data_9BXT
# 
_entry.id   9BXT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BXT         pdb_00009bxt 10.2210/pdb9bxt/pdb 
WWPDB D_1000284351 ?            ?                   
EMDB  EMD-45011    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'EM metadata'     1 0 2025-03-19 ? 
3 'Half map'        1 0 2025-03-19 1 
4 'Half map'        1 0 2025-03-19 2 
5 Image             1 0 2025-03-19 ? 
6 'Primary map'     1 0 2025-03-19 ? 
7 'Structure model' 1 1 2025-03-26 ? 
8 'EM metadata'     1 1 2025-03-26 ? 
# 
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' ? ? 
# 
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 7 'Structure model' 'Structure summary'    
4 8 'EM metadata'     'Database references'  
5 8 'EM metadata'     'Experimental summary' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 7 'Structure model' citation 
2 7 'Structure model' em_admin 
3 7 'Structure model' struct   
4 8 'EM metadata'     citation 
5 8 '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.page_last'               
2  7 'Structure model' '_citation.pdbx_database_id_PubMed' 
3  7 'Structure model' '_citation.title'                   
4  7 'Structure model' '_em_admin.last_update'             
5  7 'Structure model' '_em_admin.title'                   
6  7 'Structure model' '_struct.title'                     
7  8 'EM metadata'     '_citation.page_last'               
8  8 'EM metadata'     '_citation.pdbx_database_id_PubMed' 
9  8 'EM metadata'     '_citation.title'                   
10 8 'EM metadata'     '_em_admin.last_update'             
11 8 'EM metadata'     '_em_admin.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXT 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                                              EMD-45004 
'consensus EM volume'  
EMDB 'TrxA focus-classified model for re-reduction condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45011 
'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     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 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 polymer     man Thioredoxin                                          11404.136 1 ?        ? ? ? 
4 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                      24.305    2 ?        ? ? ? 
6 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
7 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                           443.201   2 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Ribonucleotide reductase large subunit' 
2 'Ribonucleotide reductase small subunit' 
3 Trx                                      
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
A,B ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
C,D ? 
3 'polypeptide(L)' no no 
;MAIVKATDQSFSAETSEGVVLADFWAPWCGPCKMIAPVLEELDQEMGDKLKIVKIDVDENQETAGKYGVMSIPTLLVLKD
GEVVETSVGFKPKEALQELVNKHL
;
;MAIVKATDQSFSAETSEGVVLADFWAPWCGPCKMIAPVLEELDQEMGDKLKIVKIDVDENQETAGKYGVMSIPTLLVLKD
GEVVETSVGFKPKEALQELVNKHL
;
E   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "THYMIDINE-5'-TRIPHOSPHATE" TTP 
5 'MAGNESIUM ION'             MG  
6 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
7 "GUANOSINE-5'-DIPHOSPHATE"  GDP 
# 
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   SER n 
1 3   GLN n 
1 4   ASN n 
1 5   GLN n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   TRP n 
1 10  ILE n 
1 11  GLN n 
1 12  LEU n 
1 13  ASN n 
1 14  ASN n 
1 15  GLU n 
1 16  ILE n 
1 17  MET n 
1 18  ILE n 
1 19  GLN n 
1 20  LYS n 
1 21  ASP n 
1 22  GLY n 
1 23  LYS n 
1 24  PHE n 
1 25  GLN n 
1 26  PHE n 
1 27  ASP n 
1 28  LYS n 
1 29  ASP n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  VAL n 
1 34  HIS n 
1 35  SER n 
1 36  TYR n 
1 37  PHE n 
1 38  VAL n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ASN n 
1 43  GLN n 
1 44  ASN n 
1 45  THR n 
1 46  VAL n 
1 47  PHE n 
1 48  PHE n 
