143.467 138.273 1.00 141.35 ? 533  LEU A C    1 
ATOM   8047 O O    . LEU B 1 533 ? 184.036 142.967 139.386 1.00 141.38 ? 533  LEU A O    1 
ATOM   8048 C CB   . LEU B 1 533 ? 185.472 143.103 136.406 1.00 139.77 ? 533  LEU A CB   1 
ATOM   8049 C CG   . LEU B 1 533 ? 186.591 143.496 137.375 1.00 139.38 ? 533  LEU A CG   1 
ATOM   8050 C CD1  . LEU B 1 533 ? 187.156 142.271 138.082 1.00 138.88 ? 533  LEU A CD1  1 
ATOM   8051 C CD2  . LEU B 1 533 ? 187.690 144.255 136.648 1.00 140.98 ? 533  LEU A CD2  1 
ATOM   8052 N N    . ILE B 1 534 ? 183.373 144.711 138.126 1.00 141.90 ? 534  ILE A N    1 
ATOM   8053 C CA   . ILE B 1 534 ? 183.067 145.532 139.295 1.00 140.57 ? 534  ILE A CA   1 
ATOM   8054 C C    . ILE B 1 534 ? 181.912 144.925 140.086 1.00 140.34 ? 534  ILE A C    1 
ATOM   8055 O O    . ILE B 1 534 ? 181.983 144.784 141.313 1.00 138.85 ? 534  ILE A O    1 
ATOM   8056 C CB   . ILE B 1 534 ? 182.767 146.979 138.861 1.00 140.65 ? 534  ILE A CB   1 
ATOM   8057 C CG1  . ILE B 1 534 ? 184.069 147.744 138.620 1.00 141.90 ? 534  ILE A CG1  1 
ATOM   8058 C CG2  . ILE B 1 534 ? 181.918 147.702 139.894 1.00 139.46 ? 534  ILE A CG2  1 
ATOM   8059 C CD1  . ILE B 1 534 ? 183.870 149.090 137.960 1.00 141.73 ? 534  ILE A CD1  1 
ATOM   8060 N N    . ALA B 1 535 ? 180.832 144.557 139.392 1.00 146.19 ? 535  ALA A N    1 
ATOM   8061 C CA   . ALA B 1 535 ? 179.687 143.935 140.052 1.00 146.44 ? 535  ALA A CA   1 
ATOM   8062 C C    . ALA B 1 535 ? 180.030 142.561 140.619 1.00 147.09 ? 535  ALA A C    1 
ATOM   8063 O O    . ALA B 1 535 ? 179.598 142.216 141.726 1.00 146.37 ? 535  ALA A O    1 
ATOM   8064 C CB   . ALA B 1 535 ? 178.511 143.839 139.082 1.00 143.65 ? 535  ALA A CB   1 
ATOM   8065 N N    . GLY B 1 536 ? 180.789 141.759 139.868 1.00 151.42 ? 536  GLY A N    1 
ATOM   8066 C CA   . GLY B 1 536 ? 181.120 140.416 140.322 1.00 150.52 ? 536  GLY A CA   1 
ATOM   8067 C C    . GLY B 1 536 ? 181.995 140.383 141.561 1.00 151.65 ? 536  GLY A C    1 
ATOM   8068 O O    . GLY B 1 536 ? 181.766 139.574 142.466 1.00 151.09 ? 536  GLY A O    1 
ATOM   8069 N N    . ILE B 1 537 ? 183.024 141.234 141.606 1.00 153.84 ? 537  ILE A N    1 
ATOM   8070 C CA   . ILE B 1 537 ? 183.974 141.212 142.718 1.00 152.52 ? 537  ILE A CA   1 
ATOM   8071 C C    . ILE B 1 537 ? 183.279 141.554 144.030 1.00 153.88 ? 537  ILE A C    1 
ATOM   8072 O O    . ILE B 1 537 ? 183.541 140.935 145.068 1.00 153.61 ? 537  ILE A O    1 
ATOM   8073 C CB   . ILE B 1 537 ? 185.149 142.166 142.436 1.00 151.88 ? 537  ILE A CB   1 
ATOM   8074 N N    . SER B 1 538 ? 182.397 142.557 144.007 1.00 157.44 ? 538  SER A N    1 
ATOM   8075 C CA   . SER B 1 538 ? 181.694 142.964 145.219 1.00 157.16 ? 538  SER A CA   1 
ATOM   8076 C C    . SER B 1 538 ? 180.768 141.867 145.734 1.00 157.07 ? 538  SER A C    1 
ATOM   8077 O O    . SER B 1 538 ? 180.658 141.662 146.949 1.00 155.72 ? 538  SER A O    1 
ATOM   8078 C CB   . SER B 1 538 ? 180.907 144.246 144.952 1.00 155.88 ? 538  SER A CB   1 
ATOM   8079 N N    . LEU B 1 539 ? 180.078 141.168 144.827 1.00 163.54 ? 539  LEU A N    1 
ATOM   8080 C CA   . LEU B 1 539 ? 179.083 140.179 145.237 1.00 163.95 ? 539  LEU A CA   1 
ATOM   8081 C C    . LEU B 1 539 ? 179.716 138.996 145.963 1.00 164.75 ? 539  LEU A C    1 
ATOM   8082 O O    . LEU B 1 539 ? 179.198 138.545 146.992 1.00 164.78 ? 539  LEU A O    1 
ATOM   8083 C CB   . LEU B 1 539 ? 178.294 139.697 144.021 1.00 163.06 ? 539  LEU A CB   1 
ATOM   8084 N N    . MET B 1 540 ? 180.828 138.471 145.436 1.00 167.97 ? 540  MET A N    1 
ATOM   8085 C CA   . MET B 1 540 ? 181.524 137.371 146.101 1.00 167.67 ? 540  MET A CA   1 
ATOM   8086 C C    . MET B 1 540 ? 182.101 137.785 147.449 1.00 168.00 ? 540  MET A C    1 
ATOM   8087 O O    . MET B 1 540 ? 182.244 136.943 148.344 1.00 167.74 ? 540  MET A O    1 
ATOM   8088 C CB   . MET B 1 540 ? 182.632 136.832 145.197 1.00 166.61 ? 540  MET A CB   1 
ATOM   8089 N N    . CYS B 1 541 ? 182.440 139.065 147.611 1.00 167.78 ? 541  CYS A N    1 
ATOM   8090 C CA   . CYS B 1 541 ? 182.914 139.556 148.900 1.00 167.78 ? 541  CYS A CA   1 
ATOM   8091 C C    . CYS B 1 541 ? 181.812 139.547 149.953 1.00 168.85 ? 541  CYS A C    1 
ATOM   8092 O O    . CYS B 1 541 ? 182.088 139.306 151.133 1.00 168.33 ? 541  CYS A O    1 
ATOM   8093 C CB   . CYS B 1 541 ? 183.496 140.958 148.741 1.00 166.99 ? 541  CYS A CB   1 
ATOM   8094 N N    . MET B 1 542 ? 180.568 139.817 149.547 1.00 173.92 ? 542  MET A N    1 
ATOM   8095 C CA   . MET B 1 542 ? 179.442 139.799 150.478 1.00 174.00 ? 542  MET A CA   1 
ATOM   8096 C C    . MET B 1 542 ? 179.221 138.410 151.067 1.00 173.85 ? 542  MET A C    1 
ATOM   8097 O O    . MET B 1 542 ? 178.983 138.270 152.272 1.00 172.55 ? 542  MET A O    1 
ATOM   8098 C CB   . MET B 1 542 ? 178.175 140.290 149.778 1.00 172.81 ? 542  MET A CB   1 
ATOM   8099 N N    . ASN B 1 543 ? 179.273 137.375 150.224 1.00 176.12 ? 543  ASN A N    1 
ATOM   8100 C CA   . ASN B 1 543 ? 179.085 136.005 150.695 1.00 175.99 ? 543  ASN A CA   1 
ATOM   8101 C C    . ASN B 1 543 ? 180.175 135.592 151.677 1.00 176.58 ? 543  ASN A C    1 
ATOM   8102 O O    . ASN B 1 543 ? 179.888 134.966 152.705 1.00 176.70 ? 543  ASN A O    1 
ATOM   8103 C CB   . ASN B 1 543 ? 179.043 135.045 149.507 1.00 175.20 ? 543  ASN A CB   1 
ATOM   8104 N N    . GLN B 1 544 ? 181.434 135.921 151.375 1.00 177.33 ? 544  GLN A N    1 
ATOM   8105 C CA   . GLN B 1 544 ? 182.523 135.581 152.287 1.00 177.41 ? 544  GLN A CA   1 
ATOM   8106 C C    . GLN B 1 544 ? 182.445 136.384 153.582 1.00 177.90 ? 544  GLN A C    1 
ATOM   8107 O O    . GLN B 1 544 ? 182.647 135.830 154.669 1.00 178.06 ? 544  GLN A O    1 
ATOM   8108 C CB   . GLN B 1 544 ? 183.869 135.804 151.599 1.00 176.22 ? 544  GLN A CB   1 
ATOM   8109 N N    . THR B 1 545 ? 182.174 137.684 153.489 1.00 177.40 ? 545  THR A N    1 
ATOM   8110 C CA   . THR B 1 545 ? 182.115 138.547 154.669 1.00 177.59 ? 545  THR A CA   1 
ATOM   8111 C C    . THR B 1 545 ? 180.980 138.147 155.610 1.00 177.22 ? 545  THR A C    1 
ATOM   8112 O O    . THR B 1 545 ? 181.206 137.501 156.633 1.00 176.95 ? 545  THR A O    1 
ATOM   8113 C CB   . THR B 1 545 ? 181.939 140.028 154.285 1.00 176.81 ? 545  THR A CB   1 
ATOM   8114 N N    . GLN B 1 654 ? 165.545 146.294 150.688 1.00 103.08 ? 654  GLN A N    1 
ATOM   8115 C CA   . GLN B 1 654 ? 165.671 145.063 151.458 1.00 102.59 ? 654  GLN A CA   1 
ATOM   8116 C C    . GLN B 1 654 ? 166.654 144.087 150.803 1.00 105.64 ? 654  GLN A C    1 
ATOM   8117 O O    . GLN B 1 654 ? 166.568 143.816 149.605 1.00 107.89 ? 654  GLN A O    1 
ATOM   8118 C CB   . GLN B 1 654 ? 164.290 144.413 151.647 1.00 103.31 ? 654  GLN A CB   1 
ATOM   8119 C CG   . GLN B 1 654 ? 163.535 144.094 150.359 1.00 103.14 ? 654  GLN A CG   1 
ATOM   8120 C CD   . GLN B 1 654 ? 162.032 144.234 150.508 1.00 103.08 ? 654  GLN A CD   1 
ATOM   8121 O OE1  . GLN B 1 654 ? 161.516 144.369 151.617 1.00 105.20 ? 654  GLN A OE1  1 
ATOM   8122 N NE2  . GLN B 1 654 ? 161.321 144.203 149.386 1.00 102.34 ? 654  GLN A NE2  1 
ATOM   8123 N N    . LEU B 1 655 ? 167.622 143.621 151.604 1.00 105.26 ? 655  LEU A N    1 
ATOM   8124 C CA   . LEU B 1 655 ? 168.678 142.735 151.110 1.00 105.56 ? 655  LEU A CA   1 
ATOM   8125 C C    . LEU B 1 655 ? 168.096 141.488 150.458 1.00 105.10 ? 655  LEU A C    1 
ATOM   8126 O O    . LEU B 1 655 ? 168.426 141.179 149.307 1.00 105.83 ? 655  LEU A O    1 
ATOM   8127 C CB   . LEU B 1 655 ? 169.612 142.346 152.257 1.00 104.37 ? 655  LEU A CB   1 
ATOM   8128 C CG   . LEU B 1 655 ? 170.346 143.441 153.040 1.00 104.93 ? 655  LEU A CG   1 
ATOM   8129 C CD1  . LEU B 1 655 ? 171.591 142.871 153.701 1.00 104.88 ? 655  LEU A CD1  1 
ATOM   8130 C CD2  . LEU B 1 655 ? 170.709 144.633 152.167 1.00 104.71 ? 655  LEU A CD2  1 
ATOM   8131 N N    . THR B 1 656 ? 167.282 140.745 151.223 1.00 104.61 ? 656  THR A N    1 
ATOM   8132 C CA   . THR B 1 656 ? 166.641 139.479 150.845 1.00 106.34 ? 656  THR A CA   1 
ATOM   8133 C C    . THR B 1 656 ? 166.208 139.427 149.377 1.00 104.72 ? 656  THR A C    1 
ATOM   8134 O O    . THR B 1 656 ? 166.318 138.378 148.729 1.00 104.39 ? 656  THR A O    1 
ATOM   8135 C CB   . THR B 1 656 ? 165.450 139.225 151.773 1.00 108.97 ? 656  THR A CB   1 
ATOM   8136 O OG1  . THR B 1 656 ? 165.923 139.088 153.119 1.00 108.50 ? 656  THR A OG1  1 
ATOM   8137 C CG2  . THR B 1 656 ? 164.724 137.946 151.396 1.00 105.27 ? 656  THR A CG2  1 
ATOM   8138 N N    . ARG B 1 657 ? 165.767 140.556 148.818 1.00 97.38  ? 657  ARG A N    1 
ATOM   8139 C CA   . ARG B 1 657 ? 165.369 140.583 147.413 1.00 97.50  ? 657  ARG A CA   1 
ATOM   8140 C C    . ARG B 1 657 ? 166.428 141.229 146.528 1.00 99.57  ? 657  ARG A C    1 
ATOM   8141 O O    . ARG B 1 657 ? 166.871 140.606 145.557 1.00 100.50 ? 657  ARG A O    1 
ATOM   8142 C CB   . ARG B 1 657 ? 164.031 141.310 147.264 1.00 98.40  ? 657  ARG A CB   1 
ATOM   8143 C CG   . ARG B 1 657 ? 163.020 140.984 148.348 1.00 98.51  ? 657  ARG A CG   1 
ATOM   8144 C CD   . ARG B 1 657 ? 162.120 139.837 147.919 1.00 98.93  ? 657  ARG A CD   1 
ATOM   8145 N NE   . ARG B 1 657 ? 161.137 139.495 148.939 1.00 103.58 ? 657  ARG A NE   1 
ATOM   8146 C CZ   . ARG B 1 657 ? 160.053 138.766 148.716 1.00 102.04 ? 657  ARG A CZ   1 
ATOM   8147 N NH1  . ARG B 1 657 ? 159.782 138.281 147.516 1.00 99.48  ? 657  ARG A NH1  1 
ATOM   8148 N NH2  . ARG B 1 657 ? 159.221 138.514 149.724 1.00 98.33  ? 657  ARG A NH2  1 
ATOM   8149 N N    . HIS B 1 658 ? 166.766 142.507 146.784 1.00 98.67  ? 658  HIS A N    1 
ATOM   8150 C CA   . HIS B 1 658 ? 167.797 143.285 146.078 1.00 98.19  ? 658  HIS A CA   1 
ATOM   8151 C C    . HIS B 1 658 ? 168.889 142.443 145.425 1.00 102.29 ? 658  HIS A C    1 
ATOM   8152 O O    . HIS B 1 658 ? 169.141 142.578 144.223 1.00 106.90 ? 658  HIS A O    1 
ATOM   8153 C CB   . HIS B 1 658 ? 168.474 144.264 147.042 1.00 99.94  ? 658  HIS A CB   1 
ATOM   8154 C CG   . HIS B 1 658 ? 167.861 145.630 147.066 1.00 101.25 ? 658  HIS A CG   1 
ATOM   8155 N ND1  . HIS B 1 658 ? 166.532 145.848 147.353 1.00 101.72 ? 658  HIS A ND1  1 
ATOM   8156 C CD2  . HIS B 1 658 ? 168.406 146.851 146.851 1.00 101.46 ? 658  HIS A CD2  1 
ATOM   8157 C CE1  . HIS B 1 658 ? 166.282 147.145 147.311 1.00 101.84 ? 658  HIS A CE1  1 
ATOM   8158 N NE2  . HIS B 1 658 ? 167.402 147.775 147.007 1.00 101.32 ? 658  HIS A NE2  1 
ATOM   8159 N N    . VAL B 1 659 ? 169.575 141.633 146.244 1.00 103.13 ? 659  VAL A N    1 
ATOM   8160 C CA   . VAL B 1 659 ? 170.686 140.784 145.802 1.00 104.12 ? 659  VAL A CA   1 
ATOM   8161 C C    . VAL B 1 659 ? 170.327 140.007 144.538 1.00 102.15 ? 659  VAL A C    1 
ATOM   8162 O O    . VAL B 1 659 ? 171.125 139.908 143.597 1.00 100.25 ? 659  VAL A O    1 
ATOM   8163 C CB   . VAL B 1 659 ? 171.113 139.839 146.943 1.00 104.49 ? 659  VAL A CB   1 
ATOM   8164 C CG1  . VAL B 1 659 ? 172.087 138.782 146.442 1.00 105.43 ? 659  VAL A CG1  1 
ATOM   8165 C CG2  . VAL B 1 659 ? 171.723 140.631 148.088 1.00 102.21 ? 659  VAL A CG2  1 
ATOM   8166 N N    . LEU B 1 660 ? 169.112 139.447 144.504 1.00 94.59  ? 660  LEU A N    1 
ATOM   8167 C CA   . LEU B 1 660 ? 168.674 138.620 143.381 1.00 94.40  ? 660  LEU A CA   1 
ATOM   8168 C C    . LEU B 1 660 ? 168.602 139.403 142.076 1.00 96.81  ? 660  LEU A C    1 
ATOM   8169 O O    . LEU B 1 660 ? 168.954 138.874 141.015 1.00 101.81 ? 660  LEU A O    1 
ATOM   8170 C CB   . LEU B 1 660 ? 167.315 137.992 143.694 1.00 96.26  ? 660  LEU A CB   1 
ATOM   8171 C CG   . LEU B 1 660 ? 167.244 136.466 143.783 1.00 97.90  ? 660  LEU A CG   1 
