data_8ZQO
# 
_entry.id   8ZQO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZQO         pdb_00008zqo 10.2210/pdb8zqo/pdb 
WWPDB D_1300045453 ?            ?                   
EMDB  EMD-60386    ?            ?                   
# 
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 2024-12-04 ? 
2  'EM metadata'     1 0 2024-12-04 ? 
3  'Half map'        1 0 2024-12-04 1 
4  'Half map'        1 0 2024-12-04 2 
5  Image             1 0 2024-12-04 ? 
6  'Primary map'     1 0 2024-12-04 ? 
7  'Structure model' 1 1 2024-12-25 ? 
8  'Half map'        1 0 2024-12-04 1 
9  'Half map'        1 0 2024-12-04 2 
10 Image             1 0 2024-12-04 ? 
11 'Primary map'     1 0 2024-12-04 ? 
12 'Structure model' 1 2 2025-02-26 ? 
13 'EM metadata'     1 1 2025-02-26 ? 
# 
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 12 'Structure model' 'Database references'  
5 13 'EM metadata'     'Database references'  
6 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' citation_author 
3 7  'Structure model' em_admin        
4 12 'Structure model' citation        
5 12 'Structure model' em_admin        
6 13 'EM metadata'     citation        
7 13 'EM metadata'     em_admin        
# 
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.pdbx_database_id_PubMed' 
2  7  'Structure model' '_citation.title'                   
3  7  'Structure model' '_em_admin.last_update'             
4  12 'Structure model' '_citation.journal_volume'          
5  12 'Structure model' '_citation.page_first'              
6  12 'Structure model' '_citation.year'                    
7  12 'Structure model' '_em_admin.last_update'             
8  13 'EM metadata'     '_citation.journal_volume'          
9  13 'EM metadata'     '_citation.page_first'              
10 13 'EM metadata'     '_citation.year'                    
11 13 'EM metadata'     '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZQO 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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        
'Human high-affinity choline transporter CHT1 bound to HC-3 under NaCl condition, with sodium and chloride ions coordinated.' 
_pdbx_database_related.db_id          EMD-60386 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              zhaoy@ibp.ac.cn 
_pdbx_contact_author.name_first         Yan 
_pdbx_contact_author.name_last          Zhao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4348-256X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qiu, Y.'  1 0000-0002-1170-7365 
'Gao, Y.'  2 0000-0001-8169-9332 
'Zhao, Y.' 3 0000-0002-4348-256X 
# 
_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            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                321 
_citation.page_last                 ? 
_citation.title                     
'Ion coupling and inhibitory mechanisms of the human presynaptic high-affinity choline transporter CHT1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.11.009 
_citation.pdbx_database_id_PubMed   39657660 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Qiu, Y.'  1 ? 
primary 'Gao, Y.'  2 ? 
primary 'Bai, Q.'  3 ? 
primary 'Zhao, Y.' 4 ? 
# 
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 'High affinity choline transporter 1' 63239.145 1 ? ? ? ? 
2 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   1 ? 
? ? ? 
3 non-polymer syn 'SODIUM ION' 22.990    2 ? ? ? ? 
4 non-polymer syn "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" 414.538   1 ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION' 35.453    1 ? ? ? ? 
6 water       nat water 18.015    1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Hemicholinium-3-sensitive choline transporter,CHT,Solute carrier family 5 member 7' 
# 
_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       
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SODIUM ION'                                                                 NA  
4 "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" HC6 
5 'CHLORIDE ION'                                                               CL  
6 water                                                                        HOH 
# 
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   ALA n 
1 3   PHE n 
1 4   HIS n 
1 5   VAL n 
1 6   GLU n 
1 7   GLY n 
1 8   LEU n 
1 9   ILE n 
1 10  ALA n 
1 11  ILE n 
1 12  ILE n 
1 13  VAL n 
1 14  PHE n 
1 15  TYR n 
1 16  LEU n 
1 17  LEU n 
1 18  ILE n 
1 19  LEU n 
1 20  LEU n 
1 21  VAL n 
1 22  GLY n 
1 23  ILE n 
1 24  TRP n 
1 25  ALA n 
1 26  ALA n 
1 27  TRP n 
1 28  ARG n 
1 29  THR n 
1 30  LYS n 
1 31  ASN n 
1 32  SER n 
1 33  GLY n 
1 34  SER n 
1 35  ALA n 
1 36  GLU n 
1 37  GLU n 
1 38  ARG n 
1 39  SER n 
1 40  GLU n 
1 41  ALA n 
1 42  ILE n 
1 43  ILE n 
1 44  VAL n 
1 45  GLY n 
1 46  GLY n 
1 47  ARG n 
1 48  ASP n 
1 49  ILE n 
1 50  GLY n 
1 51  LEU n 
1 52  LEU n 
1 53  VAL n 
1 54  GLY n 
1 55  GLY n 
1 56  PHE n 
1 57  THR n 
1 58  MET n 
1 59  THR n 
1 60  ALA n 
1 61  THR n 
1 62  TRP n 
1 63  VAL n 
1 64  GLY n 
1 65  GLY n 
1 66  GLY n 
1 67  TYR n 
1 68  ILE n 
1 69  ASN n 
1 70  GLY n 
1 71  THR n 
1 72  ALA n 
1 73  GLU n 
1 74  ALA n 
1 75  VAL n 
1 76  TYR n 
1 77  VAL n 
1 78  PRO n 
1 79  GLY n 
1 80  TYR n 
1 81  GLY n 
1 82  LEU n 
1 83  ALA n 
1 84  TRP n 
1 85  ALA n 
1 86  GLN n 
1 87  ALA n 
1 88  PRO n 
1 89  ILE n 
1 90  GLY n 
1 91  TYR n 
1 92  SER n 
1 93  LEU n 
1 94  SER n 
1 95  LEU n 
1 96  ILE n 
1 97  LEU n 
1 98  GLY n 
1 99  GLY n 
1 100 LEU n 
1 101 PHE n 
1 102 PHE n 
1 103 ALA n 
1 104 LYS n 
1 105 PRO n 
1 106 MET n 
1 107 ARG n 
1 108 SER n 
1 109 LYS n 
1 110 GLY n 
1 111 TYR n 
1 112 VAL n 
1 113 THR n 
1 114 MET n 
1 115 LEU n 
1 116 ASP n 
1 117 PRO n 
1 118 PHE n 
1 119 GLN n 
1 120 GLN n 
1 121 ILE n 
1 122 TYR n 
1 123 GLY n 
1 124 LYS n 
1 125 ARG n 
1 126 MET n 
1 127 GLY n 
1 128 GLY n 
1 129 LEU n 
1 130 LEU n 
1 131 PHE n 
1 132 ILE n 
1 133 PRO n 
1 134 ALA n 
1 135 LEU n 
1 136 MET n 
1 137 GLY n 
1 138 GLU n 
1 139 MET n 
1 140 PHE n 
1 141 TRP n 
1 142 ALA n 
1 143 ALA n 
1 144 ALA n 
1 145 ILE n 
1 146 PHE n 
1 147 SER n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 ALA n 
1 152 THR n 
1 153 ILE n 
1 154 SER n 
1 155 VAL n 
1 156 ILE n 
1 157 ILE n 
1 158 ASP n 
1 159 VAL n 
1 160 ASP n 
1 161 MET n 
1 162 HIS n 
1 163 ILE n 
1 164 SER n 
1 165 VAL n 
1 166 ILE n 
1 167 ILE n 
1 168 SER n 
1 169 ALA n 
1 170 LEU n 
1 171 ILE n 
1 172 ALA n 
1 173 THR n 
1 174 LEU n 
1 175 TYR n 
1 176 THR n 
1 177 LEU n 
1 178 VAL n 
1 179 GLY n 
1 180 GLY n 
1 181 LEU n 
1 182 TYR n 
1 183 SER n 
1 184 VAL n 
1 185 ALA n 
1 186 TYR n 
1 187 THR n 
1 188 ASP n 
1 189 VAL n 
1 190 VAL n 
1 191 GLN n 
1 192 LEU n 
1 193 PHE n 
1 194 CYS n 
1 195 ILE n 
1 196 PHE n 
1 197 VAL n 
1 198 GLY n 
1 199 LEU n 
1 200 TRP n 
1 201 ILE n 
1 202 SER n 
1 203 VAL n 
1 204 PRO n 
1 205 PHE n 
1 206 ALA n 
1 207 LEU n 
1 208 SER n 
1 209 HIS n 
1 210 PRO n 
1 211 ALA n 
1 212 VAL n 
1 213 ALA n 
1 214 ASP n 
1 215 ILE n 
1 216 GLY n 
1 217 PHE n 
1 218 THR n 
1 219 ALA n 
1 220 VAL n 
1 221 HIS n 
1 222 ALA n 
1 223 LYS n 
1 224 TYR n 
1 225 GLN n 
1 226 LYS n 
1 227 PRO n 
1 228 TRP n 
1 229 LEU n 
1 230 GLY n 
1 231 THR n 
1 232 VAL n 
1 233 ASP n 
1 234 SER n 
1 235 SER n 
1 236 GLU n 
1 237 VAL n 
1 238 TYR n 
1 239 SER n 
1 240 TRP n 
1 241 LEU n 
1 242 ASP n 
1 243 SER n 
1 244 PHE n 
1 245 LEU n 
1 246 LEU n 
1 247 LEU n 
1 248 MET n 
1 249 LEU n 
1 250 GLY n 
1 251 GLY n 
1 252 ILE n 
1 253 PRO n 
1 254 TRP n 
1 255 GLN n 
1 256 ALA n 
1 257 TYR n 
1 258 PHE n 
1 259 GLN n 
1 260 ARG n 
1 261 VAL n 
1 262 LEU n 
1 263 SER n 
1 264 SER n 
1 265 SER n 
1 266 SER n 
1 267 ALA n 
1 268 THR n 
1 269 TYR n 
1 270 ALA n 
1 271 GLN n 
1 272 VAL n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 LEU n 
1 277 ALA n 
1 278 ALA n 
1 279 PHE n 
1 280 GLY n 
1 281 CYS n 
1 282 LEU n 
1 283 VAL n 
1 284 MET n 
1 285 ALA n 
1 286 ILE n 
1 287 PRO n 
1 288 ALA n 
1 289 ILE n 
1 290 LEU n 
1 291 ILE n 
1 292 GLY n 
1 293 ALA n 
1 294 ILE n 
1 295 GLY n 
1 296 ALA n 
1 297 SER n 
1 298 THR n 
1 299 ASP n 
1 300 TRP n 
1 301 ASN n 
1 302 GLN n 
1 303 THR n 
1 304 ALA n 
1 305 TYR n 
1 306 GLY n 
1 307 LEU n 
1 308 PRO n 
1 309 ASP n 
1 310 PRO n 
1 311 LYS n 
1 312 THR n 
1 313 THR n 
1 314 GLU n 
1 315 GLU n 
1 316 ALA n 
1 317 ASP n 
1 318 MET n 
1 319 ILE n 
1 320 LEU n 
1 321 PRO n 
1 322 ILE n 
1 323 VAL n 
1 324 LEU n 
1 325 GLN n 
1 326 TYR n 
1 327 LEU n 
1 328 CYS n 
1 329 PRO n 
1 330 VAL n 
1 331 TYR n 
1 332 ILE n 
1 333 SER n 
1 334 PHE n 
1 335 PHE n 
1 336 GLY n 
1 337 LEU n 
1 338 GLY n 
1 339 ALA n 
1 340 VAL n 
1 341 SER n 
1 342 ALA n 
1 343 ALA n 
1 344 VAL n 
1 345 MET n 
1 346 SER n 
1 347 SER n 
1 348 ALA n 
1 349 ASP n 
1 350 SER n 
1 351 SER n 
1 352 ILE n 
1 353 LEU n 
1 354 SER n 
1 355 ALA n 
1 356 SER n 
1 357 SER n 
1 358 MET n 
1 359 PHE n 
1 360 ALA n 
1 361 ARG n 
1 362 ASN n 
1 363 ILE n 
1 364 TYR n 
1 365 GLN n 
1 366 LEU n 
1 367 SER n 
1 368 PHE n 
1 369 ARG n 
1 370 GLN n 
1 371 ASN n 
1 372 ALA n 
1 373 SER n 
1 374 ASP n 
1 375 LYS n 
1 376 GLU n 
1 377 ILE n 
1 378 VAL n 
1 379 TRP n 
1 380 VAL n 
1 381 MET n 
1 382 ARG n 
1 383 ILE n 
1 384 THR n 
1 385 VAL n 
1 386 PHE n 
1 387 VAL n 
1 388 PHE n 
1 389 GLY n 
1 390 ALA n 
1 391 SER n 
1 392 ALA n 
1 393 THR n 
1 394 ALA n 
1 395 MET n 
1 396 ALA n 
1 397 LEU n 
1 398 LEU n 
1 399 THR n 
1 400 LYS n 
1 401 THR n 
1 402 VAL n 
1 403 TYR n 
1 404 GLY n 
1 405 LEU n 
1 406 TRP n 
1 407 TYR n 
1 408 LEU n 
1 409 SER n 
1 410 SER n 
1 411 ASP n 
1 412 LEU n 
1 413 VAL n 
1 414 TYR n 
1 415 ILE n 
1 416 VAL n 
1 417 ILE n 
1 418 PHE n 
1 419 PRO n 
1 420 GLN n 
1 421 LEU n 
1 422 LEU n 
1 423 CYS n 
1 424 VAL n 
1 425 LEU n 
1 426 PHE n 
1 427 VAL n 
1 428 LYS n 
1 429 GLY n 
1 430 THR n 
1 431 ASN n 
1 432 THR n 
1 433 TYR n 
1 434 GLY n 
1 435 ALA n 
1 436 VAL n 
1 437 ALA n 
1 438 GLY n 
1 439 TYR n 
1 440 VAL n 
1 441 SER n 
1 442 GLY n 
1 443 LEU n 
1 444 PHE n 
1 445 LEU n 
1 446 ARG n 
1 447 ILE n 
1 448 THR n 
1 449 GLY n 
1 450 GLY n 
1 451 GLU n 
1 452 PRO n 
1 453 TYR n 
1 454 LEU n 
1 455 TYR n 
1 456 LEU n 
1 457 GLN n 
1 458 PRO n 
1 459 LEU n 
1 460 ILE n 
1 461 PHE n 
1 462 TYR n 
1 463 PRO n 
1 464 GLY n 
1 465 TYR n 
1 466 TYR n 
1 467 PRO n 
1 468 ASP n 
1 469 ASP n 
1 470 ASN n 
1 471 GLY n 
1 472 ILE n 
1 473 TYR n 
1 474 ASN n 
1 475 GLN n 
1 476 LYS n 
1 477 PHE n 
1 478 PRO n 
1 479 PHE n 
1 480 LYS n 
1 481 THR n 
1 482 LEU n 
1 483 ALA n 
1 484 MET n 
1 485 VAL n 
1 486 THR n 
1 487 SER n 
1 488 PHE n 
1 489 LEU n 
1 490 THR n 
1 491 ASN n 
1 492 ILE n 
1 493 CYS n 
1 494 ILE n 
1 495 SER n 
1 496 TYR n 
1 497 LEU n 
1 498 ALA n 
1 499 LYS n 
1 500 TYR n 
1 501 LEU n 
1 502 PHE n 
1 503 GLU n 
1 504 SER n 
1 505 GLY n 
1 506 THR n 
1 507 LEU n 
1 508 PRO n 
1 509 PRO n 
1 510 LYS n 
1 511 LEU n 
1 512 ASP n 
1 513 VAL n 
1 514 PHE n 
1 515 ASP n 
1 516 ALA n 
1 517 VAL n 
1 518 VAL n 
1 519 ALA n 
1 520 ARG n 
1 521 HIS n 
1 522 SER n 
1 523 GLU n 
1 524 GLU n 
1 525 ASN n 
1 526 MET n 
1 527 ASP n 
1 528 LYS n 
1 529 THR n 
1 530 ILE n 
1 531 LEU n 
1 532 VAL n 
1 533 LYS n 
1 534 ASN n 
1 535 GLU n 
1 536 ASN n 
1 537 ILE n 
1 538 LYS n 
1 539 LEU n 
1 540 ASP n 
1 541 GLU n 
1 542 LEU n 
1 543 ALA n 
1 544 LEU n 
1 545 VAL n 
1 546 LYS n 
1 547 PRO n 
1 548 ARG n 
1 549 GLN n 
1 550 SER n 
1 551 MET n 
1 552 THR n 
1 553 LEU n 
1 554 SER n 
1 555 SER n 
1 556 THR n 
1 557 PHE n 
1 558 THR n 
1 559 ASN n 
1 560 LYS n 
1 561 GLU n 
1 562 ALA n 
1 563 PHE n 
1 564 LEU n 
1 565 ASP n 
1 566 VAL n 
1 567 ASP n 
1 568 SER n 
1 569 SER n 
1 570 PRO n 
1 571 GLU n 
1 572 GLY n 
1 573 SER n 
1 574 GLY n 
1 575 THR n 
1 576 GLU n 
1 577 ASP n 
1 578 ASN n 
1 579 LEU n 
1 580 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   580 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC5A7, CHT1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            'HEK 293-F' 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
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 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                                                         
'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'       180.156 
CL  non-polymer                  . 'CHLORIDE ION'                                                               ? 'Cl -1' 35.453  
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  
HC6 non-polymer                  . "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" ? 
'C24 H34 N2 O4 2' 414.538 
HIS 'L-peptide linking'          y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer                  . WATER                                                                        ? 'H2 O' 18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                                                                   ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking'          y LEUCINE                                                                      ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking'          y LYSINE                                                                       ? 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking'          y METHIONINE                                                                   ? 'C5 H11 N O2 S' 
149.211 
NA  non-polymer                  . 'SODIUM ION'                                                                 ? 'Na 1' 22.990  
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 
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 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
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   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  TRP 27  27  27  TRP TRP A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  MET 58  58  58  MET MET A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  TRP 84  84  84  TRP TRP A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 MET 114 114 114 MET MET A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 MET 126 126 126 MET MET A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 TRP 141 141 141 TRP TRP A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 MET 161 161 161 MET MET A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 CYS 194 194 194 CYS CYS A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 GLN 225 225 225 GLN GLN A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 TRP 228 228 228 TRP TRP A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 TRP 240 240 240 TRP TRP A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 MET 248 248 248 MET MET A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 CYS 281 281 281 CYS CYS A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 MET 284 284 284 MET MET A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 THR 298 298 298 THR THR A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 ILE 319 319 319 ILE ILE A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 PRO 321 321 321 PRO PRO A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 MET 345 345 345 MET MET A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 SER 354 354 354 SER SER A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 MET 358 358 358 MET MET A . n 
A 1 359 PHE 359 359 359 PHE PHE A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 ARG 361 361 361 ARG ARG A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 GLN 365 365 365 GLN GLN A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 SER 367 367 367 SER SER A . n 
A 1 368 PHE 368 368 368 PHE PHE A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 TRP 379 379 379 TRP TRP A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 MET 381 381 381 MET MET A . n 
A 1 382 ARG 382 382 382 ARG ARG A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 MET 395 395 395 MET MET A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ASP 411 411 411 ASP ASP A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 VAL 416 416 416 VAL VAL A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 PRO 419 419 419 PRO PRO A . n 
A 1 420 GLN 420 420 420 GLN GLN A . n 
A 1 421 LEU 421 421 421 LEU LEU A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 CYS 423 423 423 CYS CYS A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 LYS 428 428 428 LYS LYS A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 THR 430 430 430 THR THR A . n 
A 1 431 ASN 431 431 431 ASN ASN A . n 
A 1 432 THR 432 432 432 THR THR A . n 
A 1 433 TYR 433 433 433 TYR TYR A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 ALA 435 435 435 ALA ALA A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 TYR 439 439 439 TYR TYR A . n 
A 1 440 VAL 440 440 440 VAL VAL A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 GLY 442 442 442 GLY GLY A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ILE 447 447 447 ILE ILE A . n 
A 1 448 THR 448 448 448 THR THR A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 PRO 452 452 452 PRO PRO A . n 
A 1 453 TYR 453 453 453 TYR TYR A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 TYR 455 455 455 TYR TYR A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 PRO 458 458 458 PRO PRO A . n 
A 1 459 LEU 459 459 459 LEU LEU A . n 
A 1 460 ILE 460 460 460 ILE ILE A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 TYR 462 462 462 TYR TYR A . n 
A 1 463 PRO 463 463 463 PRO PRO A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 TYR 466 466 466 TYR TYR A . n 
A 1 467 PRO 467 467 467 PRO PRO A . n 
A 1 468 ASP 468 468 468 ASP ASP A . n 
A 1 469 ASP 469 469 469 ASP ASP A . n 
A 1 470 ASN 470 470 470 ASN ASN A . n 
A 1 471 GLY 471 471 471 GLY GLY A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 TYR 473 473 473 TYR TYR A . n 
A 1 474 ASN 474 474 474 ASN ASN A . n 
A 1 475 GLN 475 475 475 GLN GLN A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 PHE 477 477 477 PHE PHE A . n 
A 1 478 PRO 478 478 478 PRO PRO A . n 
A 1 479 PHE 479 479 479 PHE PHE A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 ALA 483 483 483 ALA ALA A . n 
A 1 484 MET 484 484 484 MET MET A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 THR 486 486 486 THR THR A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 PHE 488 488 488 PHE PHE A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 ASN 491 491 491 ASN ASN A . n 
A 1 492 ILE 492 492 492 ILE ILE A . n 
A 1 493 CYS 493 493 493 CYS CYS A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 SER 495 495 495 SER SER A . n 
A 1 496 TYR 496 496 496 TYR TYR A . n 
A 1 497 LEU 497 497 497 LEU LEU A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 LYS 499 499 499 LYS LYS A . n 
A 1 500 TYR 500 500 500 TYR TYR A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 PHE 502 502 502 PHE PHE A . n 
A 1 503 GLU 503 503 503 GLU GLU A . n 
A 1 504 SER 504 504 504 SER SER A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 THR 506 506 506 THR THR A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 PRO 508 508 508 PRO PRO A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 ASP 512 512 512 ASP ASP A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 ALA 516 516 516 ALA ALA A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 VAL 518 518 ?   ?   ?   A . n 
A 1 519 ALA 519 519 ?   ?   ?   A . n 
A 1 520 ARG 520 520 ?   ?   ?   A . n 
A 1 521 HIS 521 521 ?   ?   ?   A . n 
A 1 522 SER 522 522 ?   ?   ?   A . n 
A 1 523 GLU 523 523 ?   ?   ?   A . n 
A 1 524 GLU 524 524 ?   ?   ?   A . n 
A 1 525 ASN 525 525 ?   ?   ?   A . n 
A 1 526 MET 526 526 ?   ?   ?   A . n 
A 1 527 ASP 527 527 ?   ?   ?   A . n 
A 1 528 LYS 528 528 ?   ?   ?   A . n 
A 1 529 THR 529 529 ?   ?   ?   A . n 
A 1 530 ILE 530 530 ?   ?   ?   A . n 
A 1 531 LEU 531 531 ?   ?   ?   A . n 
A 1 532 VAL 532 532 ?   ?   ?   A . n 
A 1 533 LYS 533 533 ?   ?   ?   A . n 
A 1 534 ASN 534 534 ?   ?   ?   A . n 
A 1 535 GLU 535 535 ?   ?   ?   A . n 
A 1 536 ASN 536 536 ?   ?   ?   A . n 
A 1 537 ILE 537 537 ?   ?   ?   A . n 
A 1 538 LYS 538 538 ?   ?   ?   A . n 
A 1 539 LEU 539 539 ?   ?   ?   A . n 
A 1 540 ASP 540 540 ?   ?   ?   A . n 
A 1 541 GLU 541 541 ?   ?   ?   A . n 
A 1 542 LEU 542 542 ?   ?   ?   A . n 
A 1 543 ALA 543 543 ?   ?   ?   A . n 
A 1 544 LEU 544 544 ?   ?   ?   A . n 
A 1 545 VAL 545 545 ?   ?   ?   A . n 
A 1 546 LYS 546 546 ?   ?   ?   A . n 
A 1 547 PRO 547 547 ?   ?   ?   A . n 
A 1 548 ARG 548 548 ?   ?   ?   A . n 
A 1 549 GLN 549 549 ?   ?   ?   A . n 
A 1 550 SER 550 550 ?   ?   ?   A . n 
A 1 551 MET 551 551 ?   ?   ?   A . n 
A 1 552 THR 552 552 ?   ?   ?   A . n 
A 1 553 LEU 553 553 ?   ?   ?   A . n 
A 1 554 SER 554 554 ?   ?   ?   A . n 
A 1 555 SER 555 555 ?   ?   ?   A . n 
A 1 556 THR 556 556 ?   ?   ?   A . n 
A 1 557 PHE 557 557 ?   ?   ?   A . n 
A 1 558 THR 558 558 ?   ?   ?   A . n 
A 1 559 ASN 559 559 ?   ?   ?   A . n 
A 1 560 LYS 560 560 ?   ?   ?   A . n 
A 1 561 GLU 561 561 ?   ?   ?   A . n 
A 1 562 ALA 562 562 ?   ?   ?   A . n 
A 1 563 PHE 563 563 ?   ?   ?   A . n 
A 1 564 LEU 564 564 ?   ?   ?   A . n 
A 1 565 ASP 565 565 ?   ?   ?   A . n 
A 1 566 VAL 566 566 ?   ?   ?   A . n 
A 1 567 ASP 567 567 ?   ?   ?   A . n 
A 1 568 SER 568 568 ?   ?   ?   A . n 
A 1 569 SER 569 569 ?   ?   ?   A . n 
A 1 570 PRO 570 570 ?   ?   ?   A . n 
A 1 571 GLU 571 571 ?   ?   ?   A . n 
A 1 572 GLY 572 572 ?   ?   ?   A . n 
A 1 573 SER 573 573 ?   ?   ?   A . n 
A 1 574 GLY 574 574 ?   ?   ?   A . n 
A 1 575 THR 575 575 ?   ?   ?   A . n 
A 1 576 GLU 576 576 ?   ?   ?   A . n 
A 1 577 ASP 577 577 ?   ?   ?   A . n 
A 1 578 ASN 578 578 ?   ?   ?   A . n 
A 1 579 LEU 579 579 ?   ?   ?   A . n 
A 1 580 GLN 580 580 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 A NAG 518 n 
B 2 NAG 2 B NAG 2 A NAG 519 n 
B 2 BMA 3 B BMA 3 A BMA 520 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HC6 ? ? HC6 ? ? 'SUBJECT OF INVESTIGATION' ? 
3 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 NA  1 601 3   NA  NA  A . 
D 3 NA  1 602 4   NA  NA  A . 
E 4 HC6 1 603 521 HC6 HC6 A . 
F 5 CL  1 604 1   CL  CL  A . 
G 6 HOH 1 701 1   HOH HOH A . 
# 
_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                     8ZQO 
_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                         8ZQO 
_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                   8ZQO 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8ZQO 
_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' ? 0.003 ? 4143 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.521 ? 5665 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 3.939 ? 584  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.038 ? 660  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 683  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8ZQO 
_struct.title                        
'Human high-affinity choline transporter CHT1 bound to HC-3 under NaCl condition, with sodium and chloride ions coordinated.' 
_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        8ZQO 
_struct_keywords.text            'transporter, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL 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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SC5A7_HUMAN 
_struct_ref.pdbx_db_accession          Q9GZV3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQ
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZQO 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 580 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9GZV3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  580 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       580 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 4   ? THR A 29  ? HIS A 4   THR A 29  1 ? 26 
HELX_P HELX_P2  AA2 GLU A 37  ? GLY A 45  ? GLU A 37  GLY A 45  1 ? 9  
HELX_P HELX_P3  AA3 GLY A 50  ? VAL A 63  ? GLY A 50  VAL A 63  1 ? 14 
HELX_P HELX_P4  AA4 GLY A 64  ? VAL A 77  ? GLY A 64  VAL A 77  1 ? 14 
HELX_P HELX_P5  AA5 GLY A 81  ? ALA A 85  ? GLY A 81  ALA A 85  5 ? 5  
HELX_P HELX_P6  AA6 GLN A 86  ? PHE A 102 ? GLN A 86  PHE A 102 1 ? 17 
HELX_P HELX_P7  AA7 LYS A 104 ? LYS A 109 ? LYS A 104 LYS A 109 1 ? 6  
HELX_P HELX_P8  AA8 MET A 114 ? GLY A 123 ? MET A 114 GLY A 123 1 ? 10 
HELX_P HELX_P9  AA9 GLY A 123 ? LEU A 130 ? GLY A 123 LEU A 130 1 ? 8  
HELX_P HELX_P10 AB1 LEU A 130 ? ILE A 157 ? LEU A 130 ILE A 157 1 ? 28 
HELX_P HELX_P11 AB2 ASP A 160 ? GLY A 179 ? ASP A 160 GLY A 179 1 ? 20 
HELX_P HELX_P12 AB3 GLY A 180 ? SER A 208 ? GLY A 180 SER A 208 1 ? 29 
HELX_P HELX_P13 AB4 ASP A 214 ? ALA A 219 ? ASP A 214 ALA A 219 1 ? 6  
HELX_P HELX_P14 AB5 GLU A 236 ? GLY A 250 ? GLU A 236 GLY A 250 1 ? 15 
HELX_P HELX_P15 AB6 TRP A 254 ? LEU A 262 ? TRP A 254 LEU A 262 1 ? 9  
HELX_P HELX_P16 AB7 SER A 266 ? ALA A 285 ? SER A 266 ALA A 285 1 ? 20 
HELX_P HELX_P17 AB8 ALA A 285 ? SER A 297 ? ALA A 285 SER A 297 1 ? 13 
HELX_P HELX_P18 AB9 ASP A 299 ? THR A 303 ? ASP A 299 THR A 303 5 ? 5  
HELX_P HELX_P19 AC1 GLU A 315 ? ASP A 317 ? GLU A 315 ASP A 317 5 ? 3  
HELX_P HELX_P20 AC2 MET A 318 ? CYS A 328 ? MET A 318 CYS A 328 1 ? 11 
HELX_P HELX_P21 AC3 PRO A 329 ? ILE A 363 ? PRO A 329 ILE A 363 1 ? 35 
HELX_P HELX_P22 AC4 ILE A 363 ? PHE A 368 ? ILE A 363 PHE A 368 1 ? 6  
HELX_P HELX_P23 AC5 SER A 373 ? THR A 399 ? SER A 373 THR A 399 1 ? 27 
HELX_P HELX_P24 AC6 THR A 401 ? VAL A 427 ? THR A 401 VAL A 427 1 ? 27 
HELX_P HELX_P25 AC7 ASN A 431 ? THR A 448 ? ASN A 431 THR A 448 1 ? 18 
HELX_P HELX_P26 AC8 GLU A 451 ? TYR A 455 ? GLU A 451 TYR A 455 5 ? 5  
HELX_P HELX_P27 AC9 PRO A 478 ? SER A 504 ? PRO A 478 SER A 504 1 ? 27 
HELX_P HELX_P28 AD1 PRO A 508 ? ASP A 512 ? PRO A 508 ASP A 512 5 ? 5  
# 
_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 301 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 301 B NAG 1   1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale2  covale both ? B NAG .   O4  ? ? ? 1_555 B NAG . C1 ? ? B NAG 1   B NAG 2   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale3  covale both ? B NAG .   O4  ? ? ? 1_555 B BMA . C1 ? ? B NAG 2   B BMA 3   1_555 ? ? ? ? ? ? ? 1.448 ? ?               
metalc1  metalc ?    ? A ALA 60  O   ? ? ? 1_555 C NA  . NA ? ? A ALA 60  A NA  601 1_555 ? ? ? ? ? ? ? 2.271 ? ?               
metalc2  metalc ?    ? A VAL 63  O   ? ? ? 1_555 C NA  . NA ? ? A VAL 63  A NA  601 1_555 ? ? ? ? ? ? ? 2.232 ? ?               
metalc3  metalc ?    ? A ASP 188 OD1 ? ? ? 1_555 D NA  . NA ? ? A ASP 188 A NA  602 1_555 ? ? ? ? ? ? ? 2.676 ? ?               
metalc4  metalc ?    ? A ASP 188 OD2 ? ? ? 1_555 D NA  . NA ? ? A ASP 188 A NA  602 1_555 ? ? ? ? ? ? ? 2.155 ? ?               
metalc5  metalc ?    ? A ALA 343 O   ? ? ? 1_555 C NA  . NA ? ? A ALA 343 A NA  601 1_555 ? ? ? ? ? ? ? 2.716 ? ?               
metalc6  metalc ?    ? A SER 346 OG  ? ? ? 1_555 C NA  . NA ? ? A SER 346 A NA  601 1_555 ? ? ? ? ? ? ? 2.189 ? ?               
metalc7  metalc ?    ? A SER 346 O   ? ? ? 1_555 D NA  . NA ? ? A SER 346 A NA  602 1_555 ? ? ? ? ? ? ? 2.483 ? ?               
metalc8  metalc ?    ? A SER 347 OG  ? ? ? 1_555 C NA  . NA ? ? A SER 347 A NA  601 1_555 ? ? ? ? ? ? ? 2.966 ? ?               
metalc9  metalc ?    ? A ASP 349 OD1 ? ? ? 1_555 D NA  . NA ? ? A ASP 349 A NA  602 1_555 ? ? ? ? ? ? ? 2.943 ? ?               
metalc10 metalc ?    ? A SER 350 OG  ? ? ? 1_555 D NA  . NA ? ? A SER 350 A NA  602 1_555 ? ? ? ? ? ? ? 2.173 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ALA 60  ? A ALA 60  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A VAL 63  ? A VAL 63  ? 1_555 102.7 ? 
2  O   ? A ALA 60  ? A ALA 60  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A ALA 343 ? A ALA 343 ? 1_555 161.7 ? 
3  O   ? A VAL 63  ? A VAL 63  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A ALA 343 ? A ALA 343 ? 1_555 95.5  ? 
4  O   ? A ALA 60  ? A ALA 60  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 346 ? A SER 346 ? 1_555 90.6  ? 
5  O   ? A VAL 63  ? A VAL 63  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 346 ? A SER 346 ? 1_555 132.4 ? 
6  O   ? A ALA 343 ? A ALA 343 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 346 ? A SER 346 ? 1_555 74.9  ? 
7  O   ? A ALA 60  ? A ALA 60  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 347 ? A SER 347 ? 1_555 94.3  ? 
8  O   ? A VAL 63  ? A VAL 63  ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 347 ? A SER 347 ? 1_555 105.9 ? 
9  O   ? A ALA 343 ? A ALA 343 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 347 ? A SER 347 ? 1_555 83.2  ? 
10 OG  ? A SER 346 ? A SER 346 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OG  ? A SER 347 ? A SER 347 ? 1_555 118.6 ? 
11 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OD2 ? A ASP 188 ? A ASP 188 ? 1_555 52.6  ? 
12 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A SER 346 ? A SER 346 ? 1_555 94.7  ? 
13 OD2 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A SER 346 ? A SER 346 ? 1_555 134.8 ? 
14 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 94.9  ? 
15 OD2 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 136.4 ? 
16 O   ? A SER 346 ? A SER 346 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 65.7  ? 
17 OD1 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OG  ? A SER 350 ? A SER 350 ? 1_555 165.5 ? 
18 OD2 ? A ASP 188 ? A ASP 188 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OG  ? A SER 350 ? A SER 350 ? 1_555 135.7 ? 
19 O   ? A SER 346 ? A SER 346 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OG  ? A SER 350 ? A SER 350 ? 1_555 83.9  ? 
20 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 OG  ? A SER 350 ? A SER 350 ? 1_555 71.4  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      NAG 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     ASN 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      301 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       NAG 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        1 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      ASN 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       301 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C1 
_pdbx_modification_feature.modified_residue_id_linking_atom   ND2 
_pdbx_modification_feature.modified_residue_id                ASN 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        NAG 
_pdbx_modification_feature.type                               N-Glycosylation 
_pdbx_modification_feature.category                           Carbohydrate 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           307 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            307 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    308 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     308 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.41 
# 
_pdbx_entry_details.entry_id                   8ZQO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 103 ? ? 73.04   -11.29  
2 1 ILE A 363 ? ? -90.64  -64.92  
3 1 ASP A 468 ? ? -121.16 -169.51 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8ZQO 
_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      'AB INITIO MODEL' 
# 
_em_3d_reconstruction.entry_id                    8ZQO 
_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                  2.8 
_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               842831 
_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            7.5 
# 
_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                 
'Human high-affinity choline transporter CHT1 bound to HC-3 under NaCl condition, with sodium and chloride ions coordinated.' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8ZQO 
_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                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             2200 
_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_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8ZQO 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8ZQO 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8ZQO 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A VAL 518 ? A VAL 518 
4  1 Y 1 A ALA 519 ? A ALA 519 
5  1 Y 1 A ARG 520 ? A ARG 520 
6  1 Y 1 A HIS 521 ? A HIS 521 
7  1 Y 1 A SER 522 ? A SER 522 
8  1 Y 1 A GLU 523 ? A GLU 523 
9  1 Y 1 A GLU 524 ? A GLU 524 
10 1 Y 1 A ASN 525 ? A ASN 525 
11 1 Y 1 A MET 526 ? A MET 526 
12 1 Y 1 A ASP 527 ? A ASP 527 
13 1 Y 1 A LYS 528 ? A LYS 528 
14 1 Y 1 A THR 529 ? A THR 529 
15 1 Y 1 A ILE 530 ? A ILE 530 
16 1 Y 1 A LEU 531 ? A LEU 531 
17 1 Y 1 A VAL 532 ? A VAL 532 
18 1 Y 1 A LYS 533 ? A LYS 533 
19 1 Y 1 A ASN 534 ? A ASN 534 
20 1 Y 1 A GLU 535 ? A GLU 535 
21 1 Y 1 A ASN 536 ? A ASN 536 
22 1 Y 1 A ILE 537 ? A ILE 537 
23 1 Y 1 A LYS 538 ? A LYS 538 
24 1 Y 1 A LEU 539 ? A LEU 539 
25 1 Y 1 A ASP 540 ? A ASP 540 
26 1 Y 1 A GLU 541 ? A GLU 541 
27 1 Y 1 A LEU 542 ? A LEU 542 
28 1 Y 1 A ALA 543 ? A ALA 543 
29 1 Y 1 A LEU 544 ? A LEU 544 
30 1 Y 1 A VAL 545 ? A VAL 545 
31 1 Y 1 A LYS 546 ? A LYS 546 
32 1 Y 1 A PRO 547 ? A PRO 547 
33 1 Y 1 A ARG 548 ? A ARG 548 
34 1 Y 1 A GLN 549 ? A GLN 549 
35 1 Y 1 A SER 550 ? A SER 550 
36 1 Y 1 A MET 551 ? A MET 551 
37 1 Y 1 A THR 552 ? A THR 552 
38 1 Y 1 A LEU 553 ? A LEU 553 
39 1 Y 1 A SER 554 ? A SER 554 
40 1 Y 1 A SER 555 ? A SER 555 
41 1 Y 1 A THR 556 ? A THR 556 
42 1 Y 1 A PHE 557 ? A PHE 557 
43 1 Y 1 A THR 558 ? A THR 558 
44 1 Y 1 A ASN 559 ? A ASN 559 
45 1 Y 1 A LYS 560 ? A LYS 560 
46 1 Y 1 A GLU 561 ? A GLU 561 
47 1 Y 1 A ALA 562 ? A ALA 562 
48 1 Y 1 A PHE 563 ? A PHE 563 
49 1 Y 1 A LEU 564 ? A LEU 564 
50 1 Y 1 A ASP 565 ? A ASP 565 
51 1 Y 1 A VAL 566 ? A VAL 566 
52 1 Y 1 A ASP 567 ? A ASP 567 
53 1 Y 1 A SER 568 ? A SER 568 
54 1 Y 1 A SER 569 ? A SER 569 
55 1 Y 1 A PRO 570 ? A PRO 570 
56 1 Y 1 A GLU 571 ? A GLU 571 
57 1 Y 1 A GLY 572 ? A GLY 572 
58 1 Y 1 A SER 573 ? A SER 573 
59 1 Y 1 A GLY 574 ? A GLY 574 
60 1 Y 1 A THR 575 ? A THR 575 
61 1 Y 1 A GLU 576 ? A GLU 576 
62 1 Y 1 A ASP 577 ? A ASP 577 
63 1 Y 1 A ASN 578 ? A ASN 578 
64 1 Y 1 A LEU 579 ? A LEU 579 
65 1 Y 1 A GLN 580 ? A GLN 580 
# 
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  
BMA C1   C  N R 74  
BMA C2   C  N S 75  
BMA C3   C  N S 76  
BMA C4   C  N S 77  
BMA C5   C  N R 78  
BMA C6   C  N N 79  
BMA O1   O  N N 80  
BMA O2   O  N N 81  
BMA O3   O  N N 82  
BMA O4   O  N N 83  
BMA O5   O  N N 84  
BMA O6   O  N N 85  
BMA H1   H  N N 86  
BMA H2   H  N N 87  
BMA H3   H  N N 88  
BMA H4   H  N N 89  
BMA H5   H  N N 90  
BMA H61  H  N N 91  
BMA H62  H  N N 92  
BMA HO1  H  N N 93  
BMA HO2  H  N N 94  
BMA HO3  H  N N 95  
BMA HO4  H  N N 96  
BMA HO6  H  N N 97  
CL  CL   CL N N 98  
CYS N    N  N N 99  
CYS CA   C  N R 100 
CYS C    C  N N 101 
CYS O    O  N N 102 
CYS CB   C  N N 103 
CYS SG   S  N N 104 
CYS OXT  O  N N 105 
CYS H    H  N N 106 
CYS H2   H  N N 107 
CYS HA   H  N N 108 
CYS HB2  H  N N 109 
CYS HB3  H  N N 110 
CYS HG   H  N N 111 
CYS HXT  H  N N 112 
GLN N    N  N N 113 
GLN CA   C  N S 114 
GLN C    C  N N 115 
GLN O    O  N N 116 
GLN CB   C  N N 117 
GLN CG   C  N N 118 
GLN CD   C  N N 119 
GLN OE1  O  N N 120 
GLN NE2  N  N N 121 
GLN OXT  O  N N 122 
GLN H    H  N N 123 
GLN H2   H  N N 124 
GLN HA   H  N N 125 
GLN HB2  H  N N 126 
GLN HB3  H  N N 127 
GLN HG2  H  N N 128 
GLN HG3  H  N N 129 
GLN HE21 H  N N 130 
GLN HE22 H  N N 131 
GLN HXT  H  N N 132 
GLU N    N  N N 133 
GLU CA   C  N S 134 
GLU C    C  N N 135 
GLU O    O  N N 136 
GLU CB   C  N N 137 
GLU CG   C  N N 138 
GLU CD   C  N N 139 
GLU OE1  O  N N 140 
GLU OE2  O  N N 141 
GLU OXT  O  N N 142 
GLU H    H  N N 143 
GLU H2   H  N N 144 
GLU HA   H  N N 145 
GLU HB2  H  N N 146 
GLU HB3  H  N N 147 
GLU HG2  H  N N 148 
GLU HG3  H  N N 149 
GLU HE2  H  N N 150 
GLU HXT  H  N N 151 
GLY N    N  N N 152 
GLY CA   C  N N 153 
GLY C    C  N N 154 
GLY O    O  N N 155 
GLY OXT  O  N N 156 
GLY H    H  N N 157 
GLY H2   H  N N 158 
GLY HA2  H  N N 159 
GLY HA3  H  N N 160 
GLY HXT  H  N N 161 
HC6 CAC  C  N N 162 
HC6 NAA  N  N N 163 
HC6 CBA  C  N N 164 
HC6 CBB  C  N N 165 
HC6 CAB  C  N N 166 
HC6 CAF  C  N N 167 
HC6 OAE  O  N N 168 
HC6 CAD  C  N S 169 
HC6 OBC  O  N N 170 
HC6 CAG  C  Y N 171 
HC6 CAL  C  Y N 172 
HC6 CAK  C  Y N 173 
HC6 CAH  C  Y N 174 
HC6 CAI  C  Y N 175 
HC6 CAJ  C  Y N 176 
HC6 CAM  C  Y N 177 
HC6 CAR  C  Y N 178 
HC6 CAQ  C  Y N 179 
HC6 CAN  C  Y N 180 
HC6 CAO  C  Y N 181 
HC6 CAP  C  Y N 182 
HC6 CAS  C  N S 183 
HC6 OBD  O  N N 184 
HC6 CAX  C  N N 185 
HC6 OAT  O  N N 186 
HC6 CAU  C  N N 187 
HC6 CAV  C  N N 188 
HC6 NAW  N  N N 189 
HC6 CAZ  C  N N 190 
HC6 CAY  C  N N 191 
HC6 HAC  H  N N 192 
HC6 HACA H  N N 193 
HC6 HBA  H  N N 194 
HC6 HBAA H  N N 195 
HC6 HBAB H  N N 196 
HC6 HBB  H  N N 197 
HC6 HBBA H  N N 198 
HC6 HBBB H  N N 199 
HC6 HAB  H  N N 200 
HC6 HABA H  N N 201 
HC6 HAF  H  N N 202 
HC6 HAFA H  N N 203 
HC6 HAL  H  N N 204 
HC6 HAK  H  N N 205 
HC6 HAH  H  N N 206 
HC6 HAI  H  N N 207 
HC6 HAR  H  N N 208 
HC6 HAQ  H  N N 209 
HC6 HAN  H  N N 210 
HC6 HAO  H  N N 211 
HC6 HAX  H  N N 212 
HC6 HAXA H  N N 213 
HC6 HAU  H  N N 214 
HC6 HAUA H  N N 215 
HC6 HAV  H  N N 216 
HC6 HAVA H  N N 217 
HC6 HAZ  H  N N 218 
HC6 HAZA H  N N 219 
HC6 HAZB H  N N 220 
HC6 HAY  H  N N 221 
HC6 HAYA H  N N 222 
HC6 HAYB H  N N 223 
HC6 H33  H  N N 224 
HC6 H34  H  N N 225 
HIS N    N  N N 226 
HIS CA   C  N S 227 
HIS C    C  N N 228 
HIS O    O  N N 229 
HIS CB   C  N N 230 
HIS CG   C  Y N 231 
HIS ND1  N  Y N 232 
HIS CD2  C  Y N 233 
HIS CE1  C  Y N 234 
HIS NE2  N  Y N 235 
HIS OXT  O  N N 236 
HIS H    H  N N 237 
HIS H2   H  N N 238 
HIS HA   H  N N 239 
HIS HB2  H  N N 240 
HIS HB3  H  N N 241 
HIS HD1  H  N N 242 
HIS HD2  H  N N 243 
HIS HE1  H  N N 244 
HIS HE2  H  N N 245 
HIS HXT  H  N N 246 
HOH O    O  N N 247 
HOH H1   H  N N 248 
HOH H2   H  N N 249 
ILE N    N  N N 250 
ILE CA   C  N S 251 
ILE C    C  N N 252 
ILE O    O  N N 253 
ILE CB   C  N S 254 
ILE CG1  C  N N 255 
ILE CG2  C  N N 256 
ILE CD1  C  N N 257 
ILE OXT  O  N N 258 
ILE H    H  N N 259 
ILE H2   H  N N 260 
ILE HA   H  N N 261 
ILE HB   H  N N 262 
ILE HG12 H  N N 263 
ILE HG13 H  N N 264 
ILE HG21 H  N N 265 
ILE HG22 H  N N 266 
ILE HG23 H  N N 267 
ILE HD11 H  N N 268 
ILE HD12 H  N N 269 
ILE HD13 H  N N 270 
ILE HXT  H  N N 271 
LEU N    N  N N 272 
LEU CA   C  N S 273 
LEU C    C  N N 274 
LEU O    O  N N 275 
LEU CB   C  N N 276 
LEU CG   C  N N 277 
LEU CD1  C  N N 278 
LEU CD2  C  N N 279 
LEU OXT  O  N N 280 
LEU H    H  N N 281 
LEU H2   H  N N 282 
LEU HA   H  N N 283 
LEU HB2  H  N N 284 
LEU HB3  H  N N 285 
LEU HG   H  N N 286 
LEU HD11 H  N N 287 
LEU HD12 H  N N 288 
LEU HD13 H  N N 289 
LEU HD21 H  N N 290 
LEU HD22 H  N N 291 
LEU HD23 H  N N 292 
LEU HXT  H  N N 293 
LYS N    N  N N 294 
LYS CA   C  N S 295 
LYS C    C  N N 296 
LYS O    O  N N 297 
LYS CB   C  N N 298 
LYS CG   C  N N 299 
LYS CD   C  N N 300 
LYS CE   C  N N 301 
LYS NZ   N  N N 302 
LYS OXT  O  N N 303 
LYS H    H  N N 304 
LYS H2   H  N N 305 
LYS HA   H  N N 306 
LYS HB2  H  N N 307 
LYS HB3  H  N N 308 
LYS HG2  H  N N 309 
LYS HG3  H  N N 310 
LYS HD2  H  N N 311 
LYS HD3  H  N N 312 
LYS HE2  H  N N 313 
LYS HE3  H  N N 314 
LYS HZ1  H  N N 315 
LYS HZ2  H  N N 316 
LYS HZ3  H  N N 317 
LYS HXT  H  N N 318 
MET N    N  N N 319 
MET CA   C  N S 320 
MET C    C  N N 321 
MET O    O  N N 322 
MET CB   C  N N 323 
MET CG   C  N N 324 
MET SD   S  N N 325 
MET CE   C  N N 326 
MET OXT  O  N N 327 
MET H    H  N N 328 
MET H2   H  N N 329 
MET HA   H  N N 330 
MET HB2  H  N N 331 
MET HB3  H  N N 332 
MET HG2  H  N N 333 
MET HG3  H  N N 334 
MET HE1  H  N N 335 
MET HE2  H  N N 336 
MET HE3  H  N N 337 
MET HXT  H  N N 338 
NA  NA   NA N N 339 
NAG C1   C  N R 340 
NAG C2   C  N R 341 
NAG C3   C  N R 342 
NAG C4   C  N S 343 
NAG C5   C  N R 344 
NAG C6   C  N N 345 
NAG C7   C  N N 346 
NAG C8   C  N N 347 
NAG N2   N  N N 348 
NAG O1   O  N N 349 
NAG O3   O  N N 350 
NAG O4   O  N N 351 
NAG O5   O  N N 352 
NAG O6   O  N N 353 
NAG O7   O  N N 354 
NAG H1   H  N N 355 
NAG H2   H  N N 356 
NAG H3   H  N N 357 
NAG H4   H  N N 358 
NAG H5   H  N N 359 
NAG H61  H  N N 360 
NAG H62  H  N N 361 
NAG H81  H  N N 362 
NAG H82  H  N N 363 
NAG H83  H  N N 364 
NAG HN2  H  N N 365 
NAG HO1  H  N N 366 
NAG HO3  H  N N 367 
NAG HO4  H  N N 368 
NAG HO6  H  N N 369 
PHE N    N  N N 370 
PHE CA   C  N S 371 
PHE C    C  N N 372 
PHE O    O  N N 373 
PHE CB   C  N N 374 
PHE CG   C  Y N 375 
PHE CD1  C  Y N 376 
PHE CD2  C  Y N 377 
PHE CE1  C  Y N 378 
PHE CE2  C  Y N 379 
PHE CZ   C  Y N 380 
PHE OXT  O  N N 381 
PHE H    H  N N 382 
PHE H2   H  N N 383 
PHE HA   H  N N 384 
PHE HB2  H  N N 385 
PHE HB3  H  N N 386 
PHE HD1  H  N N 387 
PHE HD2  H  N N 388 
PHE HE1  H  N N 389 
PHE HE2  H  N N 390 
PHE HZ   H  N N 391 
PHE HXT  H  N N 392 
PRO N    N  N N 393 
PRO CA   C  N S 394 
PRO C    C  N N 395 
PRO O    O  N N 396 
PRO CB   C  N N 397 
PRO CG   C  N N 398 
PRO CD   C  N N 399 
PRO OXT  O  N N 400 
PRO H    H  N N 401 
PRO HA   H  N N 402 
PRO HB2  H  N N 403 
PRO HB3  H  N N 404 
PRO HG2  H  N N 405 
PRO HG3  H  N N 406 
PRO HD2  H  N N 407 
PRO HD3  H  N N 408 
PRO HXT  H  N N 409 
SER N    N  N N 410 
SER CA   C  N S 411 
SER C    C  N N 412 
SER O    O  N N 413 
SER CB   C  N N 414 
SER OG   O  N N 415 
SER OXT  O  N N 416 
SER H    H  N N 417 
SER H2   H  N N 418 
SER HA   H  N N 419 
SER HB2  H  N N 420 
SER HB3  H  N N 421 
SER HG   H  N N 422 
SER HXT  H  N N 423 
THR N    N  N N 424 
THR CA   C  N S 425 
THR C    C  N N 426 
THR O    O  N N 427 
THR CB   C  N R 428 
THR OG1  O  N N 429 
THR CG2  C  N N 430 
THR OXT  O  N N 431 
THR H    H  N N 432 
THR H2   H  N N 433 
THR HA   H  N N 434 
THR HB   H  N N 435 
THR HG1  H  N N 436 
THR HG21 H  N N 437 
THR HG22 H  N N 438 
THR HG23 H  N N 439 
THR HXT  H  N N 440 
TRP N    N  N N 441 
TRP CA   C  N S 442 
TRP C    C  N N 443 
TRP O    O  N N 444 
TRP CB   C  N N 445 
TRP CG   C  Y N 446 
TRP CD1  C  Y N 447 
TRP CD2  C  Y N 448 
TRP NE1  N  Y N 449 
TRP CE2  C  Y N 450 
TRP CE3  C  Y N 451 
TRP CZ2  C  Y N 452 
TRP CZ3  C  Y N 453 
TRP CH2  C  Y N 454 
TRP OXT  O  N N 455 
TRP H    H  N N 456 
TRP H2   H  N N 457 
TRP HA   H  N N 458 
TRP HB2  H  N N 459 
TRP HB3  H  N N 460 
TRP HD1  H  N N 461 
TRP HE1  H  N N 462 
TRP HE3  H  N N 463 
TRP HZ2  H  N N 464 
TRP HZ3  H  N N 465 
TRP HH2  H  N N 466 
TRP HXT  H  N N 467 
TYR N    N  N N 468 
TYR CA   C  N S 469 
TYR C    C  N N 470 
TYR O    O  N N 471 
TYR CB   C  N N 472 
TYR CG   C  Y N 473 
TYR CD1  C  Y N 474 
TYR CD2  C  Y N 475 
TYR CE1  C  Y N 476 
TYR CE2  C  Y N 477 
TYR CZ   C  Y N 478 
TYR OH   O  N N 479 
TYR OXT  O  N N 480 
TYR H    H  N N 481 
TYR H2   H  N N 482 
TYR HA   H  N N 483 
TYR HB2  H  N N 484 
TYR HB3  H  N N 485 
TYR HD1  H  N N 486 
TYR HD2  H  N N 487 
TYR HE1  H  N N 488 
TYR HE2  H  N N 489 
TYR HH   H  N N 490 
TYR HXT  H  N N 491 
VAL N    N  N N 492 
VAL CA   C  N S 493 
VAL C    C  N N 494 
VAL O    O  N N 495 
VAL CB   C  N N 496 
VAL CG1  C  N N 497 
VAL CG2  C  N N 498 
VAL OXT  O  N N 499 
VAL H    H  N N 500 
VAL H2   H  N N 501 
VAL HA   H  N N 502 
VAL HB   H  N N 503 
VAL HG11 H  N N 504 
VAL HG12 H  N N 505 
VAL HG13 H  N N 506 
VAL HG21 H  N N 507 
VAL HG22 H  N N 508 
VAL HG23 H  N N 509 
VAL HXT  H  N N 510 
# 
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  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HC6 CAC NAA  sing N N 153 
HC6 CAC CAD  sing N N 154 
HC6 CAC HAC  sing N N 155 
HC6 CAC HACA sing N N 156 
HC6 NAA CBA  sing N N 157 
HC6 NAA CBB  sing N N 158 
HC6 NAA CAB  sing N N 159 
HC6 CBA HBA  sing N N 160 
HC6 CBA HBAA sing N N 161 
HC6 CBA HBAB sing N N 162 
HC6 CBB HBB  sing N N 163 
HC6 CBB HBBA sing N N 164 
HC6 CBB HBBB sing N N 165 
HC6 CAB CAF  sing N N 166 
HC6 CAB HAB  sing N N 167 
HC6 CAB HABA sing N N 168 
HC6 CAF OAE  sing N N 169 
HC6 CAF HAF  sing N N 170 
HC6 CAF HAFA sing N N 171 
HC6 OAE CAD  sing N N 172 
HC6 CAD OBC  sing N N 173 
HC6 CAD CAG  sing N N 174 
HC6 CAG CAL  doub Y N 175 
HC6 CAG CAH  sing Y N 176 
HC6 CAL CAK  sing Y N 177 
HC6 CAL HAL  sing N N 178 
HC6 CAK CAJ  doub Y N 179 
HC6 CAK HAK  sing N N 180 
HC6 CAH CAI  doub Y N 181 
HC6 CAH HAH  sing N N 182 
HC6 CAI CAJ  sing Y N 183 
HC6 CAI HAI  sing N N 184 
HC6 CAJ CAM  sing Y N 185 
HC6 CAM CAR  doub Y N 186 
HC6 CAM CAN  sing Y N 187 
HC6 CAR CAQ  sing Y N 188 
HC6 CAR HAR  sing N N 189 
HC6 CAQ CAP  doub Y N 190 
HC6 CAQ HAQ  sing N N 191 
HC6 CAN CAO  doub Y N 192 
HC6 CAN HAN  sing N N 193 
HC6 CAO CAP  sing Y N 194 
HC6 CAO HAO  sing N N 195 
HC6 CAP CAS  sing N N 196 
HC6 OBD CAS  sing N N 197 
HC6 CAS CAX  sing N N 198 
HC6 CAS OAT  sing N N 199 
HC6 CAX NAW  sing N N 200 
HC6 CAX HAX  sing N N 201 
HC6 CAX HAXA sing N N 202 
HC6 OAT CAU  sing N N 203 
HC6 CAU CAV  sing N N 204 
HC6 CAU HAU  sing N N 205 
HC6 CAU HAUA sing N N 206 
HC6 CAV NAW  sing N N 207 
HC6 CAV HAV  sing N N 208 
HC6 CAV HAVA sing N N 209 
HC6 NAW CAZ  sing N N 210 
HC6 NAW CAY  sing N N 211 
HC6 CAZ HAZ  sing N N 212 
HC6 CAZ HAZA sing N N 213 
HC6 CAZ HAZB sing N N 214 
HC6 CAY HAY  sing N N 215 
HC6 CAY HAYA sing N N 216 
HC6 CAY HAYB sing N N 217 
HC6 OBC H33  sing N N 218 
HC6 OBD H34  sing N N 219 
HIS N   CA   sing N N 220 
HIS N   H    sing N N 221 
HIS N   H2   sing N N 222 
HIS CA  C    sing N N 223 
HIS CA  CB   sing N N 224 
HIS CA  HA   sing N N 225 
HIS C   O    doub N N 226 
HIS C   OXT  sing N N 227 
HIS CB  CG   sing N N 228 
HIS CB  HB2  sing N N 229 
HIS CB  HB3  sing N N 230 
HIS CG  ND1  sing Y N 231 
HIS CG  CD2  doub Y N 232 
HIS ND1 CE1  doub Y N 233 
HIS ND1 HD1  sing N N 234 
HIS CD2 NE2  sing Y N 235 
HIS CD2 HD2  sing N N 236 
HIS CE1 NE2  sing Y N 237 
HIS CE1 HE1  sing N N 238 
HIS NE2 HE2  sing N N 239 
HIS OXT HXT  sing N N 240 
HOH O   H1   sing N N 241 
HOH O   H2   sing N N 242 
ILE N   CA   sing N N 243 
ILE N   H    sing N N 244 
ILE N   H2   sing N N 245 
ILE CA  C    sing N N 246 
ILE CA  CB   sing N N 247 
ILE CA  HA   sing N N 248 
ILE C   O    doub N N 249 
ILE C   OXT  sing N N 250 
ILE CB  CG1  sing N N 251 
ILE CB  CG2  sing N N 252 
ILE CB  HB   sing N N 253 
ILE CG1 CD1  sing N N 254 
ILE CG1 HG12 sing N N 255 
ILE CG1 HG13 sing N N 256 
ILE CG2 HG21 sing N N 257 
ILE CG2 HG22 sing N N 258 
ILE CG2 HG23 sing N N 259 
ILE CD1 HD11 sing N N 260 
ILE CD1 HD12 sing N N 261 
ILE CD1 HD13 sing N N 262 
ILE OXT HXT  sing N N 263 
LEU N   CA   sing N N 264 
LEU N   H    sing N N 265 
LEU N   H2   sing N N 266 
LEU CA  C    sing N N 267 
LEU CA  CB   sing N N 268 
LEU CA  HA   sing N N 269 
LEU C   O    doub N N 270 
LEU C   OXT  sing N N 271 
LEU CB  CG   sing N N 272 
LEU CB  HB2  sing N N 273 
LEU CB  HB3  sing N N 274 
LEU CG  CD1  sing N N 275 
LEU CG  CD2  sing N N 276 
LEU CG  HG   sing N N 277 
LEU CD1 HD11 sing N N 278 
LEU CD1 HD12 sing N N 279 
LEU CD1 HD13 sing N N 280 
LEU CD2 HD21 sing N N 281 
LEU CD2 HD22 sing N N 282 
LEU CD2 HD23 sing N N 283 
LEU OXT HXT  sing N N 284 
LYS N   CA   sing N N 285 
LYS N   H    sing N N 286 
LYS N   H2   sing N N 287 
LYS CA  C    sing N N 288 
LYS CA  CB   sing N N 289 
LYS CA  HA   sing N N 290 
LYS C   O    doub N N 291 
LYS C   OXT  sing N N 292 
LYS CB  CG   sing N N 293 
LYS CB  HB2  sing N N 294 
LYS CB  HB3  sing N N 295 
LYS CG  CD   sing N N 296 
LYS CG  HG2  sing N N 297 
LYS CG  HG3  sing N N 298 
LYS CD  CE   sing N N 299 
LYS CD  HD2  sing N N 300 
LYS CD  HD3  sing N N 301 
LYS CE  NZ   sing N N 302 
LYS CE  HE2  sing N N 303 
LYS CE  HE3  sing N N 304 
LYS NZ  HZ1  sing N N 305 
LYS NZ  HZ2  sing N N 306 
LYS NZ  HZ3  sing N N 307 
LYS OXT HXT  sing N N 308 
MET N   CA   sing N N 309 
MET N   H    sing N N 310 
MET N   H2   sing N N 311 
MET CA  C    sing N N 312 
MET CA  CB   sing N N 313 
MET CA  HA   sing N N 314 
MET C   O    doub N N 315 
MET C   OXT  sing N N 316 
MET CB  CG   sing N N 317 
MET CB  HB2  sing N N 318 
MET CB  HB3  sing N N 319 
MET CG  SD   sing N N 320 
MET CG  HG2  sing N N 321 
MET CG  HG3  sing N N 322 
MET SD  CE   sing N N 323 
MET CE  HE1  sing N N 324 
MET CE  HE2  sing N N 325 
MET CE  HE3  sing N N 326 
MET OXT HXT  sing N N 327 
NAG C1  C2   sing N N 328 
NAG C1  O1   sing N N 329 
NAG C1  O5   sing N N 330 
NAG C1  H1   sing N N 331 
NAG C2  C3   sing N N 332 
NAG C2  N2   sing N N 333 
NAG C2  H2   sing N N 334 
NAG C3  C4   sing N N 335 
NAG C3  O3   sing N N 336 
NAG C3  H3   sing N N 337 
NAG C4  C5   sing N N 338 
NAG C4  O4   sing N N 339 
NAG C4  H4   sing N N 340 
NAG C5  C6   sing N N 341 
NAG C5  O5   sing N N 342 
NAG C5  H5   sing N N 343 
NAG C6  O6   sing N N 344 
NAG C6  H61  sing N N 345 
NAG C6  H62  sing N N 346 
NAG C7  C8   sing N N 347 
NAG C7  N2   sing N N 348 
NAG C7  O7   doub N N 349 
NAG C8  H81  sing N N 350 
NAG C8  H82  sing N N 351 
NAG C8  H83  sing N N 352 
NAG N2  HN2  sing N N 353 
NAG O1  HO1  sing N N 354 
NAG O3  HO3  sing N N 355 
NAG O4  HO4  sing N N 356 
NAG O6  HO6  sing N N 357 
PHE N   CA   sing N N 358 
PHE N   H    sing N N 359 
PHE N   H2   sing N N 360 
PHE CA  C    sing N N 361 
PHE CA  CB   sing N N 362 
PHE CA  HA   sing N N 363 
PHE C   O    doub N N 364 
PHE C   OXT  sing N N 365 
PHE CB  CG   sing N N 366 
PHE CB  HB2  sing N N 367 
PHE CB  HB3  sing N N 368 
PHE CG  CD1  doub Y N 369 
PHE CG  CD2  sing Y N 370 
PHE CD1 CE1  sing Y N 371 
PHE CD1 HD1  sing N N 372 
PHE CD2 CE2  doub Y N 373 
PHE CD2 HD2  sing N N 374 
PHE CE1 CZ   doub Y N 375 
PHE CE1 HE1  sing N N 376 
PHE CE2 CZ   sing Y N 377 
PHE CE2 HE2  sing N N 378 
PHE CZ  HZ   sing N N 379 
PHE OXT HXT  sing N N 380 
PRO N   CA   sing N N 381 
PRO N   CD   sing N N 382 
PRO N   H    sing N N 383 
PRO CA  C    sing N N 384 
PRO CA  CB   sing N N 385 
PRO CA  HA   sing N N 386 
PRO C   O    doub N N 387 
PRO C   OXT  sing N N 388 
PRO CB  CG   sing N N 389 
PRO CB  HB2  sing N N 390 
PRO CB  HB3  sing N N 391 
PRO CG  CD   sing N N 392 
PRO CG  HG2  sing N N 393 
PRO CG  HG3  sing N N 394 
PRO CD  HD2  sing N N 395 
PRO CD  HD3  sing N N 396 
PRO OXT HXT  sing N N 397 
SER N   CA   sing N N 398 
SER N   H    sing N N 399 
SER N   H2   sing N N 400 
SER CA  C    sing N N 401 
SER CA  CB   sing N N 402 
SER CA  HA   sing N N 403 
SER C   O    doub N N 404 
SER C   OXT  sing N N 405 
SER CB  OG   sing N N 406 
SER CB  HB2  sing N N 407 
SER CB  HB3  sing N N 408 
SER OG  HG   sing N N 409 
SER OXT HXT  sing N N 410 
THR N   CA   sing N N 411 
THR N   H    sing N N 412 
THR N   H2   sing N N 413 
THR CA  C    sing N N 414 
THR CA  CB   sing N N 415 
THR CA  HA   sing N N 416 
THR C   O    doub N N 417 
THR C   OXT  sing N N 418 
THR CB  OG1  sing N N 419 
THR CB  CG2  sing N N 420 
THR CB  HB   sing N N 421 
THR OG1 HG1  sing N N 422 
THR CG2 HG21 sing N N 423 
THR CG2 HG22 sing N N 424 
THR CG2 HG23 sing N N 425 
THR OXT HXT  sing N N 426 
TRP N   CA   sing N N 427 
TRP N   H    sing N N 428 
TRP N   H2   sing N N 429 
TRP CA  C    sing N N 430 
TRP CA  CB   sing N N 431 
TRP CA  HA   sing N N 432 
TRP C   O    doub N N 433 
TRP C   OXT  sing N N 434 
TRP CB  CG   sing N N 435 
TRP CB  HB2  sing N N 436 
TRP CB  HB3  sing N N 437 
TRP CG  CD1  doub Y N 438 
TRP CG  CD2  sing Y N 439 
TRP CD1 NE1  sing Y N 440 
TRP CD1 HD1  sing N N 441 
TRP CD2 CE2  doub Y N 442 
TRP CD2 CE3  sing Y N 443 
TRP NE1 CE2  sing Y N 444 
TRP NE1 HE1  sing N N 445 
TRP CE2 CZ2  sing Y N 446 
TRP CE3 CZ3  doub Y N 447 
TRP CE3 HE3  sing N N 448 
TRP CZ2 CH2  doub Y N 449 
TRP CZ2 HZ2  sing N N 450 
TRP CZ3 CH2  sing Y N 451 
TRP CZ3 HZ3  sing N N 452 
TRP CH2 HH2  sing N N 453 
TRP OXT HXT  sing N N 454 
TYR N   CA   sing N N 455 
TYR N   H    sing N N 456 
TYR N   H2   sing N N 457 
TYR CA  C    sing N N 458 
TYR CA  CB   sing N N 459 
TYR CA  HA   sing N N 460 
TYR C   O    doub N N 461 
TYR C   OXT  sing N N 462 
TYR CB  CG   sing N N 463 
TYR CB  HB2  sing N N 464 
TYR CB  HB3  sing N N 465 
TYR CG  CD1  doub Y N 466 
TYR CG  CD2  sing Y N 467 
TYR CD1 CE1  sing Y N 468 
TYR CD1 HD1  sing N N 469 
TYR CD2 CE2  doub Y N 470 
TYR CD2 HD2  sing N N 471 
TYR CE1 CZ   doub Y N 472 
TYR CE1 HE1  sing N N 473 
TYR CE2 CZ   sing Y N 474 
TYR CE2 HE2  sing N N 475 
TYR CZ  OH   sing N N 476 
TYR OH  HH   sing N N 477 
TYR OXT HXT  sing N N 478 
VAL N   CA   sing N N 479 
VAL N   H    sing N N 480 
VAL N   H2   sing N N 481 
VAL CA  C    sing N N 482 
VAL CA  CB   sing N N 483 
VAL CA  HA   sing N N 484 
VAL C   O    doub N N 485 
VAL C   OXT  sing N N 486 
VAL CB  CG1  sing N N 487 
VAL CB  CG2  sing N N 488 
VAL CB  HB   sing N N 489 
VAL CG1 HG11 sing N N 490 
VAL CG1 HG12 sing N N 491 
VAL CG1 HG13 sing N N 492 
VAL CG2 HG21 sing N N 493 
VAL CG2 HG22 sing N N 494 
VAL CG2 HG23 sing N N 495 
VAL OXT HXT  sing N N 496 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-03 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8ZQO 
_em_admin.last_update        2025-02-26 
_em_admin.map_release_date   2024-12-04 
_em_admin.title              
'Human high-affinity choline transporter CHT1 bound to HC-3 under NaCl condition, with sodium and chloride ions coordinated.' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING ONLY' 
# 
_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                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_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         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (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                     ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   842831 
_em_particle_selection.reference_model          ? 
# 
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 ? ? cryoSPARC      ?           
'IMAGE ACQUISITION'             ? 2  ? ? 1 EPU            ?           
MASKING                         ? 3  ? ? ? ?              ?           
'CTF CORRECTION'                ? 4  1 ? ? ?              ?           
'LAYERLINE INDEXING'            ? 5  ? ? ? ?              ?           
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?              ?           
'MODEL FITTING'                 ? 7  ? 1 ? 'UCSF Chimera' 1.15        
OTHER                           ? 8  ? ? ? ?              ?           
'INITIAL EULER ASSIGNMENT'      ? 9  1 ? ? cryoSPARC      ?           
'FINAL EULER ASSIGNMENT'        ? 10 1 ? ? cryoSPARC      ?           
CLASSIFICATION                  ? 11 1 ? ? cryoSPARC      ?           
RECONSTRUCTION                  ? 12 1 ? ? cryoSPARC      ?           
'MODEL REFINEMENT'              ? 13 ? 1 ? Coot           0.9.6.2-pre 
'VOLUME SELECTION'              ? 14 1 1 1 ?              ?           
'SERIES ALIGNMENT'              ? 15 1 1 1 ?              ?           
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?              ?           
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?              ?           
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?              ?           
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?              ?           
# 
_em_specimen.concentration           10 
_em_specimen.details                 
'This sample was obtained from the monodispersed peak fractions of the size-exclusion chromatography.' 