1 49  HIS n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  GLU n 
1 54  LYS n 
1 55  LEU n 
1 56  ASP n 
1 57  TYR n 
1 58  LEU n 
1 59  VAL n 
1 60  GLU n 
1 61  ASN n 
1 62  GLN n 
1 63  TYR n 
1 64  TYR n 
1 65  GLU n 
1 66  GLU n 
1 67  GLU n 
1 68  PHE n 
1 69  LEU n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  SER n 
1 74  PHE n 
1 75  GLU n 
1 76  ASP n 
1 77  ILE n 
1 78  LYS n 
1 79  GLU n 
1 80  VAL n 
1 81  PHE n 
1 82  LYS n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ALA n 
1 87  LYS n 
1 88  LYS n 
1 89  PHE n 
1 90  ARG n 
1 91  PHE n 
1 92  PRO n 
1 93  SER n 
1 94  PHE n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  PHE n 
1 99  LYS n 
1 100 PHE n 
1 101 TYR n 
1 102 ASN n 
1 103 ASP n 
1 104 TYR n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 THR n 
1 109 ASN n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ARG n 
1 118 TYR n 
1 119 GLU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 SER n 
1 124 ILE n 
1 125 VAL n 
1 126 ALA n 
1 127 LEU n 
1 128 PHE n 
1 129 PHE n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ASP n 
1 134 THR n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 LYS n 
1 139 GLU n 
1 140 TYR n 
1 141 VAL n 
1 142 ASN n 
1 143 LEU n 
1 144 MET n 
1 145 ILE n 
1 146 ASN n 
1 147 GLN n 
1 148 GLU n 
1 149 TYR n 
1 150 GLN n 
1 151 PRO n 
1 152 SER n 
1 153 THR n 
1 154 PRO n 
1 155 THR n 
1 156 PHE n 
1 157 LEU n 
1 158 ASN n 
1 159 ALA n 
1 160 GLY n 
1 161 ARG n 
1 162 LYS n 
1 163 ARG n 
1 164 ARG n 
1 165 GLY n 
1 166 GLU n 
1 167 LEU n 
1 168 VAL n 
1 169 SER n 
1 170 CYS n 
1 171 PHE n 
1 172 LEU n 
1 173 LEU n 
1 174 GLU n 
1 175 VAL n 
1 176 ASN n 
1 177 ASP n 
1 178 SER n 
1 179 LEU n 
1 180 ASN n 
1 181 ASP n 
1 182 ILE n 
1 183 SER n 
1 184 ARG n 
1 185 ALA n 
1 186 ILE n 
1 187 ASP n 
1 188 ILE n 
1 189 SER n 
1 190 MET n 
1 191 GLN n 
1 192 LEU n 
1 193 SER n 
1 194 LYS n 
1 195 LEU n 
1 196 GLY n 
1 197 GLY n 
1 198 GLY n 
1 199 VAL n 
1 200 SER n 
1 201 LEU n 
1 202 ASN n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 ARG n 
1 208 ALA n 
1 209 LYS n 
1 210 GLY n 
1 211 GLU n 
1 212 ALA n 
1 213 ILE n 
1 214 LYS n 
1 215 ASP n 
1 216 VAL n 
1 217 GLU n 
1 218 ASN n 
1 219 ALA n 
1 220 THR n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 VAL n 
1 225 GLY n 
1 226 VAL n 
1 227 MET n 
1 228 LYS n 
1 229 LEU n 
1 230 LEU n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 PHE n 
1 235 ARG n 
1 236 TYR n 
1 237 ALA n 
1 238 ASP n 
1 239 GLN n 
1 240 MET n 
1 241 GLY n 
1 242 GLN n 
1 243 ARG n 
1 244 GLN n 
1 245 GLY n 
1 246 SER n 
1 247 GLY n 
1 248 ALA n 
1 249 ALA n 
1 250 TYR n 
1 251 LEU n 
1 252 ASN n 
1 253 ILE n 
1 254 PHE n 
1 255 HIS n 
1 256 ARG n 
1 257 ASP n 
1 258 ILE n 
1 259 ASN n 
1 260 ASP n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 THR n 
1 265 LYS n 
1 266 LYS n 
1 267 ILE n 
1 268 SER n 
1 269 ALA n 
1 270 ASP n 
1 271 GLU n 
1 272 ASP n 
1 273 VAL n 
1 274 ARG n 
1 275 VAL n 
1 276 LYS n 
1 277 THR n 
1 278 LEU n 
1 279 SER n 
1 280 ILE n 
1 281 GLY n 
1 282 VAL n 
1 283 VAL n 
1 284 ILE n 
1 285 PRO n 
1 286 ASP n 
1 287 LYS n 
1 288 PHE n 
1 289 VAL n 
1 290 GLU n 
1 291 LEU n 
1 292 ALA n 
1 293 ARG n 
1 294 GLU n 
1 295 ASP n 
1 296 LYS n 
1 297 ALA n 
1 298 ALA n 
1 299 TYR n 
1 300 VAL n 
1 301 PHE n 
1 302 TYR n 
1 303 PRO n 
1 304 HIS n 
1 305 THR n 
1 306 ILE n 
1 307 TYR n 
1 308 LYS n 
1 309 GLU n 
1 310 TYR n 
1 311 GLY n 
1 312 GLN n 
1 313 HIS n 
1 314 MET n 
1 315 ASP n 
1 316 GLU n 
1 317 MET n 
1 318 ASP n 
1 319 MET n 
1 320 ASN n 
1 321 GLU n 
1 322 MET n 
1 323 TYR n 
1 324 ASP n 
1 325 LYS n 
1 326 PHE n 
1 327 VAL n 
1 328 ASP n 
1 329 ASN n 
1 330 PRO n 
1 331 ARG n 
1 332 VAL n 
1 333 LYS n 
1 334 LYS n 
1 335 GLU n 
1 336 LYS n 
1 337 ILE n 
1 338 ASN n 
1 339 PRO n 
1 340 ARG n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 GLU n 
1 345 LYS n 