ATOM   8172 C CD1  . LEU B 1 660 ? 165.797 135.999 143.796 1.00 97.27  ? 660  LEU A CD1  1 
ATOM   8173 C CD2  . LEU B 1 660 ? 168.004 135.820 142.635 1.00 99.65  ? 660  LEU A CD2  1 
ATOM   8174 N N    . LEU B 1 661 ? 168.112 140.646 142.125 1.00 88.70  ? 661  LEU A N    1 
ATOM   8175 C CA   . LEU B 1 661 ? 168.093 141.479 140.924 1.00 90.46  ? 661  LEU A CA   1 
ATOM   8176 C C    . LEU B 1 661 ? 169.493 141.681 140.357 1.00 91.89  ? 661  LEU A C    1 
ATOM   8177 O O    . LEU B 1 661 ? 169.678 141.699 139.135 1.00 94.80  ? 661  LEU A O    1 
ATOM   8178 C CB   . LEU B 1 661 ? 167.442 142.827 141.237 1.00 89.00  ? 661  LEU A CB   1 
ATOM   8179 C CG   . LEU B 1 661 ? 167.270 143.810 140.078 1.00 88.27  ? 661  LEU A CG   1 
ATOM   8180 C CD1  . LEU B 1 661 ? 165.913 143.637 139.420 1.00 91.00  ? 661  LEU A CD1  1 
ATOM   8181 C CD2  . LEU B 1 661 ? 167.455 145.238 140.562 1.00 87.93  ? 661  LEU A CD2  1 
ATOM   8182 N N    . CYS B 1 662 ? 170.490 141.841 141.229 1.00 96.21  ? 662  CYS A N    1 
ATOM   8183 C CA   . CYS B 1 662 ? 171.876 141.872 140.773 1.00 98.82  ? 662  CYS A CA   1 
ATOM   8184 C C    . CYS B 1 662 ? 172.295 140.538 140.164 1.00 100.83 ? 662  CYS A C    1 
ATOM   8185 O O    . CYS B 1 662 ? 172.960 140.506 139.121 1.00 96.38  ? 662  CYS A O    1 
ATOM   8186 C CB   . CYS B 1 662 ? 172.800 142.247 141.931 1.00 95.93  ? 662  CYS A CB   1 
ATOM   8187 S SG   . CYS B 1 662 ? 173.091 144.022 142.103 1.00 99.12  ? 662  CYS A SG   1 
ATOM   8188 N N    . LEU B 1 663 ? 171.933 139.429 140.818 1.00 104.09 ? 663  LEU A N    1 
ATOM   8189 C CA   . LEU B 1 663 ? 172.333 138.103 140.352 1.00 101.60 ? 663  LEU A CA   1 
ATOM   8190 C C    . LEU B 1 663 ? 171.757 137.773 138.979 1.00 97.75  ? 663  LEU A C    1 
ATOM   8191 O O    . LEU B 1 663 ? 172.464 137.253 138.109 1.00 98.13  ? 663  LEU A O    1 
ATOM   8192 C CB   . LEU B 1 663 ? 171.912 137.048 141.376 1.00 100.79 ? 663  LEU A CB   1 
ATOM   8193 C CG   . LEU B 1 663 ? 172.509 135.650 141.202 1.00 101.20 ? 663  LEU A CG   1 
ATOM   8194 C CD1  . LEU B 1 663 ? 173.171 135.188 142.490 1.00 98.10  ? 663  LEU A CD1  1 
ATOM   8195 C CD2  . LEU B 1 663 ? 171.441 134.662 140.761 1.00 100.77 ? 663  LEU A CD2  1 
ATOM   8196 N N    . LEU B 1 664 ? 170.467 138.052 138.769 1.00 85.15  ? 664  LEU A N    1 
ATOM   8197 C CA   . LEU B 1 664 ? 169.862 137.775 137.468 1.00 85.84  ? 664  LEU A CA   1 
ATOM   8198 C C    . LEU B 1 664 ? 170.446 138.658 136.373 1.00 91.22  ? 664  LEU A C    1 
ATOM   8199 O O    . LEU B 1 664 ? 170.628 138.204 135.237 1.00 93.21  ? 664  LEU A O    1 
ATOM   8200 C CB   . LEU B 1 664 ? 168.346 137.951 137.542 1.00 85.10  ? 664  LEU A CB   1 
ATOM   8201 C CG   . LEU B 1 664 ? 167.558 136.800 138.169 1.00 84.73  ? 664  LEU A CG   1 
ATOM   8202 C CD1  . LEU B 1 664 ? 166.297 137.314 138.843 1.00 89.83  ? 664  LEU A CD1  1 
ATOM   8203 C CD2  . LEU B 1 664 ? 167.220 135.754 137.120 1.00 86.69  ? 664  LEU A CD2  1 
ATOM   8204 N N    . LEU B 1 665 ? 170.727 139.925 136.688 1.00 94.02  ? 665  LEU A N    1 
ATOM   8205 C CA   . LEU B 1 665 ? 171.309 140.828 135.698 1.00 93.61  ? 665  LEU A CA   1 
ATOM   8206 C C    . LEU B 1 665 ? 172.704 140.381 135.273 1.00 96.12  ? 665  LEU A C    1 
ATOM   8207 O O    . LEU B 1 665 ? 173.038 140.430 134.083 1.00 95.38  ? 665  LEU A O    1 
ATOM   8208 C CB   . LEU B 1 665 ? 171.345 142.255 136.246 1.00 93.32  ? 665  LEU A CB   1 
ATOM   8209 C CG   . LEU B 1 665 ? 170.068 143.082 136.079 1.00 95.11  ? 665  LEU A CG   1 
ATOM   8210 C CD1  . LEU B 1 665 ? 170.334 144.553 136.364 1.00 94.24  ? 665  LEU A CD1  1 
ATOM   8211 C CD2  . LEU B 1 665 ? 169.481 142.903 134.688 1.00 93.80  ? 665  LEU A CD2  1 
ATOM   8212 N N    . ILE B 1 666 ? 173.538 139.973 136.235 1.00 100.97 ? 666  ILE A N    1 
ATOM   8213 C CA   . ILE B 1 666 ? 174.896 139.522 135.931 1.00 101.14 ? 666  ILE A CA   1 
ATOM   8214 C C    . ILE B 1 666 ? 174.880 138.315 134.997 1.00 99.88  ? 666  ILE A C    1 
ATOM   8215 O O    . ILE B 1 666 ? 175.706 138.213 134.079 1.00 99.67  ? 666  ILE A O    1 
ATOM   8216 C CB   . ILE B 1 666 ? 175.650 139.233 137.245 1.00 98.40  ? 666  ILE A CB   1 
ATOM   8217 C CG1  . ILE B 1 666 ? 176.227 140.530 137.813 1.00 99.00  ? 666  ILE A CG1  1 
ATOM   8218 C CG2  . ILE B 1 666 ? 176.756 138.204 137.053 1.00 97.97  ? 666  ILE A CG2  1 
ATOM   8219 C CD1  . ILE B 1 666 ? 177.210 141.203 136.884 1.00 103.09 ? 666  ILE A CD1  1 
ATOM   8220 N N    . ILE B 1 667 ? 173.932 137.395 135.201 1.00 95.36  ? 667  ILE A N    1 
ATOM   8221 C CA   . ILE B 1 667 ? 173.754 136.274 134.279 1.00 92.20  ? 667  ILE A CA   1 
ATOM   8222 C C    . ILE B 1 667 ? 173.427 136.774 132.876 1.00 90.30  ? 667  ILE A C    1 
ATOM   8223 O O    . ILE B 1 667 ? 173.939 136.253 131.876 1.00 91.48  ? 667  ILE A O    1 
ATOM   8224 C CB   . ILE B 1 667 ? 172.667 135.322 134.819 1.00 92.90  ? 667  ILE A CB   1 
ATOM   8225 C CG1  . ILE B 1 667 ? 173.239 134.441 135.934 1.00 92.67  ? 667  ILE A CG1  1 
ATOM   8226 C CG2  . ILE B 1 667 ? 172.069 134.467 133.703 1.00 92.25  ? 667  ILE A CG2  1 
ATOM   8227 C CD1  . ILE B 1 667 ? 172.350 133.275 136.327 1.00 92.01  ? 667  ILE A CD1  1 
ATOM   8228 N N    . GLY B 1 668 ? 172.601 137.817 132.784 1.00 95.20  ? 668  GLY A N    1 
ATOM   8229 C CA   . GLY B 1 668 ? 172.263 138.377 131.487 1.00 98.94  ? 668  GLY A CA   1 
ATOM   8230 C C    . GLY B 1 668 ? 173.430 139.034 130.774 1.00 101.36 ? 668  GLY A C    1 
ATOM   8231 O O    . GLY B 1 668 ? 173.599 138.863 129.564 1.00 102.02 ? 668  GLY A O    1 
ATOM   8232 N N    . LEU B 1 669 ? 174.239 139.808 131.506 1.00 98.71  ? 669  LEU A N    1 
ATOM   8233 C CA   . LEU B 1 669 ? 175.357 140.512 130.881 1.00 96.67  ? 669  LEU A CA   1 
ATOM   8234 C C    . LEU B 1 669 ? 176.395 139.553 130.315 1.00 100.37 ? 669  LEU A C    1 
ATOM   8235 O O    . LEU B 1 669 ? 177.034 139.864 129.303 1.00 99.77  ? 669  LEU A O    1 
ATOM   8236 C CB   . LEU B 1 669 ? 176.012 141.458 131.887 1.00 95.05  ? 669  LEU A CB   1 
ATOM   8237 C CG   . LEU B 1 669 ? 175.115 142.506 132.544 1.00 98.89  ? 669  LEU A CG   1 
ATOM   8238 C CD1  . LEU B 1 669 ? 175.775 143.059 133.794 1.00 98.76  ? 669  LEU A CD1  1 
ATOM   8239 C CD2  . LEU B 1 669 ? 174.794 143.624 131.566 1.00 100.61 ? 669  LEU A CD2  1 
ATOM   8240 N N    . PHE B 1 670 ? 176.597 138.402 130.961 1.00 106.36 ? 670  PHE A N    1 
ATOM   8241 C CA   . PHE B 1 670 ? 177.533 137.413 130.435 1.00 104.61 ? 670  PHE A CA   1 
ATOM   8242 C C    . PHE B 1 670 ? 177.071 136.880 129.084 1.00 104.88 ? 670  PHE A C    1 
ATOM   8243 O O    . PHE B 1 670 ? 177.883 136.701 128.167 1.00 103.86 ? 670  PHE A O    1 
ATOM   8244 C CB   . PHE B 1 670 ? 177.707 136.271 131.437 1.00 105.13 ? 670  PHE A CB   1 
ATOM   8245 C CG   . PHE B 1 670 ? 178.987 136.344 132.219 1.00 105.20 ? 670  PHE A CG   1 
ATOM   8246 C CD1  . PHE B 1 670 ? 180.209 136.394 131.569 1.00 105.20 ? 670  PHE A CD1  1 
ATOM   8247 C CD2  . PHE B 1 670 ? 178.968 136.363 133.604 1.00 104.92 ? 670  PHE A CD2  1 
ATOM   8248 C CE1  . PHE B 1 670 ? 181.390 136.462 132.285 1.00 105.15 ? 670  PHE A CE1  1 
ATOM   8249 C CE2  . PHE B 1 670 ? 180.145 136.430 134.327 1.00 104.04 ? 670  PHE A CE2  1 
ATOM   8250 C CZ   . PHE B 1 670 ? 181.358 136.479 133.666 1.00 104.96 ? 670  PHE A CZ   1 
ATOM   8251 N N    . ALA B 1 671 ? 175.769 136.606 128.951 1.00 106.20 ? 671  ALA A N    1 
ATOM   8252 C CA   . ALA B 1 671 ? 175.223 136.116 127.688 1.00 105.13 ? 671  ALA A CA   1 
ATOM   8253 C C    . ALA B 1 671 ? 175.382 137.142 126.573 1.00 105.43 ? 671  ALA A C    1 
ATOM   8254 O O    . ALA B 1 671 ? 175.722 136.787 125.439 1.00 107.08 ? 671  ALA A O    1 
ATOM   8255 C CB   . ALA B 1 671 ? 173.752 135.741 127.864 1.00 104.59 ? 671  ALA A CB   1 
ATOM   8256 N N    . ASN B 1 672 ? 175.115 138.416 126.872 1.00 108.05 ? 672  ASN A N    1 
ATOM   8257 C CA   . ASN B 1 672 ? 175.288 139.467 125.874 1.00 108.74 ? 672  ASN A CA   1 
ATOM   8258 C C    . ASN B 1 672 ? 176.745 139.595 125.450 1.00 110.88 ? 672  ASN A C    1 
ATOM   8259 O O    . ASN B 1 672 ? 177.037 139.724 124.257 1.00 108.76 ? 672  ASN A O    1 
ATOM   8260 C CB   . ASN B 1 672 ? 174.775 140.803 126.419 1.00 108.12 ? 672  ASN A CB   1 
ATOM   8261 C CG   . ASN B 1 672 ? 174.288 141.742 125.323 1.00 107.38 ? 672  ASN A CG   1 
ATOM   8262 O OD1  . ASN B 1 672 ? 173.460 142.617 125.568 1.00 108.30 ? 672  ASN A OD1  1 
ATOM   8263 N ND2  . ASN B 1 672 ? 174.798 141.562 124.110 1.00 107.00 ? 672  ASN A ND2  1 
ATOM   8264 N N    . LEU B 1 673 ? 177.671 139.530 126.413 1.00 116.00 ? 673  LEU A N    1 
ATOM   8265 C CA   . LEU B 1 673 ? 179.091 139.705 126.117 1.00 113.34 ? 673  LEU A CA   1 
ATOM   8266 C C    . LEU B 1 673 ? 179.612 138.639 125.159 1.00 116.32 ? 673  LEU A C    1 
ATOM   8267 O O    . LEU B 1 673 ? 180.380 138.948 124.239 1.00 116.00 ? 673  LEU A O    1 
ATOM   8268 C CB   . LEU B 1 673 ? 179.898 139.698 127.416 1.00 111.26 ? 673  LEU A CB   1 
ATOM   8269 C CG   . LEU B 1 673 ? 181.422 139.751 127.284 1.00 112.37 ? 673  LEU A CG   1 
ATOM   8270 C CD1  . LEU B 1 673 ? 181.856 141.022 126.569 1.00 114.33 ? 673  LEU A CD1  1 
ATOM   8271 C CD2  . LEU B 1 673 ? 182.084 139.647 128.648 1.00 113.45 ? 673  LEU A CD2  1 
ATOM   8272 N N    . SER B 1 674 ? 179.225 137.377 125.370 1.00 119.54 ? 674  SER A N    1 
ATOM   8273 C CA   . SER B 1 674 ? 179.640 136.312 124.459 1.00 117.07 ? 674  SER A CA   1 
ATOM   8274 C C    . SER B 1 674 ? 179.126 136.548 123.042 1.00 116.88 ? 674  SER A C    1 
ATOM   8275 O O    . SER B 1 674 ? 179.802 136.203 122.066 1.00 116.98 ? 674  SER A O    1 
ATOM   8276 C CB   . SER B 1 674 ? 179.160 134.960 124.985 1.00 116.10 ? 674  SER A CB   1 
ATOM   8277 O OG   . SER B 1 674 ? 178.916 134.057 123.922 1.00 118.77 ? 674  SER A OG   1 
ATOM   8278 N N    . SER B 1 675 ? 177.922 137.116 122.909 1.00 118.37 ? 675  SER A N    1 
ATOM   8279 C CA   . SER B 1 675 ? 177.408 137.469 121.588 1.00 116.93 ? 675  SER A CA   1 
ATOM   8280 C C    . SER B 1 675 ? 178.281 138.527 120.922 1.00 117.20 ? 675  SER A C    1 
ATOM   8281 O O    . SER B 1 675 ? 178.555 138.453 119.718 1.00 119.31 ? 675  SER A O    1 
ATOM   8282 C CB   . SER B 1 675 ? 175.963 137.953 121.698 1.00 118.42 ? 675  SER A CB   1 
ATOM   8283 O OG   . SER B 1 675 ? 175.075 136.866 121.888 1.00 117.45 ? 675  SER A OG   1 
ATOM   8284 N N    . CYS B 1 676 ? 178.711 139.527 121.694 1.00 123.45 ? 676  CYS A N    1 
ATOM   8285 C CA   . CYS B 1 676 ? 179.626 140.546 121.188 1.00 125.58 ? 676  CYS A CA   1 
ATOM   8286 C C    . CYS B 1 676 ? 180.970 139.959 120.772 1.00 126.72 ? 676  CYS A C    1 
ATOM   8287 O O    . CYS B 1 676 ? 181.505 140.308 119.714 1.00 129.08 ? 676  CYS A O    1 
ATOM   8288 C CB   . CYS B 1 676 ? 179.834 141.660 122.217 1.00 126.47 ? 676  CYS A CB   1 
ATOM   8289 S SG   . CYS B 1 676 ? 178.365 142.227 123.090 1.00 129.99 ? 676  CYS A SG   1 
ATOM   8290 N N    . LEU B 1 677 ? 181.521 139.061 121.588 1.00 125.04 ? 677  LEU A N    1 
ATOM   8291 C CA   . LEU B 1 677 ? 182.833 138.484 121.307 1.00 126.02 ? 677  LEU A CA   1 
ATOM   8292 C C    . LEU B 1 677 ? 182.850 137.647 120.031 1.00 128.54 ? 677  LEU A C    1 
ATOM   8293 O O    . LEU B 1 677 ? 183.839 137.671 119.288 1.00 126.59 ? 677  LEU A O    1 
ATOM   8294 C CB   . LEU B 1 677 ? 183.257 137.639 122.511 1.00 124.83 ? 677  LEU A CB   1 
ATOM   8295 C CG   . LEU B 1 677 ? 184.716 137.320 122.818 1.00 124.73 ? 677  LEU A CG   1 
ATOM   8296 C CD1  . LEU B 1 677 ? 184.935 137.309 124.318 1.00 126.38 ? 677  LEU A CD1  1 
ATOM   8297 C CD2  . LEU B 1 677 ? 185.061 135.960 122.242 1.00 126.11 ? 677  LEU A CD2  1 