_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   'Chinese Academy of Sciences' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           XDB37030304 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
# 
_atom_sites.entry_id                    8ZQO 
_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  
CL 
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PHE A 1 3   ? 86.793  106.852 83.749  1.00 94.27  ? 3   PHE A N   1 
ATOM   2    C  CA  . PHE A 1 3   ? 87.926  105.969 83.499  1.00 94.98  ? 3   PHE A CA  1 
ATOM   3    C  C   . PHE A 1 3   ? 88.700  106.400 82.258  1.00 93.43  ? 3   PHE A C   1 
ATOM   4    O  O   . PHE A 1 3   ? 88.218  106.258 81.135  1.00 92.56  ? 3   PHE A O   1 
ATOM   5    C  CB  . PHE A 1 3   ? 87.454  104.522 83.343  1.00 91.60  ? 3   PHE A CB  1 
ATOM   6    C  CG  . PHE A 1 3   ? 88.570  103.517 83.341  1.00 93.13  ? 3   PHE A CG  1 
ATOM   7    C  CD1 . PHE A 1 3   ? 89.743  103.762 84.034  1.00 93.69  ? 3   PHE A CD1 1 
ATOM   8    C  CD2 . PHE A 1 3   ? 88.446  102.327 82.645  1.00 93.85  ? 3   PHE A CD2 1 
ATOM   9    C  CE1 . PHE A 1 3   ? 90.771  102.839 84.033  1.00 93.85  ? 3   PHE A CE1 1 
ATOM   10   C  CE2 . PHE A 1 3   ? 89.470  101.399 82.641  1.00 93.69  ? 3   PHE A CE2 1 
ATOM   11   C  CZ  . PHE A 1 3   ? 90.633  101.656 83.336  1.00 94.35  ? 3   PHE A CZ  1 
ATOM   12   N  N   . HIS A 1 4   ? 89.902  106.926 82.470  1.00 88.12  ? 4   HIS A N   1 
ATOM   13   C  CA  . HIS A 1 4   ? 90.789  107.339 81.391  1.00 88.61  ? 4   HIS A CA  1 
ATOM   14   C  C   . HIS A 1 4   ? 91.961  106.369 81.326  1.00 91.33  ? 4   HIS A C   1 
ATOM   15   O  O   . HIS A 1 4   ? 92.686  106.200 82.312  1.00 91.92  ? 4   HIS A O   1 
ATOM   16   C  CB  . HIS A 1 4   ? 91.277  108.772 81.600  1.00 87.45  ? 4   HIS A CB  1 
ATOM   17   C  CG  . HIS A 1 4   ? 90.280  109.813 81.195  1.00 90.52  ? 4   HIS A CG  1 
ATOM   18   N  ND1 . HIS A 1 4   ? 90.181  110.286 79.905  1.00 91.47  ? 4   HIS A ND1 1 
ATOM   19   C  CD2 . HIS A 1 4   ? 89.336  110.469 81.910  1.00 90.66  ? 4   HIS A CD2 1 
ATOM   20   C  CE1 . HIS A 1 4   ? 89.220  111.190 79.842  1.00 90.94  ? 4   HIS A CE1 1 
ATOM   21   N  NE2 . HIS A 1 4   ? 88.691  111.320 81.045  1.00 91.05  ? 4   HIS A NE2 1 
ATOM   22   N  N   . VAL A 1 5   ? 92.139  105.732 80.166  1.00 83.33  ? 5   VAL A N   1 
ATOM   23   C  CA  . VAL A 1 5   ? 93.211  104.754 80.011  1.00 82.04  ? 5   VAL A CA  1 
ATOM   24   C  C   . VAL A 1 5   ? 94.574  105.432 79.991  1.00 82.82  ? 5   VAL A C   1 
ATOM   25   O  O   . VAL A 1 5   ? 95.581  104.826 80.381  1.00 83.35  ? 5   VAL A O   1 
ATOM   26   C  CB  . VAL A 1 5   ? 92.982  103.911 78.744  1.00 79.33  ? 5   VAL A CB  1 
ATOM   27   C  CG1 . VAL A 1 5   ? 91.876  102.896 78.976  1.00 79.12  ? 5   VAL A CG1 1 
ATOM   28   C  CG2 . VAL A 1 5   ? 92.649  104.809 77.562  1.00 78.97  ? 5   VAL A CG2 1 
ATOM   29   N  N   . GLU A 1 6   ? 94.637  106.686 79.535  1.00 76.43  ? 6   GLU A N   1 
ATOM   30   C  CA  . GLU A 1 6   ? 95.921  107.371 79.413  1.00 77.21  ? 6   GLU A CA  1 
ATOM   31   C  C   . GLU A 1 6   ? 96.598  107.536 80.769  1.00 77.71  ? 6   GLU A C   1 
ATOM   32   O  O   . GLU A 1 6   ? 97.816  107.356 80.890  1.00 76.70  ? 6   GLU A O   1 
ATOM   33   C  CB  . GLU A 1 6   ? 95.726  108.728 78.740  1.00 77.12  ? 6   GLU A CB  1 
ATOM   34   C  CG  . GLU A 1 6   ? 95.807  108.680 77.225  1.00 79.56  ? 6   GLU A CG  1 
ATOM   35   C  CD  . GLU A 1 6   ? 94.445  108.540 76.574  1.00 80.93  ? 6   GLU A CD  1 
ATOM   36   O  OE1 . GLU A 1 6   ? 93.429  108.655 77.290  1.00 79.49  ? 6   GLU A OE1 1 
ATOM   37   O  OE2 . GLU A 1 6   ? 94.391  108.314 75.347  1.00 80.78  ? 6   GLU A OE2 1 
ATOM   38   N  N   . GLY A 1 7   ? 95.826  107.881 81.802  1.00 66.70  ? 7   GLY A N   1 
ATOM   39   C  CA  . GLY A 1 7   ? 96.401  107.995 83.132  1.00 67.14  ? 7   GLY A CA  1 
ATOM   40   C  C   . GLY A 1 7   ? 96.941  106.676 83.649  1.00 72.38  ? 7   GLY A C   1 
ATOM   41   O  O   . GLY A 1 7   ? 98.008  106.629 84.270  1.00 77.35  ? 7   GLY A O   1 
ATOM   42   N  N   . LEU A 1 8   ? 96.213  105.585 83.401  1.00 62.09  ? 8   LEU A N   1 
ATOM   43   C  CA  . LEU A 1 8   ? 96.687  104.269 83.816  1.00 63.60  ? 8   LEU A CA  1 
ATOM   44   C  C   . LEU A 1 8   ? 97.980  103.897 83.100  1.00 63.63  ? 8   LEU A C   1 
ATOM   45   O  O   . LEU A 1 8   ? 98.919  103.383 83.722  1.00 62.46  ? 8   LEU A O   1 
ATOM   46   C  CB  . LEU A 1 8   ? 95.606  103.221 83.557  1.00 64.02  ? 8   LEU A CB  1 
ATOM   47   C  CG  . LEU A 1 8   ? 95.439  102.151 84.635  1.00 66.28  ? 8   LEU A CG  1 
ATOM   48   C  CD1 . LEU A 1 8   ? 95.350  102.792 86.008  1.00 64.43  ? 8   LEU A CD1 1 
ATOM   49   C  CD2 . LEU A 1 8   ? 94.212  101.302 84.355  1.00 65.67  ? 8   LEU A CD2 1 
ATOM   50   N  N   . ILE A 1 9   ? 98.052  104.160 81.793  1.00 58.63  ? 9   ILE A N   1 
ATOM   51   C  CA  . ILE A 1 9   ? 99.270  103.868 81.043  1.00 56.87  ? 9   ILE A CA  1 
ATOM   52   C  C   . ILE A 1 9   ? 100.433 104.692 81.579  1.00 59.39  ? 9   ILE A C   1 
ATOM   53   O  O   . ILE A 1 9   ? 101.552 104.186 81.742  1.00 62.19  ? 9   ILE A O   1 
ATOM   54   C  CB  . ILE A 1 9   ? 99.048  104.114 79.539  1.00 56.18  ? 9   ILE A CB  1 
ATOM   55   C  CG1 . ILE A 1 9   ? 97.904  103.245 79.014  1.00 55.15  ? 9   ILE A CG1 1 
ATOM   56   C  CG2 . ILE A 1 9   ? 100.322 103.839 78.758  1.00 60.40  ? 9   ILE A CG2 1 
ATOM   57   C  CD1 . ILE A 1 9   ? 98.112  101.765 79.224  1.00 58.50  ? 9   ILE A CD1 1 
ATOM   58   N  N   . ALA A 1 10  ? 100.189 105.974 81.865  1.00 52.32  ? 10  ALA A N   1 
ATOM   59   C  CA  . ALA A 1 10  ? 101.247 106.833 82.385  1.00 50.26  ? 10  ALA A CA  1 
ATOM   60   C  C   . ALA A 1 10  ? 101.746 106.346 83.740  1.00 51.80  ? 10  ALA A C   1 
ATOM   61   O  O   . ALA A 1 10  ? 102.958 106.321 83.990  1.00 58.60  ? 10  ALA A O   1 
ATOM   62   C  CB  . ALA A 1 10  ? 100.749 108.274 82.483  1.00 49.49  ? 10  ALA A CB  1 
ATOM   63   N  N   . ILE A 1 11  ? 100.832 105.948 84.628  1.00 40.32  ? 11  ILE A N   1 
ATOM   64   C  CA  . ILE A 1 11  ? 101.254 105.497 85.951  1.00 47.22  ? 11  ILE A CA  1 
ATOM   65   C  C   . ILE A 1 11  ? 102.004 104.170 85.857  1.00 51.62  ? 11  ILE A C   1 
ATOM   66   O  O   . ILE A 1 11  ? 102.973 103.938 86.593  1.00 54.24  ? 11  ILE A O   1 
ATOM   67   C  CB  . ILE A 1 11  ? 100.047 105.433 86.911  1.00 49.90  ? 11  ILE A CB  1 
ATOM   68   C  CG1 . ILE A 1 11  ? 100.491 105.738 88.344  1.00 50.46  ? 11  ILE A CG1 1 
ATOM   69   C  CG2 . ILE A 1 11  ? 99.334  104.093 86.848  1.00 53.29  ? 11  ILE A CG2 1 
ATOM   70   C  CD1 . ILE A 1 11  ? 100.520 107.212 88.673  1.00 48.01  ? 11  ILE A CD1 1 
ATOM   71   N  N   . ILE A 1 12  ? 101.598 103.291 84.935  1.00 46.66  ? 12  ILE A N   1 
ATOM   72   C  CA  . ILE A 1 12  ? 102.316 102.033 84.751  1.00 42.07  ? 12  ILE A CA  1 
ATOM   73   C  C   . ILE A 1 12  ? 103.725 102.290 84.227  1.00 44.76  ? 12  ILE A C   1 
ATOM   74   O  O   . ILE A 1 12  ? 104.698 101.676 84.687  1.00 49.32  ? 12  ILE A O   1 
ATOM   75   C  CB  . ILE A 1 12  ? 101.519 101.097 83.825  1.00 43.90  ? 12  ILE A CB  1 
ATOM   76   C  CG1 . ILE A 1 12  ? 100.279 100.569 84.549  1.00 45.08  ? 12  ILE A CG1 1 
ATOM   77   C  CG2 . ILE A 1 12  ? 102.385 99.944  83.344  1.00 41.82  ? 12  ILE A CG2 1 
ATOM   78   C  CD1 . ILE A 1 12  ? 99.319  99.825  83.651  1.00 48.22  ? 12  ILE A CD1 1 
ATOM   79   N  N   . VAL A 1 13  ? 103.860 103.205 83.263  1.00 37.55  ? 13  VAL A N   1 
ATOM   80   C  CA  . VAL A 1 13  ? 105.179 103.544 82.735  1.00 34.55  ? 13  VAL A CA  1 
ATOM   81   C  C   . VAL A 1 13  ? 106.055 104.147 83.828  1.00 42.67  ? 13  VAL A C   1 
ATOM   82   O  O   . VAL A 1 13  ? 107.252 103.848 83.922  1.00 51.36  ? 13  VAL A O   1 
ATOM   83   C  CB  . VAL A 1 13  ? 105.040 104.489 81.526  1.00 38.15  ? 13  VAL A CB  1 
ATOM   84   C  CG1 . VAL A 1 13  ? 106.382 105.098 81.161  1.00 41.27  ? 13  VAL A CG1 1 
ATOM   85   C  CG2 . VAL A 1 13  ? 104.456 103.741 80.341  1.00 39.12  ? 13  VAL A CG2 1 
ATOM   86   N  N   . PHE A 1 14  ? 105.471 104.999 84.674  1.00 35.42  ? 14  PHE A N   1 
ATOM   87   C  CA  . PHE A 1 14  ? 106.221 105.589 85.780  1.00 31.27  ? 14  PHE A CA  1 
ATOM   88   C  C   . PHE A 1 14  ? 106.716 104.520 86.751  1.00 35.58  ? 14  PHE A C   1 
ATOM   89   O  O   . PHE A 1 14  ? 107.877 104.550 87.188  1.00 42.39  ? 14  PHE A O   1 
ATOM   90   C  CB  . PHE A 1 14  ? 105.341 106.616 86.493  1.00 36.45  ? 14  PHE A CB  1 
ATOM   91   C  CG  . PHE A 1 14  ? 106.023 107.333 87.620  1.00 41.48  ? 14  PHE A CG  1 
ATOM   92   C  CD1 . PHE A 1 14  ? 107.211 108.010 87.413  1.00 42.05  ? 14  PHE A CD1 1 
ATOM   93   C  CD2 . PHE A 1 14  ? 105.462 107.347 88.885  1.00 36.68  ? 14  PHE A CD2 1 
ATOM   94   C  CE1 . PHE A 1 14  ? 107.833 108.674 88.449  1.00 39.22  ? 14  PHE A CE1 1 
ATOM   95   C  CE2 . PHE A 1 14  ? 106.079 108.009 89.923  1.00 38.23  ? 14  PHE A CE2 1 
ATOM   96   C  CZ  . PHE A 1 14  ? 107.266 108.673 89.705  1.00 38.74  ? 14  PHE A CZ  1 
ATOM   97   N  N   . TYR A 1 15  ? 105.852 103.560 87.094  1.00 31.95  ? 15  TYR A N   1 
ATOM   98   C  CA  . TYR A 1 15  ? 106.257 102.486 87.999  1.00 31.73  ? 15  TYR A CA  1 
ATOM   99   C  C   . TYR A 1 15  ? 107.377 101.647 87.393  1.00 37.05  ? 15  TYR A C   1 
ATOM   100  O  O   . TYR A 1 15  ? 108.340 101.282 88.084  1.00 37.49  ? 15  TYR A O   1 
ATOM   101  C  CB  . TYR A 1 15  ? 105.058 101.598 88.337  1.00 36.24  ? 15  TYR A CB  1 
ATOM   102  C  CG  . TYR A 1 15  ? 104.074 102.190 89.323  1.00 41.26  ? 15  TYR A CG  1 
ATOM   103  C  CD1 . TYR A 1 15  ? 104.013 103.558 89.547  1.00 40.17  ? 15  TYR A CD1 1 
ATOM   104  C  CD2 . TYR A 1 15  ? 103.198 101.374 90.025  1.00 41.24  ? 15  TYR A CD2 1 
ATOM   105  C  CE1 . TYR A 1 15  ? 103.108 104.096 90.440  1.00 42.47  ? 15  TYR A CE1 1 
ATOM   106  C  CE2 . TYR A 1 15  ? 102.293 101.902 90.922  1.00 33.38  ? 15  TYR A CE2 1 
ATOM   107  C  CZ  . TYR A 1 15  ? 102.251 103.262 91.126  1.00 38.28  ? 15  TYR A CZ  1 
ATOM   108  O  OH  . TYR A 1 15  ? 101.351 103.790 92.021  1.00 40.91  ? 15  TYR A OH  1 
ATOM   109  N  N   . LEU A 1 16  ? 107.266 101.329 86.101  1.00 33.93  ? 16  LEU A N   1 
ATOM   110  C  CA  . LEU A 1 16  ? 108.305 100.543 85.442  1.00 29.76  ? 16  LEU A CA  1 
ATOM   111  C  C   . LEU A 1 16  ? 109.629 101.296 85.404  1.00 32.56  ? 16  LEU A C   1 
ATOM   112  O  O   . LEU A 1 16  ? 110.696 100.697 85.582  1.00 43.65  ? 16  LEU A O   1 
ATOM   113  C  CB  . LEU A 1 16  ? 107.859 100.160 84.033  1.00 29.54  ? 16  LEU A CB  1 
ATOM   114  C  CG  . LEU A 1 16  ? 106.669 99.200  83.956  1.00 36.54  ? 16  LEU A CG  1 
ATOM   115  C  CD1 . LEU A 1 16  ? 106.287 98.928  82.511  1.00 39.63  ? 16  LEU A CD1 1 
ATOM   116  C  CD2 . LEU A 1 16  ? 106.972 97.905  84.688  1.00 37.68  ? 16  LEU A CD2 1 
ATOM   117  N  N   . LEU A 1 17  ? 109.582 102.610 85.173  1.00 24.15  ? 17  LEU A N   1 
ATOM   118  C  CA  . LEU A 1 17  ? 110.806 103.407 85.181  1.00 31.14  ? 17  LEU A CA  1 
ATOM   119  C  C   . LEU A 1 17  ? 111.462 103.412 86.558  1.00 31.51  ? 17  LEU A C   1 
ATOM   120  O  O   . LEU A 1 17  ? 112.691 103.304 86.670  1.00 37.21  ? 17  LEU A O   1 
ATOM   121  C  CB  . LEU A 1 17  ? 110.506 104.832 84.725  1.00 31.34  ? 17  LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 17  ? 110.620 105.078 83.221  1.00 37.14  ? 17  LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 17  ? 109.768 106.263 82.801  1.00 37.17  ? 17  LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 17  ? 112.071 105.291 82.830  1.00 36.34  ? 17  LEU A CD2 1 
ATOM   125  N  N   . ILE A 1 18  ? 110.660 103.539 87.619  1.00 22.13  ? 18  ILE A N   1 
ATOM   126  C  CA  . ILE A 1 18  ? 111.223 103.509 88.969  1.00 19.45  ? 18  ILE A CA  1 
ATOM   127  C  C   . ILE A 1 18  ? 111.872 102.157 89.250  1.00 24.37  ? 18  ILE A C   1 
ATOM   128  O  O   . ILE A 1 18  ? 112.973 102.081 89.818  1.00 31.68  ? 18  ILE A O   1 
ATOM   129  C  CB  . ILE A 1 18  ? 110.140 103.853 90.009  1.00 27.31  ? 18  ILE A CB  1 
ATOM   130  C  CG1 . ILE A 1 18  ? 109.791 105.339 89.939  1.00 28.43  ? 18  ILE A CG1 1 
ATOM   131  C  CG2 . ILE A 1 18  ? 110.602 103.494 91.410  1.00 19.67  ? 18  ILE A CG2 1 
ATOM   132  C  CD1 . ILE A 1 18  ? 110.924 106.250 90.348  1.00 24.07  ? 18  ILE A CD1 1 
ATOM   133  N  N   . LEU A 1 19  ? 111.208 101.069 88.849  1.00 23.29  ? 19  LEU A N   1 
ATOM   134  C  CA  . LEU A 1 19  ? 111.784 99.741  89.047  1.00 21.74  ? 19  LEU A CA  1 
ATOM   135  C  C   . LEU A 1 19  ? 113.092 99.580  88.278  1.00 24.42  ? 19  LEU A C   1 
ATOM   136  O  O   . LEU A 1 19  ? 114.056 98.992  88.787  1.00 25.64  ? 19  LEU A O   1 
ATOM   137  C  CB  . LEU A 1 19  ? 110.781 98.667  88.630  1.00 28.20  ? 19  LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 19  ? 111.214 97.214  88.826  1.00 30.69  ? 19  LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 19  ? 111.275 96.862  90.302  1.00 28.98  ? 19  LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 19  ? 110.277 96.278  88.087  1.00 27.65  ? 19  LEU A CD2 1 
ATOM   141  N  N   . LEU A 1 20  ? 113.143 100.094 87.045  1.00 29.31  ? 20  LEU A N   1 
ATOM   142  C  CA  . LEU A 1 20  ? 114.369 100.016 86.256  1.00 23.00  ? 20  LEU A CA  1 
ATOM   143  C  C   . LEU A 1 20  ? 115.505 100.782 86.920  1.00 31.47  ? 20  LEU A C   1 
ATOM   144  O  O   . LEU A 1 20  ? 116.650 100.312 86.943  1.00 35.11  ? 20  LEU A O   1 
ATOM   145  C  CB  . LEU A 1 20  ? 114.121 100.551 84.847  1.00 26.85  ? 20  LEU A CB  1 
ATOM   146  C  CG  . LEU A 1 20  ? 113.755 99.529  83.771  1.00 38.51  ? 20  LEU A CG  1 
ATOM   147  C  CD1 . LEU A 1 20  ? 113.007 100.202 82.633  1.00 36.66  ? 20  LEU A CD1 1 
ATOM   148  C  CD2 . LEU A 1 20  ? 114.999 98.828  83.256  1.00 34.82  ? 20  LEU A CD2 1 
ATOM   149  N  N   . VAL A 1 21  ? 115.211 101.968 87.459  1.00 30.18  ? 21  VAL A N   1 
ATOM   150  C  CA  . VAL A 1 21  ? 116.243 102.748 88.141  1.00 29.48  ? 21  VAL A CA  1 
ATOM   151  C  C   . VAL A 1 21  ? 116.764 101.992 89.359  1.00 27.31  ? 21  VAL A C   1 
ATOM   152  O  O   . VAL A 1 21  ? 117.977 101.948 89.610  1.00 24.93  ? 21  VAL A O   1 
ATOM   153  C  CB  . VAL A 1 21  ? 115.702 104.139 88.521  1.00 32.06  ? 21  VAL A CB  1 
ATOM   154  C  CG1 . VAL A 1 21  ? 116.527 104.753 89.642  1.00 25.21  ? 21  VAL A CG1 1 
ATOM   155  C  CG2 . VAL A 1 21  ? 115.695 105.051 87.307  1.00 26.81  ? 21  VAL A CG2 1 
ATOM   156  N  N   . GLY A 1 22  ? 115.861 101.382 90.129  1.00 25.10  ? 22  GLY A N   1 
ATOM   157  C  CA  . GLY A 1 22  ? 116.299 100.609 91.284  1.00 22.13  ? 22  GLY A CA  1 
ATOM   158  C  C   . GLY A 1 22  ? 117.177 99.428  90.908  1.00 30.13  ? 22  GLY A C   1 
ATOM   159  O  O   . GLY A 1 22  ? 118.196 99.165  91.557  1.00 35.02  ? 22  GLY A O   1 
ATOM   160  N  N   . ILE A 1 23  ? 116.797 98.703  89.853  1.00 36.54  ? 23  ILE A N   1 
ATOM   161  C  CA  . ILE A 1 23  ? 117.594 97.561  89.410  1.00 30.26  ? 23  ILE A CA  1 
ATOM   162  C  C   . ILE A 1 23  ? 118.967 98.017  88.928  1.00 31.24  ? 23  ILE A C   1 
ATOM   163  O  O   . ILE A 1 23  ? 119.986 97.371  89.211  1.00 35.14  ? 23  ILE A O   1 
ATOM   164  C  CB  . ILE A 1 23  ? 116.844 96.769  88.322  1.00 33.04  ? 23  ILE A CB  1 
ATOM   165  C  CG1 . ILE A 1 23  ? 115.601 96.102  88.909  1.00 31.75  ? 23  ILE A CG1 1 
ATOM   166  C  CG2 . ILE A 1 23  ? 117.751 95.725  87.695  1.00 30.30  ? 23  ILE A CG2 1 
ATOM   167  C  CD1 . ILE A 1 23  ? 114.781 95.346  87.890  1.00 29.91  ? 23  ILE A CD1 1 
ATOM   168  N  N   . TRP A 1 24  ? 119.020 99.131  88.192  1.00 25.74  ? 24  TRP A N   1 
ATOM   169  C  CA  . TRP A 1 24  ? 120.308 99.648  87.737  1.00 27.17  ? 24  TRP A CA  1 
ATOM   170  C  C   . TRP A 1 24  ? 121.195 100.041 88.911  1.00 32.91  ? 24  TRP A C   1 
ATOM   171  O  O   . TRP A 1 24  ? 122.406 99.791  88.893  1.00 36.24  ? 24  TRP A O   1 
ATOM   172  C  CB  . TRP A 1 24  ? 120.108 100.844 86.809  1.00 31.95  ? 24  TRP A CB  1 
ATOM   173  C  CG  . TRP A 1 24  ? 121.367 101.628 86.599  1.00 36.64  ? 24  TRP A CG  1 
ATOM   174  C  CD1 . TRP A 1 24  ? 122.387 101.325 85.748  1.00 36.69  ? 24  TRP A CD1 1 
ATOM   175  C  CD2 . TRP A 1 24  ? 121.749 102.837 87.267  1.00 40.44  ? 24  TRP A CD2 1 
ATOM   176  N  NE1 . TRP A 1 24  ? 123.377 102.272 85.838  1.00 32.75  ? 24  TRP A NE1 1 
ATOM   177  C  CE2 . TRP A 1 24  ? 123.009 103.211 86.764  1.00 38.33  ? 24  TRP A CE2 1 
ATOM   178  C  CE3 . TRP A 1 24  ? 121.145 103.640 88.239  1.00 36.58  ? 24  TRP A CE3 1 
ATOM   179  C  CZ2 . TRP A 1 24  ? 123.676 104.353 87.199  1.00 38.32  ? 24  TRP A CZ2 1 
ATOM   180  C  CZ3 . TRP A 1 24  ? 121.808 104.771 88.669  1.00 33.73  ? 24  TRP A CZ3 1 
ATOM   181  C  CH2 . TRP A 1 24  ? 123.059 105.118 88.149  1.00 38.12  ? 24  TRP A CH2 1 
ATOM   182  N  N   . ALA A 1 25  ? 120.616 100.675 89.934  1.00 36.20  ? 25  ALA A N   1 
ATOM   183  C  CA  . ALA A 1 25  ? 121.402 101.037 91.111  1.00 27.44  ? 25  ALA A CA  1 
ATOM   184  C  C   . ALA A 1 25  ? 121.955 99.800  91.805  1.00 29.50  ? 25  ALA A C   1 
ATOM   185  O  O   . ALA A 1 25  ? 123.127 99.773  92.211  1.00 35.80  ? 25  ALA A O   1 
ATOM   186  C  CB  . ALA A 1 25  ? 120.550 101.854 92.079  1.00 23.25  ? 25  ALA A CB  1 
ATOM   187  N  N   . ALA A 1 26  ? 121.123 98.764  91.951  1.00 33.30  ? 26  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 26  ? 121.588 97.528  92.574  1.00 31.56  ? 26  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 26  ? 122.719 96.898  91.773  1.00 36.97  ? 26  ALA A C   1 
ATOM   190  O  O   . ALA A 1 26  ? 123.697 96.405  92.346  1.00 35.75  ? 26  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 26  ? 120.430 96.545  92.725  1.00 33.15  ? 26  ALA A CB  1 
ATOM   192  N  N   . TRP A 1 27  ? 122.693 96.887  90.464  1.00 52.11  ? 27  TRP A N   1 
ATOM   193  C  CA  . TRP A 1 27  ? 123.834 96.337  89.701  1.00 44.78  ? 27  TRP A CA  1 
ATOM   194  C  C   . TRP A 1 27  ? 125.067 97.179  89.926  1.00 43.68  ? 27  TRP A C   1 
ATOM   195  O  O   . TRP A 1 27  ? 126.069 96.652  90.348  1.00 48.42  ? 27  TRP A O   1 
ATOM   196  C  CB  . TRP A 1 27  ? 123.521 96.336  88.215  1.00 46.41  ? 27  TRP A CB  1 
ATOM   197  C  CG  . TRP A 1 27  ? 124.687 95.968  87.354  1.00 53.47  ? 27  TRP A CG  1 
ATOM   198  C  CD1 . TRP A 1 27  ? 125.261 94.738  87.224  1.00 54.95  ? 27  TRP A CD1 1 
ATOM   199  C  CD2 . TRP A 1 27  ? 125.425 96.848  86.491  1.00 51.69  ? 27  TRP A CD2 1 
ATOM   200  N  NE1 . TRP A 1 27  ? 126.304 94.793  86.342  1.00 52.35  ? 27  TRP A NE1 1 
ATOM   201  C  CE2 . TRP A 1 27  ? 126.429 96.074  85.876  1.00 49.80  ? 27  TRP A CE2 1 
ATOM   202  C  CE3 . TRP A 1 27  ? 125.335 98.208  86.180  1.00 53.39  ? 27  TRP A CE3 1 
ATOM   203  C  CZ2 . TRP A 1 27  ? 127.334 96.620  84.971  1.00 53.67  ? 27  TRP A CZ2 1 
ATOM   204  C  CZ3 . TRP A 1 27  ? 126.232 98.747  85.287  1.00 55.68  ? 27  TRP A CZ3 1 
ATOM   205  C  CH2 . TRP A 1 27  ? 127.217 97.961  84.692  1.00 56.51  ? 27  TRP A CH2 1 
ATOM   206  N  N   . ARG A 1 28  ? 124.965 98.467  89.659  1.00 45.54  ? 28  ARG A N   1 
ATOM   207  C  CA  . ARG A 1 28  ? 126.234 99.246  89.727  1.00 46.06  ? 28  ARG A CA  1 
ATOM   208  C  C   . ARG A 1 28  ? 126.828 99.366  91.131  1.00 46.88  ? 28  ARG A C   1 
ATOM   209  O  O   . ARG A 1 28  ? 127.980 99.724  91.209  1.00 49.17  ? 28  ARG A O   1 
ATOM   210  C  CB  . ARG A 1 28  ? 125.978 100.686 89.287  1.00 47.76  ? 28  ARG A CB  1 
ATOM   211  C  CG  . ARG A 1 28  ? 127.190 101.601 89.315  1.00 46.38  ? 28  ARG A CG  1 
ATOM   212  C  CD  . ARG A 1 28  ? 126.756 103.017 89.008  1.00 50.27  ? 28  ARG A CD  1 
ATOM   213  N  NE  . ARG A 1 28  ? 127.761 103.993 89.390  1.00 56.18  ? 28  ARG A NE  1 
ATOM   214  C  CZ  . ARG A 1 28  ? 127.582 104.906 90.333  1.00 52.38  ? 28  ARG A CZ  1 
ATOM   215  N  NH1 . ARG A 1 28  ? 126.506 104.859 91.094  1.00 48.91  ? 28  ARG A NH1 1 
ATOM   216  N  NH2 . ARG A 1 28  ? 128.481 105.855 90.521  1.00 46.87  ? 28  ARG A NH2 1 
ATOM   217  N  N   . THR A 1 29  ? 126.058 99.197  92.208  1.00 51.91  ? 29  THR A N   1 
ATOM   218  C  CA  . THR A 1 29  ? 126.671 99.288  93.531  1.00 42.59  ? 29  THR A CA  1 
ATOM   219  C  C   . THR A 1 29  ? 126.926 97.912  94.141  1.00 49.96  ? 29  THR A C   1 
ATOM   220  O  O   . THR A 1 29  ? 126.797 97.718  95.350  1.00 51.03  ? 29  THR A O   1 
ATOM   221  C  CB  . THR A 1 29  ? 125.809 100.132 94.462  1.00 42.93  ? 29  THR A CB  1 
ATOM   222  O  OG1 . THR A 1 29  ? 124.425 99.901  94.171  1.00 54.30  ? 29  THR A OG1 1 
ATOM   223  C  CG2 . THR A 1 29  ? 126.119 101.606 94.275  1.00 41.86  ? 29  THR A CG2 1 
ATOM   224  N  N   . LYS A 1 30  ? 127.299 96.942  93.303  1.00 62.39  ? 30  LYS A N   1 
ATOM   225  C  CA  . LYS A 1 30  ? 127.506 95.579  93.785  1.00 62.09  ? 30  LYS A CA  1 
ATOM   226  C  C   . LYS A 1 30  ? 128.816 95.425  94.548  1.00 62.50  ? 30  LYS A C   1 
ATOM   227  O  O   . LYS A 1 30  ? 128.872 94.677  95.530  1.00 64.36  ? 30  LYS A O   1 
ATOM   228  C  CB  . LYS A 1 30  ? 127.473 94.597  92.615  1.00 63.33  ? 30  LYS A CB  1 
ATOM   229  C  CG  . LYS A 1 30  ? 127.413 93.139  93.040  1.00 63.98  ? 30  LYS A CG  1 
ATOM   230  C  CD  . LYS A 1 30  ? 127.492 92.187  91.855  1.00 64.78  ? 30  LYS A CD  1 
ATOM   231  C  CE  . LYS A 1 30  ? 127.033 92.835  90.560  1.00 63.07  ? 30  LYS A CE  1 
ATOM   232  N  NZ  . LYS A 1 30  ? 126.703 91.812  89.533  1.00 64.49  ? 30  LYS A NZ  1 
ATOM   233  N  N   . ASN A 1 31  ? 129.876 96.110  94.118  1.00 64.22  ? 31  ASN A N   1 
ATOM   234  C  CA  . ASN A 1 31  ? 131.212 95.905  94.666  1.00 65.31  ? 31  ASN A CA  1 
ATOM   235  C  C   . ASN A 1 31  ? 131.590 96.950  95.711  1.00 67.10  ? 31  ASN A C   1 
ATOM   236  O  O   . ASN A 1 31  ? 132.780 97.204  95.923  1.00 69.42  ? 31  ASN A O   1 
ATOM   237  C  CB  . ASN A 1 31  ? 132.246 95.888  93.539  1.00 67.02  ? 31  ASN A CB  1 
ATOM   238  C  CG  . ASN A 1 31  ? 132.334 94.541  92.848  1.00 71.47  ? 31  ASN A CG  1 
ATOM   239  O  OD1 . ASN A 1 31  ? 132.434 93.502  93.499  1.00 70.98  ? 31  ASN A OD1 1 
ATOM   240  N  ND2 . ASN A 1 31  ? 132.299 94.553  91.521  1.00 72.23  ? 31  ASN A ND2 1 
ATOM   241  N  N   . SER A 1 32  ? 130.610 97.559  96.371  1.00 65.20  ? 32  SER A N   1 
ATOM   242  C  CA  . SER A 1 32  ? 130.874 98.564  97.392  1.00 65.81  ? 32  SER A CA  1 
ATOM   243  C  C   . SER A 1 32  ? 130.880 97.903  98.765  1.00 64.06  ? 32  SER A C   1 
ATOM   244  O  O   . SER A 1 32  ? 129.882 97.302  99.175  1.00 65.20  ? 32  SER A O   1 
ATOM   245  C  CB  . SER A 1 32  ? 129.833 99.681  97.336  1.00 63.56  ? 32  SER A CB  1 
ATOM   246  O  OG  . SER A 1 32  ? 130.010 100.480 96.180  1.00 69.48  ? 32  SER A OG  1 
ATOM   247  N  N   . GLY A 1 33  ? 131.996 98.020  99.470  1.00 71.10  ? 33  GLY A N   1 
ATOM   248  C  CA  . GLY A 1 33  ? 132.159 97.429  100.783 1.00 71.55  ? 33  GLY A CA  1 
ATOM   249  C  C   . GLY A 1 33  ? 133.115 96.248  100.752 1.00 72.95  ? 33  GLY A C   1 
ATOM   250  O  O   . GLY A 1 33  ? 133.726 95.923  99.733  1.00 71.08  ? 33  GLY A O   1 
ATOM   251  N  N   . SER A 1 34  ? 133.232 95.608  101.912 1.00 78.88  ? 34  SER A N   1 
ATOM   252  C  CA  . SER A 1 34  ? 134.091 94.441  102.041 1.00 77.23  ? 34  SER A CA  1 
ATOM   253  C  C   . SER A 1 34  ? 133.519 93.263  101.261 1.00 78.03  ? 34  SER A C   1 
ATOM   254  O  O   . SER A 1 34  ? 132.302 93.100  101.139 1.00 80.93  ? 34  SER A O   1 
ATOM   255  C  CB  . SER A 1 34  ? 134.258 94.061  103.512 1.00 78.06  ? 34  SER A CB  1 
ATOM   256  O  OG  . SER A 1 34  ? 134.286 95.213  104.336 1.00 82.63  ? 34  SER A OG  1 
ATOM   257  N  N   . ALA A 1 35  ? 134.417 92.434  100.726 1.00 78.98  ? 35  ALA A N   1 
ATOM   258  C  CA  . ALA A 1 35  ? 133.998 91.259  99.972  1.00 80.15  ? 35  ALA A CA  1 
ATOM   259  C  C   . ALA A 1 35  ? 133.441 90.155  100.860 1.00 80.38  ? 35  ALA A C   1 
ATOM   260  O  O   . ALA A 1 35  ? 132.852 89.203  100.337 1.00 77.88  ? 35  ALA A O   1 
ATOM   261  C  CB  . ALA A 1 35  ? 135.168 90.719  99.149  1.00 79.82  ? 35  ALA A CB  1 
ATOM   262  N  N   . GLU A 1 36  ? 133.610 90.255  102.177 1.00 80.87  ? 36  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 133.097 89.262  103.110 1.00 80.27  ? 36  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 131.901 89.741  103.916 1.00 78.59  ? 36  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 131.053 88.924  104.278 1.00 79.62  ? 36  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 134.202 88.823  104.080 1.00 79.18  ? 36  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 134.857 89.972  104.828 1.00 80.31  ? 36  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 136.129 89.559  105.538 1.00 83.16  ? 36  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 136.875 88.723  104.986 1.00 83.49  ? 36  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 136.383 90.072  106.648 1.00 81.63  ? 36  GLU A OE2 1 
ATOM   271  N  N   . GLU A 1 37  ? 131.812 91.037  104.206 1.00 69.83  ? 37  GLU A N   1 
ATOM   272  C  CA  . GLU A 1 37  ? 130.703 91.585  104.986 1.00 70.45  ? 37  GLU A CA  1 
ATOM   273  C  C   . GLU A 1 37  ? 129.633 92.135  104.045 1.00 67.49  ? 37  GLU A C   1 
ATOM   274  O  O   . GLU A 1 37  ? 129.427 93.341  103.911 1.00 69.96  ? 37  GLU A O   1 
ATOM   275  C  CB  . GLU A 1 37  ? 131.212 92.653  105.949 1.00 70.23  ? 37  GLU A CB  1 
ATOM   276  C  CG  . GLU A 1 37  ? 131.982 92.101  107.136 1.00 68.34  ? 37  GLU A CG  1 
ATOM   277  C  CD  . GLU A 1 37  ? 132.773 93.169  107.863 1.00 71.32  ? 37  GLU A CD  1 
ATOM   278  O  OE1 . GLU A 1 37  ? 133.759 93.676  107.288 1.00 72.47  ? 37  GLU A OE1 1 
ATOM   279  O  OE2 . GLU A 1 37  ? 132.410 93.503  109.010 1.00 68.94  ? 37  GLU A OE2 1 
ATOM   280  N  N   . ARG A 1 38  ? 128.946 91.205  103.379 1.00 58.41  ? 38  ARG A N   1 
ATOM   281  C  CA  . ARG A 1 38  ? 127.877 91.586  102.462 1.00 60.62  ? 38  ARG A CA  1 
ATOM   282  C  C   . ARG A 1 38  ? 126.624 92.015  103.217 1.00 56.44  ? 38  ARG A C   1 
ATOM   283  O  O   . ARG A 1 38  ? 125.918 92.938  102.789 1.00 56.55  ? 38  ARG A O   1 
ATOM   284  C  CB  . ARG A 1 38  ? 127.567 90.427  101.517 1.00 62.03  ? 38  ARG A CB  1 
ATOM   285  C  CG  . ARG A 1 38  ? 128.672 90.128  100.518 1.00 61.53  ? 38  ARG A CG  1 
ATOM   286  C  CD  . ARG A 1 38  ? 128.593 91.054  99.316  1.00 62.63  ? 38  ARG A CD  1 
ATOM   287  N  NE  . ARG A 1 38  ? 129.447 92.225  99.473  1.00 65.95  ? 38  ARG A NE  1 
ATOM   288  C  CZ  . ARG A 1 38  ? 129.326 93.340  98.766  1.00 64.52  ? 38  ARG A CZ  1 
ATOM   289  N  NH1 . ARG A 1 38  ? 128.397 93.469  97.833  1.00 62.15  ? 38  ARG A NH1 1 
ATOM   290  N  NH2 . ARG A 1 38  ? 130.156 94.351  99.002  1.00 61.86  ? 38  ARG A NH2 1 
ATOM   291  N  N   . SER A 1 39  ? 126.329 91.352  104.338 1.00 48.47  ? 39  SER A N   1 
ATOM   292  C  CA  . SER A 1 39  ? 125.137 91.687  105.110 1.00 49.94  ? 39  SER A CA  1 
ATOM   293  C  C   . SER A 1 39  ? 125.209 93.107  105.655 1.00 52.36  ? 39  SER A C   1 
ATOM   294  O  O   . SER A 1 39  ? 124.226 93.854  105.590 1.00 53.87  ? 39  SER A O   1 
ATOM   295  C  CB  . SER A 1 39  ? 124.955 90.686  106.250 1.00 54.59  ? 39  SER A CB  1 
ATOM   296  O  OG  . SER A 1 39  ? 126.116 90.619  107.058 1.00 56.55  ? 39  SER A OG  1 
ATOM   297  N  N   . GLU A 1 40  ? 126.363 93.497  106.199 1.00 49.67  ? 40  GLU A N   1 
ATOM   298  C  CA  . GLU A 1 40  ? 126.528 94.868  106.669 1.00 46.79  ? 40  GLU A CA  1 
ATOM   299  C  C   . GLU A 1 40  ? 126.554 95.851  105.506 1.00 44.94  ? 40  GLU A C   1 
ATOM   300  O  O   . GLU A 1 40  ? 126.139 97.007  105.660 1.00 47.19  ? 40  GLU A O   1 
ATOM   301  C  CB  . GLU A 1 40  ? 127.799 94.978  107.515 1.00 47.79  ? 40  GLU A CB  1 
ATOM   302  C  CG  . GLU A 1 40  ? 128.580 96.267  107.335 1.00 49.64  ? 40  GLU A CG  1 
ATOM   303  C  CD  . GLU A 1 40  ? 129.941 96.218  107.991 1.00 55.64  ? 40  GLU A CD  1 
ATOM   304  O  OE1 . GLU A 1 40  ? 129.999 96.050  109.226 1.00 54.21  ? 40  GLU A OE1 1 
ATOM   305  O  OE2 . GLU A 1 40  ? 130.952 96.348  107.271 1.00 59.18  ? 40  GLU A OE2 1 
ATOM   306  N  N   . ALA A 1 41  ? 127.039 95.411  104.343 1.00 40.83  ? 41  ALA A N   1 
ATOM   307  C  CA  . ALA A 1 41  ? 126.997 96.255  103.157 1.00 36.74  ? 41  ALA A CA  1 
ATOM   308  C  C   . ALA A 1 41  ? 125.563 96.605  102.791 1.00 36.68  ? 41  ALA A C   1 
ATOM   309  O  O   . ALA A 1 41  ? 125.241 97.775  102.576 1.00 42.74  ? 41  ALA A O   1 
ATOM   310  C  CB  . ALA A 1 41  ? 127.701 95.564  101.990 1.00 42.31  ? 41  ALA A CB  1 
ATOM   311  N  N   . ILE A 1 42  ? 124.673 95.608  102.781 1.00 36.83  ? 42  ILE A N   1 
ATOM   312  C  CA  . ILE A 1 42  ? 123.273 95.855  102.433 1.00 34.93  ? 42  ILE A CA  1 
ATOM   313  C  C   . ILE A 1 42  ? 122.653 96.903  103.352 1.00 37.02  ? 42  ILE A C   1 
ATOM   314  O  O   . ILE A 1 42  ? 121.712 97.605  102.961 1.00 37.80  ? 42  ILE A O   1 
ATOM   315  C  CB  . ILE A 1 42  ? 122.479 94.530  102.462 1.00 32.83  ? 42  ILE A CB  1 
ATOM   316  C  CG1 . ILE A 1 42  ? 123.065 93.534  101.462 1.00 37.82  ? 42  ILE A CG1 1 
ATOM   317  C  CG2 . ILE A 1 42  ? 121.011 94.758  102.146 1.00 36.52  ? 42  ILE A CG2 1 
ATOM   318  C  CD1 . ILE A 1 42  ? 122.399 92.177  101.494 1.00 39.42  ? 42  ILE A CD1 1 
ATOM   319  N  N   . ILE A 1 43  ? 123.180 97.055  104.562 1.00 34.22  ? 43  ILE A N   1 
ATOM   320  C  CA  . ILE A 1 43  ? 122.596 97.971  105.536 1.00 27.42  ? 43  ILE A CA  1 
ATOM   321  C  C   . ILE A 1 43  ? 123.215 99.363  105.451 1.00 32.27  ? 43  ILE A C   1 
ATOM   322  O  O   . ILE A 1 43  ? 122.497 100.366 105.467 1.00 32.33  ? 43  ILE A O   1 
ATOM   323  C  CB  . ILE A 1 43  ? 122.720 97.380  106.956 1.00 35.79  ? 43  ILE A CB  1 
ATOM   324  C  CG1 . ILE A 1 43  ? 121.905 96.091  107.067 1.00 30.10  ? 43  ILE A CG1 1 
ATOM   325  C  CG2 . ILE A 1 43  ? 122.260 98.384  107.996 1.00 30.95  ? 43  ILE A CG2 1 
ATOM   326  C  CD1 . ILE A 1 43  ? 122.133 95.334  108.350 1.00 27.59  ? 43  ILE A CD1 1 
ATOM   327  N  N   . VAL A 1 44  ? 124.543 99.474  105.361 1.00 31.51  ? 44  VAL A N   1 
ATOM   328  C  CA  . VAL A 1 44  ? 125.191 100.782 105.481 1.00 26.27  ? 44  VAL A CA  1 
ATOM   329  C  C   . VAL A 1 44  ? 125.791 101.308 104.182 1.00 31.47  ? 44  VAL A C   1 
ATOM   330  O  O   . VAL A 1 44  ? 126.154 102.495 104.136 1.00 34.61  ? 44  VAL A O   1 
ATOM   331  C  CB  . VAL A 1 44  ? 126.267 100.796 106.590 1.00 21.69  ? 44  VAL A CB  1 
ATOM   332  C  CG1 . VAL A 1 44  ? 125.633 100.623 107.958 1.00 24.56  ? 44  VAL A CG1 1 
ATOM   333  C  CG2 . VAL A 1 44  ? 127.335 99.752  106.337 1.00 37.32  ? 44  VAL A CG2 1 
ATOM   334  N  N   . GLY A 1 45  ? 125.916 100.497 103.133 1.00 30.32  ? 45  GLY A N   1 
ATOM   335  C  CA  . GLY A 1 45  ? 126.430 100.997 101.877 1.00 31.41  ? 45  GLY A CA  1 
ATOM   336  C  C   . GLY A 1 45  ? 127.923 101.222 101.820 1.00 38.93  ? 45  GLY A C   1 
ATOM   337  O  O   . GLY A 1 45  ? 128.406 101.797 100.839 1.00 52.47  ? 45  GLY A O   1 
ATOM   338  N  N   . GLY A 1 46  ? 128.674 100.788 102.827 1.00 31.77  ? 46  GLY A N   1 
ATOM   339  C  CA  . GLY A 1 46  ? 130.094 101.062 102.854 1.00 31.53  ? 46  GLY A CA  1 
ATOM   340  C  C   . GLY A 1 46  ? 130.475 102.434 103.362 1.00 42.09  ? 46  GLY A C   1 
ATOM   341  O  O   . GLY A 1 46  ? 131.660 102.782 103.315 1.00 39.27  ? 46  GLY A O   1 
ATOM   342  N  N   . ARG A 1 47  ? 129.509 103.223 103.841 1.00 32.57  ? 47  ARG A N   1 
ATOM   343  C  CA  . ARG A 1 47  ? 129.749 104.552 104.407 1.00 18.22  ? 47  ARG A CA  1 
ATOM   344  C  C   . ARG A 1 47  ? 130.460 105.462 103.402 1.00 25.78  ? 47  ARG A C   1 
ATOM   345  O  O   . ARG A 1 47  ? 131.577 105.931 103.624 1.00 30.93  ? 47  ARG A O   1 
ATOM   346  C  CB  . ARG A 1 47  ? 130.532 104.455 105.720 1.00 17.03  ? 47  ARG A CB  1 
ATOM   347  C  CG  . ARG A 1 47  ? 129.941 103.481 106.725 1.00 19.20  ? 47  ARG A CG  1 
ATOM   348  C  CD  . ARG A 1 47  ? 130.900 103.215 107.870 1.00 24.62  ? 47  ARG A CD  1 
ATOM   349  N  NE  . ARG A 1 47  ? 130.257 102.521 108.979 1.00 29.23  ? 47  ARG A NE  1 
ATOM   350  C  CZ  . ARG A 1 47  ? 130.328 101.213 109.187 1.00 32.12  ? 47  ARG A CZ  1 
ATOM   351  N  NH1 . ARG A 1 47  ? 131.000 100.419 108.372 1.00 31.22  ? 47  ARG A NH1 1 
ATOM   352  N  NH2 . ARG A 1 47  ? 129.712 100.690 110.242 1.00 30.94  ? 47  ARG A NH2 1 
ATOM   353  N  N   . ASP A 1 48  ? 129.777 105.713 102.282 1.00 34.42  ? 48  ASP A N   1 
ATOM   354  C  CA  . ASP A 1 48  ? 130.361 106.497 101.202 1.00 23.47  ? 48  ASP A CA  1 
ATOM   355  C  C   . ASP A 1 48  ? 129.390 107.500 100.589 1.00 33.50  ? 48  ASP A C   1 
ATOM   356  O  O   . ASP A 1 48  ? 129.734 108.128 99.581  1.00 40.53  ? 48  ASP A O   1 
ATOM   357  C  CB  . ASP A 1 48  ? 130.890 105.571 100.100 1.00 30.62  ? 48  ASP A CB  1 
ATOM   358  C  CG  . ASP A 1 48  ? 132.371 105.290 100.236 1.00 48.77  ? 48  ASP A CG  1 
ATOM   359  O  OD1 . ASP A 1 48  ? 133.157 106.258 100.303 1.00 49.34  ? 48  ASP A OD1 1 
ATOM   360  O  OD2 . ASP A 1 48  ? 132.750 104.101 100.272 1.00 44.90  ? 48  ASP A OD2 1 
ATOM   361  N  N   . ILE A 1 49  ? 128.202 107.673 101.153 1.00 32.06  ? 49  ILE A N   1 
ATOM   362  C  CA  . ILE A 1 49  ? 127.192 108.545 100.565 1.00 28.16  ? 49  ILE A CA  1 
ATOM   363  C  C   . ILE A 1 49  ? 127.562 110.000 100.817 1.00 32.56  ? 49  ILE A C   1 
ATOM   364  O  O   . ILE A 1 49  ? 128.013 110.366 101.908 1.00 34.06  ? 49  ILE A O   1 
ATOM   365  C  CB  . ILE A 1 49  ? 125.801 108.204 101.127 1.00 23.11  ? 49  ILE A CB  1 
ATOM   366  C  CG1 . ILE A 1 49  ? 125.502 106.720 100.910 1.00 21.63  ? 49  ILE A CG1 1 
ATOM   367  C  CG2 . ILE A 1 49  ? 124.733 109.057 100.472 1.00 29.74  ? 49  ILE A CG2 1 
ATOM   368  C  CD1 . ILE A 1 49  ? 124.047 106.352 101.070 1.00 31.84  ? 49  ILE A CD1 1 
ATOM   369  N  N   . GLY A 1 50  ? 127.373 110.837 99.800  1.00 35.28  ? 50  GLY A N   1 
ATOM   370  C  CA  . GLY A 1 50  ? 127.765 112.229 99.861  1.00 27.86  ? 50  GLY A CA  1 
ATOM   371  C  C   . GLY A 1 50  ? 126.745 113.102 100.563 1.00 35.87  ? 50  GLY A C   1 
ATOM   372  O  O   . GLY A 1 50  ? 125.957 112.648 101.396 1.00 39.23  ? 50  GLY A O   1 
ATOM   373  N  N   . LEU A 1 51  ? 126.772 114.388 100.215 1.00 31.78  ? 51  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 51  ? 125.928 115.390 100.856 1.00 29.67  ? 51  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 51  ? 124.583 115.556 100.156 1.00 30.28  ? 51  LEU A C   1 
ATOM   376  O  O   . LEU A 1 51  ? 123.531 115.471 100.799 1.00 37.51  ? 51  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 51  ? 126.659 116.734 100.899 1.00 29.88  ? 51  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 51  ? 127.027 117.267 102.281 1.00 33.90  ? 51  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 51  ? 127.663 118.640 102.165 1.00 33.59  ? 51  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 51  ? 125.801 117.310 103.170 1.00 28.67  ? 51  LEU A CD2 1 
ATOM   381  N  N   . LEU A 1 52  ? 124.605 115.813 98.846  1.00 23.61  ? 52  LEU A N   1 
ATOM   382  C  CA  . LEU A 1 52  ? 123.365 116.057 98.117  1.00 25.33  ? 52  LEU A CA  1 
ATOM   383  C  C   . LEU A 1 52  ? 122.461 114.833 98.130  1.00 33.92  ? 52  LEU A C   1 
ATOM   384  O  O   . LEU A 1 52  ? 121.248 114.951 98.336  1.00 41.97  ? 52  LEU A O   1 
ATOM   385  C  CB  . LEU A 1 52  ? 123.677 116.477 96.682  1.00 27.97  ? 52  LEU A CB  1 
ATOM   386  C  CG  . LEU A 1 52  ? 124.352 117.838 96.510  1.00 34.48  ? 52  LEU A CG  1 
ATOM   387  C  CD1 . LEU A 1 52  ? 124.656 118.097 95.045  1.00 35.94  ? 52  LEU A CD1 1 
ATOM   388  C  CD2 . LEU A 1 52  ? 123.485 118.946 97.086  1.00 32.35  ? 52  LEU A CD2 1 
ATOM   389  N  N   . VAL A 1 53  ? 123.034 113.647 97.916  1.00 27.82  ? 53  VAL A N   1 
ATOM   390  C  CA  . VAL A 1 53  ? 122.236 112.424 97.925  1.00 22.09  ? 53  VAL A CA  1 
ATOM   391  C  C   . VAL A 1 53  ? 121.624 112.199 99.300  1.00 26.55  ? 53  VAL A C   1 
ATOM   392  O  O   . VAL A 1 53  ? 120.446 111.842 99.419  1.00 33.33  ? 53  VAL A O   1 
ATOM   393  C  CB  . VAL A 1 53  ? 123.089 111.224 97.474  1.00 24.15  ? 53  VAL A CB  1 
ATOM   394  C  CG1 . VAL A 1 53  ? 122.340 109.922 97.697  1.00 18.94  ? 53  VAL A CG1 1 
ATOM   395  C  CG2 . VAL A 1 53  ? 123.468 111.370 96.012  1.00 23.29  ? 53  VAL A CG2 1 
ATOM   396  N  N   . GLY A 1 54  ? 122.409 112.407 100.360 1.00 20.15  ? 54  GLY A N   1 
ATOM   397  C  CA  . GLY A 1 54  ? 121.885 112.226 101.705 1.00 19.05  ? 54  GLY A CA  1 
ATOM   398  C  C   . GLY A 1 54  ? 120.758 113.186 102.033 1.00 28.41  ? 54  GLY A C   1 
ATOM   399  O  O   . GLY A 1 54  ? 119.732 112.787 102.593 1.00 43.15  ? 54  GLY A O   1 
ATOM   400  N  N   . GLY A 1 55  ? 120.927 114.463 101.685 1.00 19.14  ? 55  GLY A N   1 
ATOM   401  C  CA  . GLY A 1 55  ? 119.861 115.425 101.919 1.00 16.77  ? 55  GLY A CA  1 
ATOM   402  C  C   . GLY A 1 55  ? 118.604 115.106 101.132 1.00 17.33  ? 55  GLY A C   1 
ATOM   403  O  O   . GLY A 1 55  ? 117.491 115.174 101.665 1.00 19.00  ? 55  GLY A O   1 
ATOM   404  N  N   . PHE A 1 56  ? 118.764 114.740 99.857  1.00 18.64  ? 56  PHE A N   1 
ATOM   405  C  CA  . PHE A 1 56  ? 117.610 114.409 99.028  1.00 24.01  ? 56  PHE A CA  1 
ATOM   406  C  C   . PHE A 1 56  ? 116.874 113.188 99.562  1.00 21.50  ? 56  PHE A C   1 
ATOM   407  O  O   . PHE A 1 56  ? 115.639 113.175 99.616  1.00 27.69  ? 56  PHE A O   1 
ATOM   408  C  CB  . PHE A 1 56  ? 118.050 114.173 97.584  1.00 24.96  ? 56  PHE A CB  1 
ATOM   409  C  CG  . PHE A 1 56  ? 118.164 115.428 96.769  1.00 28.93  ? 56  PHE A CG  1 
ATOM   410  C  CD1 . PHE A 1 56  ? 118.732 116.572 97.302  1.00 22.39  ? 56  PHE A CD1 1 
ATOM   411  C  CD2 . PHE A 1 56  ? 117.705 115.462 95.464  1.00 33.86  ? 56  PHE A CD2 1 
ATOM   412  C  CE1 . PHE A 1 56  ? 118.839 117.724 96.551  1.00 25.76  ? 56  PHE A CE1 1 
ATOM   413  C  CE2 . PHE A 1 56  ? 117.808 116.613 94.708  1.00 32.56  ? 56  PHE A CE2 1 
ATOM   414  C  CZ  . PHE A 1 56  ? 118.376 117.745 95.253  1.00 28.91  ? 56  PHE A CZ  1 
ATOM   415  N  N   . THR A 1 57  ? 117.611 112.152 99.969  1.00 7.87   ? 57  THR A N   1 
ATOM   416  C  CA  . THR A 1 57  ? 116.950 110.943 100.444 1.00 11.70  ? 57  THR A CA  1 
ATOM   417  C  C   . THR A 1 57  ? 116.305 111.154 101.810 1.00 16.73  ? 57  THR A C   1 
ATOM   418  O  O   . THR A 1 57  ? 115.238 110.592 102.073 1.00 27.45  ? 57  THR A O   1 
ATOM   419  C  CB  . THR A 1 57  ? 117.931 109.762 100.458 1.00 20.57  ? 57  THR A CB  1 
ATOM   420  O  OG1 . THR A 1 57  ? 117.219 108.547 100.723 1.00 28.19  ? 57  THR A OG1 1 
ATOM   421  C  CG2 . THR A 1 57  ? 119.010 109.938 101.502 1.00 17.75  ? 57  THR A CG2 1 
ATOM   422  N  N   . MET A 1 58  ? 116.897 111.986 102.674 1.00 9.08   ? 58  MET A N   1 
ATOM   423  C  CA  . MET A 1 58  ? 116.238 112.305 103.937 1.00 16.43  ? 58  MET A CA  1 
ATOM   424  C  C   . MET A 1 58  ? 114.951 113.094 103.709 1.00 23.28  ? 58  MET A C   1 
ATOM   425  O  O   . MET A 1 58  ? 113.917 112.808 104.333 1.00 24.69  ? 58  MET A O   1 
ATOM   426  C  CB  . MET A 1 58  ? 117.195 113.078 104.844 1.00 10.84  ? 58  MET A CB  1 
ATOM   427  C  CG  . MET A 1 58  ? 116.839 113.026 106.321 1.00 16.24  ? 58  MET A CG  1 
ATOM   428  S  SD  . MET A 1 58  ? 116.795 111.354 106.990 1.00 37.04  ? 58  MET A SD  1 
ATOM   429  C  CE  . MET A 1 58  ? 115.208 111.357 107.812 1.00 12.07  ? 58  MET A CE  1 
ATOM   430  N  N   . THR A 1 59  ? 114.990 114.083 102.810 1.00 19.37  ? 59  THR A N   1 
ATOM   431  C  CA  . THR A 1 59  ? 113.786 114.852 102.510 1.00 14.69  ? 59  THR A CA  1 
ATOM   432  C  C   . THR A 1 59  ? 112.699 113.966 101.915 1.00 22.71  ? 59  THR A C   1 
ATOM   433  O  O   . THR A 1 59  ? 111.522 114.096 102.267 1.00 21.30  ? 59  THR A O   1 
ATOM   434  C  CB  . THR A 1 59  ? 114.119 116.003 101.561 1.00 20.24  ? 59  THR A CB  1 
ATOM   435  O  OG1 . THR A 1 59  ? 115.233 116.742 102.075 1.00 30.64  ? 59  THR A OG1 1 
ATOM   436  C  CG2 . THR A 1 59  ? 112.930 116.935 101.411 1.00 10.94  ? 59  THR A CG2 1 
ATOM   437  N  N   . ALA A 1 60  ? 113.073 113.058 101.011 1.00 20.03  ? 60  ALA A N   1 
ATOM   438  C  CA  . ALA A 1 60  ? 112.092 112.143 100.436 1.00 10.92  ? 60  ALA A CA  1 
ATOM   439  C  C   . ALA A 1 60  ? 111.522 111.206 101.494 1.00 16.74  ? 60  ALA A C   1 
ATOM   440  O  O   . ALA A 1 60  ? 110.328 110.886 101.470 1.00 15.28  ? 60  ALA A O   1 
ATOM   441  C  CB  . ALA A 1 60  ? 112.720 111.350 99.294  1.00 12.70  ? 60  ALA A CB  1 
ATOM   442  N  N   . THR A 1 61  ? 112.362 110.747 102.424 1.00 19.92  ? 61  THR A N   1 
ATOM   443  C  CA  . THR A 1 61  ? 111.888 109.865 103.485 1.00 16.72  ? 61  THR A CA  1 
ATOM   444  C  C   . THR A 1 61  ? 110.861 110.556 104.372 1.00 19.46  ? 61  THR A C   1 
ATOM   445  O  O   . THR A 1 61  ? 109.825 109.968 104.702 1.00 21.86  ? 61  THR A O   1 
ATOM   446  C  CB  . THR A 1 61  ? 113.068 109.377 104.324 1.00 19.34  ? 61  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 61  ? 114.057 108.797 103.468 1.00 22.07  ? 61  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 61  ? 112.612 108.345 105.340 1.00 10.33  ? 61  THR A CG2 1 
ATOM   449  N  N   . TRP A 1 62  ? 111.127 111.801 104.773 1.00 18.04  ? 62  TRP A N   1 
ATOM   450  C  CA  . TRP A 1 62  ? 110.209 112.461 105.699 1.00 15.37  ? 62  TRP A CA  1 
ATOM   451  C  C   . TRP A 1 62  ? 108.930 112.960 105.030 1.00 20.89  ? 62  TRP A C   1 
ATOM   452  O  O   . TRP A 1 62  ? 107.864 112.937 105.651 1.00 18.50  ? 62  TRP A O   1 
ATOM   453  C  CB  . TRP A 1 62  ? 110.910 113.619 106.412 1.00 15.55  ? 62  TRP A CB  1 
ATOM   454  C  CG  . TRP A 1 62  ? 111.320 113.383 107.870 1.00 17.97  ? 62  TRP A CG  1 
ATOM   455  C  CD1 . TRP A 1 62  ? 111.666 114.349 108.766 1.00 21.85  ? 62  TRP A CD1 1 
ATOM   456  C  CD2 . TRP A 1 62  ? 111.448 112.127 108.575 1.00 24.99  ? 62  TRP A CD2 1 
ATOM   457  N  NE1 . TRP A 1 62  ? 111.987 113.790 109.975 1.00 17.59  ? 62  TRP A NE1 1 
ATOM   458  C  CE2 . TRP A 1 62  ? 111.864 112.430 109.886 1.00 21.29  ? 62  TRP A CE2 1 
ATOM   459  C  CE3 . TRP A 1 62  ? 111.250 110.783 108.230 1.00 21.51  ? 62  TRP A CE3 1 
ATOM   460  C  CZ2 . TRP A 1 62  ? 112.083 111.446 110.848 1.00 19.25  ? 62  TRP A CZ2 1 
ATOM   461  C  CZ3 . TRP A 1 62  ? 111.466 109.811 109.188 1.00 17.98  ? 62  TRP A CZ3 1 
ATOM   462  C  CH2 . TRP A 1 62  ? 111.879 110.146 110.479 1.00 17.97  ? 62  TRP A CH2 1 
ATOM   463  N  N   . VAL A 1 63  ? 109.004 113.413 103.781 1.00 24.47  ? 63  VAL A N   1 
ATOM   464  C  CA  . VAL A 1 63  ? 107.813 113.896 103.088 1.00 11.25  ? 63  VAL A CA  1 
ATOM   465  C  C   . VAL A 1 63  ? 106.934 112.823 102.456 1.00 19.94  ? 63  VAL A C   1 
ATOM   466  O  O   . VAL A 1 63  ? 107.162 112.408 101.315 1.00 30.17  ? 63  VAL A O   1 
ATOM   467  C  CB  . VAL A 1 63  ? 108.191 114.865 101.960 1.00 14.83  ? 63  VAL A CB  1 
ATOM   468  C  CG1 . VAL A 1 63  ? 106.963 115.253 101.158 1.00 10.19  ? 63  VAL A CG1 1 
ATOM   469  C  CG2 . VAL A 1 63  ? 108.867 116.100 102.529 1.00 17.26  ? 63  VAL A CG2 1 
ATOM   470  N  N   . GLY A 1 64  ? 105.920 112.378 103.193 1.00 22.29  ? 64  GLY A N   1 
ATOM   471  C  CA  . GLY A 1 64  ? 105.024 111.349 102.701 1.00 13.14  ? 64  GLY A CA  1 
ATOM   472  C  C   . GLY A 1 64  ? 103.602 111.749 102.365 1.00 18.95  ? 64  GLY A C   1 
ATOM   473  O  O   . GLY A 1 64  ? 103.254 112.930 102.428 1.00 27.73  ? 64  GLY A O   1 
ATOM   474  N  N   . GLY A 1 65  ? 102.774 110.778 101.988 1.00 20.33  ? 65  GLY A N   1 
ATOM   475  C  CA  . GLY A 1 65  ? 101.399 111.055 101.622 1.00 23.44  ? 65  GLY A CA  1 
ATOM   476  C  C   . GLY A 1 65  ? 100.679 111.687 102.794 1.00 28.30  ? 65  GLY A C   1 
ATOM   477  O  O   . GLY A 1 65  ? 100.113 112.780 102.676 1.00 30.64  ? 65  GLY A O   1 
ATOM   478  N  N   . GLY A 1 66  ? 100.696 111.001 103.934 1.00 26.36  ? 66  GLY A N   1 
ATOM   479  C  CA  . GLY A 1 66  ? 100.096 111.516 105.146 1.00 14.25  ? 66  GLY A CA  1 
ATOM   480  C  C   . GLY A 1 66  ? 100.414 112.958 105.475 1.00 26.68  ? 66  GLY A C   1 
ATOM   481  O  O   . GLY A 1 66  ? 99.517  113.732 105.796 1.00 42.88  ? 66  GLY A O   1 
ATOM   482  N  N   . TYR A 1 67  ? 101.693 113.325 105.387 1.00 25.86  ? 67  TYR A N   1 
ATOM   483  C  CA  . TYR A 1 67  ? 102.114 114.706 105.613 1.00 27.11  ? 67  TYR A CA  1 
ATOM   484  C  C   . TYR A 1 67  ? 101.384 115.669 104.679 1.00 23.34  ? 67  TYR A C   1 
ATOM   485  O  O   . TYR A 1 67  ? 100.750 116.637 105.132 1.00 21.38  ? 67  TYR A O   1 
ATOM   486  C  CB  . TYR A 1 67  ? 103.632 114.774 105.418 1.00 17.39  ? 67  TYR A CB  1 
ATOM   487  C  CG  . TYR A 1 67  ? 104.306 116.122 105.541 1.00 22.31  ? 67  TYR A CG  1 
ATOM   488  C  CD1 . TYR A 1 67  ? 104.470 116.733 106.774 1.00 30.70  ? 67  TYR A CD1 1 
ATOM   489  C  CD2 . TYR A 1 67  ? 104.833 116.753 104.423 1.00 20.44  ? 67  TYR A CD2 1 
ATOM   490  C  CE1 . TYR A 1 67  ? 105.110 117.953 106.885 1.00 26.95  ? 67  TYR A CE1 1 
ATOM   491  C  CE2 . TYR A 1 67  ? 105.471 117.970 104.524 1.00 23.19  ? 67  TYR A CE2 1 
ATOM   492  C  CZ  . TYR A 1 67  ? 105.608 118.566 105.756 1.00 28.90  ? 67  TYR A CZ  1 
ATOM   493  O  OH  . TYR A 1 67  ? 106.246 119.779 105.856 1.00 28.72  ? 67  TYR A OH  1 
ATOM   494  N  N   . ILE A 1 68  ? 101.427 115.387 103.376 1.00 18.47  ? 68  ILE A N   1 
ATOM   495  C  CA  . ILE A 1 68  ? 100.839 116.260 102.367 1.00 19.96  ? 68  ILE A CA  1 
ATOM   496  C  C   . ILE A 1 68  ? 99.326  116.353 102.517 1.00 31.34  ? 68  ILE A C   1 
ATOM   497  O  O   . ILE A 1 68  ? 98.761  117.450 102.442 1.00 29.70  ? 68  ILE A O   1 
ATOM   498  C  CB  . ILE A 1 68  ? 101.234 115.765 100.964 1.00 26.52  ? 68  ILE A CB  1 
ATOM   499  C  CG1 . ILE A 1 68  ? 102.723 116.004 100.714 1.00 25.50  ? 68  ILE A CG1 1 
ATOM   500  C  CG2 . ILE A 1 68  ? 100.399 116.445 99.892  1.00 29.49  ? 68  ILE A CG2 1 
ATOM   501  C  CD1 . ILE A 1 68  ? 103.105 117.460 100.674 1.00 28.19  ? 68  ILE A CD1 1 
ATOM   502  N  N   . ASN A 1 69  ? 98.642  115.225 102.724 1.00 28.32  ? 69  ASN A N   1 
ATOM   503  C  CA  . ASN A 1 69  ? 97.190  115.265 102.858 1.00 17.92  ? 69  ASN A CA  1 
ATOM   504  C  C   . ASN A 1 69  ? 96.760  115.905 104.175 1.00 22.65  ? 69  ASN A C   1 
ATOM   505  O  O   . ASN A 1 69  ? 95.781  116.661 104.210 1.00 30.76  ? 69  ASN A O   1 
ATOM   506  C  CB  . ASN A 1 69  ? 96.617  113.854 102.734 1.00 22.88  ? 69  ASN A CB  1 
ATOM   507  C  CG  . ASN A 1 69  ? 96.429  113.425 101.292 1.00 26.86  ? 69  ASN A CG  1 
ATOM   508  O  OD1 . ASN A 1 69  ? 96.819  114.133 100.366 1.00 29.80  ? 69  ASN A OD1 1 
ATOM   509  N  ND2 . ASN A 1 69  ? 95.830  112.259 101.095 1.00 31.43  ? 69  ASN A ND2 1 
ATOM   510  N  N   . GLY A 1 70  ? 97.480  115.621 105.262 1.00 17.79  ? 70  GLY A N   1 
ATOM   511  C  CA  . GLY A 1 70  ? 97.096  116.139 106.560 1.00 18.39  ? 70  GLY A CA  1 
ATOM   512  C  C   . GLY A 1 70  ? 97.269  117.638 106.685 1.00 22.14  ? 70  GLY A C   1 
ATOM   513  O  O   . GLY A 1 70  ? 96.464  118.302 107.339 1.00 30.60  ? 70  GLY A O   1 
ATOM   514  N  N   . THR A 1 71  ? 98.326  118.195 106.085 1.00 20.59  ? 71  THR A N   1 
ATOM   515  C  CA  . THR A 1 71  ? 98.489  119.647 106.139 1.00 22.40  ? 71  THR A CA  1 
ATOM   516  C  C   . THR A 1 71  ? 97.315  120.354 105.464 1.00 20.66  ? 71  THR A C   1 
ATOM   517  O  O   . THR A 1 71  ? 96.738  121.304 106.016 1.00 18.79  ? 71  THR A O   1 
ATOM   518  C  CB  . THR A 1 71  ? 99.815  120.052 105.494 1.00 29.16  ? 71  THR A CB  1 
ATOM   519  O  OG1 . THR A 1 71  ? 100.881 119.299 106.084 1.00 28.39  ? 71  THR A OG1 1 
ATOM   520  C  CG2 . THR A 1 71  ? 100.080 121.533 105.703 1.00 24.62  ? 71  THR A CG2 1 
ATOM   521  N  N   . ALA A 1 72  ? 96.930  119.881 104.276 1.00 18.26  ? 72  ALA A N   1 
ATOM   522  C  CA  . ALA A 1 72  ? 95.798  120.467 103.568 1.00 25.37  ? 72  ALA A CA  1 
ATOM   523  C  C   . ALA A 1 72  ? 94.501  120.287 104.347 1.00 30.02  ? 72  ALA A C   1 
ATOM   524  O  O   . ALA A 1 72  ? 93.684  121.213 104.427 1.00 25.19  ? 72  ALA A O   1 
ATOM   525  C  CB  . ALA A 1 72  ? 95.678  119.852 102.175 1.00 12.23  ? 72  ALA A CB  1 
ATOM   526  N  N   . GLU A 1 73  ? 94.293  119.102 104.929 1.00 25.24  ? 73  GLU A N   1 
ATOM   527  C  CA  . GLU A 1 73  ? 93.080  118.872 105.707 1.00 11.16  ? 73  GLU A CA  1 
ATOM   528  C  C   . GLU A 1 73  ? 93.018  119.789 106.922 1.00 27.65  ? 73  GLU A C   1 
ATOM   529  O  O   . GLU A 1 73  ? 91.956  120.334 107.243 1.00 38.27  ? 73  GLU A O   1 
ATOM   530  C  CB  . GLU A 1 73  ? 92.999  117.409 106.137 1.00 19.41  ? 73  GLU A CB  1 
ATOM   531  C  CG  . GLU A 1 73  ? 91.773  117.086 106.967 1.00 33.10  ? 73  GLU A CG  1 
ATOM   532  C  CD  . GLU A 1 73  ? 91.966  115.873 107.850 1.00 42.69  ? 73  GLU A CD  1 
ATOM   533  O  OE1 . GLU A 1 73  ? 93.041  115.244 107.771 1.00 43.35  ? 73  GLU A OE1 1 
ATOM   534  O  OE2 . GLU A 1 73  ? 91.044  115.548 108.625 1.00 39.67  ? 73  GLU A OE2 1 
ATOM   535  N  N   . ALA A 1 74  ? 94.145  119.967 107.613 1.00 30.69  ? 74  ALA A N   1 
ATOM   536  C  CA  . ALA A 1 74  ? 94.170  120.832 108.787 1.00 23.90  ? 74  ALA A CA  1 
ATOM   537  C  C   . ALA A 1 74  ? 93.875  122.277 108.415 1.00 22.61  ? 74  ALA A C   1 
ATOM   538  O  O   . ALA A 1 74  ? 93.149  122.972 109.134 1.00 24.55  ? 74  ALA A O   1 
ATOM   539  C  CB  . ALA A 1 74  ? 95.523  120.726 109.490 1.00 19.49  ? 74  ALA A CB  1 
ATOM   540  N  N   . VAL A 1 75  ? 94.431  122.752 107.299 1.00 27.51  ? 75  VAL A N   1 
ATOM   541  C  CA  . VAL A 1 75  ? 94.157  124.128 106.891 1.00 16.39  ? 75  VAL A CA  1 
ATOM   542  C  C   . VAL A 1 75  ? 92.700  124.288 106.462 1.00 22.20  ? 75  VAL A C   1 
ATOM   543  O  O   . VAL A 1 75  ? 92.073  125.320 106.725 1.00 29.27  ? 75  VAL A O   1 
ATOM   544  C  CB  . VAL A 1 75  ? 95.133  124.566 105.785 1.00 19.80  ? 75  VAL A CB  1 
ATOM   545  C  CG1 . VAL A 1 75  ? 94.800  125.965 105.304 1.00 15.92  ? 75  VAL A CG1 1 
ATOM   546  C  CG2 . VAL A 1 75  ? 96.558  124.519 106.297 1.00 22.96  ? 75  VAL A CG2 1 
ATOM   547  N  N   . TYR A 1 76  ? 92.132  123.270 105.808 1.00 24.12  ? 76  TYR A N   1 
ATOM   548  C  CA  . TYR A 1 76  ? 90.791  123.410 105.241 1.00 19.51  ? 76  TYR A CA  1 
ATOM   549  C  C   . TYR A 1 76  ? 89.703  123.376 106.311 1.00 26.17  ? 76  TYR A C   1 
ATOM   550  O  O   . TYR A 1 76  ? 88.746  124.156 106.250 1.00 20.10  ? 76  TYR A O   1 
ATOM   551  C  CB  . TYR A 1 76  ? 90.544  122.313 104.207 1.00 24.70  ? 76  TYR A CB  1 
ATOM   552  C  CG  . TYR A 1 76  ? 89.098  122.183 103.786 1.00 26.11  ? 76  TYR A CG  1 
ATOM   553  C  CD1 . TYR A 1 76  ? 88.463  123.201 103.092 1.00 22.67  ? 76  TYR A CD1 1 
ATOM   554  C  CD2 . TYR A 1 76  ? 88.366  121.042 104.083 1.00 26.25  ? 76  TYR A CD2 1 
ATOM   555  C  CE1 . TYR A 1 76  ? 87.146  123.089 102.706 1.00 21.27  ? 76  TYR A CE1 1 
ATOM   556  C  CE2 . TYR A 1 76  ? 87.046  120.922 103.700 1.00 19.88  ? 76  TYR A CE2 1 
ATOM   557  C  CZ  . TYR A 1 76  ? 86.443  121.949 103.012 1.00 25.91  ? 76  TYR A CZ  1 
ATOM   558  O  OH  . TYR A 1 76  ? 85.129  121.840 102.626 1.00 32.31  ? 76  TYR A OH  1 
ATOM   559  N  N   . VAL A 1 77  ? 89.821  122.481 107.284 1.00 28.28  ? 77  VAL A N   1 
ATOM   560  C  CA  . VAL A 1 77  ? 88.716  122.220 108.218 1.00 22.95  ? 77  VAL A CA  1 
ATOM   561  C  C   . VAL A 1 77  ? 88.506  123.436 109.116 1.00 27.24  ? 77  VAL A C   1 
ATOM   562  O  O   . VAL A 1 77  ? 89.481  123.957 109.685 1.00 29.06  ? 77  VAL A O   1 
ATOM   563  C  CB  . VAL A 1 77  ? 89.006  120.967 109.046 1.00 23.10  ? 77  VAL A CB  1 
ATOM   564  C  CG1 . VAL A 1 77  ? 88.067  120.883 110.233 1.00 24.56  ? 77  VAL A CG1 1 
ATOM   565  C  CG2 . VAL A 1 77  ? 88.876  119.726 108.182 1.00 29.36  ? 77  VAL A CG2 1 
ATOM   566  N  N   . PRO A 1 78  ? 87.275  123.925 109.268 1.00 37.70  ? 78  PRO A N   1 
ATOM   567  C  CA  . PRO A 1 78  ? 87.034  125.043 110.186 1.00 34.96  ? 78  PRO A CA  1 
ATOM   568  C  C   . PRO A 1 78  ? 87.322  124.654 111.626 1.00 35.79  ? 78  PRO A C   1 
ATOM   569  O  O   . PRO A 1 78  ? 87.108  123.515 112.044 1.00 43.73  ? 78  PRO A O   1 
ATOM   570  C  CB  . PRO A 1 78  ? 85.547  125.358 109.984 1.00 27.99  ? 78  PRO A CB  1 
ATOM   571  C  CG  . PRO A 1 78  ? 85.188  124.734 108.679 1.00 30.87  ? 78  PRO A CG  1 
ATOM   572  C  CD  . PRO A 1 78  ? 86.050  123.520 108.562 1.00 34.94  ? 78  PRO A CD  1 