1 346 LEU n 
1 347 ALA n 
1 348 MET n 
1 349 LEU n 
1 350 ARG n 
1 351 SER n 
1 352 GLU n 
1 353 SER n 
1 354 GLY n 
1 355 TYR n 
1 356 PRO n 
1 357 TYR n 
1 358 ILE n 
1 359 MET n 
1 360 PHE n 
1 361 GLN n 
1 362 ASP n 
1 363 ASN n 
1 364 VAL n 
1 365 ASN n 
1 366 LYS n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ASN n 
1 371 ASN n 
1 372 HIS n 
1 373 ILE n 
1 374 SER n 
1 375 LYS n 
1 376 VAL n 
1 377 LYS n 
1 378 PHE n 
1 379 SER n 
1 380 ASN n 
1 381 LEU n 
1 382 CYS n 
1 383 SER n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 ALA n 
1 389 SER n 
1 390 GLN n 
1 391 VAL n 
1 392 SER n 
1 393 SER n 
1 394 TYR n 
1 395 THR n 
1 396 ASP n 
1 397 TYR n 
1 398 ASP n 
1 399 GLU n 
1 400 GLU n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 GLY n 
1 405 LEU n 
1 406 ASP n 
1 407 ILE n 
1 408 SER n 
1 409 CYS n 
1 410 ASN n 
1 411 LEU n 
1 412 GLY n 
1 413 SER n 
1 414 LEU n 
1 415 ASN n 
1 416 ILE n 
1 417 LEU n 
1 418 ASN n 
1 419 VAL n 
1 420 MET n 
1 421 GLU n 
1 422 HIS n 
1 423 LYS n 
1 424 SER n 
1 425 ILE n 
1 426 GLU n 
1 427 LYS n 
1 428 THR n 
1 429 VAL n 
1 430 LYS n 
1 431 LEU n 
1 432 ALA n 
1 433 THR n 
1 434 ASP n 
1 435 SER n 
1 436 LEU n 
1 437 THR n 
1 438 HIS n 
1 439 VAL n 
1 440 SER n 
1 441 GLU n 
1 442 THR n 
1 443 THR n 
1 444 ASP n 
1 445 ILE n 
1 446 ARG n 
1 447 ASN n 
1 448 ALA n 
1 449 PRO n 
1 450 ALA n 
1 451 VAL n 
1 452 ARG n 
1 453 ARG n 
1 454 ALA n 
1 455 ASN n 
1 456 LYS n 
1 457 ALA n 
1 458 MET n 
1 459 LYS n 
1 460 SER n 
1 461 ILE n 
1 462 GLY n 
1 463 LEU n 
1 464 GLY n 
1 465 ALA n 
1 466 MET n 
1 467 ASN n 
1 468 LEU n 
1 469 HIS n 
1 470 GLY n 
1 471 TYR n 
1 472 LEU n 
1 473 ALA n 
1 474 GLN n 
1 475 ASN n 
1 476 GLY n 
1 477 ILE n 
1 478 ALA n 
1 479 TYR n 
1 480 GLU n 
1 481 SER n 
1 482 PRO n 
1 483 GLU n 
1 484 ALA n 
1 485 ARG n 
1 486 ASP n 
1 487 PHE n 
1 488 ALA n 
1 489 ASN n 
1 490 THR n 
1 491 PHE n 
1 492 PHE n 
1 493 MET n 
1 494 MET n 
1 495 VAL n 
1 496 ASN n 
1 497 PHE n 
1 498 TYR n 
1 499 SER n 
1 500 ILE n 
1 501 GLN n 
1 502 ARG n 
1 503 SER n 
1 504 ALA n 
1 505 GLU n 
1 506 ILE n 
1 507 ALA n 
1 508 LYS n 
1 509 GLU n 
1 510 LYS n 
1 511 GLY n 
1 512 GLU n 
1 513 THR n 
1 514 PHE n 
1 515 ASP n 
1 516 GLN n 
1 517 TYR n 
1 518 GLU n 
1 519 GLY n 
1 520 SER n 
1 521 THR n 
1 522 TYR n 
1 523 ALA n 
1 524 THR n 
1 525 GLY n 
1 526 GLU n 
1 527 TYR n 
1 528 PHE n 
1 529 ASP n 
1 530 LYS n 
1 531 TYR n 
1 532 VAL n 
1 533 SER n 
1 534 THR n 
1 535 ASP n 
1 536 PHE n 
1 537 SER n 
1 538 PRO n 
1 539 LYS n 
1 540 TYR n 
1 541 GLU n 
1 542 LYS n 
1 543 ILE n 
1 544 ALA n 
1 545 ASN n 
1 546 LEU n 
1 547 PHE n 
1 548 GLU n 
1 549 GLY n 
1 550 MET n 
1 551 HIS n 
1 552 ILE n 
1 553 PRO n 
1 554 THR n 
1 555 THR n 
1 556 GLU n 
1 557 ASP n 
1 558 TRP n 
1 559 LYS n 
1 560 LYS n 
1 561 LEU n 
1 562 LYS n 
1 563 ALA n 
1 564 PHE n 
1 565 VAL n 
1 566 ALA n 
1 567 GLU n 
1 568 HIS n 
1 569 GLY n 
1 570 MET n 
1 571 TYR n 
1 572 HIS n 
1 573 SER n 
1 574 TYR n 
1 575 ARG n 
1 576 LEU n 
1 577 CYS n 
1 578 ILE n 
1 579 ALA n 
1 580 PRO n 
1 581 THR n 
1 582 GLY n 
1 583 SER n 
1 584 ILE n 
1 585 SER n 
1 586 TYR n 
1 587 VAL n 
1 588 GLN n 
1 589 SER n 
1 590 SER n 
1 591 THR n 
1 592 ALA n 
1 593 SER n 
1 594 VAL n 
1 595 MET n 
1 596 PRO n 
1 597 ILE n 
1 598 MET n 
1 599 GLU n 
1 600 ARG n 
1 601 ILE n 
1 602 GLU n 
1 603 GLU n 
1 604 ARG n 
1 605 THR n 
1 606 TYR n 
1 607 GLY n 
1 608 ASN n 
1 609 SER n 
1 610 LYS n 
1 611 THR n 
1 612 TYR n 
1 613 TYR n 
1 614 PRO n 
1 615 MET n 
1 616 PRO n 
1 617 GLY n 
1 618 LEU n 
1 619 ALA n 
1 620 SER n 
1 621 ASN n 
1 622 ASN n 
1 623 TRP n 
1 624 PHE n 
1 625 PHE n 
1 626 TYR n 
1 627 LYS n 
1 628 GLU n 
1 629 ALA n 
1 630 TYR n 
1 631 ASP n 
1 632 MET n 
1 633 ASP n 
1 634 MET n 
1 635 PHE n 
1 636 LYS n 
1 637 VAL n 
1 638 VAL n 
1 639 ASP n 
1 640 MET n 
1 641 ILE n 
1 642 ALA n 
1 643 THR n 