ATOM   8298 N N    . TRP B 1 678 ? 181.787 136.882 119.769 1.00 134.07 ? 678  TRP A N    1 
ATOM   8299 C CA   . TRP B 1 678 ? 181.773 136.011 118.594 1.00 130.89 ? 678  TRP A CA   1 
ATOM   8300 C C    . TRP B 1 678 ? 181.873 136.786 117.279 1.00 129.44 ? 678  TRP A C    1 
ATOM   8301 O O    . TRP B 1 678 ? 182.612 136.386 116.372 1.00 131.65 ? 678  TRP A O    1 
ATOM   8302 C CB   . TRP B 1 678 ? 180.502 135.160 118.600 1.00 129.05 ? 678  TRP A CB   1 
ATOM   8303 C CG   . TRP B 1 678 ? 180.611 133.882 117.822 1.00 129.94 ? 678  TRP A CG   1 
ATOM   8304 C CD1  . TRP B 1 678 ? 179.885 133.533 116.721 1.00 130.10 ? 678  TRP A CD1  1 
ATOM   8305 C CD2  . TRP B 1 678 ? 181.481 132.776 118.095 1.00 131.33 ? 678  TRP A CD2  1 
ATOM   8306 N NE1  . TRP B 1 678 ? 180.255 132.285 116.284 1.00 130.67 ? 678  TRP A NE1  1 
ATOM   8307 C CE2  . TRP B 1 678 ? 181.233 131.798 117.111 1.00 130.98 ? 678  TRP A CE2  1 
ATOM   8308 C CE3  . TRP B 1 678 ? 182.448 132.520 119.072 1.00 130.92 ? 678  TRP A CE3  1 
ATOM   8309 C CZ2  . TRP B 1 678 ? 181.915 130.584 117.076 1.00 130.29 ? 678  TRP A CZ2  1 
ATOM   8310 C CZ3  . TRP B 1 678 ? 183.125 131.314 119.035 1.00 131.46 ? 678  TRP A CZ3  1 
ATOM   8311 C CH2  . TRP B 1 678 ? 182.855 130.362 118.044 1.00 131.22 ? 678  TRP A CH2  1 
ATOM   8312 N N    . TRP B 1 679 ? 181.130 137.890 117.155 1.00 126.32 ? 679  TRP A N    1 
ATOM   8313 C CA   . TRP B 1 679 ? 181.117 138.664 115.912 1.00 126.79 ? 679  TRP A CA   1 
ATOM   8314 C C    . TRP B 1 679 ? 182.461 139.325 115.601 1.00 128.71 ? 679  TRP A C    1 
ATOM   8315 O O    . TRP B 1 679 ? 182.909 139.309 114.448 1.00 130.79 ? 679  TRP A O    1 
ATOM   8316 C CB   . TRP B 1 679 ? 179.997 139.706 115.966 1.00 125.26 ? 679  TRP A CB   1 
ATOM   8317 C CG   . TRP B 1 679 ? 179.905 140.587 114.747 1.00 127.79 ? 679  TRP A CG   1 
ATOM   8318 C CD1  . TRP B 1 679 ? 179.121 140.374 113.650 1.00 128.93 ? 679  TRP A CD1  1 
ATOM   8319 C CD2  . TRP B 1 679 ? 180.592 141.824 114.512 1.00 130.07 ? 679  TRP A CD2  1 
ATOM   8320 N NE1  . TRP B 1 679 ? 179.288 141.389 112.742 1.00 128.54 ? 679  TRP A NE1  1 
ATOM   8321 C CE2  . TRP B 1 679 ? 180.185 142.293 113.247 1.00 128.75 ? 679  TRP A CE2  1 
ATOM   8322 C CE3  . TRP B 1 679 ? 181.515 142.576 115.244 1.00 130.31 ? 679  TRP A CE3  1 
ATOM   8323 C CZ2  . TRP B 1 679 ? 180.668 143.478 112.699 1.00 127.85 ? 679  TRP A CZ2  1 
ATOM   8324 C CZ3  . TRP B 1 679 ? 181.996 143.752 114.697 1.00 129.26 ? 679  TRP A CZ3  1 
ATOM   8325 C CH2  . TRP B 1 679 ? 181.570 144.192 113.438 1.00 128.56 ? 679  TRP A CH2  1 
ATOM   8326 N N    . LEU B 1 680 ? 183.111 139.921 116.606 1.00 135.72 ? 680  LEU A N    1 
ATOM   8327 C CA   . LEU B 1 680 ? 184.332 140.696 116.368 1.00 137.00 ? 680  LEU A CA   1 
ATOM   8328 C C    . LEU B 1 680 ? 185.526 139.836 115.949 1.00 138.78 ? 680  LEU A C    1 
ATOM   8329 O O    . LEU B 1 680 ? 186.374 140.302 115.180 1.00 139.01 ? 680  LEU A O    1 
ATOM   8330 C CB   . LEU B 1 680 ? 184.664 141.555 117.591 1.00 138.26 ? 680  LEU A CB   1 
ATOM   8331 C CG   . LEU B 1 680 ? 185.119 140.983 118.928 1.00 140.70 ? 680  LEU A CG   1 
ATOM   8332 C CD1  . LEU B 1 680 ? 186.603 141.199 119.039 1.00 139.60 ? 680  LEU A CD1  1 
ATOM   8333 C CD2  . LEU B 1 680 ? 184.407 141.676 120.073 1.00 138.78 ? 680  LEU A CD2  1 
ATOM   8334 N N    . PHE B 1 681 ? 185.618 138.597 116.428 1.00 138.61 ? 681  PHE A N    1 
ATOM   8335 C CA   . PHE B 1 681 ? 186.788 137.753 116.186 1.00 139.00 ? 681  PHE A CA   1 
ATOM   8336 C C    . PHE B 1 681 ? 186.686 136.864 114.954 1.00 138.83 ? 681  PHE A C    1 
ATOM   8337 O O    . PHE B 1 681 ? 187.729 136.459 114.428 1.00 139.01 ? 681  PHE A O    1 
ATOM   8338 C CB   . PHE B 1 681 ? 187.120 136.871 117.395 1.00 137.41 ? 681  PHE A CB   1 
ATOM   8339 C CG   . PHE B 1 681 ? 187.653 137.623 118.582 1.00 138.60 ? 681  PHE A CG   1 
ATOM   8340 C CD1  . PHE B 1 681 ? 188.815 138.372 118.463 1.00 139.90 ? 681  PHE A CD1  1 
ATOM   8341 C CD2  . PHE B 1 681 ? 187.036 137.551 119.814 1.00 138.89 ? 681  PHE A CD2  1 
ATOM   8342 C CE1  . PHE B 1 681 ? 189.339 139.050 119.547 1.00 140.29 ? 681  PHE A CE1  1 
ATOM   8343 C CE2  . PHE B 1 681 ? 187.554 138.232 120.905 1.00 138.75 ? 681  PHE A CE2  1 
ATOM   8344 C CZ   . PHE B 1 681 ? 188.707 138.981 120.770 1.00 139.57 ? 681  PHE A CZ   1 
ATOM   8345 N N    . ASN B 1 682 ? 185.492 136.542 114.469 1.00 136.21 ? 682  ASN A N    1 
ATOM   8346 C CA   . ASN B 1 682 ? 185.377 135.670 113.303 1.00 136.18 ? 682  ASN A CA   1 
ATOM   8347 C C    . ASN B 1 682 ? 184.842 136.475 112.121 1.00 136.87 ? 682  ASN A C    1 
ATOM   8348 O O    . ASN B 1 682 ? 183.648 136.477 111.817 1.00 135.55 ? 682  ASN A O    1 
ATOM   8349 C CB   . ASN B 1 682 ? 184.481 134.468 113.618 1.00 137.41 ? 682  ASN A CB   1 
ATOM   8350 C CG   . ASN B 1 682 ? 185.085 133.551 114.663 1.00 136.81 ? 682  ASN A CG   1 
ATOM   8351 O OD1  . ASN B 1 682 ? 186.290 133.301 114.664 1.00 137.28 ? 682  ASN A OD1  1 
ATOM   8352 N ND2  . ASN B 1 682 ? 184.247 133.042 115.558 1.00 135.45 ? 682  ASN A ND2  1 
ATOM   8353 N N    . GLN B 1 683 ? 185.780 137.144 111.439 1.00 145.88 ? 683  GLN A N    1 
ATOM   8354 C CA   . GLN B 1 683 ? 185.597 138.001 110.269 1.00 147.21 ? 683  GLN A CA   1 
ATOM   8355 C C    . GLN B 1 683 ? 184.358 138.889 110.289 1.00 147.94 ? 683  GLN A C    1 
ATOM   8356 O O    . GLN B 1 683 ? 184.002 139.469 111.320 1.00 146.96 ? 683  GLN A O    1 
ATOM   8357 C CB   . GLN B 1 683 ? 185.572 137.135 109.006 1.00 145.72 ? 683  GLN A CB   1 
ATOM   8358 N N    . GLU B 1 684 ? 183.707 138.986 109.139 1.00 150.69 ? 684  GLU A N    1 
ATOM   8359 C CA   . GLU B 1 684 ? 182.511 139.742 108.823 1.00 149.98 ? 684  GLU A CA   1 
ATOM   8360 C C    . GLU B 1 684 ? 181.306 138.820 108.812 1.00 150.57 ? 684  GLU A C    1 
ATOM   8361 O O    . GLU B 1 684 ? 181.284 137.833 108.068 1.00 149.51 ? 684  GLU A O    1 
ATOM   8362 C CB   . GLU B 1 684 ? 182.653 140.429 107.461 1.00 147.09 ? 684  GLU A CB   1 
ATOM   8363 N N    . PRO B 1 685 ? 180.311 139.091 109.709 1.00 153.01 ? 685  PRO A N    1 
ATOM   8364 C CA   . PRO B 1 685 ? 179.042 138.334 109.759 1.00 151.33 ? 685  PRO A CA   1 
ATOM   8365 C C    . PRO B 1 685 ? 179.219 136.861 110.100 1.00 151.69 ? 685  PRO A C    1 
ATOM   8366 O O    . PRO B 1 685 ? 179.671 136.048 109.287 1.00 151.81 ? 685  PRO A O    1 
ATOM   8367 C CB   . PRO B 1 685 ? 178.419 138.551 108.368 1.00 149.69 ? 685  PRO A CB   1 
ATOM   8368 N N    . GLY B 1 686 ? 178.806 136.509 111.311 1.00 148.05 ? 686  GLY A N    1 
ATOM   8369 C CA   . GLY B 1 686 ? 178.943 135.162 111.815 1.00 147.22 ? 686  GLY A CA   1 
ATOM   8370 C C    . GLY B 1 686 ? 177.931 134.229 111.184 1.00 147.30 ? 686  GLY A C    1 
ATOM   8371 O O    . GLY B 1 686 ? 177.120 134.608 110.337 1.00 147.98 ? 686  GLY A O    1 
ATOM   8372 N N    . ARG B 1 687 ? 178.004 132.959 111.595 1.00 142.99 ? 687  ARG A N    1 
ATOM   8373 C CA   . ARG B 1 687 ? 177.084 131.962 111.060 1.00 143.47 ? 687  ARG A CA   1 
ATOM   8374 C C    . ARG B 1 687 ? 175.636 132.286 111.402 1.00 144.27 ? 687  ARG A C    1 
ATOM   8375 O O    . ARG B 1 687 ? 174.725 131.880 110.671 1.00 143.48 ? 687  ARG A O    1 
ATOM   8376 C CB   . ARG B 1 687 ? 177.454 130.573 111.583 1.00 143.33 ? 687  ARG A CB   1 
ATOM   8377 N N    . LEU B 1 688 ? 175.393 133.012 112.504 1.00 135.73 ? 688  LEU A N    1 
ATOM   8378 C CA   . LEU B 1 688 ? 174.034 133.440 112.831 1.00 134.94 ? 688  LEU A CA   1 
ATOM   8379 C C    . LEU B 1 688 ? 174.093 134.896 113.315 1.00 134.85 ? 688  LEU A C    1 
ATOM   8380 O O    . LEU B 1 688 ? 173.931 135.194 114.506 1.00 132.91 ? 688  LEU A O    1 
ATOM   8381 C CB   . LEU B 1 688 ? 173.419 132.510 113.871 1.00 131.46 ? 688  LEU A CB   1 
ATOM   8382 N N    . TYR B 1 689 ? 174.244 135.821 112.359 1.00 122.53 ? 689  TYR A N    1 
ATOM   8383 C CA   . TYR B 1 689 ? 174.189 137.244 112.685 1.00 119.76 ? 689  TYR A CA   1 
ATOM   8384 C C    . TYR B 1 689 ? 172.798 137.656 113.147 1.00 118.02 ? 689  TYR A C    1 
ATOM   8385 O O    . TYR B 1 689 ? 172.658 138.460 114.078 1.00 118.80 ? 689  TYR A O    1 
ATOM   8386 C CB   . TYR B 1 689 ? 174.621 138.074 111.476 1.00 118.77 ? 689  TYR A CB   1 
ATOM   8387 N N    . VAL B 1 690 ? 171.763 137.128 112.490 1.00 100.19 ? 690  VAL A N    1 
ATOM   8388 C CA   . VAL B 1 690 ? 170.385 137.440 112.856 1.00 98.02  ? 690  VAL A CA   1 
ATOM   8389 C C    . VAL B 1 690 ? 170.087 136.956 114.267 1.00 101.03 ? 690  VAL A C    1 
ATOM   8390 O O    . VAL B 1 690 ? 169.468 137.666 115.068 1.00 104.31 ? 690  VAL A O    1 
ATOM   8391 C CB   . VAL B 1 690 ? 169.410 136.838 111.828 1.00 99.64  ? 690  VAL A CB   1 
ATOM   8392 C CG1  . VAL B 1 690 ? 167.977 137.192 112.185 1.00 100.29 ? 690  VAL A CG1  1 
ATOM   8393 C CG2  . VAL B 1 690 ? 169.753 137.326 110.430 1.00 102.00 ? 690  VAL A CG2  1 
ATOM   8394 N N    . GLU B 1 691 ? 170.539 135.742 114.592 1.00 104.89 ? 691  GLU A N    1 
ATOM   8395 C CA   . GLU B 1 691 ? 170.383 135.200 115.939 1.00 106.79 ? 691  GLU A CA   1 
ATOM   8396 C C    . GLU B 1 691 ? 171.113 136.042 116.976 1.00 107.50 ? 691  GLU A C    1 
ATOM   8397 O O    . GLU B 1 691 ? 170.567 136.318 118.054 1.00 105.28 ? 691  GLU A O    1 
ATOM   8398 C CB   . GLU B 1 691 ? 170.901 133.765 115.972 1.00 104.89 ? 691  GLU A CB   1 
ATOM   8399 C CG   . GLU B 1 691 ? 169.926 132.711 115.489 1.00 105.52 ? 691  GLU A CG   1 
ATOM   8400 C CD   . GLU B 1 691 ? 169.560 132.844 114.020 1.00 107.79 ? 691  GLU A CD   1 
ATOM   8401 O OE1  . GLU B 1 691 ? 170.384 133.356 113.233 1.00 108.14 ? 691  GLU A OE1  1 
ATOM   8402 O OE2  . GLU B 1 691 ? 168.440 132.433 113.652 1.00 108.17 ? 691  GLU A OE2  1 
ATOM   8403 N N    . LEU B 1 692 ? 172.341 136.474 116.669 1.00 105.88 ? 692  LEU A N    1 
ATOM   8404 C CA   . LEU B 1 692 ? 173.073 137.293 117.630 1.00 105.37 ? 692  LEU A CA   1 
ATOM   8405 C C    . LEU B 1 692 ? 172.361 138.620 117.864 1.00 102.76 ? 692  LEU A C    1 
ATOM   8406 O O    . LEU B 1 692 ? 172.160 139.033 119.015 1.00 101.95 ? 692  LEU A O    1 
ATOM   8407 C CB   . LEU B 1 692 ? 174.502 137.524 117.141 1.00 104.02 ? 692  LEU A CB   1 
ATOM   8408 C CG   . LEU B 1 692 ? 175.446 136.324 117.218 1.00 104.93 ? 692  LEU A CG   1 
ATOM   8409 C CD1  . LEU B 1 692 ? 176.836 136.705 116.735 1.00 107.21 ? 692  LEU A CD1  1 
ATOM   8410 C CD2  . LEU B 1 692 ? 175.499 135.770 118.634 1.00 105.40 ? 692  LEU A CD2  1 
ATOM   8411 N N    . GLN B 1 693 ? 171.968 139.299 116.780 1.00 90.69  ? 693  GLN A N    1 
ATOM   8412 C CA   . GLN B 1 693 ? 171.296 140.588 116.915 1.00 90.10  ? 693  GLN A CA   1 
ATOM   8413 C C    . GLN B 1 693 ? 169.982 140.445 117.672 1.00 88.46  ? 693  GLN A C    1 
ATOM   8414 O O    . GLN B 1 693 ? 169.627 141.308 118.485 1.00 89.87  ? 693  GLN A O    1 
ATOM   8415 C CB   . GLN B 1 693 ? 171.057 141.207 115.538 1.00 92.28  ? 693  GLN A CB   1 
ATOM   8416 C CG   . GLN B 1 693 ? 172.211 142.055 115.027 1.00 90.93  ? 693  GLN A CG   1 
ATOM   8417 C CD   . GLN B 1 693 ? 172.144 142.291 113.531 1.00 91.67  ? 693  GLN A CD   1 
ATOM   8418 O OE1  . GLN B 1 693 ? 171.100 142.664 112.996 1.00 91.85  ? 693  GLN A OE1  1 
ATOM   8419 N NE2  . GLN B 1 693 ? 173.262 142.076 112.847 1.00 91.85  ? 693  GLN A NE2  1 
ATOM   8420 N N    . PHE B 1 694 ? 169.229 139.376 117.386 1.00 79.39  ? 694  PHE A N    1 
ATOM   8421 C CA   . PHE B 1 694 ? 168.007 139.095 118.128 1.00 82.11  ? 694  PHE A CA   1 
ATOM   8422 C C    . PHE B 1 694 ? 168.282 138.901 119.614 1.00 85.57  ? 694  PHE A C    1 