ATOM   573  N  N   . GLY A 1 79  ? 87.804  125.630 112.393 1.00 35.32  ? 79  GLY A N   1 
ATOM   574  C  CA  . GLY A 1 79  ? 88.202  125.399 113.761 1.00 32.47  ? 79  GLY A CA  1 
ATOM   575  C  C   . GLY A 1 79  ? 89.641  124.975 113.943 1.00 39.75  ? 79  GLY A C   1 
ATOM   576  O  O   . GLY A 1 79  ? 90.098  124.866 115.088 1.00 40.06  ? 79  GLY A O   1 
ATOM   577  N  N   . TYR A 1 80  ? 90.370  124.725 112.855 1.00 37.95  ? 80  TYR A N   1 
ATOM   578  C  CA  . TYR A 1 80  ? 91.787  124.397 112.920 1.00 28.36  ? 80  TYR A CA  1 
ATOM   579  C  C   . TYR A 1 80  ? 92.650  125.477 112.282 1.00 38.22  ? 80  TYR A C   1 
ATOM   580  O  O   . TYR A 1 80  ? 93.511  126.054 112.948 1.00 46.37  ? 80  TYR A O   1 
ATOM   581  C  CB  . TYR A 1 80  ? 92.038  123.041 112.245 1.00 27.03  ? 80  TYR A CB  1 
ATOM   582  C  CG  . TYR A 1 80  ? 91.681  121.852 113.103 1.00 35.70  ? 80  TYR A CG  1 
ATOM   583  C  CD1 . TYR A 1 80  ? 92.580  121.345 114.029 1.00 38.86  ? 80  TYR A CD1 1 
ATOM   584  C  CD2 . TYR A 1 80  ? 90.443  121.237 112.990 1.00 36.69  ? 80  TYR A CD2 1 
ATOM   585  C  CE1 . TYR A 1 80  ? 92.257  120.260 114.816 1.00 39.45  ? 80  TYR A CE1 1 
ATOM   586  C  CE2 . TYR A 1 80  ? 90.112  120.151 113.773 1.00 36.63  ? 80  TYR A CE2 1 
ATOM   587  C  CZ  . TYR A 1 80  ? 91.023  119.666 114.684 1.00 37.86  ? 80  TYR A CZ  1 
ATOM   588  O  OH  . TYR A 1 80  ? 90.699  118.584 115.468 1.00 41.41  ? 80  TYR A OH  1 
ATOM   589  N  N   . GLY A 1 81  ? 92.428  125.781 111.009 1.00 34.27  ? 81  GLY A N   1 
ATOM   590  C  CA  . GLY A 1 81  ? 93.181  126.822 110.342 1.00 25.38  ? 81  GLY A CA  1 
ATOM   591  C  C   . GLY A 1 81  ? 94.658  126.493 110.180 1.00 22.43  ? 81  GLY A C   1 
ATOM   592  O  O   . GLY A 1 81  ? 95.116  125.372 110.394 1.00 24.96  ? 81  GLY A O   1 
ATOM   593  N  N   . LEU A 1 82  ? 95.410  127.527 109.797 1.00 22.61  ? 82  LEU A N   1 
ATOM   594  C  CA  . LEU A 1 82  ? 96.854  127.384 109.645 1.00 24.17  ? 82  LEU A CA  1 
ATOM   595  C  C   . LEU A 1 82  ? 97.552  127.245 110.992 1.00 29.12  ? 82  LEU A C   1 
ATOM   596  O  O   . LEU A 1 82  ? 98.631  126.647 111.070 1.00 34.76  ? 82  LEU A O   1 
ATOM   597  C  CB  . LEU A 1 82  ? 97.419  128.579 108.876 1.00 27.45  ? 82  LEU A CB  1 
ATOM   598  C  CG  . LEU A 1 82  ? 98.927  128.612 108.614 1.00 27.55  ? 82  LEU A CG  1 
ATOM   599  C  CD1 . LEU A 1 82  ? 99.378  127.355 107.894 1.00 22.30  ? 82  LEU A CD1 1 
ATOM   600  C  CD2 . LEU A 1 82  ? 99.314  129.853 107.827 1.00 25.87  ? 82  LEU A CD2 1 
ATOM   601  N  N   . ALA A 1 83  ? 96.953  127.778 112.058 1.00 30.49  ? 83  ALA A N   1 
ATOM   602  C  CA  . ALA A 1 83  ? 97.599  127.750 113.365 1.00 26.70  ? 83  ALA A CA  1 
ATOM   603  C  C   . ALA A 1 83  ? 97.737  126.334 113.908 1.00 28.35  ? 83  ALA A C   1 
ATOM   604  O  O   . ALA A 1 83  ? 98.605  126.080 114.750 1.00 31.20  ? 83  ALA A O   1 
ATOM   605  C  CB  . ALA A 1 83  ? 96.822  128.619 114.351 1.00 23.93  ? 83  ALA A CB  1 
ATOM   606  N  N   . TRP A 1 84  ? 96.901  125.405 113.451 1.00 29.56  ? 84  TRP A N   1 
ATOM   607  C  CA  . TRP A 1 84  ? 96.919  124.034 113.941 1.00 22.27  ? 84  TRP A CA  1 
ATOM   608  C  C   . TRP A 1 84  ? 97.587  123.065 112.972 1.00 26.02  ? 84  TRP A C   1 
ATOM   609  O  O   . TRP A 1 84  ? 97.516  121.851 113.182 1.00 32.46  ? 84  TRP A O   1 
ATOM   610  C  CB  . TRP A 1 84  ? 95.497  123.571 114.259 1.00 25.40  ? 84  TRP A CB  1 
ATOM   611  C  CG  . TRP A 1 84  ? 94.968  124.131 115.548 1.00 36.28  ? 84  TRP A CG  1 
ATOM   612  C  CD1 . TRP A 1 84  ? 94.306  125.311 115.719 1.00 34.71  ? 84  TRP A CD1 1 
ATOM   613  C  CD2 . TRP A 1 84  ? 95.069  123.538 116.847 1.00 34.23  ? 84  TRP A CD2 1 
ATOM   614  N  NE1 . TRP A 1 84  ? 93.984  125.488 117.040 1.00 28.16  ? 84  TRP A NE1 1 
ATOM   615  C  CE2 . TRP A 1 84  ? 94.441  124.413 117.755 1.00 34.70  ? 84  TRP A CE2 1 
ATOM   616  C  CE3 . TRP A 1 84  ? 95.627  122.352 117.331 1.00 29.71  ? 84  TRP A CE3 1 
ATOM   617  C  CZ2 . TRP A 1 84  ? 94.354  124.139 119.116 1.00 32.55  ? 84  TRP A CZ2 1 
ATOM   618  C  CZ3 . TRP A 1 84  ? 95.540  122.083 118.681 1.00 36.25  ? 84  TRP A CZ3 1 
ATOM   619  C  CH2 . TRP A 1 84  ? 94.909  122.972 119.559 1.00 32.00  ? 84  TRP A CH2 1 
ATOM   620  N  N   . ALA A 1 85  ? 98.230  123.568 111.920 1.00 28.57  ? 85  ALA A N   1 
ATOM   621  C  CA  . ALA A 1 85  ? 99.023  122.735 111.016 1.00 29.43  ? 85  ALA A CA  1 
ATOM   622  C  C   . ALA A 1 85  ? 100.451 122.719 111.544 1.00 35.42  ? 85  ALA A C   1 
ATOM   623  O  O   . ALA A 1 85  ? 101.280 123.557 111.189 1.00 36.72  ? 85  ALA A O   1 
ATOM   624  C  CB  . ALA A 1 85  ? 98.948  123.259 109.588 1.00 22.64  ? 85  ALA A CB  1 
ATOM   625  N  N   . GLN A 1 86  ? 100.743 121.746 112.407 1.00 22.81  ? 86  GLN A N   1 
ATOM   626  C  CA  . GLN A 1 86  ? 101.992 121.716 113.153 1.00 22.92  ? 86  GLN A CA  1 
ATOM   627  C  C   . GLN A 1 86  ? 103.065 120.833 112.529 1.00 24.05  ? 86  GLN A C   1 
ATOM   628  O  O   . GLN A 1 86  ? 104.193 120.820 113.029 1.00 32.67  ? 86  GLN A O   1 
ATOM   629  C  CB  . GLN A 1 86  ? 101.731 121.242 114.588 1.00 28.49  ? 86  GLN A CB  1 
ATOM   630  C  CG  . GLN A 1 86  ? 100.963 122.231 115.444 1.00 25.36  ? 86  GLN A CG  1 
ATOM   631  C  CD  . GLN A 1 86  ? 100.341 121.578 116.657 1.00 29.20  ? 86  GLN A CD  1 
ATOM   632  O  OE1 . GLN A 1 86  ? 99.853  120.453 116.586 1.00 36.49  ? 86  GLN A OE1 1 
ATOM   633  N  NE2 . GLN A 1 86  ? 100.361 122.279 117.781 1.00 22.71  ? 86  GLN A NE2 1 
ATOM   634  N  N   . ALA A 1 87  ? 102.747 120.097 111.465 1.00 20.76  ? 87  ALA A N   1 
ATOM   635  C  CA  . ALA A 1 87  ? 103.716 119.162 110.895 1.00 16.50  ? 87  ALA A CA  1 
ATOM   636  C  C   . ALA A 1 87  ? 104.968 119.837 110.344 1.00 26.75  ? 87  ALA A C   1 
ATOM   637  O  O   . ALA A 1 87  ? 106.076 119.368 110.656 1.00 29.26  ? 87  ALA A O   1 
ATOM   638  C  CB  . ALA A 1 87  ? 103.031 118.299 109.830 1.00 22.18  ? 87  ALA A CB  1 
ATOM   639  N  N   . PRO A 1 88  ? 104.889 120.901 109.532 1.00 31.37  ? 88  PRO A N   1 
ATOM   640  C  CA  . PRO A 1 88  ? 106.130 121.445 108.942 1.00 25.64  ? 88  PRO A CA  1 
ATOM   641  C  C   . PRO A 1 88  ? 107.128 121.966 109.964 1.00 22.57  ? 88  PRO A C   1 
ATOM   642  O  O   . PRO A 1 88  ? 108.311 121.591 109.926 1.00 27.97  ? 88  PRO A O   1 
ATOM   643  C  CB  . PRO A 1 88  ? 105.610 122.566 108.031 1.00 22.41  ? 88  PRO A CB  1 
ATOM   644  C  CG  . PRO A 1 88  ? 104.202 122.200 107.745 1.00 21.99  ? 88  PRO A CG  1 
ATOM   645  C  CD  . PRO A 1 88  ? 103.700 121.592 109.001 1.00 19.22  ? 88  PRO A CD  1 
ATOM   646  N  N   . ILE A 1 89  ? 106.682 122.837 110.871 1.00 25.02  ? 89  ILE A N   1 
ATOM   647  C  CA  . ILE A 1 89  ? 107.581 123.414 111.865 1.00 26.14  ? 89  ILE A CA  1 
ATOM   648  C  C   . ILE A 1 89  ? 108.135 122.328 112.776 1.00 28.62  ? 89  ILE A C   1 
ATOM   649  O  O   . ILE A 1 89  ? 109.321 122.336 113.128 1.00 37.02  ? 89  ILE A O   1 
ATOM   650  C  CB  . ILE A 1 89  ? 106.855 124.515 112.662 1.00 27.15  ? 89  ILE A CB  1 
ATOM   651  C  CG1 . ILE A 1 89  ? 106.534 125.703 111.753 1.00 34.22  ? 89  ILE A CG1 1 
ATOM   652  C  CG2 . ILE A 1 89  ? 107.689 124.963 113.854 1.00 26.23  ? 89  ILE A CG2 1 
ATOM   653  C  CD1 . ILE A 1 89  ? 107.625 126.749 111.695 1.00 28.12  ? 89  ILE A CD1 1 
ATOM   654  N  N   . GLY A 1 90  ? 107.289 121.372 113.166 1.00 10.98  ? 90  GLY A N   1 
ATOM   655  C  CA  . GLY A 1 90  ? 107.758 120.282 114.007 1.00 15.23  ? 90  GLY A CA  1 
ATOM   656  C  C   . GLY A 1 90  ? 108.824 119.439 113.334 1.00 22.27  ? 90  GLY A C   1 
ATOM   657  O  O   . GLY A 1 90  ? 109.847 119.113 113.940 1.00 29.98  ? 90  GLY A O   1 
ATOM   658  N  N   . TYR A 1 91  ? 108.603 119.082 112.066 1.00 20.57  ? 91  TYR A N   1 
ATOM   659  C  CA  . TYR A 1 91  ? 109.591 118.297 111.329 1.00 23.04  ? 91  TYR A CA  1 
ATOM   660  C  C   . TYR A 1 91  ? 110.909 119.051 111.212 1.00 18.25  ? 91  TYR A C   1 
ATOM   661  O  O   . TYR A 1 91  ? 111.988 118.487 111.440 1.00 29.53  ? 91  TYR A O   1 
ATOM   662  C  CB  . TYR A 1 91  ? 109.062 117.952 109.935 1.00 24.36  ? 91  TYR A CB  1 
ATOM   663  C  CG  . TYR A 1 91  ? 108.040 116.837 109.873 1.00 24.16  ? 91  TYR A CG  1 
ATOM   664  C  CD1 . TYR A 1 91  ? 107.274 116.495 110.978 1.00 24.12  ? 91  TYR A CD1 1 
ATOM   665  C  CD2 . TYR A 1 91  ? 107.834 116.135 108.695 1.00 24.88  ? 91  TYR A CD2 1 
ATOM   666  C  CE1 . TYR A 1 91  ? 106.337 115.483 110.910 1.00 23.30  ? 91  TYR A CE1 1 
ATOM   667  C  CE2 . TYR A 1 91  ? 106.903 115.123 108.619 1.00 26.85  ? 91  TYR A CE2 1 
ATOM   668  C  CZ  . TYR A 1 91  ? 106.157 114.801 109.728 1.00 27.25  ? 91  TYR A CZ  1 
ATOM   669  O  OH  . TYR A 1 91  ? 105.228 113.792 109.650 1.00 28.48  ? 91  TYR A OH  1 
ATOM   670  N  N   . SER A 1 92  ? 110.839 120.336 110.848 1.00 11.85  ? 92  SER A N   1 
ATOM   671  C  CA  . SER A 1 92  ? 112.057 121.120 110.673 1.00 13.89  ? 92  SER A CA  1 
ATOM   672  C  C   . SER A 1 92  ? 112.826 121.249 111.980 1.00 20.58  ? 92  SER A C   1 
ATOM   673  O  O   . SER A 1 92  ? 114.054 121.093 112.004 1.00 33.21  ? 92  SER A O   1 
ATOM   674  C  CB  . SER A 1 92  ? 111.714 122.500 110.118 1.00 28.90  ? 92  SER A CB  1 
ATOM   675  O  OG  . SER A 1 92  ? 110.844 122.392 109.008 1.00 38.45  ? 92  SER A OG  1 
ATOM   676  N  N   . LEU A 1 93  ? 112.125 121.529 113.079 1.00 18.09  ? 93  LEU A N   1 
ATOM   677  C  CA  . LEU A 1 93  ? 112.804 121.681 114.359 1.00 16.75  ? 93  LEU A CA  1 
ATOM   678  C  C   . LEU A 1 93  ? 113.385 120.358 114.839 1.00 16.75  ? 93  LEU A C   1 
ATOM   679  O  O   . LEU A 1 93  ? 114.473 120.334 115.424 1.00 29.39  ? 93  LEU A O   1 
ATOM   680  C  CB  . LEU A 1 93  ? 111.848 122.270 115.395 1.00 19.18  ? 93  LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 93  ? 111.680 123.788 115.296 1.00 18.85  ? 93  LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 93  ? 110.833 124.319 116.434 1.00 20.76  ? 93  LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 93  ? 113.034 124.475 115.273 1.00 25.24  ? 93  LEU A CD2 1 
ATOM   684  N  N   . SER A 1 94  ? 112.685 119.246 114.597 1.00 9.80   ? 94  SER A N   1 
ATOM   685  C  CA  . SER A 1 94  ? 113.234 117.944 114.963 1.00 17.68  ? 94  SER A CA  1 
ATOM   686  C  C   . SER A 1 94  ? 114.513 117.649 114.192 1.00 24.39  ? 94  SER A C   1 
ATOM   687  O  O   . SER A 1 94  ? 115.500 117.179 114.770 1.00 21.15  ? 94  SER A O   1 
ATOM   688  C  CB  . SER A 1 94  ? 112.197 116.847 114.722 1.00 9.59   ? 94  SER A CB  1 
ATOM   689  O  OG  . SER A 1 94  ? 112.200 116.422 113.373 1.00 20.29  ? 94  SER A OG  1 
ATOM   690  N  N   . LEU A 1 95  ? 114.521 117.926 112.885 1.00 20.10  ? 95  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 95  ? 115.724 117.684 112.094 1.00 12.31  ? 95  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 95  ? 116.874 118.587 112.531 1.00 18.79  ? 95  LEU A C   1 
ATOM   693  O  O   . LEU A 1 95  ? 118.027 118.144 112.599 1.00 18.56  ? 95  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 95  ? 115.424 117.872 110.608 1.00 18.24  ? 95  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 95  ? 114.754 116.687 109.910 1.00 15.87  ? 95  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 95  ? 114.168 117.112 108.581 1.00 19.68  ? 95  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 95  ? 115.737 115.550 109.722 1.00 9.59   ? 95  LEU A CD2 1 
ATOM   698  N  N   . ILE A 1 96  ? 116.582 119.857 112.829 1.00 17.79  ? 96  ILE A N   1 
ATOM   699  C  CA  . ILE A 1 96  ? 117.629 120.773 113.274 1.00 14.13  ? 96  ILE A CA  1 
ATOM   700  C  C   . ILE A 1 96  ? 118.204 120.323 114.612 1.00 16.67  ? 96  ILE A C   1 
ATOM   701  O  O   . ILE A 1 96  ? 119.424 120.329 114.810 1.00 21.52  ? 96  ILE A O   1 
ATOM   702  C  CB  . ILE A 1 96  ? 117.092 122.215 113.342 1.00 22.61  ? 96  ILE A CB  1 
ATOM   703  C  CG1 . ILE A 1 96  ? 116.885 122.773 111.935 1.00 16.77  ? 96  ILE A CG1 1 
ATOM   704  C  CG2 . ILE A 1 96  ? 118.045 123.110 114.115 1.00 21.00  ? 96  ILE A CG2 1 
ATOM   705  C  CD1 . ILE A 1 96  ? 116.175 124.102 111.911 1.00 19.76  ? 96  ILE A CD1 1 
ATOM   706  N  N   . LEU A 1 97  ? 117.410 119.897 115.562 1.00 13.87  ? 97  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 97  ? 117.883 119.380 116.842 1.00 16.95  ? 97  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 97  ? 118.632 118.124 116.735 1.00 18.31  ? 97  LEU A C   1 
ATOM   709  O  O   . LEU A 1 97  ? 119.534 117.911 117.466 1.00 17.24  ? 97  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 97  ? 116.717 119.189 117.802 1.00 17.74  ? 97  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 97  ? 116.665 119.775 119.195 1.00 21.37  ? 97  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 97  ? 117.131 121.214 119.205 1.00 23.57  ? 97  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 97  ? 115.222 119.684 119.607 1.00 25.34  ? 97  LEU A CD2 1 
ATOM   714  N  N   . GLY A 1 98  ? 118.213 117.259 115.826 1.00 21.69  ? 98  GLY A N   1 
ATOM   715  C  CA  . GLY A 1 98  ? 118.997 116.066 115.570 1.00 9.51   ? 98  GLY A CA  1 
ATOM   716  C  C   . GLY A 1 98  ? 120.378 116.393 115.042 1.00 19.11  ? 98  GLY A C   1 
ATOM   717  O  O   . GLY A 1 98  ? 121.383 115.972 115.612 1.00 20.74  ? 98  GLY A O   1 
ATOM   718  N  N   . GLY A 1 99  ? 120.444 117.204 113.985 1.00 24.31  ? 99  GLY A N   1 
ATOM   719  C  CA  . GLY A 1 99  ? 121.737 117.583 113.440 1.00 9.54   ? 99  GLY A CA  1 
ATOM   720  C  C   . GLY A 1 99  ? 122.618 118.293 114.450 1.00 17.41  ? 99  GLY A C   1 
ATOM   721  O  O   . GLY A 1 99  ? 123.829 118.071 114.494 1.00 24.05  ? 99  GLY A O   1 
ATOM   722  N  N   . LEU A 1 100 ? 122.021 119.141 115.289 1.00 25.21  ? 100 LEU A N   1 
ATOM   723  C  CA  . LEU A 1 100 ? 122.806 119.907 116.250 1.00 25.63  ? 100 LEU A CA  1 
ATOM   724  C  C   . LEU A 1 100 ? 123.402 119.019 117.337 1.00 24.73  ? 100 LEU A C   1 
ATOM   725  O  O   . LEU A 1 100 ? 124.577 119.171 117.688 1.00 26.10  ? 100 LEU A O   1 
ATOM   726  C  CB  . LEU A 1 100 ? 121.944 121.003 116.876 1.00 26.04  ? 100 LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 100 ? 122.139 122.428 116.360 1.00 24.96  ? 100 LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 100 ? 121.244 123.393 117.115 1.00 21.53  ? 100 LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 100 ? 123.593 122.845 116.470 1.00 22.01  ? 100 LEU A CD2 1 
ATOM   730  N  N   . PHE A 1 101 ? 122.618 118.095 117.890 1.00 25.22  ? 101 PHE A N   1 
ATOM   731  C  CA  . PHE A 1 101 ? 123.056 117.375 119.082 1.00 18.05  ? 101 PHE A CA  1 
ATOM   732  C  C   . PHE A 1 101 ? 123.342 115.898 118.860 1.00 24.81  ? 101 PHE A C   1 
ATOM   733  O  O   . PHE A 1 101 ? 124.348 115.395 119.361 1.00 33.37  ? 101 PHE A O   1 
ATOM   734  C  CB  . PHE A 1 101 ? 122.019 117.533 120.197 1.00 17.55  ? 101 PHE A CB  1 
ATOM   735  C  CG  . PHE A 1 101 ? 121.911 118.937 120.713 1.00 23.76  ? 101 PHE A CG  1 
ATOM   736  C  CD1 . PHE A 1 101 ? 122.917 119.480 121.493 1.00 24.09  ? 101 PHE A CD1 1 
ATOM   737  C  CD2 . PHE A 1 101 ? 120.817 119.722 120.400 1.00 23.52  ? 101 PHE A CD2 1 
ATOM   738  C  CE1 . PHE A 1 101 ? 122.828 120.772 121.960 1.00 20.15  ? 101 PHE A CE1 1 
ATOM   739  C  CE2 . PHE A 1 101 ? 120.723 121.015 120.865 1.00 26.96  ? 101 PHE A CE2 1 
ATOM   740  C  CZ  . PHE A 1 101 ? 121.730 121.541 121.646 1.00 24.13  ? 101 PHE A CZ  1 
ATOM   741  N  N   . PHE A 1 102 ? 122.489 115.178 118.141 1.00 28.83  ? 102 PHE A N   1 
ATOM   742  C  CA  . PHE A 1 102 ? 122.724 113.771 117.883 1.00 22.08  ? 102 PHE A CA  1 
ATOM   743  C  C   . PHE A 1 102 ? 123.470 113.633 116.559 1.00 30.06  ? 102 PHE A C   1 
ATOM   744  O  O   . PHE A 1 102 ? 123.848 114.620 115.925 1.00 45.10  ? 102 PHE A O   1 
ATOM   745  C  CB  . PHE A 1 102 ? 121.402 113.000 117.858 1.00 23.34  ? 102 PHE A CB  1 
ATOM   746  C  CG  . PHE A 1 102 ? 120.541 113.217 119.075 1.00 27.13  ? 102 PHE A CG  1 
ATOM   747  C  CD1 . PHE A 1 102 ? 119.758 114.354 119.198 1.00 22.25  ? 102 PHE A CD1 1 
ATOM   748  C  CD2 . PHE A 1 102 ? 120.504 112.276 120.088 1.00 26.14  ? 102 PHE A CD2 1 
ATOM   749  C  CE1 . PHE A 1 102 ? 118.971 114.554 120.312 1.00 19.68  ? 102 PHE A CE1 1 
ATOM   750  C  CE2 . PHE A 1 102 ? 119.713 112.469 121.204 1.00 23.58  ? 102 PHE A CE2 1 
ATOM   751  C  CZ  . PHE A 1 102 ? 118.947 113.609 121.315 1.00 24.23  ? 102 PHE A CZ  1 
ATOM   752  N  N   . ALA A 1 103 ? 123.722 112.388 116.161 1.00 22.01  ? 103 ALA A N   1 
ATOM   753  C  CA  . ALA A 1 103 ? 124.220 112.028 114.837 1.00 31.65  ? 103 ALA A CA  1 
ATOM   754  C  C   . ALA A 1 103 ? 125.686 112.382 114.614 1.00 21.94  ? 103 ALA A C   1 
ATOM   755  O  O   . ALA A 1 103 ? 126.277 111.952 113.620 1.00 35.66  ? 103 ALA A O   1 
ATOM   756  C  CB  . ALA A 1 103 ? 123.368 112.685 113.747 1.00 23.82  ? 103 ALA A CB  1 
ATOM   757  N  N   . LYS A 1 104 ? 126.287 113.159 115.504 1.00 23.69  ? 104 LYS A N   1 
ATOM   758  C  CA  . LYS A 1 104 ? 127.743 113.232 115.514 1.00 25.02  ? 104 LYS A CA  1 
ATOM   759  C  C   . LYS A 1 104 ? 128.331 112.124 116.390 1.00 35.29  ? 104 LYS A C   1 
ATOM   760  O  O   . LYS A 1 104 ? 129.237 111.411 115.940 1.00 34.66  ? 104 LYS A O   1 
ATOM   761  C  CB  . LYS A 1 104 ? 128.227 114.614 115.954 1.00 34.68  ? 104 LYS A CB  1 
ATOM   762  C  CG  . LYS A 1 104 ? 129.715 114.828 115.743 1.00 35.45  ? 104 LYS A CG  1 
ATOM   763  C  CD  . LYS A 1 104 ? 129.994 116.182 115.121 1.00 29.22  ? 104 LYS A CD  1 
ATOM   764  C  CE  . LYS A 1 104 ? 131.484 116.407 114.941 1.00 32.84  ? 104 LYS A CE  1 
ATOM   765  N  NZ  . LYS A 1 104 ? 131.765 117.645 114.166 1.00 41.36  ? 104 LYS A NZ  1 
ATOM   766  N  N   . PRO A 1 105 ? 127.860 111.938 117.634 1.00 33.58  ? 105 PRO A N   1 
ATOM   767  C  CA  . PRO A 1 105 ? 128.370 110.807 118.425 1.00 32.71  ? 105 PRO A CA  1 
ATOM   768  C  C   . PRO A 1 105 ? 128.011 109.451 117.848 1.00 31.41  ? 105 PRO A C   1 
ATOM   769  O  O   . PRO A 1 105 ? 128.744 108.483 118.077 1.00 40.45  ? 105 PRO A O   1 
ATOM   770  C  CB  . PRO A 1 105 ? 127.731 111.015 119.807 1.00 29.52  ? 105 PRO A CB  1 
ATOM   771  C  CG  . PRO A 1 105 ? 127.262 112.412 119.822 1.00 21.36  ? 105 PRO A CG  1 
ATOM   772  C  CD  . PRO A 1 105 ? 126.917 112.752 118.422 1.00 22.22  ? 105 PRO A CD  1 
ATOM   773  N  N   . MET A 1 106 ? 126.895 109.343 117.126 1.00 23.11  ? 106 MET A N   1 
ATOM   774  C  CA  . MET A 1 106 ? 126.516 108.063 116.542 1.00 24.14  ? 106 MET A CA  1 
ATOM   775  C  C   . MET A 1 106 ? 127.382 107.718 115.337 1.00 23.28  ? 106 MET A C   1 
ATOM   776  O  O   . MET A 1 106 ? 127.783 106.561 115.170 1.00 26.67  ? 106 MET A O   1 
ATOM   777  C  CB  . MET A 1 106 ? 125.037 108.080 116.155 1.00 22.86  ? 106 MET A CB  1 
ATOM   778  C  CG  . MET A 1 106 ? 124.097 108.301 117.327 1.00 23.62  ? 106 MET A CG  1 
ATOM   779  S  SD  . MET A 1 106 ? 123.758 106.802 118.270 1.00 42.36  ? 106 MET A SD  1 
ATOM   780  C  CE  . MET A 1 106 ? 123.005 105.767 117.020 1.00 22.01  ? 106 MET A CE  1 
ATOM   781  N  N   . ARG A 1 107 ? 127.677 108.702 114.485 1.00 18.20  ? 107 ARG A N   1 
ATOM   782  C  CA  . ARG A 1 107 ? 128.534 108.457 113.331 1.00 20.38  ? 107 ARG A CA  1 
ATOM   783  C  C   . ARG A 1 107 ? 130.002 108.341 113.724 1.00 29.07  ? 107 ARG A C   1 
ATOM   784  O  O   . ARG A 1 107 ? 130.772 107.669 113.030 1.00 31.78  ? 107 ARG A O   1 
ATOM   785  C  CB  . ARG A 1 107 ? 128.345 109.567 112.295 1.00 21.70  ? 107 ARG A CB  1 
ATOM   786  C  CG  . ARG A 1 107 ? 129.110 109.362 110.997 1.00 21.38  ? 107 ARG A CG  1 
ATOM   787  C  CD  . ARG A 1 107 ? 128.867 107.984 110.408 1.00 21.06  ? 107 ARG A CD  1 
ATOM   788  N  NE  . ARG A 1 107 ? 129.703 107.733 109.241 1.00 22.47  ? 107 ARG A NE  1 
ATOM   789  C  CZ  . ARG A 1 107 ? 130.956 107.302 109.293 1.00 20.40  ? 107 ARG A CZ  1 
ATOM   790  N  NH1 . ARG A 1 107 ? 131.558 107.063 110.446 1.00 23.01  ? 107 ARG A NH1 1 
ATOM   791  N  NH2 . ARG A 1 107 ? 131.623 107.106 108.160 1.00 15.92  ? 107 ARG A NH2 1 
ATOM   792  N  N   . SER A 1 108 ? 130.408 108.977 114.825 1.00 24.45  ? 108 SER A N   1 
ATOM   793  C  CA  . SER A 1 108 ? 131.795 108.867 115.264 1.00 22.55  ? 108 SER A CA  1 
ATOM   794  C  C   . SER A 1 108 ? 132.138 107.454 115.717 1.00 36.72  ? 108 SER A C   1 
ATOM   795  O  O   . SER A 1 108 ? 133.295 107.035 115.605 1.00 40.67  ? 108 SER A O   1 
ATOM   796  C  CB  . SER A 1 108 ? 132.070 109.861 116.391 1.00 27.65  ? 108 SER A CB  1 
ATOM   797  O  OG  . SER A 1 108 ? 132.118 111.188 115.899 1.00 43.12  ? 108 SER A OG  1 
ATOM   798  N  N   . LYS A 1 109 ? 131.161 106.711 116.230 1.00 27.29  ? 109 LYS A N   1 
ATOM   799  C  CA  . LYS A 1 109 ? 131.400 105.373 116.754 1.00 26.39  ? 109 LYS A CA  1 
ATOM   800  C  C   . LYS A 1 109 ? 131.228 104.276 115.712 1.00 32.33  ? 109 LYS A C   1 
ATOM   801  O  O   . LYS A 1 109 ? 131.498 103.110 116.016 1.00 37.59  ? 109 LYS A O   1 
ATOM   802  C  CB  . LYS A 1 109 ? 130.476 105.102 117.942 1.00 19.30  ? 109 LYS A CB  1 
ATOM   803  C  CG  . LYS A 1 109 ? 130.804 105.926 119.169 1.00 27.82  ? 109 LYS A CG  1 
ATOM   804  C  CD  . LYS A 1 109 ? 130.880 105.058 120.409 1.00 32.91  ? 109 LYS A CD  1 
ATOM   805  C  CE  . LYS A 1 109 ? 131.929 105.572 121.376 1.00 39.17  ? 109 LYS A CE  1 
ATOM   806  N  NZ  . LYS A 1 109 ? 131.593 105.238 122.787 1.00 42.23  ? 109 LYS A NZ  1 
ATOM   807  N  N   . GLY A 1 110 ? 130.796 104.614 114.501 1.00 25.22  ? 110 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 110 ? 130.662 103.632 113.444 1.00 24.28  ? 110 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 110 ? 129.646 102.546 113.729 1.00 25.24  ? 110 GLY A C   1 
ATOM   810  O  O   . GLY A 1 110 ? 129.923 101.360 113.533 1.00 25.30  ? 110 GLY A O   1 
ATOM   811  N  N   . TYR A 1 111 ? 128.468 102.939 114.202 1.00 27.60  ? 111 TYR A N   1 
ATOM   812  C  CA  . TYR A 1 111 ? 127.394 101.994 114.453 1.00 22.87  ? 111 TYR A CA  1 
ATOM   813  C  C   . TYR A 1 111 ? 126.752 101.550 113.140 1.00 26.30  ? 111 TYR A C   1 
ATOM   814  O  O   . TYR A 1 111 ? 126.823 102.236 112.118 1.00 34.48  ? 111 TYR A O   1 
ATOM   815  C  CB  . TYR A 1 111 ? 126.337 102.610 115.369 1.00 26.05  ? 111 TYR A CB  1 
ATOM   816  C  CG  . TYR A 1 111 ? 126.792 102.815 116.795 1.00 24.71  ? 111 TYR A CG  1 
ATOM   817  C  CD1 . TYR A 1 111 ? 127.437 101.805 117.491 1.00 25.13  ? 111 TYR A CD1 1 
ATOM   818  C  CD2 . TYR A 1 111 ? 126.571 104.019 117.447 1.00 17.11  ? 111 TYR A CD2 1 
ATOM   819  C  CE1 . TYR A 1 111 ? 127.850 101.988 118.793 1.00 24.39  ? 111 TYR A CE1 1 
ATOM   820  C  CE2 . TYR A 1 111 ? 126.980 104.212 118.747 1.00 22.12  ? 111 TYR A CE2 1 
ATOM   821  C  CZ  . TYR A 1 111 ? 127.619 103.192 119.416 1.00 29.91  ? 111 TYR A CZ  1 
ATOM   822  O  OH  . TYR A 1 111 ? 128.030 103.378 120.715 1.00 29.18  ? 111 TYR A OH  1 
ATOM   823  N  N   . VAL A 1 112 ? 126.122 100.381 113.180 1.00 22.45  ? 112 VAL A N   1 
ATOM   824  C  CA  . VAL A 1 112 ? 125.414 99.837  112.029 1.00 24.61  ? 112 VAL A CA  1 
ATOM   825  C  C   . VAL A 1 112 ? 123.914 100.082 112.127 1.00 29.36  ? 112 VAL A C   1 
ATOM   826  O  O   . VAL A 1 112 ? 123.270 100.412 111.130 1.00 26.45  ? 112 VAL A O   1 
ATOM   827  C  CB  . VAL A 1 112 ? 125.724 98.332  111.876 1.00 27.14  ? 112 VAL A CB  1 
ATOM   828  C  CG1 . VAL A 1 112 ? 125.026 97.762  110.652 1.00 25.23  ? 112 VAL A CG1 1 
ATOM   829  C  CG2 . VAL A 1 112 ? 127.224 98.104  111.789 1.00 25.40  ? 112 VAL A CG2 1 
ATOM   830  N  N   . THR A 1 113 ? 123.348 99.931  113.321 1.00 29.32  ? 113 THR A N   1 
ATOM   831  C  CA  . THR A 1 113 ? 121.922 100.105 113.549 1.00 23.98  ? 113 THR A CA  1 
ATOM   832  C  C   . THR A 1 113 ? 121.742 100.895 114.841 1.00 28.17  ? 113 THR A C   1 
ATOM   833  O  O   . THR A 1 113 ? 122.604 100.878 115.723 1.00 30.86  ? 113 THR A O   1 
ATOM   834  C  CB  . THR A 1 113 ? 121.209 98.737  113.600 1.00 25.70  ? 113 THR A CB  1 
ATOM   835  O  OG1 . THR A 1 113 ? 121.201 98.156  112.292 1.00 27.89  ? 113 THR A OG1 1 
ATOM   836  C  CG2 . THR A 1 113 ? 119.774 98.863  114.066 1.00 29.35  ? 113 THR A CG2 1 
ATOM   837  N  N   . MET A 1 114 ? 120.621 101.616 114.934 1.00 26.56  ? 114 MET A N   1 
ATOM   838  C  CA  . MET A 1 114 ? 120.329 102.424 116.113 1.00 18.89  ? 114 MET A CA  1 
ATOM   839  C  C   . MET A 1 114 ? 120.298 101.600 117.397 1.00 27.64  ? 114 MET A C   1 
ATOM   840  O  O   . MET A 1 114 ? 120.563 102.141 118.475 1.00 38.03  ? 114 MET A O   1 
ATOM   841  C  CB  . MET A 1 114 ? 118.999 103.158 115.912 1.00 20.51  ? 114 MET A CB  1 
ATOM   842  C  CG  . MET A 1 114 ? 118.411 103.800 117.159 1.00 33.05  ? 114 MET A CG  1 
ATOM   843  S  SD  . MET A 1 114 ? 116.805 104.563 116.870 1.00 46.38  ? 114 MET A SD  1 
ATOM   844  C  CE  . MET A 1 114 ? 115.707 103.217 117.300 1.00 21.24  ? 114 MET A CE  1 
ATOM   845  N  N   . LEU A 1 115 ? 120.004 100.302 117.309 1.00 24.52  ? 115 LEU A N   1 
ATOM   846  C  CA  . LEU A 1 115 ? 119.932 99.460  118.497 1.00 25.00  ? 115 LEU A CA  1 
ATOM   847  C  C   . LEU A 1 115 ? 121.295 99.000  119.000 1.00 20.27  ? 115 LEU A C   1 
ATOM   848  O  O   . LEU A 1 115 ? 121.356 98.352  120.049 1.00 32.17  ? 115 LEU A O   1 
ATOM   849  C  CB  . LEU A 1 115 ? 119.056 98.234  118.228 1.00 28.24  ? 115 LEU A CB  1 
ATOM   850  C  CG  . LEU A 1 115 ? 117.570 98.467  117.952 1.00 26.66  ? 115 LEU A CG  1 
ATOM   851  C  CD1 . LEU A 1 115 ? 116.852 97.141  117.791 1.00 23.72  ? 115 LEU A CD1 1 
ATOM   852  C  CD2 . LEU A 1 115 ? 116.936 99.289  119.057 1.00 27.27  ? 115 LEU A CD2 1 
ATOM   853  N  N   . ASP A 1 116 ? 122.379 99.299  118.284 1.00 23.29  ? 116 ASP A N   1 
ATOM   854  C  CA  . ASP A 1 116 ? 123.704 98.881  118.742 1.00 24.45  ? 116 ASP A CA  1 
ATOM   855  C  C   . ASP A 1 116 ? 124.109 99.511  120.071 1.00 31.54  ? 116 ASP A C   1 
ATOM   856  O  O   . ASP A 1 116 ? 124.577 98.771  120.957 1.00 34.53  ? 116 ASP A O   1 
ATOM   857  C  CB  . ASP A 1 116 ? 124.742 99.166  117.650 1.00 23.70  ? 116 ASP A CB  1 
ATOM   858  C  CG  . ASP A 1 116 ? 124.632 98.215  116.479 1.00 37.16  ? 116 ASP A CG  1 
ATOM   859  O  OD1 . ASP A 1 116 ? 123.551 97.623  116.290 1.00 40.15  ? 116 ASP A OD1 1 
ATOM   860  O  OD2 . ASP A 1 116 ? 125.630 98.054  115.748 1.00 37.16  ? 116 ASP A OD2 1 
ATOM   861  N  N   . PRO A 1 117 ? 123.996 100.833 120.282 1.00 31.55  ? 117 PRO A N   1 
ATOM   862  C  CA  . PRO A 1 117 ? 124.346 101.373 121.609 1.00 26.75  ? 117 PRO A CA  1 
ATOM   863  C  C   . PRO A 1 117 ? 123.516 100.783 122.734 1.00 29.27  ? 117 PRO A C   1 
ATOM   864  O  O   . PRO A 1 117 ? 124.056 100.478 123.806 1.00 36.17  ? 117 PRO A O   1 
ATOM   865  C  CB  . PRO A 1 117 ? 124.100 102.882 121.462 1.00 25.67  ? 117 PRO A CB  1 
ATOM   866  C  CG  . PRO A 1 117 ? 123.339 103.060 120.210 1.00 18.84  ? 117 PRO A CG  1 
ATOM   867  C  CD  . PRO A 1 117 ? 123.628 101.900 119.335 1.00 22.78  ? 117 PRO A CD  1 
ATOM   868  N  N   . PHE A 1 118 ? 122.212 100.597 122.507 1.00 20.74  ? 118 PHE A N   1 
ATOM   869  C  CA  . PHE A 1 118 ? 121.351 100.031 123.539 1.00 23.92  ? 118 PHE A CA  1 
ATOM   870  C  C   . PHE A 1 118 ? 121.825 98.643  123.937 1.00 28.00  ? 118 PHE A C   1 
ATOM   871  O  O   . PHE A 1 118 ? 121.951 98.335  125.127 1.00 24.30  ? 118 PHE A O   1 
ATOM   872  C  CB  . PHE A 1 118 ? 119.905 99.975  123.047 1.00 23.24  ? 118 PHE A CB  1 
ATOM   873  C  CG  . PHE A 1 118 ? 119.255 101.318 122.913 1.00 24.53  ? 118 PHE A CG  1 
ATOM   874  C  CD1 . PHE A 1 118 ? 119.110 102.145 124.011 1.00 22.12  ? 118 PHE A CD1 1 
ATOM   875  C  CD2 . PHE A 1 118 ? 118.776 101.749 121.689 1.00 28.09  ? 118 PHE A CD2 1 
ATOM   876  C  CE1 . PHE A 1 118 ? 118.509 103.377 123.887 1.00 28.33  ? 118 PHE A CE1 1 
ATOM   877  C  CE2 . PHE A 1 118 ? 118.173 102.980 121.562 1.00 27.43  ? 118 PHE A CE2 1 
ATOM   878  C  CZ  . PHE A 1 118 ? 118.040 103.795 122.661 1.00 27.40  ? 118 PHE A CZ  1 
ATOM   879  N  N   . GLN A 1 119 ? 122.107 97.795  122.947 1.00 35.61  ? 119 GLN A N   1 
ATOM   880  C  CA  . GLN A 1 119 ? 122.581 96.449  123.243 1.00 30.11  ? 119 GLN A CA  1 
ATOM   881  C  C   . GLN A 1 119 ? 123.908 96.492  123.983 1.00 35.63  ? 119 GLN A C   1 
ATOM   882  O  O   . GLN A 1 119 ? 124.024 95.952  125.087 1.00 43.66  ? 119 GLN A O   1 
ATOM   883  C  CB  . GLN A 1 119 ? 122.706 95.640  121.954 1.00 26.32  ? 119 GLN A CB  1 
ATOM   884  C  CG  . GLN A 1 119 ? 121.378 95.216  121.365 1.00 32.55  ? 119 GLN A CG  1 
ATOM   885  C  CD  . GLN A 1 119 ? 121.519 94.083  120.377 1.00 39.62  ? 119 GLN A CD  1 
ATOM   886  O  OE1 . GLN A 1 119 ? 122.381 94.113  119.502 1.00 44.37  ? 119 GLN A OE1 1 
ATOM   887  N  NE2 . GLN A 1 119 ? 120.670 93.073  120.510 1.00 41.91  ? 119 GLN A NE2 1 
ATOM   888  N  N   . GLN A 1 120 ? 124.892 97.207  123.430 1.00 38.44  ? 120 GLN A N   1 
ATOM   889  C  CA  . GLN A 1 120 ? 126.231 97.206  124.008 1.00 36.37  ? 120 GLN A CA  1 
ATOM   890  C  C   . GLN A 1 120 ? 126.281 97.823  125.399 1.00 35.65  ? 120 GLN A C   1 
ATOM   891  O  O   . GLN A 1 120 ? 127.205 97.518  126.159 1.00 37.55  ? 120 GLN A O   1 
ATOM   892  C  CB  . GLN A 1 120 ? 127.204 97.940  123.084 1.00 37.53  ? 120 GLN A CB  1 
ATOM   893  C  CG  . GLN A 1 120 ? 127.358 97.304  121.714 1.00 39.05  ? 120 GLN A CG  1 
ATOM   894  C  CD  . GLN A 1 120 ? 128.206 98.139  120.778 1.00 43.01  ? 120 GLN A CD  1 
ATOM   895  O  OE1 . GLN A 1 120 ? 128.724 99.186  121.161 1.00 46.35  ? 120 GLN A OE1 1 
ATOM   896  N  NE2 . GLN A 1 120 ? 128.350 97.680  119.541 1.00 41.20  ? 120 GLN A NE2 1 
ATOM   897  N  N   . ILE A 1 121 ? 125.324 98.674  125.760 1.00 35.27  ? 121 ILE A N   1 
ATOM   898  C  CA  . ILE A 1 121 ? 125.326 99.306  127.073 1.00 34.81  ? 121 ILE A CA  1 
ATOM   899  C  C   . ILE A 1 121 ? 124.472 98.537  128.078 1.00 34.90  ? 121 ILE A C   1 
ATOM   900  O  O   . ILE A 1 121 ? 124.856 98.408  129.240 1.00 37.22  ? 121 ILE A O   1 
ATOM   901  C  CB  . ILE A 1 121 ? 124.881 100.781 126.960 1.00 38.23  ? 121 ILE A CB  1 
ATOM   902  C  CG1 . ILE A 1 121 ? 126.013 101.623 126.369 1.00 42.17  ? 121 ILE A CG1 1 
ATOM   903  C  CG2 . ILE A 1 121 ? 124.501 101.342 128.317 1.00 32.18  ? 121 ILE A CG2 1 
ATOM   904  C  CD1 . ILE A 1 121 ? 125.546 102.808 125.556 1.00 38.75  ? 121 ILE A CD1 1 
ATOM   905  N  N   . TYR A 1 122 ? 123.327 97.994  127.661 1.00 34.82  ? 122 TYR A N   1 
ATOM   906  C  CA  . TYR A 1 122 ? 122.414 97.339  128.591 1.00 34.00  ? 122 TYR A CA  1 
ATOM   907  C  C   . TYR A 1 122 ? 122.478 95.817  128.532 1.00 38.50  ? 122 TYR A C   1 
ATOM   908  O  O   . TYR A 1 122 ? 122.624 95.167  129.570 1.00 49.32  ? 122 TYR A O   1 
ATOM   909  C  CB  . TYR A 1 122 ? 120.976 97.803  128.329 1.00 34.49  ? 122 TYR A CB  1 
ATOM   910  C  CG  . TYR A 1 122 ? 120.734 99.264  128.628 1.00 39.53  ? 122 TYR A CG  1 
ATOM   911  C  CD1 . TYR A 1 122 ? 121.292 99.867  129.746 1.00 40.25  ? 122 TYR A CD1 1 
ATOM   912  C  CD2 . TYR A 1 122 ? 119.948 100.040 127.790 1.00 37.86  ? 122 TYR A CD2 1 
ATOM   913  C  CE1 . TYR A 1 122 ? 121.073 101.201 130.021 1.00 36.73  ? 122 TYR A CE1 1 
ATOM   914  C  CE2 . TYR A 1 122 ? 119.723 101.373 128.057 1.00 32.74  ? 122 TYR A CE2 1 
ATOM   915  C  CZ  . TYR A 1 122 ? 120.288 101.949 129.172 1.00 38.80  ? 122 TYR A CZ  1 
ATOM   916  O  OH  . TYR A 1 122 ? 120.065 103.279 129.439 1.00 39.73  ? 122 TYR A OH  1 
ATOM   917  N  N   . GLY A 1 123 ? 122.364 95.232  127.353 1.00 38.99  ? 123 GLY A N   1 
ATOM   918  C  CA  . GLY A 1 123 ? 122.210 93.797  127.216 1.00 34.31  ? 123 GLY A CA  1 
ATOM   919  C  C   . GLY A 1 123 ? 121.333 93.453  126.028 1.00 39.53  ? 123 GLY A C   1 
ATOM   920  O  O   . GLY A 1 123 ? 120.537 94.261  125.543 1.00 42.70  ? 123 GLY A O   1 
ATOM   921  N  N   . LYS A 1 124 ? 121.481 92.215  125.552 1.00 45.98  ? 124 LYS A N   1 
ATOM   922  C  CA  . LYS A 1 124 ? 120.716 91.764  124.395 1.00 42.45  ? 124 LYS A CA  1 
ATOM   923  C  C   . LYS A 1 124 ? 119.225 91.711  124.701 1.00 42.03  ? 124 LYS A C   1 
ATOM   924  O  O   . LYS A 1 124 ? 118.395 91.985  123.828 1.00 40.21  ? 124 LYS A O   1 
ATOM   925  C  CB  . LYS A 1 124 ? 121.219 90.397  123.934 1.00 41.68  ? 124 LYS A CB  1 
ATOM   926  C  CG  . LYS A 1 124 ? 122.715 90.339  123.690 1.00 40.04  ? 124 LYS A CG  1 
ATOM   927  C  CD  . LYS A 1 124 ? 123.070 90.886  122.319 1.00 43.83  ? 124 LYS A CD  1 
ATOM   928  C  CE  . LYS A 1 124 ? 124.465 90.457  121.895 1.00 46.34  ? 124 LYS A CE  1 
ATOM   929  N  NZ  . LYS A 1 124 ? 124.906 89.216  122.588 1.00 43.77  ? 124 LYS A NZ  1 
ATOM   930  N  N   . ARG A 1 125 ? 118.864 91.356  125.936 1.00 45.16  ? 125 ARG A N   1 
ATOM   931  C  CA  . ARG A 1 125 ? 117.452 91.288  126.296 1.00 45.27  ? 125 ARG A CA  1 
ATOM   932  C  C   . ARG A 1 125 ? 116.796 92.664  126.258 1.00 46.09  ? 125 ARG A C   1 
ATOM   933  O  O   . ARG A 1 125 ? 115.682 92.810  125.744 1.00 52.04  ? 125 ARG A O   1 
ATOM   934  C  CB  . ARG A 1 125 ? 117.295 90.645  127.672 1.00 49.58  ? 125 ARG A CB  1 
ATOM   935  C  CG  . ARG A 1 125 ? 117.304 89.127  127.632 1.00 49.68  ? 125 ARG A CG  1 
ATOM   936  C  CD  . ARG A 1 125 ? 116.789 88.532  128.928 1.00 51.55  ? 125 ARG A CD  1 
ATOM   937  N  NE  . ARG A 1 125 ? 117.659 88.846  130.054 1.00 55.68  ? 125 ARG A NE  1 
ATOM   938  C  CZ  . ARG A 1 125 ? 118.610 88.043  130.510 1.00 56.73  ? 125 ARG A CZ  1 
ATOM   939  N  NH1 . ARG A 1 125 ? 118.844 86.865  129.957 1.00 54.60  ? 125 ARG A NH1 1 
ATOM   940  N  NH2 . ARG A 1 125 ? 119.345 88.433  131.547 1.00 55.78  ? 125 ARG A NH2 1 
ATOM   941  N  N   . MET A 1 126 ? 117.470 93.688  126.786 1.00 42.79  ? 126 MET A N   1 
ATOM   942  C  CA  . MET A 1 126 ? 116.928 95.042  126.703 1.00 41.44  ? 126 MET A CA  1 
ATOM   943  C  C   . MET A 1 126 ? 116.909 95.542  125.263 1.00 41.23  ? 126 MET A C   1 
ATOM   944  O  O   . MET A 1 126 ? 115.959 96.220  124.847 1.00 45.99  ? 126 MET A O   1 
ATOM   945  C  CB  . MET A 1 126 ? 117.731 95.991  127.591 1.00 43.71  ? 126 MET A CB  1 
ATOM   946  C  CG  . MET A 1 126 ? 117.255 96.049  129.033 1.00 45.35  ? 126 MET A CG  1 
ATOM   947  S  SD  . MET A 1 126 ? 115.556 96.629  129.216 1.00 67.49  ? 126 MET A SD  1 
ATOM   948  C  CE  . MET A 1 126 ? 115.587 98.123  128.231 1.00 41.07  ? 126 MET A CE  1 
ATOM   949  N  N   . GLY A 1 127 ? 117.948 95.221  124.488 1.00 34.40  ? 127 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 127 ? 117.951 95.602  123.086 1.00 35.02  ? 127 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 127 ? 116.806 94.980  122.309 1.00 43.87  ? 127 GLY A C   1 
ATOM   952  O  O   . GLY A 1 127 ? 116.260 95.593  121.391 1.00 43.66  ? 127 GLY A O   1 
ATOM   953  N  N   . GLY A 1 128 ? 116.439 93.744  122.657 1.00 40.42  ? 128 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 128 ? 115.304 93.104  122.019 1.00 28.34  ? 128 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 128 ? 113.967 93.601  122.518 1.00 33.59  ? 128 GLY A C   1 
ATOM   956  O  O   . GLY A 1 128 ? 112.992 93.620  121.762 1.00 46.41  ? 128 GLY A O   1 
ATOM   957  N  N   . LEU A 1 129 ? 113.892 93.997  123.790 1.00 36.63  ? 129 LEU A N   1 
ATOM   958  C  CA  . LEU A 1 129 ? 112.670 94.607  124.304 1.00 31.02  ? 129 LEU A CA  1 
ATOM   959  C  C   . LEU A 1 129 ? 112.399 95.944  123.628 1.00 28.70  ? 129 LEU A C   1 
ATOM   960  O  O   . LEU A 1 129 ? 111.244 96.285  123.354 1.00 35.80  ? 129 LEU A O   1 
ATOM   961  C  CB  . LEU A 1 129 ? 112.762 94.782  125.819 1.00 33.89  ? 129 LEU A CB  1 
ATOM   962  C  CG  . LEU A 1 129 ? 112.264 93.624  126.684 1.00 33.34  ? 129 LEU A CG  1 
ATOM   963  C  CD1 . LEU A 1 129 ? 112.823 93.737  128.090 1.00 34.10  ? 129 LEU A CD1 1 
ATOM   964  C  CD2 . LEU A 1 129 ? 110.748 93.587  126.715 1.00 33.94  ? 129 LEU A CD2 1 
ATOM   965  N  N   . LEU A 1 130 ? 113.454 96.690  123.317 1.00 29.34  ? 130 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 130 ? 113.291 97.987  122.658 1.00 20.50  ? 130 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 130 ? 112.994 97.860  121.165 1.00 22.38  ? 130 LEU A C   1 
ATOM   968  O  O   . LEU A 1 130 ? 112.798 98.866  120.484 1.00 33.30  ? 130 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 130 ? 114.529 98.862  122.870 1.00 30.04  ? 130 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 130 ? 114.391 100.027 123.854 1.00 30.50  ? 130 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 130 ? 113.318 100.999 123.395 1.00 33.86  ? 130 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 130 ? 114.085 99.527  125.254 1.00 27.25  ? 130 LEU A CD2 1 
ATOM   973  N  N   . PHE A 1 131 ? 112.959 96.633  120.655 1.00 25.45  ? 131 PHE A N   1 
ATOM   974  C  CA  . PHE A 1 131 ? 112.713 96.424  119.231 1.00 24.32  ? 131 PHE A CA  1 
ATOM   975  C  C   . PHE A 1 131 ? 111.232 96.509  118.867 1.00 29.60  ? 131 PHE A C   1 
ATOM   976  O  O   . PHE A 1 131 ? 110.901 96.914  117.748 1.00 34.84  ? 131 PHE A O   1 
ATOM   977  C  CB  . PHE A 1 131 ? 113.288 95.070  118.808 1.00 23.49  ? 131 PHE A CB  1 
ATOM   978  C  CG  . PHE A 1 131 ? 112.927 94.658  117.408 1.00 30.48  ? 131 PHE A CG  1 
ATOM   979  C  CD1 . PHE A 1 131 ? 113.305 95.428  116.323 1.00 28.96  ? 131 PHE A CD1 1 
ATOM   980  C  CD2 . PHE A 1 131 ? 112.216 93.492  117.179 1.00 22.39  ? 131 PHE A CD2 1 
ATOM   981  C  CE1 . PHE A 1 131 ? 112.976 95.047  115.039 1.00 20.87  ? 131 PHE A CE1 1 
ATOM   982  C  CE2 . PHE A 1 131 ? 111.885 93.108  115.898 1.00 23.79  ? 131 PHE A CE2 1 
ATOM   983  C  CZ  . PHE A 1 131 ? 112.265 93.886  114.826 1.00 25.65  ? 131 PHE A CZ  1 
ATOM   984  N  N   . ILE A 1 132 ? 110.336 96.127  119.781 1.00 22.79  ? 132 ILE A N   1 
ATOM   985  C  CA  . ILE A 1 132 ? 108.909 96.074  119.449 1.00 23.31  ? 132 ILE A CA  1 
ATOM   986  C  C   . ILE A 1 132 ? 108.328 97.441  119.096 1.00 32.56  ? 132 ILE A C   1 
ATOM   987  O  O   . ILE A 1 132 ? 107.649 97.549  118.059 1.00 35.34  ? 132 ILE A O   1 
ATOM   988  C  CB  . ILE A 1 132 ? 108.131 95.378  120.581 1.00 25.57  ? 132 ILE A CB  1 
ATOM   989  C  CG1 . ILE A 1 132 ? 108.796 94.050  120.945 1.00 22.74  ? 132 ILE A CG1 1 
ATOM   990  C  CG2 . ILE A 1 132 ? 106.681 95.165  120.185 1.00 27.35  ? 132 ILE A CG2 1 
ATOM   991  C  CD1 . ILE A 1 132 ? 108.260 93.431  122.211 1.00 22.08  ? 132 ILE A CD1 1 
ATOM   992  N  N   . PRO A 1 133 ? 108.517 98.503  119.898 1.00 25.35  ? 133 PRO A N   1 
ATOM   993  C  CA  . PRO A 1 133 ? 107.915 99.796  119.524 1.00 20.22  ? 133 PRO A CA  1 
ATOM   994  C  C   . PRO A 1 133 ? 108.380 100.326 118.179 1.00 20.07  ? 133 PRO A C   1 
ATOM   995  O  O   . PRO A 1 133 ? 107.573 100.896 117.436 1.00 32.00  ? 133 PRO A O   1 
ATOM   996  C  CB  . PRO A 1 133 ? 108.332 100.720 120.676 1.00 24.35  ? 133 PRO A CB  1 
ATOM   997  C  CG  . PRO A 1 133 ? 108.594 99.814  121.812 1.00 18.94  ? 133 PRO A CG  1 
ATOM   998  C  CD  . PRO A 1 133 ? 109.189 98.589  121.208 1.00 18.05  ? 133 PRO A CD  1 
ATOM   999  N  N   . ALA A 1 134 ? 109.658 100.147 117.838 1.00 20.06  ? 134 ALA A N   1 
ATOM   1000 C  CA  . ALA A 1 134 ? 110.153 100.622 116.549 1.00 20.58  ? 134 ALA A CA  1 
ATOM   1001 C  C   . ALA A 1 134 ? 109.491 99.884  115.392 1.00 26.26  ? 134 ALA A C   1 
ATOM   1002 O  O   . ALA A 1 134 ? 109.071 100.503 114.405 1.00 37.22  ? 134 ALA A O   1 
ATOM   1003 C  CB  . ALA A 1 134 ? 111.671 100.467 116.487 1.00 25.52  ? 134 ALA A CB  1 
ATOM   1004 N  N   . LEU A 1 135 ? 109.384 98.557  115.500 1.00 16.92  ? 135 LEU A N   1 
ATOM   1005 C  CA  . LEU A 1 135 ? 108.743 97.773  114.451 1.00 15.33  ? 135 LEU A CA  1 
ATOM   1006 C  C   . LEU A 1 135 ? 107.279 98.159  114.291 1.00 24.51  ? 135 LEU A C   1 
ATOM   1007 O  O   . LEU A 1 135 ? 106.784 98.300  113.163 1.00 34.86  ? 135 LEU A O   1 
ATOM   1008 C  CB  . LEU A 1 135 ? 108.877 96.283  114.763 1.00 20.45  ? 135 LEU A CB  1 
ATOM   1009 C  CG  . LEU A 1 135 ? 108.105 95.305  113.878 1.00 23.44  ? 135 LEU A CG  1 
ATOM   1010 C  CD1 . LEU A 1 135 ? 108.795 95.137  112.537 1.00 22.67  ? 135 LEU A CD1 1 
ATOM   1011 C  CD2 . LEU A 1 135 ? 107.950 93.967  114.575 1.00 21.70  ? 135 LEU A CD2 1 
ATOM   1012 N  N   . MET A 1 136 ? 106.571 98.339  115.410 1.00 22.41  ? 136 MET A N   1 
ATOM   1013 C  CA  . MET A 1 136 ? 105.175 98.755  115.331 1.00 17.69  ? 136 MET A CA  1 
ATOM   1014 C  C   . MET A 1 136 ? 105.046 100.129 114.686 1.00 20.36  ? 136 MET A C   1 
ATOM   1015 O  O   . MET A 1 136 ? 104.161 100.351 113.850 1.00 28.94  ? 136 MET A O   1 
ATOM   1016 C  CB  . MET A 1 136 ? 104.545 98.751  116.724 1.00 16.63  ? 136 MET A CB  1 
ATOM   1017 C  CG  . MET A 1 136 ? 103.748 97.498  117.038 1.00 26.40  ? 136 MET A CG  1 
ATOM   1018 S  SD  . MET A 1 136 ? 103.642 97.135  118.801 1.00 56.66  ? 136 MET A SD  1 
ATOM   1019 C  CE  . MET A 1 136 ? 103.713 98.780  119.499 1.00 27.30  ? 136 MET A CE  1 
ATOM   1020 N  N   . GLY A 1 137 ? 105.930 101.061 115.053 1.00 17.75  ? 137 GLY A N   1 
ATOM   1021 C  CA  . GLY A 1 137 ? 105.884 102.391 114.474 1.00 17.96  ? 137 GLY A CA  1 
ATOM   1022 C  C   . GLY A 1 137 ? 106.134 102.409 112.981 1.00 23.87  ? 137 GLY A C   1 
ATOM   1023 O  O   . GLY A 1 137 ? 105.520 103.196 112.257 1.00 34.41  ? 137 GLY A O   1 
ATOM   1024 N  N   . GLU A 1 138 ? 107.044 101.561 112.496 1.00 23.52  ? 138 GLU A N   1 
ATOM   1025 C  CA  . GLU A 1 138 ? 107.260 101.492 111.052 1.00 17.32  ? 138 GLU A CA  1 
ATOM   1026 C  C   . GLU A 1 138 ? 106.070 100.856 110.335 1.00 29.64  ? 138 GLU A C   1 
ATOM   1027 O  O   . GLU A 1 138 ? 105.577 101.398 109.333 1.00 35.69  ? 138 GLU A O   1 
ATOM   1028 C  CB  . GLU A 1 138 ? 108.547 100.728 110.740 1.00 16.55  ? 138 GLU A CB  1 
ATOM   1029 C  CG  . GLU A 1 138 ? 109.770 101.213 111.500 1.00 23.70  ? 138 GLU A CG  1 
ATOM   1030 C  CD  . GLU A 1 138 ? 110.416 102.438 110.880 1.00 34.86  ? 138 GLU A CD  1 
ATOM   1031 O  OE1 . GLU A 1 138 ? 109.921 102.919 109.840 1.00 40.82  ? 138 GLU A OE1 1 
ATOM   1032 O  OE2 . GLU A 1 138 ? 111.421 102.924 111.437 1.00 31.17  ? 138 GLU A OE2 1 
ATOM   1033 N  N   . MET A 1 139 ? 105.587 99.713  110.838 1.00 20.93  ? 139 MET A N   1 
ATOM   1034 C  CA  . MET A 1 139 ? 104.522 98.989  110.144 1.00 15.01  ? 139 MET A CA  1 
ATOM   1035 C  C   . MET A 1 139 ? 103.214 99.770  110.108 1.00 23.58  ? 139 MET A C   1 
ATOM   1036 O  O   . MET A 1 139 ? 102.546 99.813  109.067 1.00 33.74  ? 139 MET A O   1 
ATOM   1037 C  CB  . MET A 1 139 ? 104.316 97.618  110.785 1.00 24.72  ? 139 MET A CB  1 
ATOM   1038 C  CG  . MET A 1 139 ? 105.354 96.597  110.371 1.00 34.82  ? 139 MET A CG  1 
ATOM   1039 S  SD  . MET A 1 139 ? 105.880 96.899  108.672 1.00 64.14  ? 139 MET A SD  1 
ATOM   1040 C  CE  . MET A 1 139 ? 107.652 96.900  108.843 1.00 31.04  ? 139 MET A CE  1 
ATOM   1041 N  N   . PHE A 1 140 ? 102.817 100.385 111.224 1.00 20.62  ? 140 PHE A N   1 
ATOM   1042 C  CA  . PHE A 1 140 ? 101.536 101.083 111.235 1.00 15.87  ? 140 PHE A CA  1 
ATOM   1043 C  C   . PHE A 1 140 ? 101.574 102.327 110.355 1.00 19.60  ? 140 PHE A C   1 
ATOM   1044 O  O   . PHE A 1 140 ? 100.594 102.636 109.666 1.00 27.95  ? 140 PHE A O   1 
ATOM   1045 C  CB  . PHE A 1 140 ? 101.144 101.424 112.669 1.00 21.42  ? 140 PHE A CB  1 
ATOM   1046 C  CG  . PHE A 1 140 ? 100.853 100.216 113.511 1.00 22.65  ? 140 PHE A CG  1 
ATOM   1047 C  CD1 . PHE A 1 140 ? 100.305 99.081  112.943 1.00 20.05  ? 140 PHE A CD1 1 
ATOM   1048 C  CD2 . PHE A 1 140 ? 101.129 100.212 114.865 1.00 26.15  ? 140 PHE A CD2 1 
ATOM   1049 C  CE1 . PHE A 1 140 ? 100.038 97.966  113.707 1.00 20.21  ? 140 PHE A CE1 1 
ATOM   1050 C  CE2 . PHE A 1 140 ? 100.860 99.099  115.635 1.00 26.89  ? 140 PHE A CE2 1 
ATOM   1051 C  CZ  . PHE A 1 140 ? 100.315 97.975  115.055 1.00 22.04  ? 140 PHE A CZ  1 
ATOM   1052 N  N   . TRP A 1 141 ? 102.704 103.036 110.345 1.00 13.53  ? 141 TRP A N   1 
ATOM   1053 C  CA  . TRP A 1 141 ? 102.858 104.183 109.455 1.00 6.12   ? 141 TRP A CA  1 
ATOM   1054 C  C   . TRP A 1 141 ? 102.767 103.761 107.992 1.00 12.62  ? 141 TRP A C   1 
ATOM   1055 O  O   . TRP A 1 141 ? 102.063 104.399 107.193 1.00 18.84  ? 141 TRP A O   1 
ATOM   1056 C  CB  . TRP A 1 141 ? 104.188 104.880 109.749 1.00 9.60   ? 141 TRP A CB  1 
ATOM   1057 C  CG  . TRP A 1 141 ? 104.550 106.003 108.819 1.00 15.52  ? 141 TRP A CG  1 
ATOM   1058 C  CD1 . TRP A 1 141 ? 103.698 106.881 108.219 1.00 17.68  ? 141 TRP A CD1 1 
ATOM   1059 C  CD2 . TRP A 1 141 ? 105.868 106.375 108.401 1.00 16.67  ? 141 TRP A CD2 1 
ATOM   1060 N  NE1 . TRP A 1 141 ? 104.402 107.770 107.447 1.00 12.70  ? 141 TRP A NE1 1 
ATOM   1061 C  CE2 . TRP A 1 141 ? 105.737 107.480 107.542 1.00 13.96  ? 141 TRP A CE2 1 
ATOM   1062 C  CE3 . TRP A 1 141 ? 107.146 105.877 108.668 1.00 19.30  ? 141 TRP A CE3 1 
ATOM   1063 C  CZ2 . TRP A 1 141 ? 106.834 108.095 106.944 1.00 15.30  ? 141 TRP A CZ2 1 
ATOM   1064 C  CZ3 . TRP A 1 141 ? 108.234 106.490 108.076 1.00 13.23  ? 141 TRP A CZ3 1 
ATOM   1065 C  CH2 . TRP A 1 141 ? 108.071 107.588 107.226 1.00 13.48  ? 141 TRP A CH2 1 
ATOM   1066 N  N   . ALA A 1 142 ? 103.455 102.673 107.624 1.00 14.19  ? 142 ALA A N   1 
ATOM   1067 C  CA  . ALA A 1 142 ? 103.401 102.209 106.241 1.00 12.52  ? 142 ALA A CA  1 
ATOM   1068 C  C   . ALA A 1 142 ? 101.987 101.794 105.845 1.00 19.06  ? 142 ALA A C   1 
ATOM   1069 O  O   . ALA A 1 142 ? 101.515 102.130 104.750 1.00 24.92  ? 142 ALA A O   1 
ATOM   1070 C  CB  . ALA A 1 142 ? 104.379 101.054 106.036 1.00 9.47   ? 142 ALA A CB  1 
ATOM   1071 N  N   . ALA A 1 143 ? 101.292 101.068 106.725 1.00 17.11  ? 143 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 143 ? 99.931  100.639 106.416 1.00 11.22  ? 143 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 143 ? 98.991  101.829 106.259 1.00 18.22  ? 143 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 143 ? 98.155  101.855 105.345 1.00 27.98  ? 143 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 143 ? 99.424  99.689  107.500 1.00 14.48  ? 143 ALA A CB  1 
ATOM   1076 N  N   . ALA A 1 144 ? 99.113  102.827 107.140 1.00 20.88  ? 144 ALA A N   1 
ATOM   1077 C  CA  . ALA A 1 144 ? 98.250  103.999 107.049 1.00 13.80  ? 144 ALA A CA  1 
ATOM   1078 C  C   . ALA A 1 144 ? 98.478  104.764 105.751 1.00 19.56  ? 144 ALA A C   1 
ATOM   1079 O  O   . ALA A 1 144 ? 97.517  105.189 105.095 1.00 23.22  ? 144 ALA A O   1 
ATOM   1080 C  CB  . ALA A 1 144 ? 98.473  104.909 108.256 1.00 13.45  ? 144 ALA A CB  1 
ATOM   1081 N  N   . ILE A 1 145 ? 99.741  104.953 105.355 1.00 17.65  ? 145 ILE A N   1 
ATOM   1082 C  CA  . ILE A 1 145 ? 99.965  105.706 104.122 1.00 12.34  ? 145 ILE A CA  1 
ATOM   1083 C  C   . ILE A 1 145 ? 99.547  104.895 102.896 1.00 18.94  ? 145 ILE A C   1 
ATOM   1084 O  O   . ILE A 1 145 ? 99.108  105.468 101.891 1.00 21.31  ? 145 ILE A O   1 
ATOM   1085 C  CB  . ILE A 1 145 ? 101.421 106.203 104.022 1.00 20.92  ? 145 ILE A CB  1 
ATOM   1086 C  CG1 . ILE A 1 145 ? 102.417 105.046 104.000 1.00 20.90  ? 145 ILE A CG1 1 
ATOM   1087 C  CG2 . ILE A 1 145 ? 101.730 107.157 105.162 1.00 14.26  ? 145 ILE A CG2 1 
ATOM   1088 C  CD1 . ILE A 1 145 ? 103.854 105.502 103.935 1.00 12.53  ? 145 ILE A CD1 1 
ATOM   1089 N  N   . PHE A 1 146 ? 99.652  103.562 102.948 1.00 19.38  ? 146 PHE A N   1 
ATOM   1090 C  CA  . PHE A 1 146 ? 99.131  102.754 101.846 1.00 14.55  ? 146 PHE A CA  1 
ATOM   1091 C  C   . PHE A 1 146 ? 97.615  102.889 101.729 1.00 18.86  ? 146 PHE A C   1 
ATOM   1092 O  O   . PHE A 1 146 ? 97.074  102.984 100.618 1.00 27.60  ? 146 PHE A O   1 
ATOM   1093 C  CB  . PHE A 1 146 ? 99.532  101.291 102.026 1.00 12.40  ? 146 PHE A CB  1 
ATOM   1094 C  CG  . PHE A 1 146 ? 100.864 100.948 101.422 1.00 24.73  ? 146 PHE A CG  1 
ATOM   1095 C  CD1 . PHE A 1 146 ? 101.226 101.444 100.183 1.00 24.31  ? 146 PHE A CD1 1 
ATOM   1096 C  CD2 . PHE A 1 146 ? 101.754 100.128 102.094 1.00 27.08  ? 146 PHE A CD2 1 
ATOM   1097 C  CE1 . PHE A 1 146 ? 102.450 101.133 99.628  1.00 16.89  ? 146 PHE A CE1 1 
ATOM   1098 C  CE2 . PHE A 1 146 ? 102.980 99.814  101.543 1.00 18.46  ? 146 PHE A CE2 1 
ATOM   1099 C  CZ  . PHE A 1 146 ? 103.327 100.316 100.308 1.00 15.51  ? 146 PHE A CZ  1 
ATOM   1100 N  N   . SER A 1 147 ? 96.937  102.933 102.879 1.00 21.55  ? 147 SER A N   1 
ATOM   1101 C  CA  . SER A 1 147 ? 95.466  103.137 102.871 1.00 15.86  ? 147 SER A CA  1 
ATOM   1102 C  C   . SER A 1 147 ? 95.152  104.502 102.252 1.00 23.09  ? 147 SER A C   1 
ATOM   1103 O  O   . SER A 1 147 ? 94.220  104.575 101.427 1.00 30.08  ? 147 SER A O   1 
ATOM   1104 C  CB  . SER A 1 147 ? 94.898  103.020 104.261 1.00 14.23  ? 147 SER A CB  1 
ATOM   1105 O  OG  . SER A 1 147 ? 93.497  103.250 104.253 1.00 35.90  ? 147 SER A OG  1 
ATOM   1106 N  N   . ALA A 1 148 ? 95.911  105.537 102.630 1.00 20.64  ? 148 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 148 ? 95.676  106.875 102.094 1.00 16.25  ? 148 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 148 ? 95.888  106.916 100.585 1.00 20.53  ? 148 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 148 ? 95.117  107.556 99.859  1.00 24.76  ? 148 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 148 ? 96.584  107.887 102.792 1.00 15.76  ? 148 ALA A CB  1 
ATOM   1111 N  N   . LEU A 1 149 ? 96.933  106.244 100.094 1.00 21.65  ? 149 LEU A N   1 
ATOM   1112 C  CA  . LEU A 1 149 ? 97.165  106.186 98.653  1.00 20.71  ? 149 LEU A CA  1 
ATOM   1113 C  C   . LEU A 1 149 ? 96.021  105.478 97.938  1.00 24.08  ? 149 LEU A C   1 
ATOM   1114 O  O   . LEU A 1 149 ? 95.598  105.903 96.854  1.00 24.83  ? 149 LEU A O   1 
ATOM   1115 C  CB  . LEU A 1 149 ? 98.492  105.488 98.357  1.00 17.56  ? 149 LEU A CB  1 
ATOM   1116 C  CG  . LEU A 1 149 ? 98.833  105.293 96.877  1.00 19.53  ? 149 LEU A CG  1 
ATOM   1117 C  CD1 . LEU A 1 149 ? 98.760  106.607 96.118  1.00 22.51  ? 149 LEU A CD1 1 
ATOM   1118 C  CD2 . LEU A 1 149 ? 100.200 104.655 96.719  1.00 24.91  ? 149 LEU A CD2 1 
ATOM   1119 N  N   . GLY A 1 150 ? 95.517  104.388 98.520  1.00 28.93  ? 150 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 150 ? 94.376  103.713 97.921  1.00 24.04  ? 150 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 150 ? 93.155  104.608 97.827  1.00 24.46  ? 150 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 150 ? 92.472  104.639 96.798  1.00 23.97  ? 150 GLY A O   1 
ATOM   1123 N  N   . ALA A 1 151 ? 92.874  105.360 98.894  1.00 34.71  ? 151 ALA A N   1 
ATOM   1124 C  CA  . ALA A 1 151 ? 91.741  106.284 98.875  1.00 21.70  ? 151 ALA A CA  1 
ATOM   1125 C  C   . ALA A 1 151 ? 91.929  107.374 97.823  1.00 32.43  ? 151 ALA A C   1 
ATOM   1126 O  O   . ALA A 1 151 ? 90.984  107.737 97.111  1.00 29.08  ? 151 ALA A O   1 
ATOM   1127 C  CB  . ALA A 1 151 ? 91.545  106.898 100.260 1.00 12.31  ? 151 ALA A CB  1 
ATOM   1128 N  N   . THR A 1 152 ? 93.146  107.915 97.718  1.00 35.36  ? 152 THR A N   1 
ATOM   1129 C  CA  . THR A 1 152 ? 93.425  108.942 96.715  1.00 21.62  ? 152 THR A CA  1 
ATOM   1130 C  C   . THR A 1 152 ? 93.215  108.417 95.299  1.00 27.71  ? 152 THR A C   1 
ATOM   1131 O  O   . THR A 1 152 ? 92.609  109.097 94.458  1.00 27.40  ? 152 THR A O   1 
ATOM   1132 C  CB  . THR A 1 152 ? 94.856  109.455 96.879  1.00 19.75  ? 152 THR A CB  1 
ATOM   1133 O  OG1 . THR A 1 152 ? 95.112  109.733 98.261  1.00 25.78  ? 152 THR A OG1 1 
ATOM   1134 C  CG2 . THR A 1 152 ? 95.080  110.706 96.053  1.00 27.12  ? 152 THR A CG2 1 
ATOM   1135 N  N   . ILE A 1 153 ? 93.718  107.213 95.016  1.00 37.22  ? 153 ILE A N   1 
ATOM   1136 C  CA  . ILE A 1 153 ? 93.545  106.629 93.688  1.00 33.94  ? 153 ILE A CA  1 
ATOM   1137 C  C   . ILE A 1 153 ? 92.069  106.394 93.403  1.00 34.63  ? 153 ILE A C   1 
ATOM   1138 O  O   . ILE A 1 153 ? 91.585  106.661 92.297  1.00 36.50  ? 153 ILE A O   1 
ATOM   1139 C  CB  . ILE A 1 153 ? 94.364  105.331 93.560  1.00 37.01  ? 153 ILE A CB  1 
ATOM   1140 C  CG1 . ILE A 1 153 ? 95.859  105.644 93.522  1.00 34.42  ? 153 ILE A CG1 1 
ATOM   1141 C  CG2 . ILE A 1 153 ? 93.960  104.565 92.312  1.00 34.81  ? 153 ILE A CG2 1 
ATOM   1142 C  CD1 . ILE A 1 153 ? 96.736  104.415 93.436  1.00 33.64  ? 153 ILE A CD1 1 
ATOM   1143 N  N   . SER A 1 154 ? 91.333  105.927 94.408  1.00 42.31  ? 154 SER A N   1 
ATOM   1144 C  CA  . SER A 1 154 ? 89.901  105.674 94.241  1.00 39.89  ? 154 SER A CA  1 