1 644 ILE n 
1 645 GLN n 
1 646 GLN n 
1 647 HIS n 
1 648 ILE n 
1 649 ASP n 
1 650 GLN n 
1 651 GLY n 
1 652 ILE n 
1 653 SER n 
1 654 PHE n 
1 655 THR n 
1 656 LEU n 
1 657 PHE n 
1 658 LEU n 
1 659 LYS n 
1 660 ASP n 
1 661 THR n 
1 662 MET n 
1 663 THR n 
1 664 THR n 
1 665 ARG n 
1 666 ASP n 
1 667 LEU n 
1 668 ASN n 
1 669 ARG n 
1 670 ILE n 
1 671 ASP n 
1 672 LEU n 
1 673 TYR n 
1 674 ALA n 
1 675 HIS n 
1 676 HIS n 
1 677 ARG n 
1 678 GLY n 
1 679 ILE n 
1 680 LYS n 
1 681 THR n 
1 682 ILE n 
1 683 TYR n 
1 684 TYR n 
1 685 ALA n 
1 686 ARG n 
1 687 THR n 
1 688 LYS n 
1 689 ASP n 
1 690 THR n 
1 691 GLY n 
1 692 GLN n 
1 693 ASP n 
1 694 SER n 
1 695 CYS n 
1 696 LEU n 
1 697 SER n 
1 698 CYS n 
1 699 VAL n 
1 700 VAL n 
2 1   MET n 
2 2   GLY n 
2 3   SER n 
2 4   SER n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  HIS n 
2 11  SER n 
2 12  SER n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  PRO n 
2 17  ARG n 
2 18  GLY n 
2 19  SER n 
2 20  HIS n 
2 21  MET n 
2 22  MET n 
2 23  THR n 
2 24  LYS n 
2 25  ILE n 
2 26  TYR n 
2 27  ASP n 
2 28  ALA n 
2 29  ALA n 
2 30  ASN n 
2 31  TRP n 
2 32  SER n 
2 33  LYS n 
2 34  HIS n 
2 35  GLU n 
2 36  ASP n 
2 37  ASP n 
2 38  PHE n 
2 39  THR n 
2 40  GLN n 
2 41  MET n 
2 42  PHE n 
2 43  TYR n 
2 44  ASN n 
2 45  GLN n 
2 46  ASN n 
2 47  VAL n 
2 48  LYS n 
2 49  GLN n 
2 50  PHE n 
2 51  TRP n 
2 52  LEU n 
2 53  PRO n 
2 54  GLU n 
2 55  GLU n 
2 56  ILE n 
2 57  ALA n 
2 58  LEU n 
2 59  ASN n 
2 60  GLY n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  THR n 
2 65  TRP n 
2 66  LYS n 
2 67  TYR n 
2 68  LEU n 
2 69  GLY n 
2 70  LYS n 
2 71  ASN n 
2 72  GLU n 
2 73  GLN n 
2 74  ASP n 
2 75  THR n 
2 76  TYR n 
2 77  MET n 
2 78  LYS n 
2 79  VAL n 
2 80  LEU n 
2 81  ALA n 
2 82  GLY n 
2 83  LEU n 
2 84  THR n 
2 85  LEU n 
2 86  LEU n 
2 87  ASP n 
2 88  THR n 
2 89  GLU n 
2 90  GLN n 
2 91  GLY n 
2 92  ASN n 
2 93  THR n 
2 94  GLY n 
2 95  MET n 
2 96  PRO n 
2 97  ILE n 
2 98  VAL n 
2 99  ALA n 
2 100 GLU n 
2 101 HIS n 
2 102 VAL n 
2 103 ASP n 
2 104 GLY n 
2 105 HIS n 
2 106 GLN n 
2 107 ARG n 
2 108 LYS n 
2 109 ALA n 
2 110 VAL n 
2 111 LEU n 
2 112 ASN n 
2 113 PHE n 
2 114 MET n 
2 115 ALA n 
2 116 MET n 
2 117 MET n 
2 118 GLU n 
2 119 ASN n 
2 120 ALA n 
2 121 VAL n 
2 122 HIS n 
2 123 ALA n 
2 124 LYS n 
2 125 SER n 
2 126 TYR n 
2 127 SER n 
2 128 ASN n 
2 129 ILE n 
2 130 PHE n 
2 131 MET n 
2 132 THR n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 GLU n 
2 138 THR n 
2 139 ILE n 
2 140 ASN n 
2 141 GLU n 
2 142 VAL n 
2 143 PHE n 
2 144 GLU n 
2 145 TRP n 
2 146 VAL n 
2 147 LYS n 
2 148 GLN n 
2 149 ASN n 
2 150 LYS n 
2 151 TYR n 
2 152 LEU n 
2 153 GLN n 
2 154 LYS n 
2 155 LYS n 
2 156 ALA n 
2 157 GLN n 
2 158 MET n 
2 159 ILE n 
2 160 VAL n 
2 161 GLY n 
2 162 LEU n 
2 163 TYR n 
2 164 LYS n 
2 165 ALA n 
2 166 ILE n 
2 167 GLN n 
2 168 LYS n 
2 169 ASP n 
2 170 ASP n 
2 171 GLU n 
2 172 ILE n 
2 173 SER n 
2 174 LEU n 
2 175 PHE n 
2 176 LYS n 
2 177 ALA n 
2 178 MET n 
2 179 VAL n 
2 180 ALA n 
2 181 SER n 
2 182 VAL n 
2 183 TYR n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 PHE n 
2 190 TYR n 
2 191 SER n 
2 192 GLY n 
2 193 PHE n 
2 194 TYR n 
2 195 TYR n 
2 196 PRO n 
2 197 LEU n 
2 198 TYR n 
2 199 PHE n 
2 200 TYR n 
2 201 GLY n 
2 202 GLN n 
2 203 GLY n 
2 204 LYS n 
2 205 LEU n 
2 206 MET n 
2 207 GLN n 
2 208 SER n 
2 209 GLY n 
2 210 GLU n 
2 211 ILE n 
2 212 ILE n 
2 213 ASN n 
2 214 LEU n 
2 215 ILE n 
2 216 LEU n 
2 217 ARG n 
2 218 ASP n 
2 219 GLU n 
2 220 ALA n 
2 221 ILE n 
2 222 HIS n 
2 223 GLY n 
2 224 VAL n 
2 225 TYR n 
2 226 VAL n 
2 227 GLY n 
2 228 LEU n 
2 229 LEU n 
2 230 ALA n 
2 231 GLN n 
2 232 GLU n 
2 233 ILE n 
2 234 TYR n 
2 235 ASN n 
2 236 LYS n 
2 237 GLN n 
2 238 THR n 
2 239 GLU n 
2 240 GLU n 
2 241 LYS n 
2 242 LYS n 
2 243 ALA n 
2 244 GLU n 