ATOM   8423 O O    . PHE B 1 694 ? 167.501 139.356 120.461 1.00 90.47  ? 694  PHE A O    1 
ATOM   8424 C CB   . PHE B 1 694 ? 167.342 137.852 117.532 1.00 82.97  ? 694  PHE A CB   1 
ATOM   8425 C CG   . PHE B 1 694 ? 166.021 137.496 118.149 1.00 80.34  ? 694  PHE A CG   1 
ATOM   8426 C CD1  . PHE B 1 694 ? 164.849 138.060 117.681 1.00 75.11  ? 694  PHE A CD1  1 
ATOM   8427 C CD2  . PHE B 1 694 ? 165.949 136.571 119.179 1.00 80.55  ? 694  PHE A CD2  1 
ATOM   8428 C CE1  . PHE B 1 694 ? 163.634 137.721 118.238 1.00 77.02  ? 694  PHE A CE1  1 
ATOM   8429 C CE2  . PHE B 1 694 ? 164.736 136.234 119.743 1.00 79.38  ? 694  PHE A CE2  1 
ATOM   8430 C CZ   . PHE B 1 694 ? 163.577 136.811 119.272 1.00 79.57  ? 694  PHE A CZ   1 
ATOM   8431 N N    . PHE B 1 695 ? 169.412 138.265 119.955 1.00 90.22  ? 695  PHE A N    1 
ATOM   8432 C CA   . PHE B 1 695 ? 169.748 138.120 121.369 1.00 92.17  ? 695  PHE A CA   1 
ATOM   8433 C C    . PHE B 1 695 ? 170.039 139.468 122.015 1.00 92.08  ? 695  PHE A C    1 
ATOM   8434 O O    . PHE B 1 695 ? 169.611 139.722 123.152 1.00 90.08  ? 695  PHE A O    1 
ATOM   8435 C CB   . PHE B 1 695 ? 170.932 137.168 121.541 1.00 91.59  ? 695  PHE A CB   1 
ATOM   8436 C CG   . PHE B 1 695 ? 170.541 135.716 121.611 1.00 91.00  ? 695  PHE A CG   1 
ATOM   8437 C CD1  . PHE B 1 695 ? 169.382 135.260 121.003 1.00 90.16  ? 695  PHE A CD1  1 
ATOM   8438 C CD2  . PHE B 1 695 ? 171.333 134.809 122.296 1.00 92.26  ? 695  PHE A CD2  1 
ATOM   8439 C CE1  . PHE B 1 695 ? 169.022 133.927 121.072 1.00 93.88  ? 695  PHE A CE1  1 
ATOM   8440 C CE2  . PHE B 1 695 ? 170.979 133.473 122.368 1.00 93.47  ? 695  PHE A CE2  1 
ATOM   8441 C CZ   . PHE B 1 695 ? 169.823 133.032 121.755 1.00 93.79  ? 695  PHE A CZ   1 
ATOM   8442 N N    . CYS B 1 696 ? 170.770 140.342 121.312 1.00 87.21  ? 696  CYS A N    1 
ATOM   8443 C CA   . CYS B 1 696 ? 171.043 141.660 121.883 1.00 86.26  ? 696  CYS A CA   1 
ATOM   8444 C C    . CYS B 1 696 ? 169.754 142.447 122.072 1.00 83.73  ? 696  CYS A C    1 
ATOM   8445 O O    . CYS B 1 696 ? 169.572 143.115 123.093 1.00 86.01  ? 696  CYS A O    1 
ATOM   8446 C CB   . CYS B 1 696 ? 172.032 142.470 121.037 1.00 88.58  ? 696  CYS A CB   1 
ATOM   8447 S SG   . CYS B 1 696 ? 173.312 141.589 120.136 1.00 88.32  ? 696  CYS A SG   1 
ATOM   8448 N N    . ALA B 1 697 ? 168.854 142.384 121.088 1.00 72.26  ? 697  ALA A N    1 
ATOM   8449 C CA   . ALA B 1 697 ? 167.574 143.081 121.181 1.00 71.67  ? 697  ALA A CA   1 
ATOM   8450 C C    . ALA B 1 697 ? 166.726 142.592 122.352 1.00 73.03  ? 697  ALA A C    1 
ATOM   8451 O O    . ALA B 1 697 ? 166.154 143.405 123.094 1.00 79.60  ? 697  ALA A O    1 
ATOM   8452 C CB   . ALA B 1 697 ? 166.804 142.934 119.870 1.00 73.55  ? 697  ALA A CB   1 
ATOM   8453 N N    . VAL B 1 698 ? 166.671 141.272 122.564 1.00 70.74  ? 698  VAL A N    1 
ATOM   8454 C CA   . VAL B 1 698 ? 165.916 140.736 123.698 1.00 70.75  ? 698  VAL A CA   1 
ATOM   8455 C C    . VAL B 1 698 ? 166.544 141.139 125.029 1.00 76.53  ? 698  VAL A C    1 
ATOM   8456 O O    . VAL B 1 698 ? 165.837 141.556 125.954 1.00 77.24  ? 698  VAL A O    1 
ATOM   8457 C CB   . VAL B 1 698 ? 165.774 139.208 123.574 1.00 69.79  ? 698  VAL A CB   1 
ATOM   8458 C CG1  . VAL B 1 698 ? 165.100 138.634 124.807 1.00 73.11  ? 698  VAL A CG1  1 
ATOM   8459 C CG2  . VAL B 1 698 ? 164.956 138.861 122.346 1.00 69.81  ? 698  VAL A CG2  1 
ATOM   8460 N N    . PHE B 1 699 ? 167.870 141.044 125.157 1.00 84.20  ? 699  PHE A N    1 
ATOM   8461 C CA   . PHE B 1 699 ? 168.442 141.361 126.463 1.00 80.29  ? 699  PHE A CA   1 
ATOM   8462 C C    . PHE B 1 699 ? 168.549 142.864 126.702 1.00 75.28  ? 699  PHE A C    1 
ATOM   8463 O O    . PHE B 1 699 ? 168.641 143.300 127.855 1.00 73.59  ? 699  PHE A O    1 
ATOM   8464 C CB   . PHE B 1 699 ? 169.818 140.714 126.648 1.00 84.67  ? 699  PHE A CB   1 
ATOM   8465 C CG   . PHE B 1 699 ? 170.470 141.075 127.954 1.00 83.75  ? 699  PHE A CG   1 
ATOM   8466 C CD1  . PHE B 1 699 ? 169.844 140.775 129.154 1.00 83.26  ? 699  PHE A CD1  1 
ATOM   8467 C CD2  . PHE B 1 699 ? 171.667 141.766 127.985 1.00 84.97  ? 699  PHE A CD2  1 
ATOM   8468 C CE1  . PHE B 1 699 ? 170.415 141.132 130.357 1.00 86.00  ? 699  PHE A CE1  1 
ATOM   8469 C CE2  . PHE B 1 699 ? 172.248 142.120 129.188 1.00 84.17  ? 699  PHE A CE2  1 
ATOM   8470 C CZ   . PHE B 1 699 ? 171.619 141.804 130.375 1.00 83.90  ? 699  PHE A CZ   1 
ATOM   8471 N N    . ASN B 1 700 ? 168.440 143.670 125.655 1.00 72.69  ? 700  ASN A N    1 
ATOM   8472 C CA   . ASN B 1 700 ? 168.480 145.115 125.806 1.00 73.14  ? 700  ASN A CA   1 
ATOM   8473 C C    . ASN B 1 700 ? 167.115 145.707 126.112 1.00 69.75  ? 700  ASN A C    1 
ATOM   8474 O O    . ASN B 1 700 ? 167.005 146.564 126.995 1.00 70.91  ? 700  ASN A O    1 
ATOM   8475 C CB   . ASN B 1 700 ? 169.058 145.762 124.545 1.00 69.87  ? 700  ASN A CB   1 
ATOM   8476 C CG   . ASN B 1 700 ? 170.571 145.691 124.498 1.00 71.77  ? 700  ASN A CG   1 
ATOM   8477 O OD1  . ASN B 1 700 ? 171.226 145.478 125.517 1.00 75.64  ? 700  ASN A OD1  1 
ATOM   8478 N ND2  . ASN B 1 700 ? 171.134 145.869 123.309 1.00 70.20  ? 700  ASN A ND2  1 
ATOM   8479 N N    . PHE B 1 701 ? 166.065 145.288 125.408 1.00 56.78  ? 701  PHE A N    1 
ATOM   8480 C CA   . PHE B 1 701 ? 164.776 145.923 125.632 1.00 51.94  ? 701  PHE A CA   1 
ATOM   8481 C C    . PHE B 1 701 ? 163.876 145.185 126.618 1.00 59.67  ? 701  PHE A C    1 
ATOM   8482 O O    . PHE B 1 701 ? 162.824 145.722 126.976 1.00 65.17  ? 701  PHE A O    1 
ATOM   8483 C CB   . PHE B 1 701 ? 164.054 146.074 124.288 1.00 55.01  ? 701  PHE A CB   1 
ATOM   8484 C CG   . PHE B 1 701 ? 164.813 146.900 123.283 1.00 62.45  ? 701  PHE A CG   1 
ATOM   8485 C CD1  . PHE B 1 701 ? 165.781 147.810 123.686 1.00 64.51  ? 701  PHE A CD1  1 
ATOM   8486 C CD2  . PHE B 1 701 ? 164.624 146.697 121.929 1.00 67.84  ? 701  PHE A CD2  1 
ATOM   8487 C CE1  . PHE B 1 701 ? 166.493 148.543 122.762 1.00 66.33  ? 701  PHE A CE1  1 
ATOM   8488 C CE2  . PHE B 1 701 ? 165.345 147.419 121.001 1.00 67.83  ? 701  PHE A CE2  1 
ATOM   8489 C CZ   . PHE B 1 701 ? 166.277 148.347 121.419 1.00 64.07  ? 701  PHE A CZ   1 
ATOM   8490 N N    . GLY B 1 702 ? 164.240 143.983 127.066 1.00 62.35  ? 702  GLY A N    1 
ATOM   8491 C CA   . GLY B 1 702 ? 163.397 143.274 128.008 1.00 59.36  ? 702  GLY A CA   1 
ATOM   8492 C C    . GLY B 1 702 ? 163.797 143.348 129.470 1.00 61.89  ? 702  GLY A C    1 
ATOM   8493 O O    . GLY B 1 702 ? 163.131 142.730 130.307 1.00 66.51  ? 702  GLY A O    1 
ATOM   8494 N N    . GLN B 1 703 ? 164.869 144.075 129.800 1.00 54.98  ? 703  GLN A N    1 
ATOM   8495 C CA   . GLN B 1 703 ? 165.351 144.181 131.178 1.00 47.10  ? 703  GLN A CA   1 
ATOM   8496 C C    . GLN B 1 703 ? 164.328 144.814 132.119 1.00 53.13  ? 703  GLN A C    1 
ATOM   8497 O O    . GLN B 1 703 ? 164.252 144.443 133.303 1.00 63.59  ? 703  GLN A O    1 
ATOM   8498 C CB   . GLN B 1 703 ? 166.681 144.934 131.201 1.00 48.76  ? 703  GLN A CB   1 
ATOM   8499 C CG   . GLN B 1 703 ? 166.668 146.304 130.562 1.00 51.17  ? 703  GLN A CG   1 
ATOM   8500 C CD   . GLN B 1 703 ? 168.030 146.961 130.621 1.00 58.24  ? 703  GLN A CD   1 
ATOM   8501 O OE1  . GLN B 1 703 ? 168.930 146.479 131.306 1.00 62.91  ? 703  GLN A OE1  1 
ATOM   8502 N NE2  . GLN B 1 703 ? 168.194 148.059 129.893 1.00 58.12  ? 703  GLN A NE2  1 
ATOM   8503 N N    . GLY B 1 704 ? 163.543 145.767 131.612 1.00 53.09  ? 704  GLY A N    1 
ATOM   8504 C CA   . GLY B 1 704 ? 162.502 146.383 132.420 1.00 53.92  ? 704  GLY A CA   1 
ATOM   8505 C C    . GLY B 1 704 ? 161.471 145.401 132.937 1.00 50.19  ? 704  GLY A C    1 
ATOM   8506 O O    . GLY B 1 704 ? 160.987 145.539 134.061 1.00 56.91  ? 704  GLY A O    1 
ATOM   8507 N N    . PHE B 1 705 ? 161.099 144.416 132.117 1.00 42.70  ? 705  PHE A N    1 
ATOM   8508 C CA   . PHE B 1 705 ? 160.149 143.399 132.561 1.00 45.55  ? 705  PHE A CA   1 
ATOM   8509 C C    . PHE B 1 705 ? 160.702 142.621 133.754 1.00 46.93  ? 705  PHE A C    1 
ATOM   8510 O O    . PHE B 1 705 ? 159.983 142.364 134.732 1.00 50.68  ? 705  PHE A O    1 
ATOM   8511 C CB   . PHE B 1 705 ? 159.826 142.461 131.400 1.00 46.99  ? 705  PHE A CB   1 
ATOM   8512 C CG   . PHE B 1 705 ? 158.468 141.839 131.481 1.00 48.72  ? 705  PHE A CG   1 
ATOM   8513 C CD1  . PHE B 1 705 ? 157.415 142.514 132.076 1.00 47.57  ? 705  PHE A CD1  1 
ATOM   8514 C CD2  . PHE B 1 705 ? 158.239 140.583 130.951 1.00 53.48  ? 705  PHE A CD2  1 
ATOM   8515 C CE1  . PHE B 1 705 ? 156.161 141.943 132.145 1.00 51.64  ? 705  PHE A CE1  1 
ATOM   8516 C CE2  . PHE B 1 705 ? 156.989 140.005 131.018 1.00 50.39  ? 705  PHE A CE2  1 
ATOM   8517 C CZ   . PHE B 1 705 ? 155.949 140.685 131.615 1.00 50.45  ? 705  PHE A CZ   1 
ATOM   8518 N N    . ILE B 1 706 ? 161.988 142.262 133.693 1.00 47.44  ? 706  ILE A N    1 
ATOM   8519 C CA   . ILE B 1 706 ? 162.631 141.519 134.775 1.00 47.19  ? 706  ILE A CA   1 
ATOM   8520 C C    . ILE B 1 706 ? 162.654 142.361 136.044 1.00 48.91  ? 706  ILE A C    1 
ATOM   8521 O O    . ILE B 1 706 ? 162.364 141.866 137.141 1.00 51.02  ? 706  ILE A O    1 
ATOM   8522 C CB   . ILE B 1 706 ? 164.044 141.075 134.345 1.00 47.28  ? 706  ILE A CB   1 
ATOM   8523 C CG1  . ILE B 1 706 ? 163.972 139.767 133.557 1.00 46.68  ? 706  ILE A CG1  1 
ATOM   8524 C CG2  . ILE B 1 706 ? 164.965 140.901 135.547 1.00 46.03  ? 706  ILE A CG2  1 
ATOM   8525 C CD1  . ILE B 1 706 ? 165.151 139.545 132.638 1.00 47.36  ? 706  ILE A CD1  1 
ATOM   8526 N N    . SER B 1 707 ? 163.002 143.645 135.915 1.00 53.43  ? 707  SER A N    1 
ATOM   8527 C CA   . SER B 1 707 ? 163.026 144.528 137.081 1.00 52.33  ? 707  SER A CA   1 
ATOM   8528 C C    . SER B 1 707 ? 161.627 144.677 137.680 1.00 56.50  ? 707  SER A C    1 
ATOM   8529 O O    . SER B 1 707 ? 161.465 144.707 138.911 1.00 58.42  ? 707  SER A O    1 
ATOM   8530 C CB   . SER B 1 707 ? 163.613 145.886 136.707 1.00 46.78  ? 707  SER A CB   1 
ATOM   8531 O OG   . SER B 1 707 ? 164.151 146.509 137.857 1.00 50.84  ? 707  SER A OG   1 
ATOM   8532 N N    . PHE B 1 708 ? 160.617 144.825 136.813 1.00 50.80  ? 708  PHE A N    1 
ATOM   8533 C CA   . PHE B 1 708 ? 159.232 145.018 137.233 1.00 41.15  ? 708  PHE A CA   1 
ATOM   8534 C C    . PHE B 1 708 ? 158.758 143.819 138.036 1.00 46.96  ? 708  PHE A C    1 
ATOM   8535 O O    . PHE B 1 708 ? 158.098 143.980 139.068 1.00 56.49  ? 708  PHE A O    1 
ATOM   8536 C CB   . PHE B 1 708 ? 158.340 145.219 136.002 1.00 47.30  ? 708  PHE A CB   1 
ATOM   8537 C CG   . PHE B 1 708 ? 156.910 144.724 136.163 1.00 48.95  ? 708  PHE A CG   1 
ATOM   8538 C CD1  . PHE B 1 708 ? 156.067 145.237 137.148 1.00 53.44  ? 708  PHE A CD1  1 
ATOM   8539 C CD2  . PHE B 1 708 ? 156.433 143.701 135.360 1.00 50.73  ? 708  PHE A CD2  1 
ATOM   8540 C CE1  . PHE B 1 708 ? 154.775 144.768 137.290 1.00 51.83  ? 708  PHE A CE1  1 
ATOM   8541 C CE2  . PHE B 1 708 ? 155.141 143.228 135.502 1.00 48.22  ? 708  PHE A CE2  1 
ATOM   8542 C CZ   . PHE B 1 708 ? 154.313 143.761 136.468 1.00 48.50  ? 708  PHE A CZ   1 
ATOM   8543 N N    . GLY B 1 709 ? 159.087 142.611 137.572 1.00 61.05  ? 709  GLY A N    1 
ATOM   8544 C CA   . GLY B 1 709 ? 158.628 141.406 138.250 1.00 64.32  ? 709  GLY A CA   1 
ATOM   8545 C C    . GLY B 1 709 ? 159.046 141.362 139.709 1.00 63.60  ? 709  GLY A C    1 
ATOM   8546 O O    . GLY B 1 709 ? 158.259 140.978 140.576 1.00 62.30  ? 709  GLY A O    1 
ATOM   8547 N N    . ILE B 1 710 ? 160.280 141.763 140.001 1.00 62.22  ? 710  ILE A N    1 
ATOM   8548 C CA   . ILE B 1 710 ? 160.772 141.739 141.376 1.00 60.80  ? 710  ILE A CA   1 