ATOM   1145 C  C   . SER A 1 154 ? 89.122  106.959 93.978  1.00 37.10  ? 154 SER A C   1 
ATOM   1146 O  O   . SER A 1 154 ? 88.126  106.945 93.256  1.00 38.61  ? 154 SER A O   1 
ATOM   1147 C  CB  . SER A 1 154 ? 89.334  104.957 95.467  1.00 43.35  ? 154 SER A CB  1 
ATOM   1148 O  OG  . SER A 1 154 ? 87.948  104.708 95.316  1.00 45.94  ? 154 SER A OG  1 
ATOM   1149 N  N   . VAL A 1 155 ? 89.560  108.066 94.569  1.00 41.55  ? 155 VAL A N   1 
ATOM   1150 C  CA  . VAL A 1 155 ? 88.906  109.349 94.327  1.00 39.06  ? 155 VAL A CA  1 
ATOM   1151 C  C   . VAL A 1 155 ? 89.206  109.850 92.918  1.00 36.65  ? 155 VAL A C   1 
ATOM   1152 O  O   . VAL A 1 155 ? 88.304  110.284 92.192  1.00 38.92  ? 155 VAL A O   1 
ATOM   1153 C  CB  . VAL A 1 155 ? 89.321  110.380 95.392  1.00 35.37  ? 155 VAL A CB  1 
ATOM   1154 C  CG1 . VAL A 1 155 ? 88.974  111.785 94.933  1.00 27.12  ? 155 VAL A CG1 1 
ATOM   1155 C  CG2 . VAL A 1 155 ? 88.645  110.074 96.716  1.00 43.70  ? 155 VAL A CG2 1 
ATOM   1156 N  N   . ILE A 1 156 ? 90.476  109.801 92.508  1.00 45.31  ? 156 ILE A N   1 
ATOM   1157 C  CA  . ILE A 1 156 ? 90.854  110.414 91.234  1.00 43.40  ? 156 ILE A CA  1 
ATOM   1158 C  C   . ILE A 1 156 ? 90.358  109.579 90.054  1.00 45.36  ? 156 ILE A C   1 
ATOM   1159 O  O   . ILE A 1 156 ? 89.793  110.115 89.094  1.00 45.04  ? 156 ILE A O   1 
ATOM   1160 C  CB  . ILE A 1 156 ? 92.373  110.651 91.173  1.00 42.93  ? 156 ILE A CB  1 
ATOM   1161 C  CG1 . ILE A 1 156 ? 92.735  111.905 91.969  1.00 38.83  ? 156 ILE A CG1 1 
ATOM   1162 C  CG2 . ILE A 1 156 ? 92.833  110.805 89.736  1.00 37.08  ? 156 ILE A CG2 1 
ATOM   1163 C  CD1 . ILE A 1 156 ? 94.215  112.155 92.088  1.00 40.16  ? 156 ILE A CD1 1 
ATOM   1164 N  N   . ILE A 1 157 ? 90.557  108.259 90.101  1.00 54.17  ? 157 ILE A N   1 
ATOM   1165 C  CA  . ILE A 1 157 ? 90.140  107.377 89.017  1.00 49.41  ? 157 ILE A CA  1 
ATOM   1166 C  C   . ILE A 1 157 ? 89.324  106.224 89.587  1.00 52.74  ? 157 ILE A C   1 
ATOM   1167 O  O   . ILE A 1 157 ? 89.344  105.948 90.787  1.00 56.47  ? 157 ILE A O   1 
ATOM   1168 C  CB  . ILE A 1 157 ? 91.333  106.835 88.198  1.00 45.00  ? 157 ILE A CB  1 
ATOM   1169 C  CG1 . ILE A 1 157 ? 92.424  106.290 89.120  1.00 47.77  ? 157 ILE A CG1 1 
ATOM   1170 C  CG2 . ILE A 1 157 ? 91.889  107.917 87.289  1.00 47.84  ? 157 ILE A CG2 1 
ATOM   1171 C  CD1 . ILE A 1 157 ? 93.739  106.031 88.418  1.00 51.14  ? 157 ILE A CD1 1 
ATOM   1172 N  N   . ASP A 1 158 ? 88.601  105.543 88.698  1.00 62.39  ? 158 ASP A N   1 
ATOM   1173 C  CA  . ASP A 1 158 ? 87.672  104.488 89.083  1.00 66.52  ? 158 ASP A CA  1 
ATOM   1174 C  C   . ASP A 1 158 ? 88.325  103.112 89.169  1.00 69.89  ? 158 ASP A C   1 
ATOM   1175 O  O   . ASP A 1 158 ? 87.610  102.106 89.236  1.00 72.24  ? 158 ASP A O   1 
ATOM   1176 C  CB  . ASP A 1 158 ? 86.497  104.438 88.103  1.00 68.96  ? 158 ASP A CB  1 
ATOM   1177 C  CG  . ASP A 1 158 ? 85.723  105.738 88.055  1.00 70.34  ? 158 ASP A CG  1 
ATOM   1178 O  OD1 . ASP A 1 158 ? 86.285  106.780 88.451  1.00 70.50  ? 158 ASP A OD1 1 
ATOM   1179 O  OD2 . ASP A 1 158 ? 84.551  105.719 87.622  1.00 71.11  ? 158 ASP A OD2 1 
ATOM   1180 N  N   . VAL A 1 159 ? 89.655  103.041 89.164  1.00 63.68  ? 159 VAL A N   1 
ATOM   1181 C  CA  . VAL A 1 159 ? 90.341  101.760 89.279  1.00 60.34  ? 159 VAL A CA  1 
ATOM   1182 C  C   . VAL A 1 159 ? 90.152  101.206 90.686  1.00 63.90  ? 159 VAL A C   1 
ATOM   1183 O  O   . VAL A 1 159 ? 90.167  101.951 91.675  1.00 66.73  ? 159 VAL A O   1 
ATOM   1184 C  CB  . VAL A 1 159 ? 91.829  101.927 88.925  1.00 59.97  ? 159 VAL A CB  1 
ATOM   1185 C  CG1 . VAL A 1 159 ? 92.648  100.745 89.417  1.00 58.92  ? 159 VAL A CG1 1 
ATOM   1186 C  CG2 . VAL A 1 159 ? 91.994  102.103 87.426  1.00 63.76  ? 159 VAL A CG2 1 
ATOM   1187 N  N   . ASP A 1 160 ? 89.955  99.890  90.779  1.00 59.99  ? 160 ASP A N   1 
ATOM   1188 C  CA  . ASP A 1 160 ? 89.746  99.242  92.068  1.00 59.61  ? 160 ASP A CA  1 
ATOM   1189 C  C   . ASP A 1 160 ? 90.929  99.490  92.997  1.00 61.74  ? 160 ASP A C   1 
ATOM   1190 O  O   . ASP A 1 160 ? 92.088  99.457  92.578  1.00 67.78  ? 160 ASP A O   1 
ATOM   1191 C  CB  . ASP A 1 160 ? 89.531  97.741  91.871  1.00 62.98  ? 160 ASP A CB  1 
ATOM   1192 C  CG  . ASP A 1 160 ? 88.923  97.073  93.087  1.00 67.06  ? 160 ASP A CG  1 
ATOM   1193 O  OD1 . ASP A 1 160 ? 88.054  97.694  93.735  1.00 65.91  ? 160 ASP A OD1 1 
ATOM   1194 O  OD2 . ASP A 1 160 ? 89.310  95.927  93.393  1.00 66.36  ? 160 ASP A OD2 1 
ATOM   1195 N  N   . MET A 1 161 ? 90.624  99.744  94.272  1.00 55.42  ? 161 MET A N   1 
ATOM   1196 C  CA  . MET A 1 161 ? 91.655  100.158 95.219  1.00 57.21  ? 161 MET A CA  1 
ATOM   1197 C  C   . MET A 1 161 ? 92.598  99.012  95.570  1.00 61.46  ? 161 MET A C   1 
ATOM   1198 O  O   . MET A 1 161 ? 93.810  99.223  95.717  1.00 63.26  ? 161 MET A O   1 
ATOM   1199 C  CB  . MET A 1 161 ? 90.999  100.729 96.478  1.00 51.55  ? 161 MET A CB  1 
ATOM   1200 C  CG  . MET A 1 161 ? 91.750  100.451 97.768  1.00 55.88  ? 161 MET A CG  1 
ATOM   1201 S  SD  . MET A 1 161 ? 90.935  101.161 99.209  1.00 73.53  ? 161 MET A SD  1 
ATOM   1202 C  CE  . MET A 1 161 ? 92.285  101.184 100.387 1.00 58.70  ? 161 MET A CE  1 
ATOM   1203 N  N   . HIS A 1 162 ? 92.065  97.794  95.710  1.00 54.29  ? 162 HIS A N   1 
ATOM   1204 C  CA  . HIS A 1 162 ? 92.886  96.664  96.137  1.00 53.30  ? 162 HIS A CA  1 
ATOM   1205 C  C   . HIS A 1 162 ? 94.018  96.401  95.152  1.00 53.04  ? 162 HIS A C   1 
ATOM   1206 O  O   . HIS A 1 162 ? 95.175  96.216  95.549  1.00 57.30  ? 162 HIS A O   1 
ATOM   1207 C  CB  . HIS A 1 162 ? 92.021  95.413  96.295  1.00 57.44  ? 162 HIS A CB  1 
ATOM   1208 C  CG  . HIS A 1 162 ? 90.868  95.583  97.235  1.00 61.25  ? 162 HIS A CG  1 
ATOM   1209 N  ND1 . HIS A 1 162 ? 89.762  96.345  96.928  1.00 61.09  ? 162 HIS A ND1 1 
ATOM   1210 C  CD2 . HIS A 1 162 ? 90.645  95.079  98.472  1.00 59.39  ? 162 HIS A CD2 1 
ATOM   1211 C  CE1 . HIS A 1 162 ? 88.910  96.308  97.938  1.00 60.83  ? 162 HIS A CE1 1 
ATOM   1212 N  NE2 . HIS A 1 162 ? 89.423  95.546  98.887  1.00 60.29  ? 162 HIS A NE2 1 
ATOM   1213 N  N   . ILE A 1 163 ? 93.698  96.387  93.856  1.00 40.68  ? 163 ILE A N   1 
ATOM   1214 C  CA  . ILE A 1 163 ? 94.706  96.116  92.837  1.00 43.45  ? 163 ILE A CA  1 
ATOM   1215 C  C   . ILE A 1 163 ? 95.784  97.190  92.857  1.00 44.99  ? 163 ILE A C   1 
ATOM   1216 O  O   . ILE A 1 163 ? 96.982  96.891  92.771  1.00 48.28  ? 163 ILE A O   1 
ATOM   1217 C  CB  . ILE A 1 163 ? 94.040  96.000  91.453  1.00 44.93  ? 163 ILE A CB  1 
ATOM   1218 C  CG1 . ILE A 1 163 ? 93.189  94.732  91.378  1.00 47.63  ? 163 ILE A CG1 1 
ATOM   1219 C  CG2 . ILE A 1 163 ? 95.083  95.997  90.351  1.00 48.78  ? 163 ILE A CG2 1 
ATOM   1220 C  CD1 . ILE A 1 163 ? 92.334  94.644  90.136  1.00 49.87  ? 163 ILE A CD1 1 
ATOM   1221 N  N   . SER A 1 164 ? 95.378  98.455  92.981  1.00 40.98  ? 164 SER A N   1 
ATOM   1222 C  CA  . SER A 1 164 ? 96.338  99.554  92.985  1.00 40.55  ? 164 SER A CA  1 
ATOM   1223 C  C   . SER A 1 164 ? 97.280  99.466  94.179  1.00 42.28  ? 164 SER A C   1 
ATOM   1224 O  O   . SER A 1 164 ? 98.500  99.625  94.036  1.00 38.84  ? 164 SER A O   1 
ATOM   1225 C  CB  . SER A 1 164 ? 95.593  100.888 92.986  1.00 44.57  ? 164 SER A CB  1 
ATOM   1226 O  OG  . SER A 1 164 ? 94.478  100.846 92.115  1.00 47.34  ? 164 SER A OG  1 
ATOM   1227 N  N   . VAL A 1 165 ? 96.731  99.213  95.370  1.00 30.06  ? 165 VAL A N   1 
ATOM   1228 C  CA  . VAL A 1 165 ? 97.568  99.130  96.565  1.00 30.94  ? 165 VAL A CA  1 
ATOM   1229 C  C   . VAL A 1 165 ? 98.527  97.950  96.465  1.00 38.85  ? 165 VAL A C   1 
ATOM   1230 O  O   . VAL A 1 165 ? 99.718  98.067  96.792  1.00 42.93  ? 165 VAL A O   1 
ATOM   1231 C  CB  . VAL A 1 165 ? 96.692  99.048  97.829  1.00 36.02  ? 165 VAL A CB  1 
ATOM   1232 C  CG1 . VAL A 1 165 ? 97.557  98.874  99.067  1.00 35.43  ? 165 VAL A CG1 1 
ATOM   1233 C  CG2 . VAL A 1 165 ? 95.836  100.291 97.957  1.00 39.85  ? 165 VAL A CG2 1 
ATOM   1234 N  N   . ILE A 1 166 ? 98.029  96.799  96.002  1.00 34.75  ? 166 ILE A N   1 
ATOM   1235 C  CA  . ILE A 1 166 ? 98.880  95.621  95.866  1.00 29.56  ? 166 ILE A CA  1 
ATOM   1236 C  C   . ILE A 1 166 ? 100.014 95.890  94.885  1.00 26.05  ? 166 ILE A C   1 
ATOM   1237 O  O   . ILE A 1 166 ? 101.173 95.551  95.149  1.00 31.99  ? 166 ILE A O   1 
ATOM   1238 C  CB  . ILE A 1 166 ? 98.040  94.401  95.445  1.00 31.91  ? 166 ILE A CB  1 
ATOM   1239 C  CG1 . ILE A 1 166 ? 97.180  93.918  96.613  1.00 35.36  ? 166 ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A 1 166 ? 98.932  93.272  94.957  1.00 30.53  ? 166 ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A 1 166 ? 96.413  92.650  96.325  1.00 31.36  ? 166 ILE A CD1 1 
ATOM   1242 N  N   . ILE A 1 167 ? 99.703  96.513  93.746  1.00 20.16  ? 167 ILE A N   1 
ATOM   1243 C  CA  . ILE A 1 167 ? 100.723 96.767  92.734  1.00 22.91  ? 167 ILE A CA  1 
ATOM   1244 C  C   . ILE A 1 167 ? 101.769 97.750  93.248  1.00 28.72  ? 167 ILE A C   1 
ATOM   1245 O  O   . ILE A 1 167 ? 102.973 97.555  93.039  1.00 40.31  ? 167 ILE A O   1 
ATOM   1246 C  CB  . ILE A 1 167 ? 100.067 97.254  91.431  1.00 30.56  ? 167 ILE A CB  1 
ATOM   1247 C  CG1 . ILE A 1 167 ? 99.406  96.079  90.709  1.00 28.57  ? 167 ILE A CG1 1 
ATOM   1248 C  CG2 . ILE A 1 167 ? 101.089 97.921  90.527  1.00 29.32  ? 167 ILE A CG2 1 
ATOM   1249 C  CD1 . ILE A 1 167 ? 98.685  96.468  89.443  1.00 34.66  ? 167 ILE A CD1 1 
ATOM   1250 N  N   . SER A 1 168 ? 101.338 98.818  93.926  1.00 26.49  ? 168 SER A N   1 
ATOM   1251 C  CA  . SER A 1 168 ? 102.294 99.793  94.447  1.00 23.29  ? 168 SER A CA  1 
ATOM   1252 C  C   . SER A 1 168 ? 103.222 99.162  95.480  1.00 26.45  ? 168 SER A C   1 
ATOM   1253 O  O   . SER A 1 168 ? 104.449 99.349  95.438  1.00 23.08  ? 168 SER A O   1 
ATOM   1254 C  CB  . SER A 1 168 ? 101.545 100.981 95.050  1.00 29.65  ? 168 SER A CB  1 
ATOM   1255 O  OG  . SER A 1 168 ? 101.148 101.897 94.047  1.00 39.46  ? 168 SER A OG  1 
ATOM   1256 N  N   . ALA A 1 169 ? 102.650 98.394  96.414  1.00 23.55  ? 169 ALA A N   1 
ATOM   1257 C  CA  . ALA A 1 169 ? 103.466 97.741  97.431  1.00 19.00  ? 169 ALA A CA  1 
ATOM   1258 C  C   . ALA A 1 169 ? 104.429 96.740  96.807  1.00 27.21  ? 169 ALA A C   1 
ATOM   1259 O  O   . ALA A 1 169 ? 105.589 96.640  97.227  1.00 24.36  ? 169 ALA A O   1 
ATOM   1260 C  CB  . ALA A 1 169 ? 102.570 97.058  98.460  1.00 17.24  ? 169 ALA A CB  1 
ATOM   1261 N  N   . LEU A 1 170 ? 103.966 95.988  95.805  1.00 28.24  ? 170 LEU A N   1 
ATOM   1262 C  CA  . LEU A 1 170 ? 104.830 95.025  95.133  1.00 15.86  ? 170 LEU A CA  1 
ATOM   1263 C  C   . LEU A 1 170 ? 105.987 95.718  94.427  1.00 23.30  ? 170 LEU A C   1 
ATOM   1264 O  O   . LEU A 1 170 ? 107.131 95.255  94.497  1.00 34.81  ? 170 LEU A O   1 
ATOM   1265 C  CB  . LEU A 1 170 ? 104.012 94.198  94.142  1.00 20.44  ? 170 LEU A CB  1 
ATOM   1266 C  CG  . LEU A 1 170 ? 104.650 92.936  93.565  1.00 30.73  ? 170 LEU A CG  1 
ATOM   1267 C  CD1 . LEU A 1 170 ? 103.664 91.786  93.610  1.00 32.26  ? 170 LEU A CD1 1 
ATOM   1268 C  CD2 . LEU A 1 170 ? 105.120 93.178  92.143  1.00 29.12  ? 170 LEU A CD2 1 
ATOM   1269 N  N   . ILE A 1 171 ? 105.711 96.835  93.750  1.00 16.18  ? 171 ILE A N   1 
ATOM   1270 C  CA  . ILE A 1 171 ? 106.770 97.556  93.050  1.00 19.95  ? 171 ILE A CA  1 
ATOM   1271 C  C   . ILE A 1 171 ? 107.819 98.056  94.035  1.00 22.95  ? 171 ILE A C   1 
ATOM   1272 O  O   . ILE A 1 171 ? 109.025 97.933  93.790  1.00 30.56  ? 171 ILE A O   1 
ATOM   1273 C  CB  . ILE A 1 171 ? 106.181 98.709  92.216  1.00 26.67  ? 171 ILE A CB  1 
ATOM   1274 C  CG1 . ILE A 1 171 ? 105.427 98.161  91.003  1.00 27.17  ? 171 ILE A CG1 1 
ATOM   1275 C  CG2 . ILE A 1 171 ? 107.278 99.664  91.772  1.00 22.15  ? 171 ILE A CG2 1 
ATOM   1276 C  CD1 . ILE A 1 171 ? 106.320 97.729  89.868  1.00 26.03  ? 171 ILE A CD1 1 
ATOM   1277 N  N   . ALA A 1 172 ? 107.384 98.621  95.164  1.00 20.91  ? 172 ALA A N   1 
ATOM   1278 C  CA  . ALA A 1 172 ? 108.355 99.105  96.145  1.00 15.98  ? 172 ALA A CA  1 
ATOM   1279 C  C   . ALA A 1 172 ? 109.181 97.958  96.724  1.00 22.96  ? 172 ALA A C   1 
ATOM   1280 O  O   . ALA A 1 172 ? 110.422 98.021  96.769  1.00 25.25  ? 172 ALA A O   1 
ATOM   1281 C  CB  . ALA A 1 172 ? 107.640 99.871  97.258  1.00 17.83  ? 172 ALA A CB  1 
ATOM   1282 N  N   . THR A 1 173 ? 108.504 96.889  97.158  1.00 27.33  ? 173 THR A N   1 
ATOM   1283 C  CA  . THR A 1 173 ? 109.186 95.774  97.803  1.00 16.12  ? 173 THR A CA  1 
ATOM   1284 C  C   . THR A 1 173 ? 110.153 95.080  96.855  1.00 19.33  ? 173 THR A C   1 
ATOM   1285 O  O   . THR A 1 173 ? 111.199 94.595  97.292  1.00 17.06  ? 173 THR A O   1 
ATOM   1286 C  CB  . THR A 1 173 ? 108.154 94.780  98.345  1.00 23.22  ? 173 THR A CB  1 
ATOM   1287 O  OG1 . THR A 1 173 ? 107.336 95.429  99.326  1.00 32.10  ? 173 THR A OG1 1 
ATOM   1288 C  CG2 . THR A 1 173 ? 108.830 93.580  98.987  1.00 22.39  ? 173 THR A CG2 1 
ATOM   1289 N  N   . LEU A 1 174 ? 109.842 95.044  95.557  1.00 21.70  ? 174 LEU A N   1 
ATOM   1290 C  CA  . LEU A 1 174 ? 110.711 94.355  94.610  1.00 21.56  ? 174 LEU A CA  1 
ATOM   1291 C  C   . LEU A 1 174 ? 112.102 94.978  94.570  1.00 29.20  ? 174 LEU A C   1 
ATOM   1292 O  O   . LEU A 1 174 ? 113.111 94.282  94.741  1.00 29.45  ? 174 LEU A O   1 
ATOM   1293 C  CB  . LEU A 1 174 ? 110.075 94.364  93.221  1.00 20.37  ? 174 LEU A CB  1 
ATOM   1294 C  CG  . LEU A 1 174 ? 109.672 93.002  92.661  1.00 25.84  ? 174 LEU A CG  1 
ATOM   1295 C  CD1 . LEU A 1 174 ? 109.055 93.155  91.285  1.00 32.32  ? 174 LEU A CD1 1 
ATOM   1296 C  CD2 . LEU A 1 174 ? 110.874 92.077  92.611  1.00 23.80  ? 174 LEU A CD2 1 
ATOM   1297 N  N   . TYR A 1 175 ? 112.182 96.296  94.360  1.00 27.16  ? 175 TYR A N   1 
ATOM   1298 C  CA  . TYR A 1 175 ? 113.506 96.904  94.281  1.00 28.43  ? 175 TYR A CA  1 
ATOM   1299 C  C   . TYR A 1 175 ? 114.153 97.017  95.655  1.00 19.92  ? 175 TYR A C   1 
ATOM   1300 O  O   . TYR A 1 175 ? 115.381 96.915  95.757  1.00 15.18  ? 175 TYR A O   1 
ATOM   1301 C  CB  . TYR A 1 175 ? 113.461 98.260  93.555  1.00 20.07  ? 175 TYR A CB  1 
ATOM   1302 C  CG  . TYR A 1 175 ? 112.765 99.421  94.242  1.00 17.83  ? 175 TYR A CG  1 
ATOM   1303 C  CD1 . TYR A 1 175 ? 113.331 100.061 95.337  1.00 17.39  ? 175 TYR A CD1 1 
ATOM   1304 C  CD2 . TYR A 1 175 ? 111.567 99.918  93.749  1.00 23.97  ? 175 TYR A CD2 1 
ATOM   1305 C  CE1 . TYR A 1 175 ? 112.702 101.127 95.946  1.00 11.15  ? 175 TYR A CE1 1 
ATOM   1306 C  CE2 . TYR A 1 175 ? 110.934 100.985 94.350  1.00 23.51  ? 175 TYR A CE2 1 
ATOM   1307 C  CZ  . TYR A 1 175 ? 111.504 101.585 95.447  1.00 11.15  ? 175 TYR A CZ  1 
ATOM   1308 O  OH  . TYR A 1 175 ? 110.871 102.647 96.044  1.00 25.23  ? 175 TYR A OH  1 
ATOM   1309 N  N   . THR A 1 176 ? 113.363 97.184  96.726  1.00 15.49  ? 176 THR A N   1 
ATOM   1310 C  CA  . THR A 1 176 ? 113.974 97.165  98.054  1.00 13.02  ? 176 THR A CA  1 
ATOM   1311 C  C   . THR A 1 176 ? 114.598 95.807  98.363  1.00 18.71  ? 176 THR A C   1 
ATOM   1312 O  O   . THR A 1 176 ? 115.616 95.735  99.060  1.00 18.75  ? 176 THR A O   1 
ATOM   1313 C  CB  . THR A 1 176 ? 112.946 97.537  99.123  1.00 24.46  ? 176 THR A CB  1 
ATOM   1314 O  OG1 . THR A 1 176 ? 112.277 98.744  98.742  1.00 30.63  ? 176 THR A OG1 1 
ATOM   1315 C  CG2 . THR A 1 176 ? 113.626 97.750  100.464 1.00 10.20  ? 176 THR A CG2 1 
ATOM   1316 N  N   . LEU A 1 177 ? 114.006 94.725  97.856  1.00 31.77  ? 177 LEU A N   1 
ATOM   1317 C  CA  . LEU A 1 177 ? 114.576 93.396  98.053  1.00 26.10  ? 177 LEU A CA  1 
ATOM   1318 C  C   . LEU A 1 177 ? 115.801 93.181  97.175  1.00 33.57  ? 177 LEU A C   1 
ATOM   1319 O  O   . LEU A 1 177 ? 116.806 92.624  97.631  1.00 31.37  ? 177 LEU A O   1 
ATOM   1320 C  CB  . LEU A 1 177 ? 113.515 92.335  97.763  1.00 27.28  ? 177 LEU A CB  1 
ATOM   1321 C  CG  . LEU A 1 177 ? 113.818 90.875  98.090  1.00 25.74  ? 177 LEU A CG  1 
ATOM   1322 C  CD1 . LEU A 1 177 ? 112.599 90.227  98.711  1.00 28.69  ? 177 LEU A CD1 1 
ATOM   1323 C  CD2 . LEU A 1 177 ? 114.239 90.119  96.841  1.00 23.81  ? 177 LEU A CD2 1 
ATOM   1324 N  N   . VAL A 1 178 ? 115.737 93.608  95.910  1.00 31.09  ? 178 VAL A N   1 
ATOM   1325 C  CA  . VAL A 1 178 ? 116.856 93.384  94.997  1.00 25.20  ? 178 VAL A CA  1 
ATOM   1326 C  C   . VAL A 1 178 ? 118.087 94.154  95.461  1.00 28.70  ? 178 VAL A C   1 
ATOM   1327 O  O   . VAL A 1 178 ? 119.189 93.600  95.551  1.00 34.87  ? 178 VAL A O   1 
ATOM   1328 C  CB  . VAL A 1 178 ? 116.463 93.757  93.557  1.00 31.93  ? 178 VAL A CB  1 
ATOM   1329 C  CG1 . VAL A 1 178 ? 117.687 93.760  92.661  1.00 32.56  ? 178 VAL A CG1 1 
ATOM   1330 C  CG2 . VAL A 1 178 ? 115.428 92.783  93.028  1.00 33.86  ? 178 VAL A CG2 1 
ATOM   1331 N  N   . GLY A 1 179 ? 117.922 95.435  95.766  1.00 33.04  ? 179 GLY A N   1 
ATOM   1332 C  CA  . GLY A 1 179 ? 119.002 96.227  96.318  1.00 25.47  ? 179 GLY A CA  1 
ATOM   1333 C  C   . GLY A 1 179 ? 118.523 96.977  97.541  1.00 35.13  ? 179 GLY A C   1 
ATOM   1334 O  O   . GLY A 1 179 ? 117.349 97.320  97.663  1.00 49.05  ? 179 GLY A O   1 
ATOM   1335 N  N   . GLY A 1 180 ? 119.453 97.236  98.450  1.00 14.50  ? 180 GLY A N   1 
ATOM   1336 C  CA  . GLY A 1 180 ? 119.072 97.821  99.719  1.00 10.06  ? 180 GLY A CA  1 
ATOM   1337 C  C   . GLY A 1 180 ? 119.119 99.333  99.772  1.00 25.73  ? 180 GLY A C   1 
ATOM   1338 O  O   . GLY A 1 180 ? 118.332 100.024 99.109  1.00 31.26  ? 180 GLY A O   1 
ATOM   1339 N  N   . LEU A 1 181 ? 120.048 99.847  100.580 1.00 25.98  ? 181 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 181 ? 120.120 101.280 100.840 1.00 16.38  ? 181 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 181 ? 120.428 102.067 99.574  1.00 19.31  ? 181 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 181 ? 119.871 103.150 99.359  1.00 37.55  ? 181 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 181 ? 121.171 101.554 101.915 1.00 22.49  ? 181 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 181 ? 121.471 103.016 102.243 1.00 31.51  ? 181 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 181 ? 120.328 103.646 103.021 1.00 24.09  ? 181 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 181 ? 122.765 103.114 103.015 1.00 22.07  ? 181 LEU A CD2 1 
ATOM   1347 N  N   . TYR A 1 182 ? 121.327 101.551 98.733  1.00 10.42  ? 182 TYR A N   1 
ATOM   1348 C  CA  . TYR A 1 182 ? 121.699 102.268 97.517  1.00 18.76  ? 182 TYR A CA  1 
ATOM   1349 C  C   . TYR A 1 182 ? 120.506 102.426 96.584  1.00 20.68  ? 182 TYR A C   1 
ATOM   1350 O  O   . TYR A 1 182 ? 120.260 103.515 96.049  1.00 26.15  ? 182 TYR A O   1 
ATOM   1351 C  CB  . TYR A 1 182 ? 122.847 101.543 96.815  1.00 11.50  ? 182 TYR A CB  1 
ATOM   1352 C  CG  . TYR A 1 182 ? 124.208 101.882 97.372  1.00 15.66  ? 182 TYR A CG  1 
ATOM   1353 C  CD1 . TYR A 1 182 ? 124.640 103.198 97.440  1.00 26.76  ? 182 TYR A CD1 1 
ATOM   1354 C  CD2 . TYR A 1 182 ? 125.061 100.890 97.832  1.00 27.37  ? 182 TYR A CD2 1 
ATOM   1355 C  CE1 . TYR A 1 182 ? 125.881 103.516 97.946  1.00 27.70  ? 182 TYR A CE1 1 
ATOM   1356 C  CE2 . TYR A 1 182 ? 126.307 101.199 98.341  1.00 21.20  ? 182 TYR A CE2 1 
ATOM   1357 C  CZ  . TYR A 1 182 ? 126.710 102.515 98.395  1.00 26.16  ? 182 TYR A CZ  1 
ATOM   1358 O  OH  . TYR A 1 182 ? 127.948 102.834 98.900  1.00 35.87  ? 182 TYR A OH  1 
ATOM   1359 N  N   . SER A 1 183 ? 119.741 101.349 96.387  1.00 17.68  ? 183 SER A N   1 
ATOM   1360 C  CA  . SER A 1 183 ? 118.554 101.429 95.543  1.00 16.26  ? 183 SER A CA  1 
ATOM   1361 C  C   . SER A 1 183 ? 117.513 102.364 96.143  1.00 18.15  ? 183 SER A C   1 
ATOM   1362 O  O   . SER A 1 183 ? 116.893 103.158 95.422  1.00 28.00  ? 183 SER A O   1 
ATOM   1363 C  CB  . SER A 1 183 ? 117.964 100.037 95.331  1.00 10.73  ? 183 SER A CB  1 
ATOM   1364 O  OG  . SER A 1 183 ? 118.947 99.137  94.857  1.00 26.91  ? 183 SER A OG  1 
ATOM   1365 N  N   . VAL A 1 184 ? 117.318 102.296 97.462  1.00 9.32   ? 184 VAL A N   1 
ATOM   1366 C  CA  . VAL A 1 184 ? 116.334 103.162 98.107  1.00 10.21  ? 184 VAL A CA  1 
ATOM   1367 C  C   . VAL A 1 184 ? 116.697 104.629 97.897  1.00 15.23  ? 184 VAL A C   1 
ATOM   1368 O  O   . VAL A 1 184 ? 115.855 105.445 97.502  1.00 26.86  ? 184 VAL A O   1 
ATOM   1369 C  CB  . VAL A 1 184 ? 116.213 102.813 99.602  1.00 16.17  ? 184 VAL A CB  1 
ATOM   1370 C  CG1 . VAL A 1 184 ? 115.552 103.942 100.367 1.00 16.11  ? 184 VAL A CG1 1 
ATOM   1371 C  CG2 . VAL A 1 184 ? 115.434 101.524 99.780  1.00 7.84   ? 184 VAL A CG2 1 
ATOM   1372 N  N   . ALA A 1 185 ? 117.965 104.977 98.126  1.00 13.48  ? 185 ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 185 ? 118.399 106.364 97.980  1.00 10.47  ? 185 ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 185 ? 118.317 106.834 96.531  1.00 21.13  ? 185 ALA A C   1 
ATOM   1375 O  O   . ALA A 1 185 ? 117.872 107.961 96.257  1.00 34.98  ? 185 ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 185 ? 119.822 106.519 98.512  1.00 11.88  ? 185 ALA A CB  1 
ATOM   1377 N  N   . TYR A 1 186 ? 118.746 105.992 95.588  1.00 15.50  ? 186 TYR A N   1 
ATOM   1378 C  CA  . TYR A 1 186 ? 118.762 106.415 94.194  1.00 10.68  ? 186 TYR A CA  1 
ATOM   1379 C  C   . TYR A 1 186 ? 117.354 106.560 93.637  1.00 14.92  ? 186 TYR A C   1 
ATOM   1380 O  O   . TYR A 1 186 ? 117.130 107.378 92.738  1.00 24.36  ? 186 TYR A O   1 
ATOM   1381 C  CB  . TYR A 1 186 ? 119.581 105.438 93.351  1.00 18.86  ? 186 TYR A CB  1 
ATOM   1382 C  CG  . TYR A 1 186 ? 121.080 105.536 93.564  1.00 25.77  ? 186 TYR A CG  1 
ATOM   1383 C  CD1 . TYR A 1 186 ? 121.608 106.237 94.640  1.00 22.93  ? 186 TYR A CD1 1 
ATOM   1384 C  CD2 . TYR A 1 186 ? 121.965 104.929 92.686  1.00 27.78  ? 186 TYR A CD2 1 
ATOM   1385 C  CE1 . TYR A 1 186 ? 122.969 106.324 94.838  1.00 20.83  ? 186 TYR A CE1 1 
ATOM   1386 C  CE2 . TYR A 1 186 ? 123.329 105.010 92.877  1.00 23.30  ? 186 TYR A CE2 1 
ATOM   1387 C  CZ  . TYR A 1 186 ? 123.825 105.709 93.954  1.00 30.24  ? 186 TYR A CZ  1 
ATOM   1388 O  OH  . TYR A 1 186 ? 125.183 105.795 94.146  1.00 36.69  ? 186 TYR A OH  1 
ATOM   1389 N  N   . THR A 1 187 ? 116.392 105.787 94.150  1.00 15.17  ? 187 THR A N   1 
ATOM   1390 C  CA  . THR A 1 187 ? 115.005 106.017 93.761  1.00 18.06  ? 187 THR A CA  1 
ATOM   1391 C  C   . THR A 1 187 ? 114.435 107.261 94.435  1.00 21.63  ? 187 THR A C   1 
ATOM   1392 O  O   . THR A 1 187 ? 113.653 107.996 93.820  1.00 19.84  ? 187 THR A O   1 
ATOM   1393 C  CB  . THR A 1 187 ? 114.150 104.793 94.088  1.00 22.54  ? 187 THR A CB  1 
ATOM   1394 O  OG1 . THR A 1 187 ? 114.353 104.417 95.455  1.00 31.76  ? 187 THR A OG1 1 
ATOM   1395 C  CG2 . THR A 1 187 ? 114.521 103.633 93.185  1.00 6.15   ? 187 THR A CG2 1 
ATOM   1396 N  N   . ASP A 1 188 ? 114.814 107.507 95.696  1.00 21.80  ? 188 ASP A N   1 
ATOM   1397 C  CA  . ASP A 1 188 ? 114.346 108.699 96.398  1.00 16.13  ? 188 ASP A CA  1 
ATOM   1398 C  C   . ASP A 1 188 ? 114.767 109.974 95.687  1.00 13.95  ? 188 ASP A C   1 
ATOM   1399 O  O   . ASP A 1 188 ? 114.019 110.959 95.685  1.00 33.71  ? 188 ASP A O   1 
ATOM   1400 C  CB  . ASP A 1 188 ? 114.874 108.711 97.832  1.00 5.37   ? 188 ASP A CB  1 
ATOM   1401 C  CG  . ASP A 1 188 ? 114.218 107.667 98.703  1.00 22.95  ? 188 ASP A CG  1 
ATOM   1402 O  OD1 . ASP A 1 188 ? 113.170 107.128 98.296  1.00 32.40  ? 188 ASP A OD1 1 
ATOM   1403 O  OD2 . ASP A 1 188 ? 114.752 107.383 99.792  1.00 20.88  ? 188 ASP A OD2 1 
ATOM   1404 N  N   . VAL A 1 189 ? 115.958 109.978 95.085  1.00 17.75  ? 189 VAL A N   1 
ATOM   1405 C  CA  . VAL A 1 189 ? 116.422 111.171 94.376  1.00 20.05  ? 189 VAL A CA  1 
ATOM   1406 C  C   . VAL A 1 189 ? 115.445 111.553 93.265  1.00 20.90  ? 189 VAL A C   1 
ATOM   1407 O  O   . VAL A 1 189 ? 115.075 112.724 93.116  1.00 21.88  ? 189 VAL A O   1 
ATOM   1408 C  CB  . VAL A 1 189 ? 117.845 110.956 93.829  1.00 19.45  ? 189 VAL A CB  1 
ATOM   1409 C  CG1 . VAL A 1 189 ? 118.219 112.069 92.865  1.00 9.18   ? 189 VAL A CG1 1 
ATOM   1410 C  CG2 . VAL A 1 189 ? 118.844 110.886 94.970  1.00 16.87  ? 189 VAL A CG2 1 
ATOM   1411 N  N   . VAL A 1 190 ? 115.010 110.573 92.469  1.00 21.50  ? 190 VAL A N   1 
ATOM   1412 C  CA  . VAL A 1 190 ? 114.072 110.846 91.381  1.00 17.25  ? 190 VAL A CA  1 
ATOM   1413 C  C   . VAL A 1 190 ? 112.683 111.168 91.926  1.00 19.71  ? 190 VAL A C   1 
ATOM   1414 O  O   . VAL A 1 190 ? 111.979 112.054 91.412  1.00 24.62  ? 190 VAL A O   1 
ATOM   1415 C  CB  . VAL A 1 190 ? 114.034 109.652 90.408  1.00 18.37  ? 190 VAL A CB  1 
ATOM   1416 C  CG1 . VAL A 1 190 ? 113.138 109.953 89.222  1.00 17.46  ? 190 VAL A CG1 1 
ATOM   1417 C  CG2 . VAL A 1 190 ? 115.435 109.302 89.944  1.00 13.24  ? 190 VAL A CG2 1 
ATOM   1418 N  N   . GLN A 1 191 ? 112.259 110.446 92.965  1.00 25.83  ? 191 GLN A N   1 
ATOM   1419 C  CA  . GLN A 1 191 ? 110.901 110.613 93.470  1.00 18.46  ? 191 GLN A CA  1 
ATOM   1420 C  C   . GLN A 1 191 ? 110.698 111.976 94.122  1.00 23.62  ? 191 GLN A C   1 
ATOM   1421 O  O   . GLN A 1 191 ? 109.596 112.531 94.049  1.00 32.37  ? 191 GLN A O   1 
ATOM   1422 C  CB  . GLN A 1 191 ? 110.569 109.479 94.436  1.00 15.44  ? 191 GLN A CB  1 
ATOM   1423 C  CG  . GLN A 1 191 ? 110.440 108.131 93.741  1.00 21.70  ? 191 GLN A CG  1 
ATOM   1424 C  CD  . GLN A 1 191 ? 110.461 106.959 94.697  1.00 21.54  ? 191 GLN A CD  1 
ATOM   1425 O  OE1 . GLN A 1 191 ? 111.208 106.949 95.672  1.00 30.26  ? 191 GLN A OE1 1 
ATOM   1426 N  NE2 . GLN A 1 191 ? 109.645 105.955 94.414  1.00 23.35  ? 191 GLN A NE2 1 
ATOM   1427 N  N   . LEU A 1 192 ? 111.735 112.538 94.748  1.00 13.87  ? 192 LEU A N   1 
ATOM   1428 C  CA  . LEU A 1 192 ? 111.611 113.885 95.301  1.00 15.51  ? 192 LEU A CA  1 
ATOM   1429 C  C   . LEU A 1 192 ? 111.362 114.915 94.204  1.00 22.06  ? 192 LEU A C   1 
ATOM   1430 O  O   . LEU A 1 192 ? 110.532 115.820 94.363  1.00 27.04  ? 192 LEU A O   1 
ATOM   1431 C  CB  . LEU A 1 192 ? 112.864 114.244 96.097  1.00 19.57  ? 192 LEU A CB  1 
ATOM   1432 C  CG  . LEU A 1 192 ? 112.772 115.518 96.937  1.00 20.80  ? 192 LEU A CG  1 
ATOM   1433 C  CD1 . LEU A 1 192 ? 111.590 115.447 97.888  1.00 16.38  ? 192 LEU A CD1 1 
ATOM   1434 C  CD2 . LEU A 1 192 ? 114.062 115.748 97.698  1.00 16.76  ? 192 LEU A CD2 1 
ATOM   1435 N  N   . PHE A 1 193 ? 112.081 114.798 93.086  1.00 22.45  ? 193 PHE A N   1 
ATOM   1436 C  CA  . PHE A 1 193 ? 111.861 115.697 91.958  1.00 22.99  ? 193 PHE A CA  1 
ATOM   1437 C  C   . PHE A 1 193 ? 110.449 115.546 91.409  1.00 23.97  ? 193 PHE A C   1 
ATOM   1438 O  O   . PHE A 1 193 ? 109.795 116.541 91.059  1.00 25.34  ? 193 PHE A O   1 
ATOM   1439 C  CB  . PHE A 1 193 ? 112.904 115.420 90.874  1.00 22.29  ? 193 PHE A CB  1 
ATOM   1440 C  CG  . PHE A 1 193 ? 112.688 116.190 89.605  1.00 35.50  ? 193 PHE A CG  1 
ATOM   1441 C  CD1 . PHE A 1 193 ? 113.126 117.497 89.489  1.00 34.59  ? 193 PHE A CD1 1 
ATOM   1442 C  CD2 . PHE A 1 193 ? 112.063 115.600 88.518  1.00 38.35  ? 193 PHE A CD2 1 
ATOM   1443 C  CE1 . PHE A 1 193 ? 112.934 118.205 88.319  1.00 35.24  ? 193 PHE A CE1 1 
ATOM   1444 C  CE2 . PHE A 1 193 ? 111.867 116.304 87.347  1.00 35.97  ? 193 PHE A CE2 1 
ATOM   1445 C  CZ  . PHE A 1 193 ? 112.304 117.608 87.247  1.00 34.70  ? 193 PHE A CZ  1 
ATOM   1446 N  N   . CYS A 1 194 ? 109.963 114.304 91.327  1.00 20.44  ? 194 CYS A N   1 
ATOM   1447 C  CA  . CYS A 1 194 ? 108.589 114.086 90.880  1.00 25.29  ? 194 CYS A CA  1 
ATOM   1448 C  C   . CYS A 1 194 ? 107.584 114.755 91.815  1.00 31.93  ? 194 CYS A C   1 
ATOM   1449 O  O   . CYS A 1 194 ? 106.642 115.412 91.354  1.00 27.09  ? 194 CYS A O   1 
ATOM   1450 C  CB  . CYS A 1 194 ? 108.303 112.590 90.762  1.00 29.61  ? 194 CYS A CB  1 
ATOM   1451 S  SG  . CYS A 1 194 ? 109.271 111.754 89.490  1.00 53.50  ? 194 CYS A SG  1 
ATOM   1452 N  N   . ILE A 1 195 ? 107.775 114.608 93.131  1.00 28.48  ? 195 ILE A N   1 
ATOM   1453 C  CA  . ILE A 1 195 ? 106.884 115.252 94.098  1.00 22.84  ? 195 ILE A CA  1 
ATOM   1454 C  C   . ILE A 1 195 ? 106.886 116.761 93.897  1.00 22.98  ? 195 ILE A C   1 
ATOM   1455 O  O   . ILE A 1 195 ? 105.829 117.399 93.821  1.00 24.73  ? 195 ILE A O   1 
ATOM   1456 C  CB  . ILE A 1 195 ? 107.291 114.895 95.539  1.00 19.92  ? 195 ILE A CB  1 
ATOM   1457 C  CG1 . ILE A 1 195 ? 107.198 113.394 95.792  1.00 25.74  ? 195 ILE A CG1 1 
ATOM   1458 C  CG2 . ILE A 1 195 ? 106.428 115.644 96.539  1.00 16.17  ? 195 ILE A CG2 1 
ATOM   1459 C  CD1 . ILE A 1 195 ? 108.010 112.947 96.987  1.00 19.17  ? 195 ILE A CD1 1 
ATOM   1460 N  N   . PHE A 1 196 ? 108.081 117.352 93.808  1.00 23.62  ? 196 PHE A N   1 
ATOM   1461 C  CA  . PHE A 1 196 ? 108.194 118.801 93.678  1.00 19.24  ? 196 PHE A CA  1 
ATOM   1462 C  C   . PHE A 1 196 ? 107.461 119.303 92.442  1.00 26.21  ? 196 PHE A C   1 
ATOM   1463 O  O   . PHE A 1 196 ? 106.614 120.203 92.529  1.00 22.83  ? 196 PHE A O   1 
ATOM   1464 C  CB  . PHE A 1 196 ? 109.670 119.200 93.629  1.00 17.53  ? 196 PHE A CB  1 
ATOM   1465 C  CG  . PHE A 1 196 ? 109.903 120.682 93.544  1.00 29.42  ? 196 PHE A CG  1 
ATOM   1466 C  CD1 . PHE A 1 196 ? 109.922 121.461 94.687  1.00 31.57  ? 196 PHE A CD1 1 
ATOM   1467 C  CD2 . PHE A 1 196 ? 110.122 121.294 92.322  1.00 32.20  ? 196 PHE A CD2 1 
ATOM   1468 C  CE1 . PHE A 1 196 ? 110.144 122.822 94.611  1.00 27.27  ? 196 PHE A CE1 1 
ATOM   1469 C  CE2 . PHE A 1 196 ? 110.342 122.655 92.240  1.00 31.51  ? 196 PHE A CE2 1 
ATOM   1470 C  CZ  . PHE A 1 196 ? 110.353 123.419 93.386  1.00 28.31  ? 196 PHE A CZ  1 
ATOM   1471 N  N   . VAL A 1 197 ? 107.761 118.718 91.280  1.00 34.18  ? 197 VAL A N   1 
ATOM   1472 C  CA  . VAL A 1 197 ? 107.169 119.207 90.037  1.00 27.56  ? 197 VAL A CA  1 
ATOM   1473 C  C   . VAL A 1 197 ? 105.658 119.005 90.048  1.00 29.20  ? 197 VAL A C   1 
ATOM   1474 O  O   . VAL A 1 197 ? 104.890 119.919 89.717  1.00 34.19  ? 197 VAL A O   1 
ATOM   1475 C  CB  . VAL A 1 197 ? 107.824 118.525 88.822  1.00 32.23  ? 197 VAL A CB  1 
ATOM   1476 C  CG1 . VAL A 1 197 ? 107.105 118.917 87.544  1.00 28.67  ? 197 VAL A CG1 1 
ATOM   1477 C  CG2 . VAL A 1 197 ? 109.291 118.899 88.740  1.00 26.79  ? 197 VAL A CG2 1 
ATOM   1478 N  N   . GLY A 1 198 ? 105.207 117.808 90.440  1.00 29.77  ? 198 GLY A N   1 
ATOM   1479 C  CA  . GLY A 1 198 ? 103.784 117.521 90.408  1.00 28.60  ? 198 GLY A CA  1 
ATOM   1480 C  C   . GLY A 1 198 ? 102.980 118.402 91.341  1.00 30.88  ? 198 GLY A C   1 
ATOM   1481 O  O   . GLY A 1 198 ? 101.882 118.845 90.996  1.00 33.17  ? 198 GLY A O   1 
ATOM   1482 N  N   . LEU A 1 199 ? 103.508 118.670 92.538  1.00 32.62  ? 199 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 199 ? 102.784 119.526 93.470  1.00 23.47  ? 199 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 199 ? 102.789 120.979 93.014  1.00 28.78  ? 199 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 199 ? 101.757 121.654 93.083  1.00 38.33  ? 199 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 199 ? 103.375 119.403 94.872  1.00 30.21  ? 199 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 199 ? 102.731 118.368 95.794  1.00 30.68  ? 199 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 199 ? 103.055 118.684 97.240  1.00 29.78  ? 199 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 199 ? 101.228 118.309 95.577  1.00 21.76  ? 199 LEU A CD2 1 
ATOM   1490 N  N   . TRP A 1 200 ? 103.931 121.483 92.541  1.00 35.73  ? 200 TRP A N   1 
ATOM   1491 C  CA  . TRP A 1 200 ? 104.007 122.901 92.213  1.00 30.22  ? 200 TRP A CA  1 
ATOM   1492 C  C   . TRP A 1 200 ? 103.336 123.255 90.892  1.00 33.87  ? 200 TRP A C   1 
ATOM   1493 O  O   . TRP A 1 200 ? 103.008 124.427 90.683  1.00 35.29  ? 200 TRP A O   1 
ATOM   1494 C  CB  . TRP A 1 200 ? 105.465 123.360 92.186  1.00 30.21  ? 200 TRP A CB  1 
ATOM   1495 C  CG  . TRP A 1 200 ? 105.933 123.912 93.494  1.00 27.76  ? 200 TRP A CG  1 
ATOM   1496 C  CD1 . TRP A 1 200 ? 106.824 123.342 94.351  1.00 28.82  ? 200 TRP A CD1 1 
ATOM   1497 C  CD2 . TRP A 1 200 ? 105.527 125.144 94.099  1.00 35.06  ? 200 TRP A CD2 1 
ATOM   1498 N  NE1 . TRP A 1 200 ? 107.004 124.142 95.451  1.00 31.40  ? 200 TRP A NE1 1 
ATOM   1499 C  CE2 . TRP A 1 200 ? 106.218 125.256 95.320  1.00 33.06  ? 200 TRP A CE2 1 
ATOM   1500 C  CE3 . TRP A 1 200 ? 104.647 126.164 93.726  1.00 38.51  ? 200 TRP A CE3 1 
ATOM   1501 C  CZ2 . TRP A 1 200 ? 106.058 126.347 96.171  1.00 29.76  ? 200 TRP A CZ2 1 
ATOM   1502 C  CZ3 . TRP A 1 200 ? 104.488 127.246 94.572  1.00 32.66  ? 200 TRP A CZ3 1 
ATOM   1503 C  CH2 . TRP A 1 200 ? 105.190 127.329 95.780  1.00 32.40  ? 200 TRP A CH2 1 
ATOM   1504 N  N   . ILE A 1 201 ? 103.117 122.289 89.997  1.00 34.08  ? 201 ILE A N   1 
ATOM   1505 C  CA  . ILE A 1 201 ? 102.503 122.633 88.717  1.00 30.16  ? 201 ILE A CA  1 
ATOM   1506 C  C   . ILE A 1 201 ? 101.000 122.878 88.841  1.00 35.66  ? 201 ILE A C   1 
ATOM   1507 O  O   . ILE A 1 201 ? 100.412 123.538 87.976  1.00 43.19  ? 201 ILE A O   1 
ATOM   1508 C  CB  . ILE A 1 201 ? 102.792 121.532 87.680  1.00 36.55  ? 201 ILE A CB  1 
ATOM   1509 C  CG1 . ILE A 1 201 ? 102.297 121.934 86.290  1.00 38.47  ? 201 ILE A CG1 1 
ATOM   1510 C  CG2 . ILE A 1 201 ? 102.132 120.229 88.089  1.00 38.11  ? 201 ILE A CG2 1 
ATOM   1511 C  CD1 . ILE A 1 201 ? 102.971 121.187 85.167  1.00 38.89  ? 201 ILE A CD1 1 
ATOM   1512 N  N   . SER A 1 202 ? 100.365 122.400 89.911  1.00 39.43  ? 202 SER A N   1 
ATOM   1513 C  CA  . SER A 1 202 ? 98.908  122.380 89.995  1.00 38.57  ? 202 SER A CA  1 
ATOM   1514 C  C   . SER A 1 202 ? 98.302  123.639 90.607  1.00 38.14  ? 202 SER A C   1 
ATOM   1515 O  O   . SER A 1 202 ? 97.141  123.952 90.320  1.00 31.54  ? 202 SER A O   1 
ATOM   1516 C  CB  . SER A 1 202 ? 98.455  121.164 90.807  1.00 35.44  ? 202 SER A CB  1 
ATOM   1517 O  OG  . SER A 1 202 ? 98.926  121.240 92.140  1.00 37.55  ? 202 SER A OG  1 
ATOM   1518 N  N   . VAL A 1 203 ? 99.048  124.360 91.447  1.00 34.33  ? 203 VAL A N   1 
ATOM   1519 C  CA  . VAL A 1 203 ? 98.463  125.485 92.183  1.00 28.95  ? 203 VAL A CA  1 
ATOM   1520 C  C   . VAL A 1 203 ? 97.979  126.607 91.268  1.00 34.87  ? 203 VAL A C   1 
ATOM   1521 O  O   . VAL A 1 203 ? 96.854  127.095 91.470  1.00 34.05  ? 203 VAL A O   1 
ATOM   1522 C  CB  . VAL A 1 203 ? 99.446  125.979 93.259  1.00 31.88  ? 203 VAL A CB  1 
ATOM   1523 C  CG1 . VAL A 1 203 ? 98.868  127.168 94.001  1.00 34.23  ? 203 VAL A CG1 1 
ATOM   1524 C  CG2 . VAL A 1 203 ? 99.770  124.857 94.229  1.00 31.20  ? 203 VAL A CG2 1 
ATOM   1525 N  N   . PRO A 1 204 ? 98.755  127.079 90.281  1.00 41.60  ? 204 PRO A N   1 
ATOM   1526 C  CA  . PRO A 1 204 ? 98.235  128.152 89.414  1.00 34.57  ? 204 PRO A CA  1 
ATOM   1527 C  C   . PRO A 1 204 ? 96.980  127.769 88.650  1.00 36.61  ? 204 PRO A C   1 
ATOM   1528 O  O   . PRO A 1 204 ? 96.156  128.644 88.358  1.00 38.45  ? 204 PRO A O   1 
ATOM   1529 C  CB  . PRO A 1 204 ? 99.408  128.439 88.464  1.00 32.72  ? 204 PRO A CB  1 
ATOM   1530 C  CG  . PRO A 1 204 ? 100.294 127.252 88.561  1.00 32.22  ? 204 PRO A CG  1 
ATOM   1531 C  CD  . PRO A 1 204 ? 100.161 126.774 89.963  1.00 34.22  ? 204 PRO A CD  1 
ATOM   1532 N  N   . PHE A 1 205 ? 96.814  126.492 88.302  1.00 34.75  ? 205 PHE A N   1 
ATOM   1533 C  CA  . PHE A 1 205 ? 95.608  126.072 87.595  1.00 33.90  ? 205 PHE A CA  1 
ATOM   1534 C  C   . PHE A 1 205 ? 94.383  126.131 88.500  1.00 41.29  ? 205 PHE A C   1 
ATOM   1535 O  O   . PHE A 1 205 ? 93.297  126.521 88.058  1.00 43.85  ? 205 PHE A O   1 
ATOM   1536 C  CB  . PHE A 1 205 ? 95.794  124.666 87.030  1.00 30.41  ? 205 PHE A CB  1 
ATOM   1537 C  CG  . PHE A 1 205 ? 96.571  124.630 85.747  1.00 37.36  ? 205 PHE A CG  1 
ATOM   1538 C  CD1 . PHE A 1 205 ? 95.946  124.872 84.538  1.00 37.64  ? 205 PHE A CD1 1 
ATOM   1539 C  CD2 . PHE A 1 205 ? 97.927  124.358 85.750  1.00 38.93  ? 205 PHE A CD2 1 
ATOM   1540 C  CE1 . PHE A 1 205 ? 96.656  124.843 83.357  1.00 33.36  ? 205 PHE A CE1 1 
ATOM   1541 C  CE2 . PHE A 1 205 ? 98.642  124.327 84.573  1.00 38.13  ? 205 PHE A CE2 1 
ATOM   1542 C  CZ  . PHE A 1 205 ? 98.005  124.570 83.375  1.00 36.46  ? 205 PHE A CZ  1 
ATOM   1543 N  N   . ALA A 1 206 ? 94.535  125.743 89.767  1.00 36.58  ? 206 ALA A N   1 
ATOM   1544 C  CA  . ALA A 1 206 ? 93.413  125.783 90.697  1.00 25.14  ? 206 ALA A CA  1 
ATOM   1545 C  C   . ALA A 1 206 ? 93.093  127.200 91.152  1.00 34.28  ? 206 ALA A C   1 
ATOM   1546 O  O   . ALA A 1 206 ? 91.936  127.497 91.464  1.00 37.35  ? 206 ALA A O   1 
ATOM   1547 C  CB  . ALA A 1 206 ? 93.699  124.898 91.910  1.00 23.01  ? 206 ALA A CB  1 
ATOM   1548 N  N   . LEU A 1 207 ? 94.093  128.083 91.200  1.00 38.90  ? 207 LEU A N   1 
ATOM   1549 C  CA  . LEU A 1 207 ? 93.849  129.452 91.643  1.00 28.57  ? 207 LEU A CA  1 
ATOM   1550 C  C   . LEU A 1 207 ? 93.009  130.252 90.656  1.00 29.38  ? 207 LEU A C   1 
ATOM   1551 O  O   . LEU A 1 207 ? 92.442  131.280 91.040  1.00 35.45  ? 207 LEU A O   1 
ATOM   1552 C  CB  . LEU A 1 207 ? 95.175  130.174 91.883  1.00 31.20  ? 207 LEU A CB  1 
ATOM   1553 C  CG  . LEU A 1 207 ? 95.725  130.169 93.309  1.00 34.42  ? 207 LEU A CG  1 
ATOM   1554 C  CD1 . LEU A 1 207 ? 97.121  130.762 93.340  1.00 32.60  ? 207 LEU A CD1 1 
ATOM   1555 C  CD2 . LEU A 1 207 ? 94.801  130.925 94.242  1.00 29.22  ? 207 LEU A CD2 1 
ATOM   1556 N  N   . SER A 1 208 ? 92.915  129.814 89.403  1.00 38.22  ? 208 SER A N   1 
ATOM   1557 C  CA  . SER A 1 208 ? 92.253  130.579 88.356  1.00 40.01  ? 208 SER A CA  1 
ATOM   1558 C  C   . SER A 1 208 ? 90.843  130.088 88.052  1.00 43.02  ? 208 SER A C   1 
ATOM   1559 O  O   . SER A 1 208 ? 90.227  130.570 87.096  1.00 43.80  ? 208 SER A O   1 
ATOM   1560 C  CB  . SER A 1 208 ? 93.095  130.557 87.080  1.00 41.94  ? 208 SER A CB  1 
ATOM   1561 O  OG  . SER A 1 208 ? 94.474  130.673 87.381  1.00 46.28  ? 208 SER A OG  1 
ATOM   1562 N  N   . HIS A 1 209 ? 90.320  129.146 88.829  1.00 42.74  ? 209 HIS A N   1 
ATOM   1563 C  CA  . HIS A 1 209 ? 88.971  128.658 88.586  1.00 37.61  ? 209 HIS A CA  1 
ATOM   1564 C  C   . HIS A 1 209 ? 87.952  129.745 88.920  1.00 39.45  ? 209 HIS A C   1 
ATOM   1565 O  O   . HIS A 1 209 ? 88.141  130.500 89.879  1.00 47.21  ? 209 HIS A O   1 
ATOM   1566 C  CB  . HIS A 1 209 ? 88.695  127.405 89.414  1.00 37.98  ? 209 HIS A CB  1 
ATOM   1567 C  CG  . HIS A 1 209 ? 87.615  126.534 88.851  1.00 43.49  ? 209 HIS A CG  1 
ATOM   1568 N  ND1 . HIS A 1 209 ? 86.291  126.665 89.207  1.00 42.14  ? 209 HIS A ND1 1 
ATOM   1569 C  CD2 . HIS A 1 209 ? 87.664  125.521 87.955  1.00 43.83  ? 209 HIS A CD2 1 
ATOM   1570 C  CE1 . HIS A 1 209 ? 85.570  125.771 88.555  1.00 36.44  ? 209 HIS A CE1 1 
ATOM   1571 N  NE2 . HIS A 1 209 ? 86.380  125.063 87.789  1.00 41.74  ? 209 HIS A NE2 1 
ATOM   1572 N  N   . PRO A 1 210 ? 86.870  129.860 88.144  1.00 37.29  ? 210 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 210 ? 85.869  130.901 88.431  1.00 40.56  ? 210 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 210 ? 85.207  130.762 89.791  1.00 45.11  ? 210 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 210 ? 84.747  131.767 90.348  1.00 51.04  ? 210 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 210 ? 84.853  130.730 87.293  1.00 40.80  ? 210 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 210 ? 85.605  130.046 86.208  1.00 44.56  ? 210 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 210 ? 86.579  129.142 86.893  1.00 39.32  ? 210 PRO A CD  1 
ATOM   1579 N  N   . ALA A 1 211 ? 85.136  129.551 90.343  1.00 41.98  ? 211 ALA A N   1 
ATOM   1580 C  CA  . ALA A 1 211 ? 84.465  129.330 91.617  1.00 36.23  ? 211 ALA A CA  1 
ATOM   1581 C  C   . ALA A 1 211 ? 85.308  129.729 92.820  1.00 35.92  ? 211 ALA A C   1 
ATOM   1582 O  O   . ALA A 1 211 ? 84.778  129.775 93.934  1.00 40.62  ? 211 ALA A O   1 
ATOM   1583 C  CB  . ALA A 1 211 ? 84.059  127.862 91.748  1.00 35.52  ? 211 ALA A CB  1 
ATOM   1584 N  N   . VAL A 1 212 ? 86.588  130.018 92.631  1.00 29.87  ? 212 VAL A N   1 
ATOM   1585 C  CA  . VAL A 1 212 ? 87.487  130.342 93.733  1.00 31.80  ? 212 VAL A CA  1 
ATOM   1586 C  C   . VAL A 1 212 ? 87.577  131.853 93.882  1.00 37.83  ? 212 VAL A C   1 
ATOM   1587 O  O   . VAL A 1 212 ? 87.694  132.586 92.894  1.00 41.66  ? 212 VAL A O   1 
ATOM   1588 C  CB  . VAL A 1 212 ? 88.877  129.718 93.505  1.00 30.11  ? 212 VAL A CB  1 
ATOM   1589 C  CG1 . VAL A 1 212 ? 89.710  129.797 94.773  1.00 24.11  ? 212 VAL A CG1 1 
ATOM   1590 C  CG2 . VAL A 1 212 ? 88.739  128.279 93.047  1.00 28.97  ? 212 VAL A CG2 1 
ATOM   1591 N  N   . ALA A 1 213 ? 87.518  132.322 95.125  1.00 31.62  ? 213 ALA A N   1 
ATOM   1592 C  CA  . ALA A 1 213 ? 87.613  133.736 95.439  1.00 32.06  ? 213 ALA A CA  1 
ATOM   1593 C  C   . ALA A 1 213 ? 89.044  134.090 95.835  1.00 37.82  ? 213 ALA A C   1 
ATOM   1594 O  O   . ALA A 1 213 ? 89.944  133.247 95.840  1.00 46.93  ? 213 ALA A O   1 
ATOM   1595 C  CB  . ALA A 1 213 ? 86.626  134.104 96.548  1.00 33.25  ? 213 ALA A CB  1 
ATOM   1596 N  N   . ASP A 1 214 ? 89.254  135.361 96.166  1.00 39.56  ? 214 ASP A N   1 
ATOM   1597 C  CA  . ASP A 1 214 ? 90.566  135.819 96.605  1.00 35.05  ? 214 ASP A CA  1 
ATOM   1598 C  C   . ASP A 1 214 ? 90.937  135.153 97.923  1.00 30.72  ? 214 ASP A C   1 
ATOM   1599 O  O   . ASP A 1 214 ? 90.140  135.135 98.865  1.00 34.88  ? 214 ASP A O   1 
ATOM   1600 C  CB  . ASP A 1 214 ? 90.568  137.338 96.758  1.00 35.09  ? 214 ASP A CB  1 
ATOM   1601 C  CG  . ASP A 1 214 ? 91.966  137.924 96.792  1.00 42.17  ? 214 ASP A CG  1 
ATOM   1602 O  OD1 . ASP A 1 214 ? 92.934  137.160 96.984  1.00 46.39  ? 214 ASP A OD1 1 
ATOM   1603 O  OD2 . ASP A 1 214 ? 92.098  139.154 96.628  1.00 45.65  ? 214 ASP A OD2 1 
ATOM   1604 N  N   . ILE A 1 215 ? 92.152  134.607 97.992  1.00 26.86  ? 215 ILE A N   1 
ATOM   1605 C  CA  . ILE A 1 215 ? 92.589  133.952 99.220  1.00 34.36  ? 215 ILE A CA  1 
ATOM   1606 C  C   . ILE A 1 215 ? 93.188  134.940 100.212 1.00 37.95  ? 215 ILE A C   1 
ATOM   1607 O  O   . ILE A 1 215 ? 93.308  134.615 101.399 1.00 42.39  ? 215 ILE A O   1 
ATOM   1608 C  CB  . ILE A 1 215 ? 93.582  132.817 98.915  1.00 34.60  ? 215 ILE A CB  1 
ATOM   1609 C  CG1 . ILE A 1 215 ? 94.946  133.376 98.514  1.00 36.57  ? 215 ILE A CG1 1 
ATOM   1610 C  CG2 . ILE A 1 215 ? 93.035  131.905 97.829  1.00 29.98  ? 215 ILE A CG2 1 
ATOM   1611 C  CD1 . ILE A 1 215 ? 96.060  132.361 98.601  1.00 34.52  ? 215 ILE A CD1 1 
ATOM   1612 N  N   . GLY A 1 216 ? 93.581  136.132 99.762  1.00 37.04  ? 216 GLY A N   1 
ATOM   1613 C  CA  . GLY A 1 216 ? 93.952  137.177 100.702 1.00 33.12  ? 216 GLY A CA  1 
ATOM   1614 C  C   . GLY A 1 216 ? 92.762  137.700 101.483 1.00 37.70  ? 216 GLY A C   1 
ATOM   1615 O  O   . GLY A 1 216 ? 92.864  137.966 102.684 1.00 42.18  ? 216 GLY A O   1 
ATOM   1616 N  N   . PHE A 1 217 ? 91.620  137.859 100.812 1.00 38.09  ? 217 PHE A N   1 
ATOM   1617 C  CA  . PHE A 1 217 ? 90.405  138.304 101.486 1.00 36.31  ? 217 PHE A CA  1 
ATOM   1618 C  C   . PHE A 1 217 ? 89.884  137.239 102.444 1.00 39.24  ? 217 PHE A C   1 
ATOM   1619 O  O   . PHE A 1 217 ? 89.501  137.543 103.578 1.00 44.72  ? 217 PHE A O   1 
ATOM   1620 C  CB  . PHE A 1 217 ? 89.342  138.660 100.446 1.00 41.59  ? 217 PHE A CB  1 
ATOM   1621 C  CG  . PHE A 1 217 ? 88.078  139.221 101.030 1.00 43.51  ? 217 PHE A CG  1 
ATOM   1622 C  CD1 . PHE A 1 217 ? 88.036  140.517 101.512 1.00 45.72  ? 217 PHE A CD1 1 
ATOM   1623 C  CD2 . PHE A 1 217 ? 86.929  138.452 101.090 1.00 43.87  ? 217 PHE A CD2 1 
ATOM   1624 C  CE1 . PHE A 1 217 ? 86.872  141.034 102.046 1.00 47.29  ? 217 PHE A CE1 1 
ATOM   1625 C  CE2 . PHE A 1 217 ? 85.764  138.963 101.623 1.00 46.37  ? 217 PHE A CE2 1 
ATOM   1626 C  CZ  . PHE A 1 217 ? 85.734  140.255 102.101 1.00 46.75  ? 217 PHE A CZ  1 
ATOM   1627 N  N   . THR A 1 218 ? 89.865  135.982 102.000 1.00 37.39  ? 218 THR A N   1 
ATOM   1628 C  CA  . THR A 1 218 ? 89.317  134.889 102.793 1.00 37.03  ? 218 THR A CA  1 
ATOM   1629 C  C   . THR A 1 218 ? 90.149  134.589 104.035 1.00 35.73  ? 218 THR A C   1 
ATOM   1630 O  O   . THR A 1 218 ? 89.583  134.187 105.058 1.00 40.50  ? 218 THR A O   1 
ATOM   1631 C  CB  . THR A 1 218 ? 89.181  133.647 101.902 1.00 35.14  ? 218 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 218 ? 87.974  133.744 101.136 1.00 37.43  ? 218 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 218 ? 89.133  132.373 102.721 1.00 40.82  ? 218 THR A CG2 1 
ATOM   1634 N  N   . ALA A 1 219 ? 91.464  134.806 103.986 1.00 33.11  ? 219 ALA A N   1 
ATOM   1635 C  CA  . ALA A 1 219 ? 92.319  134.526 105.135 1.00 33.55  ? 219 ALA A CA  1 
ATOM   1636 C  C   . ALA A 1 219 ? 91.965  135.376 106.348 1.00 43.73  ? 219 ALA A C   1 
ATOM   1637 O  O   . ALA A 1 219 ? 92.262  134.982 107.481 1.00 43.98  ? 219 ALA A O   1 
ATOM   1638 C  CB  . ALA A 1 219 ? 93.785  134.747 104.764 1.00 26.06  ? 219 ALA A CB  1 
ATOM   1639 N  N   . VAL A 1 220 ? 91.335  136.534 106.137 1.00 45.03  ? 220 VAL A N   1 
ATOM   1640 C  CA  . VAL A 1 220 ? 91.016  137.456 107.219 1.00 40.20  ? 220 VAL A CA  1 
ATOM   1641 C  C   . VAL A 1 220 ? 89.519  137.630 107.423 1.00 40.29  ? 220 VAL A C   1 
ATOM   1642 O  O   . VAL A 1 220 ? 89.078  137.812 108.559 1.00 50.99  ? 220 VAL A O   1 
ATOM   1643 C  CB  . VAL A 1 220 ? 91.696  138.823 106.982 1.00 44.26  ? 220 VAL A CB  1 
ATOM   1644 C  CG1 . VAL A 1 220 ? 90.948  139.960 107.665 1.00 43.57  ? 220 VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A 1 220 ? 93.145  138.778 107.446 1.00 40.56  ? 220 VAL A CG2 1 
ATOM   1646 N  N   . HIS A 1 221 ? 88.710  137.516 106.371 1.00 38.03  ? 221 HIS A N   1 
ATOM   1647 C  CA  . HIS A 1 221 ? 87.274  137.726 106.475 1.00 42.68  ? 221 HIS A CA  1 
ATOM   1648 C  C   . HIS A 1 221 ? 86.538  136.468 106.041 1.00 44.46  ? 221 HIS A C   1 
ATOM   1649 O  O   . HIS A 1 221 ? 87.033  135.692 105.220 1.00 53.04  ? 221 HIS A O   1 
ATOM   1650 C  CB  . HIS A 1 221 ? 86.823  138.924 105.629 1.00 47.05  ? 221 HIS A CB  1 
ATOM   1651 C  CG  . HIS A 1 221 ? 87.318  140.241 106.139 1.00 49.20  ? 221 HIS A CG  1 
ATOM   1652 N  ND1 . HIS A 1 221 ? 88.169  141.048 105.416 1.00 47.86  ? 221 HIS A ND1 1 
ATOM   1653 C  CD2 . HIS A 1 221 ? 87.083  140.890 107.304 1.00 49.93  ? 221 HIS A CD2 1 
ATOM   1654 C  CE1 . HIS A 1 221 ? 88.437  142.137 106.113 1.00 50.18  ? 221 HIS A CE1 1 
ATOM   1655 N  NE2 . HIS A 1 221 ? 87.791  142.067 107.262 1.00 52.95  ? 221 HIS A NE2 1 
ATOM   1656 N  N   . ALA A 1 222 ? 85.347  136.275 106.601 1.00 45.85  ? 222 ALA A N   1 
ATOM   1657 C  CA  . ALA A 1 222 ? 84.542  135.091 106.331 1.00 47.94  ? 222 ALA A CA  1 
ATOM   1658 C  C   . ALA A 1 222 ? 83.635  135.329 105.130 1.00 48.93  ? 222 ALA A C   1 
ATOM   1659 O  O   . ALA A 1 222 ? 82.865  136.295 105.107 1.00 51.03  ? 222 ALA A O   1 
ATOM   1660 C  CB  . ALA A 1 222 ? 83.707  134.720 107.556 1.00 44.61  ? 222 ALA A CB  1 
ATOM   1661 N  N   . LYS A 1 223 ? 83.727  134.445 104.135 1.00 42.66  ? 223 LYS A N   1 
ATOM   1662 C  CA  . LYS A 1 223 ? 82.887  134.541 102.948 1.00 42.70  ? 223 LYS A CA  1 
ATOM   1663 C  C   . LYS A 1 223 ? 81.938  133.353 102.857 1.00 48.39  ? 223 LYS A C   1 
ATOM   1664 O  O   . LYS A 1 223 ? 80.717  133.528 102.795 1.00 49.13  ? 223 LYS A O   1 
ATOM   1665 C  CB  . LYS A 1 223 ? 83.748  134.630 101.689 1.00 41.52  ? 223 LYS A CB  1 
ATOM   1666 C  CG  . LYS A 1 223 ? 83.017  135.185 100.481 1.00 42.27  ? 223 LYS A CG  1 
ATOM   1667 C  CD  . LYS A 1 223 ? 83.973  135.456 99.338  1.00 46.59  ? 223 LYS A CD  1 
ATOM   1668 C  CE  . LYS A 1 223 ? 83.318  136.311 98.269  1.00 48.67  ? 223 LYS A CE  1 
ATOM   1669 N  NZ  . LYS A 1 223 ? 81.939  135.850 97.965  1.00 48.46  ? 223 LYS A NZ  1 
ATOM   1670 N  N   . TYR A 1 224 ? 82.491  132.140 102.849 1.00 49.02  ? 224 TYR A N   1 
ATOM   1671 C  CA  . TYR A 1 224 ? 81.699  130.919 102.869 1.00 43.15  ? 224 TYR A CA  1 
ATOM   1672 C  C   . TYR A 1 224 ? 81.850  130.128 104.157 1.00 43.55  ? 224 TYR A C   1 
ATOM   1673 O  O   . TYR A 1 224 ? 81.034  129.235 104.411 1.00 45.02  ? 224 TYR A O   1 
ATOM   1674 C  CB  . TYR A 1 224 ? 82.070  130.007 101.687 1.00 37.17  ? 224 TYR A CB  1 
ATOM   1675 C  CG  . TYR A 1 224 ? 82.057  130.686 100.338 1.00 38.60  ? 224 TYR A CG  1 
ATOM   1676 C  CD1 . TYR A 1 224 ? 80.863  131.056 99.736  1.00 39.19  ? 224 TYR A CD1 1 
ATOM   1677 C  CD2 . TYR A 1 224 ? 83.240  130.947 99.662  1.00 44.73  ? 224 TYR A CD2 1 
ATOM   1678 C  CE1 . TYR A 1 224 ? 80.848  131.675 98.503  1.00 40.52  ? 224 TYR A CE1 1 
ATOM   1679 C  CE2 . TYR A 1 224 ? 83.235  131.564 98.429  1.00 45.94  ? 224 TYR A CE2 1 
ATOM   1680 C  CZ  . TYR A 1 224 ? 82.037  131.925 97.854  1.00 45.12  ? 224 TYR A CZ  1 
ATOM   1681 O  OH  . TYR A 1 224 ? 82.030  132.540 96.624  1.00 47.72  ? 224 TYR A OH  1 
ATOM   1682 N  N   . GLN A 1 225 ? 82.857  130.424 104.969 1.00 39.51  ? 225 GLN A N   1 
ATOM   1683 C  CA  . GLN A 1 225 ? 83.117  129.703 106.209 1.00 36.27  ? 225 GLN A CA  1 
ATOM   1684 C  C   . GLN A 1 225 ? 84.108  130.526 107.024 1.00 40.14  ? 225 GLN A C   1 
ATOM   1685 O  O   . GLN A 1 225 ? 84.466  131.648 106.653 1.00 44.13  ? 225 GLN A O   1 
ATOM   1686 C  CB  . GLN A 1 225 ? 83.629  128.287 105.932 1.00 30.34  ? 225 GLN A CB  1 
ATOM   1687 C  CG  . GLN A 1 225 ? 85.047  128.218 105.397 1.00 32.74  ? 225 GLN A CG  1 
ATOM   1688 C  CD  . GLN A 1 225 ? 85.518  126.794 105.183 1.00 40.76  ? 225 GLN A CD  1 
ATOM   1689 O  OE1 . GLN A 1 225 ? 84.860  126.008 104.507 1.00 37.21  ? 225 GLN A OE1 1 
ATOM   1690 N  NE2 . GLN A 1 225 ? 86.665  126.456 105.758 1.00 41.88  ? 225 GLN A NE2 1 
ATOM   1691 N  N   . LYS A 1 226 ? 84.540  129.961 108.144 1.00 40.59  ? 226 LYS A N   1 
ATOM   1692 C  CA  . LYS A 1 226 ? 85.470  130.650 109.026 1.00 38.88  ? 226 LYS A CA  1 
ATOM   1693 C  C   . LYS A 1 226 ? 86.811  130.856 108.322 1.00 42.20  ? 226 LYS A C   1 
ATOM   1694 O  O   . LYS A 1 226 ? 87.251  129.988 107.560 1.00 46.01  ? 226 LYS A O   1 
ATOM   1695 C  CB  . LYS A 1 226 ? 85.652  129.839 110.311 1.00 38.45  ? 226 LYS A CB  1 
ATOM   1696 C  CG  . LYS A 1 226 ? 86.596  130.433 111.338 1.00 45.60  ? 226 LYS A CG  1 
ATOM   1697 C  CD  . LYS A 1 226 ? 86.601  129.619 112.623 1.00 45.34  ? 226 LYS A CD  1 
ATOM   1698 C  CE  . LYS A 1 226 ? 85.218  129.074 112.946 1.00 46.56  ? 226 LYS A CE  1 
ATOM   1699 N  NZ  . LYS A 1 226 ? 85.227  128.230 114.172 1.00 49.42  ? 226 LYS A NZ  1 
ATOM   1700 N  N   . PRO A 1 227 ? 87.482  132.002 108.544 1.00 34.93  ? 227 PRO A N   1 
ATOM   1701 C  CA  . PRO A 1 227 ? 88.772  132.251 107.880 1.00 34.52  ? 227 PRO A CA  1 
ATOM   1702 C  C   . PRO A 1 227 ? 89.813  131.182 108.176 1.00 29.77  ? 227 PRO A C   1 
ATOM   1703 O  O   . PRO A 1 227 ? 89.857  130.641 109.284 1.00 37.53  ? 227 PRO A O   1 
ATOM   1704 C  CB  . PRO A 1 227 ? 89.194  133.614 108.441 1.00 35.80  ? 227 PRO A CB  1 
ATOM   1705 C  CG  . PRO A 1 227 ? 87.919  134.278 108.804 1.00 31.98  ? 227 PRO A CG  1 
ATOM   1706 C  CD  . PRO A 1 227 ? 86.999  133.190 109.270 1.00 32.30  ? 227 PRO A CD  1 
ATOM   1707 N  N   . TRP A 1 228 ? 90.659  130.876 107.193 1.00 22.68  ? 228 TRP A N   1 
ATOM   1708 C  CA  . TRP A 1 228 ? 91.549  129.724 107.266 1.00 24.32  ? 228 TRP A CA  1 
ATOM   1709 C  C   . TRP A 1 228 ? 92.857  130.004 107.992 1.00 28.16  ? 228 TRP A C   1 
ATOM   1710 O  O   . TRP A 1 228 ? 93.682  129.093 108.112 1.00 26.86  ? 228 TRP A O   1 
ATOM   1711 C  CB  . TRP A 1 228 ? 91.846  129.187 105.860 1.00 24.15  ? 228 TRP A CB  1 
ATOM   1712 C  CG  . TRP A 1 228 ? 92.504  130.160 104.927 1.00 19.74  ? 228 TRP A CG  1 
ATOM   1713 C  CD1 . TRP A 1 228 ? 91.885  130.975 104.033 1.00 19.41  ? 228 TRP A CD1 1 
ATOM   1714 C  CD2 . TRP A 1 228 ? 93.909  130.398 104.779 1.00 26.17  ? 228 TRP A CD2 1 
ATOM   1715 N  NE1 . TRP A 1 228 ? 92.811  131.715 103.342 1.00 19.57  ? 228 TRP A NE1 1 
ATOM   1716 C  CE2 . TRP A 1 228 ? 94.063  131.379 103.783 1.00 20.02  ? 228 TRP A CE2 1 
ATOM   1717 C  CE3 . TRP A 1 228 ? 95.052  129.879 105.395 1.00 25.50  ? 228 TRP A CE3 1 
ATOM   1718 C  CZ2 . TRP A 1 228 ? 95.311  131.851 103.388 1.00 15.91  ? 228 TRP A CZ2 1 
ATOM   1719 C  CZ3 . TRP A 1 228 ? 96.288  130.350 105.003 1.00 22.66  ? 228 TRP A CZ3 1 