2 245 LEU n 
2 246 ARG n 
2 247 GLU n 
2 248 PHE n 
2 249 ALA n 
2 250 ILE n 
2 251 ASP n 
2 252 LEU n 
2 253 LEU n 
2 254 ASN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 GLU n 
2 259 ASN n 
2 260 GLU n 
2 261 LEU n 
2 262 GLU n 
2 263 TYR n 
2 264 THR n 
2 265 GLU n 
2 266 ASP n 
2 267 LEU n 
2 268 TYR n 
2 269 ASP n 
2 270 GLN n 
2 271 VAL n 
2 272 GLY n 
2 273 LEU n 
2 274 SER n 
2 275 HIS n 
2 276 ASP n 
2 277 VAL n 
2 278 LYS n 
2 279 LYS n 
2 280 PHE n 
2 281 ILE n 
2 282 ARG n 
2 283 TYR n 
2 284 ASN n 
2 285 ALA n 
2 286 ASN n 
2 287 LYS n 
2 288 ALA n 
2 289 LEU n 
2 290 MET n 
2 291 ASN n 
2 292 LEU n 
2 293 GLY n 
2 294 PHE n 
2 295 ASP n 
2 296 PRO n 
2 297 TYR n 
2 298 PHE n 
2 299 GLU n 
2 300 GLU n 
2 301 GLU n 
2 302 ASP n 
2 303 ILE n 
2 304 ASN n 
2 305 PRO n 
2 306 ILE n 
2 307 VAL n 
2 308 LEU n 
2 309 ASN n 
2 310 GLY n 
2 311 LEU n 
2 312 ASN n 
2 313 THR n 
2 314 LYS n 
2 315 THR n 
2 316 LYS n 
2 317 SER n 
2 318 HIS n 
2 319 ASP n 
2 320 PHE n 
2 321 PHE n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLY n 
2 326 ASN n 
2 327 GLY n 
2 328 TYR n 
2 329 LYS n 
2 330 LYS n 
2 331 ALA n 
2 332 THR n 
2 333 VAL n 
2 334 GLU n 
2 335 PRO n 
2 336 LEU n 
2 337 LYS n 
2 338 ASP n 
2 339 ASP n 
2 340 ASP n 
2 341 PHE n 
2 342 TYR n 
2 343 PHE n 
2 344 GLU n 
2 345 ASP n 
2 346 GLU n 
2 347 LYS n 
2 348 GLU n 
2 349 GLN n 
2 350 ILE n 
3 1   MET n 
3 2   ALA n 
3 3   ILE n 
3 4   VAL n 
3 5   LYS n 
3 6   ALA n 
3 7   THR n 
3 8   ASP n 
3 9   GLN n 
3 10  SER n 
3 11  PHE n 
3 12  SER n 
3 13  ALA n 
3 14  GLU n 
3 15  THR n 
3 16  SER n 
3 17  GLU n 
3 18  GLY n 
3 19  VAL n 
3 20  VAL n 
3 21  LEU n 
3 22  ALA n 
3 23  ASP n 
3 24  PHE n 
3 25  TRP n 
3 26  ALA n 
3 27  PRO n 
3 28  TRP n 
3 29  CYS n 
3 30  GLY n 
3 31  PRO n 
3 32  CYS n 
3 33  LYS n 
3 34  MET n 
3 35  ILE n 
3 36  ALA n 
3 37  PRO n 
3 38  VAL n 
3 39  LEU n 
3 40  GLU n 
3 41  GLU n 
3 42  LEU n 
3 43  ASP n 
3 44  GLN n 
3 45  GLU n 
3 46  MET n 
3 47  GLY n 
3 48  ASP n 
3 49  LYS n 
3 50  LEU n 
3 51  LYS n 
3 52  ILE n 
3 53  VAL n 
3 54  LYS n 
3 55  ILE n 
3 56  ASP n 
3 57  VAL n 
3 58  ASP n 
3 59  GLU n 
3 60  ASN n 
3 61  GLN n 
3 62  GLU n 
3 63  THR n 
3 64  ALA n 
3 65  GLY n 
3 66  LYS n 
3 67  TYR n 
3 68  GLY n 
3 69  VAL n 
3 70  MET n 
3 71  SER n 
3 72  ILE n 
3 73  PRO n 
3 74  THR n 
3 75  LEU n 
3 76  LEU n 
3 77  VAL n 
3 78  LEU n 
3 79  LYS n 
3 80  ASP n 
3 81  GLY n 
3 82  GLU n 
3 83  VAL n 
3 84  VAL n 
3 85  GLU n 
3 86  THR n 
3 87  SER n 
3 88  VAL n 
3 89  GLY n 
3 90  PHE n 
3 91  LYS n 
3 92  PRO n 
3 93  LYS n 
3 94  GLU n 
3 95  ALA n 
3 96  LEU n 
3 97  GLN n 
3 98  GLU n 
3 99  LEU n 
3 100 VAL n 
3 101 ASN n 
3 102 LYS n 
3 103 HIS n 
3 104 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 700 ? ? 'nrdE, nrdA, BSU17380' ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 ? ? 'nrdF, BSU17390'       ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 104 ? ? 'trxA, trx, BSU28500'  ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TTP non-polymer         . "THYMIDINE-5'-TRIPHOSPHATE" ? 'C10 H17 N2 O14 P3' 482.168 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 CYS 170 170 170 CYS CYS A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 MET 190 190 190 MET MET 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 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 TYR 307 307 307 TYR TYR A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 HIS 313 313 313 HIS HIS A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 MET 317 317 317 MET MET A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 MET 319 319 319 MET MET A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ARG 331 331 331 ARG ARG A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 MET 359 359 359 MET MET A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 CYS 382 382 382 CYS CYS A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ASP 401 401 401 ASP ASP A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 ILE 403 403 403 ILE ILE 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 ASP 406 406 406 ASP ASP A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 ASN 418 418 418 ASN ASN A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 HIS 422 422 422 HIS HIS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 THR 428 428 428 THR THR A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 HIS 438 438 438 HIS HIS A . n 