ATOM   8549 C C    . ILE B 1 710 ? 160.246 142.933 142.170 1.00 63.88  ? 710  ILE A C    1 
ATOM   8550 O O    . ILE B 1 710 ? 159.641 142.767 143.236 1.00 67.78  ? 710  ILE A O    1 
ATOM   8551 C CB   . ILE B 1 710 ? 162.312 141.696 141.401 1.00 64.14  ? 710  ILE A CB   1 
ATOM   8552 C CG1  . ILE B 1 710 ? 162.849 140.797 140.287 1.00 65.53  ? 710  ILE A CG1  1 
ATOM   8553 C CG2  . ILE B 1 710 ? 162.815 141.264 142.775 1.00 66.44  ? 710  ILE A CG2  1 
ATOM   8554 C CD1  . ILE B 1 710 ? 162.501 139.336 140.456 1.00 65.87  ? 710  ILE A CD1  1 
ATOM   8555 N N    . PHE B 1 711 ? 160.462 144.151 141.670 1.00 69.83  ? 711  PHE A N    1 
ATOM   8556 C CA   . PHE B 1 711 ? 160.170 145.348 142.462 1.00 69.34  ? 711  PHE A CA   1 
ATOM   8557 C C    . PHE B 1 711 ? 158.721 145.831 142.403 1.00 69.04  ? 711  PHE A C    1 
ATOM   8558 O O    . PHE B 1 711 ? 158.145 146.162 143.445 1.00 70.20  ? 711  PHE A O    1 
ATOM   8559 C CB   . PHE B 1 711 ? 161.128 146.481 142.088 1.00 70.99  ? 711  PHE A CB   1 
ATOM   8560 C CG   . PHE B 1 711 ? 162.393 146.467 142.895 1.00 74.27  ? 711  PHE A CG   1 
ATOM   8561 C CD1  . PHE B 1 711 ? 162.946 145.263 143.301 1.00 71.03  ? 711  PHE A CD1  1 
ATOM   8562 C CD2  . PHE B 1 711 ? 162.992 147.644 143.307 1.00 74.97  ? 711  PHE A CD2  1 
ATOM   8563 C CE1  . PHE B 1 711 ? 164.094 145.230 144.063 1.00 72.75  ? 711  PHE A CE1  1 
ATOM   8564 C CE2  . PHE B 1 711 ? 164.140 147.614 144.076 1.00 72.84  ? 711  PHE A CE2  1 
ATOM   8565 C CZ   . PHE B 1 711 ? 164.691 146.405 144.451 1.00 73.81  ? 711  PHE A CZ   1 
ATOM   8566 N N    . GLY B 1 712 ? 158.124 145.896 141.213 1.00 59.54  ? 712  GLY A N    1 
ATOM   8567 C CA   . GLY B 1 712 ? 156.810 146.509 141.075 1.00 60.46  ? 712  GLY A CA   1 
ATOM   8568 C C    . GLY B 1 712 ? 155.708 145.733 141.773 1.00 61.77  ? 712  GLY A C    1 
ATOM   8569 O O    . GLY B 1 712 ? 154.869 146.320 142.461 1.00 64.39  ? 712  GLY A O    1 
ATOM   8570 N N    . LEU B 1 713 ? 155.688 144.412 141.610 1.00 57.96  ? 713  LEU A N    1 
ATOM   8571 C CA   . LEU B 1 713 ? 154.625 143.592 142.187 1.00 58.97  ? 713  LEU A CA   1 
ATOM   8572 C C    . LEU B 1 713 ? 154.967 143.252 143.640 1.00 62.27  ? 713  LEU A C    1 
ATOM   8573 O O    . LEU B 1 713 ? 155.164 142.100 144.022 1.00 63.60  ? 713  LEU A O    1 
ATOM   8574 C CB   . LEU B 1 713 ? 154.446 142.333 141.354 1.00 55.57  ? 713  LEU A CB   1 
ATOM   8575 C CG   . LEU B 1 713 ? 153.474 142.407 140.186 1.00 59.50  ? 713  LEU A CG   1 
ATOM   8576 C CD1  . LEU B 1 713 ? 153.507 141.087 139.461 1.00 54.32  ? 713  LEU A CD1  1 
ATOM   8577 C CD2  . LEU B 1 713 ? 152.076 142.734 140.674 1.00 61.17  ? 713  LEU A CD2  1 
ATOM   8578 N N    . ASP B 1 714 ? 155.032 144.308 144.452 1.00 75.30  ? 714  ASP A N    1 
ATOM   8579 C CA   . ASP B 1 714 ? 155.331 144.239 145.876 1.00 75.25  ? 714  ASP A CA   1 
ATOM   8580 C C    . ASP B 1 714 ? 154.334 145.090 146.650 1.00 77.87  ? 714  ASP A C    1 
ATOM   8581 O O    . ASP B 1 714 ? 153.831 146.097 146.145 1.00 78.73  ? 714  ASP A O    1 
ATOM   8582 C CB   . ASP B 1 714 ? 156.767 144.713 146.178 1.00 73.81  ? 714  ASP A CB   1 
ATOM   8583 C CG   . ASP B 1 714 ? 157.280 144.228 147.532 1.00 77.17  ? 714  ASP A CG   1 
ATOM   8584 O OD1  . ASP B 1 714 ? 156.554 144.348 148.543 1.00 75.93  ? 714  ASP A OD1  1 
ATOM   8585 O OD2  . ASP B 1 714 ? 158.417 143.715 147.583 1.00 81.45  ? 714  ASP A OD2  1 
ATOM   8586 N N    . LYS B 1 715 ? 154.051 144.673 147.883 1.00 82.46  ? 715  LYS A N    1 
ATOM   8587 C CA   . LYS B 1 715 ? 153.103 145.390 148.725 1.00 79.92  ? 715  LYS A CA   1 
ATOM   8588 C C    . LYS B 1 715 ? 153.812 146.539 149.431 1.00 82.11  ? 715  LYS A C    1 
ATOM   8589 O O    . LYS B 1 715 ? 154.794 146.328 150.150 1.00 80.96  ? 715  LYS A O    1 
ATOM   8590 C CB   . LYS B 1 715 ? 152.476 144.461 149.765 1.00 80.35  ? 715  LYS A CB   1 
ATOM   8591 C CG   . LYS B 1 715 ? 151.969 143.139 149.229 1.00 83.04  ? 715  LYS A CG   1 
ATOM   8592 C CD   . LYS B 1 715 ? 150.878 142.574 150.128 1.00 83.87  ? 715  LYS A CD   1 
ATOM   8593 C CE   . LYS B 1 715 ? 150.924 141.057 150.168 1.00 83.27  ? 715  LYS A CE   1 
ATOM   8594 N NZ   . LYS B 1 715 ? 150.260 140.448 148.982 1.00 81.12  ? 715  LYS A NZ   1 
ATOM   8595 N N    . HIS B 1 716 ? 153.308 147.753 149.225 1.00 98.13  ? 716  HIS A N    1 
ATOM   8596 C CA   . HIS B 1 716 ? 153.860 148.939 149.869 1.00 98.66  ? 716  HIS A CA   1 
ATOM   8597 C C    . HIS B 1 716 ? 152.725 149.902 150.169 1.00 99.48  ? 716  HIS A C    1 
ATOM   8598 O O    . HIS B 1 716 ? 152.077 150.397 149.240 1.00 100.36 ? 716  HIS A O    1 
ATOM   8599 C CB   . HIS B 1 716 ? 154.911 149.614 148.987 1.00 96.84  ? 716  HIS A CB   1 
ATOM   8600 C CG   . HIS B 1 716 ? 156.295 149.077 149.170 1.00 98.47  ? 716  HIS A CG   1 
ATOM   8601 N ND1  . HIS B 1 716 ? 157.204 149.002 148.137 1.00 100.10 ? 716  HIS A ND1  1 
ATOM   8602 C CD2  . HIS B 1 716 ? 156.931 148.599 150.266 1.00 98.65  ? 716  HIS A CD2  1 
ATOM   8603 C CE1  . HIS B 1 716 ? 158.339 148.497 148.587 1.00 98.65  ? 716  HIS A CE1  1 
ATOM   8604 N NE2  . HIS B 1 716 ? 158.199 148.244 149.876 1.00 99.20  ? 716  HIS A NE2  1 
ATOM   8605 N N    . LEU B 1 717 ? 152.473 150.129 151.458 1.00 101.09 ? 717  LEU A N    1 
ATOM   8606 C CA   . LEU B 1 717 ? 151.407 151.023 151.896 1.00 101.48 ? 717  LEU A CA   1 
ATOM   8607 C C    . LEU B 1 717 ? 151.600 152.426 151.327 1.00 103.27 ? 717  LEU A C    1 
ATOM   8608 O O    . LEU B 1 717 ? 152.694 152.995 151.391 1.00 102.19 ? 717  LEU A O    1 
ATOM   8609 C CB   . LEU B 1 717 ? 151.339 151.061 153.429 1.00 101.69 ? 717  LEU A CB   1 
ATOM   8610 C CG   . LEU B 1 717 ? 152.408 151.750 154.292 1.00 102.29 ? 717  LEU A CG   1 
ATOM   8611 C CD1  . LEU B 1 717 ? 151.853 152.083 155.667 1.00 101.11 ? 717  LEU A CD1  1 
ATOM   8612 C CD2  . LEU B 1 717 ? 153.666 150.901 154.437 1.00 99.98  ? 717  LEU A CD2  1 
ATOM   8613 N N    . ILE B 1 718 ? 150.538 152.969 150.742 1.00 103.71 ? 718  ILE A N    1 
ATOM   8614 C CA   . ILE B 1 718 ? 150.586 154.299 150.152 1.00 103.90 ? 718  ILE A CA   1 
ATOM   8615 C C    . ILE B 1 718 ? 150.472 155.358 151.241 1.00 104.68 ? 718  ILE A C    1 
ATOM   8616 O O    . ILE B 1 718 ? 151.457 155.698 151.894 1.00 103.71 ? 718  ILE A O    1 
ATOM   8617 C CB   . ILE B 1 718 ? 149.482 154.483 149.098 1.00 101.47 ? 718  ILE A CB   1 
ATOM   8618 C CG1  . ILE B 1 718 ? 149.425 153.272 148.164 1.00 101.50 ? 718  ILE A CG1  1 
ATOM   8619 C CG2  . ILE B 1 718 ? 149.711 155.760 148.305 1.00 101.11 ? 718  ILE A CG2  1 
ATOM   8620 C CD1  . ILE B 1 718 ? 150.698 153.041 147.376 1.00 102.47 ? 718  ILE A CD1  1 
HETATM 8621 N N    . POV C 2 .   ? 121.385 115.380 148.371 1.00 80.89  ? 1101 POV B N    1 
HETATM 8622 P P    . POV C 2 .   ? 116.765 117.403 147.517 1.00 98.95  ? 1101 POV B P    1 
HETATM 8623 C C1   . POV C 2 .   ? 116.602 116.496 145.042 1.00 79.97  ? 1101 POV B C1   1 
HETATM 8624 C C2   . POV C 2 .   ? 117.278 116.605 143.669 1.00 75.68  ? 1101 POV B C2   1 
HETATM 8625 C C3   . POV C 2 .   ? 118.741 116.232 143.695 1.00 78.09  ? 1101 POV B C3   1 
HETATM 8626 C C210 . POV C 2 .   ? 112.545 119.341 133.141 1.00 80.85  ? 1101 POV B C210 1 
HETATM 8627 C C310 . POV C 2 .   ? 116.790 116.492 131.932 1.00 78.83  ? 1101 POV B C310 1 
HETATM 8628 C C11  . POV C 2 .   ? 119.300 116.682 147.527 1.00 79.41  ? 1101 POV B C11  1 
HETATM 8629 O O11  . POV C 2 .   ? 117.293 117.290 145.982 1.00 87.33  ? 1101 POV B O11  1 
HETATM 8630 C C211 . POV C 2 .   ? 112.852 118.625 131.864 1.00 79.38  ? 1101 POV B C211 1 
HETATM 8631 C C311 . POV C 2 .   ? 117.294 115.483 130.909 1.00 77.76  ? 1101 POV B C311 1 
HETATM 8632 C C12  . POV C 2 .   ? 119.956 115.367 147.889 1.00 79.15  ? 1101 POV B C12  1 
HETATM 8633 O O12  . POV C 2 .   ? 118.154 116.947 148.300 1.00 81.37  ? 1101 POV B O12  1 
HETATM 8634 C C212 . POV C 2 .   ? 112.207 119.309 130.658 1.00 81.39  ? 1101 POV B C212 1 
HETATM 8635 C C312 . POV C 2 .   ? 116.210 115.032 129.939 1.00 78.94  ? 1101 POV B C312 1 
HETATM 8636 C C13  . POV C 2 .   ? 121.709 114.140 149.129 1.00 80.48  ? 1101 POV B C13  1 
HETATM 8637 O O13  . POV C 2 .   ? 116.534 118.857 147.796 1.00 86.27  ? 1101 POV B O13  1 
HETATM 8638 C C213 . POV C 2 .   ? 113.087 120.385 130.033 1.00 80.54  ? 1101 POV B C213 1 
HETATM 8639 C C313 . POV C 2 .   ? 116.712 114.087 128.856 1.00 81.51  ? 1101 POV B C313 1 
HETATM 8640 C C14  . POV C 2 .   ? 122.252 115.437 147.162 1.00 77.87  ? 1101 POV B C14  1 
HETATM 8641 O O14  . POV C 2 .   ? 115.700 116.391 147.798 1.00 79.00  ? 1101 POV B O14  1 
HETATM 8642 C C214 . POV C 2 .   ? 114.264 119.812 129.253 1.00 75.68  ? 1101 POV B C214 1 
HETATM 8643 C C314 . POV C 2 .   ? 117.442 114.810 127.732 1.00 78.59  ? 1101 POV B C314 1 
HETATM 8644 C C15  . POV C 2 .   ? 121.690 116.570 149.218 1.00 77.72  ? 1101 POV B C15  1 
HETATM 8645 C C215 . POV C 2 .   ? 113.854 118.800 128.189 1.00 76.16  ? 1101 POV B C215 1 
HETATM 8646 C C315 . POV C 2 .   ? 118.175 113.878 126.775 1.00 76.27  ? 1101 POV B C315 1 
HETATM 8647 C C216 . POV C 2 .   ? 115.005 118.363 127.293 1.00 77.94  ? 1101 POV B C216 1 
HETATM 8648 C C316 . POV C 2 .   ? 117.261 112.835 126.149 1.00 79.15  ? 1101 POV B C316 1 
HETATM 8649 C C217 . POV C 2 .   ? 114.588 117.367 126.218 1.00 78.30  ? 1101 POV B C217 1 
HETATM 8650 C C218 . POV C 2 .   ? 115.718 117.012 125.262 1.00 76.69  ? 1101 POV B C218 1 
HETATM 8651 C C21  . POV C 2 .   ? 116.083 118.369 142.565 1.00 76.44  ? 1101 POV B C21  1 
HETATM 8652 O O21  . POV C 2 .   ? 117.209 117.925 143.122 1.00 74.46  ? 1101 POV B O21  1 
HETATM 8653 C C22  . POV C 2 .   ? 116.172 118.375 141.063 1.00 78.41  ? 1101 POV B C22  1 
HETATM 8654 O O22  . POV C 2 .   ? 115.121 118.726 143.197 1.00 75.30  ? 1101 POV B O22  1 
HETATM 8655 C C23  . POV C 2 .   ? 114.880 118.800 140.384 1.00 79.37  ? 1101 POV B C23  1 
HETATM 8656 C C24  . POV C 2 .   ? 115.072 119.091 138.901 1.00 75.74  ? 1101 POV B C24  1 
HETATM 8657 C C25  . POV C 2 .   ? 114.798 117.890 138.004 1.00 76.67  ? 1101 POV B C25  1 
HETATM 8658 C C26  . POV C 2 .   ? 113.714 118.153 136.966 1.00 72.60  ? 1101 POV B C26  1 
HETATM 8659 C C27  . POV C 2 .   ? 113.799 117.225 135.762 1.00 76.07  ? 1101 POV B C27  1 
HETATM 8660 C C28  . POV C 2 .   ? 112.636 117.399 134.784 1.00 80.27  ? 1101 POV B C28  1 
HETATM 8661 C C29  . POV C 2 .   ? 112.453 118.825 134.367 1.00 82.04  ? 1101 POV B C29  1 
HETATM 8662 C C31  . POV C 2 .   ? 119.506 115.164 141.731 1.00 79.93  ? 1101 POV B C31  1 
HETATM 8663 O O31  . POV C 2 .   ? 119.231 116.297 142.362 1.00 78.37  ? 1101 POV B O31  1 
HETATM 8664 C C32  . POV C 2 .   ? 119.847 115.428 140.293 1.00 76.60  ? 1101 POV B C32  1 
HETATM 8665 O O32  . POV C 2 .   ? 119.481 114.081 142.261 1.00 85.94  ? 1101 POV B O32  1 
HETATM 8666 C C33  . POV C 2 .   ? 119.127 114.542 139.293 1.00 77.00  ? 1101 POV B C33  1 
HETATM 8667 C C34  . POV C 2 .   ? 119.729 114.705 137.904 1.00 81.10  ? 1101 POV B C34  1 
HETATM 8668 C C35  . POV C 2 .   ? 118.978 113.966 136.808 1.00 82.08  ? 1101 POV B C35  1 
HETATM 8669 C C36  . POV C 2 .   ? 118.028 114.874 136.036 1.00 77.95  ? 1101 POV B C36  1 
HETATM 8670 C C37  . POV C 2 .   ? 117.320 114.171 134.885 1.00 78.48  ? 1101 POV B C37  1 
HETATM 8671 C C38  . POV C 2 .   ? 116.482 115.115 134.031 1.00 78.43  ? 1101 POV B C38  1 
HETATM 8672 C C39  . POV C 2 .   ? 117.284 116.215 133.346 1.00 81.56  ? 1101 POV B C39  1 
HETATM 8673 O O1   . IOS D 3 .   ? 122.319 141.377 132.728 1.00 30.65  ? 1102 IOS B O1   1 