ATOM   1720 C  CH2 . TRP A 1 228 ? 96.408  131.326 104.009 1.00 20.40  ? 228 TRP A CH2 1 
ATOM   1721 N  N   . LEU A 1 229 ? 93.080  131.229 108.473 1.00 35.74  ? 229 LEU A N   1 
ATOM   1722 C  CA  . LEU A 1 229 ? 94.265  131.476 109.288 1.00 32.96  ? 229 LEU A CA  1 
ATOM   1723 C  C   . LEU A 1 229 ? 94.156  130.803 110.649 1.00 33.47  ? 229 LEU A C   1 
ATOM   1724 O  O   . LEU A 1 229 ? 95.167  130.358 111.202 1.00 36.12  ? 229 LEU A O   1 
ATOM   1725 C  CB  . LEU A 1 229 ? 94.496  132.977 109.455 1.00 33.54  ? 229 LEU A CB  1 
ATOM   1726 C  CG  . LEU A 1 229 ? 95.400  133.646 108.419 1.00 33.44  ? 229 LEU A CG  1 
ATOM   1727 C  CD1 . LEU A 1 229 ? 95.610  135.111 108.763 1.00 33.44  ? 229 LEU A CD1 1 
ATOM   1728 C  CD2 . LEU A 1 229 ? 96.731  132.923 108.313 1.00 27.62  ? 229 LEU A CD2 1 
ATOM   1729 N  N   . GLY A 1 230 ? 92.950  130.724 111.203 1.00 32.42  ? 230 GLY A N   1 
ATOM   1730 C  CA  . GLY A 1 230 ? 92.739  130.050 112.465 1.00 30.19  ? 230 GLY A CA  1 
ATOM   1731 C  C   . GLY A 1 230 ? 93.133  130.898 113.657 1.00 38.48  ? 230 GLY A C   1 
ATOM   1732 O  O   . GLY A 1 230 ? 93.592  132.035 113.542 1.00 48.85  ? 230 GLY A O   1 
ATOM   1733 N  N   . THR A 1 231 ? 92.937  130.317 114.837 1.00 41.71  ? 231 THR A N   1 
ATOM   1734 C  CA  . THR A 1 231 ? 93.303  130.969 116.085 1.00 41.91  ? 231 THR A CA  1 
ATOM   1735 C  C   . THR A 1 231 ? 93.445  129.904 117.161 1.00 43.03  ? 231 THR A C   1 
ATOM   1736 O  O   . THR A 1 231 ? 92.906  128.801 117.042 1.00 47.68  ? 231 THR A O   1 
ATOM   1737 C  CB  . THR A 1 231 ? 92.270  132.031 116.491 1.00 49.02  ? 231 THR A CB  1 
ATOM   1738 O  OG1 . THR A 1 231 ? 92.876  132.982 117.375 1.00 54.08  ? 231 THR A OG1 1 
ATOM   1739 C  CG2 . THR A 1 231 ? 91.072  131.393 117.178 1.00 41.91  ? 231 THR A CG2 1 
ATOM   1740 N  N   . VAL A 1 232 ? 94.186  130.246 118.210 1.00 44.06  ? 232 VAL A N   1 
ATOM   1741 C  CA  . VAL A 1 232 ? 94.395  129.365 119.353 1.00 50.85  ? 232 VAL A CA  1 
ATOM   1742 C  C   . VAL A 1 232 ? 93.792  130.038 120.576 1.00 49.11  ? 232 VAL A C   1 
ATOM   1743 O  O   . VAL A 1 232 ? 94.219  131.134 120.962 1.00 49.31  ? 232 VAL A O   1 
ATOM   1744 C  CB  . VAL A 1 232 ? 95.884  129.052 119.575 1.00 46.08  ? 232 VAL A CB  1 
ATOM   1745 C  CG1 . VAL A 1 232 ? 96.050  128.027 120.683 1.00 45.37  ? 232 VAL A CG1 1 
ATOM   1746 C  CG2 . VAL A 1 232 ? 96.520  128.552 118.289 1.00 42.65  ? 232 VAL A CG2 1 
ATOM   1747 N  N   . ASP A 1 233 ? 92.802  129.388 121.181 1.00 56.34  ? 233 ASP A N   1 
ATOM   1748 C  CA  . ASP A 1 233 ? 92.150  129.942 122.356 1.00 60.97  ? 233 ASP A CA  1 
ATOM   1749 C  C   . ASP A 1 233 ? 93.069  129.854 123.570 1.00 61.84  ? 233 ASP A C   1 
ATOM   1750 O  O   . ASP A 1 233 ? 94.017  129.066 123.612 1.00 65.51  ? 233 ASP A O   1 
ATOM   1751 C  CB  . ASP A 1 233 ? 90.837  129.213 122.639 1.00 62.33  ? 233 ASP A CB  1 
ATOM   1752 C  CG  . ASP A 1 233 ? 89.916  129.179 121.435 1.00 68.36  ? 233 ASP A CG  1 
ATOM   1753 O  OD1 . ASP A 1 233 ? 90.198  129.889 120.447 1.00 70.09  ? 233 ASP A OD1 1 
ATOM   1754 O  OD2 . ASP A 1 233 ? 88.909  128.443 121.478 1.00 65.50  ? 233 ASP A OD2 1 
ATOM   1755 N  N   . SER A 1 234 ? 92.776  130.687 124.571 1.00 63.34  ? 234 SER A N   1 
ATOM   1756 C  CA  . SER A 1 234 ? 93.574  130.695 125.791 1.00 63.99  ? 234 SER A CA  1 
ATOM   1757 C  C   . SER A 1 234 ? 93.453  129.394 126.574 1.00 66.19  ? 234 SER A C   1 
ATOM   1758 O  O   . SER A 1 234 ? 94.331  129.094 127.389 1.00 68.20  ? 234 SER A O   1 
ATOM   1759 C  CB  . SER A 1 234 ? 93.169  131.876 126.674 1.00 67.07  ? 234 SER A CB  1 
ATOM   1760 O  OG  . SER A 1 234 ? 91.761  132.034 126.701 1.00 68.28  ? 234 SER A OG  1 
ATOM   1761 N  N   . SER A 1 235 ? 92.394  128.621 126.349 1.00 63.21  ? 235 SER A N   1 
ATOM   1762 C  CA  . SER A 1 235 ? 92.196  127.351 127.033 1.00 61.06  ? 235 SER A CA  1 
ATOM   1763 C  C   . SER A 1 235 ? 92.758  126.165 126.260 1.00 64.37  ? 235 SER A C   1 
ATOM   1764 O  O   . SER A 1 235 ? 92.633  125.027 126.725 1.00 67.14  ? 235 SER A O   1 
ATOM   1765 C  CB  . SER A 1 235 ? 90.706  127.126 127.304 1.00 63.32  ? 235 SER A CB  1 
ATOM   1766 O  OG  . SER A 1 235 ? 89.923  127.486 126.180 1.00 67.19  ? 235 SER A OG  1 
ATOM   1767 N  N   . GLU A 1 236 ? 93.371  126.397 125.097 1.00 58.87  ? 236 GLU A N   1 
ATOM   1768 C  CA  . GLU A 1 236 ? 93.942  125.327 124.288 1.00 57.51  ? 236 GLU A CA  1 
ATOM   1769 C  C   . GLU A 1 236 ? 95.443  125.499 124.083 1.00 57.81  ? 236 GLU A C   1 
ATOM   1770 O  O   . GLU A 1 236 ? 96.004  124.936 123.138 1.00 62.03  ? 236 GLU A O   1 
ATOM   1771 C  CB  . GLU A 1 236 ? 93.231  125.242 122.936 1.00 56.86  ? 236 GLU A CB  1 
ATOM   1772 C  CG  . GLU A 1 236 ? 91.794  124.770 123.024 1.00 59.13  ? 236 GLU A CG  1 
ATOM   1773 C  CD  . GLU A 1 236 ? 91.001  125.092 121.776 1.00 66.20  ? 236 GLU A CD  1 
ATOM   1774 O  OE1 . GLU A 1 236 ? 91.562  125.731 120.862 1.00 66.32  ? 236 GLU A OE1 1 
ATOM   1775 O  OE2 . GLU A 1 236 ? 89.815  124.707 121.710 1.00 67.05  ? 236 GLU A OE2 1 
ATOM   1776 N  N   . VAL A 1 237 ? 96.106  126.271 124.945 1.00 43.14  ? 237 VAL A N   1 
ATOM   1777 C  CA  . VAL A 1 237 ? 97.544  126.473 124.807 1.00 45.17  ? 237 VAL A CA  1 
ATOM   1778 C  C   . VAL A 1 237 ? 98.303  125.198 125.154 1.00 46.02  ? 237 VAL A C   1 
ATOM   1779 O  O   . VAL A 1 237 ? 99.255  124.814 124.462 1.00 45.43  ? 237 VAL A O   1 
ATOM   1780 C  CB  . VAL A 1 237 ? 97.996  127.660 125.677 1.00 45.04  ? 237 VAL A CB  1 
ATOM   1781 C  CG1 . VAL A 1 237 ? 99.509  127.765 125.697 1.00 46.52  ? 237 VAL A CG1 1 
ATOM   1782 C  CG2 . VAL A 1 237 ? 97.376  128.950 125.173 1.00 43.50  ? 237 VAL A CG2 1 
ATOM   1783 N  N   . TYR A 1 238 ? 97.890  124.516 126.225 1.00 43.54  ? 238 TYR A N   1 
ATOM   1784 C  CA  . TYR A 1 238 ? 98.635  123.354 126.699 1.00 36.31  ? 238 TYR A CA  1 
ATOM   1785 C  C   . TYR A 1 238 ? 98.493  122.169 125.752 1.00 38.98  ? 238 TYR A C   1 
ATOM   1786 O  O   . TYR A 1 238 ? 99.453  121.421 125.546 1.00 45.63  ? 238 TYR A O   1 
ATOM   1787 C  CB  . TYR A 1 238 ? 98.180  122.987 128.109 1.00 40.16  ? 238 TYR A CB  1 
ATOM   1788 C  CG  . TYR A 1 238 ? 98.491  124.058 129.126 1.00 45.33  ? 238 TYR A CG  1 
ATOM   1789 C  CD1 . TYR A 1 238 ? 99.763  124.605 129.217 1.00 44.67  ? 238 TYR A CD1 1 
ATOM   1790 C  CD2 . TYR A 1 238 ? 97.511  124.533 129.985 1.00 45.67  ? 238 TYR A CD2 1 
ATOM   1791 C  CE1 . TYR A 1 238 ? 100.053 125.589 130.140 1.00 41.46  ? 238 TYR A CE1 1 
ATOM   1792 C  CE2 . TYR A 1 238 ? 97.792  125.517 130.912 1.00 46.31  ? 238 TYR A CE2 1 
ATOM   1793 C  CZ  . TYR A 1 238 ? 99.064  126.042 130.985 1.00 46.92  ? 238 TYR A CZ  1 
ATOM   1794 O  OH  . TYR A 1 238 ? 99.348  127.022 131.907 1.00 52.49  ? 238 TYR A OH  1 
ATOM   1795 N  N   . SER A 1 239 ? 97.309  121.978 125.165 1.00 37.03  ? 239 SER A N   1 
ATOM   1796 C  CA  . SER A 1 239 ? 97.146  120.920 124.170 1.00 36.16  ? 239 SER A CA  1 
ATOM   1797 C  C   . SER A 1 239 ? 97.998  121.191 122.936 1.00 38.59  ? 239 SER A C   1 
ATOM   1798 O  O   . SER A 1 239 ? 98.616  120.272 122.379 1.00 42.22  ? 239 SER A O   1 
ATOM   1799 C  CB  . SER A 1 239 ? 95.673  120.786 123.786 1.00 36.59  ? 239 SER A CB  1 
ATOM   1800 O  OG  . SER A 1 239 ? 94.931  120.167 124.820 1.00 45.86  ? 239 SER A OG  1 
ATOM   1801 N  N   . TRP A 1 240 ? 98.040  122.451 122.497 1.00 30.05  ? 240 TRP A N   1 
ATOM   1802 C  CA  . TRP A 1 240 ? 98.892  122.832 121.377 1.00 30.12  ? 240 TRP A CA  1 
ATOM   1803 C  C   . TRP A 1 240 ? 100.355 122.534 121.677 1.00 32.78  ? 240 TRP A C   1 
ATOM   1804 O  O   . TRP A 1 240 ? 101.068 121.964 120.841 1.00 31.57  ? 240 TRP A O   1 
ATOM   1805 C  CB  . TRP A 1 240 ? 98.691  124.319 121.071 1.00 27.25  ? 240 TRP A CB  1 
ATOM   1806 C  CG  . TRP A 1 240 ? 99.209  124.771 119.740 1.00 30.17  ? 240 TRP A CG  1 
ATOM   1807 C  CD1 . TRP A 1 240 ? 98.487  124.944 118.599 1.00 26.13  ? 240 TRP A CD1 1 
ATOM   1808 C  CD2 . TRP A 1 240 ? 100.559 125.128 119.418 1.00 33.43  ? 240 TRP A CD2 1 
ATOM   1809 N  NE1 . TRP A 1 240 ? 99.301  125.377 117.584 1.00 28.57  ? 240 TRP A NE1 1 
ATOM   1810 C  CE2 . TRP A 1 240 ? 100.579 125.498 118.062 1.00 31.34  ? 240 TRP A CE2 1 
ATOM   1811 C  CE3 . TRP A 1 240 ? 101.753 125.166 120.145 1.00 32.01  ? 240 TRP A CE3 1 
ATOM   1812 C  CZ2 . TRP A 1 240 ? 101.744 125.898 117.416 1.00 29.03  ? 240 TRP A CZ2 1 
ATOM   1813 C  CZ3 . TRP A 1 240 ? 102.907 125.564 119.502 1.00 30.18  ? 240 TRP A CZ3 1 
ATOM   1814 C  CH2 . TRP A 1 240 ? 102.895 125.924 118.151 1.00 24.81  ? 240 TRP A CH2 1 
ATOM   1815 N  N   . LEU A 1 241 ? 100.815 122.900 122.877 1.00 31.75  ? 241 LEU A N   1 
ATOM   1816 C  CA  . LEU A 1 241 ? 102.202 122.643 123.249 1.00 28.58  ? 241 LEU A CA  1 
ATOM   1817 C  C   . LEU A 1 241 ? 102.487 121.150 123.336 1.00 32.27  ? 241 LEU A C   1 
ATOM   1818 O  O   . LEU A 1 241 ? 103.568 120.696 122.949 1.00 38.14  ? 241 LEU A O   1 
ATOM   1819 C  CB  . LEU A 1 241 ? 102.526 123.331 124.573 1.00 28.17  ? 241 LEU A CB  1 
ATOM   1820 C  CG  . LEU A 1 241 ? 102.847 124.823 124.487 1.00 31.52  ? 241 LEU A CG  1 
ATOM   1821 C  CD1 . LEU A 1 241 ? 102.833 125.454 125.867 1.00 34.70  ? 241 LEU A CD1 1 
ATOM   1822 C  CD2 . LEU A 1 241 ? 104.187 125.043 123.810 1.00 31.19  ? 241 LEU A CD2 1 
ATOM   1823 N  N   . ASP A 1 242 ? 101.533 120.372 123.851 1.00 29.75  ? 242 ASP A N   1 
ATOM   1824 C  CA  . ASP A 1 242 ? 101.713 118.928 123.956 1.00 32.00  ? 242 ASP A CA  1 
ATOM   1825 C  C   . ASP A 1 242 ? 101.874 118.293 122.577 1.00 30.49  ? 242 ASP A C   1 
ATOM   1826 O  O   . ASP A 1 242 ? 102.790 117.491 122.348 1.00 30.02  ? 242 ASP A O   1 
ATOM   1827 C  CB  . ASP A 1 242 ? 100.522 118.330 124.708 1.00 35.24  ? 242 ASP A CB  1 
ATOM   1828 C  CG  . ASP A 1 242 ? 100.732 116.882 125.094 1.00 40.30  ? 242 ASP A CG  1 
ATOM   1829 O  OD1 . ASP A 1 242 ? 101.601 116.616 125.948 1.00 41.01  ? 242 ASP A OD1 1 
ATOM   1830 O  OD2 . ASP A 1 242 ? 100.011 116.012 124.564 1.00 42.81  ? 242 ASP A OD2 1 
ATOM   1831 N  N   . SER A 1 243 ? 101.001 118.665 121.634 1.00 31.84  ? 243 SER A N   1 
ATOM   1832 C  CA  . SER A 1 243 ? 101.111 118.137 120.276 1.00 26.95  ? 243 SER A CA  1 
ATOM   1833 C  C   . SER A 1 243 ? 102.417 118.565 119.615 1.00 33.60  ? 243 SER A C   1 
ATOM   1834 O  O   . SER A 1 243 ? 103.083 117.759 118.947 1.00 37.79  ? 243 SER A O   1 
ATOM   1835 C  CB  . SER A 1 243 ? 99.918  118.595 119.438 1.00 26.72  ? 243 SER A CB  1 
ATOM   1836 O  OG  . SER A 1 243 ? 98.737  117.911 119.810 1.00 41.52  ? 243 SER A OG  1 
ATOM   1837 N  N   . PHE A 1 244 ? 102.798 119.834 119.786 1.00 30.73  ? 244 PHE A N   1 
ATOM   1838 C  CA  . PHE A 1 244 ? 104.027 120.319 119.171 1.00 25.65  ? 244 PHE A CA  1 
ATOM   1839 C  C   . PHE A 1 244 ? 105.248 119.605 119.734 1.00 27.45  ? 244 PHE A C   1 
ATOM   1840 O  O   . PHE A 1 244 ? 106.167 119.257 118.986 1.00 25.18  ? 244 PHE A O   1 
ATOM   1841 C  CB  . PHE A 1 244 ? 104.154 121.827 119.367 1.00 27.90  ? 244 PHE A CB  1 
ATOM   1842 C  CG  . PHE A 1 244 ? 105.337 122.423 118.670 1.00 31.76  ? 244 PHE A CG  1 
ATOM   1843 C  CD1 . PHE A 1 244 ? 105.308 122.653 117.307 1.00 31.90  ? 244 PHE A CD1 1 
ATOM   1844 C  CD2 . PHE A 1 244 ? 106.484 122.741 119.375 1.00 31.17  ? 244 PHE A CD2 1 
ATOM   1845 C  CE1 . PHE A 1 244 ? 106.397 123.197 116.663 1.00 36.66  ? 244 PHE A CE1 1 
ATOM   1846 C  CE2 . PHE A 1 244 ? 107.576 123.283 118.735 1.00 26.14  ? 244 PHE A CE2 1 
ATOM   1847 C  CZ  . PHE A 1 244 ? 107.531 123.511 117.378 1.00 27.51  ? 244 PHE A CZ  1 
ATOM   1848 N  N   . LEU A 1 245 ? 105.281 119.388 121.050 1.00 29.73  ? 245 LEU A N   1 
ATOM   1849 C  CA  . LEU A 1 245 ? 106.402 118.677 121.651 1.00 24.45  ? 245 LEU A CA  1 
ATOM   1850 C  C   . LEU A 1 245 ? 106.458 117.238 121.167 1.00 22.24  ? 245 LEU A C   1 
ATOM   1851 O  O   . LEU A 1 245 ? 107.545 116.702 120.928 1.00 23.09  ? 245 LEU A O   1 
ATOM   1852 C  CB  . LEU A 1 245 ? 106.310 118.732 123.174 1.00 21.11  ? 245 LEU A CB  1 
ATOM   1853 C  CG  . LEU A 1 245 ? 106.785 120.035 123.814 1.00 24.78  ? 245 LEU A CG  1 
ATOM   1854 C  CD1 . LEU A 1 245 ? 106.762 119.923 125.326 1.00 34.31  ? 245 LEU A CD1 1 
ATOM   1855 C  CD2 . LEU A 1 245 ? 108.172 120.400 123.319 1.00 27.13  ? 245 LEU A CD2 1 
ATOM   1856 N  N   . LEU A 1 246 ? 105.284 116.629 120.984 1.00 24.69  ? 246 LEU A N   1 
ATOM   1857 C  CA  . LEU A 1 246 ? 105.232 115.246 120.440 1.00 27.45  ? 246 LEU A CA  1 
ATOM   1858 C  C   . LEU A 1 246 ? 105.893 115.232 119.059 1.00 26.90  ? 246 LEU A C   1 
ATOM   1859 O  O   . LEU A 1 246 ? 106.748 114.356 118.826 1.00 23.89  ? 246 LEU A O   1 
ATOM   1860 C  CB  . LEU A 1 246 ? 103.768 114.806 120.349 1.00 31.11  ? 246 LEU A CB  1 
ATOM   1861 C  CG  . LEU A 1 246 ? 103.515 113.529 119.549 1.00 27.72  ? 246 LEU A CG  1 
ATOM   1862 C  CD1 . LEU A 1 246 ? 103.804 112.294 120.388 1.00 32.24  ? 246 LEU A CD1 1 
ATOM   1863 C  CD2 . LEU A 1 246 ? 102.090 113.494 119.019 1.00 28.56  ? 246 LEU A CD2 1 
ATOM   1864 N  N   . LEU A 1 247 ? 105.516 116.172 118.184 1.00 28.62  ? 247 LEU A N   1 
ATOM   1865 C  CA  . LEU A 1 247 ? 106.067 116.201 116.829 1.00 21.44  ? 247 LEU A CA  1 
ATOM   1866 C  C   . LEU A 1 247 ? 107.555 116.541 116.824 1.00 29.78  ? 247 LEU A C   1 
ATOM   1867 O  O   . LEU A 1 247 ? 108.308 116.032 115.986 1.00 31.01  ? 247 LEU A O   1 
ATOM   1868 C  CB  . LEU A 1 247 ? 105.298 117.191 115.957 1.00 25.78  ? 247 LEU A CB  1 
ATOM   1869 C  CG  . LEU A 1 247 ? 103.984 116.700 115.351 1.00 32.44  ? 247 LEU A CG  1 
ATOM   1870 C  CD1 . LEU A 1 247 ? 103.166 117.871 114.851 1.00 26.44  ? 247 LEU A CD1 1 
ATOM   1871 C  CD2 . LEU A 1 247 ? 104.250 115.715 114.227 1.00 26.35  ? 247 LEU A CD2 1 
ATOM   1872 N  N   . MET A 1 248 ? 108.000 117.409 117.737 1.00 33.99  ? 248 MET A N   1 
ATOM   1873 C  CA  . MET A 1 248 ? 109.371 117.906 117.668 1.00 26.02  ? 248 MET A CA  1 
ATOM   1874 C  C   . MET A 1 248 ? 110.365 116.941 118.308 1.00 26.89  ? 248 MET A C   1 
ATOM   1875 O  O   . MET A 1 248 ? 111.461 116.735 117.777 1.00 28.49  ? 248 MET A O   1 
ATOM   1876 C  CB  . MET A 1 248 ? 109.460 119.284 118.323 1.00 27.07  ? 248 MET A CB  1 
ATOM   1877 C  CG  . MET A 1 248 ? 110.874 119.735 118.642 1.00 26.29  ? 248 MET A CG  1 
ATOM   1878 S  SD  . MET A 1 248 ? 110.994 121.509 118.927 1.00 38.53  ? 248 MET A SD  1 
ATOM   1879 C  CE  . MET A 1 248 ? 111.339 121.547 120.682 1.00 31.13  ? 248 MET A CE  1 
ATOM   1880 N  N   . LEU A 1 249 ? 110.016 116.343 119.446 1.00 33.17  ? 249 LEU A N   1 
ATOM   1881 C  CA  . LEU A 1 249 ? 110.946 115.465 120.144 1.00 23.33  ? 249 LEU A CA  1 
ATOM   1882 C  C   . LEU A 1 249 ? 110.756 113.991 119.818 1.00 26.94  ? 249 LEU A C   1 
ATOM   1883 O  O   . LEU A 1 249 ? 111.699 113.212 119.980 1.00 36.31  ? 249 LEU A O   1 
ATOM   1884 C  CB  . LEU A 1 249 ? 110.831 115.662 121.660 1.00 22.42  ? 249 LEU A CB  1 
ATOM   1885 C  CG  . LEU A 1 249 ? 111.154 117.059 122.194 1.00 22.21  ? 249 LEU A CG  1 
ATOM   1886 C  CD1 . LEU A 1 249 ? 110.692 117.208 123.633 1.00 24.93  ? 249 LEU A CD1 1 
ATOM   1887 C  CD2 . LEU A 1 249 ? 112.638 117.353 122.075 1.00 24.94  ? 249 LEU A CD2 1 
ATOM   1888 N  N   . GLY A 1 250 ? 109.573 113.581 119.361 1.00 13.69  ? 250 GLY A N   1 
ATOM   1889 C  CA  . GLY A 1 250 ? 109.363 112.196 119.011 1.00 16.13  ? 250 GLY A CA  1 
ATOM   1890 C  C   . GLY A 1 250 ? 109.787 111.805 117.618 1.00 29.19  ? 250 GLY A C   1 
ATOM   1891 O  O   . GLY A 1 250 ? 109.652 110.636 117.249 1.00 36.37  ? 250 GLY A O   1 
ATOM   1892 N  N   . GLY A 1 251 ? 110.294 112.748 116.825 1.00 22.57  ? 251 GLY A N   1 
ATOM   1893 C  CA  . GLY A 1 251 ? 110.750 112.454 115.482 1.00 18.01  ? 251 GLY A CA  1 
ATOM   1894 C  C   . GLY A 1 251 ? 112.207 112.081 115.352 1.00 30.33  ? 251 GLY A C   1 
ATOM   1895 O  O   . GLY A 1 251 ? 112.636 111.664 114.274 1.00 36.93  ? 251 GLY A O   1 
ATOM   1896 N  N   . ILE A 1 252 ? 112.983 112.223 116.422 1.00 20.33  ? 252 ILE A N   1 
ATOM   1897 C  CA  . ILE A 1 252 ? 114.412 111.916 116.404 1.00 12.32  ? 252 ILE A CA  1 
ATOM   1898 C  C   . ILE A 1 252 ? 114.667 110.413 116.505 1.00 20.35  ? 252 ILE A C   1 
ATOM   1899 O  O   . ILE A 1 252 ? 115.366 109.863 115.643 1.00 19.81  ? 252 ILE A O   1 
ATOM   1900 C  CB  . ILE A 1 252 ? 115.151 112.677 117.518 1.00 19.60  ? 252 ILE A CB  1 
ATOM   1901 C  CG1 . ILE A 1 252 ? 114.929 114.184 117.376 1.00 18.47  ? 252 ILE A CG1 1 
ATOM   1902 C  CG2 . ILE A 1 252 ? 116.633 112.345 117.501 1.00 11.56  ? 252 ILE A CG2 1 
ATOM   1903 C  CD1 . ILE A 1 252 ? 115.540 114.999 118.493 1.00 19.06  ? 252 ILE A CD1 1 
ATOM   1904 N  N   . PRO A 1 253 ? 114.136 109.693 117.519 1.00 30.10  ? 253 PRO A N   1 
ATOM   1905 C  CA  . PRO A 1 253 ? 114.597 108.297 117.691 1.00 21.54  ? 253 PRO A CA  1 
ATOM   1906 C  C   . PRO A 1 253 ? 113.942 107.318 116.722 1.00 20.76  ? 253 PRO A C   1 
ATOM   1907 O  O   . PRO A 1 253 ? 113.169 106.429 117.091 1.00 21.61  ? 253 PRO A O   1 
ATOM   1908 C  CB  . PRO A 1 253 ? 114.230 108.015 119.150 1.00 14.16  ? 253 PRO A CB  1 
ATOM   1909 C  CG  . PRO A 1 253 ? 112.997 108.800 119.360 1.00 13.58  ? 253 PRO A CG  1 
ATOM   1910 C  CD  . PRO A 1 253 ? 113.159 110.064 118.562 1.00 20.71  ? 253 PRO A CD  1 
ATOM   1911 N  N   . TRP A 1 254 ? 114.270 107.463 115.441 1.00 15.42  ? 254 TRP A N   1 
ATOM   1912 C  CA  . TRP A 1 254 ? 113.763 106.588 114.395 1.00 9.71   ? 254 TRP A CA  1 
ATOM   1913 C  C   . TRP A 1 254 ? 114.925 106.035 113.588 1.00 17.73  ? 254 TRP A C   1 
ATOM   1914 O  O   . TRP A 1 254 ? 115.877 106.757 113.281 1.00 31.10  ? 254 TRP A O   1 
ATOM   1915 C  CB  . TRP A 1 254 ? 112.788 107.329 113.473 1.00 10.04  ? 254 TRP A CB  1 
ATOM   1916 C  CG  . TRP A 1 254 ? 111.485 107.657 114.128 1.00 19.64  ? 254 TRP A CG  1 
ATOM   1917 C  CD1 . TRP A 1 254 ? 111.260 108.619 115.067 1.00 15.37  ? 254 TRP A CD1 1 
ATOM   1918 C  CD2 . TRP A 1 254 ? 110.224 107.018 113.900 1.00 24.74  ? 254 TRP A CD2 1 
ATOM   1919 N  NE1 . TRP A 1 254 ? 109.940 108.620 115.437 1.00 25.34  ? 254 TRP A NE1 1 
ATOM   1920 C  CE2 . TRP A 1 254 ? 109.282 107.646 114.734 1.00 25.03  ? 254 TRP A CE2 1 
ATOM   1921 C  CE3 . TRP A 1 254 ? 109.802 105.976 113.070 1.00 15.42  ? 254 TRP A CE3 1 
ATOM   1922 C  CZ2 . TRP A 1 254 ? 107.944 107.268 114.763 1.00 16.22  ? 254 TRP A CZ2 1 
ATOM   1923 C  CZ3 . TRP A 1 254 ? 108.475 105.604 113.101 1.00 18.25  ? 254 TRP A CZ3 1 
ATOM   1924 C  CH2 . TRP A 1 254 ? 107.561 106.248 113.941 1.00 15.45  ? 254 TRP A CH2 1 
ATOM   1925 N  N   . GLN A 1 255 ? 114.845 104.747 113.249 1.00 24.08  ? 255 GLN A N   1 
ATOM   1926 C  CA  . GLN A 1 255 ? 115.882 104.123 112.436 1.00 16.24  ? 255 GLN A CA  1 
ATOM   1927 C  C   . GLN A 1 255 ? 115.852 104.619 110.995 1.00 19.76  ? 255 GLN A C   1 
ATOM   1928 O  O   . GLN A 1 255 ? 116.874 104.551 110.307 1.00 16.70  ? 255 GLN A O   1 
ATOM   1929 C  CB  . GLN A 1 255 ? 115.738 102.597 112.501 1.00 18.51  ? 255 GLN A CB  1 
ATOM   1930 C  CG  . GLN A 1 255 ? 116.555 101.803 111.486 1.00 21.80  ? 255 GLN A CG  1 
ATOM   1931 C  CD  . GLN A 1 255 ? 118.022 101.706 111.846 1.00 33.04  ? 255 GLN A CD  1 
ATOM   1932 O  OE1 . GLN A 1 255 ? 118.436 102.117 112.927 1.00 41.44  ? 255 GLN A OE1 1 
ATOM   1933 N  NE2 . GLN A 1 255 ? 118.819 101.160 110.937 1.00 17.58  ? 255 GLN A NE2 1 
ATOM   1934 N  N   . ALA A 1 256 ? 114.717 105.148 110.532 1.00 21.27  ? 256 ALA A N   1 
ATOM   1935 C  CA  . ALA A 1 256 ? 114.659 105.746 109.204 1.00 16.85  ? 256 ALA A CA  1 
ATOM   1936 C  C   . ALA A 1 256 ? 115.526 106.994 109.089 1.00 25.76  ? 256 ALA A C   1 
ATOM   1937 O  O   . ALA A 1 256 ? 115.878 107.388 107.973 1.00 27.04  ? 256 ALA A O   1 
ATOM   1938 C  CB  . ALA A 1 256 ? 113.212 106.078 108.841 1.00 14.76  ? 256 ALA A CB  1 
ATOM   1939 N  N   . TYR A 1 257 ? 115.870 107.625 110.212 1.00 15.91  ? 257 TYR A N   1 
ATOM   1940 C  CA  . TYR A 1 257 ? 116.775 108.767 110.245 1.00 16.67  ? 257 TYR A CA  1 
ATOM   1941 C  C   . TYR A 1 257 ? 118.226 108.340 110.451 1.00 18.07  ? 257 TYR A C   1 
ATOM   1942 O  O   . TYR A 1 257 ? 119.131 108.814 109.749 1.00 16.80  ? 257 TYR A O   1 
ATOM   1943 C  CB  . TYR A 1 257 ? 116.337 109.733 111.353 1.00 12.26  ? 257 TYR A CB  1 
ATOM   1944 C  CG  . TYR A 1 257 ? 117.303 110.859 111.639 1.00 17.64  ? 257 TYR A CG  1 
ATOM   1945 C  CD1 . TYR A 1 257 ? 117.609 111.802 110.669 1.00 13.19  ? 257 TYR A CD1 1 
ATOM   1946 C  CD2 . TYR A 1 257 ? 117.904 110.983 112.883 1.00 11.75  ? 257 TYR A CD2 1 
ATOM   1947 C  CE1 . TYR A 1 257 ? 118.487 112.831 110.928 1.00 13.87  ? 257 TYR A CE1 1 
ATOM   1948 C  CE2 . TYR A 1 257 ? 118.785 112.009 113.150 1.00 16.35  ? 257 TYR A CE2 1 
ATOM   1949 C  CZ  . TYR A 1 257 ? 119.071 112.930 112.169 1.00 19.07  ? 257 TYR A CZ  1 
ATOM   1950 O  OH  . TYR A 1 257 ? 119.948 113.954 112.429 1.00 18.54  ? 257 TYR A OH  1 
ATOM   1951 N  N   . PHE A 1 258 ? 118.468 107.432 111.396 1.00 9.43   ? 258 PHE A N   1 
ATOM   1952 C  CA  . PHE A 1 258 ? 119.826 106.977 111.649 1.00 13.97  ? 258 PHE A CA  1 
ATOM   1953 C  C   . PHE A 1 258 ? 120.366 106.111 110.520 1.00 18.45  ? 258 PHE A C   1 
ATOM   1954 O  O   . PHE A 1 258 ? 121.584 105.948 110.416 1.00 19.34  ? 258 PHE A O   1 
ATOM   1955 C  CB  . PHE A 1 258 ? 119.885 106.227 112.978 1.00 18.05  ? 258 PHE A CB  1 
ATOM   1956 C  CG  . PHE A 1 258 ? 119.764 107.122 114.176 1.00 21.24  ? 258 PHE A CG  1 
ATOM   1957 C  CD1 . PHE A 1 258 ? 120.796 107.973 114.528 1.00 25.92  ? 258 PHE A CD1 1 
ATOM   1958 C  CD2 . PHE A 1 258 ? 118.613 107.123 114.944 1.00 16.25  ? 258 PHE A CD2 1 
ATOM   1959 C  CE1 . PHE A 1 258 ? 120.686 108.802 115.627 1.00 24.07  ? 258 PHE A CE1 1 
ATOM   1960 C  CE2 . PHE A 1 258 ? 118.498 107.950 116.044 1.00 14.06  ? 258 PHE A CE2 1 
ATOM   1961 C  CZ  . PHE A 1 258 ? 119.536 108.789 116.385 1.00 17.04  ? 258 PHE A CZ  1 
ATOM   1962 N  N   . GLN A 1 259 ? 119.497 105.563 109.668 1.00 18.22  ? 259 GLN A N   1 
ATOM   1963 C  CA  . GLN A 1 259 ? 119.973 104.857 108.484 1.00 21.02  ? 259 GLN A CA  1 
ATOM   1964 C  C   . GLN A 1 259 ? 120.696 105.807 107.538 1.00 23.82  ? 259 GLN A C   1 
ATOM   1965 O  O   . GLN A 1 259 ? 121.724 105.451 106.952 1.00 25.89  ? 259 GLN A O   1 
ATOM   1966 C  CB  . GLN A 1 259 ? 118.804 104.175 107.776 1.00 17.25  ? 259 GLN A CB  1 
ATOM   1967 C  CG  . GLN A 1 259 ? 119.211 103.259 106.633 1.00 23.93  ? 259 GLN A CG  1 
ATOM   1968 C  CD  . GLN A 1 259 ? 118.809 101.818 106.870 1.00 31.08  ? 259 GLN A CD  1 
ATOM   1969 O  OE1 . GLN A 1 259 ? 117.818 101.541 107.542 1.00 33.42  ? 259 GLN A OE1 1 
ATOM   1970 N  NE2 . GLN A 1 259 ? 119.577 100.890 106.315 1.00 24.87  ? 259 GLN A NE2 1 
ATOM   1971 N  N   . ARG A 1 260 ? 120.169 107.029 107.414 1.00 26.78  ? 260 ARG A N   1 
ATOM   1972 C  CA  . ARG A 1 260 ? 120.838 108.053 106.570 1.00 20.46  ? 260 ARG A CA  1 
ATOM   1973 C  C   . ARG A 1 260 ? 122.040 108.614 107.336 1.00 23.24  ? 260 ARG A C   1 
ATOM   1974 O  O   . ARG A 1 260 ? 123.068 108.897 106.690 1.00 24.39  ? 260 ARG A O   1 
ATOM   1975 C  CB  . ARG A 1 260 ? 119.869 109.183 106.207 1.00 9.13   ? 260 ARG A CB  1 
ATOM   1976 C  CG  . ARG A 1 260 ? 118.843 108.821 105.142 1.00 21.19  ? 260 ARG A CG  1 
ATOM   1977 C  CD  . ARG A 1 260 ? 117.725 107.938 105.659 1.00 21.58  ? 260 ARG A CD  1 
ATOM   1978 N  NE  . ARG A 1 260 ? 116.684 107.730 104.662 1.00 22.68  ? 260 ARG A NE  1 
ATOM   1979 C  CZ  . ARG A 1 260 ? 116.320 106.542 104.194 1.00 29.74  ? 260 ARG A CZ  1 
ATOM   1980 N  NH1 . ARG A 1 260 ? 116.791 105.440 104.749 1.00 29.19  ? 260 ARG A NH1 1 
ATOM   1981 N  NH2 . ARG A 1 260 ? 115.485 106.461 103.172 1.00 27.61  ? 260 ARG A NH2 1 
ATOM   1982 N  N   . VAL A 1 261 ? 121.914 108.765 108.659 1.00 25.18  ? 261 VAL A N   1 
ATOM   1983 C  CA  . VAL A 1 261 ? 122.999 109.353 109.445 1.00 18.43  ? 261 VAL A CA  1 
ATOM   1984 C  C   . VAL A 1 261 ? 124.242 108.467 109.400 1.00 21.17  ? 261 VAL A C   1 
ATOM   1985 O  O   . VAL A 1 261 ? 125.360 108.948 109.181 1.00 24.29  ? 261 VAL A O   1 
ATOM   1986 C  CB  . VAL A 1 261 ? 122.538 109.608 110.891 1.00 13.38  ? 261 VAL A CB  1 
ATOM   1987 C  CG1 . VAL A 1 261 ? 123.731 109.650 111.830 1.00 10.32  ? 261 VAL A CG1 1 
ATOM   1988 C  CG2 . VAL A 1 261 ? 121.755 110.898 110.968 1.00 12.57  ? 261 VAL A CG2 1 
ATOM   1989 N  N   . LEU A 1 262 ? 124.068 107.159 109.594 1.00 23.91  ? 262 LEU A N   1 
ATOM   1990 C  CA  . LEU A 1 262 ? 125.197 106.248 109.743 1.00 19.22  ? 262 LEU A CA  1 
ATOM   1991 C  C   . LEU A 1 262 ? 125.831 105.838 108.420 1.00 21.93  ? 262 LEU A C   1 
ATOM   1992 O  O   . LEU A 1 262 ? 126.874 105.177 108.435 1.00 29.30  ? 262 LEU A O   1 
ATOM   1993 C  CB  . LEU A 1 262 ? 124.764 104.993 110.505 1.00 14.38  ? 262 LEU A CB  1 
ATOM   1994 C  CG  . LEU A 1 262 ? 124.285 105.171 111.947 1.00 14.43  ? 262 LEU A CG  1 
ATOM   1995 C  CD1 . LEU A 1 262 ? 123.490 103.962 112.403 1.00 8.96   ? 262 LEU A CD1 1 
ATOM   1996 C  CD2 . LEU A 1 262 ? 125.453 105.422 112.879 1.00 17.03  ? 262 LEU A CD2 1 
ATOM   1997 N  N   . SER A 1 263 ? 125.238 106.200 107.286 1.00 22.69  ? 263 SER A N   1 
ATOM   1998 C  CA  . SER A 1 263 ? 125.779 105.851 105.981 1.00 16.41  ? 263 SER A CA  1 
ATOM   1999 C  C   . SER A 1 263 ? 126.624 106.959 105.368 1.00 24.86  ? 263 SER A C   1 
ATOM   2000 O  O   . SER A 1 263 ? 127.111 106.797 104.247 1.00 25.19  ? 263 SER A O   1 
ATOM   2001 C  CB  . SER A 1 263 ? 124.642 105.489 105.023 1.00 19.37  ? 263 SER A CB  1 
ATOM   2002 O  OG  . SER A 1 263 ? 123.630 104.762 105.691 1.00 27.33  ? 263 SER A OG  1 
ATOM   2003 N  N   . SER A 1 264 ? 126.760 108.073 106.093 1.00 24.97  ? 264 SER A N   1 
ATOM   2004 C  CA  . SER A 1 264 ? 127.485 109.251 105.549 1.00 17.23  ? 264 SER A CA  1 
ATOM   2005 C  C   . SER A 1 264 ? 128.999 109.037 105.588 1.00 26.51  ? 264 SER A C   1 
ATOM   2006 O  O   . SER A 1 264 ? 129.455 108.147 106.333 1.00 32.29  ? 264 SER A O   1 
ATOM   2007 C  CB  . SER A 1 264 ? 127.097 110.503 106.296 1.00 19.52  ? 264 SER A CB  1 
ATOM   2008 O  OG  . SER A 1 264 ? 127.842 111.619 105.830 1.00 31.54  ? 264 SER A OG  1 
ATOM   2009 N  N   . SER A 1 265 ? 129.752 109.820 104.825 1.00 22.65  ? 265 SER A N   1 
ATOM   2010 C  CA  . SER A 1 265 ? 131.204 109.703 104.829 1.00 24.76  ? 265 SER A CA  1 
ATOM   2011 C  C   . SER A 1 265 ? 131.787 110.202 106.147 1.00 33.67  ? 265 SER A C   1 
ATOM   2012 O  O   . SER A 1 265 ? 132.758 109.632 106.646 1.00 38.85  ? 265 SER A O   1 
ATOM   2013 C  CB  . SER A 1 265 ? 131.797 110.486 103.658 1.00 30.17  ? 265 SER A CB  1 
ATOM   2014 O  OG  . SER A 1 265 ? 131.228 110.067 102.429 1.00 35.37  ? 265 SER A OG  1 
ATOM   2015 N  N   . SER A 1 266 ? 131.200 111.253 106.717 1.00 29.70  ? 266 SER A N   1 
ATOM   2016 C  CA  . SER A 1 266 ? 131.727 111.822 107.949 1.00 21.00  ? 266 SER A CA  1 
ATOM   2017 C  C   . SER A 1 266 ? 130.569 112.266 108.830 1.00 34.13  ? 266 SER A C   1 
ATOM   2018 O  O   . SER A 1 266 ? 129.402 112.207 108.436 1.00 44.74  ? 266 SER A O   1 
ATOM   2019 C  CB  . SER A 1 266 ? 132.672 112.992 107.663 1.00 29.24  ? 266 SER A CB  1 
ATOM   2020 O  OG  . SER A 1 266 ? 133.902 112.533 107.136 1.00 39.19  ? 266 SER A OG  1 
ATOM   2021 N  N   . ALA A 1 267 ? 130.908 112.709 110.043 1.00 26.65  ? 267 ALA A N   1 
ATOM   2022 C  CA  . ALA A 1 267 ? 129.893 113.214 110.964 1.00 32.68  ? 267 ALA A CA  1 
ATOM   2023 C  C   . ALA A 1 267 ? 129.420 114.608 110.565 1.00 42.03  ? 267 ALA A C   1 
ATOM   2024 O  O   . ALA A 1 267 ? 128.224 114.922 110.667 1.00 48.44  ? 267 ALA A O   1 
ATOM   2025 C  CB  . ALA A 1 267 ? 130.442 113.216 112.389 1.00 31.54  ? 267 ALA A CB  1 
ATOM   2026 N  N   . THR A 1 268 ? 130.343 115.459 110.111 1.00 28.23  ? 268 THR A N   1 
ATOM   2027 C  CA  . THR A 1 268 ? 129.962 116.797 109.673 1.00 32.58  ? 268 THR A CA  1 
ATOM   2028 C  C   . THR A 1 268 ? 129.017 116.731 108.482 1.00 31.97  ? 268 THR A C   1 
ATOM   2029 O  O   . THR A 1 268 ? 128.097 117.549 108.359 1.00 39.34  ? 268 THR A O   1 
ATOM   2030 C  CB  . THR A 1 268 ? 131.207 117.616 109.331 1.00 33.19  ? 268 THR A CB  1 
ATOM   2031 O  OG1 . THR A 1 268 ? 131.557 117.410 107.958 1.00 42.66  ? 268 THR A OG1 1 
ATOM   2032 C  CG2 . THR A 1 268 ? 132.375 117.199 110.206 1.00 32.43  ? 268 THR A CG2 1 
ATOM   2033 N  N   . TYR A 1 269 ? 129.222 115.753 107.598 1.00 18.90  ? 269 TYR A N   1 
ATOM   2034 C  CA  . TYR A 1 269 ? 128.304 115.565 106.483 1.00 23.37  ? 269 TYR A CA  1 
ATOM   2035 C  C   . TYR A 1 269 ? 126.919 115.160 106.970 1.00 27.53  ? 269 TYR A C   1 
ATOM   2036 O  O   . TYR A 1 269 ? 125.910 115.580 106.396 1.00 29.87  ? 269 TYR A O   1 
ATOM   2037 C  CB  . TYR A 1 269 ? 128.866 114.533 105.509 1.00 26.63  ? 269 TYR A CB  1 
ATOM   2038 C  CG  . TYR A 1 269 ? 129.791 115.132 104.477 1.00 32.15  ? 269 TYR A CG  1 
ATOM   2039 C  CD1 . TYR A 1 269 ? 130.228 116.444 104.592 1.00 33.78  ? 269 TYR A CD1 1 
ATOM   2040 C  CD2 . TYR A 1 269 ? 130.218 114.394 103.385 1.00 33.11  ? 269 TYR A CD2 1 
ATOM   2041 C  CE1 . TYR A 1 269 ? 131.070 117.001 103.654 1.00 33.06  ? 269 TYR A CE1 1 
ATOM   2042 C  CE2 . TYR A 1 269 ? 131.060 114.943 102.440 1.00 38.19  ? 269 TYR A CE2 1 
ATOM   2043 C  CZ  . TYR A 1 269 ? 131.483 116.247 102.580 1.00 37.61  ? 269 TYR A CZ  1 
ATOM   2044 O  OH  . TYR A 1 269 ? 132.322 116.801 101.643 1.00 42.54  ? 269 TYR A OH  1 
ATOM   2045 N  N   . ALA A 1 270 ? 126.849 114.350 108.030 1.00 19.79  ? 270 ALA A N   1 
ATOM   2046 C  CA  . ALA A 1 270 ? 125.556 114.011 108.618 1.00 22.40  ? 270 ALA A CA  1 
ATOM   2047 C  C   . ALA A 1 270 ? 124.857 115.251 109.165 1.00 33.90  ? 270 ALA A C   1 
ATOM   2048 O  O   . ALA A 1 270 ? 123.650 115.445 108.953 1.00 36.18  ? 270 ALA A O   1 
ATOM   2049 C  CB  . ALA A 1 270 ? 125.743 112.968 109.718 1.00 15.57  ? 270 ALA A CB  1 
ATOM   2050 N  N   . GLN A 1 271 ? 125.607 116.108 109.860 1.00 28.31  ? 271 GLN A N   1 
ATOM   2051 C  CA  . GLN A 1 271 ? 125.052 117.365 110.356 1.00 17.86  ? 271 GLN A CA  1 
ATOM   2052 C  C   . GLN A 1 271 ? 124.481 118.207 109.216 1.00 26.21  ? 271 GLN A C   1 
ATOM   2053 O  O   . GLN A 1 271 ? 123.331 118.677 109.273 1.00 32.91  ? 271 GLN A O   1 
ATOM   2054 C  CB  . GLN A 1 271 ? 126.149 118.130 111.096 1.00 13.88  ? 271 GLN A CB  1 
ATOM   2055 C  CG  . GLN A 1 271 ? 125.677 119.100 112.151 1.00 34.25  ? 271 GLN A CG  1 
ATOM   2056 C  CD  . GLN A 1 271 ? 126.701 119.282 113.253 1.00 37.01  ? 271 GLN A CD  1 
ATOM   2057 O  OE1 . GLN A 1 271 ? 127.790 118.713 113.201 1.00 32.63  ? 271 GLN A OE1 1 
ATOM   2058 N  NE2 . GLN A 1 271 ? 126.358 120.080 114.256 1.00 35.80  ? 271 GLN A NE2 1 
ATOM   2059 N  N   . VAL A 1 272 ? 125.273 118.395 108.160 1.00 13.02  ? 272 VAL A N   1 
ATOM   2060 C  CA  . VAL A 1 272 ? 124.849 119.256 107.062 1.00 16.71  ? 272 VAL A CA  1 
ATOM   2061 C  C   . VAL A 1 272 ? 123.656 118.650 106.329 1.00 28.27  ? 272 VAL A C   1 
ATOM   2062 O  O   . VAL A 1 272 ? 122.759 119.373 105.880 1.00 34.92  ? 272 VAL A O   1 
ATOM   2063 C  CB  . VAL A 1 272 ? 126.029 119.537 106.113 1.00 18.62  ? 272 VAL A CB  1 
ATOM   2064 C  CG1 . VAL A 1 272 ? 125.600 120.463 104.991 1.00 23.96  ? 272 VAL A CG1 1 
ATOM   2065 C  CG2 . VAL A 1 272 ? 127.181 120.155 106.879 1.00 18.67  ? 272 VAL A CG2 1 
ATOM   2066 N  N   . LEU A 1 273 ? 123.617 117.321 106.198 1.00 18.16  ? 273 LEU A N   1 
ATOM   2067 C  CA  . LEU A 1 273 ? 122.480 116.695 105.530 1.00 17.42  ? 273 LEU A CA  1 
ATOM   2068 C  C   . LEU A 1 273 ? 121.206 116.853 106.351 1.00 27.29  ? 273 LEU A C   1 
ATOM   2069 O  O   . LEU A 1 273 ? 120.122 117.034 105.787 1.00 26.34  ? 273 LEU A O   1 
ATOM   2070 C  CB  . LEU A 1 273 ? 122.775 115.220 105.230 1.00 14.65  ? 273 LEU A CB  1 
ATOM   2071 C  CG  . LEU A 1 273 ? 122.573 114.074 106.229 1.00 22.19  ? 273 LEU A CG  1 
ATOM   2072 C  CD1 . LEU A 1 273 ? 121.134 113.578 106.266 1.00 26.61  ? 273 LEU A CD1 1 
ATOM   2073 C  CD2 . LEU A 1 273 ? 123.502 112.927 105.882 1.00 21.82  ? 273 LEU A CD2 1 
ATOM   2074 N  N   . SER A 1 274 ? 121.313 116.800 107.683 1.00 23.84  ? 274 SER A N   1 
ATOM   2075 C  CA  . SER A 1 274 ? 120.140 117.066 108.513 1.00 16.54  ? 274 SER A CA  1 
ATOM   2076 C  C   . SER A 1 274 ? 119.629 118.490 108.309 1.00 23.31  ? 274 SER A C   1 
ATOM   2077 O  O   . SER A 1 274 ? 118.414 118.716 108.185 1.00 28.55  ? 274 SER A O   1 
ATOM   2078 C  CB  . SER A 1 274 ? 120.467 116.820 109.984 1.00 12.49  ? 274 SER A CB  1 
ATOM   2079 O  OG  . SER A 1 274 ? 121.276 115.670 110.143 1.00 26.67  ? 274 SER A OG  1 
ATOM   2080 N  N   . PHE A 1 275 ? 120.542 119.465 108.259 1.00 23.26  ? 275 PHE A N   1 
ATOM   2081 C  CA  . PHE A 1 275 ? 120.117 120.846 108.025 1.00 20.87  ? 275 PHE A CA  1 
ATOM   2082 C  C   . PHE A 1 275 ? 119.447 121.005 106.658 1.00 22.85  ? 275 PHE A C   1 
ATOM   2083 O  O   . PHE A 1 275 ? 118.402 121.668 106.531 1.00 31.28  ? 275 PHE A O   1 
ATOM   2084 C  CB  . PHE A 1 275 ? 121.312 121.789 108.153 1.00 17.22  ? 275 PHE A CB  1 
ATOM   2085 C  CG  . PHE A 1 275 ? 121.964 121.761 109.507 1.00 19.95  ? 275 PHE A CG  1 
ATOM   2086 C  CD1 . PHE A 1 275 ? 121.223 121.486 110.643 1.00 13.83  ? 275 PHE A CD1 1 
ATOM   2087 C  CD2 . PHE A 1 275 ? 123.318 122.014 109.645 1.00 20.78  ? 275 PHE A CD2 1 
ATOM   2088 C  CE1 . PHE A 1 275 ? 121.819 121.461 111.885 1.00 17.14  ? 275 PHE A CE1 1 
ATOM   2089 C  CE2 . PHE A 1 275 ? 123.918 121.988 110.887 1.00 17.26  ? 275 PHE A CE2 1 
ATOM   2090 C  CZ  . PHE A 1 275 ? 123.167 121.711 112.008 1.00 17.43  ? 275 PHE A CZ  1 
ATOM   2091 N  N   . LEU A 1 276 ? 120.028 120.392 105.625 1.00 11.45  ? 276 LEU A N   1 
ATOM   2092 C  CA  . LEU A 1 276 ? 119.444 120.470 104.289 1.00 14.22  ? 276 LEU A CA  1 
ATOM   2093 C  C   . LEU A 1 276 ? 118.074 119.806 104.242 1.00 19.95  ? 276 LEU A C   1 
ATOM   2094 O  O   . LEU A 1 276 ? 117.169 120.285 103.550 1.00 21.58  ? 276 LEU A O   1 
ATOM   2095 C  CB  . LEU A 1 276 ? 120.384 119.832 103.268 1.00 19.61  ? 276 LEU A CB  1 
ATOM   2096 C  CG  . LEU A 1 276 ? 121.736 120.509 103.046 1.00 20.62  ? 276 LEU A CG  1 
ATOM   2097 C  CD1 . LEU A 1 276 ? 122.538 119.762 101.996 1.00 20.81  ? 276 LEU A CD1 1 
ATOM   2098 C  CD2 . LEU A 1 276 ? 121.553 121.964 102.650 1.00 20.65  ? 276 LEU A CD2 1 
ATOM   2099 N  N   . ALA A 1 277 ? 117.903 118.696 104.964 1.00 14.47  ? 277 ALA A N   1 
ATOM   2100 C  CA  . ALA A 1 277 ? 116.603 118.035 105.009 1.00 11.63  ? 277 ALA A CA  1 
ATOM   2101 C  C   . ALA A 1 277 ? 115.555 118.913 105.680 1.00 21.63  ? 277 ALA A C   1 
ATOM   2102 O  O   . ALA A 1 277 ? 114.396 118.947 105.248 1.00 20.03  ? 277 ALA A O   1 
ATOM   2103 C  CB  . ALA A 1 277 ? 116.723 116.694 105.729 1.00 15.72  ? 277 ALA A CB  1 
ATOM   2104 N  N   . ALA A 1 278 ? 115.938 119.620 106.747 1.00 28.03  ? 278 ALA A N   1 
ATOM   2105 C  CA  . ALA A 1 278 ? 115.002 120.547 107.382 1.00 20.56  ? 278 ALA A CA  1 
ATOM   2106 C  C   . ALA A 1 278 ? 114.556 121.627 106.402 1.00 20.02  ? 278 ALA A C   1 
ATOM   2107 O  O   . ALA A 1 278 ? 113.356 121.927 106.280 1.00 30.54  ? 278 ALA A O   1 
ATOM   2108 C  CB  . ALA A 1 278 ? 115.642 121.172 108.620 1.00 13.53  ? 278 ALA A CB  1 
ATOM   2109 N  N   . PHE A 1 279 ? 115.513 122.210 105.674 1.00 17.73  ? 279 PHE A N   1 
ATOM   2110 C  CA  . PHE A 1 279 ? 115.153 123.222 104.684 1.00 19.46  ? 279 PHE A CA  1 
ATOM   2111 C  C   . PHE A 1 279 ? 114.248 122.642 103.598 1.00 23.30  ? 279 PHE A C   1 
ATOM   2112 O  O   . PHE A 1 279 ? 113.302 123.301 103.147 1.00 20.61  ? 279 PHE A O   1 
ATOM   2113 C  CB  . PHE A 1 279 ? 116.409 123.833 104.066 1.00 20.06  ? 279 PHE A CB  1 
ATOM   2114 C  CG  . PHE A 1 279 ? 116.124 124.804 102.956 1.00 26.10  ? 279 PHE A CG  1 
ATOM   2115 C  CD1 . PHE A 1 279 ? 115.649 126.073 103.232 1.00 27.66  ? 279 PHE A CD1 1 
ATOM   2116 C  CD2 . PHE A 1 279 ? 116.328 124.445 101.635 1.00 26.34  ? 279 PHE A CD2 1 
ATOM   2117 C  CE1 . PHE A 1 279 ? 115.385 126.965 102.213 1.00 26.75  ? 279 PHE A CE1 1 
ATOM   2118 C  CE2 . PHE A 1 279 ? 116.065 125.333 100.613 1.00 24.82  ? 279 PHE A CE2 1 
ATOM   2119 C  CZ  . PHE A 1 279 ? 115.594 126.594 100.902 1.00 25.00  ? 279 PHE A CZ  1 
ATOM   2120 N  N   . GLY A 1 280 ? 114.524 121.410 103.165 1.00 21.01  ? 280 GLY A N   1 
ATOM   2121 C  CA  . GLY A 1 280 ? 113.702 120.793 102.136 1.00 15.07  ? 280 GLY A CA  1 
ATOM   2122 C  C   . GLY A 1 280 ? 112.274 120.544 102.584 1.00 23.90  ? 280 GLY A C   1 
ATOM   2123 O  O   . GLY A 1 280 ? 111.330 120.734 101.814 1.00 24.38  ? 280 GLY A O   1 
ATOM   2124 N  N   . CYS A 1 281 ? 112.095 120.098 103.831 1.00 20.87  ? 281 CYS A N   1 
ATOM   2125 C  CA  . CYS A 1 281 ? 110.744 119.923 104.361 1.00 19.02  ? 281 CYS A CA  1 
ATOM   2126 C  C   . CYS A 1 281 ? 110.000 121.253 104.415 1.00 26.94  ? 281 CYS A C   1 
ATOM   2127 O  O   . CYS A 1 281 ? 108.818 121.335 104.038 1.00 28.58  ? 281 CYS A O   1 
ATOM   2128 C  CB  . CYS A 1 281 ? 110.800 119.285 105.750 1.00 22.73  ? 281 CYS A CB  1 
ATOM   2129 S  SG  . CYS A 1 281 ? 111.196 117.525 105.759 1.00 39.10  ? 281 CYS A SG  1 
ATOM   2130 N  N   . LEU A 1 282 ? 110.680 122.311 104.872 1.00 31.85  ? 282 LEU A N   1 
ATOM   2131 C  CA  . LEU A 1 282 ? 110.050 123.629 104.885 1.00 21.75  ? 282 LEU A CA  1 
ATOM   2132 C  C   . LEU A 1 282 ? 109.631 124.054 103.484 1.00 22.56  ? 282 LEU A C   1 
ATOM   2133 O  O   . LEU A 1 282 ? 108.549 124.621 103.297 1.00 27.80  ? 282 LEU A O   1 
ATOM   2134 C  CB  . LEU A 1 282 ? 110.993 124.665 105.492 1.00 26.77  ? 282 LEU A CB  1 
ATOM   2135 C  CG  . LEU A 1 282 ? 110.888 124.909 106.996 1.00 31.20  ? 282 LEU A CG  1 
ATOM   2136 C  CD1 . LEU A 1 282 ? 111.893 125.960 107.428 1.00 24.53  ? 282 LEU A CD1 1 
ATOM   2137 C  CD2 . LEU A 1 282 ? 109.478 125.319 107.376 1.00 27.58  ? 282 LEU A CD2 1 
ATOM   2138 N  N   . VAL A 1 283 ? 110.478 123.794 102.486 1.00 31.16  ? 283 VAL A N   1 
ATOM   2139 C  CA  . VAL A 1 283 ? 110.145 124.160 101.111 1.00 26.36  ? 283 VAL A CA  1 
ATOM   2140 C  C   . VAL A 1 283 ? 108.940 123.366 100.616 1.00 27.08  ? 283 VAL A C   1 
ATOM   2141 O  O   . VAL A 1 283 ? 108.043 123.912 99.962  1.00 31.21  ? 283 VAL A O   1 
ATOM   2142 C  CB  . VAL A 1 283 ? 111.371 123.970 100.198 1.00 21.90  ? 283 VAL A CB  1 
ATOM   2143 C  CG1 . VAL A 1 283 ? 110.947 123.701 98.763  1.00 19.46  ? 283 VAL A CG1 1 
ATOM   2144 C  CG2 . VAL A 1 283 ? 112.267 125.191 100.264 1.00 26.97  ? 283 VAL A CG2 1 
ATOM   2145 N  N   . MET A 1 284 ? 108.899 122.066 100.917 1.00 27.87  ? 284 MET A N   1 
ATOM   2146 C  CA  . MET A 1 284 ? 107.814 121.218 100.432 1.00 23.93  ? 284 MET A CA  1 
ATOM   2147 C  C   . MET A 1 284 ? 106.474 121.534 101.084 1.00 31.31  ? 284 MET A C   1 
ATOM   2148 O  O   . MET A 1 284 ? 105.430 121.221 100.502 1.00 29.14  ? 284 MET A O   1 
ATOM   2149 C  CB  . MET A 1 284 ? 108.147 119.744 100.664 1.00 23.13  ? 284 MET A CB  1 
ATOM   2150 C  CG  . MET A 1 284 ? 109.225 119.186 99.756  1.00 31.16  ? 284 MET A CG  1 
ATOM   2151 S  SD  . MET A 1 284 ? 108.702 119.026 98.043  1.00 44.64  ? 284 MET A SD  1 
ATOM   2152 C  CE  . MET A 1 284 ? 110.291 119.030 97.224  1.00 30.76  ? 284 MET A CE  1 
ATOM   2153 N  N   . ALA A 1 285 ? 106.474 122.129 102.279 1.00 34.23  ? 285 ALA A N   1 
ATOM   2154 C  CA  . ALA A 1 285 ? 105.213 122.330 102.993 1.00 24.98  ? 285 ALA A CA  1 
ATOM   2155 C  C   . ALA A 1 285 ? 104.278 123.365 102.364 1.00 22.23  ? 285 ALA A C   1 
ATOM   2156 O  O   . ALA A 1 285 ? 103.107 123.412 102.752 1.00 29.43  ? 285 ALA A O   1 
ATOM   2157 C  CB  . ALA A 1 285 ? 105.497 122.733 104.437 1.00 26.56  ? 285 ALA A CB  1 
ATOM   2158 N  N   . ILE A 1 286 ? 104.738 124.184 101.422 1.00 23.02  ? 286 ILE A N   1 
ATOM   2159 C  CA  . ILE A 1 286 ? 103.986 125.361 100.972 1.00 27.23  ? 286 ILE A CA  1 
ATOM   2160 C  C   . ILE A 1 286 ? 102.807 125.030 100.053 1.00 31.59  ? 286 ILE A C   1 
ATOM   2161 O  O   . ILE A 1 286 ? 101.691 125.530 100.294 1.00 30.36  ? 286 ILE A O   1 
ATOM   2162 C  CB  . ILE A 1 286 ? 104.927 126.376 100.298 1.00 26.47  ? 286 ILE A CB  1 
ATOM   2163 C  CG1 . ILE A 1 286 ? 105.948 126.904 101.305 1.00 28.48  ? 286 ILE A CG1 1 
ATOM   2164 C  CG2 . ILE A 1 286 ? 104.138 127.522 99.687  1.00 25.70  ? 286 ILE A CG2 1 
ATOM   2165 C  CD1 . ILE A 1 286 ? 107.063 127.704 100.678 1.00 26.20  ? 286 ILE A CD1 1 
ATOM   2166 N  N   . PRO A 1 287 ? 102.983 124.240 98.983  1.00 31.63  ? 287 PRO A N   1 
ATOM   2167 C  CA  . PRO A 1 287 ? 101.838 123.980 98.092  1.00 24.41  ? 287 PRO A CA  1 
ATOM   2168 C  C   . PRO A 1 287 ? 100.665 123.296 98.776  1.00 28.24  ? 287 PRO A C   1 
ATOM   2169 O  O   . PRO A 1 287 ? 99.517  123.529 98.382  1.00 33.20  ? 287 PRO A O   1 
ATOM   2170 C  CB  . PRO A 1 287 ? 102.444 123.101 96.988  1.00 28.16  ? 287 PRO A CB  1 
ATOM   2171 C  CG  . PRO A 1 287 ? 103.666 122.522 97.586  1.00 33.41  ? 287 PRO A CG  1 
ATOM   2172 C  CD  . PRO A 1 287 ? 104.203 123.586 98.477  1.00 30.72  ? 287 PRO A CD  1 
ATOM   2173 N  N   . ALA A 1 288 ? 100.911 122.460 99.787  1.00 22.25  ? 288 ALA A N   1 
ATOM   2174 C  CA  . ALA A 1 288 ? 99.808  121.855 100.528 1.00 22.41  ? 288 ALA A CA  1 
ATOM   2175 C  C   . ALA A 1 288 ? 98.977  122.915 101.244 1.00 27.65  ? 288 ALA A C   1 
ATOM   2176 O  O   . ALA A 1 288 ? 97.740  122.860 101.234 1.00 26.90  ? 288 ALA A O   1 
ATOM   2177 C  CB  . ALA A 1 288 ? 100.346 120.829 101.524 1.00 20.52  ? 288 ALA A CB  1 
ATOM   2178 N  N   . ILE A 1 289 ? 99.641  123.892 101.866 1.00 26.74  ? 289 ILE A N   1 
ATOM   2179 C  CA  . ILE A 1 289 ? 98.933  124.987 102.521 1.00 24.80  ? 289 ILE A CA  1 
ATOM   2180 C  C   . ILE A 1 289 ? 98.130  125.786 101.502 1.00 22.53  ? 289 ILE A C   1 
ATOM   2181 O  O   . ILE A 1 289 ? 96.979  126.167 101.754 1.00 32.08  ? 289 ILE A O   1 
ATOM   2182 C  CB  . ILE A 1 289 ? 99.927  125.883 103.284 1.00 25.43  ? 289 ILE A CB  1 
ATOM   2183 C  CG1 . ILE A 1 289 ? 100.619 125.091 104.395 1.00 29.42  ? 289 ILE A CG1 1 
ATOM   2184 C  CG2 . ILE A 1 289 ? 99.224  127.104 103.855 1.00 23.15  ? 289 ILE A CG2 1 
ATOM   2185 C  CD1 . ILE A 1 289 ? 101.860 125.762 104.935 1.00 26.25  ? 289 ILE A CD1 1 
ATOM   2186 N  N   . LEU A 1 290 ? 98.725  126.058 100.338 1.00 19.40  ? 290 LEU A N   1 
ATOM   2187 C  CA  . LEU A 1 290 ? 98.000  126.807 99.314  1.00 18.73  ? 290 LEU A CA  1 
ATOM   2188 C  C   . LEU A 1 290 ? 96.767  126.047 98.834  1.00 22.95  ? 290 LEU A C   1 
ATOM   2189 O  O   . LEU A 1 290 ? 95.702  126.642 98.631  1.00 22.61  ? 290 LEU A O   1 
ATOM   2190 C  CB  . LEU A 1 290 ? 98.924  127.133 98.143  1.00 22.69  ? 290 LEU A CB  1 
ATOM   2191 C  CG  . LEU A 1 290 ? 99.945  128.242 98.400  1.00 23.20  ? 290 LEU A CG  1 
ATOM   2192 C  CD1 . LEU A 1 290 ? 100.928 128.351 97.249  1.00 25.97  ? 290 LEU A CD1 1 
ATOM   2193 C  CD2 . LEU A 1 290 ? 99.245  129.566 98.638  1.00 23.62  ? 290 LEU A CD2 1 
ATOM   2194 N  N   . ILE A 1 291 ? 96.892  124.730 98.650  1.00 22.46  ? 291 ILE A N   1 
ATOM   2195 C  CA  . ILE A 1 291 ? 95.755  123.920 98.213  1.00 19.85  ? 291 ILE A CA  1 
ATOM   2196 C  C   . ILE A 1 291 ? 94.659  123.914 99.273  1.00 31.34  ? 291 ILE A C   1 
ATOM   2197 O  O   . ILE A 1 291 ? 93.466  124.006 98.954  1.00 27.51  ? 291 ILE A O   1 
ATOM   2198 C  CB  . ILE A 1 291 ? 96.221  122.494 97.863  1.00 21.68  ? 291 ILE A CB  1 
ATOM   2199 C  CG1 . ILE A 1 291 ? 97.019  122.501 96.558  1.00 26.07  ? 291 ILE A CG1 1 
ATOM   2200 C  CG2 . ILE A 1 291 ? 95.039  121.549 97.750  1.00 22.48  ? 291 ILE A CG2 1 
ATOM   2201 C  CD1 . ILE A 1 291 ? 97.757  121.211 96.285  1.00 20.86  ? 291 ILE A CD1 1 
ATOM   2202 N  N   . GLY A 1 292 ? 95.041  123.801 100.547 1.00 28.79  ? 292 GLY A N   1 
ATOM   2203 C  CA  . GLY A 1 292 ? 94.049  123.860 101.611 1.00 14.53  ? 292 GLY A CA  1 
ATOM   2204 C  C   . GLY A 1 292 ? 93.308  125.184 101.650 1.00 25.29  ? 292 GLY A C   1 
ATOM   2205 O  O   . GLY A 1 292 ? 92.086  125.220 101.822 1.00 29.47  ? 292 GLY A O   1 
ATOM   2206 N  N   . ALA A 1 293 ? 94.037  126.291 101.486 1.00 32.21  ? 293 ALA A N   1 
ATOM   2207 C  CA  . ALA A 1 293 ? 93.394  127.602 101.448 1.00 13.52  ? 293 ALA A CA  1 
ATOM   2208 C  C   . ALA A 1 293 ? 92.451  127.727 100.255 1.00 23.01  ? 293 ALA A C   1 
ATOM   2209 O  O   . ALA A 1 293 ? 91.346  128.274 100.381 1.00 21.24  ? 293 ALA A O   1 
ATOM   2210 C  CB  . ALA A 1 293 ? 94.452  128.703 101.412 1.00 12.85  ? 293 ALA A CB  1 
ATOM   2211 N  N   . ILE A 1 294 ? 92.869  127.226 99.088  1.00 25.98  ? 294 ILE A N   1 
ATOM   2212 C  CA  . ILE A 1 294 ? 92.007  127.261 97.909  1.00 26.63  ? 294 ILE A CA  1 
ATOM   2213 C  C   . ILE A 1 294 ? 90.729  126.472 98.162  1.00 26.75  ? 294 ILE A C   1 
ATOM   2214 O  O   . ILE A 1 294 ? 89.628  126.913 97.812  1.00 24.05  ? 294 ILE A O   1 
ATOM   2215 C  CB  . ILE A 1 294 ? 92.759  126.729 96.674  1.00 23.63  ? 294 ILE A CB  1 
ATOM   2216 C  CG1 . ILE A 1 294 ? 93.851  127.706 96.241  1.00 33.46  ? 294 ILE A CG1 1 
ATOM   2217 C  CG2 . ILE A 1 294 ? 91.796  126.483 95.525  1.00 18.06  ? 294 ILE A CG2 1 
ATOM   2218 C  CD1 . ILE A 1 294 ? 94.852  127.107 95.279  1.00 27.29  ? 294 ILE A CD1 1 
ATOM   2219 N  N   . GLY A 1 295 ? 90.856  125.293 98.771  1.00 28.91  ? 295 GLY A N   1 
ATOM   2220 C  CA  . GLY A 1 295 ? 89.676  124.502 99.081  1.00 23.91  ? 295 GLY A CA  1 
ATOM   2221 C  C   . GLY A 1 295 ? 88.752  125.191 100.066 1.00 25.48  ? 295 GLY A C   1 
ATOM   2222 O  O   . GLY A 1 295 ? 87.528  125.107 99.946  1.00 26.88  ? 295 GLY A O   1 
ATOM   2223 N  N   . ALA A 1 296 ? 89.324  125.879 101.056 1.00 33.59  ? 296 ALA A N   1 
ATOM   2224 C  CA  . ALA A 1 296 ? 88.508  126.597 102.029 1.00 23.48  ? 296 ALA A CA  1 
ATOM   2225 C  C   . ALA A 1 296 ? 87.866  127.851 101.449 1.00 22.96  ? 296 ALA A C   1 
ATOM   2226 O  O   . ALA A 1 296 ? 86.887  128.346 102.015 1.00 28.44  ? 296 ALA A O   1 
ATOM   2227 C  CB  . ALA A 1 296 ? 89.345  126.967 103.252 1.00 21.58  ? 296 ALA A CB  1 
ATOM   2228 N  N   . SER A 1 297 ? 88.390  128.377 100.343 1.00 36.77  ? 297 SER A N   1 
ATOM   2229 C  CA  . SER A 1 297 ? 87.898  129.619 99.758  1.00 30.94  ? 297 SER A CA  1 
ATOM   2230 C  C   . SER A 1 297 ? 87.113  129.397 98.465  1.00 32.01  ? 297 SER A C   1 
ATOM   2231 O  O   . SER A 1 297 ? 87.170  130.226 97.555  1.00 36.45  ? 297 SER A O   1 
ATOM   2232 C  CB  . SER A 1 297 ? 89.064  130.573 99.507  1.00 26.73  ? 297 SER A CB  1 
ATOM   2233 O  OG  . SER A 1 297 ? 88.692  131.604 98.614  1.00 42.49  ? 297 SER A OG  1 
ATOM   2234 N  N   . THR A 1 298 ? 86.360  128.303 98.373  1.00 36.24  ? 298 THR A N   1 
ATOM   2235 C  CA  . THR A 1 298 ? 85.717  127.897 97.129  1.00 34.24  ? 298 THR A CA  1 
ATOM   2236 C  C   . THR A 1 298 ? 84.206  127.811 97.297  1.00 37.74  ? 298 THR A C   1 
ATOM   2237 O  O   . THR A 1 298 ? 83.709  127.345 98.327  1.00 51.40  ? 298 THR A O   1 
ATOM   2238 C  CB  . THR A 1 298 ? 86.261  126.544 96.652  1.00 29.24  ? 298 THR A CB  1 
ATOM   2239 O  OG1 . THR A 1 298 ? 87.689  126.610 96.557  1.00 39.60  ? 298 THR A OG1 1 
ATOM   2240 C  CG2 . THR A 1 298 ? 85.690  126.177 95.293  1.00 22.78  ? 298 THR A CG2 1 
ATOM   2241 N  N   . ASP A 1 299 ? 83.479  128.270 96.277  1.00 35.59  ? 299 ASP A N   1 
ATOM   2242 C  CA  . ASP A 1 299 ? 82.025  128.128 96.201  1.00 35.97  ? 299 ASP A CA  1 
ATOM   2243 C  C   . ASP A 1 299 ? 81.722  126.786 95.547  1.00 44.59  ? 299 ASP A C   1 
ATOM   2244 O  O   . ASP A 1 299 ? 81.639  126.669 94.325  1.00 45.64  ? 299 ASP A O   1 
ATOM   2245 C  CB  . ASP A 1 299 ? 81.413  129.285 95.422  1.00 39.41  ? 299 ASP A CB  1 
ATOM   2246 C  CG  . ASP A 1 299 ? 79.898  129.237 95.394  1.00 44.69  ? 299 ASP A CG  1 
ATOM   2247 O  OD1 . ASP A 1 299 ? 79.304  128.471 96.179  1.00 44.96  ? 299 ASP A OD1 1 
ATOM   2248 O  OD2 . ASP A 1 299 ? 79.298  129.971 94.583  1.00 50.09  ? 299 ASP A OD2 1 
ATOM   2249 N  N   . TRP A 1 300 ? 81.542  125.756 96.377  1.00 46.92  ? 300 TRP A N   1 
ATOM   2250 C  CA  . TRP A 1 300 ? 81.410  124.392 95.877  1.00 40.63  ? 300 TRP A CA  1 
ATOM   2251 C  C   . TRP A 1 300 ? 80.118  124.156 95.110  1.00 41.76  ? 300 TRP A C   1 
ATOM   2252 O  O   . TRP A 1 300 ? 79.998  123.125 94.441  1.00 45.11  ? 300 TRP A O   1 
ATOM   2253 C  CB  . TRP A 1 300 ? 81.516  123.402 97.035  1.00 29.37  ? 300 TRP A CB  1 
ATOM   2254 C  CG  . TRP A 1 300 ? 82.921  123.211 97.502  1.00 37.46  ? 300 TRP A CG  1 
ATOM   2255 C  CD1 . TRP A 1 300 ? 83.447  123.605 98.694  1.00 33.82  ? 300 TRP A CD1 1 
ATOM   2256 C  CD2 . TRP A 1 300 ? 83.987  122.584 96.780  1.00 38.87  ? 300 TRP A CD2 1 
ATOM   2257 N  NE1 . TRP A 1 300 ? 84.774  123.260 98.763  1.00 36.80  ? 300 TRP A NE1 1 
ATOM   2258 C  CE2 . TRP A 1 300 ? 85.130  122.632 97.600  1.00 38.15  ? 300 TRP A CE2 1 
ATOM   2259 C  CE3 . TRP A 1 300 ? 84.085  121.985 95.521  1.00 33.51  ? 300 TRP A CE3 1 
ATOM   2260 C  CZ2 . TRP A 1 300 ? 86.355  122.105 97.202  1.00 37.20  ? 300 TRP A CZ2 1 
ATOM   2261 C  CZ3 . TRP A 1 300 ? 85.302  121.463 95.129  1.00 36.24  ? 300 TRP A CZ3 1 
ATOM   2262 C  CH2 . TRP A 1 300 ? 86.420  121.526 95.966  1.00 39.11  ? 300 TRP A CH2 1 
ATOM   2263 N  N   . ASN A 1 301 ? 79.155  125.073 95.187  1.00 53.17  ? 301 ASN A N   1 
ATOM   2264 C  CA  . ASN A 1 301 ? 77.929  124.927 94.416  1.00 48.73  ? 301 ASN A CA  1 
ATOM   2265 C  C   . ASN A 1 301 ? 78.142  125.208 92.933  1.00 54.77  ? 301 ASN A C   1 
ATOM   2266 O  O   . ASN A 1 301 ? 77.346  124.750 92.107  1.00 59.65  ? 301 ASN A O   1 
ATOM   2267 C  CB  . ASN A 1 301 ? 76.852  125.852 94.982  1.00 56.96  ? 301 ASN A CB  1 
ATOM   2268 C  CG  . ASN A 1 301 ? 75.526  125.700 94.275  1.00 61.83  ? 301 ASN A CG  1 
ATOM   2269 O  OD1 . ASN A 1 301 ? 75.192  124.625 93.778  1.00 65.55  ? 301 ASN A OD1 1 
ATOM   2270 N  ND2 . ASN A 1 301 ? 74.761  126.777 94.221  1.00 61.58  ? 301 ASN A ND2 1 
ATOM   2271 N  N   . GLN A 1 302 ? 79.197  125.935 92.576  1.00 55.70  ? 302 GLN A N   1 
ATOM   2272 C  CA  . GLN A 1 302 ? 79.472  126.285 91.189  1.00 52.68  ? 302 GLN A CA  1 
ATOM   2273 C  C   . GLN A 1 302 ? 80.324  125.249 90.467  1.00 52.85  ? 302 GLN A C   1 
ATOM   2274 O  O   . GLN A 1 302 ? 80.587  125.412 89.271  1.00 54.91  ? 302 GLN A O   1 
ATOM   2275 C  CB  . GLN A 1 302 ? 80.162  127.649 91.117  1.00 51.86  ? 302 GLN A CB  1 
ATOM   2276 C  CG  . GLN A 1 302 ? 79.210  128.823 91.001  1.00 52.30  ? 302 GLN A CG  1 
ATOM   2277 C  CD  . GLN A 1 302 ? 79.935  130.154 90.971  1.00 59.05  ? 302 GLN A CD  1 
ATOM   2278 O  OE1 . GLN A 1 302 ? 80.925  130.319 90.260  1.00 57.08  ? 302 GLN A OE1 1 
ATOM   2279 N  NE2 . GLN A 1 302 ? 79.442  131.113 91.746  1.00 57.23  ? 302 GLN A NE2 1 
ATOM   2280 N  N   . THR A 1 303 ? 80.766  124.202 91.154  1.00 44.53  ? 303 THR A N   1 
ATOM   2281 C  CA  . THR A 1 303 ? 81.573  123.156 90.551  1.00 44.91  ? 303 THR A CA  1 
ATOM   2282 C  C   . THR A 1 303 ? 80.708  121.932 90.258  1.00 47.33  ? 303 THR A C   1 
ATOM   2283 O  O   . THR A 1 303 ? 79.488  121.940 90.433  1.00 47.34  ? 303 THR A O   1 
ATOM   2284 C  CB  . THR A 1 303 ? 82.748  122.792 91.461  1.00 43.99  ? 303 THR A CB  1 
ATOM   2285 O  OG1 . THR A 1 303 ? 82.253  122.351 92.730  1.00 44.39  ? 303 THR A OG1 1 
ATOM   2286 C  CG2 . THR A 1 303 ? 83.649  123.994 91.671  1.00 42.70  ? 303 THR A CG2 1 
ATOM   2287 N  N   . ALA A 1 304 ? 81.356  120.863 89.795  1.00 48.35  ? 304 ALA A N   1 
ATOM   2288 C  CA  . ALA A 1 304 ? 80.665  119.606 89.544  1.00 43.47  ? 304 ALA A CA  1 
ATOM   2289 C  C   . ALA A 1 304 ? 80.458  118.780 90.807  1.00 45.31  ? 304 ALA A C   1 
ATOM   2290 O  O   . ALA A 1 304 ? 79.664  117.835 90.783  1.00 48.95  ? 304 ALA A O   1 
ATOM   2291 C  CB  . ALA A 1 304 ? 81.432  118.779 88.511  1.00 40.60  ? 304 ALA A CB  1 
ATOM   2292 N  N   . TYR A 1 305 ? 81.155  119.106 91.898  1.00 40.32  ? 305 TYR A N   1 
ATOM   2293 C  CA  . TYR A 1 305 ? 80.944  118.394 93.154  1.00 32.57  ? 305 TYR A CA  1 
ATOM   2294 C  C   . TYR A 1 305 ? 79.537  118.629 93.689  1.00 43.05  ? 305 TYR A C   1 
ATOM   2295 O  O   . TYR A 1 305 ? 78.880  117.694 94.161  1.00 47.95  ? 305 TYR A O   1 
ATOM   2296 C  CB  . TYR A 1 305 ? 81.991  118.827 94.180  1.00 35.12  ? 305 TYR A CB  1 
ATOM   2297 C  CG  . TYR A 1 305 ? 82.114  117.901 95.367  1.00 35.30  ? 305 TYR A CG  1 