A 1 439 VAL 439 439 439 VAL VAL A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 LYS 456 456 456 LYS LYS A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 MET 466 466 466 MET MET A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 LEU 468 468 468 LEU LEU A . n 
A 1 469 HIS 469 469 469 HIS HIS A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 TYR 471 471 471 TYR TYR A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 TYR 479 479 479 TYR TYR A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 PRO 482 482 482 PRO PRO A . n 
A 1 483 GLU 483 483 483 GLU GLU A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 PHE 491 491 491 PHE PHE A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 MET 493 493 493 MET MET A . n 
A 1 494 MET 494 494 494 MET MET A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ASN 496 496 496 ASN ASN A . n 
A 1 497 PHE 497 497 497 PHE PHE A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 GLN 501 501 501 GLN GLN A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 LYS 508 508 508 LYS LYS A . n 
A 1 509 GLU 509 509 509 GLU GLU A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 GLY 511 511 511 GLY GLY A . n 
A 1 512 GLU 512 512 512 GLU GLU A . n 
A 1 513 THR 513 513 513 THR THR 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 GLN 516 516 516 GLN GLN A . n 
A 1 517 TYR 517 517 517 TYR TYR A . n 
A 1 518 GLU 518 518 518 GLU GLU A . n 
A 1 519 GLY 519 519 519 GLY GLY A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 THR 521 521 521 THR THR A . n 
A 1 522 TYR 522 522 522 TYR TYR A . n 
A 1 523 ALA 523 523 523 ALA ALA A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 GLU 526 526 526 GLU GLU A . n 
A 1 527 TYR 527 527 527 TYR TYR A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 ASP 529 529 529 ASP ASP A . n 
A 1 530 LYS 530 530 530 LYS LYS A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 VAL 532 532 532 VAL VAL A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 PHE 536 536 536 PHE PHE A . n 
A 1 537 SER 537 537 537 SER SER A . n 
A 1 538 PRO 538 538 538 PRO PRO A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 GLU 541 541 541 GLU GLU A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ALA 544 544 544 ALA ALA A . n 
A 1 545 ASN 545 545 545 ASN ASN A . n 
A 1 546 LEU 546 546 546 LEU LEU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 MET 550 550 550 MET MET A . n 
A 1 551 HIS 551 551 551 HIS HIS A . n 
A 1 552 ILE 552 552 552 ILE ILE A . n 
A 1 553 PRO 553 553 553 PRO PRO A . n 
A 1 554 THR 554 554 554 THR THR A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 ASP 557 557 557 ASP ASP A . n 
A 1 558 TRP 558 558 558 TRP TRP A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 PHE 564 564 564 PHE PHE A . n 
A 1 565 VAL 565 565 565 VAL VAL A . n 
A 1 566 ALA 566 566 566 ALA ALA A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 HIS 568 568 568 HIS HIS A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 MET 570 570 570 MET MET A . n 
A 1 571 TYR 571 571 571 TYR TYR A . n 
A 1 572 HIS 572 572 572 HIS HIS A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 TYR 574 574 574 TYR TYR A . n 
A 1 575 ARG 575 575 575 ARG ARG A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 CYS 577 577 577 CYS CYS A . n 
A 1 578 ILE 578 578 578 ILE ILE A . n 