HETATM 8674 N N1   . IOS D 3 .   ? 123.347 140.910 135.936 1.00 25.95  ? 1102 IOS B N1   1 
HETATM 8675 C C1   . IOS D 3 .   ? 123.114 141.700 134.860 1.00 25.01  ? 1102 IOS B C1   1 
HETATM 8676 C C2   . IOS D 3 .   ? 122.666 140.890 133.992 1.00 25.30  ? 1102 IOS B C2   1 
HETATM 8677 C C3   . IOS D 3 .   ? 122.519 139.539 134.246 1.00 23.73  ? 1102 IOS B C3   1 
HETATM 8678 C C4   . IOS D 3 .   ? 122.098 138.402 133.613 1.00 22.36  ? 1102 IOS B C4   1 
HETATM 8679 C C5   . IOS D 3 .   ? 122.119 137.183 134.298 1.00 27.02  ? 1102 IOS B C5   1 
HETATM 8680 C C6   . IOS D 3 .   ? 122.573 137.117 135.636 1.00 23.12  ? 1102 IOS B C6   1 
HETATM 8681 C C7   . IOS D 3 .   ? 123.009 138.269 136.302 1.00 24.42  ? 1102 IOS B C7   1 
HETATM 8682 C C8   . IOS D 3 .   ? 122.997 139.476 135.653 1.00 27.69  ? 1102 IOS B C8   1 
HETATM 8683 S S    . IOS D 3 .   ? 120.879 142.178 132.591 1.00 50.78  ? 1102 IOS B S    1 
HETATM 8684 O O2   . IOS D 3 .   ? 119.802 141.369 132.021 1.00 22.97  ? 1102 IOS B O2   1 
HETATM 8685 O O3   . IOS D 3 .   ? 120.931 143.356 131.724 1.00 35.06  ? 1102 IOS B O3   1 
HETATM 8686 O O4   . IOS D 3 .   ? 120.337 142.686 133.853 1.00 35.10  ? 1102 IOS B O4   1 
HETATM 8687 C C1   . CLR E 4 .   ? 101.740 129.756 139.385 1.00 47.97  ? 1103 CLR B C1   1 
HETATM 8688 C C2   . CLR E 4 .   ? 102.130 129.062 140.685 1.00 49.49  ? 1103 CLR B C2   1 
HETATM 8689 C C3   . CLR E 4 .   ? 102.968 129.977 141.552 1.00 43.79  ? 1103 CLR B C3   1 
HETATM 8690 C C4   . CLR E 4 .   ? 102.181 131.250 141.840 1.00 39.74  ? 1103 CLR B C4   1 
HETATM 8691 C C5   . CLR E 4 .   ? 101.741 131.939 140.574 1.00 46.73  ? 1103 CLR B C5   1 
HETATM 8692 C C6   . CLR E 4 .   ? 101.958 133.243 140.414 1.00 48.99  ? 1103 CLR B C6   1 
HETATM 8693 C C7   . CLR E 4 .   ? 101.597 134.024 139.195 1.00 44.11  ? 1103 CLR B C7   1 
HETATM 8694 C C8   . CLR E 4 .   ? 100.611 133.301 138.286 1.00 45.74  ? 1103 CLR B C8   1 
HETATM 8695 C C9   . CLR E 4 .   ? 100.969 131.813 138.178 1.00 45.63  ? 1103 CLR B C9   1 
HETATM 8696 C C10  . CLR E 4 .   ? 100.993 131.097 139.554 1.00 46.00  ? 1103 CLR B C10  1 
HETATM 8697 C C11  . CLR E 4 .   ? 100.090 131.113 137.135 1.00 50.20  ? 1103 CLR B C11  1 
HETATM 8698 C C12  . CLR E 4 .   ? 100.055 131.822 135.776 1.00 50.23  ? 1103 CLR B C12  1 
HETATM 8699 C C13  . CLR E 4 .   ? 99.663  133.301 135.883 1.00 46.70  ? 1103 CLR B C13  1 
HETATM 8700 C C14  . CLR E 4 .   ? 100.638 133.920 136.900 1.00 44.34  ? 1103 CLR B C14  1 
HETATM 8701 C C15  . CLR E 4 .   ? 100.420 135.417 136.772 1.00 44.02  ? 1103 CLR B C15  1 
HETATM 8702 C C16  . CLR E 4 .   ? 100.235 135.598 135.256 1.00 38.24  ? 1103 CLR B C16  1 
HETATM 8703 C C17  . CLR E 4 .   ? 99.933  134.200 134.643 1.00 38.74  ? 1103 CLR B C17  1 
HETATM 8704 C C18  . CLR E 4 .   ? 98.201  133.445 136.318 1.00 44.58  ? 1103 CLR B C18  1 
HETATM 8705 C C19  . CLR E 4 .   ? 99.576  130.837 140.086 1.00 43.38  ? 1103 CLR B C19  1 
HETATM 8706 C C20  . CLR E 4 .   ? 98.884  134.292 133.518 1.00 41.53  ? 1103 CLR B C20  1 
HETATM 8707 C C21  . CLR E 4 .   ? 98.854  133.076 132.594 1.00 42.32  ? 1103 CLR B C21  1 
HETATM 8708 C C22  . CLR E 4 .   ? 99.077  135.580 132.697 1.00 43.41  ? 1103 CLR B C22  1 
HETATM 8709 C C23  . CLR E 4 .   ? 100.023 135.490 131.503 1.00 45.91  ? 1103 CLR B C23  1 
HETATM 8710 C C24  . CLR E 4 .   ? 99.674  136.505 130.420 1.00 43.44  ? 1103 CLR B C24  1 
HETATM 8711 C C25  . CLR E 4 .   ? 99.283  135.906 129.067 1.00 49.16  ? 1103 CLR B C25  1 
HETATM 8712 C C26  . CLR E 4 .   ? 97.973  135.131 129.175 1.00 50.88  ? 1103 CLR B C26  1 
HETATM 8713 C C27  . CLR E 4 .   ? 99.191  136.959 127.969 1.00 38.13  ? 1103 CLR B C27  1 
HETATM 8714 O O1   . CLR E 4 .   ? 103.313 129.292 142.738 1.00 45.56  ? 1103 CLR B O1   1 
HETATM 8715 N N    . POV F 2 .   ? 108.223 124.736 146.693 1.00 54.25  ? 1104 POV B N    1 
HETATM 8716 P P    . POV F 2 .   ? 111.888 126.704 144.660 1.00 60.34  ? 1104 POV B P    1 
HETATM 8717 C C1   . POV F 2 .   ? 111.881 127.397 142.142 1.00 49.44  ? 1104 POV B C1   1 
HETATM 8718 C C2   . POV F 2 .   ? 111.172 126.963 140.854 1.00 49.48  ? 1104 POV B C2   1 
HETATM 8719 C C3   . POV F 2 .   ? 109.743 126.518 141.068 1.00 54.64  ? 1104 POV B C3   1 
HETATM 8720 C C210 . POV F 2 .   ? 111.227 124.003 130.006 1.00 52.45  ? 1104 POV B C210 1 
HETATM 8721 C C310 . POV F 2 .   ? 100.899 128.500 131.787 1.00 49.91  ? 1104 POV B C310 1 
HETATM 8722 C C11  . POV F 2 .   ? 109.631 125.385 144.602 1.00 47.97  ? 1104 POV B C11  1 
HETATM 8723 O O11  . POV F 2 .   ? 111.868 126.346 143.078 1.00 48.76  ? 1104 POV B O11  1 
HETATM 8724 C C211 . POV F 2 .   ? 110.597 124.288 128.681 1.00 47.40  ? 1104 POV B C211 1 
HETATM 8725 C C311 . POV F 2 .   ? 101.322 129.859 131.246 1.00 42.11  ? 1104 POV B C311 1 
HETATM 8726 C C12  . POV F 2 .   ? 109.442 124.522 145.830 1.00 51.53  ? 1104 POV B C12  1 
HETATM 8727 O O12  . POV F 2 .   ? 110.255 126.608 144.898 1.00 51.92  ? 1104 POV B O12  1 
HETATM 8728 C C212 . POV F 2 .   ? 111.644 124.565 127.603 1.00 43.83  ? 1104 POV B C212 1 
HETATM 8729 C C312 . POV F 2 .   ? 100.423 130.359 130.122 1.00 43.98  ? 1104 POV B C312 1 
HETATM 8730 C C13  . POV F 2 .   ? 108.390 125.915 147.588 1.00 52.41  ? 1104 POV B C13  1 
HETATM 8731 O O13  . POV F 2 .   ? 112.290 128.143 144.775 1.00 46.33  ? 1104 POV B O13  1 
HETATM 8732 C C213 . POV F 2 .   ? 111.055 125.274 126.392 1.00 40.42  ? 1104 POV B C213 1 
HETATM 8733 C C313 . POV F 2 .   ? 100.177 129.326 129.030 1.00 49.62  ? 1104 POV B C313 1 
HETATM 8734 C C14  . POV F 2 .   ? 107.061 124.977 145.790 1.00 50.56  ? 1104 POV B C14  1 
HETATM 8735 O O14  . POV F 2 .   ? 112.564 125.640 145.463 1.00 51.71  ? 1104 POV B O14  1 
HETATM 8736 C C214 . POV F 2 .   ? 109.865 124.531 125.802 1.00 40.37  ? 1104 POV B C214 1 
HETATM 8737 C C314 . POV F 2 .   ? 100.184 129.915 127.625 1.00 56.63  ? 1104 POV B C314 1 
HETATM 8738 C C15  . POV F 2 .   ? 107.915 123.533 147.518 1.00 49.65  ? 1104 POV B C15  1 
HETATM 8739 C C215 . POV F 2 .   ? 108.783 125.456 125.262 1.00 44.06  ? 1104 POV B C215 1 
HETATM 8740 C C315 . POV F 2 .   ? 99.000  130.827 127.324 1.00 54.45  ? 1104 POV B C315 1 
HETATM 8741 C C216 . POV F 2 .   ? 107.679 124.720 124.517 1.00 45.12  ? 1104 POV B C216 1 
HETATM 8742 C C316 . POV F 2 .   ? 99.000  131.331 125.888 1.00 40.87  ? 1104 POV B C316 1 
HETATM 8743 C C217 . POV F 2 .   ? 106.872 123.777 125.400 1.00 43.73  ? 1104 POV B C217 1 
HETATM 8744 C C218 . POV F 2 .   ? 106.097 124.500 126.491 1.00 41.16  ? 1104 POV B C218 1 
HETATM 8745 C C21  . POV F 2 .   ? 112.885 126.166 139.367 1.00 49.34  ? 1104 POV B C21  1 
HETATM 8746 O O21  . POV F 2 .   ? 111.847 125.905 140.163 1.00 49.44  ? 1104 POV B O21  1 
HETATM 8747 C C22  . POV F 2 .   ? 113.207 124.998 138.477 1.00 48.38  ? 1104 POV B C22  1 
HETATM 8748 O O22  . POV F 2 .   ? 113.488 127.204 139.374 1.00 54.87  ? 1104 POV B O22  1 
HETATM 8749 C C23  . POV F 2 .   ? 113.028 125.237 136.987 1.00 46.34  ? 1104 POV B C23  1 
HETATM 8750 C C24  . POV F 2 .   ? 114.162 126.066 136.400 1.00 50.02  ? 1104 POV B C24  1 
HETATM 8751 C C25  . POV F 2 .   ? 113.909 126.458 134.951 1.00 50.73  ? 1104 POV B C25  1 
HETATM 8752 C C26  . POV F 2 .   ? 113.469 125.278 134.099 1.00 52.97  ? 1104 POV B C26  1 
HETATM 8753 C C27  . POV F 2 .   ? 112.484 125.661 133.006 1.00 52.90  ? 1104 POV B C27  1 
HETATM 8754 C C28  . POV F 2 .   ? 111.754 124.442 132.445 1.00 56.80  ? 1104 POV B C28  1 
HETATM 8755 C C29  . POV F 2 .   ? 111.124 124.726 131.119 1.00 53.47  ? 1104 POV B C29  1 
HETATM 8756 C C31  . POV F 2 .   ? 107.570 127.380 140.718 1.00 53.04  ? 1104 POV B C31  1 
HETATM 8757 O O31  . POV F 2 .   ? 108.881 127.561 140.627 1.00 51.93  ? 1104 POV B O31  1 
HETATM 8758 C C32  . POV F 2 .   ? 106.840 128.240 139.727 1.00 45.83  ? 1104 POV B C32  1 
HETATM 8759 O O32  . POV F 2 .   ? 107.060 126.620 141.503 1.00 55.79  ? 1104 POV B O32  1 
HETATM 8760 C C33  . POV F 2 .   ? 105.526 127.667 139.232 1.00 51.67  ? 1104 POV B C33  1 
HETATM 8761 C C34  . POV F 2 .   ? 105.005 128.433 138.022 1.00 47.45  ? 1104 POV B C34  1 
HETATM 8762 C C35  . POV F 2 .   ? 103.918 127.684 137.265 1.00 49.87  ? 1104 POV B C35  1 
HETATM 8763 C C36  . POV F 2 .   ? 103.256 128.527 136.183 1.00 48.07  ? 1104 POV B C36  1 
HETATM 8764 C C37  . POV F 2 .   ? 102.213 127.770 135.371 1.00 46.90  ? 1104 POV B C37  1 
HETATM 8765 C C38  . POV F 2 .   ? 101.653 128.588 134.214 1.00 48.57  ? 1104 POV B C38  1 
HETATM 8766 C C39  . POV F 2 .   ? 101.830 127.929 132.851 1.00 51.56  ? 1104 POV B C39  1 
HETATM 8767 P P    . POV G 2 .   ? 98.393  146.316 152.476 1.00 87.49  ? 1105 POV B P    1 
HETATM 8768 C C1   . POV G 2 .   ? 97.270  146.957 150.176 1.00 77.39  ? 1105 POV B C1   1 
HETATM 8769 C C2   . POV G 2 .   ? 97.188  146.254 148.815 1.00 77.73  ? 1105 POV B C2   1 
HETATM 8770 C C3   . POV G 2 .   ? 98.463  146.337 148.007 1.00 76.97  ? 1105 POV B C3   1 
HETATM 8771 C C210 . POV G 2 .   ? 93.537  147.889 138.015 1.00 72.03  ? 1105 POV B C210 1 
HETATM 8772 C C310 . POV G 2 .   ? 97.836  147.678 137.511 1.00 75.67  ? 1105 POV B C310 1 
HETATM 8773 O O11  . POV G 2 .   ? 98.420  146.515 150.862 1.00 81.73  ? 1105 POV B O11  1 
HETATM 8774 C C211 . POV G 2 .   ? 93.226  146.467 137.666 1.00 74.75  ? 1105 POV B C211 1 
HETATM 8775 C C311 . POV G 2 .   ? 98.182  146.582 136.513 1.00 72.05  ? 1105 POV B C311 1 
HETATM 8776 O O12  . POV G 2 .   ? 98.455  147.917 152.897 1.00 77.48  ? 1105 POV B O12  1 
HETATM 8777 C C212 . POV G 2 .   ? 91.985  146.357 136.778 1.00 73.31  ? 1105 POV B C212 1 
HETATM 8778 C C312 . POV G 2 .   ? 97.230  146.567 135.324 1.00 72.25  ? 1105 POV B C312 1 
HETATM 8779 O O13  . POV G 2 .   ? 97.035  145.790 152.830 1.00 77.61  ? 1105 POV B O13  1 
HETATM 8780 C C313 . POV G 2 .   ? 97.203  145.241 134.577 1.00 74.63  ? 1105 POV B C313 1 
HETATM 8781 O O14  . POV G 2 .   ? 99.634  145.637 152.963 1.00 75.26  ? 1105 POV B O14  1 
HETATM 8782 C C314 . POV G 2 .   ? 96.120  144.294 135.079 1.00 73.87  ? 1105 POV B C314 1 
HETATM 8783 C C315 . POV G 2 .   ? 94.773  144.490 134.393 1.00 76.55  ? 1105 POV B C315 1 
HETATM 8784 C C316 . POV G 2 .   ? 94.532  143.494 133.268 1.00 75.04  ? 1105 POV B C316 1 
HETATM 8785 C C21  . POV G 2 .   ? 94.994  146.134 147.877 1.00 75.76  ? 1105 POV B C21  1 
HETATM 8786 O O21  . POV G 2 .   ? 96.142  146.794 148.005 1.00 76.89  ? 1105 POV B O21  1 
HETATM 8787 C C22  . POV G 2 .   ? 95.172  144.870 147.081 1.00 75.21  ? 1105 POV B C22  1 
HETATM 8788 O O22  . POV G 2 .   ? 93.954  146.519 148.348 1.00 76.06  ? 1105 POV B O22  1 
HETATM 8789 C C23  . POV G 2 .   ? 95.472  145.101 145.609 1.00 73.29  ? 1105 POV B C23  1 
HETATM 8790 C C24  . POV G 2 .   ? 94.356  145.875 144.919 1.00 73.87  ? 1105 POV B C24  1 
HETATM 8791 C C25  . POV G 2 .   ? 94.748  146.386 143.539 1.00 72.46  ? 1105 POV B C25  1 
HETATM 8792 C C26  . POV G 2 .   ? 93.604  147.074 142.805 1.00 75.32  ? 1105 POV B C26  1 
HETATM 8793 C C27  . POV G 2 .   ? 94.049  147.774 141.528 1.00 74.63  ? 1105 POV B C27  1 
HETATM 8794 C C28  . POV G 2 .   ? 92.936  147.879 140.485 1.00 73.14  ? 1105 POV B C28  1 
HETATM 8795 C C29  . POV G 2 .   ? 93.417  148.482 139.202 1.00 71.59  ? 1105 POV B C29  1 
HETATM 8796 C C31  . POV G 2 .   ? 98.523  147.956 146.279 1.00 75.73  ? 1105 POV B C31  1 
HETATM 8797 O O31  . POV G 2 .   ? 98.663  147.676 147.570 1.00 73.42  ? 1105 POV B O31  1 
HETATM 8798 C C32  . POV G 2 .   ? 99.750  148.626 145.736 1.00 75.54  ? 1105 POV B C32  1 
HETATM 8799 O O32  . POV G 2 .   ? 97.534  147.698 145.641 1.00 76.33  ? 1105 POV B O32  1 