ATOM   2298 C  CD1 . TYR A 1 305 ? 82.987  116.826 95.346  1.00 36.21  ? 305 TYR A CD1 1 
ATOM   2299 C  CD2 . TYR A 1 305 ? 81.358  118.105 96.511  1.00 39.58  ? 305 TYR A CD2 1 
ATOM   2300 C  CE1 . TYR A 1 305 ? 83.102  115.978 96.426  1.00 31.67  ? 305 TYR A CE1 1 
ATOM   2301 C  CE2 . TYR A 1 305 ? 81.466  117.262 97.595  1.00 40.78  ? 305 TYR A CE2 1 
ATOM   2302 C  CZ  . TYR A 1 305 ? 82.340  116.201 97.548  1.00 34.33  ? 305 TYR A CZ  1 
ATOM   2303 O  OH  . TYR A 1 305 ? 82.450  115.359 98.628  1.00 37.23  ? 305 TYR A OH  1 
ATOM   2304 N  N   . GLY A 1 306 ? 79.062  119.870 93.632  1.00 44.17  ? 306 GLY A N   1 
ATOM   2305 C  CA  . GLY A 1 306 ? 77.723  120.200 94.069  1.00 40.95  ? 306 GLY A CA  1 
ATOM   2306 C  C   . GLY A 1 306 ? 77.589  120.228 95.580  1.00 47.41  ? 306 GLY A C   1 
ATOM   2307 O  O   . GLY A 1 306 ? 78.454  119.774 96.331  1.00 46.45  ? 306 GLY A O   1 
ATOM   2308 N  N   . LEU A 1 307 ? 76.467  120.785 96.032  1.00 49.83  ? 307 LEU A N   1 
ATOM   2309 C  CA  . LEU A 1 307 ? 76.159  120.809 97.452  1.00 48.90  ? 307 LEU A CA  1 
ATOM   2310 C  C   . LEU A 1 307 ? 75.658  119.441 97.911  1.00 47.98  ? 307 LEU A C   1 
ATOM   2311 O  O   . LEU A 1 307 ? 75.005  118.725 97.149  1.00 49.56  ? 307 LEU A O   1 
ATOM   2312 C  CB  . LEU A 1 307 ? 75.108  121.872 97.751  1.00 48.83  ? 307 LEU A CB  1 
ATOM   2313 C  CG  . LEU A 1 307 ? 75.597  123.321 97.741  1.00 49.78  ? 307 LEU A CG  1 
ATOM   2314 C  CD1 . LEU A 1 307 ? 74.498  124.261 98.205  1.00 50.12  ? 307 LEU A CD1 1 
ATOM   2315 C  CD2 . LEU A 1 307 ? 76.841  123.477 98.603  1.00 46.09  ? 307 LEU A CD2 1 
ATOM   2316 N  N   . PRO A 1 308 ? 75.940  119.054 99.164  1.00 45.53  ? 308 PRO A N   1 
ATOM   2317 C  CA  . PRO A 1 308 ? 76.665  119.789 100.214 1.00 48.22  ? 308 PRO A CA  1 
ATOM   2318 C  C   . PRO A 1 308 ? 78.184  119.806 100.047 1.00 49.26  ? 308 PRO A C   1 
ATOM   2319 O  O   . PRO A 1 308 ? 78.743  119.182 99.151  1.00 46.33  ? 308 PRO A O   1 
ATOM   2320 C  CB  . PRO A 1 308 ? 76.253  119.042 101.488 1.00 46.53  ? 308 PRO A CB  1 
ATOM   2321 C  CG  . PRO A 1 308 ? 76.044  117.637 101.032 1.00 48.83  ? 308 PRO A CG  1 
ATOM   2322 C  CD  . PRO A 1 308 ? 75.439  117.758 99.658  1.00 45.26  ? 308 PRO A CD  1 
ATOM   2323 N  N   . ASP A 1 309 ? 78.861  120.533 100.934 1.00 49.44  ? 309 ASP A N   1 
ATOM   2324 C  CA  . ASP A 1 309 ? 80.303  120.694 100.875 1.00 39.87  ? 309 ASP A CA  1 
ATOM   2325 C  C   . ASP A 1 309 ? 81.012  119.378 101.187 1.00 45.94  ? 309 ASP A C   1 
ATOM   2326 O  O   . ASP A 1 309 ? 80.420  118.464 101.765 1.00 45.96  ? 309 ASP A O   1 
ATOM   2327 C  CB  . ASP A 1 309 ? 80.748  121.765 101.868 1.00 41.81  ? 309 ASP A CB  1 
ATOM   2328 C  CG  . ASP A 1 309 ? 80.414  123.164 101.403 1.00 53.66  ? 309 ASP A CG  1 
ATOM   2329 O  OD1 . ASP A 1 309 ? 79.867  123.304 100.291 1.00 59.18  ? 309 ASP A OD1 1 
ATOM   2330 O  OD2 . ASP A 1 309 ? 80.698  124.123 102.151 1.00 55.02  ? 309 ASP A OD2 1 
ATOM   2331 N  N   . PRO A 1 310 ? 82.284  119.252 100.794 1.00 40.41  ? 310 PRO A N   1 
ATOM   2332 C  CA  . PRO A 1 310 ? 83.049  118.054 101.175 1.00 39.16  ? 310 PRO A CA  1 
ATOM   2333 C  C   . PRO A 1 310 ? 83.156  117.842 102.675 1.00 40.79  ? 310 PRO A C   1 
ATOM   2334 O  O   . PRO A 1 310 ? 83.253  116.692 103.118 1.00 39.53  ? 310 PRO A O   1 
ATOM   2335 C  CB  . PRO A 1 310 ? 84.423  118.309 100.544 1.00 34.76  ? 310 PRO A CB  1 
ATOM   2336 C  CG  . PRO A 1 310 ? 84.138  119.182 99.386  1.00 34.07  ? 310 PRO A CG  1 
ATOM   2337 C  CD  . PRO A 1 310 ? 83.009  120.074 99.811  1.00 37.54  ? 310 PRO A CD  1 
ATOM   2338 N  N   . LYS A 1 311 ? 83.158  118.911 103.476 1.00 41.26  ? 311 LYS A N   1 
ATOM   2339 C  CA  . LYS A 1 311 ? 83.205  118.734 104.924 1.00 39.93  ? 311 LYS A CA  1 
ATOM   2340 C  C   . LYS A 1 311 ? 81.869  118.254 105.477 1.00 45.05  ? 311 LYS A C   1 
ATOM   2341 O  O   . LYS A 1 311 ? 81.841  117.522 106.472 1.00 49.77  ? 311 LYS A O   1 
ATOM   2342 C  CB  . LYS A 1 311 ? 83.634  120.034 105.606 1.00 40.97  ? 311 LYS A CB  1 
ATOM   2343 C  CG  . LYS A 1 311 ? 82.755  121.233 105.305 1.00 44.07  ? 311 LYS A CG  1 
ATOM   2344 C  CD  . LYS A 1 311 ? 83.311  122.490 105.950 1.00 42.66  ? 311 LYS A CD  1 
ATOM   2345 C  CE  . LYS A 1 311 ? 82.512  123.714 105.547 1.00 43.58  ? 311 LYS A CE  1 
ATOM   2346 N  NZ  . LYS A 1 311 ? 81.264  123.849 106.341 1.00 41.79  ? 311 LYS A NZ  1 
ATOM   2347 N  N   . THR A 1 312 ? 80.758  118.660 104.859 1.00 45.78  ? 312 THR A N   1 
ATOM   2348 C  CA  . THR A 1 312 ? 79.453  118.163 105.280 1.00 44.60  ? 312 THR A CA  1 
ATOM   2349 C  C   . THR A 1 312 ? 79.289  116.688 104.934 1.00 45.27  ? 312 THR A C   1 
ATOM   2350 O  O   . THR A 1 312 ? 78.689  115.925 105.701 1.00 52.62  ? 312 THR A O   1 
ATOM   2351 C  CB  . THR A 1 312 ? 78.345  118.998 104.637 1.00 46.28  ? 312 THR A CB  1 
ATOM   2352 O  OG1 . THR A 1 312 ? 78.512  120.374 104.998 1.00 49.46  ? 312 THR A OG1 1 
ATOM   2353 C  CG2 . THR A 1 312 ? 76.979  118.527 105.099 1.00 43.96  ? 312 THR A CG2 1 
ATOM   2354 N  N   . THR A 1 313 ? 79.832  116.265 103.796 1.00 44.58  ? 313 THR A N   1 
ATOM   2355 C  CA  . THR A 1 313 ? 79.761  114.885 103.332 1.00 44.60  ? 313 THR A CA  1 
ATOM   2356 C  C   . THR A 1 313 ? 80.727  113.969 104.100 1.00 45.60  ? 313 THR A C   1 
ATOM   2357 O  O   . THR A 1 313 ? 80.835  112.778 103.791 1.00 48.44  ? 313 THR A O   1 
ATOM   2358 C  CB  . THR A 1 313 ? 80.033  114.865 101.817 1.00 48.78  ? 313 THR A CB  1 
ATOM   2359 O  OG1 . THR A 1 313 ? 79.054  115.679 101.163 1.00 52.79  ? 313 THR A OG1 1 
ATOM   2360 C  CG2 . THR A 1 313 ? 79.902  113.471 101.213 1.00 48.38  ? 313 THR A CG2 1 
ATOM   2361 N  N   . GLU A 1 314 ? 81.382  114.490 105.141 1.00 46.52  ? 314 GLU A N   1 
ATOM   2362 C  CA  . GLU A 1 314 ? 82.383  113.746 105.910 1.00 48.56  ? 314 GLU A CA  1 
ATOM   2363 C  C   . GLU A 1 314 ? 83.514  113.255 105.008 1.00 50.50  ? 314 GLU A C   1 
ATOM   2364 O  O   . GLU A 1 314 ? 83.948  112.105 105.092 1.00 52.28  ? 314 GLU A O   1 
ATOM   2365 C  CB  . GLU A 1 314 ? 81.754  112.580 106.678 1.00 50.93  ? 314 GLU A CB  1 
ATOM   2366 C  CG  . GLU A 1 314 ? 80.358  112.858 107.212 1.00 52.08  ? 314 GLU A CG  1 
ATOM   2367 C  CD  . GLU A 1 314 ? 80.378  113.488 108.585 1.00 56.44  ? 314 GLU A CD  1 
ATOM   2368 O  OE1 . GLU A 1 314 ? 79.646  114.478 108.794 1.00 54.39  ? 314 GLU A OE1 1 
ATOM   2369 O  OE2 . GLU A 1 314 ? 81.128  112.998 109.454 1.00 58.84  ? 314 GLU A OE2 1 
ATOM   2370 N  N   . GLU A 1 315 ? 83.995  114.142 104.138 1.00 46.07  ? 315 GLU A N   1 
ATOM   2371 C  CA  . GLU A 1 315 ? 85.056  113.828 103.189 1.00 41.48  ? 315 GLU A CA  1 
ATOM   2372 C  C   . GLU A 1 315 ? 86.180  114.854 103.259 1.00 37.84  ? 315 GLU A C   1 
ATOM   2373 O  O   . GLU A 1 315 ? 86.799  115.172 102.242 1.00 43.59  ? 315 GLU A O   1 
ATOM   2374 C  CB  . GLU A 1 315 ? 84.502  113.748 101.767 1.00 41.17  ? 315 GLU A CB  1 
ATOM   2375 C  CG  . GLU A 1 315 ? 84.151  112.352 101.301 1.00 40.73  ? 315 GLU A CG  1 
ATOM   2376 C  CD  . GLU A 1 315 ? 84.138  112.242 99.791  1.00 49.22  ? 315 GLU A CD  1 
ATOM   2377 O  OE1 . GLU A 1 315 ? 83.303  112.919 99.156  1.00 48.83  ? 315 GLU A OE1 1 
ATOM   2378 O  OE2 . GLU A 1 315 ? 84.963  111.485 99.237  1.00 52.15  ? 315 GLU A OE2 1 
ATOM   2379 N  N   . ALA A 1 316 ? 86.456  115.382 104.452 1.00 31.82  ? 316 ALA A N   1 
ATOM   2380 C  CA  . ALA A 1 316 ? 87.445  116.443 104.597 1.00 32.27  ? 316 ALA A CA  1 
ATOM   2381 C  C   . ALA A 1 316 ? 88.878  115.944 104.483 1.00 32.35  ? 316 ALA A C   1 
ATOM   2382 O  O   . ALA A 1 316 ? 89.775  116.746 104.206 1.00 35.25  ? 316 ALA A O   1 
ATOM   2383 C  CB  . ALA A 1 316 ? 87.258  117.157 105.937 1.00 32.76  ? 316 ALA A CB  1 
ATOM   2384 N  N   . ASP A 1 317 ? 89.113  114.649 104.670 1.00 31.20  ? 317 ASP A N   1 
ATOM   2385 C  CA  . ASP A 1 317 ? 90.465  114.089 104.549 1.00 25.67  ? 317 ASP A CA  1 
ATOM   2386 C  C   . ASP A 1 317 ? 90.919  113.979 103.099 1.00 30.04  ? 317 ASP A C   1 
ATOM   2387 O  O   . ASP A 1 317 ? 92.108  113.801 102.834 1.00 37.13  ? 317 ASP A O   1 
ATOM   2388 C  CB  . ASP A 1 317 ? 90.542  112.717 105.227 1.00 25.47  ? 317 ASP A CB  1 
ATOM   2389 C  CG  . ASP A 1 317 ? 89.649  111.679 104.562 1.00 40.23  ? 317 ASP A CG  1 
ATOM   2390 O  OD1 . ASP A 1 317 ? 88.528  112.024 104.130 1.00 46.80  ? 317 ASP A OD1 1 
ATOM   2391 O  OD2 . ASP A 1 317 ? 90.069  110.506 104.484 1.00 41.58  ? 317 ASP A OD2 1 
ATOM   2392 N  N   . MET A 1 318 ? 89.987  114.088 102.161 1.00 20.83  ? 318 MET A N   1 
ATOM   2393 C  CA  . MET A 1 318 ? 90.289  113.964 100.742 1.00 24.44  ? 318 MET A CA  1 
ATOM   2394 C  C   . MET A 1 318 ? 90.141  115.293 100.008 1.00 29.87  ? 318 MET A C   1 
ATOM   2395 O  O   . MET A 1 318 ? 89.762  115.319 98.836  1.00 35.46  ? 318 MET A O   1 
ATOM   2396 C  CB  . MET A 1 318 ? 89.398  112.902 100.100 1.00 34.55  ? 318 MET A CB  1 
ATOM   2397 C  CG  . MET A 1 318 ? 89.611  111.498 100.638 1.00 35.03  ? 318 MET A CG  1 
ATOM   2398 S  SD  . MET A 1 318 ? 90.938  110.630 99.784  1.00 48.79  ? 318 MET A SD  1 
ATOM   2399 C  CE  . MET A 1 318 ? 92.179  110.552 101.070 1.00 28.34  ? 318 MET A CE  1 
ATOM   2400 N  N   . ILE A 1 319 ? 90.443  116.405 100.681 1.00 24.43  ? 319 ILE A N   1 
ATOM   2401 C  CA  . ILE A 1 319 ? 90.249  117.716 100.071 1.00 19.57  ? 319 ILE A CA  1 
ATOM   2402 C  C   . ILE A 1 319 ? 91.255  117.951 98.946  1.00 25.09  ? 319 ILE A C   1 
ATOM   2403 O  O   . ILE A 1 319 ? 90.915  118.533 97.910  1.00 26.94  ? 319 ILE A O   1 
ATOM   2404 C  CB  . ILE A 1 319 ? 90.305  118.823 101.145 1.00 22.00  ? 319 ILE A CB  1 
ATOM   2405 C  CG1 . ILE A 1 319 ? 90.020  120.195 100.525 1.00 21.45  ? 319 ILE A CG1 1 
ATOM   2406 C  CG2 . ILE A 1 319 ? 91.632  118.812 101.887 1.00 21.14  ? 319 ILE A CG2 1 
ATOM   2407 C  CD1 . ILE A 1 319 ? 88.622  120.335 99.964  1.00 17.35  ? 319 ILE A CD1 1 
ATOM   2408 N  N   . LEU A 1 320 ? 92.502  117.513 99.127  1.00 20.10  ? 320 LEU A N   1 
ATOM   2409 C  CA  . LEU A 1 320 ? 93.499  117.669 98.068  1.00 19.76  ? 320 LEU A CA  1 
ATOM   2410 C  C   . LEU A 1 320 ? 93.139  116.894 96.804  1.00 30.45  ? 320 LEU A C   1 
ATOM   2411 O  O   . LEU A 1 320 ? 93.161  117.494 95.713  1.00 29.07  ? 320 LEU A O   1 
ATOM   2412 C  CB  . LEU A 1 320 ? 94.882  117.281 98.606  1.00 26.83  ? 320 LEU A CB  1 
ATOM   2413 C  CG  . LEU A 1 320 ? 96.119  117.600 97.762  1.00 30.55  ? 320 LEU A CG  1 
ATOM   2414 C  CD1 . LEU A 1 320 ? 97.214  118.189 98.628  1.00 23.25  ? 320 LEU A CD1 1 
ATOM   2415 C  CD2 . LEU A 1 320 ? 96.623  116.360 97.045  1.00 23.47  ? 320 LEU A CD2 1 
ATOM   2416 N  N   . PRO A 1 321 ? 92.806  115.595 96.858  1.00 24.85  ? 321 PRO A N   1 
ATOM   2417 C  CA  . PRO A 1 321 ? 92.339  114.927 95.632  1.00 19.63  ? 321 PRO A CA  1 
ATOM   2418 C  C   . PRO A 1 321 ? 91.081  115.544 95.050  1.00 25.72  ? 321 PRO A C   1 
ATOM   2419 O  O   . PRO A 1 321 ? 90.947  115.609 93.824  1.00 32.71  ? 321 PRO A O   1 
ATOM   2420 C  CB  . PRO A 1 321 ? 92.103  113.483 96.094  1.00 22.66  ? 321 PRO A CB  1 
ATOM   2421 C  CG  . PRO A 1 321 ? 92.978  113.323 97.271  1.00 18.93  ? 321 PRO A CG  1 
ATOM   2422 C  CD  . PRO A 1 321 ? 92.929  114.634 97.970  1.00 20.29  ? 321 PRO A CD  1 
ATOM   2423 N  N   . ILE A 1 322 ? 90.153  116.002 95.894  1.00 19.55  ? 322 ILE A N   1 
ATOM   2424 C  CA  . ILE A 1 322 ? 88.935  116.626 95.387  1.00 25.43  ? 322 ILE A CA  1 
ATOM   2425 C  C   . ILE A 1 322 ? 89.262  117.922 94.657  1.00 27.94  ? 322 ILE A C   1 
ATOM   2426 O  O   . ILE A 1 322 ? 88.710  118.203 93.586  1.00 32.84  ? 322 ILE A O   1 
ATOM   2427 C  CB  . ILE A 1 322 ? 87.929  116.854 96.531  1.00 26.11  ? 322 ILE A CB  1 
ATOM   2428 C  CG1 . ILE A 1 322 ? 87.270  115.534 96.933  1.00 27.11  ? 322 ILE A CG1 1 
ATOM   2429 C  CG2 . ILE A 1 322 ? 86.866  117.860 96.124  1.00 23.64  ? 322 ILE A CG2 1 
ATOM   2430 C  CD1 . ILE A 1 322 ? 86.539  115.598 98.250  1.00 20.98  ? 322 ILE A CD1 1 
ATOM   2431 N  N   . VAL A 1 323 ? 90.160  118.732 95.222  1.00 26.95  ? 323 VAL A N   1 
ATOM   2432 C  CA  . VAL A 1 323 ? 90.566  119.972 94.564  1.00 28.89  ? 323 VAL A CA  1 
ATOM   2433 C  C   . VAL A 1 323 ? 91.222  119.667 93.223  1.00 34.10  ? 323 VAL A C   1 
ATOM   2434 O  O   . VAL A 1 323 ? 90.900  120.285 92.201  1.00 35.12  ? 323 VAL A O   1 
ATOM   2435 C  CB  . VAL A 1 323 ? 91.498  120.786 95.481  1.00 24.94  ? 323 VAL A CB  1 
ATOM   2436 C  CG1 . VAL A 1 323 ? 92.323  121.772 94.672  1.00 22.56  ? 323 VAL A CG1 1 
ATOM   2437 C  CG2 . VAL A 1 323 ? 90.695  121.516 96.541  1.00 25.62  ? 323 VAL A CG2 1 
ATOM   2438 N  N   . LEU A 1 324 ? 92.129  118.685 93.202  1.00 32.61  ? 324 LEU A N   1 
ATOM   2439 C  CA  . LEU A 1 324 ? 92.801  118.329 91.954  1.00 23.58  ? 324 LEU A CA  1 
ATOM   2440 C  C   . LEU A 1 324 ? 91.811  117.829 90.908  1.00 25.06  ? 324 LEU A C   1 
ATOM   2441 O  O   . LEU A 1 324 ? 91.936  118.150 89.721  1.00 33.66  ? 324 LEU A O   1 
ATOM   2442 C  CB  . LEU A 1 324 ? 93.872  117.270 92.213  1.00 27.50  ? 324 LEU A CB  1 
ATOM   2443 C  CG  . LEU A 1 324 ? 95.175  117.706 92.881  1.00 29.62  ? 324 LEU A CG  1 
ATOM   2444 C  CD1 . LEU A 1 324 ? 95.992  116.493 93.286  1.00 26.04  ? 324 LEU A CD1 1 
ATOM   2445 C  CD2 . LEU A 1 324 ? 95.976  118.603 91.957  1.00 29.20  ? 324 LEU A CD2 1 
ATOM   2446 N  N   . GLN A 1 325 ? 90.822  117.040 91.326  1.00 24.50  ? 325 GLN A N   1 
ATOM   2447 C  CA  . GLN A 1 325 ? 89.889  116.439 90.381  1.00 28.84  ? 325 GLN A CA  1 
ATOM   2448 C  C   . GLN A 1 325 ? 88.872  117.445 89.853  1.00 32.34  ? 325 GLN A C   1 
ATOM   2449 O  O   . GLN A 1 325 ? 88.512  117.398 88.672  1.00 38.31  ? 325 GLN A O   1 
ATOM   2450 C  CB  . GLN A 1 325 ? 89.182  115.254 91.043  1.00 27.93  ? 325 GLN A CB  1 
ATOM   2451 C  CG  . GLN A 1 325 ? 87.953  114.749 90.308  1.00 33.61  ? 325 GLN A CG  1 
ATOM   2452 C  CD  . GLN A 1 325 ? 88.294  113.980 89.051  1.00 37.28  ? 325 GLN A CD  1 
ATOM   2453 O  OE1 . GLN A 1 325 ? 89.432  113.558 88.857  1.00 38.77  ? 325 GLN A OE1 1 
ATOM   2454 N  NE2 . GLN A 1 325 ? 87.305  113.792 88.188  1.00 40.02  ? 325 GLN A NE2 1 
ATOM   2455 N  N   . TYR A 1 326 ? 88.403  118.367 90.695  1.00 30.56  ? 326 TYR A N   1 
ATOM   2456 C  CA  . TYR A 1 326 ? 87.275  119.214 90.338  1.00 34.74  ? 326 TYR A CA  1 
ATOM   2457 C  C   . TYR A 1 326 ? 87.641  120.655 90.009  1.00 39.62  ? 326 TYR A C   1 
ATOM   2458 O  O   . TYR A 1 326 ? 86.780  121.388 89.511  1.00 41.54  ? 326 TYR A O   1 
ATOM   2459 C  CB  . TYR A 1 326 ? 86.235  119.208 91.469  1.00 36.04  ? 326 TYR A CB  1 
ATOM   2460 C  CG  . TYR A 1 326 ? 85.479  117.904 91.587  1.00 40.32  ? 326 TYR A CG  1 
ATOM   2461 C  CD1 . TYR A 1 326 ? 84.478  117.577 90.684  1.00 37.07  ? 326 TYR A CD1 1 
ATOM   2462 C  CD2 . TYR A 1 326 ? 85.769  116.999 92.599  1.00 39.13  ? 326 TYR A CD2 1 
ATOM   2463 C  CE1 . TYR A 1 326 ? 83.786  116.389 90.785  1.00 37.27  ? 326 TYR A CE1 1 
ATOM   2464 C  CE2 . TYR A 1 326 ? 85.082  115.807 92.708  1.00 35.71  ? 326 TYR A CE2 1 
ATOM   2465 C  CZ  . TYR A 1 326 ? 84.092  115.508 91.798  1.00 41.29  ? 326 TYR A CZ  1 
ATOM   2466 O  OH  . TYR A 1 326 ? 83.403  114.323 91.901  1.00 44.04  ? 326 TYR A OH  1 
ATOM   2467 N  N   . LEU A 1 327 ? 88.876  121.089 90.264  1.00 32.50  ? 327 LEU A N   1 
ATOM   2468 C  CA  . LEU A 1 327 ? 89.274  122.457 89.967  1.00 33.77  ? 327 LEU A CA  1 
ATOM   2469 C  C   . LEU A 1 327 ? 90.443  122.550 88.996  1.00 37.59  ? 327 LEU A C   1 
ATOM   2470 O  O   . LEU A 1 327 ? 90.928  123.657 88.741  1.00 40.19  ? 327 LEU A O   1 
ATOM   2471 C  CB  . LEU A 1 327 ? 89.628  123.204 91.262  1.00 33.54  ? 327 LEU A CB  1 
ATOM   2472 C  CG  . LEU A 1 327 ? 88.512  123.380 92.297  1.00 36.19  ? 327 LEU A CG  1 
ATOM   2473 C  CD1 . LEU A 1 327 ? 89.065  123.940 93.596  1.00 33.05  ? 327 LEU A CD1 1 
ATOM   2474 C  CD2 . LEU A 1 327 ? 87.408  124.270 91.758  1.00 28.53  ? 327 LEU A CD2 1 
ATOM   2475 N  N   . CYS A 1 328 ? 90.899  121.435 88.445  1.00 36.64  ? 328 CYS A N   1 
ATOM   2476 C  CA  . CYS A 1 328 ? 92.055  121.374 87.567  1.00 29.15  ? 328 CYS A CA  1 
ATOM   2477 C  C   . CYS A 1 328 ? 91.724  120.527 86.351  1.00 41.84  ? 328 CYS A C   1 
ATOM   2478 O  O   . CYS A 1 328 ? 90.804  119.703 86.390  1.00 44.37  ? 328 CYS A O   1 
ATOM   2479 C  CB  . CYS A 1 328 ? 93.270  120.781 88.296  1.00 24.90  ? 328 CYS A CB  1 
ATOM   2480 S  SG  . CYS A 1 328 ? 93.930  121.807 89.624  1.00 41.12  ? 328 CYS A SG  1 
ATOM   2481 N  N   . PRO A 1 329 ? 92.447  120.716 85.240  1.00 48.96  ? 329 PRO A N   1 
ATOM   2482 C  CA  . PRO A 1 329 ? 92.265  119.828 84.083  1.00 46.26  ? 329 PRO A CA  1 
ATOM   2483 C  C   . PRO A 1 329 ? 92.712  118.400 84.366  1.00 48.58  ? 329 PRO A C   1 
ATOM   2484 O  O   . PRO A 1 329 ? 93.210  118.102 85.456  1.00 54.78  ? 329 PRO A O   1 
ATOM   2485 C  CB  . PRO A 1 329 ? 93.127  120.485 82.997  1.00 42.42  ? 329 PRO A CB  1 
ATOM   2486 C  CG  . PRO A 1 329 ? 93.254  121.904 83.419  1.00 45.23  ? 329 PRO A CG  1 
ATOM   2487 C  CD  . PRO A 1 329 ? 93.291  121.877 84.914  1.00 43.42  ? 329 PRO A CD  1 
ATOM   2488 N  N   . VAL A 1 330 ? 92.542  117.509 83.386  1.00 47.19  ? 330 VAL A N   1 
ATOM   2489 C  CA  . VAL A 1 330 ? 92.785  116.087 83.619  1.00 51.93  ? 330 VAL A CA  1 
ATOM   2490 C  C   . VAL A 1 330 ? 94.276  115.800 83.791  1.00 55.22  ? 330 VAL A C   1 
ATOM   2491 O  O   . VAL A 1 330 ? 94.675  115.035 84.681  1.00 60.03  ? 330 VAL A O   1 
ATOM   2492 C  CB  . VAL A 1 330 ? 92.163  115.250 82.485  1.00 49.21  ? 330 VAL A CB  1 
ATOM   2493 C  CG1 . VAL A 1 330 ? 90.649  115.337 82.540  1.00 45.54  ? 330 VAL A CG1 1 
ATOM   2494 C  CG2 . VAL A 1 330 ? 92.655  115.728 81.131  1.00 54.76  ? 330 VAL A CG2 1 
ATOM   2495 N  N   . TYR A 1 331 ? 95.124  116.402 82.952  1.00 41.19  ? 331 TYR A N   1 
ATOM   2496 C  CA  . TYR A 1 331 ? 96.547  116.088 83.018  1.00 43.33  ? 331 TYR A CA  1 
ATOM   2497 C  C   . TYR A 1 331 ? 97.185  116.625 84.294  1.00 49.34  ? 331 TYR A C   1 
ATOM   2498 O  O   . TYR A 1 331 ? 98.089  115.988 84.845  1.00 53.53  ? 331 TYR A O   1 
ATOM   2499 C  CB  . TYR A 1 331 ? 97.280  116.603 81.773  1.00 46.59  ? 331 TYR A CB  1 
ATOM   2500 C  CG  . TYR A 1 331 ? 96.802  117.922 81.196  1.00 51.51  ? 331 TYR A CG  1 
ATOM   2501 C  CD1 . TYR A 1 331 ? 95.633  117.999 80.446  1.00 50.99  ? 331 TYR A CD1 1 
ATOM   2502 C  CD2 . TYR A 1 331 ? 97.546  119.082 81.364  1.00 51.35  ? 331 TYR A CD2 1 
ATOM   2503 C  CE1 . TYR A 1 331 ? 95.205  119.198 79.911  1.00 51.04  ? 331 TYR A CE1 1 
ATOM   2504 C  CE2 . TYR A 1 331 ? 97.126  120.285 80.829  1.00 50.19  ? 331 TYR A CE2 1 
ATOM   2505 C  CZ  . TYR A 1 331 ? 95.956  120.337 80.105  1.00 53.43  ? 331 TYR A CZ  1 
ATOM   2506 O  OH  . TYR A 1 331 ? 95.537  121.534 79.573  1.00 51.38  ? 331 TYR A OH  1 
ATOM   2507 N  N   . ILE A 1 332 ? 96.723  117.773 84.793  1.00 39.98  ? 332 ILE A N   1 
ATOM   2508 C  CA  . ILE A 1 332 ? 97.199  118.253 86.087  1.00 40.22  ? 332 ILE A CA  1 
ATOM   2509 C  C   . ILE A 1 332 ? 96.764  117.303 87.198  1.00 39.21  ? 332 ILE A C   1 
ATOM   2510 O  O   . ILE A 1 332 ? 97.503  117.069 88.164  1.00 45.17  ? 332 ILE A O   1 
ATOM   2511 C  CB  . ILE A 1 332 ? 96.714  119.693 86.333  1.00 44.15  ? 332 ILE A CB  1 
ATOM   2512 C  CG1 . ILE A 1 332 ? 97.524  120.676 85.489  1.00 41.98  ? 332 ILE A CG1 1 
ATOM   2513 C  CG2 . ILE A 1 332 ? 96.834  120.065 87.795  1.00 45.83  ? 332 ILE A CG2 1 
ATOM   2514 C  CD1 . ILE A 1 332 ? 96.860  121.052 84.197  1.00 42.58  ? 332 ILE A CD1 1 
ATOM   2515 N  N   . SER A 1 333 ? 95.565  116.728 87.071  1.00 35.14  ? 333 SER A N   1 
ATOM   2516 C  CA  . SER A 1 333 ? 95.116  115.730 88.036  1.00 37.94  ? 333 SER A CA  1 
ATOM   2517 C  C   . SER A 1 333 ? 96.037  114.518 88.037  1.00 43.45  ? 333 SER A C   1 
ATOM   2518 O  O   . SER A 1 333 ? 96.383  113.990 89.101  1.00 45.30  ? 333 SER A O   1 
ATOM   2519 C  CB  . SER A 1 333 ? 93.680  115.309 87.724  1.00 37.66  ? 333 SER A CB  1 
ATOM   2520 O  OG  . SER A 1 333 ? 92.849  116.436 87.515  1.00 41.27  ? 333 SER A OG  1 
ATOM   2521 N  N   . PHE A 1 334 ? 96.448  114.064 86.851  1.00 38.91  ? 334 PHE A N   1 
ATOM   2522 C  CA  . PHE A 1 334 ? 97.354  112.921 86.778  1.00 35.73  ? 334 PHE A CA  1 
ATOM   2523 C  C   . PHE A 1 334 ? 98.738  113.270 87.319  1.00 41.21  ? 334 PHE A C   1 
ATOM   2524 O  O   . PHE A 1 334 ? 99.398  112.428 87.942  1.00 46.92  ? 334 PHE A O   1 
ATOM   2525 C  CB  . PHE A 1 334 ? 97.432  112.413 85.342  1.00 37.78  ? 334 PHE A CB  1 
ATOM   2526 C  CG  . PHE A 1 334 ? 96.161  111.772 84.867  1.00 44.90  ? 334 PHE A CG  1 
ATOM   2527 C  CD1 . PHE A 1 334 ? 95.538  110.799 85.630  1.00 46.15  ? 334 PHE A CD1 1 
ATOM   2528 C  CD2 . PHE A 1 334 ? 95.580  112.153 83.672  1.00 46.18  ? 334 PHE A CD2 1 
ATOM   2529 C  CE1 . PHE A 1 334 ? 94.364  110.212 85.204  1.00 45.87  ? 334 PHE A CE1 1 
ATOM   2530 C  CE2 . PHE A 1 334 ? 94.406  111.569 83.241  1.00 45.77  ? 334 PHE A CE2 1 
ATOM   2531 C  CZ  . PHE A 1 334 ? 93.797  110.598 84.008  1.00 47.07  ? 334 PHE A CZ  1 
ATOM   2532 N  N   . PHE A 1 335 ? 99.191  114.506 87.097  1.00 34.04  ? 335 PHE A N   1 
ATOM   2533 C  CA  . PHE A 1 335 ? 100.446 114.957 87.695  1.00 30.55  ? 335 PHE A CA  1 
ATOM   2534 C  C   . PHE A 1 335 ? 100.380 114.909 89.218  1.00 36.83  ? 335 PHE A C   1 
ATOM   2535 O  O   . PHE A 1 335 ? 101.317 114.439 89.878  1.00 41.71  ? 335 PHE A O   1 
ATOM   2536 C  CB  . PHE A 1 335 ? 100.770 116.375 87.225  1.00 31.72  ? 335 PHE A CB  1 
ATOM   2537 C  CG  . PHE A 1 335 ? 101.644 116.434 86.007  1.00 38.99  ? 335 PHE A CG  1 
ATOM   2538 C  CD1 . PHE A 1 335 ? 103.021 116.385 86.123  1.00 41.04  ? 335 PHE A CD1 1 
ATOM   2539 C  CD2 . PHE A 1 335 ? 101.090 116.551 84.745  1.00 39.74  ? 335 PHE A CD2 1 
ATOM   2540 C  CE1 . PHE A 1 335 ? 103.826 116.444 85.004  1.00 43.01  ? 335 PHE A CE1 1 
ATOM   2541 C  CE2 . PHE A 1 335 ? 101.889 116.610 83.622  1.00 37.06  ? 335 PHE A CE2 1 
ATOM   2542 C  CZ  . PHE A 1 335 ? 103.259 116.556 83.752  1.00 41.45  ? 335 PHE A CZ  1 
ATOM   2543 N  N   . GLY A 1 336 ? 99.277  115.393 89.793  1.00 28.30  ? 336 GLY A N   1 
ATOM   2544 C  CA  . GLY A 1 336 ? 99.115  115.326 91.238  1.00 26.62  ? 336 GLY A CA  1 
ATOM   2545 C  C   . GLY A 1 336 ? 99.044  113.901 91.756  1.00 36.64  ? 336 GLY A C   1 
ATOM   2546 O  O   . GLY A 1 336 ? 99.580  113.589 92.824  1.00 42.55  ? 336 GLY A O   1 
ATOM   2547 N  N   . LEU A 1 337 ? 98.374  113.020 91.009  1.00 29.55  ? 337 LEU A N   1 
ATOM   2548 C  CA  . LEU A 1 337 ? 98.322  111.612 91.392  1.00 28.85  ? 337 LEU A CA  1 
ATOM   2549 C  C   . LEU A 1 337 ? 99.715  110.995 91.411  1.00 33.58  ? 337 LEU A C   1 
ATOM   2550 O  O   . LEU A 1 337 ? 100.065 110.254 92.341  1.00 35.54  ? 337 LEU A O   1 
ATOM   2551 C  CB  . LEU A 1 337 ? 97.405  110.847 90.438  1.00 27.47  ? 337 LEU A CB  1 
ATOM   2552 C  CG  . LEU A 1 337 ? 97.156  109.370 90.746  1.00 34.37  ? 337 LEU A CG  1 
ATOM   2553 C  CD1 . LEU A 1 337 ? 96.747  109.182 92.198  1.00 32.99  ? 337 LEU A CD1 1 
ATOM   2554 C  CD2 . LEU A 1 337 ? 96.104  108.800 89.810  1.00 30.55  ? 337 LEU A CD2 1 
ATOM   2555 N  N   . GLY A 1 338 ? 100.527 111.293 90.394  1.00 25.66  ? 338 GLY A N   1 
ATOM   2556 C  CA  . GLY A 1 338 ? 101.896 110.805 90.385  1.00 22.26  ? 338 GLY A CA  1 
ATOM   2557 C  C   . GLY A 1 338 ? 102.714 111.348 91.542  1.00 28.19  ? 338 GLY A C   1 
ATOM   2558 O  O   . GLY A 1 338 ? 103.523 110.629 92.136  1.00 37.57  ? 338 GLY A O   1 
ATOM   2559 N  N   . ALA A 1 339 ? 102.511 112.625 91.879  1.00 20.34  ? 339 ALA A N   1 
ATOM   2560 C  CA  . ALA A 1 339 ? 103.209 113.207 93.021  1.00 17.19  ? 339 ALA A CA  1 
ATOM   2561 C  C   . ALA A 1 339 ? 102.855 112.485 94.317  1.00 19.80  ? 339 ALA A C   1 
ATOM   2562 O  O   . ALA A 1 339 ? 103.739 112.172 95.126  1.00 24.64  ? 339 ALA A O   1 
ATOM   2563 C  CB  . ALA A 1 339 ? 102.881 114.694 93.132  1.00 18.25  ? 339 ALA A CB  1 
ATOM   2564 N  N   . VAL A 1 340 ? 101.567 112.203 94.527  1.00 21.26  ? 340 VAL A N   1 
ATOM   2565 C  CA  . VAL A 1 340 ? 101.149 111.511 95.745  1.00 24.75  ? 340 VAL A CA  1 
ATOM   2566 C  C   . VAL A 1 340 ? 101.710 110.091 95.782  1.00 26.78  ? 340 VAL A C   1 
ATOM   2567 O  O   . VAL A 1 340 ? 102.146 109.608 96.836  1.00 25.84  ? 340 VAL A O   1 
ATOM   2568 C  CB  . VAL A 1 340 ? 99.614  111.525 95.871  1.00 22.29  ? 340 VAL A CB  1 
ATOM   2569 C  CG1 . VAL A 1 340 ? 99.174  110.792 97.126  1.00 19.26  ? 340 VAL A CG1 1 
ATOM   2570 C  CG2 . VAL A 1 340 ? 99.104  112.949 95.901  1.00 17.23  ? 340 VAL A CG2 1 
ATOM   2571 N  N   . SER A 1 341 ? 101.707 109.398 94.638  1.00 19.94  ? 341 SER A N   1 
ATOM   2572 C  CA  . SER A 1 341 ? 102.255 108.044 94.590  1.00 16.55  ? 341 SER A CA  1 
ATOM   2573 C  C   . SER A 1 341 ? 103.739 108.034 94.941  1.00 22.08  ? 341 SER A C   1 
ATOM   2574 O  O   . SER A 1 341 ? 104.204 107.190 95.721  1.00 30.06  ? 341 SER A O   1 
ATOM   2575 C  CB  . SER A 1 341 ? 102.031 107.439 93.204  1.00 22.84  ? 341 SER A CB  1 
ATOM   2576 O  OG  . SER A 1 341 ? 100.655 107.222 92.954  1.00 37.29  ? 341 SER A OG  1 
ATOM   2577 N  N   . ALA A 1 342 ? 104.501 108.969 94.366  1.00 16.36  ? 342 ALA A N   1 
ATOM   2578 C  CA  . ALA A 1 342 ? 105.927 109.050 94.666  1.00 18.76  ? 342 ALA A CA  1 
ATOM   2579 C  C   . ALA A 1 342 ? 106.163 109.364 96.136  1.00 17.32  ? 342 ALA A C   1 
ATOM   2580 O  O   . ALA A 1 342 ? 107.059 108.786 96.768  1.00 18.10  ? 342 ALA A O   1 
ATOM   2581 C  CB  . ALA A 1 342 ? 106.588 110.103 93.778  1.00 12.13  ? 342 ALA A CB  1 
ATOM   2582 N  N   . ALA A 1 343 ? 105.362 110.273 96.701  1.00 17.23  ? 343 ALA A N   1 
ATOM   2583 C  CA  . ALA A 1 343 ? 105.499 110.611 98.113  1.00 7.15   ? 343 ALA A CA  1 
ATOM   2584 C  C   . ALA A 1 343 ? 105.242 109.402 99.002  1.00 14.37  ? 343 ALA A C   1 
ATOM   2585 O  O   . ALA A 1 343 ? 105.941 109.199 100.001 1.00 19.00  ? 343 ALA A O   1 
ATOM   2586 C  CB  . ALA A 1 343 ? 104.552 111.753 98.474  1.00 14.30  ? 343 ALA A CB  1 
ATOM   2587 N  N   . VAL A 1 344 ? 104.237 108.594 98.664  1.00 20.30  ? 344 VAL A N   1 
ATOM   2588 C  CA  . VAL A 1 344 ? 103.931 107.417 99.476  1.00 20.38  ? 344 VAL A CA  1 
ATOM   2589 C  C   . VAL A 1 344 ? 105.057 106.390 99.385  1.00 16.32  ? 344 VAL A C   1 
ATOM   2590 O  O   . VAL A 1 344 ? 105.499 105.834 100.401 1.00 19.94  ? 344 VAL A O   1 
ATOM   2591 C  CB  . VAL A 1 344 ? 102.577 106.815 99.056  1.00 14.43  ? 344 VAL A CB  1 
ATOM   2592 C  CG1 . VAL A 1 344 ? 102.392 105.436 99.666  1.00 9.47   ? 344 VAL A CG1 1 
ATOM   2593 C  CG2 . VAL A 1 344 ? 101.441 107.735 99.462  1.00 18.34  ? 344 VAL A CG2 1 
ATOM   2594 N  N   . MET A 1 345 ? 105.538 106.123 98.166  1.00 13.51  ? 345 MET A N   1 
ATOM   2595 C  CA  . MET A 1 345 ? 106.544 105.077 97.990  1.00 12.50  ? 345 MET A CA  1 
ATOM   2596 C  C   . MET A 1 345 ? 107.875 105.451 98.635  1.00 18.75  ? 345 MET A C   1 
ATOM   2597 O  O   . MET A 1 345 ? 108.548 104.590 99.225  1.00 19.02  ? 345 MET A O   1 
ATOM   2598 C  CB  . MET A 1 345 ? 106.731 104.770 96.507  1.00 14.74  ? 345 MET A CB  1 
ATOM   2599 C  CG  . MET A 1 345 ? 105.775 103.718 95.983  1.00 22.39  ? 345 MET A CG  1 
ATOM   2600 S  SD  . MET A 1 345 ? 106.235 103.117 94.351  1.00 54.75  ? 345 MET A SD  1 
ATOM   2601 C  CE  . MET A 1 345 ? 104.811 103.634 93.409  1.00 27.13  ? 345 MET A CE  1 
ATOM   2602 N  N   . SER A 1 346 ? 108.305 106.704 98.523  1.00 22.08  ? 346 SER A N   1 
ATOM   2603 C  CA  . SER A 1 346 ? 109.565 107.161 99.118  1.00 8.25   ? 346 SER A CA  1 
ATOM   2604 C  C   . SER A 1 346 ? 109.631 107.003 100.630 1.00 10.49  ? 346 SER A C   1 
ATOM   2605 O  O   . SER A 1 346 ? 110.718 107.030 101.192 1.00 14.98  ? 346 SER A O   1 
ATOM   2606 C  CB  . SER A 1 346 ? 109.849 108.594 98.694  1.00 19.10  ? 346 SER A CB  1 
ATOM   2607 O  OG  . SER A 1 346 ? 108.799 109.454 99.088  1.00 23.80  ? 346 SER A OG  1 
ATOM   2608 N  N   . SER A 1 347 ? 108.493 106.868 101.301 1.00 7.18   ? 347 SER A N   1 
ATOM   2609 C  CA  . SER A 1 347 ? 108.468 106.583 102.729 1.00 11.79  ? 347 SER A CA  1 
ATOM   2610 C  C   . SER A 1 347 ? 108.242 105.109 103.027 1.00 19.51  ? 347 SER A C   1 
ATOM   2611 O  O   . SER A 1 347 ? 108.824 104.575 103.982 1.00 22.14  ? 347 SER A O   1 
ATOM   2612 C  CB  . SER A 1 347 ? 107.377 107.413 103.413 1.00 17.64  ? 347 SER A CB  1 
ATOM   2613 O  OG  . SER A 1 347 ? 107.663 108.796 103.341 1.00 10.17  ? 347 SER A OG  1 
ATOM   2614 N  N   . ALA A 1 348 ? 107.409 104.436 102.226 1.00 18.58  ? 348 ALA A N   1 
ATOM   2615 C  CA  . ALA A 1 348 ? 107.141 103.022 102.468 1.00 10.90  ? 348 ALA A CA  1 
ATOM   2616 C  C   . ALA A 1 348 ? 108.400 102.179 102.302 1.00 14.91  ? 348 ALA A C   1 
ATOM   2617 O  O   . ALA A 1 348 ? 108.668 101.281 103.117 1.00 24.37  ? 348 ALA A O   1 
ATOM   2618 C  CB  . ALA A 1 348 ? 106.035 102.532 101.538 1.00 13.29  ? 348 ALA A CB  1 
ATOM   2619 N  N   . ASP A 1 349 ? 109.188 102.447 101.254 1.00 11.04  ? 349 ASP A N   1 
ATOM   2620 C  CA  . ASP A 1 349 ? 110.394 101.648 101.045 1.00 12.43  ? 349 ASP A CA  1 
ATOM   2621 C  C   . ASP A 1 349 ? 111.382 101.833 102.192 1.00 15.47  ? 349 ASP A C   1 
ATOM   2622 O  O   . ASP A 1 349 ? 112.003 100.865 102.652 1.00 13.57  ? 349 ASP A O   1 
ATOM   2623 C  CB  . ASP A 1 349 ? 111.041 101.987 99.698  1.00 11.63  ? 349 ASP A CB  1 
ATOM   2624 C  CG  . ASP A 1 349 ? 111.452 103.443 99.581  1.00 18.76  ? 349 ASP A CG  1 
ATOM   2625 O  OD1 . ASP A 1 349 ? 111.328 104.194 100.567 1.00 22.30  ? 349 ASP A OD1 1 
ATOM   2626 O  OD2 . ASP A 1 349 ? 111.912 103.837 98.491  1.00 23.74  ? 349 ASP A OD2 1 
ATOM   2627 N  N   . SER A 1 350 ? 111.531 103.070 102.672 1.00 13.88  ? 350 SER A N   1 
ATOM   2628 C  CA  . SER A 1 350 ? 112.434 103.337 103.787 1.00 7.77   ? 350 SER A CA  1 
ATOM   2629 C  C   . SER A 1 350 ? 111.968 102.641 105.058 1.00 11.31  ? 350 SER A C   1 
ATOM   2630 O  O   . SER A 1 350 ? 112.784 102.088 105.801 1.00 22.61  ? 350 SER A O   1 
ATOM   2631 C  CB  . SER A 1 350 ? 112.557 104.841 104.015 1.00 18.68  ? 350 SER A CB  1 
ATOM   2632 O  OG  . SER A 1 350 ? 112.907 105.511 102.819 1.00 18.93  ? 350 SER A OG  1 
ATOM   2633 N  N   . SER A 1 351 ? 110.654 102.655 105.297 1.00 16.13  ? 351 SER A N   1 
ATOM   2634 C  CA  . SER A 1 351 ? 110.091 101.989 106.501 1.00 10.21  ? 351 SER A CA  1 
ATOM   2635 C  C   . SER A 1 351 ? 110.393 100.488 106.451 1.00 15.76  ? 351 SER A C   1 
ATOM   2636 O  O   . SER A 1 351 ? 110.848 99.945  107.477 1.00 16.23  ? 351 SER A O   1 
ATOM   2637 C  CB  . SER A 1 351 ? 108.611 102.244 106.615 1.00 11.59  ? 351 SER A CB  1 
ATOM   2638 O  OG  . SER A 1 351 ? 108.340 103.638 106.648 1.00 31.73  ? 351 SER A OG  1 
ATOM   2639 N  N   . ILE A 1 352 ? 110.154 99.849  105.301 1.00 14.60  ? 352 ILE A N   1 
ATOM   2640 C  CA  . ILE A 1 352 ? 110.366 98.408  105.178 1.00 7.28   ? 352 ILE A CA  1 
ATOM   2641 C  C   . ILE A 1 352 ? 111.845 98.067  105.326 1.00 13.81  ? 352 ILE A C   1 
ATOM   2642 O  O   . ILE A 1 352 ? 112.212 97.123  106.044 1.00 25.25  ? 352 ILE A O   1 
ATOM   2643 C  CB  . ILE A 1 352 ? 109.785 97.894  103.848 1.00 14.80  ? 352 ILE A CB  1 
ATOM   2644 C  CG1 . ILE A 1 352 ? 108.259 97.835  103.929 1.00 12.03  ? 352 ILE A CG1 1 
ATOM   2645 C  CG2 . ILE A 1 352 ? 110.346 96.524  103.506 1.00 17.28  ? 352 ILE A CG2 1 
ATOM   2646 C  CD1 . ILE A 1 352 ? 107.570 97.868  102.587 1.00 8.92   ? 352 ILE A CD1 1 
ATOM   2647 N  N   . LEU A 1 353 ? 112.719 98.835  104.665 1.00 16.06  ? 353 LEU A N   1 
ATOM   2648 C  CA  . LEU A 1 353 ? 114.153 98.589  104.778 1.00 12.06  ? 353 LEU A CA  1 
ATOM   2649 C  C   . LEU A 1 353 ? 114.635 98.754  106.212 1.00 5.53   ? 353 LEU A C   1 
ATOM   2650 O  O   . LEU A 1 353 ? 115.441 97.954  106.696 1.00 14.02  ? 353 LEU A O   1 
ATOM   2651 C  CB  . LEU A 1 353 ? 114.923 99.526  103.849 1.00 7.81   ? 353 LEU A CB  1 
ATOM   2652 C  CG  . LEU A 1 353 ? 116.450 99.515  103.968 1.00 15.45  ? 353 LEU A CG  1 
ATOM   2653 C  CD1 . LEU A 1 353 ? 117.022 98.137  103.676 1.00 9.31   ? 353 LEU A CD1 1 
ATOM   2654 C  CD2 . LEU A 1 353 ? 117.066 100.558 103.057 1.00 21.92  ? 353 LEU A CD2 1 
ATOM   2655 N  N   . SER A 1 354 ? 114.151 99.784  106.908 1.00 18.61  ? 354 SER A N   1 
ATOM   2656 C  CA  . SER A 1 354 ? 114.572 100.024 108.284 1.00 17.71  ? 354 SER A CA  1 
ATOM   2657 C  C   . SER A 1 354 ? 114.174 98.871  109.196 1.00 15.78  ? 354 SER A C   1 
ATOM   2658 O  O   . SER A 1 354 ? 114.988 98.381  109.991 1.00 19.27  ? 354 SER A O   1 
ATOM   2659 C  CB  . SER A 1 354 ? 113.968 101.337 108.780 1.00 22.81  ? 354 SER A CB  1 
ATOM   2660 O  OG  . SER A 1 354 ? 113.757 101.307 110.178 1.00 29.53  ? 354 SER A OG  1 
ATOM   2661 N  N   . ALA A 1 355 ? 112.920 98.424  109.096 1.00 20.28  ? 355 ALA A N   1 
ATOM   2662 C  CA  . ALA A 1 355 ? 112.473 97.329  109.950 1.00 22.62  ? 355 ALA A CA  1 
ATOM   2663 C  C   . ALA A 1 355 ? 113.246 96.047  109.662 1.00 23.54  ? 355 ALA A C   1 
ATOM   2664 O  O   . ALA A 1 355 ? 113.679 95.349  110.591 1.00 24.09  ? 355 ALA A O   1 
ATOM   2665 C  CB  . ALA A 1 355 ? 110.977 97.102  109.774 1.00 17.34  ? 355 ALA A CB  1 
ATOM   2666 N  N   . SER A 1 356 ? 113.434 95.723  108.378 1.00 25.09  ? 356 SER A N   1 
ATOM   2667 C  CA  . SER A 1 356 ? 114.165 94.510  108.028 1.00 19.64  ? 356 SER A CA  1 
ATOM   2668 C  C   . SER A 1 356 ? 115.610 94.573  108.503 1.00 23.91  ? 356 SER A C   1 
ATOM   2669 O  O   . SER A 1 356 ? 116.150 93.578  109.001 1.00 24.29  ? 356 SER A O   1 
ATOM   2670 C  CB  . SER A 1 356 ? 114.105 94.282  106.521 1.00 19.67  ? 356 SER A CB  1 
ATOM   2671 O  OG  . SER A 1 356 ? 112.774 94.375  106.050 1.00 28.62  ? 356 SER A OG  1 
ATOM   2672 N  N   . SER A 1 357 ? 116.257 95.733  108.348 1.00 31.06  ? 357 SER A N   1 
ATOM   2673 C  CA  . SER A 1 357 ? 117.631 95.889  108.808 1.00 12.33  ? 357 SER A CA  1 
ATOM   2674 C  C   . SER A 1 357 ? 117.729 95.675  110.309 1.00 14.03  ? 357 SER A C   1 
ATOM   2675 O  O   . SER A 1 357 ? 118.573 94.904  110.783 1.00 16.84  ? 357 SER A O   1 
ATOM   2676 C  CB  . SER A 1 357 ? 118.155 97.275  108.435 1.00 12.48  ? 357 SER A CB  1 
ATOM   2677 O  OG  . SER A 1 357 ? 118.120 97.479  107.037 1.00 22.42  ? 357 SER A OG  1 
ATOM   2678 N  N   . MET A 1 358 ? 116.860 96.342  111.075 1.00 28.54  ? 358 MET A N   1 
ATOM   2679 C  CA  . MET A 1 358 ? 116.877 96.172  112.525 1.00 28.26  ? 358 MET A CA  1 
ATOM   2680 C  C   . MET A 1 358 ? 116.729 94.704  112.900 1.00 29.49  ? 358 MET A C   1 
ATOM   2681 O  O   . MET A 1 358 ? 117.557 94.155  113.640 1.00 32.46  ? 358 MET A O   1 
ATOM   2682 C  CB  . MET A 1 358 ? 115.766 96.999  113.171 1.00 28.98  ? 358 MET A CB  1 
ATOM   2683 C  CG  . MET A 1 358 ? 116.246 98.222  113.927 1.00 26.62  ? 358 MET A CG  1 
ATOM   2684 S  SD  . MET A 1 358 ? 114.904 99.082  114.769 1.00 49.84  ? 358 MET A SD  1 
ATOM   2685 C  CE  . MET A 1 358 ? 113.802 99.437  113.405 1.00 26.00  ? 358 MET A CE  1 
ATOM   2686 N  N   . PHE A 1 359 ? 115.697 94.042  112.369 1.00 32.16  ? 359 PHE A N   1 
ATOM   2687 C  CA  . PHE A 1 359 ? 115.463 92.642  112.710 1.00 25.71  ? 359 PHE A CA  1 
ATOM   2688 C  C   . PHE A 1 359 ? 116.678 91.785  112.377 1.00 32.54  ? 359 PHE A C   1 
ATOM   2689 O  O   . PHE A 1 359 ? 117.300 91.194  113.267 1.00 32.53  ? 359 PHE A O   1 
ATOM   2690 C  CB  . PHE A 1 359 ? 114.223 92.116  111.985 1.00 19.90  ? 359 PHE A CB  1 
ATOM   2691 C  CG  . PHE A 1 359 ? 113.988 90.644  112.181 1.00 27.19  ? 359 PHE A CG  1 
ATOM   2692 C  CD1 . PHE A 1 359 ? 113.536 90.157  113.394 1.00 33.97  ? 359 PHE A CD1 1 
ATOM   2693 C  CD2 . PHE A 1 359 ? 114.226 89.747  111.155 1.00 32.92  ? 359 PHE A CD2 1 
ATOM   2694 C  CE1 . PHE A 1 359 ? 113.324 88.805  113.579 1.00 31.63  ? 359 PHE A CE1 1 
ATOM   2695 C  CE2 . PHE A 1 359 ? 114.015 88.394  111.334 1.00 32.16  ? 359 PHE A CE2 1 
ATOM   2696 C  CZ  . PHE A 1 359 ? 113.564 87.923  112.548 1.00 27.17  ? 359 PHE A CZ  1 
ATOM   2697 N  N   . ALA A 1 360 ? 117.057 91.744  111.097 1.00 40.23  ? 360 ALA A N   1 
ATOM   2698 C  CA  . ALA A 1 360 ? 118.088 90.811  110.657 1.00 28.93  ? 360 ALA A CA  1 
ATOM   2699 C  C   . ALA A 1 360 ? 119.419 91.069  111.349 1.00 34.59  ? 360 ALA A C   1 
ATOM   2700 O  O   . ALA A 1 360 ? 120.129 90.122  111.708 1.00 35.88  ? 360 ALA A O   1 
ATOM   2701 C  CB  . ALA A 1 360 ? 118.251 90.889  109.142 1.00 27.16  ? 360 ALA A CB  1 
ATOM   2702 N  N   . ARG A 1 361 ? 119.787 92.338  111.544 1.00 39.83  ? 361 ARG A N   1 
ATOM   2703 C  CA  . ARG A 1 361 ? 121.085 92.626  112.138 1.00 30.49  ? 361 ARG A CA  1 
ATOM   2704 C  C   . ARG A 1 361 ? 121.099 92.342  113.635 1.00 37.47  ? 361 ARG A C   1 
ATOM   2705 O  O   . ARG A 1 361 ? 122.062 91.759  114.145 1.00 39.57  ? 361 ARG A O   1 
ATOM   2706 C  CB  . ARG A 1 361 ? 121.479 94.076  111.859 1.00 33.88  ? 361 ARG A CB  1 
ATOM   2707 C  CG  . ARG A 1 361 ? 122.441 94.671  112.875 1.00 40.00  ? 361 ARG A CG  1 
ATOM   2708 C  CD  . ARG A 1 361 ? 123.872 94.244  112.608 1.00 32.03  ? 361 ARG A CD  1 
ATOM   2709 N  NE  . ARG A 1 361 ? 124.796 94.810  113.582 1.00 38.95  ? 361 ARG A NE  1 
ATOM   2710 C  CZ  . ARG A 1 361 ? 126.111 94.638  113.555 1.00 43.39  ? 361 ARG A CZ  1 
ATOM   2711 N  NH1 . ARG A 1 361 ? 126.694 93.915  112.614 1.00 35.40  ? 361 ARG A NH1 1 
ATOM   2712 N  NH2 . ARG A 1 361 ? 126.859 95.206  114.496 1.00 37.12  ? 361 ARG A NH2 1 
ATOM   2713 N  N   . ASN A 1 362 ? 120.048 92.729  114.362 1.00 34.19  ? 362 ASN A N   1 
ATOM   2714 C  CA  . ASN A 1 362 ? 120.145 92.744  115.814 1.00 31.64  ? 362 ASN A CA  1 
ATOM   2715 C  C   . ASN A 1 362 ? 119.491 91.556  116.504 1.00 36.59  ? 362 ASN A C   1 
ATOM   2716 O  O   . ASN A 1 362 ? 119.973 91.143  117.562 1.00 39.89  ? 362 ASN A O   1 
ATOM   2717 C  CB  . ASN A 1 362 ? 119.544 94.039  116.367 1.00 31.98  ? 362 ASN A CB  1 
ATOM   2718 C  CG  . ASN A 1 362 ? 120.516 95.197  116.309 1.00 32.74  ? 362 ASN A CG  1 
ATOM   2719 O  OD1 . ASN A 1 362 ? 120.353 96.116  115.511 1.00 30.76  ? 362 ASN A OD1 1 
ATOM   2720 N  ND2 . ASN A 1 362 ? 121.538 95.157  117.153 1.00 32.97  ? 362 ASN A ND2 1 
ATOM   2721 N  N   . ILE A 1 363 ? 118.413 90.988  115.963 1.00 39.48  ? 363 ILE A N   1 
ATOM   2722 C  CA  . ILE A 1 363 ? 117.752 89.898  116.668 1.00 37.96  ? 363 ILE A CA  1 
ATOM   2723 C  C   . ILE A 1 363 ? 118.349 88.571  116.225 1.00 39.09  ? 363 ILE A C   1 
ATOM   2724 O  O   . ILE A 1 363 ? 119.024 87.897  117.008 1.00 45.60  ? 363 ILE A O   1 
ATOM   2725 C  CB  . ILE A 1 363 ? 116.230 89.926  116.438 1.00 40.82  ? 363 ILE A CB  1 
ATOM   2726 C  CG1 . ILE A 1 363 ? 115.673 91.319  116.737 1.00 35.49  ? 363 ILE A CG1 1 
ATOM   2727 C  CG2 . ILE A 1 363 ? 115.543 88.870  117.287 1.00 38.71  ? 363 ILE A CG2 1 
ATOM   2728 C  CD1 . ILE A 1 363 ? 115.587 91.638  118.209 1.00 34.45  ? 363 ILE A CD1 1 
ATOM   2729 N  N   . TYR A 1 364 ? 118.165 88.226  114.949 1.00 41.30  ? 364 TYR A N   1 
ATOM   2730 C  CA  . TYR A 1 364 ? 118.554 86.903  114.467 1.00 43.24  ? 364 TYR A CA  1 
ATOM   2731 C  C   . TYR A 1 364 ? 120.043 86.651  114.674 1.00 45.35  ? 364 TYR A C   1 
ATOM   2732 O  O   . TYR A 1 364 ? 120.434 85.805  115.489 1.00 44.87  ? 364 TYR A O   1 
ATOM   2733 C  CB  . TYR A 1 364 ? 118.173 86.768  112.990 1.00 41.01  ? 364 TYR A CB  1 
ATOM   2734 C  CG  . TYR A 1 364 ? 118.411 85.405  112.374 1.00 44.39  ? 364 TYR A CG  1 
ATOM   2735 C  CD1 . TYR A 1 364 ? 119.682 85.008  111.978 1.00 48.72  ? 364 TYR A CD1 1 
ATOM   2736 C  CD2 . TYR A 1 364 ? 117.362 84.520  112.177 1.00 45.15  ? 364 TYR A CD2 1 
ATOM   2737 C  CE1 . TYR A 1 364 ? 119.900 83.771  111.412 1.00 44.02  ? 364 TYR A CE1 1 
ATOM   2738 C  CE2 . TYR A 1 364 ? 117.572 83.278  111.611 1.00 41.45  ? 364 TYR A CE2 1 
ATOM   2739 C  CZ  . TYR A 1 364 ? 118.843 82.911  111.231 1.00 45.62  ? 364 TYR A CZ  1 
ATOM   2740 O  OH  . TYR A 1 364 ? 119.062 81.677  110.667 1.00 53.22  ? 364 TYR A OH  1 
ATOM   2741 N  N   . GLN A 1 365 ? 120.889 87.409  113.976 1.00 45.19  ? 365 GLN A N   1 
ATOM   2742 C  CA  . GLN A 1 365 ? 122.325 87.154  113.993 1.00 45.68  ? 365 GLN A CA  1 
ATOM   2743 C  C   . GLN A 1 365 ? 122.945 87.369  115.366 1.00 48.14  ? 365 GLN A C   1 
ATOM   2744 O  O   . GLN A 1 365 ? 123.829 86.604  115.766 1.00 51.33  ? 365 GLN A O   1 
ATOM   2745 C  CB  . GLN A 1 365 ? 123.027 88.040  112.963 1.00 45.38  ? 365 GLN A CB  1 
ATOM   2746 C  CG  . GLN A 1 365 ? 124.531 87.839  112.898 1.00 47.62  ? 365 GLN A CG  1 
ATOM   2747 C  CD  . GLN A 1 365 ? 125.241 88.961  112.170 1.00 48.51  ? 365 GLN A CD  1 
ATOM   2748 O  OE1 . GLN A 1 365 ? 124.807 90.110  112.204 1.00 49.81  ? 365 GLN A OE1 1 
ATOM   2749 N  NE2 . GLN A 1 365 ? 126.340 88.631  111.506 1.00 52.31  ? 365 GLN A NE2 1 
ATOM   2750 N  N   . LEU A 1 366 ? 122.507 88.389  116.098 1.00 41.99  ? 366 LEU A N   1 
ATOM   2751 C  CA  . LEU A 1 366 ? 123.162 88.778  117.338 1.00 44.27  ? 366 LEU A CA  1 
ATOM   2752 C  C   . LEU A 1 366 ? 122.542 88.162  118.586 1.00 46.47  ? 366 LEU A C   1 
ATOM   2753 O  O   . LEU A 1 366 ? 123.041 88.413  119.685 1.00 47.51  ? 366 LEU A O   1 
ATOM   2754 C  CB  . LEU A 1 366 ? 123.171 90.304  117.468 1.00 43.87  ? 366 LEU A CB  1 
ATOM   2755 C  CG  . LEU A 1 366 ? 124.350 91.030  116.815 1.00 47.62  ? 366 LEU A CG  1 
ATOM   2756 C  CD1 . LEU A 1 366 ? 124.412 92.477  117.269 1.00 44.34  ? 366 LEU A CD1 1 
ATOM   2757 C  CD2 . LEU A 1 366 ? 125.659 90.318  117.116 1.00 44.85  ? 366 LEU A CD2 1 
ATOM   2758 N  N   . SER A 1 367 ? 121.480 87.361  118.461 1.00 48.79  ? 367 SER A N   1 
ATOM   2759 C  CA  . SER A 1 367 ? 120.920 86.734  119.650 1.00 45.65  ? 367 SER A CA  1 
ATOM   2760 C  C   . SER A 1 367 ? 120.702 85.237  119.470 1.00 50.50  ? 367 SER A C   1 
ATOM   2761 O  O   . SER A 1 367 ? 120.768 84.483  120.445 1.00 55.46  ? 367 SER A O   1 
ATOM   2762 C  CB  . SER A 1 367 ? 119.603 87.412  120.030 1.00 43.36  ? 367 SER A CB  1 
ATOM   2763 O  OG  . SER A 1 367 ? 119.740 88.821  120.042 1.00 50.88  ? 367 SER A OG  1 
ATOM   2764 N  N   . PHE A 1 368 ? 120.440 84.788  118.243 1.00 54.81  ? 368 PHE A N   1 
ATOM   2765 C  CA  . PHE A 1 368 ? 120.094 83.394  118.001 1.00 54.21  ? 368 PHE A CA  1 
ATOM   2766 C  C   . PHE A 1 368 ? 121.181 82.624  117.267 1.00 55.68  ? 368 PHE A C   1 
ATOM   2767 O  O   . PHE A 1 368 ? 121.628 81.580  117.749 1.00 58.16  ? 368 PHE A O   1 
ATOM   2768 C  CB  . PHE A 1 368 ? 118.776 83.314  117.217 1.00 51.18  ? 368 PHE A CB  1 
ATOM   2769 C  CG  . PHE A 1 368 ? 117.601 83.894  117.950 1.00 56.14  ? 368 PHE A CG  1 
ATOM   2770 C  CD1 . PHE A 1 368 ? 117.417 83.642  119.299 1.00 55.77  ? 368 PHE A CD1 1 
ATOM   2771 C  CD2 . PHE A 1 368 ? 116.681 84.693  117.293 1.00 58.97  ? 368 PHE A CD2 1 
ATOM   2772 C  CE1 . PHE A 1 368 ? 116.339 84.175  119.978 1.00 57.44  ? 368 PHE A CE1 1 
ATOM   2773 C  CE2 . PHE A 1 368 ? 115.600 85.229  117.966 1.00 55.48  ? 368 PHE A CE2 1 
ATOM   2774 C  CZ  . PHE A 1 368 ? 115.429 84.969  119.310 1.00 57.19  ? 368 PHE A CZ  1 
ATOM   2775 N  N   . ARG A 1 369 ? 121.625 83.110  116.112 1.00 55.34  ? 369 ARG A N   1 
ATOM   2776 C  CA  . ARG A 1 369 ? 122.622 82.422  115.294 1.00 57.91  ? 369 ARG A CA  1 
ATOM   2777 C  C   . ARG A 1 369 ? 123.865 83.302  115.214 1.00 59.10  ? 369 ARG A C   1 
ATOM   2778 O  O   . ARG A 1 369 ? 124.031 84.080  114.272 1.00 63.45  ? 369 ARG A O   1 
ATOM   2779 C  CB  . ARG A 1 369 ? 122.066 82.106  113.910 1.00 58.46  ? 369 ARG A CB  1 
ATOM   2780 C  CG  . ARG A 1 369 ? 120.746 81.357  113.935 1.00 56.30  ? 369 ARG A CG  1 
ATOM   2781 C  CD  . ARG A 1 369 ? 120.945 79.886  113.622 1.00 56.61  ? 369 ARG A CD  1 
ATOM   2782 N  NE  . ARG A 1 369 ? 121.653 79.690  112.363 1.00 58.72  ? 369 ARG A NE  1 
ATOM   2783 C  CZ  . ARG A 1 369 ? 122.708 78.903  112.213 1.00 62.43  ? 369 ARG A CZ  1 
ATOM   2784 N  NH1 . ARG A 1 369 ? 123.212 78.222  113.228 1.00 63.00  ? 369 ARG A NH1 1 
ATOM   2785 N  NH2 . ARG A 1 369 ? 123.274 78.798  111.014 1.00 60.25  ? 369 ARG A NH2 1 
ATOM   2786 N  N   . GLN A 1 370 ? 124.773 83.150  116.183 1.00 62.77  ? 370 GLN A N   1 
ATOM   2787 C  CA  . GLN A 1 370 ? 125.982 84.021  116.222 1.00 62.93  ? 370 GLN A CA  1 
ATOM   2788 C  C   . GLN A 1 370 ? 127.140 83.370  115.454 1.00 62.34  ? 370 GLN A C   1 
ATOM   2789 O  O   . GLN A 1 370 ? 128.212 84.001  115.378 1.00 64.01  ? 370 GLN A O   1 
ATOM   2790 C  CB  . GLN A 1 370 ? 126.348 84.341  117.674 1.00 64.13  ? 370 GLN A CB  1 
ATOM   2791 C  CG  . GLN A 1 370 ? 125.262 85.124  118.399 1.00 63.37  ? 370 GLN A CG  1 
ATOM   2792 C  CD  . GLN A 1 370 ? 125.664 85.525  119.797 1.00 64.63  ? 370 GLN A CD  1 
ATOM   2793 O  OE1 . GLN A 1 370 ? 126.762 85.223  120.260 1.00 67.33  ? 370 GLN A OE1 1 
ATOM   2794 N  NE2 . GLN A 1 370 ? 124.768 86.216  120.484 1.00 62.94  ? 370 GLN A NE2 1 
ATOM   2795 N  N   . ASN A 1 371 ? 126.939 82.167  114.906 1.00 68.80  ? 371 ASN A N   1 
ATOM   2796 C  CA  . ASN A 1 371 ? 127.965 81.522  114.099 1.00 70.60  ? 371 ASN A CA  1 
ATOM   2797 C  C   . ASN A 1 371 ? 127.556 81.379  112.638 1.00 71.17  ? 371 ASN A C   1 
ATOM   2798 O  O   . ASN A 1 371 ? 128.229 80.673  111.881 1.00 73.68  ? 371 ASN A O   1 
ATOM   2799 C  CB  . ASN A 1 371 ? 128.312 80.151  114.683 1.00 72.14  ? 371 ASN A CB  1 
ATOM   2800 C  CG  . ASN A 1 371 ? 128.976 80.250  116.040 1.00 74.47  ? 371 ASN A CG  1 
ATOM   2801 O  OD1 . ASN A 1 371 ? 129.998 80.918  116.197 1.00 73.58  ? 371 ASN A OD1 1 
ATOM   2802 N  ND2 . ASN A 1 371 ? 128.396 79.586  117.033 1.00 72.66  ? 371 ASN A ND2 1 
ATOM   2803 N  N   . ALA A 1 372 ? 126.473 82.030  112.225 1.00 64.42  ? 372 ALA A N   1 
ATOM   2804 C  CA  . ALA A 1 372 ? 125.999 81.912  110.855 1.00 62.54  ? 372 ALA A CA  1 
ATOM   2805 C  C   . ALA A 1 372 ? 126.903 82.676  109.894 1.00 63.94  ? 372 ALA A C   1 
ATOM   2806 O  O   . ALA A 1 372 ? 127.527 83.679  110.252 1.00 63.95  ? 372 ALA A O   1 
ATOM   2807 C  CB  . ALA A 1 372 ? 124.566 82.428  110.741 1.00 59.27  ? 372 ALA A CB  1 
ATOM   2808 N  N   . SER A 1 373 ? 126.965 82.189  108.659 1.00 64.96  ? 373 SER A N   1 
ATOM   2809 C  CA  . SER A 1 373 ? 127.713 82.853  107.605 1.00 63.84  ? 373 SER A CA  1 
ATOM   2810 C  C   . SER A 1 373 ? 126.937 84.062  107.086 1.00 63.11  ? 373 SER A C   1 
ATOM   2811 O  O   . SER A 1 373 ? 125.765 84.267  107.406 1.00 65.97  ? 373 SER A O   1 
ATOM   2812 C  CB  . SER A 1 373 ? 128.010 81.879  106.466 1.00 63.97  ? 373 SER A CB  1 
ATOM   2813 O  OG  . SER A 1 373 ? 126.968 80.930  106.323 1.00 62.91  ? 373 SER A OG  1 
ATOM   2814 N  N   . ASP A 1 374 ? 127.603 84.887  106.287 1.00 56.85  ? 374 ASP A N   1 
ATOM   2815 C  CA  . ASP A 1 374 ? 126.943 86.074  105.757 1.00 59.40  ? 374 ASP A CA  1 
ATOM   2816 C  C   . ASP A 1 374 ? 125.892 85.723  104.715 1.00 67.02  ? 374 ASP A C   1 
ATOM   2817 O  O   . ASP A 1 374 ? 124.910 86.441  104.571 1.00 68.79  ? 374 ASP A O   1 
ATOM   2818 C  CB  . ASP A 1 374 ? 127.949 87.076  105.194 1.00 59.89  ? 374 ASP A CB  1 
ATOM   2819 C  CG  . ASP A 1 374 ? 128.277 88.176  106.178 1.00 67.30  ? 374 ASP A CG  1 
ATOM   2820 O  OD1 . ASP A 1 374 ? 128.384 87.881  107.387 1.00 67.74  ? 374 ASP A OD1 1 
ATOM   2821 O  OD2 . ASP A 1 374 ? 128.400 89.339  105.749 1.00 68.09  ? 374 ASP A OD2 1 
ATOM   2822 N  N   . LYS A 1 375 ? 126.087 84.620  103.997 1.00 61.94  ? 375 LYS A N   1 
ATOM   2823 C  CA  . LYS A 1 375 ? 125.078 84.198  103.029 1.00 60.61  ? 375 LYS A CA  1 
ATOM   2824 C  C   . LYS A 1 375 ? 123.734 83.963  103.709 1.00 61.20  ? 375 LYS A C   1 
ATOM   2825 O  O   . LYS A 1 375 ? 122.680 84.365  103.192 1.00 59.91  ? 375 LYS A O   1 
ATOM   2826 C  CB  . LYS A 1 375 ? 125.550 82.934  102.311 1.00 59.17  ? 375 LYS A CB  1 
ATOM   2827 C  CG  . LYS A 1 375 ? 124.864 82.666  100.985 1.00 64.52  ? 375 LYS A CG  1 
ATOM   2828 C  CD  . LYS A 1 375 ? 125.156 81.257  100.496 1.00 63.91  ? 375 LYS A CD  1 
ATOM   2829 C  CE  . LYS A 1 375 ? 123.884 80.543  100.069 1.00 63.08  ? 375 LYS A CE  1 
ATOM   2830 N  NZ  . LYS A 1 375 ? 123.330 79.685  101.153 1.00 61.38  ? 375 LYS A NZ  1 
ATOM   2831 N  N   . GLU A 1 376 ? 123.758 83.321  104.880 1.00 50.79  ? 376 GLU A N   1 
ATOM   2832 C  CA  . GLU A 1 376 ? 122.535 83.110  105.643 1.00 47.52  ? 376 GLU A CA  1 
ATOM   2833 C  C   . GLU A 1 376 ? 121.896 84.434  106.035 1.00 52.83  ? 376 GLU A C   1 
ATOM   2834 O  O   . GLU A 1 376 ? 120.672 84.586  105.960 1.00 59.88  ? 376 GLU A O   1 
ATOM   2835 C  CB  . GLU A 1 376 ? 122.835 82.269  106.883 1.00 45.54  ? 376 GLU A CB  1 
ATOM   2836 C  CG  . GLU A 1 376 ? 121.616 81.606  107.497 1.00 54.32  ? 376 GLU A CG  1 
ATOM   2837 C  CD  . GLU A 1 376 ? 121.937 80.875  108.783 1.00 56.35  ? 376 GLU A CD  1 
ATOM   2838 O  OE1 . GLU A 1 376 ? 122.996 80.217  108.848 1.00 55.40  ? 376 GLU A OE1 1 
ATOM   2839 O  OE2 . GLU A 1 376 ? 121.131 80.958  109.732 1.00 55.69  ? 376 GLU A OE2 1 
ATOM   2840 N  N   . ILE A 1 377 ? 122.709 85.410  106.448 1.00 43.45  ? 377 ILE A N   1 
ATOM   2841 C  CA  . ILE A 1 377 ? 122.169 86.703  106.856 1.00 46.32  ? 377 ILE A CA  1 
ATOM   2842 C  C   . ILE A 1 377 ? 121.567 87.438  105.664 1.00 48.67  ? 377 ILE A C   1 
ATOM   2843 O  O   . ILE A 1 377 ? 120.536 88.107  105.790 1.00 53.95  ? 377 ILE A O   1 
ATOM   2844 C  CB  . ILE A 1 377 ? 123.252 87.543  107.555 1.00 44.70  ? 377 ILE A CB  1 
ATOM   2845 C  CG1 . ILE A 1 377 ? 124.030 86.685  108.551 1.00 48.17  ? 377 ILE A CG1 1 
ATOM   2846 C  CG2 . ILE A 1 377 ? 122.624 88.728  108.265 1.00 45.82  ? 377 ILE A CG2 1 
ATOM   2847 C  CD1 . ILE A 1 377 ? 123.194 86.164  109.693 1.00 47.83  ? 377 ILE A CD1 1 
ATOM   2848 N  N   . VAL A 1 378 ? 122.195 87.330  104.491 1.00 42.94  ? 378 VAL A N   1 
ATOM   2849 C  CA  . VAL A 1 378 ? 121.649 87.968  103.293 1.00 47.85  ? 378 VAL A CA  1 
ATOM   2850 C  C   . VAL A 1 378 ? 120.295 87.362  102.937 1.00 54.56  ? 378 VAL A C   1 
ATOM   2851 O  O   . VAL A 1 378 ? 119.325 88.077  102.635 1.00 57.83  ? 378 VAL A O   1 
ATOM   2852 C  CB  . VAL A 1 378 ? 122.645 87.853  102.125 1.00 45.00  ? 378 VAL A CB  1 
ATOM   2853 C  CG1 . VAL A 1 378 ? 122.003 88.314  100.829 1.00 51.17  ? 378 VAL A CG1 1 
ATOM   2854 C  CG2 . VAL A 1 378 ? 123.893 88.662  102.414 1.00 46.34  ? 378 VAL A CG2 1 
ATOM   2855 N  N   . TRP A 1 379 ? 120.205 86.029  102.975 1.00 45.47  ? 379 TRP A N   1 
ATOM   2856 C  CA  . TRP A 1 379 ? 118.935 85.377  102.669 1.00 42.43  ? 379 TRP A CA  1 
ATOM   2857 C  C   . TRP A 1 379 ? 117.864 85.741  103.691 1.00 46.94  ? 379 TRP A C   1 
ATOM   2858 O  O   . TRP A 1 379 ? 116.697 85.957  103.333 1.00 51.59  ? 379 TRP A O   1 
ATOM   2859 C  CB  . TRP A 1 379 ? 119.127 83.864  102.593 1.00 46.17  ? 379 TRP A CB  1 
ATOM   2860 C  CG  . TRP A 1 379 ? 119.780 83.419  101.320 1.00 49.84  ? 379 TRP A CG  1 
ATOM   2861 C  CD1 . TRP A 1 379 ? 120.916 82.677  101.200 1.00 53.39  ? 379 TRP A CD1 1 
ATOM   2862 C  CD2 . TRP A 1 379 ? 119.336 83.691  99.984  1.00 53.28  ? 379 TRP A CD2 1 
ATOM   2863 N  NE1 . TRP A 1 379 ? 121.209 82.470  99.875  1.00 55.01  ? 379 TRP A NE1 1 
ATOM   2864 C  CE2 . TRP A 1 379 ? 120.254 83.082  99.108  1.00 56.94  ? 379 TRP A CE2 1 
ATOM   2865 C  CE3 . TRP A 1 379 ? 118.250 84.388  99.444  1.00 52.77  ? 379 TRP A CE3 1 
ATOM   2866 C  CZ2 . TRP A 1 379 ? 120.121 83.149  97.723  1.00 54.77  ? 379 TRP A CZ2 1 
ATOM   2867 C  CZ3 . TRP A 1 379 ? 118.121 84.455  98.070  1.00 54.13  ? 379 TRP A CZ3 1 
ATOM   2868 C  CH2 . TRP A 1 379 ? 119.050 83.839  97.225  1.00 56.50  ? 379 TRP A CH2 1 
ATOM   2869 N  N   . VAL A 1 380 ? 118.244 85.821  104.969 1.00 34.66  ? 380 VAL A N   1 
ATOM   2870 C  CA  . VAL A 1 380 ? 117.301 86.218  106.009 1.00 34.47  ? 380 VAL A CA  1 
ATOM   2871 C  C   . VAL A 1 380 ? 116.816 87.643  105.774 1.00 38.60  ? 380 VAL A C   1 
ATOM   2872 O  O   . VAL A 1 380 ? 115.631 87.944  105.948 1.00 45.52  ? 380 VAL A O   1 
ATOM   2873 C  CB  . VAL A 1 380 ? 117.943 86.051  107.399 1.00 33.45  ? 380 VAL A CB  1 
ATOM   2874 C  CG1 . VAL A 1 380 ? 117.153 86.804  108.454 1.00 39.70  ? 380 VAL A CG1 1 
ATOM   2875 C  CG2 . VAL A 1 380 ? 118.039 84.579  107.760 1.00 35.94  ? 380 VAL A CG2 1 
ATOM   2876 N  N   . MET A 1 381 ? 117.720 88.537  105.364 1.00 31.06  ? 381 MET A N   1 