A 1 579 ALA 579 579 579 ALA ALA A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 SER 583 583 583 SER SER A . n 
A 1 584 ILE 584 584 584 ILE ILE A . n 
A 1 585 SER 585 585 585 SER SER A . n 
A 1 586 TYR 586 586 586 TYR TYR A . n 
A 1 587 VAL 587 587 587 VAL VAL A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 SER 589 589 589 SER SER A . n 
A 1 590 SER 590 590 590 SER SER A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 SER 593 593 593 SER SER A . n 
A 1 594 VAL 594 594 594 VAL VAL A . n 
A 1 595 MET 595 595 595 MET MET A . n 
A 1 596 PRO 596 596 596 PRO PRO A . n 
A 1 597 ILE 597 597 597 ILE ILE A . n 
A 1 598 MET 598 598 598 MET MET A . n 
A 1 599 GLU 599 599 599 GLU GLU A . n 
A 1 600 ARG 600 600 600 ARG ARG A . n 
A 1 601 ILE 601 601 601 ILE ILE A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 GLU 603 603 603 GLU GLU A . n 
A 1 604 ARG 604 604 604 ARG ARG A . n 
A 1 605 THR 605 605 605 THR THR A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLY 607 607 607 GLY GLY A . n 
A 1 608 ASN 608 608 608 ASN ASN A . n 
A 1 609 SER 609 609 609 SER SER A . n 
A 1 610 LYS 610 610 610 LYS LYS A . n 
A 1 611 THR 611 611 611 THR THR A . n 
A 1 612 TYR 612 612 612 TYR TYR A . n 
A 1 613 TYR 613 613 613 TYR TYR A . n 
A 1 614 PRO 614 614 614 PRO PRO A . n 
A 1 615 MET 615 615 615 MET MET A . n 
A 1 616 PRO 616 616 616 PRO PRO A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 TRP 623 623 623 TRP TRP A . n 
A 1 624 PHE 624 624 624 PHE PHE A . n 
A 1 625 PHE 625 625 625 PHE PHE A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LYS 627 627 627 LYS LYS A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 ALA 629 629 629 ALA ALA A . n 
A 1 630 TYR 630 630 630 TYR TYR A . n 
A 1 631 ASP 631 631 631 ASP ASP A . n 
A 1 632 MET 632 632 632 MET MET A . n 
A 1 633 ASP 633 633 633 ASP ASP A . n 
A 1 634 MET 634 634 634 MET MET A . n 
A 1 635 PHE 635 635 635 PHE PHE A . n 
A 1 636 LYS 636 636 636 LYS LYS A . n 
A 1 637 VAL 637 637 637 VAL VAL A . n 
A 1 638 VAL 638 638 638 VAL VAL A . n 
A 1 639 ASP 639 639 639 ASP ASP A . n 
A 1 640 MET 640 640 640 MET MET A . n 
A 1 641 ILE 641 641 641 ILE ILE A . n 
A 1 642 ALA 642 642 642 ALA ALA A . n 
A 1 643 THR 643 643 643 THR THR A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 GLN 645 645 645 GLN GLN A . n 
A 1 646 GLN 646 646 646 GLN GLN A . n 
A 1 647 HIS 647 647 647 HIS HIS A . n 
A 1 648 ILE 648 648 648 ILE ILE A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 GLN 650 650 650 GLN GLN A . n 
A 1 651 GLY 651 651 651 GLY GLY A . n 
A 1 652 ILE 652 652 652 ILE ILE A . n 
A 1 653 SER 653 653 653 SER SER A . n 
A 1 654 PHE 654 654 654 PHE PHE A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 PHE 657 657 657 PHE PHE A . n 
A 1 658 LEU 658 658 658 LEU LEU A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 ASP 660 660 660 ASP ASP A . n 
A 1 661 THR 661 661 661 THR THR A . n 
A 1 662 MET 662 662 662 MET MET A . n 
A 1 663 THR 663 663 663 THR THR A . n 
A 1 664 THR 664 664 664 THR THR A . n 
A 1 665 ARG 665 665 665 ARG ARG A . n 
A 1 666 ASP 666 666 666 ASP ASP A . n 
A 1 667 LEU 667 667 667 LEU LEU A . n 
A 1 668 ASN 668 668 668 ASN ASN A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 ILE 670 670 670 ILE ILE A . n 
A 1 671 ASP 671 671 671 ASP ASP A . n 
A 1 672 LEU 672 672 672 LEU LEU A . n 
A 1 673 TYR 673 673 673 TYR TYR A . n 
A 1 674 ALA 674 674 674 ALA ALA A . n 
A 1 675 HIS 675 675 675 HIS HIS A . n 
A 1 676 HIS 676 676 676 HIS HIS A . n 
A 1 677 ARG 677 677 677 ARG ARG A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 ILE 679 679 679 ILE ILE A . n 
A 1 680 LYS 680 680 680 LYS LYS A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 ILE 682 682 682 ILE ILE A . n 
A 1 683 TYR 683 683 683 TYR TYR A . n 
A 1 684 TYR 684 684 684 TYR TYR A . n 
A 1 685 ALA 685 685 685 ALA ALA A . n 
A 1 686 ARG 686 686 686 ARG ARG A . n 
A 1 687 THR 687 687 687 THR THR A . n 