HETATM 8800 C C33  . POV G 2 .   ? 100.487 147.811 144.690 1.00 76.28  ? 1105 POV B C33  1 
HETATM 8801 C C34  . POV G 2 .   ? 100.696 148.609 143.411 1.00 73.57  ? 1105 POV B C34  1 
HETATM 8802 C C35  . POV G 2 .   ? 99.413  149.088 142.749 1.00 71.74  ? 1105 POV B C35  1 
HETATM 8803 C C36  . POV G 2 .   ? 98.786  148.030 141.850 1.00 70.91  ? 1105 POV B C36  1 
HETATM 8804 C C37  . POV G 2 .   ? 99.760  147.399 140.865 1.00 67.79  ? 1105 POV B C37  1 
HETATM 8805 C C38  . POV G 2 .   ? 99.066  146.913 139.600 1.00 71.97  ? 1105 POV B C38  1 
HETATM 8806 C C39  . POV G 2 .   ? 98.930  147.986 138.527 1.00 71.63  ? 1105 POV B C39  1 
HETATM 8807 C C1   . NAG H 5 .   ? 112.897 145.965 103.244 1.00 96.26  ? 1106 NAG B C1   1 
HETATM 8808 C C2   . NAG H 5 .   ? 112.934 144.922 102.135 1.00 94.54  ? 1106 NAG B C2   1 
HETATM 8809 C C3   . NAG H 5 .   ? 112.104 145.392 100.957 1.00 97.08  ? 1106 NAG B C3   1 
HETATM 8810 C C4   . NAG H 5 .   ? 112.623 146.723 100.424 1.00 96.39  ? 1106 NAG B C4   1 
HETATM 8811 C C5   . NAG H 5 .   ? 112.880 147.772 101.517 1.00 96.99  ? 1106 NAG B C5   1 
HETATM 8812 C C6   . NAG H 5 .   ? 111.658 148.588 101.875 1.00 94.95  ? 1106 NAG B C6   1 
HETATM 8813 C C7   . NAG H 5 .   ? 115.186 143.960 102.431 1.00 95.96  ? 1106 NAG B C7   1 
HETATM 8814 C C8   . NAG H 5 .   ? 116.546 143.800 101.821 1.00 95.76  ? 1106 NAG B C8   1 
HETATM 8815 N N2   . NAG H 5 .   ? 114.302 144.661 101.712 1.00 93.63  ? 1106 NAG B N2   1 
HETATM 8816 O O3   . NAG H 5 .   ? 110.742 145.503 101.350 1.00 98.76  ? 1106 NAG B O3   1 
HETATM 8817 O O4   . NAG H 5 .   ? 113.827 146.511 99.696  1.00 92.99  ? 1106 NAG B O4   1 
HETATM 8818 O O5   . NAG H 5 .   ? 113.413 147.231 102.743 1.00 96.05  ? 1106 NAG B O5   1 
HETATM 8819 O O6   . NAG H 5 .   ? 111.961 149.574 102.853 1.00 93.84  ? 1106 NAG B O6   1 
HETATM 8820 O O7   . NAG H 5 .   ? 114.904 143.480 103.523 1.00 96.08  ? 1106 NAG B O7   1 
HETATM 8821 N N    . TRP I 6 .   ? 99.456  131.844 149.636 1.00 100.75 ? 1107 TRP B N    1 
HETATM 8822 C CA   . TRP I 6 .   ? 98.733  130.931 148.759 1.00 102.83 ? 1107 TRP B CA   1 
HETATM 8823 C C    . TRP I 6 .   ? 99.567  130.644 147.513 1.00 101.50 ? 1107 TRP B C    1 
HETATM 8824 O O    . TRP I 6 .   ? 100.177 131.547 146.941 1.00 100.00 ? 1107 TRP B O    1 
HETATM 8825 C CB   . TRP I 6 .   ? 97.373  131.522 148.378 1.00 98.26  ? 1107 TRP B CB   1 
HETATM 8826 C CG   . TRP I 6 .   ? 96.379  130.524 147.846 1.00 99.07  ? 1107 TRP B CG   1 
HETATM 8827 C CD1  . TRP I 6 .   ? 96.621  129.229 147.488 1.00 97.96  ? 1107 TRP B CD1  1 
HETATM 8828 C CD2  . TRP I 6 .   ? 94.982  130.748 147.615 1.00 101.16 ? 1107 TRP B CD2  1 
HETATM 8829 N NE1  . TRP I 6 .   ? 95.464  128.635 147.049 1.00 100.07 ? 1107 TRP B NE1  1 
HETATM 8830 C CE2  . TRP I 6 .   ? 94.443  129.546 147.117 1.00 101.55 ? 1107 TRP B CE2  1 
HETATM 8831 C CE3  . TRP I 6 .   ? 94.136  131.849 147.781 1.00 99.64  ? 1107 TRP B CE3  1 
HETATM 8832 C CZ2  . TRP I 6 .   ? 93.097  129.413 146.784 1.00 99.93  ? 1107 TRP B CZ2  1 
HETATM 8833 C CZ3  . TRP I 6 .   ? 92.800  131.715 147.449 1.00 96.64  ? 1107 TRP B CZ3  1 
HETATM 8834 C CH2  . TRP I 6 .   ? 92.294  130.507 146.956 1.00 97.91  ? 1107 TRP B CH2  1 
HETATM 8835 O OXT  . TRP I 6 .   ? 99.656  129.508 147.050 1.00 99.27  ? 1107 TRP B OXT  1 
HETATM 8836 N N    . POV J 2 .   ? 142.588 148.625 148.365 1.00 81.09  ? 1101 POV A N    1 
HETATM 8837 P P    . POV J 2 .   ? 147.205 146.597 147.487 1.00 98.51  ? 1101 POV A P    1 
HETATM 8838 C C1   . POV J 2 .   ? 147.309 147.590 145.044 1.00 79.17  ? 1101 POV A C1   1 
HETATM 8839 C C2   . POV J 2 .   ? 146.643 147.492 143.664 1.00 75.60  ? 1101 POV A C2   1 
HETATM 8840 C C3   . POV J 2 .   ? 145.160 147.776 143.702 1.00 77.91  ? 1101 POV A C3   1 
HETATM 8841 C C210 . POV J 2 .   ? 151.467 144.625 133.159 1.00 79.13  ? 1101 POV A C210 1 
HETATM 8842 C C310 . POV J 2 .   ? 147.213 147.506 131.925 1.00 78.13  ? 1101 POV A C310 1 
HETATM 8843 C C11  . POV J 2 .   ? 144.663 147.297 147.540 1.00 80.18  ? 1101 POV A C11  1 
HETATM 8844 O O11  . POV J 2 .   ? 146.663 146.731 145.958 1.00 86.68  ? 1101 POV A O11  1 
HETATM 8845 C C211 . POV J 2 .   ? 151.107 145.315 131.881 1.00 79.57  ? 1101 POV A C211 1 
HETATM 8846 C C311 . POV J 2 .   ? 146.711 148.517 130.904 1.00 76.70  ? 1101 POV A C311 1 
HETATM 8847 C C12  . POV J 2 .   ? 144.017 148.623 147.881 1.00 77.94  ? 1101 POV A C12  1 
HETATM 8848 O O12  . POV J 2 .   ? 145.830 147.055 148.291 1.00 82.48  ? 1101 POV A O12  1 
HETATM 8849 C C212 . POV J 2 .   ? 151.773 144.655 130.672 1.00 79.43  ? 1101 POV A C212 1 
HETATM 8850 C C312 . POV J 2 .   ? 147.796 148.967 129.935 1.00 77.94  ? 1101 POV A C312 1 
HETATM 8851 C C13  . POV J 2 .   ? 142.275 149.871 149.117 1.00 80.80  ? 1101 POV A C13  1 
HETATM 8852 O O13  . POV J 2 .   ? 147.430 145.139 147.750 1.00 84.69  ? 1101 POV A O13  1 
HETATM 8853 C C213 . POV J 2 .   ? 150.909 143.587 130.011 1.00 79.00  ? 1101 POV A C213 1 
HETATM 8854 C C313 . POV J 2 .   ? 147.295 149.912 128.851 1.00 81.18  ? 1101 POV A C313 1 
HETATM 8855 C C14  . POV J 2 .   ? 141.720 148.570 147.155 1.00 78.58  ? 1101 POV A C14  1 
HETATM 8856 O O14  . POV J 2 .   ? 148.280 147.598 147.767 1.00 78.42  ? 1101 POV A O14  1 
HETATM 8857 C C214 . POV J 2 .   ? 149.736 144.167 129.231 1.00 74.27  ? 1101 POV A C214 1 
HETATM 8858 C C314 . POV J 2 .   ? 146.571 149.186 127.724 1.00 78.57  ? 1101 POV A C314 1 
HETATM 8859 C C15  . POV J 2 .   ? 142.272 147.442 149.217 1.00 77.31  ? 1101 POV A C15  1 
HETATM 8860 C C215 . POV J 2 .   ? 150.150 145.198 128.187 1.00 76.11  ? 1101 POV A C215 1 
HETATM 8861 C C315 . POV J 2 .   ? 145.838 150.117 126.765 1.00 76.64  ? 1101 POV A C315 1 
HETATM 8862 C C216 . POV J 2 .   ? 149.003 145.637 127.285 1.00 78.30  ? 1101 POV A C216 1 
HETATM 8863 C C316 . POV J 2 .   ? 146.751 151.164 126.144 1.00 78.93  ? 1101 POV A C316 1 
HETATM 8864 C C217 . POV J 2 .   ? 149.423 146.639 126.216 1.00 77.78  ? 1101 POV A C217 1 
HETATM 8865 C C218 . POV J 2 .   ? 148.299 146.990 125.252 1.00 75.76  ? 1101 POV A C218 1 
HETATM 8866 C C21  . POV J 2 .   ? 147.931 145.869 142.448 1.00 77.18  ? 1101 POV A C21  1 
HETATM 8867 O O21  . POV J 2 .   ? 146.792 146.206 143.053 1.00 73.50  ? 1101 POV A O21  1 
HETATM 8868 C C22  . POV J 2 .   ? 147.735 145.595 140.983 1.00 78.06  ? 1101 POV A C22  1 
HETATM 8869 O O22  . POV J 2 .   ? 148.992 145.787 143.014 1.00 79.07  ? 1101 POV A O22  1 
HETATM 8870 C C23  . POV J 2 .   ? 149.027 145.197 140.284 1.00 79.34  ? 1101 POV A C23  1 
HETATM 8871 C C24  . POV J 2 .   ? 148.823 144.900 138.805 1.00 76.31  ? 1101 POV A C24  1 
HETATM 8872 C C25  . POV J 2 .   ? 149.106 146.097 137.906 1.00 76.94  ? 1101 POV A C25  1 
HETATM 8873 C C26  . POV J 2 .   ? 150.252 145.860 136.931 1.00 71.31  ? 1101 POV A C26  1 
HETATM 8874 C C27  . POV J 2 .   ? 150.197 146.773 135.713 1.00 74.35  ? 1101 POV A C27  1 
HETATM 8875 C C28  . POV J 2 .   ? 151.386 146.592 134.769 1.00 78.72  ? 1101 POV A C28  1 
HETATM 8876 C C29  . POV J 2 .   ? 151.586 145.163 134.373 1.00 79.96  ? 1101 POV A C29  1 
HETATM 8877 C C31  . POV J 2 .   ? 144.464 148.846 141.714 1.00 80.13  ? 1101 POV A C31  1 
HETATM 8878 O O31  . POV J 2 .   ? 144.668 147.712 142.371 1.00 79.37  ? 1101 POV A O31  1 
HETATM 8879 C C32  . POV J 2 .   ? 144.144 148.573 140.274 1.00 77.07  ? 1101 POV A C32  1 
HETATM 8880 O O32  . POV J 2 .   ? 144.528 149.935 142.227 1.00 84.69  ? 1101 POV A O32  1 
HETATM 8881 C C33  . POV J 2 .   ? 144.862 149.466 139.279 1.00 76.66  ? 1101 POV A C33  1 
HETATM 8882 C C34  . POV J 2 .   ? 144.270 149.297 137.887 1.00 79.43  ? 1101 POV A C34  1 
HETATM 8883 C C35  . POV J 2 .   ? 145.026 150.037 136.794 1.00 81.29  ? 1101 POV A C35  1 
HETATM 8884 C C36  . POV J 2 .   ? 145.978 149.128 136.025 1.00 78.17  ? 1101 POV A C36  1 
HETATM 8885 C C37  . POV J 2 .   ? 146.689 149.829 134.876 1.00 79.49  ? 1101 POV A C37  1 
HETATM 8886 C C38  . POV J 2 .   ? 147.526 148.884 134.023 1.00 78.34  ? 1101 POV A C38  1 
HETATM 8887 C C39  . POV J 2 .   ? 146.722 147.784 133.341 1.00 80.73  ? 1101 POV A C39  1 
HETATM 8888 O O1   . IOS K 3 .   ? 141.681 122.613 132.717 1.00 31.01  ? 1102 IOS A O1   1 
HETATM 8889 N N1   . IOS K 3 .   ? 140.668 123.103 135.928 1.00 27.23  ? 1102 IOS A N1   1 
HETATM 8890 C C1   . IOS K 3 .   ? 140.897 122.306 134.856 1.00 25.02  ? 1102 IOS A C1   1 
HETATM 8891 C C2   . IOS K 3 .   ? 141.339 123.110 133.980 1.00 25.67  ? 1102 IOS A C2   1 
HETATM 8892 C C3   . IOS K 3 .   ? 141.485 124.463 134.223 1.00 25.51  ? 1102 IOS A C3   1 
HETATM 8893 C C4   . IOS K 3 .   ? 141.901 125.596 133.579 1.00 25.06  ? 1102 IOS A C4   1 
HETATM 8894 C C5   . IOS K 3 .   ? 141.880 126.821 134.254 1.00 29.70  ? 1102 IOS A C5   1 
HETATM 8895 C C6   . IOS K 3 .   ? 141.433 126.896 135.594 1.00 23.40  ? 1102 IOS A C6   1 
HETATM 8896 C C7   . IOS K 3 .   ? 141.003 125.748 136.271 1.00 25.62  ? 1102 IOS A C7   1 
HETATM 8897 C C8   . IOS K 3 .   ? 141.014 124.536 135.631 1.00 31.27  ? 1102 IOS A C8   1 
HETATM 8898 S S    . IOS K 3 .   ? 143.126 121.823 132.576 1.00 50.39  ? 1102 IOS A S    1 
HETATM 8899 O O2   . IOS K 3 .   ? 144.202 122.648 132.026 1.00 23.01  ? 1102 IOS A O2   1 
HETATM 8900 O O3   . IOS K 3 .   ? 143.086 120.660 131.688 1.00 36.51  ? 1102 IOS A O3   1 
HETATM 8901 O O4   . IOS K 3 .   ? 143.663 121.297 133.832 1.00 34.33  ? 1102 IOS A O4   1 
HETATM 8902 C C1   . CLR L 4 .   ? 162.240 134.268 139.389 1.00 50.53  ? 1103 CLR A C1   1 
HETATM 8903 C C2   . CLR L 4 .   ? 161.859 134.954 140.697 1.00 50.79  ? 1103 CLR A C2   1 
HETATM 8904 C C3   . CLR L 4 .   ? 161.051 134.025 141.578 1.00 45.77  ? 1103 CLR A C3   1 
HETATM 8905 C C4   . CLR L 4 .   ? 161.863 132.764 141.847 1.00 43.84  ? 1103 CLR A C4   1 
HETATM 8906 C C5   . CLR L 4 .   ? 162.289 132.085 140.572 1.00 48.58  ? 1103 CLR A C5   1 
HETATM 8907 C C6   . CLR L 4 .   ? 162.071 130.782 140.406 1.00 51.71  ? 1103 CLR A C6   1 
HETATM 8908 C C7   . CLR L 4 .   ? 162.384 130.024 139.162 1.00 46.41  ? 1103 CLR A C7   1 
HETATM 8909 C C8   . CLR L 4 .   ? 163.380 130.740 138.261 1.00 48.31  ? 1103 CLR A C8   1 
HETATM 8910 C C9   . CLR L 4 .   ? 163.027 132.230 138.160 1.00 47.71  ? 1103 CLR A C9   1 
HETATM 8911 C C10  . CLR L 4 .   ? 163.010 132.938 139.541 1.00 49.10  ? 1103 CLR A C10  1 
HETATM 8912 C C11  . CLR L 4 .   ? 163.906 132.928 137.115 1.00 52.25  ? 1103 CLR A C11  1 
HETATM 8913 C C12  . CLR L 4 .   ? 163.947 132.217 135.756 1.00 51.37  ? 1103 CLR A C12  1 
HETATM 8914 C C13  . CLR L 4 .   ? 164.337 130.737 135.863 1.00 49.25  ? 1103 CLR A C13  1 
HETATM 8915 C C14  . CLR L 4 .   ? 163.356 130.122 136.876 1.00 47.85  ? 1103 CLR A C14  1 
HETATM 8916 C C15  . CLR L 4 .   ? 163.568 128.623 136.751 1.00 47.36  ? 1103 CLR A C15  1 
HETATM 8917 C C16  . CLR L 4 .   ? 163.762 128.439 135.237 1.00 41.64  ? 1103 CLR A C16  1 
HETATM 8918 C C17  . CLR L 4 .   ? 164.068 129.836 134.623 1.00 41.30  ? 1103 CLR A C17  1 
HETATM 8919 C C18  . CLR L 4 .   ? 165.797 130.589 136.304 1.00 47.79  ? 1103 CLR A C18  1 
HETATM 8920 C C19  . CLR L 4 .   ? 164.429 133.218 140.056 1.00 46.87  ? 1103 CLR A C19  1 
HETATM 8921 C C20  . CLR L 4 .   ? 165.118 129.738 133.500 1.00 43.15  ? 1103 CLR A C20  1 
HETATM 8922 C C21  . CLR L 4 .   ? 165.159 130.956 132.579 1.00 44.08  ? 1103 CLR A C21  1 
HETATM 8923 C C22  . CLR L 4 .   ? 164.916 128.453 132.676 1.00 45.62  ? 1103 CLR A C22  1 
HETATM 8924 C C23  . CLR L 4 .   ? 163.998 128.559 131.461 1.00 48.69  ? 1103 CLR A C23  1 