ATOM   2877 C  CA  . MET A 1 381 ? 117.332 89.913  105.068 1.00 29.14  ? 381 MET A CA  1 
ATOM   2878 C  C   . MET A 1 381 ? 116.303 89.966  103.947 1.00 36.59  ? 381 MET A C   1 
ATOM   2879 O  O   . MET A 1 381 ? 115.292 90.673  104.046 1.00 33.67  ? 381 MET A O   1 
ATOM   2880 C  CB  . MET A 1 381 ? 118.564 90.737  104.692 1.00 33.13  ? 381 MET A CB  1 
ATOM   2881 C  CG  . MET A 1 381 ? 119.099 91.626  105.798 1.00 41.50  ? 381 MET A CG  1 
ATOM   2882 S  SD  . MET A 1 381 ? 118.079 93.075  106.124 1.00 53.84  ? 381 MET A SD  1 
ATOM   2883 C  CE  . MET A 1 381 ? 118.190 93.940  104.563 1.00 38.77  ? 381 MET A CE  1 
ATOM   2884 N  N   . ARG A 1 382 ? 116.545 89.220  102.865 1.00 33.35  ? 382 ARG A N   1 
ATOM   2885 C  CA  . ARG A 1 382 ? 115.612 89.246  101.738 1.00 32.55  ? 382 ARG A CA  1 
ATOM   2886 C  C   . ARG A 1 382 ? 114.246 88.676  102.121 1.00 38.97  ? 382 ARG A C   1 
ATOM   2887 O  O   . ARG A 1 382 ? 113.199 89.256  101.783 1.00 40.36  ? 382 ARG A O   1 
ATOM   2888 C  CB  . ARG A 1 382 ? 116.206 88.485  100.555 1.00 38.22  ? 382 ARG A CB  1 
ATOM   2889 C  CG  . ARG A 1 382 ? 117.566 89.001  100.120 1.00 36.47  ? 382 ARG A CG  1 
ATOM   2890 C  CD  . ARG A 1 382 ? 117.733 88.925  98.615  1.00 38.57  ? 382 ARG A CD  1 
ATOM   2891 N  NE  . ARG A 1 382 ? 119.134 88.962  98.214  1.00 38.72  ? 382 ARG A NE  1 
ATOM   2892 C  CZ  . ARG A 1 382 ? 119.864 90.067  98.147  1.00 42.06  ? 382 ARG A CZ  1 
ATOM   2893 N  NH1 . ARG A 1 382 ? 119.361 91.249  98.463  1.00 36.73  ? 382 ARG A NH1 1 
ATOM   2894 N  NH2 . ARG A 1 382 ? 121.131 89.984  97.752  1.00 38.23  ? 382 ARG A NH2 1 
ATOM   2895 N  N   . ILE A 1 383 ? 114.236 87.547  102.836 1.00 35.48  ? 383 ILE A N   1 
ATOM   2896 C  CA  . ILE A 1 383 ? 112.971 86.945  103.250 1.00 31.85  ? 383 ILE A CA  1 
ATOM   2897 C  C   . ILE A 1 383 ? 112.215 87.880  104.188 1.00 31.79  ? 383 ILE A C   1 
ATOM   2898 O  O   . ILE A 1 383 ? 110.988 88.021  104.092 1.00 34.72  ? 383 ILE A O   1 
ATOM   2899 C  CB  . ILE A 1 383 ? 113.222 85.567  103.890 1.00 33.80  ? 383 ILE A CB  1 
ATOM   2900 C  CG1 . ILE A 1 383 ? 113.814 84.606  102.858 1.00 32.45  ? 383 ILE A CG1 1 
ATOM   2901 C  CG2 . ILE A 1 383 ? 111.937 84.995  104.460 1.00 33.20  ? 383 ILE A CG2 1 
ATOM   2902 C  CD1 . ILE A 1 383 ? 114.316 83.308  103.447 1.00 32.03  ? 383 ILE A CD1 1 
ATOM   2903 N  N   . THR A 1 384 ? 112.932 88.535  105.106 1.00 22.99  ? 384 THR A N   1 
ATOM   2904 C  CA  . THR A 1 384 ? 112.297 89.483  106.015 1.00 20.59  ? 384 THR A CA  1 
ATOM   2905 C  C   . THR A 1 384 ? 111.701 90.662  105.261 1.00 29.53  ? 384 THR A C   1 
ATOM   2906 O  O   . THR A 1 384 ? 110.608 91.131  105.598 1.00 35.22  ? 384 THR A O   1 
ATOM   2907 C  CB  . THR A 1 384 ? 113.307 89.972  107.051 1.00 26.98  ? 384 THR A CB  1 
ATOM   2908 O  OG1 . THR A 1 384 ? 114.011 88.853  107.600 1.00 36.38  ? 384 THR A OG1 1 
ATOM   2909 C  CG2 . THR A 1 384 ? 112.604 90.716  108.164 1.00 25.90  ? 384 THR A CG2 1 
ATOM   2910 N  N   . VAL A 1 385 ? 112.410 91.168  104.248 1.00 24.73  ? 385 VAL A N   1 
ATOM   2911 C  CA  . VAL A 1 385 ? 111.874 92.268  103.450 1.00 23.16  ? 385 VAL A CA  1 
ATOM   2912 C  C   . VAL A 1 385 ? 110.552 91.860  102.815 1.00 24.30  ? 385 VAL A C   1 
ATOM   2913 O  O   . VAL A 1 385 ? 109.548 92.584  102.897 1.00 27.88  ? 385 VAL A O   1 
ATOM   2914 C  CB  . VAL A 1 385 ? 112.895 92.710  102.385 1.00 24.22  ? 385 VAL A CB  1 
ATOM   2915 C  CG1 . VAL A 1 385 ? 112.209 93.500  101.284 1.00 22.62  ? 385 VAL A CG1 1 
ATOM   2916 C  CG2 . VAL A 1 385 ? 114.000 93.533  103.012 1.00 32.13  ? 385 VAL A CG2 1 
ATOM   2917 N  N   . PHE A 1 386 ? 110.530 90.680  102.187 1.00 25.87  ? 386 PHE A N   1 
ATOM   2918 C  CA  . PHE A 1 386 ? 109.300 90.230  101.538 1.00 22.91  ? 386 PHE A CA  1 
ATOM   2919 C  C   . PHE A 1 386 ? 108.163 90.073  102.544 1.00 27.34  ? 386 PHE A C   1 
ATOM   2920 O  O   . PHE A 1 386 ? 107.033 90.518  102.294 1.00 27.20  ? 386 PHE A O   1 
ATOM   2921 C  CB  . PHE A 1 386 ? 109.540 88.915  100.798 1.00 26.75  ? 386 PHE A CB  1 
ATOM   2922 C  CG  . PHE A 1 386 ? 108.333 88.411  100.060 1.00 30.52  ? 386 PHE A CG  1 
ATOM   2923 C  CD1 . PHE A 1 386 ? 107.996 88.930  98.823  1.00 31.30  ? 386 PHE A CD1 1 
ATOM   2924 C  CD2 . PHE A 1 386 ? 107.531 87.424  100.607 1.00 31.47  ? 386 PHE A CD2 1 
ATOM   2925 C  CE1 . PHE A 1 386 ? 106.886 88.475  98.145  1.00 30.18  ? 386 PHE A CE1 1 
ATOM   2926 C  CE2 . PHE A 1 386 ? 106.419 86.965  99.933  1.00 32.78  ? 386 PHE A CE2 1 
ATOM   2927 C  CZ  . PHE A 1 386 ? 106.096 87.491  98.701  1.00 33.76  ? 386 PHE A CZ  1 
ATOM   2928 N  N   . VAL A 1 387 ? 108.447 89.452  103.692 1.00 31.15  ? 387 VAL A N   1 
ATOM   2929 C  CA  . VAL A 1 387 ? 107.402 89.189  104.677 1.00 21.78  ? 387 VAL A CA  1 
ATOM   2930 C  C   . VAL A 1 387 ? 106.846 90.491  105.241 1.00 26.24  ? 387 VAL A C   1 
ATOM   2931 O  O   . VAL A 1 387 ? 105.629 90.642  105.396 1.00 28.51  ? 387 VAL A O   1 
ATOM   2932 C  CB  . VAL A 1 387 ? 107.937 88.268  105.788 1.00 21.04  ? 387 VAL A CB  1 
ATOM   2933 C  CG1 . VAL A 1 387 ? 106.985 88.247  106.968 1.00 24.68  ? 387 VAL A CG1 1 
ATOM   2934 C  CG2 . VAL A 1 387 ? 108.143 86.865  105.252 1.00 25.64  ? 387 VAL A CG2 1 
ATOM   2935 N  N   . PHE A 1 388 ? 107.719 91.450  105.559 1.00 27.34  ? 388 PHE A N   1 
ATOM   2936 C  CA  . PHE A 1 388 ? 107.249 92.714  106.117 1.00 26.99  ? 388 PHE A CA  1 
ATOM   2937 C  C   . PHE A 1 388 ? 106.436 93.506  105.100 1.00 28.32  ? 388 PHE A C   1 
ATOM   2938 O  O   . PHE A 1 388 ? 105.417 94.114  105.454 1.00 31.10  ? 388 PHE A O   1 
ATOM   2939 C  CB  . PHE A 1 388 ? 108.430 93.536  106.629 1.00 16.24  ? 388 PHE A CB  1 
ATOM   2940 C  CG  . PHE A 1 388 ? 108.930 93.096  107.973 1.00 24.13  ? 388 PHE A CG  1 
ATOM   2941 C  CD1 . PHE A 1 388 ? 108.216 92.179  108.724 1.00 31.94  ? 388 PHE A CD1 1 
ATOM   2942 C  CD2 . PHE A 1 388 ? 110.111 93.594  108.486 1.00 29.60  ? 388 PHE A CD2 1 
ATOM   2943 C  CE1 . PHE A 1 388 ? 108.673 91.769  109.959 1.00 27.37  ? 388 PHE A CE1 1 
ATOM   2944 C  CE2 . PHE A 1 388 ? 110.571 93.188  109.721 1.00 32.19  ? 388 PHE A CE2 1 
ATOM   2945 C  CZ  . PHE A 1 388 ? 109.852 92.274  110.458 1.00 26.90  ? 388 PHE A CZ  1 
ATOM   2946 N  N   . GLY A 1 389 ? 106.857 93.509  103.832 1.00 16.46  ? 389 GLY A N   1 
ATOM   2947 C  CA  . GLY A 1 389 ? 106.055 94.175  102.816 1.00 18.69  ? 389 GLY A CA  1 
ATOM   2948 C  C   . GLY A 1 389 ? 104.674 93.561  102.674 1.00 28.54  ? 389 GLY A C   1 
ATOM   2949 O  O   . GLY A 1 389 ? 103.662 94.271  102.613 1.00 24.52  ? 389 GLY A O   1 
ATOM   2950 N  N   . ALA A 1 390 ? 104.613 92.226  102.633 1.00 28.13  ? 390 ALA A N   1 
ATOM   2951 C  CA  . ALA A 1 390 ? 103.324 91.552  102.505 1.00 25.37  ? 390 ALA A CA  1 
ATOM   2952 C  C   . ALA A 1 390 ? 102.432 91.821  103.713 1.00 27.34  ? 390 ALA A C   1 
ATOM   2953 O  O   . ALA A 1 390 ? 101.223 92.038  103.565 1.00 30.37  ? 390 ALA A O   1 
ATOM   2954 C  CB  . ALA A 1 390 ? 103.535 90.050  102.314 1.00 26.14  ? 390 ALA A CB  1 
ATOM   2955 N  N   . SER A 1 391 ? 103.021 91.826  104.906 1.00 18.90  ? 391 SER A N   1 
ATOM   2956 C  CA  . SER A 1 391 ? 102.247 92.073  106.121 1.00 14.19  ? 391 SER A CA  1 
ATOM   2957 C  C   . SER A 1 391 ? 101.695 93.493  106.139 1.00 25.04  ? 391 SER A C   1 
ATOM   2958 O  O   . SER A 1 391 ? 100.549 93.706  106.530 1.00 36.17  ? 391 SER A O   1 
ATOM   2959 C  CB  . SER A 1 391 ? 103.080 91.806  107.377 1.00 21.48  ? 391 SER A CB  1 
ATOM   2960 O  OG  . SER A 1 391 ? 104.089 92.785  107.549 1.00 34.46  ? 391 SER A OG  1 
ATOM   2961 N  N   . ALA A 1 392 ? 102.501 94.465  105.717 1.00 31.17  ? 392 ALA A N   1 
ATOM   2962 C  CA  . ALA A 1 392 ? 102.021 95.843  105.651 1.00 32.65  ? 392 ALA A CA  1 
ATOM   2963 C  C   . ALA A 1 392 ? 100.881 95.984  104.651 1.00 33.87  ? 392 ALA A C   1 
ATOM   2964 O  O   . ALA A 1 392 ? 99.888  96.671  104.924 1.00 28.37  ? 392 ALA A O   1 
ATOM   2965 C  CB  . ALA A 1 392 ? 103.168 96.788  105.295 1.00 26.02  ? 392 ALA A CB  1 
ATOM   2966 N  N   . THR A 1 393 ? 101.000 95.339  103.487 1.00 36.72  ? 393 THR A N   1 
ATOM   2967 C  CA  . THR A 1 393 ? 99.919  95.402  102.504 1.00 24.14  ? 393 THR A CA  1 
ATOM   2968 C  C   . THR A 1 393 ? 98.638  94.772  103.043 1.00 27.76  ? 393 THR A C   1 
ATOM   2969 O  O   . THR A 1 393 ? 97.540  95.312  102.850 1.00 29.13  ? 393 THR A O   1 
ATOM   2970 C  CB  . THR A 1 393 ? 100.344 94.716  101.209 1.00 33.27  ? 393 THR A CB  1 
ATOM   2971 O  OG1 . THR A 1 393 ? 101.659 95.152  100.849 1.00 40.13  ? 393 THR A OG1 1 
ATOM   2972 C  CG2 . THR A 1 393 ? 99.380  95.062  100.087 1.00 34.20  ? 393 THR A CG2 1 
ATOM   2973 N  N   . ALA A 1 394 ? 98.758  93.624  103.716 1.00 31.83  ? 394 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 394 ? 97.580  92.968  104.276 1.00 34.02  ? 394 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 394 ? 96.915  93.833  105.339 1.00 33.50  ? 394 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 394 ? 95.683  93.944  105.379 1.00 29.69  ? 394 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 394 ? 97.960  91.606  104.854 1.00 30.41  ? 394 ALA A CB  1 
ATOM   2978 N  N   . MET A 1 395 ? 97.713  94.452  106.214 1.00 34.53  ? 395 MET A N   1 
ATOM   2979 C  CA  . MET A 1 395 ? 97.144  95.328  107.234 1.00 28.40  ? 395 MET A CA  1 
ATOM   2980 C  C   . MET A 1 395 ? 96.466  96.539  106.609 1.00 32.87  ? 395 MET A C   1 
ATOM   2981 O  O   . MET A 1 395 ? 95.411  96.977  107.080 1.00 33.16  ? 395 MET A O   1 
ATOM   2982 C  CB  . MET A 1 395 ? 98.225  95.771  108.220 1.00 28.48  ? 395 MET A CB  1 
ATOM   2983 C  CG  . MET A 1 395 ? 98.233  94.989  109.520 1.00 33.00  ? 395 MET A CG  1 
ATOM   2984 S  SD  . MET A 1 395 ? 99.451  95.588  110.705 1.00 56.65  ? 395 MET A SD  1 
ATOM   2985 C  CE  . MET A 1 395 ? 100.796 96.049  109.618 1.00 38.51  ? 395 MET A CE  1 
ATOM   2986 N  N   . ALA A 1 396 ? 97.057  97.101  105.552 1.00 32.00  ? 396 ALA A N   1 
ATOM   2987 C  CA  . ALA A 1 396 ? 96.427  98.230  104.876 1.00 18.40  ? 396 ALA A CA  1 
ATOM   2988 C  C   . ALA A 1 396 ? 95.090  97.835  104.264 1.00 26.42  ? 396 ALA A C   1 
ATOM   2989 O  O   . ALA A 1 396 ? 94.117  98.593  104.340 1.00 27.01  ? 396 ALA A O   1 
ATOM   2990 C  CB  . ALA A 1 396 ? 97.360  98.788  103.803 1.00 22.74  ? 396 ALA A CB  1 
ATOM   2991 N  N   . LEU A 1 397 ? 95.023  96.654  103.645 1.00 43.23  ? 397 LEU A N   1 
ATOM   2992 C  CA  . LEU A 1 397 ? 93.805  96.270  102.937 1.00 35.85  ? 397 LEU A CA  1 
ATOM   2993 C  C   . LEU A 1 397 ? 92.691  95.816  103.877 1.00 38.67  ? 397 LEU A C   1 
ATOM   2994 O  O   . LEU A 1 397 ? 91.522  96.149  103.654 1.00 40.02  ? 397 LEU A O   1 
ATOM   2995 C  CB  . LEU A 1 397 ? 94.112  95.172  101.919 1.00 38.14  ? 397 LEU A CB  1 
ATOM   2996 C  CG  . LEU A 1 397 ? 94.604  95.638  100.548 1.00 38.82  ? 397 LEU A CG  1 
ATOM   2997 C  CD1 . LEU A 1 397 ? 94.651  94.474  99.575  1.00 38.75  ? 397 LEU A CD1 1 
ATOM   2998 C  CD2 . LEU A 1 397 ? 93.726  96.755  100.010 1.00 36.57  ? 397 LEU A CD2 1 
ATOM   2999 N  N   . LEU A 1 398 ? 93.016  95.057  104.925 1.00 43.84  ? 398 LEU A N   1 
ATOM   3000 C  CA  . LEU A 1 398 ? 91.998  94.362  105.707 1.00 40.80  ? 398 LEU A CA  1 
ATOM   3001 C  C   . LEU A 1 398 ? 91.723  94.987  107.071 1.00 46.40  ? 398 LEU A C   1 
ATOM   3002 O  O   . LEU A 1 398 ? 91.067  94.352  107.903 1.00 53.86  ? 398 LEU A O   1 
ATOM   3003 C  CB  . LEU A 1 398 ? 92.387  92.893  105.892 1.00 39.59  ? 398 LEU A CB  1 
ATOM   3004 C  CG  . LEU A 1 398 ? 92.796  92.106  104.647 1.00 47.28  ? 398 LEU A CG  1 
ATOM   3005 C  CD1 . LEU A 1 398 ? 93.588  90.872  105.039 1.00 45.61  ? 398 LEU A CD1 1 
ATOM   3006 C  CD2 . LEU A 1 398 ? 91.575  91.723  103.833 1.00 43.99  ? 398 LEU A CD2 1 
ATOM   3007 N  N   . THR A 1 399 ? 92.198  96.201  107.333 1.00 47.15  ? 399 THR A N   1 
ATOM   3008 C  CA  . THR A 1 399 ? 91.985  96.834  108.628 1.00 43.97  ? 399 THR A CA  1 
ATOM   3009 C  C   . THR A 1 399 ? 91.476  98.255  108.439 1.00 49.08  ? 399 THR A C   1 
ATOM   3010 O  O   . THR A 1 399 ? 91.966  98.991  107.576 1.00 50.19  ? 399 THR A O   1 
ATOM   3011 C  CB  . THR A 1 399 ? 93.272  96.841  109.466 1.00 42.12  ? 399 THR A CB  1 
ATOM   3012 O  OG1 . THR A 1 399 ? 93.801  95.512  109.539 1.00 46.90  ? 399 THR A OG1 1 
ATOM   3013 C  CG2 . THR A 1 399 ? 92.993  97.334  110.874 1.00 39.44  ? 399 THR A CG2 1 
ATOM   3014 N  N   . LYS A 1 400 ? 90.487  98.633  109.248 1.00 49.78  ? 400 LYS A N   1 
ATOM   3015 C  CA  . LYS A 1 400 ? 89.906  99.968  109.215 1.00 52.87  ? 400 LYS A CA  1 
ATOM   3016 C  C   . LYS A 1 400 ? 90.389  100.855 110.355 1.00 50.16  ? 400 LYS A C   1 
ATOM   3017 O  O   . LYS A 1 400 ? 90.033  102.036 110.395 1.00 49.92  ? 400 LYS A O   1 
ATOM   3018 C  CB  . LYS A 1 400 ? 88.376  99.880  109.248 1.00 52.90  ? 400 LYS A CB  1 
ATOM   3019 C  CG  . LYS A 1 400 ? 87.783  98.963  108.191 1.00 53.91  ? 400 LYS A CG  1 
ATOM   3020 C  CD  . LYS A 1 400 ? 87.348  97.635  108.790 1.00 53.51  ? 400 LYS A CD  1 
ATOM   3021 C  CE  . LYS A 1 400 ? 86.605  96.790  107.769 1.00 53.31  ? 400 LYS A CE  1 
ATOM   3022 N  NZ  . LYS A 1 400 ? 87.537  96.033  106.890 1.00 54.50  ? 400 LYS A NZ  1 
ATOM   3023 N  N   . THR A 1 401 ? 91.187  100.320 111.275 1.00 47.86  ? 401 THR A N   1 
ATOM   3024 C  CA  . THR A 1 401 ? 91.714  101.070 112.409 1.00 44.65  ? 401 THR A CA  1 
ATOM   3025 C  C   . THR A 1 401 ? 93.220  101.282 112.282 1.00 42.16  ? 401 THR A C   1 
ATOM   3026 O  O   . THR A 1 401 ? 93.957  101.214 113.266 1.00 45.87  ? 401 THR A O   1 
ATOM   3027 C  CB  . THR A 1 401 ? 91.388  100.364 113.723 1.00 43.19  ? 401 THR A CB  1 
ATOM   3028 O  OG1 . THR A 1 401 ? 91.716  98.974  113.616 1.00 46.03  ? 401 THR A OG1 1 
ATOM   3029 C  CG2 . THR A 1 401 ? 89.912  100.502 114.048 1.00 43.37  ? 401 THR A CG2 1 
ATOM   3030 N  N   . VAL A 1 402 ? 93.680  101.554 111.057 1.00 34.99  ? 402 VAL A N   1 
ATOM   3031 C  CA  . VAL A 1 402 ? 95.146  101.722 110.818 1.00 34.06  ? 402 VAL A CA  1 
ATOM   3032 C  C   . VAL A 1 402 ? 95.605  103.075 111.375 1.00 39.89  ? 402 VAL A C   1 
ATOM   3033 O  O   . VAL A 1 402 ? 96.750  103.145 111.866 1.00 43.04  ? 402 VAL A O   1 
ATOM   3034 C  CB  . VAL A 1 402 ? 95.491  101.579 109.323 1.00 28.28  ? 402 VAL A CB  1 
ATOM   3035 C  CG1 . VAL A 1 402 ? 95.230  100.169 108.817 1.00 28.93  ? 402 VAL A CG1 1 
ATOM   3036 C  CG2 . VAL A 1 402 ? 94.753  102.599 108.470 1.00 34.32  ? 402 VAL A CG2 1 
ATOM   3037 N  N   . TYR A 1 403 ? 94.753  104.103 111.308 1.00 32.27  ? 403 TYR A N   1 
ATOM   3038 C  CA  . TYR A 1 403 ? 95.157  105.434 111.756 1.00 26.87  ? 403 TYR A CA  1 
ATOM   3039 C  C   . TYR A 1 403 ? 95.310  105.500 113.271 1.00 29.01  ? 403 TYR A C   1 
ATOM   3040 O  O   . TYR A 1 403 ? 96.260  106.111 113.779 1.00 38.13  ? 403 TYR A O   1 
ATOM   3041 C  CB  . TYR A 1 403 ? 94.151  106.474 111.271 1.00 24.97  ? 403 TYR A CB  1 
ATOM   3042 C  CG  . TYR A 1 403 ? 94.307  106.836 109.813 1.00 31.35  ? 403 TYR A CG  1 
ATOM   3043 C  CD1 . TYR A 1 403 ? 93.920  105.956 108.814 1.00 31.99  ? 403 TYR A CD1 1 
ATOM   3044 C  CD2 . TYR A 1 403 ? 94.843  108.057 109.437 1.00 34.16  ? 403 TYR A CD2 1 
ATOM   3045 C  CE1 . TYR A 1 403 ? 94.062  106.282 107.481 1.00 29.06  ? 403 TYR A CE1 1 
ATOM   3046 C  CE2 . TYR A 1 403 ? 94.989  108.391 108.107 1.00 34.04  ? 403 TYR A CE2 1 
ATOM   3047 C  CZ  . TYR A 1 403 ? 94.597  107.501 107.135 1.00 34.09  ? 403 TYR A CZ  1 
ATOM   3048 O  OH  . TYR A 1 403 ? 94.742  107.833 105.810 1.00 40.43  ? 403 TYR A OH  1 
ATOM   3049 N  N   . GLY A 1 404 ? 94.381  104.892 114.011 1.00 30.32  ? 404 GLY A N   1 
ATOM   3050 C  CA  . GLY A 1 404 ? 94.509  104.867 115.458 1.00 26.72  ? 404 GLY A CA  1 
ATOM   3051 C  C   . GLY A 1 404 ? 95.745  104.119 115.915 1.00 25.50  ? 404 GLY A C   1 
ATOM   3052 O  O   . GLY A 1 404 ? 96.440  104.550 116.839 1.00 38.50  ? 404 GLY A O   1 
ATOM   3053 N  N   . LEU A 1 405 ? 96.039  102.990 115.267 1.00 22.65  ? 405 LEU A N   1 
ATOM   3054 C  CA  . LEU A 1 405 ? 97.247  102.239 115.589 1.00 23.55  ? 405 LEU A CA  1 
ATOM   3055 C  C   . LEU A 1 405 ? 98.498  103.048 115.275 1.00 23.40  ? 405 LEU A C   1 
ATOM   3056 O  O   . LEU A 1 405 ? 99.470  103.019 116.036 1.00 28.34  ? 405 LEU A O   1 
ATOM   3057 C  CB  . LEU A 1 405 ? 97.252  100.914 114.830 1.00 24.67  ? 405 LEU A CB  1 
ATOM   3058 C  CG  . LEU A 1 405 ? 96.237  99.876  115.311 1.00 30.60  ? 405 LEU A CG  1 
ATOM   3059 C  CD1 . LEU A 1 405 ? 96.187  98.691  114.365 1.00 28.14  ? 405 LEU A CD1 1 
ATOM   3060 C  CD2 . LEU A 1 405 ? 96.566  99.424  116.720 1.00 29.58  ? 405 LEU A CD2 1 
ATOM   3061 N  N   . TRP A 1 406 ? 98.488  103.780 114.158 1.00 19.52  ? 406 TRP A N   1 
ATOM   3062 C  CA  . TRP A 1 406 ? 99.619  104.633 113.803 1.00 11.80  ? 406 TRP A CA  1 
ATOM   3063 C  C   . TRP A 1 406 ? 99.855  105.703 114.863 1.00 27.60  ? 406 TRP A C   1 
ATOM   3064 O  O   . TRP A 1 406 ? 100.989 105.908 115.320 1.00 33.05  ? 406 TRP A O   1 
ATOM   3065 C  CB  . TRP A 1 406 ? 99.363  105.262 112.432 1.00 10.37  ? 406 TRP A CB  1 
ATOM   3066 C  CG  . TRP A 1 406 ? 100.387 106.258 111.972 1.00 25.67  ? 406 TRP A CG  1 
ATOM   3067 C  CD1 . TRP A 1 406 ? 101.704 106.309 112.321 1.00 25.46  ? 406 TRP A CD1 1 
ATOM   3068 C  CD2 . TRP A 1 406 ? 100.174 107.340 111.058 1.00 23.04  ? 406 TRP A CD2 1 
ATOM   3069 N  NE1 . TRP A 1 406 ? 102.321 107.360 111.690 1.00 19.96  ? 406 TRP A NE1 1 
ATOM   3070 C  CE2 . TRP A 1 406 ? 101.403 108.009 110.908 1.00 21.27  ? 406 TRP A CE2 1 
ATOM   3071 C  CE3 . TRP A 1 406 ? 99.060  107.811 110.356 1.00 25.47  ? 406 TRP A CE3 1 
ATOM   3072 C  CZ2 . TRP A 1 406 ? 101.551 109.121 110.083 1.00 23.02  ? 406 TRP A CZ2 1 
ATOM   3073 C  CZ3 . TRP A 1 406 ? 99.209  108.916 109.539 1.00 25.50  ? 406 TRP A CZ3 1 
ATOM   3074 C  CH2 . TRP A 1 406 ? 100.446 109.559 109.409 1.00 20.56  ? 406 TRP A CH2 1 
ATOM   3075 N  N   . TYR A 1 407 ? 98.787  106.387 115.279 1.00 26.99  ? 407 TYR A N   1 
ATOM   3076 C  CA  . TYR A 1 407 ? 98.928  107.427 116.293 1.00 17.12  ? 407 TYR A CA  1 
ATOM   3077 C  C   . TYR A 1 407 ? 99.418  106.849 117.616 1.00 19.93  ? 407 TYR A C   1 
ATOM   3078 O  O   . TYR A 1 407 ? 100.321 107.411 118.253 1.00 29.84  ? 407 TYR A O   1 
ATOM   3079 C  CB  . TYR A 1 407 ? 97.600  108.158 116.484 1.00 24.18  ? 407 TYR A CB  1 
ATOM   3080 C  CG  . TYR A 1 407 ? 97.085  108.842 115.236 1.00 33.22  ? 407 TYR A CG  1 
ATOM   3081 C  CD1 . TYR A 1 407 ? 97.959  109.307 114.264 1.00 30.88  ? 407 TYR A CD1 1 
ATOM   3082 C  CD2 . TYR A 1 407 ? 95.724  109.026 115.035 1.00 30.83  ? 407 TYR A CD2 1 
ATOM   3083 C  CE1 . TYR A 1 407 ? 97.492  109.931 113.125 1.00 32.77  ? 407 TYR A CE1 1 
ATOM   3084 C  CE2 . TYR A 1 407 ? 95.249  109.649 113.899 1.00 28.86  ? 407 TYR A CE2 1 
ATOM   3085 C  CZ  . TYR A 1 407 ? 96.137  110.099 112.949 1.00 37.87  ? 407 TYR A CZ  1 
ATOM   3086 O  OH  . TYR A 1 407 ? 95.668  110.721 111.816 1.00 38.95  ? 407 TYR A OH  1 
ATOM   3087 N  N   . LEU A 1 408 ? 98.845  105.719 118.041 1.00 18.14  ? 408 LEU A N   1 
ATOM   3088 C  CA  . LEU A 1 408 ? 99.253  105.110 119.302 1.00 16.90  ? 408 LEU A CA  1 
ATOM   3089 C  C   . LEU A 1 408 ? 100.710 104.663 119.258 1.00 24.81  ? 408 LEU A C   1 
ATOM   3090 O  O   . LEU A 1 408 ? 101.448 104.832 120.236 1.00 31.62  ? 408 LEU A O   1 
ATOM   3091 C  CB  . LEU A 1 408 ? 98.334  103.935 119.633 1.00 22.56  ? 408 LEU A CB  1 
ATOM   3092 C  CG  . LEU A 1 408 ? 98.616  103.170 120.926 1.00 28.33  ? 408 LEU A CG  1 
ATOM   3093 C  CD1 . LEU A 1 408 ? 98.187  103.980 122.133 1.00 27.75  ? 408 LEU A CD1 1 
ATOM   3094 C  CD2 . LEU A 1 408 ? 97.913  101.828 120.908 1.00 28.18  ? 408 LEU A CD2 1 
ATOM   3095 N  N   . SER A 1 409 ? 101.147 104.092 118.133 1.00 21.65  ? 409 SER A N   1 
ATOM   3096 C  CA  . SER A 1 409 ? 102.536 103.664 118.012 1.00 22.46  ? 409 SER A CA  1 
ATOM   3097 C  C   . SER A 1 409 ? 103.490 104.852 118.044 1.00 27.59  ? 409 SER A C   1 
ATOM   3098 O  O   . SER A 1 409 ? 104.569 104.769 118.643 1.00 31.85  ? 409 SER A O   1 
ATOM   3099 C  CB  . SER A 1 409 ? 102.725 102.853 116.731 1.00 22.15  ? 409 SER A CB  1 
ATOM   3100 O  OG  . SER A 1 409 ? 102.330 103.595 115.592 1.00 31.77  ? 409 SER A OG  1 
ATOM   3101 N  N   . SER A 1 410 ? 103.121 105.962 117.397 1.00 15.69  ? 410 SER A N   1 
ATOM   3102 C  CA  . SER A 1 410 ? 103.972 107.149 117.454 1.00 20.21  ? 410 SER A CA  1 
ATOM   3103 C  C   . SER A 1 410 ? 104.082 107.690 118.877 1.00 22.25  ? 410 SER A C   1 
ATOM   3104 O  O   . SER A 1 410 ? 105.177 108.061 119.325 1.00 25.31  ? 410 SER A O   1 
ATOM   3105 C  CB  . SER A 1 410 ? 103.445 108.224 116.507 1.00 21.22  ? 410 SER A CB  1 
ATOM   3106 O  OG  . SER A 1 410 ? 103.595 107.822 115.159 1.00 21.90  ? 410 SER A OG  1 
ATOM   3107 N  N   . ASP A 1 411 ? 102.962 107.741 119.607 1.00 22.64  ? 411 ASP A N   1 
ATOM   3108 C  CA  . ASP A 1 411 ? 103.030 108.174 121.002 1.00 24.72  ? 411 ASP A CA  1 
ATOM   3109 C  C   . ASP A 1 411 ? 103.892 107.236 121.836 1.00 23.59  ? 411 ASP A C   1 
ATOM   3110 O  O   . ASP A 1 411 ? 104.653 107.687 122.700 1.00 27.28  ? 411 ASP A O   1 
ATOM   3111 C  CB  . ASP A 1 411 ? 101.632 108.291 121.614 1.00 26.23  ? 411 ASP A CB  1 
ATOM   3112 C  CG  . ASP A 1 411 ? 100.647 108.981 120.701 1.00 34.86  ? 411 ASP A CG  1 
ATOM   3113 O  OD1 . ASP A 1 411 ? 101.084 109.589 119.703 1.00 39.67  ? 411 ASP A OD1 1 
ATOM   3114 O  OD2 . ASP A 1 411 ? 99.433  108.930 120.990 1.00 33.01  ? 411 ASP A OD2 1 
ATOM   3115 N  N   . LEU A 1 412 ? 103.781 105.925 121.605 1.00 21.35  ? 412 LEU A N   1 
ATOM   3116 C  CA  . LEU A 1 412 ? 104.606 104.976 122.347 1.00 18.62  ? 412 LEU A CA  1 
ATOM   3117 C  C   . LEU A 1 412 ? 106.087 105.186 122.061 1.00 24.39  ? 412 LEU A C   1 
ATOM   3118 O  O   . LEU A 1 412 ? 106.914 105.152 122.980 1.00 27.19  ? 412 LEU A O   1 
ATOM   3119 C  CB  . LEU A 1 412 ? 104.196 103.544 122.011 1.00 25.73  ? 412 LEU A CB  1 
ATOM   3120 C  CG  . LEU A 1 412 ? 102.993 102.997 122.775 1.00 30.65  ? 412 LEU A CG  1 
ATOM   3121 C  CD1 . LEU A 1 412 ? 102.623 101.621 122.260 1.00 26.12  ? 412 LEU A CD1 1 
ATOM   3122 C  CD2 . LEU A 1 412 ? 103.289 102.956 124.262 1.00 25.24  ? 412 LEU A CD2 1 
ATOM   3123 N  N   . VAL A 1 413 ? 106.442 105.400 120.792 1.00 24.81  ? 413 VAL A N   1 
ATOM   3124 C  CA  . VAL A 1 413 ? 107.837 105.655 120.442 1.00 21.05  ? 413 VAL A CA  1 
ATOM   3125 C  C   . VAL A 1 413 ? 108.341 106.897 121.164 1.00 22.56  ? 413 VAL A C   1 
ATOM   3126 O  O   . VAL A 1 413 ? 109.385 106.870 121.827 1.00 22.13  ? 413 VAL A O   1 
ATOM   3127 C  CB  . VAL A 1 413 ? 107.997 105.787 118.917 1.00 19.27  ? 413 VAL A CB  1 
ATOM   3128 C  CG1 . VAL A 1 413 ? 109.317 106.455 118.573 1.00 10.50  ? 413 VAL A CG1 1 
ATOM   3129 C  CG2 . VAL A 1 413 ? 107.906 104.427 118.255 1.00 22.62  ? 413 VAL A CG2 1 
ATOM   3130 N  N   . TYR A 1 414 ? 107.575 107.990 121.088 1.00 30.61  ? 414 TYR A N   1 
ATOM   3131 C  CA  . TYR A 1 414 ? 107.994 109.243 121.711 1.00 18.98  ? 414 TYR A CA  1 
ATOM   3132 C  C   . TYR A 1 414 ? 108.145 109.097 123.221 1.00 17.97  ? 414 TYR A C   1 
ATOM   3133 O  O   . TYR A 1 414 ? 109.085 109.639 123.812 1.00 29.20  ? 414 TYR A O   1 
ATOM   3134 C  CB  . TYR A 1 414 ? 106.994 110.348 121.369 1.00 24.16  ? 414 TYR A CB  1 
ATOM   3135 C  CG  . TYR A 1 414 ? 107.018 111.557 122.284 1.00 28.86  ? 414 TYR A CG  1 
ATOM   3136 C  CD1 . TYR A 1 414 ? 108.161 112.331 122.423 1.00 28.95  ? 414 TYR A CD1 1 
ATOM   3137 C  CD2 . TYR A 1 414 ? 105.885 111.934 122.992 1.00 26.69  ? 414 TYR A CD2 1 
ATOM   3138 C  CE1 . TYR A 1 414 ? 108.179 113.437 123.250 1.00 22.95  ? 414 TYR A CE1 1 
ATOM   3139 C  CE2 . TYR A 1 414 ? 105.894 113.039 123.819 1.00 26.49  ? 414 TYR A CE2 1 
ATOM   3140 C  CZ  . TYR A 1 414 ? 107.042 113.786 123.943 1.00 31.44  ? 414 TYR A CZ  1 
ATOM   3141 O  OH  . TYR A 1 414 ? 107.050 114.885 124.768 1.00 34.30  ? 414 TYR A OH  1 
ATOM   3142 N  N   . ILE A 1 415 ? 107.227 108.375 123.865 1.00 20.02  ? 415 ILE A N   1 
ATOM   3143 C  CA  . ILE A 1 415 ? 107.271 108.251 125.319 1.00 17.58  ? 415 ILE A CA  1 
ATOM   3144 C  C   . ILE A 1 415 ? 108.419 107.349 125.762 1.00 20.45  ? 415 ILE A C   1 
ATOM   3145 O  O   . ILE A 1 415 ? 109.097 107.636 126.755 1.00 28.59  ? 415 ILE A O   1 
ATOM   3146 C  CB  . ILE A 1 415 ? 105.912 107.760 125.852 1.00 27.40  ? 415 ILE A CB  1 
ATOM   3147 C  CG1 . ILE A 1 415 ? 104.888 108.895 125.808 1.00 27.51  ? 415 ILE A CG1 1 
ATOM   3148 C  CG2 . ILE A 1 415 ? 106.041 107.234 127.271 1.00 22.64  ? 415 ILE A CG2 1 
ATOM   3149 C  CD1 . ILE A 1 415 ? 103.456 108.433 125.882 1.00 22.40  ? 415 ILE A CD1 1 
ATOM   3150 N  N   . VAL A 1 416 ? 108.667 106.256 125.044 1.00 23.25  ? 416 VAL A N   1 
ATOM   3151 C  CA  . VAL A 1 416 ? 109.576 105.227 125.545 1.00 22.76  ? 416 VAL A CA  1 
ATOM   3152 C  C   . VAL A 1 416 ? 110.996 105.403 125.015 1.00 25.48  ? 416 VAL A C   1 
ATOM   3153 O  O   . VAL A 1 416 ? 111.950 105.442 125.794 1.00 31.83  ? 416 VAL A O   1 
ATOM   3154 C  CB  . VAL A 1 416 ? 109.023 103.825 125.211 1.00 26.32  ? 416 VAL A CB  1 
ATOM   3155 C  CG1 . VAL A 1 416 ? 109.969 102.753 125.719 1.00 25.27  ? 416 VAL A CG1 1 
ATOM   3156 C  CG2 . VAL A 1 416 ? 107.644 103.641 125.820 1.00 27.49  ? 416 VAL A CG2 1 
ATOM   3157 N  N   . ILE A 1 417 ? 111.177 105.490 123.694 1.00 19.69  ? 417 ILE A N   1 
ATOM   3158 C  CA  . ILE A 1 417 ? 112.518 105.349 123.129 1.00 22.64  ? 417 ILE A CA  1 
ATOM   3159 C  C   . ILE A 1 417 ? 113.367 106.591 123.388 1.00 26.95  ? 417 ILE A C   1 
ATOM   3160 O  O   . ILE A 1 417 ? 114.566 106.486 123.670 1.00 20.70  ? 417 ILE A O   1 
ATOM   3161 C  CB  . ILE A 1 417 ? 112.428 105.014 121.629 1.00 22.01  ? 417 ILE A CB  1 
ATOM   3162 C  CG1 . ILE A 1 417 ? 111.688 103.691 121.429 1.00 20.42  ? 417 ILE A CG1 1 
ATOM   3163 C  CG2 . ILE A 1 417 ? 113.812 104.924 121.014 1.00 16.87  ? 417 ILE A CG2 1 
ATOM   3164 C  CD1 . ILE A 1 417 ? 111.415 103.353 119.987 1.00 18.81  ? 417 ILE A CD1 1 
ATOM   3165 N  N   . PHE A 1 418 ? 112.769 107.780 123.294 1.00 26.13  ? 418 PHE A N   1 
ATOM   3166 C  CA  . PHE A 1 418 ? 113.540 109.021 123.394 1.00 24.62  ? 418 PHE A CA  1 
ATOM   3167 C  C   . PHE A 1 418 ? 114.291 109.166 124.717 1.00 29.15  ? 418 PHE A C   1 
ATOM   3168 O  O   . PHE A 1 418 ? 115.494 109.493 124.685 1.00 26.93  ? 418 PHE A O   1 
ATOM   3169 C  CB  . PHE A 1 418 ? 112.604 110.207 123.130 1.00 13.05  ? 418 PHE A CB  1 
ATOM   3170 C  CG  . PHE A 1 418 ? 113.292 111.541 123.111 1.00 22.08  ? 418 PHE A CG  1 
ATOM   3171 C  CD1 . PHE A 1 418 ? 114.153 111.878 122.081 1.00 24.64  ? 418 PHE A CD1 1 
ATOM   3172 C  CD2 . PHE A 1 418 ? 113.064 112.466 124.115 1.00 28.11  ? 418 PHE A CD2 1 
ATOM   3173 C  CE1 . PHE A 1 418 ? 114.782 113.106 122.062 1.00 20.15  ? 418 PHE A CE1 1 
ATOM   3174 C  CE2 . PHE A 1 418 ? 113.691 113.694 124.100 1.00 18.42  ? 418 PHE A CE2 1 
ATOM   3175 C  CZ  . PHE A 1 418 ? 114.551 114.014 123.072 1.00 18.64  ? 418 PHE A CZ  1 
ATOM   3176 N  N   . PRO A 1 419 ? 113.677 108.959 125.892 1.00 25.30  ? 419 PRO A N   1 
ATOM   3177 C  CA  . PRO A 1 419 ? 114.465 109.043 127.136 1.00 25.79  ? 419 PRO A CA  1 
ATOM   3178 C  C   . PRO A 1 419 ? 115.601 108.037 127.208 1.00 24.68  ? 419 PRO A C   1 
ATOM   3179 O  O   . PRO A 1 419 ? 116.663 108.349 127.760 1.00 27.76  ? 419 PRO A O   1 
ATOM   3180 C  CB  . PRO A 1 419 ? 113.418 108.796 128.231 1.00 25.00  ? 419 PRO A CB  1 
ATOM   3181 C  CG  . PRO A 1 419 ? 112.125 109.129 127.610 1.00 20.42  ? 419 PRO A CG  1 
ATOM   3182 C  CD  . PRO A 1 419 ? 112.243 108.764 126.175 1.00 12.92  ? 419 PRO A CD  1 
ATOM   3183 N  N   . GLN A 1 420 ? 115.410 106.834 126.664 1.00 23.18  ? 420 GLN A N   1 
ATOM   3184 C  CA  . GLN A 1 420 ? 116.481 105.844 126.671 1.00 22.52  ? 420 GLN A CA  1 
ATOM   3185 C  C   . GLN A 1 420 ? 117.652 106.291 125.805 1.00 26.44  ? 420 GLN A C   1 
ATOM   3186 O  O   . GLN A 1 420 ? 118.815 106.096 126.176 1.00 26.20  ? 420 GLN A O   1 
ATOM   3187 C  CB  . GLN A 1 420 ? 115.949 104.490 126.205 1.00 23.61  ? 420 GLN A CB  1 
ATOM   3188 C  CG  . GLN A 1 420 ? 114.706 104.033 126.941 1.00 26.19  ? 420 GLN A CG  1 
ATOM   3189 C  CD  . GLN A 1 420 ? 115.000 102.959 127.963 1.00 36.62  ? 420 GLN A CD  1 
ATOM   3190 O  OE1 . GLN A 1 420 ? 116.156 102.675 128.264 1.00 43.32  ? 420 GLN A OE1 1 
ATOM   3191 N  NE2 . GLN A 1 420 ? 113.952 102.356 128.506 1.00 33.39  ? 420 GLN A NE2 1 
ATOM   3192 N  N   . LEU A 1 421 ? 117.363 106.888 124.647 1.00 24.28  ? 421 LEU A N   1 
ATOM   3193 C  CA  . LEU A 1 421 ? 118.426 107.427 123.806 1.00 17.63  ? 421 LEU A CA  1 
ATOM   3194 C  C   . LEU A 1 421 ? 119.181 108.538 124.523 1.00 26.24  ? 421 LEU A C   1 
ATOM   3195 O  O   . LEU A 1 421 ? 120.420 108.572 124.503 1.00 35.79  ? 421 LEU A O   1 
ATOM   3196 C  CB  . LEU A 1 421 ? 117.843 107.932 122.487 1.00 19.32  ? 421 LEU A CB  1 
ATOM   3197 C  CG  . LEU A 1 421 ? 118.815 108.259 121.355 1.00 21.82  ? 421 LEU A CG  1 
ATOM   3198 C  CD1 . LEU A 1 421 ? 119.590 107.026 120.926 1.00 23.69  ? 421 LEU A CD1 1 
ATOM   3199 C  CD2 . LEU A 1 421 ? 118.068 108.856 120.178 1.00 25.10  ? 421 LEU A CD2 1 
ATOM   3200 N  N   . LEU A 1 422 ? 118.453 109.449 125.178 1.00 30.23  ? 422 LEU A N   1 
ATOM   3201 C  CA  . LEU A 1 422 ? 119.121 110.500 125.942 1.00 23.84  ? 422 LEU A CA  1 
ATOM   3202 C  C   . LEU A 1 422 ? 120.019 109.910 127.022 1.00 29.18  ? 422 LEU A C   1 
ATOM   3203 O  O   . LEU A 1 422 ? 121.163 110.349 127.199 1.00 31.22  ? 422 LEU A O   1 
ATOM   3204 C  CB  . LEU A 1 422 ? 118.093 111.439 126.573 1.00 25.20  ? 422 LEU A CB  1 
ATOM   3205 C  CG  . LEU A 1 422 ? 117.400 112.485 125.702 1.00 31.29  ? 422 LEU A CG  1 
ATOM   3206 C  CD1 . LEU A 1 422 ? 116.277 113.136 126.484 1.00 29.52  ? 422 LEU A CD1 1 
ATOM   3207 C  CD2 . LEU A 1 422 ? 118.386 113.528 125.224 1.00 30.99  ? 422 LEU A CD2 1 
ATOM   3208 N  N   . CYS A 1 423 ? 119.520 108.909 127.749 1.00 30.04  ? 423 CYS A N   1 
ATOM   3209 C  CA  . CYS A 1 423 ? 120.294 108.322 128.838 1.00 26.17  ? 423 CYS A CA  1 
ATOM   3210 C  C   . CYS A 1 423 ? 121.543 107.614 128.328 1.00 33.43  ? 423 CYS A C   1 
ATOM   3211 O  O   . CYS A 1 423 ? 122.617 107.743 128.925 1.00 32.55  ? 423 CYS A O   1 
ATOM   3212 C  CB  . CYS A 1 423 ? 119.421 107.361 129.641 1.00 26.97  ? 423 CYS A CB  1 
ATOM   3213 S  SG  . CYS A 1 423 ? 118.362 108.168 130.859 1.00 53.94  ? 423 CYS A SG  1 
ATOM   3214 N  N   . VAL A 1 424 ? 121.430 106.853 127.235 1.00 34.61  ? 424 VAL A N   1 
ATOM   3215 C  CA  . VAL A 1 424 ? 122.602 106.127 126.750 1.00 23.19  ? 424 VAL A CA  1 
ATOM   3216 C  C   . VAL A 1 424 ? 123.623 107.079 126.141 1.00 34.65  ? 424 VAL A C   1 
ATOM   3217 O  O   . VAL A 1 424 ? 124.831 106.823 126.214 1.00 37.10  ? 424 VAL A O   1 
ATOM   3218 C  CB  . VAL A 1 424 ? 122.214 105.016 125.753 1.00 19.13  ? 424 VAL A CB  1 
ATOM   3219 C  CG1 . VAL A 1 424 ? 121.310 104.000 126.414 1.00 33.43  ? 424 VAL A CG1 1 
ATOM   3220 C  CG2 . VAL A 1 424 ? 121.570 105.590 124.505 1.00 20.34  ? 424 VAL A CG2 1 
ATOM   3221 N  N   . LEU A 1 425 ? 123.180 108.183 125.535 1.00 29.50  ? 425 LEU A N   1 
ATOM   3222 C  CA  . LEU A 1 425 ? 124.144 109.047 124.862 1.00 20.66  ? 425 LEU A CA  1 
ATOM   3223 C  C   . LEU A 1 425 ? 124.805 110.032 125.822 1.00 31.31  ? 425 LEU A C   1 
ATOM   3224 O  O   . LEU A 1 425 ? 126.033 110.168 125.826 1.00 36.58  ? 425 LEU A O   1 
ATOM   3225 C  CB  . LEU A 1 425 ? 123.473 109.794 123.708 1.00 26.30  ? 425 LEU A CB  1 
ATOM   3226 C  CG  . LEU A 1 425 ? 123.235 108.988 122.431 1.00 22.18  ? 425 LEU A CG  1 
ATOM   3227 C  CD1 . LEU A 1 425 ? 122.848 109.908 121.291 1.00 15.02  ? 425 LEU A CD1 1 
ATOM   3228 C  CD2 . LEU A 1 425 ? 124.463 108.175 122.070 1.00 26.93  ? 425 LEU A CD2 1 
ATOM   3229 N  N   . PHE A 1 426 ? 124.018 110.727 126.646 1.00 32.43  ? 426 PHE A N   1 
ATOM   3230 C  CA  . PHE A 1 426 ? 124.538 111.865 127.392 1.00 23.37  ? 426 PHE A CA  1 
ATOM   3231 C  C   . PHE A 1 426 ? 124.641 111.650 128.896 1.00 28.51  ? 426 PHE A C   1 
ATOM   3232 O  O   . PHE A 1 426 ? 125.239 112.489 129.577 1.00 38.21  ? 426 PHE A O   1 
ATOM   3233 C  CB  . PHE A 1 426 ? 123.676 113.107 127.124 1.00 25.17  ? 426 PHE A CB  1 
ATOM   3234 C  CG  . PHE A 1 426 ? 123.440 113.375 125.667 1.00 34.72  ? 426 PHE A CG  1 
ATOM   3235 C  CD1 . PHE A 1 426 ? 124.478 113.776 124.847 1.00 26.34  ? 426 PHE A CD1 1 
ATOM   3236 C  CD2 . PHE A 1 426 ? 122.179 113.227 125.117 1.00 31.10  ? 426 PHE A CD2 1 
ATOM   3237 C  CE1 . PHE A 1 426 ? 124.263 114.021 123.509 1.00 27.03  ? 426 PHE A CE1 1 
ATOM   3238 C  CE2 . PHE A 1 426 ? 121.959 113.474 123.780 1.00 23.43  ? 426 PHE A CE2 1 
ATOM   3239 C  CZ  . PHE A 1 426 ? 123.002 113.871 122.976 1.00 29.90  ? 426 PHE A CZ  1 
ATOM   3240 N  N   . VAL A 1 427 ? 124.093 110.565 129.435 1.00 36.63  ? 427 VAL A N   1 
ATOM   3241 C  CA  . VAL A 1 427 ? 124.107 110.309 130.872 1.00 34.87  ? 427 VAL A CA  1 
ATOM   3242 C  C   . VAL A 1 427 ? 125.067 109.162 131.152 1.00 43.31  ? 427 VAL A C   1 
ATOM   3243 O  O   . VAL A 1 427 ? 124.985 108.104 130.516 1.00 50.65  ? 427 VAL A O   1 
ATOM   3244 C  CB  . VAL A 1 427 ? 122.698 109.996 131.406 1.00 35.30  ? 427 VAL A CB  1 
ATOM   3245 C  CG1 . VAL A 1 427 ? 122.756 109.670 132.887 1.00 37.77  ? 427 VAL A CG1 1 
ATOM   3246 C  CG2 . VAL A 1 427 ? 121.768 111.168 131.159 1.00 35.88  ? 427 VAL A CG2 1 
ATOM   3247 N  N   . LYS A 1 428 ? 125.976 109.374 132.098 1.00 50.94  ? 428 LYS A N   1 
ATOM   3248 C  CA  . LYS A 1 428 ? 126.973 108.381 132.472 1.00 48.66  ? 428 LYS A CA  1 
ATOM   3249 C  C   . LYS A 1 428 ? 126.583 107.738 133.794 1.00 54.58  ? 428 LYS A C   1 
ATOM   3250 O  O   . LYS A 1 428 ? 126.203 108.434 134.741 1.00 63.68  ? 428 LYS A O   1 
ATOM   3251 C  CB  . LYS A 1 428 ? 128.358 109.018 132.584 1.00 49.27  ? 428 LYS A CB  1 
ATOM   3252 C  CG  . LYS A 1 428 ? 129.472 108.028 132.866 1.00 54.79  ? 428 LYS A CG  1 
ATOM   3253 C  CD  . LYS A 1 428 ? 130.748 108.737 133.287 1.00 55.70  ? 428 LYS A CD  1 
ATOM   3254 C  CE  . LYS A 1 428 ? 131.864 107.743 133.564 1.00 55.19  ? 428 LYS A CE  1 
ATOM   3255 N  NZ  . LYS A 1 428 ? 133.196 108.406 133.598 1.00 57.67  ? 428 LYS A NZ  1 
ATOM   3256 N  N   . GLY A 1 429 ? 126.681 106.415 133.857 1.00 45.58  ? 429 GLY A N   1 
ATOM   3257 C  CA  . GLY A 1 429 ? 126.304 105.678 135.041 1.00 45.29  ? 429 GLY A CA  1 
ATOM   3258 C  C   . GLY A 1 429 ? 124.963 104.985 134.977 1.00 48.66  ? 429 GLY A C   1 
ATOM   3259 O  O   . GLY A 1 429 ? 124.532 104.422 135.990 1.00 54.34  ? 429 GLY A O   1 
ATOM   3260 N  N   . THR A 1 430 ? 124.288 105.011 133.831 1.00 48.90  ? 430 THR A N   1 
ATOM   3261 C  CA  . THR A 1 430 ? 123.017 104.315 133.693 1.00 52.17  ? 430 THR A CA  1 
ATOM   3262 C  C   . THR A 1 430 ? 123.231 102.807 133.659 1.00 51.80  ? 430 THR A C   1 
ATOM   3263 O  O   . THR A 1 430 ? 124.206 102.314 133.087 1.00 53.10  ? 430 THR A O   1 
ATOM   3264 C  CB  . THR A 1 430 ? 122.294 104.765 132.424 1.00 49.27  ? 430 THR A CB  1 
ATOM   3265 O  OG1 . THR A 1 430 ? 123.250 105.004 131.385 1.00 47.56  ? 430 THR A OG1 1 
ATOM   3266 C  CG2 . THR A 1 430 ? 121.504 106.037 132.682 1.00 49.91  ? 430 THR A CG2 1 
ATOM   3267 N  N   . ASN A 1 431 ? 122.313 102.077 134.279 1.00 49.79  ? 431 ASN A N   1 
ATOM   3268 C  CA  . ASN A 1 431 ? 122.309 100.622 134.286 1.00 40.88  ? 431 ASN A CA  1 
ATOM   3269 C  C   . ASN A 1 431 ? 121.038 100.121 133.608 1.00 49.23  ? 431 ASN A C   1 
ATOM   3270 O  O   . ASN A 1 431 ? 120.226 100.900 133.107 1.00 57.80  ? 431 ASN A O   1 
ATOM   3271 C  CB  . ASN A 1 431 ? 122.411 100.077 135.712 1.00 47.43  ? 431 ASN A CB  1 
ATOM   3272 C  CG  . ASN A 1 431 ? 123.331 100.897 136.587 1.00 53.37  ? 431 ASN A CG  1 
ATOM   3273 O  OD1 . ASN A 1 431 ? 124.469 101.180 136.218 1.00 55.90  ? 431 ASN A OD1 1 
ATOM   3274 N  ND2 . ASN A 1 431 ? 122.841 101.286 137.757 1.00 53.30  ? 431 ASN A ND2 1 
ATOM   3275 N  N   . THR A 1 432 ? 120.872 98.799  133.594 1.00 48.59  ? 432 THR A N   1 
ATOM   3276 C  CA  . THR A 1 432 ? 119.663 98.203  133.041 1.00 48.06  ? 432 THR A CA  1 
ATOM   3277 C  C   . THR A 1 432 ? 118.487 98.243  134.010 1.00 47.18  ? 432 THR A C   1 
ATOM   3278 O  O   . THR A 1 432 ? 117.338 98.121  133.569 1.00 53.22  ? 432 THR A O   1 
ATOM   3279 C  CB  . THR A 1 432 ? 119.940 96.761  132.610 1.00 49.06  ? 432 THR A CB  1 
ATOM   3280 O  OG1 . THR A 1 432 ? 118.745 96.177  132.076 1.00 53.84  ? 432 THR A OG1 1 
ATOM   3281 C  CG2 . THR A 1 432 ? 120.423 95.944  133.783 1.00 51.86  ? 432 THR A CG2 1 
ATOM   3282 N  N   . TYR A 1 433 ? 118.744 98.416  135.309 1.00 48.53  ? 433 TYR A N   1 
ATOM   3283 C  CA  . TYR A 1 433 ? 117.653 98.568  136.268 1.00 51.06  ? 433 TYR A CA  1 
ATOM   3284 C  C   . TYR A 1 433 ? 116.821 99.803  135.954 1.00 51.28  ? 433 TYR A C   1 
ATOM   3285 O  O   . TYR A 1 433 ? 115.584 99.742  135.897 1.00 55.03  ? 433 TYR A O   1 
ATOM   3286 C  CB  . TYR A 1 433 ? 118.213 98.651  137.688 1.00 48.22  ? 433 TYR A CB  1 
ATOM   3287 C  CG  . TYR A 1 433 ? 118.995 97.436  138.126 1.00 51.66  ? 433 TYR A CG  1 
ATOM   3288 C  CD1 . TYR A 1 433 ? 118.354 96.338  138.680 1.00 52.48  ? 433 TYR A CD1 1 
ATOM   3289 C  CD2 . TYR A 1 433 ? 120.375 97.390  137.994 1.00 53.07  ? 433 TYR A CD2 1 
ATOM   3290 C  CE1 . TYR A 1 433 ? 119.064 95.227  139.086 1.00 52.61  ? 433 TYR A CE1 1 
ATOM   3291 C  CE2 . TYR A 1 433 ? 121.094 96.282  138.397 1.00 56.41  ? 433 TYR A CE2 1 
ATOM   3292 C  CZ  . TYR A 1 433 ? 120.434 95.204  138.941 1.00 53.96  ? 433 TYR A CZ  1 
ATOM   3293 O  OH  . TYR A 1 433 ? 121.144 94.098  139.343 1.00 51.46  ? 433 TYR A OH  1 
ATOM   3294 N  N   . GLY A 1 434 ? 117.489 100.937 135.741 1.00 36.83  ? 434 GLY A N   1 
ATOM   3295 C  CA  . GLY A 1 434 ? 116.783 102.141 135.350 1.00 34.73  ? 434 GLY A CA  1 
ATOM   3296 C  C   . GLY A 1 434 ? 116.094 102.010 134.009 1.00 34.11  ? 434 GLY A C   1 
ATOM   3297 O  O   . GLY A 1 434 ? 115.019 102.574 133.804 1.00 41.01  ? 434 GLY A O   1 
ATOM   3298 N  N   . ALA A 1 435 ? 116.699 101.269 133.079 1.00 26.36  ? 435 ALA A N   1 
ATOM   3299 C  CA  . ALA A 1 435 ? 116.069 101.052 131.781 1.00 29.15  ? 435 ALA A CA  1 
ATOM   3300 C  C   . ALA A 1 435 ? 114.756 100.294 131.930 1.00 40.32  ? 435 ALA A C   1 
ATOM   3301 O  O   . ALA A 1 435 ? 113.736 100.669 131.337 1.00 44.11  ? 435 ALA A O   1 
ATOM   3302 C  CB  . ALA A 1 435 ? 117.027 100.303 130.857 1.00 30.26  ? 435 ALA A CB  1 
ATOM   3303 N  N   . VAL A 1 436 ? 114.758 99.230  132.739 1.00 32.83  ? 436 VAL A N   1 
ATOM   3304 C  CA  . VAL A 1 436 ? 113.533 98.469  132.976 1.00 25.10  ? 436 VAL A CA  1 
ATOM   3305 C  C   . VAL A 1 436 ? 112.489 99.339  133.665 1.00 30.64  ? 436 VAL A C   1 
ATOM   3306 O  O   . VAL A 1 436 ? 111.303 99.322  133.301 1.00 38.66  ? 436 VAL A O   1 
ATOM   3307 C  CB  . VAL A 1 436 ? 113.844 97.200  133.793 1.00 31.11  ? 436 VAL A CB  1 
ATOM   3308 C  CG1 . VAL A 1 436 ? 112.562 96.491  134.191 1.00 31.58  ? 436 VAL A CG1 1 
ATOM   3309 C  CG2 . VAL A 1 436 ? 114.742 96.266  133.004 1.00 33.18  ? 436 VAL A CG2 1 
ATOM   3310 N  N   . ALA A 1 437 ? 112.910 100.113 134.670 1.00 29.85  ? 437 ALA A N   1 
ATOM   3311 C  CA  . ALA A 1 437 ? 111.970 100.968 135.390 1.00 24.91  ? 437 ALA A CA  1 
ATOM   3312 C  C   . ALA A 1 437 ? 111.333 101.996 134.462 1.00 27.66  ? 437 ALA A C   1 
ATOM   3313 O  O   . ALA A 1 437 ? 110.113 102.207 134.492 1.00 36.89  ? 437 ALA A O   1 
ATOM   3314 C  CB  . ALA A 1 437 ? 112.680 101.657 136.553 1.00 28.21  ? 437 ALA A CB  1 
ATOM   3315 N  N   . GLY A 1 438 ? 112.145 102.642 133.622 1.00 18.63  ? 438 GLY A N   1 
ATOM   3316 C  CA  . GLY A 1 438 ? 111.610 103.620 132.692 1.00 14.88  ? 438 GLY A CA  1 
ATOM   3317 C  C   . GLY A 1 438 ? 110.686 103.003 131.663 1.00 25.84  ? 438 GLY A C   1 
ATOM   3318 O  O   . GLY A 1 438 ? 109.652 103.581 131.320 1.00 38.19  ? 438 GLY A O   1 
ATOM   3319 N  N   . TYR A 1 439 ? 111.044 101.820 131.157 1.00 28.37  ? 439 TYR A N   1 
ATOM   3320 C  CA  . TYR A 1 439 ? 110.181 101.118 130.212 1.00 27.21  ? 439 TYR A CA  1 
ATOM   3321 C  C   . TYR A 1 439 ? 108.812 100.845 130.823 1.00 27.17  ? 439 TYR A C   1 
ATOM   3322 O  O   . TYR A 1 439 ? 107.774 101.144 130.217 1.00 24.22  ? 439 TYR A O   1 
ATOM   3323 C  CB  . TYR A 1 439 ? 110.856 99.815  129.780 1.00 25.30  ? 439 TYR A CB  1 
ATOM   3324 C  CG  . TYR A 1 439 ? 110.301 99.179  128.526 1.00 25.03  ? 439 TYR A CG  1 
ATOM   3325 C  CD1 . TYR A 1 439 ? 109.245 98.281  128.588 1.00 32.37  ? 439 TYR A CD1 1 
ATOM   3326 C  CD2 . TYR A 1 439 ? 110.848 99.456  127.282 1.00 27.05  ? 439 TYR A CD2 1 
ATOM   3327 C  CE1 . TYR A 1 439 ? 108.742 97.691  127.448 1.00 34.41  ? 439 TYR A CE1 1 
ATOM   3328 C  CE2 . TYR A 1 439 ? 110.351 98.870  126.137 1.00 27.79  ? 439 TYR A CE2 1 
ATOM   3329 C  CZ  . TYR A 1 439 ? 109.298 97.988  126.226 1.00 33.82  ? 439 TYR A CZ  1 
ATOM   3330 O  OH  . TYR A 1 439 ? 108.799 97.401  125.087 1.00 33.61  ? 439 TYR A OH  1 
ATOM   3331 N  N   . VAL A 1 440 ? 108.794 100.300 132.043 1.00 27.83  ? 440 VAL A N   1 
ATOM   3332 C  CA  . VAL A 1 440 ? 107.527 99.969  132.691 1.00 22.80  ? 440 VAL A CA  1 
ATOM   3333 C  C   . VAL A 1 440 ? 106.709 101.228 132.958 1.00 28.24  ? 440 VAL A C   1 
ATOM   3334 O  O   . VAL A 1 440 ? 105.497 101.259 132.710 1.00 33.55  ? 440 VAL A O   1 
ATOM   3335 C  CB  . VAL A 1 440 ? 107.777 99.170  133.983 1.00 25.77  ? 440 VAL A CB  1 
ATOM   3336 C  CG1 . VAL A 1 440 ? 106.474 98.944  134.727 1.00 29.11  ? 440 VAL A CG1 1 
ATOM   3337 C  CG2 . VAL A 1 440 ? 108.436 97.841  133.664 1.00 24.57  ? 440 VAL A CG2 1 
ATOM   3338 N  N   . SER A 1 441 ? 107.351 102.285 133.469 1.00 27.03  ? 441 SER A N   1 
ATOM   3339 C  CA  . SER A 1 441 ? 106.622 103.511 133.787 1.00 25.08  ? 441 SER A CA  1 
ATOM   3340 C  C   . SER A 1 441 ? 106.022 104.141 132.535 1.00 31.55  ? 441 SER A C   1 
ATOM   3341 O  O   . SER A 1 441 ? 104.854 104.558 132.531 1.00 38.01  ? 441 SER A O   1 
ATOM   3342 C  CB  . SER A 1 441 ? 107.546 104.500 134.493 1.00 27.02  ? 441 SER A CB  1 
ATOM   3343 O  OG  . SER A 1 441 ? 108.254 103.868 135.542 1.00 37.40  ? 441 SER A OG  1 
ATOM   3344 N  N   . GLY A 1 442 ? 106.809 104.223 131.460 1.00 23.69  ? 442 GLY A N   1 
ATOM   3345 C  CA  . GLY A 1 442 ? 106.299 104.797 130.229 1.00 22.32  ? 442 GLY A CA  1 
ATOM   3346 C  C   . GLY A 1 442 ? 105.166 103.987 129.634 1.00 33.66  ? 442 GLY A C   1 
ATOM   3347 O  O   . GLY A 1 442 ? 104.183 104.548 129.144 1.00 39.41  ? 442 GLY A O   1 
ATOM   3348 N  N   . LEU A 1 443 ? 105.284 102.657 129.665 1.00 35.48  ? 443 LEU A N   1 
ATOM   3349 C  CA  . LEU A 1 443 ? 104.211 101.822 129.139 1.00 31.69  ? 443 LEU A CA  1 
ATOM   3350 C  C   . LEU A 1 443 ? 102.938 101.971 129.964 1.00 34.24  ? 443 LEU A C   1 
ATOM   3351 O  O   . LEU A 1 443 ? 101.834 102.023 129.411 1.00 35.35  ? 443 LEU A O   1 
ATOM   3352 C  CB  . LEU A 1 443 ? 104.658 100.362 129.093 1.00 37.44  ? 443 LEU A CB  1 
ATOM   3353 C  CG  . LEU A 1 443 ? 104.002 99.469  128.039 1.00 35.25  ? 443 LEU A CG  1 
ATOM   3354 C  CD1 . LEU A 1 443 ? 103.699 100.254 126.775 1.00 36.55  ? 443 LEU A CD1 1 
ATOM   3355 C  CD2 . LEU A 1 443 ? 104.894 98.281  127.729 1.00 35.67  ? 443 LEU A CD2 1 
ATOM   3356 N  N   . PHE A 1 444 ? 103.070 102.042 131.291 1.00 32.07  ? 444 PHE A N   1 
ATOM   3357 C  CA  . PHE A 1 444 ? 101.892 102.128 132.148 1.00 30.75  ? 444 PHE A CA  1 
ATOM   3358 C  C   . PHE A 1 444 ? 101.176 103.463 131.987 1.00 33.38  ? 444 PHE A C   1 
ATOM   3359 O  O   . PHE A 1 444 ? 99.945  103.503 131.853 1.00 34.15  ? 444 PHE A O   1 
ATOM   3360 C  CB  . PHE A 1 444 ? 102.296 101.911 133.606 1.00 34.97  ? 444 PHE A CB  1 
ATOM   3361 C  CG  . PHE A 1 444 ? 101.151 101.984 134.574 1.00 37.86  ? 444 PHE A CG  1 
ATOM   3362 C  CD1 . PHE A 1 444 ? 100.251 100.939 134.684 1.00 38.24  ? 444 PHE A CD1 1 
ATOM   3363 C  CD2 . PHE A 1 444 ? 100.980 103.096 135.380 1.00 40.59  ? 444 PHE A CD2 1 
ATOM   3364 C  CE1 . PHE A 1 444 ? 99.200  101.004 135.579 1.00 38.89  ? 444 PHE A CE1 1 
ATOM   3365 C  CE2 . PHE A 1 444 ? 99.929  103.167 136.275 1.00 37.59  ? 444 PHE A CE2 1 
ATOM   3366 C  CZ  . PHE A 1 444 ? 99.039  102.119 136.375 1.00 39.27  ? 444 PHE A CZ  1 
ATOM   3367 N  N   . LEU A 1 445 ? 101.925 104.569 131.993 1.00 38.15  ? 445 LEU A N   1 
ATOM   3368 C  CA  . LEU A 1 445 ? 101.309 105.891 131.994 1.00 32.93  ? 445 LEU A CA  1 
ATOM   3369 C  C   . LEU A 1 445 ? 100.628 106.250 130.679 1.00 34.19  ? 445 LEU A C   1 
ATOM   3370 O  O   . LEU A 1 445 ? 99.844  107.203 130.653 1.00 40.97  ? 445 LEU A O   1 
ATOM   3371 C  CB  . LEU A 1 445 ? 102.349 106.960 132.337 1.00 34.29  ? 445 LEU A CB  1 
ATOM   3372 C  CG  . LEU A 1 445 ? 102.570 107.215 133.827 1.00 38.16  ? 445 LEU A CG  1 
ATOM   3373 C  CD1 . LEU A 1 445 ? 103.522 108.375 134.032 1.00 37.07  ? 445 LEU A CD1 1 
ATOM   3374 C  CD2 . LEU A 1 445 ? 101.249 107.477 134.525 1.00 36.02  ? 445 LEU A CD2 1 
ATOM   3375 N  N   . ARG A 1 446 ? 100.898 105.527 129.594 1.00 33.71  ? 446 ARG A N   1 
ATOM   3376 C  CA  . ARG A 1 446 ? 100.218 105.768 128.328 1.00 34.50  ? 446 ARG A CA  1 
ATOM   3377 C  C   . ARG A 1 446 ? 98.975  104.906 128.160 1.00 43.63  ? 446 ARG A C   1 
ATOM   3378 O  O   . ARG A 1 446 ? 97.952  105.393 127.670 1.00 41.68  ? 446 ARG A O   1 
ATOM   3379 C  CB  . ARG A 1 446 ? 101.174 105.528 127.155 1.00 33.77  ? 446 ARG A CB  1 
ATOM   3380 C  CG  . ARG A 1 446 ? 100.529 105.642 125.782 1.00 32.27  ? 446 ARG A CG  1 
ATOM   3381 C  CD  . ARG A 1 446 ? 99.886  107.005 125.588 1.00 35.66  ? 446 ARG A CD  1 
ATOM   3382 N  NE  . ARG A 1 446 ? 99.295  107.156 124.263 1.00 42.90  ? 446 ARG A NE  1 
ATOM   3383 C  CZ  . ARG A 1 446 ? 97.994  107.257 124.028 1.00 40.05  ? 446 ARG A CZ  1 
ATOM   3384 N  NH1 . ARG A 1 446 ? 97.107  107.197 125.006 1.00 32.41  ? 446 ARG A NH1 1 
ATOM   3385 N  NH2 . ARG A 1 446 ? 97.572  107.421 122.778 1.00 36.71  ? 446 ARG A NH2 1 
ATOM   3386 N  N   . ILE A 1 447 ? 99.040  103.636 128.560 1.00 49.22  ? 447 ILE A N   1 
ATOM   3387 C  CA  . ILE A 1 447 ? 97.855  102.784 128.539 1.00 40.82  ? 447 ILE A CA  1 
ATOM   3388 C  C   . ILE A 1 447 ? 96.803  103.308 129.506 1.00 39.77  ? 447 ILE A C   1 
ATOM   3389 O  O   . ILE A 1 447 ? 95.613  103.365 129.178 1.00 37.77  ? 447 ILE A O   1 
ATOM   3390 C  CB  . ILE A 1 447 ? 98.238  101.325 128.849 1.00 43.55  ? 447 ILE A CB  1 
ATOM   3391 C  CG1 . ILE A 1 447 ? 99.224  100.798 127.806 1.00 43.23  ? 447 ILE A CG1 1 
ATOM   3392 C  CG2 . ILE A 1 447 ? 97.000  100.449 128.902 1.00 44.67  ? 447 ILE A CG2 1 
ATOM   3393 C  CD1 . ILE A 1 447 ? 98.790  101.035 126.375 1.00 40.95  ? 447 ILE A CD1 1 
ATOM   3394 N  N   . THR A 1 448 ? 97.219  103.704 130.711 1.00 45.74  ? 448 THR A N   1 
ATOM   3395 C  CA  . THR A 1 448 ? 96.290  104.378 131.609 1.00 43.37  ? 448 THR A CA  1 
ATOM   3396 C  C   . THR A 1 448 ? 95.996  105.770 131.066 1.00 50.99  ? 448 THR A C   1 
ATOM   3397 O  O   . THR A 1 448 ? 96.828  106.678 131.170 1.00 57.10  ? 448 THR A O   1 
ATOM   3398 C  CB  . THR A 1 448 ? 96.848  104.451 133.029 1.00 49.49  ? 448 THR A CB  1 
ATOM   3399 O  OG1 . THR A 1 448 ? 98.165  105.014 132.997 1.00 62.05  ? 448 THR A OG1 1 
ATOM   3400 C  CG2 . THR A 1 448 ? 96.905  103.064 133.644 1.00 45.95  ? 448 THR A CG2 1 
ATOM   3401 N  N   . GLY A 1 449 ? 94.810  105.944 130.494 1.00 55.54  ? 449 GLY A N   1 
ATOM   3402 C  CA  . GLY A 1 449 ? 94.503  107.098 129.673 1.00 53.24  ? 449 GLY A CA  1 
ATOM   3403 C  C   . GLY A 1 449 ? 94.203  106.626 128.267 1.00 56.19  ? 449 GLY A C   1 
ATOM   3404 O  O   . GLY A 1 449 ? 95.114  106.257 127.521 1.00 60.72  ? 449 GLY A O   1 
ATOM   3405 N  N   . GLY A 1 450 ? 92.930  106.639 127.892 1.00 61.76  ? 450 GLY A N   1 
ATOM   3406 C  CA  . GLY A 1 450 ? 92.466  105.907 126.735 1.00 60.38  ? 450 GLY A CA  1 
ATOM   3407 C  C   . GLY A 1 450 ? 92.822  106.567 125.420 1.00 61.45  ? 450 GLY A C   1 
ATOM   3408 O  O   . GLY A 1 450 ? 93.470  107.612 125.354 1.00 64.93  ? 450 GLY A O   1 
ATOM   3409 N  N   . GLU A 1 451 ? 92.385  105.916 124.343 1.00 63.05  ? 451 GLU A N   1 
ATOM   3410 C  CA  . GLU A 1 451 ? 92.608  106.398 122.982 1.00 64.35  ? 451 GLU A CA  1 
ATOM   3411 C  C   . GLU A 1 451 ? 91.265  106.389 122.262 1.00 66.17  ? 451 GLU A C   1 
ATOM   3412 O  O   . GLU A 1 451 ? 90.748  105.315 121.914 1.00 66.14  ? 451 GLU A O   1 
ATOM   3413 C  CB  . GLU A 1 451 ? 93.637  105.540 122.251 1.00 62.75  ? 451 GLU A CB  1 
ATOM   3414 C  CG  . GLU A 1 451 ? 94.502  106.312 121.271 1.00 64.21  ? 451 GLU A CG  1 
ATOM   3415 C  CD  . GLU A 1 451 ? 93.949  106.297 119.865 1.00 65.97  ? 451 GLU A CD  1 
ATOM   3416 O  OE1 . GLU A 1 451 ? 92.935  105.608 119.637 1.00 68.87  ? 451 GLU A OE1 1 
ATOM   3417 O  OE2 . GLU A 1 451 ? 94.524  106.976 118.990 1.00 62.95  ? 451 GLU A OE2 1 
ATOM   3418 N  N   . PRO A 1 452 ? 90.658  107.562 122.045 1.00 70.78  ? 452 PRO A N   1 
ATOM   3419 C  CA  . PRO A 1 452 ? 89.331  107.616 121.413 1.00 71.02  ? 452 PRO A CA  1 
ATOM   3420 C  C   . PRO A 1 452 ? 89.250  106.925 120.059 1.00 71.90  ? 452 PRO A C   1 
ATOM   3421 O  O   . PRO A 1 452 ? 88.238  106.289 119.747 1.00 70.43  ? 452 PRO A O   1 
ATOM   3422 C  CB  . PRO A 1 452 ? 89.071  109.124 121.266 1.00 69.75  ? 452 PRO A CB  1 
ATOM   3423 C  CG  . PRO A 1 452 ? 90.273  109.826 121.857 1.00 70.15  ? 452 PRO A CG  1 
ATOM   3424 C  CD  . PRO A 1 452 ? 91.012  108.838 122.681 1.00 70.64  ? 452 PRO A CD  1 
ATOM   3425 N  N   . TYR A 1 453 ? 90.301  107.042 119.246 1.00 65.50  ? 453 TYR A N   1 
ATOM   3426 C  CA  . TYR A 1 453 ? 90.265  106.477 117.901 1.00 61.30  ? 453 TYR A CA  1 
ATOM   3427 C  C   . TYR A 1 453 ? 90.178  104.956 117.907 1.00 64.05  ? 453 TYR A C   1 
ATOM   3428 O  O   . TYR A 1 453 ? 89.767  104.369 116.900 1.00 67.94  ? 453 TYR A O   1 
ATOM   3429 C  CB  . TYR A 1 453 ? 91.494  106.926 117.111 1.00 64.23  ? 453 TYR A CB  1 
ATOM   3430 C  CG  . TYR A 1 453 ? 91.215  108.051 116.145 1.00 63.15  ? 453 TYR A CG  1 
ATOM   3431 C  CD1 . TYR A 1 453 ? 91.205  109.371 116.573 1.00 66.59  ? 453 TYR A CD1 1 
ATOM   3432 C  CD2 . TYR A 1 453 ? 90.965  107.796 114.805 1.00 63.74  ? 453 TYR A CD2 1 
ATOM   3433 C  CE1 . TYR A 1 453 ? 90.950  110.405 115.695 1.00 66.75  ? 453 TYR A CE1 1 
ATOM   3434 C  CE2 . TYR A 1 453 ? 90.710  108.823 113.919 1.00 68.46  ? 453 TYR A CE2 1 
ATOM   3435 C  CZ  . TYR A 1 453 ? 90.703  110.125 114.370 1.00 69.54  ? 453 TYR A CZ  1 
ATOM   3436 O  OH  . TYR A 1 453 ? 90.450  111.152 113.491 1.00 70.57  ? 453 TYR A OH  1 
ATOM   3437 N  N   . LEU A 1 454 ? 90.559  104.307 119.006 1.00 61.30  ? 454 LEU A N   1 
ATOM   3438 C  CA  . LEU A 1 454 ? 90.428  102.864 119.157 1.00 60.93  ? 454 LEU A CA  1 
ATOM   3439 C  C   . LEU A 1 454 ? 89.285  102.495 120.098 1.00 64.03  ? 454 LEU A C   1 
ATOM   3440 O  O   . LEU A 1 454 ? 89.153  101.335 120.497 1.00 68.09  ? 454 LEU A O   1 
ATOM   3441 C  CB  . LEU A 1 454 ? 91.740  102.253 119.645 1.00 59.43  ? 454 LEU A CB  1 
ATOM   3442 C  CG  . LEU A 1 454 ? 92.927  102.366 118.687 1.00 59.69  ? 454 LEU A CG  1 
ATOM   3443 C  CD1 . LEU A 1 454 ? 94.199  101.865 119.348 1.00 59.93  ? 454 LEU A CD1 1 
ATOM   3444 C  CD2 . LEU A 1 454 ? 92.652  101.608 117.401 1.00 59.04  ? 454 LEU A CD2 1 
ATOM   3445 N  N   . TYR A 1 455 ? 88.457  103.477 120.458 1.00 71.99  ? 455 TYR A N   1 
ATOM   3446 C  CA  . TYR A 1 455 ? 87.292  103.268 121.321 1.00 73.89  ? 455 TYR A CA  1 
ATOM   3447 C  C   . TYR A 1 455 ? 87.690  102.652 122.661 1.00 74.63  ? 455 TYR A C   1 
ATOM   3448 O  O   . TYR A 1 455 ? 87.081  101.690 123.134 1.00 75.22  ? 455 TYR A O   1 
ATOM   3449 C  CB  . TYR A 1 455 ? 86.236  102.414 120.616 1.00 72.97  ? 455 TYR A CB  1 
ATOM   3450 C  CG  . TYR A 1 455 ? 85.515  103.145 119.506 1.00 74.17  ? 455 TYR A CG  1 
ATOM   3451 C  CD1 . TYR A 1 455 ? 84.672  104.212 119.784 1.00 74.57  ? 455 TYR A CD1 1 
ATOM   3452 C  CD2 . TYR A 1 455 ? 85.687  102.775 118.179 1.00 73.53  ? 455 TYR A CD2 1 
ATOM   3453 C  CE1 . TYR A 1 455 ? 84.015  104.886 118.772 1.00 76.35  ? 455 TYR A CE1 1 
ATOM   3454 C  CE2 . TYR A 1 455 ? 85.034  103.443 117.161 1.00 73.29  ? 455 TYR A CE2 1 