HETATM 8925 C C24  . CLR L 4 .   ? 164.270 127.455 130.444 1.00 46.78  ? 1103 CLR A C24  1 
HETATM 8926 C C25  . CLR L 4 .   ? 164.630 127.935 129.036 1.00 51.68  ? 1103 CLR A C25  1 
HETATM 8927 C C26  . CLR L 4 .   ? 165.827 128.880 129.082 1.00 52.53  ? 1103 CLR A C26  1 
HETATM 8928 C C27  . CLR L 4 .   ? 164.910 126.775 128.086 1.00 41.73  ? 1103 CLR A C27  1 
HETATM 8929 O O1   . CLR L 4 .   ? 160.719 134.702 142.772 1.00 47.19  ? 1103 CLR A O1   1 
HETATM 8930 N N    . POV M 2 .   ? 155.791 139.276 146.700 1.00 55.09  ? 1104 POV A N    1 
HETATM 8931 P P    . POV M 2 .   ? 152.098 137.327 144.738 1.00 67.30  ? 1104 POV A P    1 
HETATM 8932 C C1   . POV M 2 .   ? 152.039 136.656 142.211 1.00 52.77  ? 1104 POV A C1   1 
HETATM 8933 C C2   . POV M 2 .   ? 152.703 137.115 140.907 1.00 51.60  ? 1104 POV A C2   1 
HETATM 8934 C C3   . POV M 2 .   ? 154.141 137.545 141.086 1.00 56.71  ? 1104 POV A C3   1 
HETATM 8935 C C210 . POV M 2 .   ? 152.809 139.956 130.019 1.00 53.37  ? 1104 POV A C210 1 
HETATM 8936 C C310 . POV M 2 .   ? 163.118 135.482 131.846 1.00 52.84  ? 1104 POV A C310 1 
HETATM 8937 C C11  . POV M 2 .   ? 154.360 138.640 144.622 1.00 49.38  ? 1104 POV A C11  1 
HETATM 8938 O O11  . POV M 2 .   ? 152.071 137.696 143.158 1.00 52.72  ? 1104 POV A O11  1 
HETATM 8939 C C211 . POV M 2 .   ? 153.423 139.608 128.701 1.00 49.67  ? 1104 POV A C211 1 
HETATM 8940 C C311 . POV M 2 .   ? 162.654 134.154 131.264 1.00 43.87  ? 1104 POV A C311 1 
HETATM 8941 C C12  . POV M 2 .   ? 154.567 139.503 145.847 1.00 51.81  ? 1104 POV A C12  1 
HETATM 8942 O O12  . POV M 2 .   ? 153.738 137.418 144.927 1.00 55.84  ? 1104 POV A O12  1 
HETATM 8943 C C212 . POV M 2 .   ? 152.368 139.429 127.610 1.00 46.99  ? 1104 POV A C212 1 
HETATM 8944 C C312 . POV M 2 .   ? 163.557 133.645 130.146 1.00 45.46  ? 1104 POV A C312 1 
HETATM 8945 C C13  . POV M 2 .   ? 155.622 138.092 147.587 1.00 54.17  ? 1104 POV A C13  1 
HETATM 8946 O O13  . POV M 2 .   ? 151.698 135.888 144.854 1.00 49.08  ? 1104 POV A O13  1 
HETATM 8947 C C213 . POV M 2 .   ? 152.923 138.751 126.366 1.00 43.31  ? 1104 POV A C213 1 
HETATM 8948 C C313 . POV M 2 .   ? 163.826 134.677 129.058 1.00 51.84  ? 1104 POV A C313 1 
HETATM 8949 C C14  . POV M 2 .   ? 156.946 139.036 145.789 1.00 55.43  ? 1104 POV A C14  1 
HETATM 8950 O O14  . POV M 2 .   ? 151.445 138.389 145.564 1.00 56.00  ? 1104 POV A O14  1 
HETATM 8951 C C214 . POV M 2 .   ? 154.127 139.482 125.791 1.00 43.07  ? 1104 POV A C214 1 
HETATM 8952 C C314 . POV M 2 .   ? 163.819 134.091 127.650 1.00 59.79  ? 1104 POV A C314 1 
HETATM 8953 C C15  . POV M 2 .   ? 156.111 140.472 147.532 1.00 49.44  ? 1104 POV A C15  1 
HETATM 8954 C C215 . POV M 2 .   ? 155.212 138.546 125.275 1.00 47.31  ? 1104 POV A C215 1 
HETATM 8955 C C315 . POV M 2 .   ? 165.000 133.178 127.347 1.00 58.49  ? 1104 POV A C315 1 
HETATM 8956 C C216 . POV M 2 .   ? 156.321 139.270 124.525 1.00 48.92  ? 1104 POV A C216 1 
HETATM 8957 C C316 . POV M 2 .   ? 165.001 132.680 125.908 1.00 44.65  ? 1104 POV A C316 1 
HETATM 8958 C C217 . POV M 2 .   ? 157.129 140.219 125.400 1.00 46.33  ? 1104 POV A C217 1 
HETATM 8959 C C218 . POV M 2 .   ? 157.907 139.504 126.494 1.00 44.12  ? 1104 POV A C218 1 
HETATM 8960 C C21  . POV M 2 .   ? 150.964 137.968 139.487 1.00 50.95  ? 1104 POV A C21  1 
HETATM 8961 O O21  . POV M 2 .   ? 152.019 138.201 140.268 1.00 52.29  ? 1104 POV A O21  1 
HETATM 8962 C C22  . POV M 2 .   ? 150.662 139.135 138.588 1.00 51.92  ? 1104 POV A C22  1 
HETATM 8963 O O22  . POV M 2 .   ? 150.331 136.948 139.516 1.00 57.18  ? 1104 POV A O22  1 
HETATM 8964 C C23  . POV M 2 .   ? 150.821 138.926 137.092 1.00 47.16  ? 1104 POV A C23  1 
HETATM 8965 C C24  . POV M 2 .   ? 149.701 138.087 136.491 1.00 52.28  ? 1104 POV A C24  1 
HETATM 8966 C C25  . POV M 2 .   ? 149.949 137.730 135.031 1.00 52.81  ? 1104 POV A C25  1 
HETATM 8967 C C26  . POV M 2 .   ? 150.523 138.885 134.223 1.00 56.05  ? 1104 POV A C26  1 
HETATM 8968 C C27  . POV M 2 .   ? 151.339 138.436 133.020 1.00 56.27  ? 1104 POV A C27  1 
HETATM 8969 C C28  . POV M 2 .   ? 152.184 139.573 132.447 1.00 59.29  ? 1104 POV A C28  1 
HETATM 8970 C C29  . POV M 2 .   ? 152.799 139.220 131.129 1.00 55.21  ? 1104 POV A C29  1 
HETATM 8971 C C31  . POV M 2 .   ? 156.299 136.674 140.675 1.00 54.32  ? 1104 POV A C31  1 
HETATM 8972 O O31  . POV M 2 .   ? 154.985 136.493 140.634 1.00 52.04  ? 1104 POV A O31  1 
HETATM 8973 C C32  . POV M 2 .   ? 156.988 135.843 139.630 1.00 48.17  ? 1104 POV A C32  1 
HETATM 8974 O O32  . POV M 2 .   ? 156.845 137.411 141.458 1.00 56.73  ? 1104 POV A O32  1 
HETATM 8975 C C33  . POV M 2 .   ? 158.373 136.329 139.245 1.00 54.35  ? 1104 POV A C33  1 
HETATM 8976 C C34  . POV M 2 .   ? 158.910 135.577 138.034 1.00 51.07  ? 1104 POV A C34  1 
HETATM 8977 C C35  . POV M 2 .   ? 160.021 136.318 137.303 1.00 52.96  ? 1104 POV A C35  1 
HETATM 8978 C C36  . POV M 2 .   ? 160.684 135.472 136.222 1.00 52.75  ? 1104 POV A C36  1 
HETATM 8979 C C37  . POV M 2 .   ? 161.707 136.235 135.390 1.00 50.77  ? 1104 POV A C37  1 
HETATM 8980 C C38  . POV M 2 .   ? 162.283 135.405 134.249 1.00 53.07  ? 1104 POV A C38  1 
HETATM 8981 C C39  . POV M 2 .   ? 162.174 136.077 132.885 1.00 55.00  ? 1104 POV A C39  1 
HETATM 8982 P P    . POV N 2 .   ? 165.606 117.718 152.481 1.00 87.32  ? 1105 POV A P    1 
HETATM 8983 C C1   . POV N 2 .   ? 166.729 117.066 150.183 1.00 75.86  ? 1105 POV A C1   1 
HETATM 8984 C C2   . POV N 2 .   ? 166.806 117.777 148.827 1.00 77.41  ? 1105 POV A C2   1 
HETATM 8985 C C3   . POV N 2 .   ? 165.520 117.720 148.033 1.00 77.04  ? 1105 POV A C3   1 
HETATM 8986 C C210 . POV N 2 .   ? 170.457 116.105 138.028 1.00 71.98  ? 1105 POV A C210 1 
HETATM 8987 C C310 . POV N 2 .   ? 166.227 116.530 137.610 1.00 75.59  ? 1105 POV A C310 1 
HETATM 8988 O O11  . POV N 2 .   ? 165.574 117.494 150.871 1.00 79.72  ? 1105 POV A O11  1 
HETATM 8989 C C211 . POV N 2 .   ? 170.769 117.526 137.676 1.00 73.72  ? 1105 POV A C211 1 
HETATM 8990 C C311 . POV N 2 .   ? 165.798 117.455 136.480 1.00 69.92  ? 1105 POV A C311 1 
HETATM 8991 O O12  . POV N 2 .   ? 165.586 116.122 152.925 1.00 75.34  ? 1105 POV A O12  1 
HETATM 8992 C C212 . POV N 2 .   ? 172.009 117.633 136.786 1.00 72.77  ? 1105 POV A C212 1 
HETATM 8993 C C312 . POV N 2 .   ? 166.723 117.358 135.274 1.00 70.92  ? 1105 POV A C312 1 
HETATM 8994 O O13  . POV N 2 .   ? 166.954 118.280 152.819 1.00 76.90  ? 1105 POV A O13  1 
HETATM 8995 C C313 . POV N 2 .   ? 166.893 118.673 134.528 1.00 73.61  ? 1105 POV A C313 1 
HETATM 8996 O O14  . POV N 2 .   ? 164.352 118.373 152.967 1.00 75.77  ? 1105 POV A O14  1 
HETATM 8997 C C314 . POV N 2 .   ? 168.025 119.528 135.082 1.00 73.35  ? 1105 POV A C314 1 
HETATM 8998 C C315 . POV N 2 .   ? 169.319 119.415 134.285 1.00 74.96  ? 1105 POV A C315 1 
HETATM 8999 C C316 . POV N 2 .   ? 169.504 120.556 133.295 1.00 73.63  ? 1105 POV A C316 1 
HETATM 9000 C C21  . POV N 2 .   ? 168.995 117.862 147.877 1.00 75.19  ? 1105 POV A C21  1 
HETATM 9001 O O21  . POV N 2 .   ? 167.833 117.226 148.000 1.00 76.54  ? 1105 POV A O21  1 
HETATM 9002 C C22  . POV N 2 .   ? 168.842 119.138 147.094 1.00 74.52  ? 1105 POV A C22  1 
HETATM 9003 O O22  . POV N 2 .   ? 170.028 117.451 148.341 1.00 75.07  ? 1105 POV A O22  1 
HETATM 9004 C C23  . POV N 2 .   ? 168.560 118.928 145.616 1.00 72.24  ? 1105 POV A C23  1 
HETATM 9005 C C24  . POV N 2 .   ? 169.662 118.123 144.939 1.00 73.16  ? 1105 POV A C24  1 
HETATM 9006 C C25  . POV N 2 .   ? 169.257 117.590 143.571 1.00 71.02  ? 1105 POV A C25  1 
HETATM 9007 C C26  . POV N 2 .   ? 170.401 116.917 142.823 1.00 73.28  ? 1105 POV A C26  1 
HETATM 9008 C C27  . POV N 2 .   ? 169.952 116.225 141.544 1.00 74.10  ? 1105 POV A C27  1 
HETATM 9009 C C28  . POV N 2 .   ? 171.062 116.121 140.498 1.00 72.94  ? 1105 POV A C28  1 
HETATM 9010 C C29  . POV N 2 .   ? 170.579 115.514 139.217 1.00 72.28  ? 1105 POV A C29  1 
HETATM 9011 C C31  . POV N 2 .   ? 165.422 116.136 146.277 1.00 75.76  ? 1105 POV A C31  1 
HETATM 9012 O O31  . POV N 2 .   ? 165.306 116.390 147.575 1.00 73.23  ? 1105 POV A O31  1 
HETATM 9013 C C32  . POV N 2 .   ? 164.213 115.415 145.759 1.00 75.21  ? 1105 POV A C32  1 
HETATM 9014 O O32  . POV N 2 .   ? 166.379 116.452 145.616 1.00 76.64  ? 1105 POV A O32  1 
HETATM 9015 C C33  . POV N 2 .   ? 163.459 116.172 144.682 1.00 74.70  ? 1105 POV A C33  1 
HETATM 9016 C C34  . POV N 2 .   ? 163.339 115.350 143.407 1.00 71.67  ? 1105 POV A C34  1 
HETATM 9017 C C35  . POV N 2 .   ? 164.671 114.967 142.777 1.00 70.63  ? 1105 POV A C35  1 
HETATM 9018 C C36  . POV N 2 .   ? 165.211 116.045 141.847 1.00 69.80  ? 1105 POV A C36  1 
HETATM 9019 C C37  . POV N 2 .   ? 164.177 116.601 140.879 1.00 67.68  ? 1105 POV A C37  1 
HETATM 9020 C C38  . POV N 2 .   ? 164.815 117.172 139.621 1.00 71.31  ? 1105 POV A C38  1 
HETATM 9021 C C39  . POV N 2 .   ? 165.106 116.122 138.558 1.00 71.75  ? 1105 POV A C39  1 
HETATM 9022 C C1   . NAG O 5 .   ? 151.189 118.069 103.316 1.00 96.52  ? 1106 NAG A C1   1 
HETATM 9023 C C2   . NAG O 5 .   ? 151.155 119.115 102.209 1.00 94.95  ? 1106 NAG A C2   1 
HETATM 9024 C C3   . NAG O 5 .   ? 151.999 118.651 101.039 1.00 96.94  ? 1106 NAG A C3   1 
HETATM 9025 C C4   . NAG O 5 .   ? 151.490 117.320 100.498 1.00 95.90  ? 1106 NAG A C4   1 
HETATM 9026 C C5   . NAG O 5 .   ? 151.221 116.267 101.585 1.00 96.46  ? 1106 NAG A C5   1 
HETATM 9027 C C6   . NAG O 5 .   ? 152.437 115.446 101.950 1.00 95.30  ? 1106 NAG A C6   1 
HETATM 9028 C C7   . NAG O 5 .   ? 148.883 120.035 102.493 1.00 95.63  ? 1106 NAG A C7   1 
HETATM 9029 C C8   . NAG O 5 .   ? 147.531 120.190 101.863 1.00 94.66  ? 1106 NAG A C8   1 
HETATM 9030 N N2   . NAG O 5 .   ? 149.790 119.367 101.772 1.00 94.59  ? 1106 NAG A N2   1 
HETATM 9031 O O3   . NAG O 5 .   ? 153.357 118.545 101.444 1.00 99.44  ? 1106 NAG A O3   1 
HETATM 9032 O O4   . NAG O 5 .   ? 150.295 117.530 99.753  1.00 92.23  ? 1106 NAG A O4   1 
HETATM 9033 O O5   . NAG O 5 .   ? 150.680 116.804 102.809 1.00 95.85  ? 1106 NAG A O5   1 
HETATM 9034 O O6   . NAG O 5 .   ? 152.108 114.408 102.862 1.00 94.27  ? 1106 NAG A O6   1 
HETATM 9035 O O7   . NAG O 5 .   ? 149.137 120.493 103.601 1.00 95.09  ? 1106 NAG A O7   1 
HETATM 9036 N N    . TRP P 6 .   ? 164.539 132.151 149.629 1.00 96.94  ? 1107 TRP A N    1 
HETATM 9037 C CA   . TRP P 6 .   ? 165.256 133.064 148.749 1.00 100.87 ? 1107 TRP A CA   1 
HETATM 9038 C C    . TRP P 6 .   ? 164.427 133.333 147.496 1.00 100.54 ? 1107 TRP A C    1 
HETATM 9039 O O    . TRP P 6 .   ? 163.831 132.420 146.926 1.00 98.57  ? 1107 TRP A O    1 
HETATM 9040 C CB   . TRP P 6 .   ? 166.625 132.486 148.379 1.00 97.38  ? 1107 TRP A CB   1 
HETATM 9041 C CG   . TRP P 6 .   ? 167.610 133.490 147.846 1.00 97.52  ? 1107 TRP A CG   1 
HETATM 9042 C CD1  . TRP P 6 .   ? 167.357 134.781 147.482 1.00 96.17  ? 1107 TRP A CD1  1 
HETATM 9043 C CD2  . TRP P 6 .   ? 169.009 133.279 147.618 1.00 98.18  ? 1107 TRP A CD2  1 
HETATM 9044 N NE1  . TRP P 6 .   ? 168.510 135.385 147.042 1.00 97.53  ? 1107 TRP A NE1  1 
HETATM 9045 C CE2  . TRP P 6 .   ? 169.539 134.483 147.116 1.00 99.34  ? 1107 TRP A CE2  1 
HETATM 9046 C CE3  . TRP P 6 .   ? 169.865 132.186 147.790 1.00 96.00  ? 1107 TRP A CE3  1 
HETATM 9047 C CZ2  . TRP P 6 .   ? 170.884 134.627 146.785 1.00 98.74  ? 1107 TRP A CZ2  1 
HETATM 9048 C CZ3  . TRP P 6 .   ? 171.201 132.331 147.461 1.00 94.04  ? 1107 TRP A CZ3  1 
HETATM 9049 C CH2  . TRP P 6 .   ? 171.697 133.542 146.964 1.00 97.03  ? 1107 TRP A CH2  1 
HETATM 9050 O OXT  . TRP P 6 .   ? 164.329 134.466 147.024 1.00 98.09  ? 1107 TRP A OXT  1 
# 