ATOM   3455 C  CZ  . TYR A 1 455 ? 84.200  104.497 117.463 1.00 76.21  ? 455 TYR A CZ  1 
ATOM   3456 O  OH  . TYR A 1 455 ? 83.548  105.165 116.453 1.00 77.46  ? 455 TYR A OH  1 
ATOM   3457 N  N   . LEU A 1 456 ? 88.722  103.217 123.281 1.00 73.61  ? 456 LEU A N   1 
ATOM   3458 C  CA  . LEU A 1 456 ? 89.211  102.768 124.576 1.00 73.70  ? 456 LEU A CA  1 
ATOM   3459 C  C   . LEU A 1 456 ? 88.939  103.843 125.621 1.00 73.13  ? 456 LEU A C   1 
ATOM   3460 O  O   . LEU A 1 456 ? 89.315  105.005 125.442 1.00 71.42  ? 456 LEU A O   1 
ATOM   3461 C  CB  . LEU A 1 456 ? 90.710  102.453 124.516 1.00 70.14  ? 456 LEU A CB  1 
ATOM   3462 C  CG  . LEU A 1 456 ? 91.268  101.302 125.361 1.00 70.96  ? 456 LEU A CG  1 
ATOM   3463 C  CD1 . LEU A 1 456 ? 92.758  101.146 125.110 1.00 72.60  ? 456 LEU A CD1 1 
ATOM   3464 C  CD2 . LEU A 1 456 ? 91.004  101.496 126.845 1.00 70.58  ? 456 LEU A CD2 1 
ATOM   3465 N  N   . GLN A 1 457 ? 88.281  103.448 126.713 1.00 72.77  ? 457 GLN A N   1 
ATOM   3466 C  CA  . GLN A 1 457 ? 87.939  104.396 127.761 1.00 72.66  ? 457 GLN A CA  1 
ATOM   3467 C  C   . GLN A 1 457 ? 89.138  104.669 128.664 1.00 72.57  ? 457 GLN A C   1 
ATOM   3468 O  O   . GLN A 1 457 ? 89.868  103.745 129.035 1.00 73.85  ? 457 GLN A O   1 
ATOM   3469 C  CB  . GLN A 1 457 ? 86.780  103.867 128.601 1.00 70.00  ? 457 GLN A CB  1 
ATOM   3470 C  CG  . GLN A 1 457 ? 85.806  104.939 129.057 1.00 71.87  ? 457 GLN A CG  1 
ATOM   3471 C  CD  . GLN A 1 457 ? 84.711  105.207 128.044 1.00 73.90  ? 457 GLN A CD  1 
ATOM   3472 O  OE1 . GLN A 1 457 ? 84.964  105.279 126.843 1.00 71.94  ? 457 GLN A OE1 1 
ATOM   3473 N  NE2 . GLN A 1 457 ? 83.484  105.357 128.526 1.00 75.84  ? 457 GLN A NE2 1 
ATOM   3474 N  N   . PRO A 1 458 ? 89.361  105.935 129.012 1.00 71.14  ? 458 PRO A N   1 
ATOM   3475 C  CA  . PRO A 1 458 ? 90.439  106.264 129.952 1.00 69.41  ? 458 PRO A CA  1 
ATOM   3476 C  C   . PRO A 1 458 ? 90.261  105.555 131.286 1.00 70.07  ? 458 PRO A C   1 
ATOM   3477 O  O   . PRO A 1 458 ? 89.143  105.369 131.770 1.00 72.87  ? 458 PRO A O   1 
ATOM   3478 C  CB  . PRO A 1 458 ? 90.315  107.788 130.111 1.00 67.67  ? 458 PRO A CB  1 
ATOM   3479 C  CG  . PRO A 1 458 ? 89.076  108.182 129.310 1.00 70.62  ? 458 PRO A CG  1 
ATOM   3480 C  CD  . PRO A 1 458 ? 88.938  107.130 128.274 1.00 72.01  ? 458 PRO A CD  1 
ATOM   3481 N  N   . LEU A 1 459 ? 91.388  105.154 131.879 1.00 67.01  ? 459 LEU A N   1 
ATOM   3482 C  CA  . LEU A 1 459 ? 91.398  104.564 133.209 1.00 66.32  ? 459 LEU A CA  1 
ATOM   3483 C  C   . LEU A 1 459 ? 91.745  105.559 134.306 1.00 67.34  ? 459 LEU A C   1 
ATOM   3484 O  O   . LEU A 1 459 ? 91.226  105.429 135.418 1.00 66.84  ? 459 LEU A O   1 
ATOM   3485 C  CB  . LEU A 1 459 ? 92.389  103.390 133.263 1.00 65.57  ? 459 LEU A CB  1 
ATOM   3486 C  CG  . LEU A 1 459 ? 92.112  102.257 134.254 1.00 69.51  ? 459 LEU A CG  1 
ATOM   3487 C  CD1 . LEU A 1 459 ? 92.661  100.948 133.715 1.00 67.72  ? 459 LEU A CD1 1 
ATOM   3488 C  CD2 . LEU A 1 459 ? 92.711  102.558 135.619 1.00 69.31  ? 459 LEU A CD2 1 
ATOM   3489 N  N   . ILE A 1 460 ? 92.597  106.542 134.023 1.00 65.64  ? 460 ILE A N   1 
ATOM   3490 C  CA  . ILE A 1 460 ? 92.901  107.632 134.943 1.00 63.74  ? 460 ILE A CA  1 
ATOM   3491 C  C   . ILE A 1 460 ? 92.365  108.918 134.334 1.00 64.09  ? 460 ILE A C   1 
ATOM   3492 O  O   . ILE A 1 460 ? 92.656  109.230 133.173 1.00 63.77  ? 460 ILE A O   1 
ATOM   3493 C  CB  . ILE A 1 460 ? 94.410  107.740 135.224 1.00 60.86  ? 460 ILE A CB  1 
ATOM   3494 C  CG1 . ILE A 1 460 ? 94.900  106.515 135.997 1.00 62.51  ? 460 ILE A CG1 1 
ATOM   3495 C  CG2 . ILE A 1 460 ? 94.718  109.009 135.998 1.00 61.66  ? 460 ILE A CG2 1 
ATOM   3496 C  CD1 . ILE A 1 460 ? 96.354  106.594 136.400 1.00 61.34  ? 460 ILE A CD1 1 
ATOM   3497 N  N   . PHE A 1 461 ? 91.580  109.659 135.110 1.00 65.35  ? 461 PHE A N   1 
ATOM   3498 C  CA  . PHE A 1 461 ? 90.895  110.852 134.629 1.00 66.03  ? 461 PHE A CA  1 
ATOM   3499 C  C   . PHE A 1 461 ? 91.630  112.089 135.124 1.00 64.40  ? 461 PHE A C   1 
ATOM   3500 O  O   . PHE A 1 461 ? 91.797  112.276 136.334 1.00 66.83  ? 461 PHE A O   1 
ATOM   3501 C  CB  . PHE A 1 461 ? 89.437  110.858 135.089 1.00 64.63  ? 461 PHE A CB  1 
ATOM   3502 C  CG  . PHE A 1 461 ? 88.600  109.791 134.445 1.00 64.22  ? 461 PHE A CG  1 
ATOM   3503 C  CD1 . PHE A 1 461 ? 88.028  109.998 133.201 1.00 66.00  ? 461 PHE A CD1 1 
ATOM   3504 C  CD2 . PHE A 1 461 ? 88.395  108.577 135.076 1.00 65.16  ? 461 PHE A CD2 1 
ATOM   3505 C  CE1 . PHE A 1 461 ? 87.262  109.017 132.603 1.00 67.04  ? 461 PHE A CE1 1 
ATOM   3506 C  CE2 . PHE A 1 461 ? 87.630  107.592 134.483 1.00 66.91  ? 461 PHE A CE2 1 
ATOM   3507 C  CZ  . PHE A 1 461 ? 87.063  107.812 133.245 1.00 66.52  ? 461 PHE A CZ  1 
ATOM   3508 N  N   . TYR A 1 462 ? 92.064  112.925 134.190 1.00 55.30  ? 462 TYR A N   1 
ATOM   3509 C  CA  . TYR A 1 462 ? 92.812  114.141 134.460 1.00 57.46  ? 462 TYR A CA  1 
ATOM   3510 C  C   . TYR A 1 462 ? 91.884  115.348 134.465 1.00 65.22  ? 462 TYR A C   1 
ATOM   3511 O  O   . TYR A 1 462 ? 90.780  115.297 133.914 1.00 69.27  ? 462 TYR A O   1 
ATOM   3512 C  CB  . TYR A 1 462 ? 93.912  114.316 133.414 1.00 58.45  ? 462 TYR A CB  1 
ATOM   3513 C  CG  . TYR A 1 462 ? 95.025  113.299 133.528 1.00 58.26  ? 462 TYR A CG  1 
ATOM   3514 C  CD1 . TYR A 1 462 ? 96.062  113.473 134.433 1.00 59.51  ? 462 TYR A CD1 1 
ATOM   3515 C  CD2 . TYR A 1 462 ? 95.037  112.163 132.731 1.00 61.17  ? 462 TYR A CD2 1 
ATOM   3516 C  CE1 . TYR A 1 462 ? 97.079  112.546 134.540 1.00 58.77  ? 462 TYR A CE1 1 
ATOM   3517 C  CE2 . TYR A 1 462 ? 96.049  111.231 132.832 1.00 60.32  ? 462 TYR A CE2 1 
ATOM   3518 C  CZ  . TYR A 1 462 ? 97.067  111.427 133.738 1.00 60.38  ? 462 TYR A CZ  1 
ATOM   3519 O  OH  . TYR A 1 462 ? 98.076  110.500 133.840 1.00 61.13  ? 462 TYR A OH  1 
ATOM   3520 N  N   . PRO A 1 463 ? 92.291  116.448 135.100 1.00 66.20  ? 463 PRO A N   1 
ATOM   3521 C  CA  . PRO A 1 463 ? 91.423  117.636 135.156 1.00 64.65  ? 463 PRO A CA  1 
ATOM   3522 C  C   . PRO A 1 463 ? 91.110  118.175 133.769 1.00 65.04  ? 463 PRO A C   1 
ATOM   3523 O  O   . PRO A 1 463 ? 91.997  118.629 133.043 1.00 64.18  ? 463 PRO A O   1 
ATOM   3524 C  CB  . PRO A 1 463 ? 92.249  118.634 135.974 1.00 64.01  ? 463 PRO A CB  1 
ATOM   3525 C  CG  . PRO A 1 463 ? 93.158  117.792 136.788 1.00 62.05  ? 463 PRO A CG  1 
ATOM   3526 C  CD  . PRO A 1 463 ? 93.493  116.609 135.937 1.00 60.65  ? 463 PRO A CD  1 
ATOM   3527 N  N   . GLY A 1 464 ? 89.831  118.129 133.407 1.00 70.12  ? 464 GLY A N   1 
ATOM   3528 C  CA  . GLY A 1 464 ? 89.388  118.679 132.142 1.00 71.13  ? 464 GLY A CA  1 
ATOM   3529 C  C   . GLY A 1 464 ? 88.879  117.648 131.157 1.00 72.67  ? 464 GLY A C   1 
ATOM   3530 O  O   . GLY A 1 464 ? 88.939  117.865 129.944 1.00 72.79  ? 464 GLY A O   1 
ATOM   3531 N  N   . TYR A 1 465 ? 88.372  116.526 131.659 1.00 73.52  ? 465 TYR A N   1 
ATOM   3532 C  CA  . TYR A 1 465 ? 87.864  115.480 130.785 1.00 72.93  ? 465 TYR A CA  1 
ATOM   3533 C  C   . TYR A 1 465 ? 86.424  115.774 130.382 1.00 76.20  ? 465 TYR A C   1 
ATOM   3534 O  O   . TYR A 1 465 ? 85.603  116.180 131.210 1.00 77.78  ? 465 TYR A O   1 
ATOM   3535 C  CB  . TYR A 1 465 ? 87.954  114.116 131.469 1.00 71.12  ? 465 TYR A CB  1 
ATOM   3536 C  CG  . TYR A 1 465 ? 87.152  113.995 132.746 1.00 73.04  ? 465 TYR A CG  1 
ATOM   3537 C  CD1 . TYR A 1 465 ? 87.683  114.391 133.964 1.00 72.90  ? 465 TYR A CD1 1 
ATOM   3538 C  CD2 . TYR A 1 465 ? 85.868  113.466 132.733 1.00 73.48  ? 465 TYR A CD2 1 
ATOM   3539 C  CE1 . TYR A 1 465 ? 86.954  114.276 135.131 1.00 74.68  ? 465 TYR A CE1 1 
ATOM   3540 C  CE2 . TYR A 1 465 ? 85.134  113.347 133.892 1.00 74.11  ? 465 TYR A CE2 1 
ATOM   3541 C  CZ  . TYR A 1 465 ? 85.681  113.753 135.088 1.00 77.65  ? 465 TYR A CZ  1 
ATOM   3542 O  OH  . TYR A 1 465 ? 84.953  113.635 136.247 1.00 78.13  ? 465 TYR A OH  1 
ATOM   3543 N  N   . TYR A 1 466 ? 86.123  115.571 129.101 1.00 79.75  ? 466 TYR A N   1 
ATOM   3544 C  CA  . TYR A 1 466 ? 84.803  115.827 128.550 1.00 79.85  ? 466 TYR A CA  1 
ATOM   3545 C  C   . TYR A 1 466 ? 84.390  114.692 127.625 1.00 79.30  ? 466 TYR A C   1 
ATOM   3546 O  O   . TYR A 1 466 ? 85.240  114.079 126.973 1.00 79.39  ? 466 TYR A O   1 
ATOM   3547 C  CB  . TYR A 1 466 ? 84.780  117.153 127.773 1.00 80.05  ? 466 TYR A CB  1 
ATOM   3548 C  CG  . TYR A 1 466 ? 85.707  117.196 126.577 1.00 79.22  ? 466 TYR A CG  1 
ATOM   3549 C  CD1 . TYR A 1 466 ? 87.043  117.548 126.722 1.00 79.17  ? 466 TYR A CD1 1 
ATOM   3550 C  CD2 . TYR A 1 466 ? 85.244  116.893 125.305 1.00 79.13  ? 466 TYR A CD2 1 
ATOM   3551 C  CE1 . TYR A 1 466 ? 87.892  117.590 125.631 1.00 80.00  ? 466 TYR A CE1 1 
ATOM   3552 C  CE2 . TYR A 1 466 ? 86.085  116.932 124.210 1.00 79.54  ? 466 TYR A CE2 1 
ATOM   3553 C  CZ  . TYR A 1 466 ? 87.407  117.281 124.379 1.00 80.62  ? 466 TYR A CZ  1 
ATOM   3554 O  OH  . TYR A 1 466 ? 88.248  117.321 123.293 1.00 80.68  ? 466 TYR A OH  1 
ATOM   3555 N  N   . PRO A 1 467 ? 83.096  114.394 127.539 1.00 85.80  ? 467 PRO A N   1 
ATOM   3556 C  CA  . PRO A 1 467 ? 82.629  113.376 126.593 1.00 86.51  ? 467 PRO A CA  1 
ATOM   3557 C  C   . PRO A 1 467 ? 82.480  113.931 125.183 1.00 86.97  ? 467 PRO A C   1 
ATOM   3558 O  O   . PRO A 1 467 ? 82.423  115.142 124.959 1.00 89.37  ? 467 PRO A O   1 
ATOM   3559 C  CB  . PRO A 1 467 ? 81.277  112.985 127.185 1.00 85.91  ? 467 PRO A CB  1 
ATOM   3560 C  CG  . PRO A 1 467 ? 80.754  114.304 127.658 1.00 86.91  ? 467 PRO A CG  1 
ATOM   3561 C  CD  . PRO A 1 467 ? 81.963  115.018 128.254 1.00 85.00  ? 467 PRO A CD  1 
ATOM   3562 N  N   . ASP A 1 468 ? 82.408  113.012 124.228 1.00 86.41  ? 468 ASP A N   1 
ATOM   3563 C  CA  . ASP A 1 468 ? 82.256  113.346 122.818 1.00 86.79  ? 468 ASP A CA  1 
ATOM   3564 C  C   . ASP A 1 468 ? 80.979  112.707 122.269 1.00 89.59  ? 468 ASP A C   1 
ATOM   3565 O  O   . ASP A 1 468 ? 80.143  112.197 123.019 1.00 89.83  ? 468 ASP A O   1 
ATOM   3566 C  CB  . ASP A 1 468 ? 83.498  112.932 122.023 1.00 88.32  ? 468 ASP A CB  1 
ATOM   3567 C  CG  . ASP A 1 468 ? 83.684  111.426 121.952 1.00 91.24  ? 468 ASP A CG  1 
ATOM   3568 O  OD1 . ASP A 1 468 ? 82.951  110.686 122.640 1.00 91.35  ? 468 ASP A OD1 1 
ATOM   3569 O  OD2 . ASP A 1 468 ? 84.579  110.980 121.201 1.00 90.01  ? 468 ASP A OD2 1 
ATOM   3570 N  N   . ASP A 1 469 ? 80.835  112.753 120.942 1.00 98.03  ? 469 ASP A N   1 
ATOM   3571 C  CA  . ASP A 1 469 ? 79.618  112.266 120.298 1.00 98.11  ? 469 ASP A CA  1 
ATOM   3572 C  C   . ASP A 1 469 ? 79.385  110.785 120.576 1.00 96.39  ? 469 ASP A C   1 
ATOM   3573 O  O   . ASP A 1 469 ? 78.251  110.368 120.840 1.00 96.88  ? 469 ASP A O   1 
ATOM   3574 C  CB  . ASP A 1 469 ? 79.691  112.519 118.791 1.00 97.92  ? 469 ASP A CB  1 
ATOM   3575 C  CG  . ASP A 1 469 ? 79.486  113.977 118.437 1.00 99.88  ? 469 ASP A CG  1 
ATOM   3576 O  OD1 . ASP A 1 469 ? 79.442  114.811 119.364 1.00 99.80  ? 469 ASP A OD1 1 
ATOM   3577 O  OD2 . ASP A 1 469 ? 79.370  114.290 117.234 1.00 99.84  ? 469 ASP A OD2 1 
ATOM   3578 N  N   . ASN A 1 470 ? 80.440  109.977 120.524 1.00 92.21  ? 470 ASN A N   1 
ATOM   3579 C  CA  . ASN A 1 470 ? 80.319  108.536 120.703 1.00 92.85  ? 470 ASN A CA  1 
ATOM   3580 C  C   . ASN A 1 470 ? 80.299  108.111 122.166 1.00 91.90  ? 470 ASN A C   1 
ATOM   3581 O  O   . ASN A 1 470 ? 80.161  106.916 122.446 1.00 91.10  ? 470 ASN A O   1 
ATOM   3582 C  CB  . ASN A 1 470 ? 81.462  107.818 119.977 1.00 91.53  ? 470 ASN A CB  1 
ATOM   3583 C  CG  . ASN A 1 470 ? 81.800  108.460 118.646 1.00 93.77  ? 470 ASN A CG  1 
ATOM   3584 O  OD1 . ASN A 1 470 ? 80.912  108.798 117.864 1.00 94.18  ? 470 ASN A OD1 1 
ATOM   3585 N  ND2 . ASN A 1 470 ? 83.090  108.628 118.380 1.00 91.06  ? 470 ASN A ND2 1 
ATOM   3586 N  N   . GLY A 1 471 ? 80.428  109.050 123.102 1.00 86.82  ? 471 GLY A N   1 
ATOM   3587 C  CA  . GLY A 1 471 ? 80.416  108.728 124.512 1.00 86.24  ? 471 GLY A CA  1 
ATOM   3588 C  C   . GLY A 1 471 ? 81.748  108.315 125.097 1.00 88.09  ? 471 GLY A C   1 
ATOM   3589 O  O   . GLY A 1 471 ? 81.797  107.942 126.276 1.00 88.57  ? 471 GLY A O   1 
ATOM   3590 N  N   . ILE A 1 472 ? 82.826  108.369 124.322 1.00 85.43  ? 472 ILE A N   1 
ATOM   3591 C  CA  . ILE A 1 472 ? 84.158  108.033 124.811 1.00 85.34  ? 472 ILE A CA  1 
ATOM   3592 C  C   . ILE A 1 472 ? 84.840  109.309 125.288 1.00 85.34  ? 472 ILE A C   1 
ATOM   3593 O  O   . ILE A 1 472 ? 84.933  110.292 124.544 1.00 86.41  ? 472 ILE A O   1 
ATOM   3594 C  CB  . ILE A 1 472 ? 84.983  107.332 123.720 1.00 83.90  ? 472 ILE A CB  1 
ATOM   3595 C  CG1 . ILE A 1 472 ? 84.741  107.993 122.364 1.00 84.33  ? 472 ILE A CG1 1 
ATOM   3596 C  CG2 . ILE A 1 472 ? 84.629  105.858 123.653 1.00 82.87  ? 472 ILE A CG2 1 
ATOM   3597 C  CD1 . ILE A 1 472 ? 85.674  107.524 121.279 1.00 83.83  ? 472 ILE A CD1 1 
ATOM   3598 N  N   . TYR A 1 473 ? 85.316  109.294 126.529 1.00 78.10  ? 473 TYR A N   1 
ATOM   3599 C  CA  . TYR A 1 473 ? 85.854  110.497 127.145 1.00 77.24  ? 473 TYR A CA  1 
ATOM   3600 C  C   . TYR A 1 473 ? 87.165  110.917 126.486 1.00 78.32  ? 473 TYR A C   1 
ATOM   3601 O  O   . TYR A 1 473 ? 87.911  110.094 125.949 1.00 78.43  ? 473 TYR A O   1 
ATOM   3602 C  CB  . TYR A 1 473 ? 86.074  110.274 128.640 1.00 77.46  ? 473 TYR A CB  1 
ATOM   3603 C  CG  . TYR A 1 473 ? 84.807  110.332 129.462 1.00 79.69  ? 473 TYR A CG  1 
ATOM   3604 C  CD1 . TYR A 1 473 ? 83.816  109.371 129.315 1.00 79.97  ? 473 TYR A CD1 1 
ATOM   3605 C  CD2 . TYR A 1 473 ? 84.600  111.349 130.381 1.00 81.06  ? 473 TYR A CD2 1 
ATOM   3606 C  CE1 . TYR A 1 473 ? 82.658  109.419 130.063 1.00 80.80  ? 473 TYR A CE1 1 
ATOM   3607 C  CE2 . TYR A 1 473 ? 83.444  111.406 131.133 1.00 81.29  ? 473 TYR A CE2 1 
ATOM   3608 C  CZ  . TYR A 1 473 ? 82.476  110.438 130.970 1.00 81.60  ? 473 TYR A CZ  1 
ATOM   3609 O  OH  . TYR A 1 473 ? 81.323  110.491 131.717 1.00 79.64  ? 473 TYR A OH  1 
ATOM   3610 N  N   . ASN A 1 474 ? 87.437  112.217 126.532 1.00 76.04  ? 474 ASN A N   1 
ATOM   3611 C  CA  . ASN A 1 474 ? 88.673  112.799 126.030 1.00 74.12  ? 474 ASN A CA  1 
ATOM   3612 C  C   . ASN A 1 474 ? 89.410  113.489 127.170 1.00 73.96  ? 474 ASN A C   1 
ATOM   3613 O  O   . ASN A 1 474 ? 88.904  113.606 128.289 1.00 73.23  ? 474 ASN A O   1 
ATOM   3614 C  CB  . ASN A 1 474 ? 88.400  113.791 124.892 1.00 73.19  ? 474 ASN A CB  1 
ATOM   3615 C  CG  . ASN A 1 474 ? 87.711  113.146 123.707 1.00 73.91  ? 474 ASN A CG  1 
ATOM   3616 O  OD1 . ASN A 1 474 ? 86.532  113.385 123.453 1.00 77.12  ? 474 ASN A OD1 1 
ATOM   3617 N  ND2 . ASN A 1 474 ? 88.448  112.327 122.971 1.00 73.02  ? 474 ASN A ND2 1 
ATOM   3618 N  N   . GLN A 1 475 ? 90.623  113.951 126.876 1.00 64.02  ? 475 GLN A N   1 
ATOM   3619 C  CA  . GLN A 1 475 ? 91.477  114.593 127.863 1.00 62.20  ? 475 GLN A CA  1 
ATOM   3620 C  C   . GLN A 1 475 ? 91.918  115.965 127.369 1.00 64.95  ? 475 GLN A C   1 
ATOM   3621 O  O   . GLN A 1 475 ? 92.021  116.215 126.166 1.00 67.82  ? 475 GLN A O   1 
ATOM   3622 C  CB  . GLN A 1 475 ? 92.710  113.735 128.180 1.00 58.75  ? 475 GLN A CB  1 
ATOM   3623 C  CG  . GLN A 1 475 ? 92.406  112.269 128.413 1.00 61.67  ? 475 GLN A CG  1 
ATOM   3624 C  CD  . GLN A 1 475 ? 92.641  111.849 129.848 1.00 63.54  ? 475 GLN A CD  1 
ATOM   3625 O  OE1 . GLN A 1 475 ? 92.138  112.476 130.780 1.00 66.00  ? 475 GLN A OE1 1 
ATOM   3626 N  NE2 . GLN A 1 475 ? 93.403  110.779 130.035 1.00 61.43  ? 475 GLN A NE2 1 
ATOM   3627 N  N   . LYS A 1 476 ? 92.176  116.859 128.326 1.00 58.56  ? 476 LYS A N   1 
ATOM   3628 C  CA  . LYS A 1 476 ? 92.667  118.195 128.028 1.00 56.26  ? 476 LYS A CA  1 
ATOM   3629 C  C   . LYS A 1 476 ? 94.015  118.495 128.667 1.00 57.00  ? 476 LYS A C   1 
ATOM   3630 O  O   . LYS A 1 476 ? 94.617  119.526 128.347 1.00 59.58  ? 476 LYS A O   1 
ATOM   3631 C  CB  . LYS A 1 476 ? 91.651  119.255 128.481 1.00 55.96  ? 476 LYS A CB  1 
ATOM   3632 C  CG  . LYS A 1 476 ? 90.755  119.772 127.371 1.00 60.99  ? 476 LYS A CG  1 
ATOM   3633 C  CD  . LYS A 1 476 ? 89.978  120.999 127.817 1.00 61.49  ? 476 LYS A CD  1 
ATOM   3634 C  CE  . LYS A 1 476 ? 90.904  122.062 128.382 1.00 60.90  ? 476 LYS A CE  1 
ATOM   3635 N  NZ  . LYS A 1 476 ? 90.153  123.242 128.888 1.00 61.62  ? 476 LYS A NZ  1 
ATOM   3636 N  N   . PHE A 1 477 ? 94.498  117.644 129.548 1.00 51.83  ? 477 PHE A N   1 
ATOM   3637 C  CA  . PHE A 1 477 ? 95.755  117.733 130.272 1.00 49.92  ? 477 PHE A CA  1 
ATOM   3638 C  C   . PHE A 1 477 ? 96.885  117.117 129.451 1.00 47.99  ? 477 PHE A C   1 
ATOM   3639 O  O   . PHE A 1 477 ? 96.705  116.068 128.825 1.00 55.58  ? 477 PHE A O   1 
ATOM   3640 C  CB  . PHE A 1 477 ? 95.639  117.013 131.614 1.00 53.90  ? 477 PHE A CB  1 
ATOM   3641 C  CG  . PHE A 1 477 ? 96.779  117.278 132.554 1.00 48.06  ? 477 PHE A CG  1 
ATOM   3642 C  CD1 . PHE A 1 477 ? 96.747  118.364 133.410 1.00 46.52  ? 477 PHE A CD1 1 
ATOM   3643 C  CD2 . PHE A 1 477 ? 97.873  116.432 132.596 1.00 48.72  ? 477 PHE A CD2 1 
ATOM   3644 C  CE1 . PHE A 1 477 ? 97.788  118.607 134.281 1.00 53.28  ? 477 PHE A CE1 1 
ATOM   3645 C  CE2 . PHE A 1 477 ? 98.917  116.670 133.465 1.00 48.50  ? 477 PHE A CE2 1 
ATOM   3646 C  CZ  . PHE A 1 477 ? 98.874  117.759 134.308 1.00 52.63  ? 477 PHE A CZ  1 
ATOM   3647 N  N   . PRO A 1 478 ? 98.059  117.749 129.425 1.00 40.60  ? 478 PRO A N   1 
ATOM   3648 C  CA  . PRO A 1 478 ? 99.183  117.183 128.666 1.00 46.32  ? 478 PRO A CA  1 
ATOM   3649 C  C   . PRO A 1 478 ? 99.795  115.977 129.358 1.00 45.27  ? 478 PRO A C   1 
ATOM   3650 O  O   . PRO A 1 478 ? 100.862 116.087 129.968 1.00 51.96  ? 478 PRO A O   1 
ATOM   3651 C  CB  . PRO A 1 478 ? 100.180 118.349 128.595 1.00 43.82  ? 478 PRO A CB  1 
ATOM   3652 C  CG  . PRO A 1 478 ? 99.391  119.569 128.980 1.00 44.49  ? 478 PRO A CG  1 
ATOM   3653 C  CD  . PRO A 1 478 ? 98.382  119.079 129.960 1.00 40.51  ? 478 PRO A CD  1 
ATOM   3654 N  N   . PHE A 1 479 ? 99.135  114.821 129.271 1.00 34.27  ? 479 PHE A N   1 
ATOM   3655 C  CA  . PHE A 1 479 ? 99.600  113.660 130.021 1.00 38.60  ? 479 PHE A CA  1 
ATOM   3656 C  C   . PHE A 1 479 ? 100.708 112.898 129.300 1.00 41.64  ? 479 PHE A C   1 
ATOM   3657 O  O   . PHE A 1 479 ? 101.452 112.150 129.944 1.00 45.66  ? 479 PHE A O   1 
ATOM   3658 C  CB  . PHE A 1 479 ? 98.415  112.742 130.351 1.00 37.72  ? 479 PHE A CB  1 
ATOM   3659 C  CG  . PHE A 1 479 ? 97.901  111.943 129.185 1.00 40.22  ? 479 PHE A CG  1 
ATOM   3660 C  CD1 . PHE A 1 479 ? 97.028  112.508 128.273 1.00 39.26  ? 479 PHE A CD1 1 
ATOM   3661 C  CD2 . PHE A 1 479 ? 98.263  110.616 129.020 1.00 41.60  ? 479 PHE A CD2 1 
ATOM   3662 C  CE1 . PHE A 1 479 ? 96.546  111.774 127.207 1.00 37.82  ? 479 PHE A CE1 1 
ATOM   3663 C  CE2 . PHE A 1 479 ? 97.782  109.879 127.955 1.00 41.22  ? 479 PHE A CE2 1 
ATOM   3664 C  CZ  . PHE A 1 479 ? 96.922  110.459 127.049 1.00 36.85  ? 479 PHE A CZ  1 
ATOM   3665 N  N   . LYS A 1 480 ? 100.858 113.087 127.986 1.00 30.84  ? 480 LYS A N   1 
ATOM   3666 C  CA  . LYS A 1 480 ? 101.911 112.382 127.257 1.00 29.32  ? 480 LYS A CA  1 
ATOM   3667 C  C   . LYS A 1 480 ? 103.293 112.952 127.569 1.00 35.94  ? 480 LYS A C   1 
ATOM   3668 O  O   . LYS A 1 480 ? 104.245 112.196 127.810 1.00 41.12  ? 480 LYS A O   1 
ATOM   3669 C  CB  . LYS A 1 480 ? 101.623 112.433 125.759 1.00 27.30  ? 480 LYS A CB  1 
ATOM   3670 C  CG  . LYS A 1 480 ? 100.438 111.579 125.343 1.00 32.68  ? 480 LYS A CG  1 
ATOM   3671 C  CD  . LYS A 1 480 ? 100.388 111.382 123.842 1.00 33.58  ? 480 LYS A CD  1 
ATOM   3672 C  CE  . LYS A 1 480 ? 99.279  112.202 123.215 1.00 37.21  ? 480 LYS A CE  1 
ATOM   3673 N  NZ  . LYS A 1 480 ? 97.967  111.508 123.295 1.00 37.73  ? 480 LYS A NZ  1 
ATOM   3674 N  N   . THR A 1 481 ? 103.425 114.280 127.570 1.00 31.11  ? 481 THR A N   1 
ATOM   3675 C  CA  . THR A 1 481 ? 104.691 114.898 127.952 1.00 27.90  ? 481 THR A CA  1 
ATOM   3676 C  C   . THR A 1 481 ? 105.037 114.595 129.404 1.00 32.64  ? 481 THR A C   1 
ATOM   3677 O  O   . THR A 1 481 ? 106.207 114.346 129.728 1.00 39.04  ? 481 THR A O   1 
ATOM   3678 C  CB  . THR A 1 481 ? 104.629 116.408 127.715 1.00 27.48  ? 481 THR A CB  1 
ATOM   3679 O  OG1 . THR A 1 481 ? 104.441 116.665 126.318 1.00 28.60  ? 481 THR A OG1 1 
ATOM   3680 C  CG2 . THR A 1 481 ? 105.911 117.081 128.170 1.00 27.93  ? 481 THR A CG2 1 
ATOM   3681 N  N   . LEU A 1 482 ? 104.011 114.580 130.260 1.00 26.65  ? 482 LEU A N   1 
ATOM   3682 C  CA  . LEU A 1 482 ? 104.230 114.206 131.681 1.00 28.13  ? 482 LEU A CA  1 
ATOM   3683 C  C   . LEU A 1 482 ? 104.778 112.778 131.722 1.00 30.02  ? 482 LEU A C   1 
ATOM   3684 O  O   . LEU A 1 482 ? 105.771 112.547 132.442 1.00 33.27  ? 482 LEU A O   1 
ATOM   3685 C  CB  . LEU A 1 482 ? 102.895 114.302 132.423 1.00 31.99  ? 482 LEU A CB  1 
ATOM   3686 C  CG  . LEU A 1 482 ? 102.850 113.604 133.782 1.00 36.95  ? 482 LEU A CG  1 
ATOM   3687 C  CD1 . LEU A 1 482 ? 103.594 114.414 134.832 1.00 34.99  ? 482 LEU A CD1 1 
ATOM   3688 C  CD2 . LEU A 1 482 ? 101.413 113.357 134.215 1.00 34.46  ? 482 LEU A CD2 1 
ATOM   3689 N  N   . ALA A 1 483 ? 104.158 111.862 130.969 1.00 28.34  ? 483 ALA A N   1 
ATOM   3690 C  CA  . ALA A 1 483 ? 104.611 110.474 130.968 1.00 26.56  ? 483 ALA A CA  1 
ATOM   3691 C  C   . ALA A 1 483 ? 106.061 110.362 130.516 1.00 34.37  ? 483 ALA A C   1 
ATOM   3692 O  O   . ALA A 1 483 ? 106.845 109.610 131.109 1.00 40.23  ? 483 ALA A O   1 
ATOM   3693 C  CB  . ALA A 1 483 ? 103.704 109.628 130.077 1.00 16.58  ? 483 ALA A CB  1 
ATOM   3694 N  N   . MET A 1 484 ? 106.437 111.101 129.470 1.00 33.00  ? 484 MET A N   1 
ATOM   3695 C  CA  . MET A 1 484 ? 107.817 111.057 128.987 1.00 22.84  ? 484 MET A CA  1 
ATOM   3696 C  C   . MET A 1 484 ? 108.793 111.562 130.048 1.00 28.56  ? 484 MET A C   1 
ATOM   3697 O  O   . MET A 1 484 ? 109.832 110.935 130.307 1.00 37.91  ? 484 MET A O   1 
ATOM   3698 C  CB  . MET A 1 484 ? 107.939 111.875 127.700 1.00 18.68  ? 484 MET A CB  1 
ATOM   3699 C  CG  . MET A 1 484 ? 109.290 111.786 127.012 1.00 25.40  ? 484 MET A CG  1 
ATOM   3700 S  SD  . MET A 1 484 ? 110.434 113.092 127.500 1.00 48.71  ? 484 MET A SD  1 
ATOM   3701 C  CE  . MET A 1 484 ? 109.651 114.525 126.770 1.00 30.97  ? 484 MET A CE  1 
ATOM   3702 N  N   . VAL A 1 485 ? 108.470 112.695 130.678 1.00 24.96  ? 485 VAL A N   1 
ATOM   3703 C  CA  . VAL A 1 485 ? 109.346 113.253 131.705 1.00 25.92  ? 485 VAL A CA  1 
ATOM   3704 C  C   . VAL A 1 485 ? 109.453 112.305 132.895 1.00 35.25  ? 485 VAL A C   1 
ATOM   3705 O  O   . VAL A 1 485 ? 110.539 112.115 133.461 1.00 43.10  ? 485 VAL A O   1 
ATOM   3706 C  CB  . VAL A 1 485 ? 108.850 114.647 132.128 1.00 33.22  ? 485 VAL A CB  1 
ATOM   3707 C  CG1 . VAL A 1 485 ? 109.684 115.184 133.276 1.00 31.05  ? 485 VAL A CG1 1 
ATOM   3708 C  CG2 . VAL A 1 485 ? 108.899 115.604 130.950 1.00 30.62  ? 485 VAL A CG2 1 
ATOM   3709 N  N   . THR A 1 486 ? 108.331 111.699 133.295 1.00 25.88  ? 486 THR A N   1 
ATOM   3710 C  CA  . THR A 1 486 ? 108.355 110.743 134.395 1.00 24.47  ? 486 THR A CA  1 
ATOM   3711 C  C   . THR A 1 486 ? 109.219 109.536 134.058 1.00 30.50  ? 486 THR A C   1 
ATOM   3712 O  O   . THR A 1 486 ? 109.964 109.043 134.911 1.00 38.88  ? 486 THR A O   1 
ATOM   3713 C  CB  . THR A 1 486 ? 106.932 110.303 134.739 1.00 29.76  ? 486 THR A CB  1 
ATOM   3714 O  OG1 . THR A 1 486 ? 106.153 111.448 135.102 1.00 31.93  ? 486 THR A OG1 1 
ATOM   3715 C  CG2 . THR A 1 486 ? 106.939 109.316 135.895 1.00 31.46  ? 486 THR A CG2 1 
ATOM   3716 N  N   . SER A 1 487 ? 109.133 109.045 132.820 1.00 25.57  ? 487 SER A N   1 
ATOM   3717 C  CA  . SER A 1 487 ? 109.961 107.913 132.416 1.00 26.73  ? 487 SER A CA  1 
ATOM   3718 C  C   . SER A 1 487 ? 111.444 108.257 132.489 1.00 30.84  ? 487 SER A C   1 
ATOM   3719 O  O   . SER A 1 487 ? 112.249 107.468 133.001 1.00 31.04  ? 487 SER A O   1 
ATOM   3720 C  CB  . SER A 1 487 ? 109.576 107.468 131.005 1.00 24.20  ? 487 SER A CB  1 
ATOM   3721 O  OG  . SER A 1 487 ? 110.592 106.680 130.416 1.00 37.37  ? 487 SER A OG  1 
ATOM   3722 N  N   . PHE A 1 488 ? 111.821 109.440 131.996 1.00 33.66  ? 488 PHE A N   1 
ATOM   3723 C  CA  . PHE A 1 488 ? 113.222 109.858 132.053 1.00 26.55  ? 488 PHE A CA  1 
ATOM   3724 C  C   . PHE A 1 488 ? 113.715 109.966 133.495 1.00 31.20  ? 488 PHE A C   1 
ATOM   3725 O  O   . PHE A 1 488 ? 114.797 109.460 133.845 1.00 39.17  ? 488 PHE A O   1 
ATOM   3726 C  CB  . PHE A 1 488 ? 113.383 111.191 131.320 1.00 25.98  ? 488 PHE A CB  1 
ATOM   3727 C  CG  . PHE A 1 488 ? 114.792 111.705 131.282 1.00 34.50  ? 488 PHE A CG  1 
ATOM   3728 C  CD1 . PHE A 1 488 ? 115.810 110.947 130.731 1.00 35.31  ? 488 PHE A CD1 1 
ATOM   3729 C  CD2 . PHE A 1 488 ? 115.096 112.959 131.782 1.00 35.70  ? 488 PHE A CD2 1 
ATOM   3730 C  CE1 . PHE A 1 488 ? 117.104 111.425 130.691 1.00 30.84  ? 488 PHE A CE1 1 
ATOM   3731 C  CE2 . PHE A 1 488 ? 116.388 113.441 131.744 1.00 34.70  ? 488 PHE A CE2 1 
ATOM   3732 C  CZ  . PHE A 1 488 ? 117.392 112.673 131.196 1.00 33.66  ? 488 PHE A CZ  1 
ATOM   3733 N  N   . LEU A 1 489 ? 112.927 110.619 134.353 1.00 33.60  ? 489 LEU A N   1 
ATOM   3734 C  CA  . LEU A 1 489 ? 113.335 110.796 135.743 1.00 36.30  ? 489 LEU A CA  1 
ATOM   3735 C  C   . LEU A 1 489 ? 113.427 109.460 136.470 1.00 37.67  ? 489 LEU A C   1 
ATOM   3736 O  O   . LEU A 1 489 ? 114.341 109.246 137.275 1.00 36.12  ? 489 LEU A O   1 
ATOM   3737 C  CB  . LEU A 1 489 ? 112.366 111.736 136.458 1.00 36.28  ? 489 LEU A CB  1 
ATOM   3738 C  CG  . LEU A 1 489 ? 112.491 113.213 136.082 1.00 35.83  ? 489 LEU A CG  1 
ATOM   3739 C  CD1 . LEU A 1 489 ? 111.485 114.049 136.850 1.00 39.37  ? 489 LEU A CD1 1 
ATOM   3740 C  CD2 . LEU A 1 489 ? 113.904 113.711 136.329 1.00 35.81  ? 489 LEU A CD2 1 
ATOM   3741 N  N   . THR A 1 490 ? 112.484 108.551 136.204 1.00 37.34  ? 490 THR A N   1 
ATOM   3742 C  CA  . THR A 1 490 ? 112.533 107.226 136.810 1.00 35.65  ? 490 THR A CA  1 
ATOM   3743 C  C   . THR A 1 490 ? 113.774 106.466 136.367 1.00 39.56  ? 490 THR A C   1 
ATOM   3744 O  O   . THR A 1 490 ? 114.437 105.818 137.185 1.00 35.66  ? 490 THR A O   1 
ATOM   3745 C  CB  . THR A 1 490 ? 111.271 106.440 136.454 1.00 28.05  ? 490 THR A CB  1 
ATOM   3746 O  OG1 . THR A 1 490 ? 110.117 107.167 136.889 1.00 38.70  ? 490 THR A OG1 1 
ATOM   3747 C  CG2 . THR A 1 490 ? 111.283 105.081 137.121 1.00 33.01  ? 490 THR A CG2 1 
ATOM   3748 N  N   . ASN A 1 491 ? 114.108 106.540 135.075 1.00 38.91  ? 491 ASN A N   1 
ATOM   3749 C  CA  . ASN A 1 491 ? 115.331 105.913 134.585 1.00 33.45  ? 491 ASN A CA  1 
ATOM   3750 C  C   . ASN A 1 491 ? 116.538 106.395 135.376 1.00 38.63  ? 491 ASN A C   1 
ATOM   3751 O  O   . ASN A 1 491 ? 117.291 105.589 135.941 1.00 38.57  ? 491 ASN A O   1 
ATOM   3752 C  CB  . ASN A 1 491 ? 115.507 106.222 133.096 1.00 32.53  ? 491 ASN A CB  1 
ATOM   3753 C  CG  . ASN A 1 491 ? 116.558 105.352 132.430 1.00 36.31  ? 491 ASN A CG  1 
ATOM   3754 O  OD1 . ASN A 1 491 ? 117.650 105.155 132.960 1.00 39.00  ? 491 ASN A OD1 1 
ATOM   3755 N  ND2 . ASN A 1 491 ? 116.234 104.838 131.250 1.00 36.15  ? 491 ASN A ND2 1 
ATOM   3756 N  N   . ILE A 1 492 ? 116.710 107.716 135.465 1.00 46.53  ? 492 ILE A N   1 
ATOM   3757 C  CA  . ILE A 1 492 ? 117.897 108.260 136.126 1.00 42.89  ? 492 ILE A CA  1 
ATOM   3758 C  C   . ILE A 1 492 ? 117.923 107.865 137.601 1.00 46.17  ? 492 ILE A C   1 
ATOM   3759 O  O   . ILE A 1 492 ? 118.947 107.397 138.124 1.00 50.59  ? 492 ILE A O   1 
ATOM   3760 C  CB  . ILE A 1 492 ? 117.959 109.787 135.950 1.00 42.89  ? 492 ILE A CB  1 
ATOM   3761 C  CG1 . ILE A 1 492 ? 118.254 110.144 134.495 1.00 37.80  ? 492 ILE A CG1 1 
ATOM   3762 C  CG2 . ILE A 1 492 ? 119.007 110.388 136.873 1.00 45.42  ? 492 ILE A CG2 1 
ATOM   3763 C  CD1 . ILE A 1 492 ? 118.569 111.601 134.287 1.00 43.60  ? 492 ILE A CD1 1 
ATOM   3764 N  N   . CYS A 1 493 ? 116.792 108.039 138.291 1.00 45.41  ? 493 CYS A N   1 
ATOM   3765 C  CA  . CYS A 1 493 ? 116.756 107.806 139.731 1.00 46.14  ? 493 CYS A CA  1 
ATOM   3766 C  C   . CYS A 1 493 ? 116.999 106.341 140.067 1.00 50.56  ? 493 CYS A C   1 
ATOM   3767 O  O   . CYS A 1 493 ? 117.776 106.028 140.976 1.00 47.22  ? 493 CYS A O   1 
ATOM   3768 C  CB  . CYS A 1 493 ? 115.419 108.275 140.304 1.00 49.04  ? 493 CYS A CB  1 
ATOM   3769 S  SG  . CYS A 1 493 ? 115.461 109.931 141.023 1.00 74.25  ? 493 CYS A SG  1 
ATOM   3770 N  N   . ILE A 1 494 ? 116.349 105.424 139.345 1.00 52.50  ? 494 ILE A N   1 
ATOM   3771 C  CA  . ILE A 1 494 ? 116.520 104.006 139.639 1.00 49.25  ? 494 ILE A CA  1 
ATOM   3772 C  C   . ILE A 1 494 ? 117.930 103.551 139.287 1.00 53.50  ? 494 ILE A C   1 
ATOM   3773 O  O   . ILE A 1 494 ? 118.532 102.751 140.014 1.00 53.00  ? 494 ILE A O   1 
ATOM   3774 C  CB  . ILE A 1 494 ? 115.447 103.173 138.915 1.00 48.02  ? 494 ILE A CB  1 
ATOM   3775 C  CG1 . ILE A 1 494 ? 114.058 103.539 139.434 1.00 50.15  ? 494 ILE A CG1 1 
ATOM   3776 C  CG2 . ILE A 1 494 ? 115.695 101.689 139.116 1.00 48.30  ? 494 ILE A CG2 1 
ATOM   3777 C  CD1 . ILE A 1 494 ? 113.848 103.202 140.891 1.00 50.61  ? 494 ILE A CD1 1 
ATOM   3778 N  N   . SER A 1 495 ? 118.490 104.058 138.181 1.00 51.59  ? 495 SER A N   1 
ATOM   3779 C  CA  . SER A 1 495 ? 119.865 103.711 137.836 1.00 44.80  ? 495 SER A CA  1 
ATOM   3780 C  C   . SER A 1 495 ? 120.824 104.106 138.950 1.00 48.79  ? 495 SER A C   1 
ATOM   3781 O  O   . SER A 1 495 ? 121.641 103.293 139.403 1.00 50.23  ? 495 SER A O   1 
ATOM   3782 C  CB  . SER A 1 495 ? 120.264 104.387 136.525 1.00 41.46  ? 495 SER A CB  1 
ATOM   3783 O  OG  . SER A 1 495 ? 119.510 103.885 135.440 1.00 49.70  ? 495 SER A OG  1 
ATOM   3784 N  N   . TYR A 1 496 ? 120.724 105.350 139.425 1.00 56.22  ? 496 TYR A N   1 
ATOM   3785 C  CA  . TYR A 1 496 ? 121.666 105.798 140.445 1.00 54.12  ? 496 TYR A CA  1 
ATOM   3786 C  C   . TYR A 1 496 ? 121.415 105.123 141.789 1.00 56.82  ? 496 TYR A C   1 
ATOM   3787 O  O   . TYR A 1 496 ? 122.371 104.838 142.522 1.00 58.01  ? 496 TYR A O   1 
ATOM   3788 C  CB  . TYR A 1 496 ? 121.619 107.318 140.574 1.00 54.80  ? 496 TYR A CB  1 
ATOM   3789 C  CG  . TYR A 1 496 ? 122.640 107.997 139.691 1.00 59.68  ? 496 TYR A CG  1 
ATOM   3790 C  CD1 . TYR A 1 496 ? 123.943 108.188 140.126 1.00 60.34  ? 496 TYR A CD1 1 
ATOM   3791 C  CD2 . TYR A 1 496 ? 122.308 108.421 138.412 1.00 57.63  ? 496 TYR A CD2 1 
ATOM   3792 C  CE1 . TYR A 1 496 ? 124.882 108.797 139.318 1.00 57.31  ? 496 TYR A CE1 1 
ATOM   3793 C  CE2 . TYR A 1 496 ? 123.239 109.030 137.598 1.00 56.58  ? 496 TYR A CE2 1 
ATOM   3794 C  CZ  . TYR A 1 496 ? 124.525 109.216 138.056 1.00 58.48  ? 496 TYR A CZ  1 
ATOM   3795 O  OH  . TYR A 1 496 ? 125.457 109.822 137.249 1.00 60.90  ? 496 TYR A OH  1 
ATOM   3796 N  N   . LEU A 1 497 ? 120.153 104.842 142.126 1.00 59.63  ? 497 LEU A N   1 
ATOM   3797 C  CA  . LEU A 1 497 ? 119.865 104.128 143.366 1.00 60.14  ? 497 LEU A CA  1 
ATOM   3798 C  C   . LEU A 1 497 ? 120.448 102.721 143.341 1.00 61.35  ? 497 LEU A C   1 
ATOM   3799 O  O   . LEU A 1 497 ? 121.046 102.273 144.327 1.00 62.26  ? 497 LEU A O   1 
ATOM   3800 C  CB  . LEU A 1 497 ? 118.357 104.079 143.605 1.00 59.55  ? 497 LEU A CB  1 
ATOM   3801 C  CG  . LEU A 1 497 ? 117.877 103.130 144.703 1.00 61.29  ? 497 LEU A CG  1 
ATOM   3802 C  CD1 . LEU A 1 497 ? 118.187 103.700 146.077 1.00 60.84  ? 497 LEU A CD1 1 
ATOM   3803 C  CD2 . LEU A 1 497 ? 116.392 102.850 144.558 1.00 62.83  ? 497 LEU A CD2 1 
ATOM   3804 N  N   . ALA A 1 498 ? 120.287 102.007 142.223 1.00 64.11  ? 498 ALA A N   1 
ATOM   3805 C  CA  . ALA A 1 498 ? 120.867 100.673 142.109 1.00 59.95  ? 498 ALA A CA  1 
ATOM   3806 C  C   . ALA A 1 498 ? 122.387 100.726 142.173 1.00 63.67  ? 498 ALA A C   1 
ATOM   3807 O  O   . ALA A 1 498 ? 123.020 99.879  142.818 1.00 63.59  ? 498 ALA A O   1 
ATOM   3808 C  CB  . ALA A 1 498 ? 120.408 100.010 140.812 1.00 60.97  ? 498 ALA A CB  1 
ATOM   3809 N  N   . LYS A 1 499 ? 122.991 101.716 141.508 1.00 74.21  ? 499 LYS A N   1 
ATOM   3810 C  CA  . LYS A 1 499 ? 124.443 101.850 141.555 1.00 72.20  ? 499 LYS A CA  1 
ATOM   3811 C  C   . LYS A 1 499 ? 124.930 102.082 142.980 1.00 74.09  ? 499 LYS A C   1 
ATOM   3812 O  O   . LYS A 1 499 ? 125.913 101.470 143.412 1.00 73.20  ? 499 LYS A O   1 
ATOM   3813 C  CB  . LYS A 1 499 ? 124.898 102.988 140.642 1.00 70.12  ? 499 LYS A CB  1 
ATOM   3814 C  CG  . LYS A 1 499 ? 126.239 102.740 139.972 1.00 73.92  ? 499 LYS A CG  1 
ATOM   3815 C  CD  . LYS A 1 499 ? 126.514 103.767 138.888 1.00 75.21  ? 499 LYS A CD  1 
ATOM   3816 C  CE  . LYS A 1 499 ? 127.028 105.068 139.481 1.00 77.95  ? 499 LYS A CE  1 
ATOM   3817 N  NZ  . LYS A 1 499 ? 128.355 104.892 140.132 1.00 75.24  ? 499 LYS A NZ  1 
ATOM   3818 N  N   . TYR A 1 500 ? 124.254 102.959 143.728 1.00 81.52  ? 500 TYR A N   1 
ATOM   3819 C  CA  . TYR A 1 500 ? 124.651 103.199 145.112 1.00 81.39  ? 500 TYR A CA  1 
ATOM   3820 C  C   . TYR A 1 500 ? 124.458 101.952 145.967 1.00 81.77  ? 500 TYR A C   1 
ATOM   3821 O  O   . TYR A 1 500 ? 125.307 101.630 146.806 1.00 81.83  ? 500 TYR A O   1 
ATOM   3822 C  CB  . TYR A 1 500 ? 123.873 104.388 145.687 1.00 80.12  ? 500 TYR A CB  1 
ATOM   3823 C  CG  . TYR A 1 500 ? 123.811 104.452 147.205 1.00 81.44  ? 500 TYR A CG  1 
ATOM   3824 C  CD1 . TYR A 1 500 ? 122.909 103.676 147.928 1.00 82.05  ? 500 TYR A CD1 1 
ATOM   3825 C  CD2 . TYR A 1 500 ? 124.671 105.279 147.916 1.00 82.12  ? 500 TYR A CD2 1 
ATOM   3826 C  CE1 . TYR A 1 500 ? 122.862 103.729 149.306 1.00 82.02  ? 500 TYR A CE1 1 
ATOM   3827 C  CE2 . TYR A 1 500 ? 124.629 105.339 149.296 1.00 82.26  ? 500 TYR A CE2 1 
ATOM   3828 C  CZ  . TYR A 1 500 ? 123.722 104.561 149.985 1.00 83.42  ? 500 TYR A CZ  1 
ATOM   3829 O  OH  . TYR A 1 500 ? 123.674 104.616 151.358 1.00 83.92  ? 500 TYR A OH  1 
ATOM   3830 N  N   . LEU A 1 501 ? 123.339 101.247 145.781 1.00 81.19  ? 501 LEU A N   1 
ATOM   3831 C  CA  . LEU A 1 501 ? 123.058 100.078 146.610 1.00 79.93  ? 501 LEU A CA  1 
ATOM   3832 C  C   . LEU A 1 501 ? 124.072 98.968  146.373 1.00 81.08  ? 501 LEU A C   1 
ATOM   3833 O  O   . LEU A 1 501 ? 124.505 98.306  147.323 1.00 80.75  ? 501 LEU A O   1 
ATOM   3834 C  CB  . LEU A 1 501 ? 121.641 99.572  146.346 1.00 80.26  ? 501 LEU A CB  1 
ATOM   3835 C  CG  . LEU A 1 501 ? 120.507 100.294 147.076 1.00 80.73  ? 501 LEU A CG  1 
ATOM   3836 C  CD1 . LEU A 1 501 ? 119.158 99.726  146.665 1.00 80.57  ? 501 LEU A CD1 1 
ATOM   3837 C  CD2 . LEU A 1 501 ? 120.697 100.201 148.581 1.00 80.92  ? 501 LEU A CD2 1 
ATOM   3838 N  N   . PHE A 1 502 ? 124.462 98.744  145.118 1.00 85.28  ? 502 PHE A N   1 
ATOM   3839 C  CA  . PHE A 1 502 ? 125.358 97.632  144.823 1.00 84.51  ? 502 PHE A CA  1 
ATOM   3840 C  C   . PHE A 1 502 ? 126.829 97.987  145.007 1.00 85.63  ? 502 PHE A C   1 
ATOM   3841 O  O   . PHE A 1 502 ? 127.615 97.139  145.442 1.00 85.72  ? 502 PHE A O   1 
ATOM   3842 C  CB  . PHE A 1 502 ? 125.115 97.125  143.400 1.00 81.75  ? 502 PHE A CB  1 
ATOM   3843 C  CG  . PHE A 1 502 ? 124.062 96.062  143.314 1.00 81.41  ? 502 PHE A CG  1 
ATOM   3844 C  CD1 . PHE A 1 502 ? 124.114 94.954  144.140 1.00 81.04  ? 502 PHE A CD1 1 
ATOM   3845 C  CD2 . PHE A 1 502 ? 123.015 96.175  142.417 1.00 82.37  ? 502 PHE A CD2 1 
ATOM   3846 C  CE1 . PHE A 1 502 ? 123.145 93.975  144.070 1.00 82.85  ? 502 PHE A CE1 1 
ATOM   3847 C  CE2 . PHE A 1 502 ? 122.043 95.200  142.342 1.00 84.03  ? 502 PHE A CE2 1 
ATOM   3848 C  CZ  . PHE A 1 502 ? 122.108 94.098  143.170 1.00 84.86  ? 502 PHE A CZ  1 
ATOM   3849 N  N   . GLU A 1 503 ? 127.223 99.221  144.681 1.00 92.04  ? 503 GLU A N   1 
ATOM   3850 C  CA  . GLU A 1 503 ? 128.624 99.606  144.812 1.00 91.78  ? 503 GLU A CA  1 
ATOM   3851 C  C   . GLU A 1 503 ? 129.070 99.589  146.269 1.00 92.55  ? 503 GLU A C   1 
ATOM   3852 O  O   . GLU A 1 503 ? 130.168 99.118  146.585 1.00 95.81  ? 503 GLU A O   1 
ATOM   3853 C  CB  . GLU A 1 503 ? 128.847 100.985 144.194 1.00 91.36  ? 503 GLU A CB  1 
ATOM   3854 C  CG  . GLU A 1 503 ? 130.306 101.393 144.097 1.00 93.89  ? 503 GLU A CG  1 
ATOM   3855 C  CD  . GLU A 1 503 ? 130.532 102.505 143.092 1.00 95.45  ? 503 GLU A CD  1 
ATOM   3856 O  OE1 . GLU A 1 503 ? 129.769 102.581 142.106 1.00 93.67  ? 503 GLU A OE1 1 
ATOM   3857 O  OE2 . GLU A 1 503 ? 131.473 103.302 143.287 1.00 94.33  ? 503 GLU A OE2 1 
ATOM   3858 N  N   . SER A 1 504 ? 128.231 100.098 147.172 1.00 91.74  ? 504 SER A N   1 
ATOM   3859 C  CA  . SER A 1 504 ? 128.549 100.104 148.599 1.00 93.47  ? 504 SER A CA  1 
ATOM   3860 C  C   . SER A 1 504 ? 127.226 100.110 149.360 1.00 95.06  ? 504 SER A C   1 
ATOM   3861 O  O   . SER A 1 504 ? 126.570 101.151 149.461 1.00 95.55  ? 504 SER A O   1 
ATOM   3862 C  CB  . SER A 1 504 ? 129.413 101.302 148.968 1.00 94.51  ? 504 SER A CB  1 
ATOM   3863 O  OG  . SER A 1 504 ? 128.958 102.479 148.325 1.00 96.71  ? 504 SER A OG  1 
ATOM   3864 N  N   . GLY A 1 505 ? 126.847 98.952  149.888 1.00 102.60 ? 505 GLY A N   1 
ATOM   3865 C  CA  . GLY A 1 505 ? 125.599 98.845  150.619 1.00 103.01 ? 505 GLY A CA  1 
ATOM   3866 C  C   . GLY A 1 505 ? 125.442 97.459  151.202 1.00 103.04 ? 505 GLY A C   1 
ATOM   3867 O  O   . GLY A 1 505 ? 126.325 96.606  151.087 1.00 102.86 ? 505 GLY A O   1 
ATOM   3868 N  N   . THR A 1 506 ? 124.290 97.247  151.837 1.00 104.59 ? 506 THR A N   1 
ATOM   3869 C  CA  . THR A 1 506 ? 123.989 95.967  152.463 1.00 106.34 ? 506 THR A CA  1 
ATOM   3870 C  C   . THR A 1 506 ? 123.590 94.892  151.462 1.00 105.58 ? 506 THR A C   1 
ATOM   3871 O  O   . THR A 1 506 ? 123.503 93.719  151.844 1.00 105.76 ? 506 THR A O   1 
ATOM   3872 C  CB  . THR A 1 506 ? 122.870 96.132  153.495 1.00 107.55 ? 506 THR A CB  1 
ATOM   3873 O  OG1 . THR A 1 506 ? 121.913 97.086  153.018 1.00 106.52 ? 506 THR A OG1 1 
ATOM   3874 C  CG2 . THR A 1 506 ? 123.437 96.607  154.826 1.00 105.01 ? 506 THR A CG2 1 
ATOM   3875 N  N   . LEU A 1 507 ? 123.344 95.252  150.210 1.00 100.37 ? 507 LEU A N   1 
ATOM   3876 C  CA  . LEU A 1 507 ? 122.924 94.271  149.217 1.00 100.08 ? 507 LEU A CA  1 
ATOM   3877 C  C   . LEU A 1 507 ? 124.098 93.378  148.838 1.00 100.69 ? 507 LEU A C   1 
ATOM   3878 O  O   . LEU A 1 507 ? 125.134 93.890  148.394 1.00 100.07 ? 507 LEU A O   1 
ATOM   3879 C  CB  . LEU A 1 507 ? 122.367 94.971  147.982 1.00 99.53  ? 507 LEU A CB  1 
ATOM   3880 C  CG  . LEU A 1 507 ? 120.843 95.078  147.899 1.00 100.18 ? 507 LEU A CG  1 
ATOM   3881 C  CD1 . LEU A 1 507 ? 120.403 95.487  146.503 1.00 99.96  ? 507 LEU A CD1 1 
ATOM   3882 C  CD2 . LEU A 1 507 ? 120.191 93.768  148.306 1.00 99.24  ? 507 LEU A CD2 1 
ATOM   3883 N  N   . PRO A 1 508 ? 123.991 92.058  148.999 1.00 103.17 ? 508 PRO A N   1 
ATOM   3884 C  CA  . PRO A 1 508 ? 125.099 91.188  148.614 1.00 101.90 ? 508 PRO A CA  1 
ATOM   3885 C  C   . PRO A 1 508 ? 125.271 91.168  147.107 1.00 101.37 ? 508 PRO A C   1 
ATOM   3886 O  O   . PRO A 1 508 ? 124.306 91.386  146.355 1.00 101.49 ? 508 PRO A O   1 
ATOM   3887 C  CB  . PRO A 1 508 ? 124.671 89.810  149.150 1.00 101.00 ? 508 PRO A CB  1 
ATOM   3888 C  CG  . PRO A 1 508 ? 123.187 89.881  149.227 1.00 101.25 ? 508 PRO A CG  1 
ATOM   3889 C  CD  . PRO A 1 508 ? 122.854 91.306  149.557 1.00 101.26 ? 508 PRO A CD  1 
ATOM   3890 N  N   . PRO A 1 509 ? 126.488 90.922  146.617 1.00 96.58  ? 509 PRO A N   1 
ATOM   3891 C  CA  . PRO A 1 509 ? 126.695 90.863  145.161 1.00 97.38  ? 509 PRO A CA  1 
ATOM   3892 C  C   . PRO A 1 509 ? 125.932 89.742  144.477 1.00 96.29  ? 509 PRO A C   1 
ATOM   3893 O  O   . PRO A 1 509 ? 125.703 89.824  143.263 1.00 95.85  ? 509 PRO A O   1 
ATOM   3894 C  CB  . PRO A 1 509 ? 128.212 90.665  145.029 1.00 96.72  ? 509 PRO A CB  1 
ATOM   3895 C  CG  . PRO A 1 509 ? 128.778 91.143  146.331 1.00 96.82  ? 509 PRO A CG  1 
ATOM   3896 C  CD  . PRO A 1 509 ? 127.751 90.796  147.362 1.00 96.09  ? 509 PRO A CD  1 
ATOM   3897 N  N   . LYS A 1 510 ? 125.533 88.699  145.208 1.00 94.60  ? 510 LYS A N   1 
ATOM   3898 C  CA  . LYS A 1 510 ? 124.833 87.577  144.593 1.00 94.65  ? 510 LYS A CA  1 
ATOM   3899 C  C   . LYS A 1 510 ? 123.449 87.958  144.085 1.00 96.42  ? 510 LYS A C   1 
ATOM   3900 O  O   . LYS A 1 510 ? 122.901 87.251  143.232 1.00 97.50  ? 510 LYS A O   1 
ATOM   3901 C  CB  . LYS A 1 510 ? 124.715 86.420  145.585 1.00 95.93  ? 510 LYS A CB  1 
ATOM   3902 C  CG  . LYS A 1 510 ? 123.868 86.733  146.806 1.00 98.69  ? 510 LYS A CG  1 
ATOM   3903 C  CD  . LYS A 1 510 ? 123.309 85.466  147.430 1.00 98.04  ? 510 LYS A CD  1 
ATOM   3904 C  CE  . LYS A 1 510 ? 122.220 84.858  146.562 1.00 96.75  ? 510 LYS A CE  1 
ATOM   3905 N  NZ  . LYS A 1 510 ? 120.875 85.407  146.891 1.00 96.61  ? 510 LYS A NZ  1 
ATOM   3906 N  N   . LEU A 1 511 ? 122.873 89.051  144.581 1.00 92.77  ? 511 LEU A N   1 
ATOM   3907 C  CA  . LEU A 1 511 ? 121.544 89.474  144.160 1.00 93.45  ? 511 LEU A CA  1 
ATOM   3908 C  C   . LEU A 1 511 ? 121.559 90.274  142.865 1.00 93.52  ? 511 LEU A C   1 
ATOM   3909 O  O   . LEU A 1 511 ? 120.494 90.704  142.409 1.00 91.35  ? 511 LEU A O   1 
ATOM   3910 C  CB  . LEU A 1 511 ? 120.876 90.292  145.268 1.00 92.13  ? 511 LEU A CB  1 
ATOM   3911 C  CG  . LEU A 1 511 ? 120.114 89.478  146.316 1.00 92.38  ? 511 LEU A CG  1 
ATOM   3912 C  CD1 . LEU A 1 511 ? 119.272 90.383  147.198 1.00 93.76  ? 511 LEU A CD1 1 
ATOM   3913 C  CD2 . LEU A 1 511 ? 119.246 88.423  145.647 1.00 91.15  ? 511 LEU A CD2 1 
ATOM   3914 N  N   . ASP A 1 512 ? 122.729 90.483  142.266 1.00 86.11  ? 512 ASP A N   1 
ATOM   3915 C  CA  . ASP A 1 512 ? 122.820 91.163  140.982 1.00 83.30  ? 512 ASP A CA  1 
ATOM   3916 C  C   . ASP A 1 512 ? 122.345 90.244  139.866 1.00 84.01  ? 512 ASP A C   1 
ATOM   3917 O  O   . ASP A 1 512 ? 123.154 89.551  139.241 1.00 86.10  ? 512 ASP A O   1 
ATOM   3918 C  CB  . ASP A 1 512 ? 124.256 91.623  140.719 1.00 82.61  ? 512 ASP A CB  1 
ATOM   3919 C  CG  . ASP A 1 512 ? 124.322 92.987  140.065 1.00 84.52  ? 512 ASP A CG  1 
ATOM   3920 O  OD1 . ASP A 1 512 ? 123.258 93.614  139.889 1.00 84.96  ? 512 ASP A OD1 1 
ATOM   3921 O  OD2 . ASP A 1 512 ? 125.438 93.432  139.725 1.00 83.57  ? 512 ASP A OD2 1 
ATOM   3922 N  N   . VAL A 1 513 ? 121.033 90.223  139.617 1.00 78.82  ? 513 VAL A N   1 
ATOM   3923 C  CA  . VAL A 1 513 ? 120.490 89.365  138.567 1.00 78.92  ? 513 VAL A CA  1 
ATOM   3924 C  C   . VAL A 1 513 ? 121.041 89.774  137.207 1.00 78.56  ? 513 VAL A C   1 
ATOM   3925 O  O   . VAL A 1 513 ? 121.415 88.923  136.391 1.00 80.20  ? 513 VAL A O   1 
ATOM   3926 C  CB  . VAL A 1 513 ? 118.950 89.389  138.595 1.00 82.06  ? 513 VAL A CB  1 
ATOM   3927 C  CG1 . VAL A 1 513 ? 118.436 88.569  139.766 1.00 82.80  ? 513 VAL A CG1 1 
ATOM   3928 C  CG2 . VAL A 1 513 ? 118.434 90.817  138.685 1.00 80.03  ? 513 VAL A CG2 1 
ATOM   3929 N  N   . PHE A 1 514 ? 121.103 91.074  136.941 1.00 76.57  ? 514 PHE A N   1 
ATOM   3930 C  CA  . PHE A 1 514 ? 121.767 91.601  135.758 1.00 75.44  ? 514 PHE A CA  1 
ATOM   3931 C  C   . PHE A 1 514 ? 123.137 92.123  136.165 1.00 77.78  ? 514 PHE A C   1 
ATOM   3932 O  O   . PHE A 1 514 ? 123.248 92.912  137.109 1.00 80.23  ? 514 PHE A O   1 
ATOM   3933 C  CB  . PHE A 1 514 ? 120.953 92.721  135.109 1.00 74.37  ? 514 PHE A CB  1 
ATOM   3934 C  CG  . PHE A 1 514 ? 119.466 92.583  135.279 1.00 74.91  ? 514 PHE A CG  1 
ATOM   3935 C  CD1 . PHE A 1 514 ? 118.798 91.466  134.808 1.00 75.28  ? 514 PHE A CD1 1 
ATOM   3936 C  CD2 . PHE A 1 514 ? 118.734 93.583  135.896 1.00 73.91  ? 514 PHE A CD2 1 
ATOM   3937 C  CE1 . PHE A 1 514 ? 117.429 91.347  134.960 1.00 77.33  ? 514 PHE A CE1 1 
ATOM   3938 C  CE2 . PHE A 1 514 ? 117.367 93.469  136.048 1.00 73.37  ? 514 PHE A CE2 1 
ATOM   3939 C  CZ  . PHE A 1 514 ? 116.714 92.349  135.581 1.00 75.08  ? 514 PHE A CZ  1 
ATOM   3940 N  N   . ASP A 1 515 ? 124.174 91.684  135.459 1.00 79.93  ? 515 ASP A N   1 
ATOM   3941 C  CA  . ASP A 1 515 ? 125.541 92.085  135.786 1.00 82.04  ? 515 ASP A CA  1 
ATOM   3942 C  C   . ASP A 1 515 ? 125.770 93.490  135.245 1.00 84.19  ? 515 ASP A C   1 
ATOM   3943 O  O   . ASP A 1 515 ? 126.208 93.682  134.110 1.00 86.29  ? 515 ASP A O   1 
ATOM   3944 C  CB  . ASP A 1 515 ? 126.546 91.092  135.220 1.00 82.91  ? 515 ASP A CB  1 
ATOM   3945 C  CG  . ASP A 1 515 ? 127.679 90.800  136.182 1.00 84.19  ? 515 ASP A CG  1 
ATOM   3946 O  OD1 . ASP A 1 515 ? 128.337 91.759  136.636 1.00 82.15  ? 515 ASP A OD1 1 
ATOM   3947 O  OD2 . ASP A 1 515 ? 127.909 89.612  136.488 1.00 86.65  ? 515 ASP A OD2 1 
ATOM   3948 N  N   . ALA A 1 516 ? 125.466 94.488  136.073 1.00 79.79  ? 516 ALA A N   1 
ATOM   3949 C  CA  . ALA A 1 516 ? 125.618 95.885  135.688 1.00 77.91  ? 516 ALA A CA  1 
ATOM   3950 C  C   . ALA A 1 516 ? 126.503 96.699  136.619 1.00 79.67  ? 516 ALA A C   1 
ATOM   3951 O  O   . ALA A 1 516 ? 127.007 97.744  136.192 1.00 79.63  ? 516 ALA A O   1 
ATOM   3952 C  CB  . ALA A 1 516 ? 124.247 96.570  135.594 1.00 76.51  ? 516 ALA A CB  1 
ATOM   3953 N  N   . VAL A 1 517 ? 126.710 96.270  137.859 1.00 83.64  ? 517 VAL A N   1 
ATOM   3954 C  CA  . VAL A 1 517 ? 127.543 97.012  138.796 1.00 83.70  ? 517 VAL A CA  1 
ATOM   3955 C  C   . VAL A 1 517 ? 128.750 96.177  139.206 1.00 81.48  ? 517 VAL A C   1 
ATOM   3956 O  O   . VAL A 1 517 ? 128.621 95.204  139.949 1.00 80.40  ? 517 VAL A O   1 
ATOM   3957 C  CB  . VAL A 1 517 ? 126.739 97.448  140.034 1.00 83.22  ? 517 VAL A CB  1 
ATOM   3958 C  CG1 . VAL A 1 517 ? 127.435 98.603  140.736 1.00 81.71  ? 517 VAL A CG1 1 
ATOM   3959 C  CG2 . VAL A 1 517 ? 125.319 97.830  139.642 1.00 79.55  ? 517 VAL A CG2 1 
HETATM 3960 C  C1  . NAG B 2 .   ? 73.498  126.691 93.544  1.00 96.09  ? 1   NAG B C1  1 
HETATM 3961 C  C2  . NAG B 2 .   ? 72.535  127.796 93.971  1.00 99.44  ? 1   NAG B C2  1 
HETATM 3962 C  C3  . NAG B 2 .   ? 71.239  127.709 93.168  1.00 99.34  ? 1   NAG B C3  1 
HETATM 3963 C  C4  . NAG B 2 .   ? 71.533  127.683 91.674  1.00 99.80  ? 1   NAG B C4  1 
HETATM 3964 C  C5  . NAG B 2 .   ? 72.539  126.581 91.358  1.00 100.81 ? 1   NAG B C5  1 
HETATM 3965 C  C6  . NAG B 2 .   ? 72.975  126.569 89.911  1.00 101.11 ? 1   NAG B C6  1 
HETATM 3966 C  C7  . NAG B 2 .   ? 72.322  128.775 96.213  1.00 99.73  ? 1   NAG B C7  1 
HETATM 3967 C  C8  . NAG B 2 .   ? 72.008  128.511 97.654  1.00 98.42  ? 1   NAG B C8  1 
HETATM 3968 N  N2  . NAG B 2 .   ? 72.259  127.718 95.397  1.00 98.91  ? 1   NAG B N2  1 
HETATM 3969 O  O3  . NAG B 2 .   ? 70.414  128.825 93.486  1.00 99.03  ? 1   NAG B O3  1 
HETATM 3970 O  O4  . NAG B 2 .   ? 70.339  127.431 90.943  1.00 103.51 ? 1   NAG B O4  1 
HETATM 3971 O  O5  . NAG B 2 .   ? 73.724  126.768 92.143  1.00 98.35  ? 1   NAG B O5  1 
HETATM 3972 O  O6  . NAG B 2 .   ? 73.343  125.262 89.491  1.00 99.25  ? 1   NAG B O6  1 
HETATM 3973 O  O7  . NAG B 2 .   ? 72.617  129.894 95.806  1.00 101.24 ? 1   NAG B O7  1 
HETATM 3974 C  C1  . NAG B 2 .   ? 69.865  128.649 90.341  1.00 127.17 ? 2   NAG B C1  1 
HETATM 3975 C  C2  . NAG B 2 .   ? 69.500  128.376 88.880  1.00 127.61 ? 2   NAG B C2  1 
HETATM 3976 C  C3  . NAG B 2 .   ? 68.906  129.627 88.238  1.00 127.26 ? 2   NAG B C3  1 
HETATM 3977 C  C4  . NAG B 2 .   ? 67.736  130.140 89.066  1.00 128.37 ? 2   NAG B C4  1 
HETATM 3978 C  C5  . NAG B 2 .   ? 68.184  130.368 90.506  1.00 127.15 ? 2   NAG B C5  1 
HETATM 3979 C  C6  . NAG B 2 .   ? 67.056  130.788 91.420  1.00 126.39 ? 2   NAG B C6  1 
HETATM 3980 C  C7  . NAG B 2 .   ? 70.568  127.094 87.079  1.00 128.03 ? 2   NAG B C7  1 
HETATM 3981 C  C8  . NAG B 2 .   ? 71.864  126.728 86.419  1.00 126.45 ? 2   NAG B C8  1 
HETATM 3982 N  N2  . NAG B 2 .   ? 70.657  127.919 88.127  1.00 127.95 ? 2   NAG B N2  1 
HETATM 3983 O  O3  . NAG B 2 .   ? 68.473  129.322 86.918  1.00 127.18 ? 2   NAG B O3  1 
HETATM 3984 O  O4  . NAG B 2 .   ? 67.234  131.352 88.513  1.00 128.51 ? 2   NAG B O4  1 
HETATM 3985 O  O5  . NAG B 2 .   ? 68.717  129.148 91.042  1.00 127.52 ? 2   NAG B O5  1 
HETATM 3986 O  O6  . NAG B 2 .   ? 66.261  129.676 91.807  1.00 127.18 ? 2   NAG B O6  1 
HETATM 3987 O  O7  . NAG B 2 .   ? 69.491  126.664 86.680  1.00 127.48 ? 2   NAG B O7  1 
HETATM 3988 C  C1  . BMA B 2 .   ? 65.900  131.128 87.997  1.00 137.83 ? 3   BMA B C1  1 
HETATM 3989 C  C2  . BMA B 2 .   ? 65.918  131.385 86.463  1.00 138.44 ? 3   BMA B C2  1 
HETATM 3990 C  C3  . BMA B 2 .   ? 64.577  130.981 85.838  1.00 138.43 ? 3   BMA B C3  1 
HETATM 3991 C  C4  . BMA B 2 .   ? 64.132  129.585 86.301  1.00 138.58 ? 3   BMA B C4  1 
HETATM 3992 C  C5  . BMA B 2 .   ? 64.118  129.529 87.834  1.00 138.51 ? 3   BMA B C5  1 
HETATM 3993 C  C6  . BMA B 2 .   ? 63.705  128.172 88.375  1.00 138.25 ? 3   BMA B C6  1 
HETATM 3994 O  O2  . BMA B 2 .   ? 66.917  130.604 85.828  1.00 138.89 ? 3   BMA B O2  1 
HETATM 3995 O  O3  . BMA B 2 .   ? 64.628  131.026 84.417  1.00 137.77 ? 3   BMA B O3  1 
HETATM 3996 O  O4  . BMA B 2 .   ? 62.834  129.298 85.804  1.00 138.41 ? 3   BMA B O4  1 
HETATM 3997 O  O5  . BMA B 2 .   ? 65.446  129.806 88.295  1.00 138.31 ? 3   BMA B O5  1 
HETATM 3998 O  O6  . BMA B 2 .   ? 63.663  128.253 89.793  1.00 137.74 ? 3   BMA B O6  1 
HETATM 3999 NA NA  . NA  C 3 .   ? 108.165 110.451 100.931 1.00 30.00  ? 601 NA  A NA  1 
HETATM 4000 NA NA  . NA  D 3 .   ? 113.126 106.500 100.897 1.00 30.00  ? 602 NA  A NA  1 
HETATM 4001 C  CAC . HC6 E 4 .   ? 106.406 111.491 112.478 1.00 33.07  ? 603 HC6 A CAC 1 
HETATM 4002 N  NAA . HC6 E 4 .   ? 107.619 110.898 111.712 1.00 39.76  ? 603 HC6 A NAA 1 
HETATM 4003 C  CBA . HC6 E 4 .   ? 108.090 111.882 110.694 1.00 35.39  ? 603 HC6 A CBA 1 
HETATM 4004 C  CBB . HC6 E 4 .   ? 108.702 110.668 112.695 1.00 38.52  ? 603 HC6 A CBB 1 
HETATM 4005 C  CAB . HC6 E 4 .   ? 107.378 109.576 110.958 1.00 23.33  ? 603 HC6 A CAB 1 
HETATM 4006 C  CAF . HC6 E 4 .   ? 106.181 108.748 111.517 1.00 36.74  ? 603 HC6 A CAF 1 
HETATM 4007 O  OAE . HC6 E 4 .   ? 105.439 109.410 112.549 1.00 50.67  ? 603 HC6 A OAE 1 
HETATM 4008 C  CAD . HC6 E 4 .   ? 105.130 110.690 112.196 1.00 33.08  ? 603 HC6 A CAD 1 
HETATM 4009 O  OBC . HC6 E 4 .   ? 104.881 110.700 110.833 1.00 35.80  ? 603 HC6 A OBC 1 
HETATM 4010 C  CAG . HC6 E 4 .   ? 103.883 111.291 112.854 1.00 23.12  ? 603 HC6 A CAG 1 
HETATM 4011 C  CAL . HC6 E 4 .   ? 103.616 111.465 114.195 1.00 33.00  ? 603 HC6 A CAL 1 
HETATM 4012 C  CAK . HC6 E 4 .   ? 102.393 112.042 114.590 1.00 34.47  ? 603 HC6 A CAK 1 
HETATM 4013 C  CAH . HC6 E 4 .   ? 102.938 111.681 111.956 1.00 30.12  ? 603 HC6 A CAH 1 
HETATM 4014 C  CAI . HC6 E 4 .   ? 101.758 112.233 112.310 1.00 29.73  ? 603 HC6 A CAI 1 
HETATM 4015 C  CAJ . HC6 E 4 .   ? 101.462 112.453 113.629 1.00 35.30  ? 603 HC6 A CAJ 1 
HETATM 4016 C  CAM . HC6 E 4 .   ? 100.181 112.993 113.829 1.00 35.73  ? 603 HC6 A CAM 1 
HETATM 4017 C  CAR . HC6 E 4 .   ? 99.429  112.656 114.938 1.00 37.16  ? 603 HC6 A CAR 1 
HETATM 4018 C  CAQ . HC6 E 4 .   ? 98.142  113.129 115.074 1.00 34.76  ? 603 HC6 A CAQ 1 
HETATM 4019 C  CAN . HC6 E 4 .   ? 99.575  113.775 112.851 1.00 38.49  ? 603 HC6 A CAN 1 
HETATM 4020 C  CAO . HC6 E 4 .   ? 98.286  114.252 113.004 1.00 31.85  ? 603 HC6 A CAO 1 
HETATM 4021 C  CAP . HC6 E 4 .   ? 97.557  113.937 114.111 1.00 32.11  ? 603 HC6 A CAP 1 
HETATM 4022 C  CAS . HC6 E 4 .   ? 96.138  114.417 114.329 1.00 40.19  ? 603 HC6 A CAS 1 
HETATM 4023 O  OBD . HC6 E 4 .   ? 96.063  115.602 115.064 1.00 46.54  ? 603 HC6 A OBD 1 
HETATM 4024 C  CAX . HC6 E 4 .   ? 95.313  114.538 113.029 1.00 34.68  ? 603 HC6 A CAX 1 
HETATM 4025 O  OAT . HC6 E 4 .   ? 95.507  113.439 115.078 1.00 41.86  ? 603 HC6 A OAT 1 
HETATM 4026 C  CAU . HC6 E 4 .   ? 94.190  113.719 115.462 1.00 40.43  ? 603 HC6 A CAU 1 
HETATM 4027 C  CAV . HC6 E 4 .   ? 93.259  113.774 114.284 1.00 38.43  ? 603 HC6 A CAV 1 
HETATM 4028 N  NAW . HC6 E 4 .   ? 93.801  114.688 113.245 1.00 44.70  ? 603 HC6 A NAW 1 
HETATM 4029 C  CAZ . HC6 E 4 .   ? 93.481  116.125 113.522 1.00 36.02  ? 603 HC6 A CAZ 1 
HETATM 4030 C  CAY . HC6 E 4 .   ? 93.017  114.296 112.016 1.00 35.41  ? 603 HC6 A CAY 1 
HETATM 4031 CL CL  . CL  F 5 .   ? 103.700 110.529 106.157 1.00 39.97  ? 604 CL  A CL  1 
HETATM 4032 O  O   . HOH G 6 .   ? 106.261 112.037 107.247 1.00 30.00  ? 701 HOH A O   1 
# 