A 1 688 LYS 688 688 688 LYS LYS A . n 
A 1 689 ASP 689 689 ?   ?   ?   A . n 
A 1 690 THR 690 690 ?   ?   ?   A . n 
A 1 691 GLY 691 691 ?   ?   ?   A . n 
A 1 692 GLN 692 692 ?   ?   ?   A . n 
A 1 693 ASP 693 693 ?   ?   ?   A . n 
A 1 694 SER 694 694 ?   ?   ?   A . n 
A 1 695 CYS 695 695 ?   ?   ?   A . n 
A 1 696 LEU 696 696 ?   ?   ?   A . n 
A 1 697 SER 697 697 ?   ?   ?   A . n 
A 1 698 CYS 698 698 ?   ?   ?   A . n 
A 1 699 VAL 699 699 ?   ?   ?   A . n 
A 1 700 VAL 700 700 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  TYR 36  36  36  TYR TYR B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  HIS 49  49  49  HIS HIS B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ILE 77  77  77  ILE ILE B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  MET 95  95  95  MET MET B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 TYR 104 104 104 TYR TYR B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 MET 144 144 144 MET MET B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 GLN 147 147 147 GLN GLN B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 CYS 170 170 170 CYS CYS B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 GLN 191 191 191 GLN GLN B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 LYS 209 209 209 LYS LYS B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ASN 218 218 218 ASN ASN B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 TYR 250 250 250 TYR TYR B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 SER 279 279 279 SER SER B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 LYS 287 287 287 LYS LYS B . n 
B 1 288 PHE 288 288 288 PHE PHE B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 TYR 307 307 307 TYR TYR B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 GLN 312 312 312 GLN GLN B . n 
B 1 313 HIS 313 313 313 HIS HIS B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 MET 317 317 317 MET MET B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 MET 319 319 319 MET MET B . n 
B 1 320 ASN 320 320 320 ASN ASN B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 MET 322 322 322 MET MET B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 PRO 330 330 330 PRO PRO B . n 
B 1 331 ARG 331 331 331 ARG ARG B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 GLU 335 335 335 GLU GLU B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 TYR 355 355 355 TYR TYR B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 MET 359 359 359 MET MET B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 GLN 361 361 361 GLN GLN B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 VAL 364 364 364 VAL VAL B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 LYS 366 366 366 LYS LYS B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 HIS 372 372 372 HIS HIS B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 SER 374 374 374 SER SER B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 SER 379 379 379 SER SER B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 CYS 382 382 382 CYS CYS B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 SER 389 389 389 SER SER B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 ASP 396 396 396 ASP ASP B . n 
B 1 397 TYR 397 397 397 TYR TYR B . n 
B 1 398 ASP 398 398 398 ASP ASP B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 ASP 401 401 401 ASP ASP B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 GLY 404 404 404 GLY GLY B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 ASP 406 406 406 ASP ASP B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ASN 415 415 415 ASN ASN B . n 
B 1 416 ILE 416 416 416 ILE ILE B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 ASN 418 418 418 ASN ASN B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 HIS 422 422 422 HIS HIS B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLU 426 426 426 GLU GLU B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 THR 428 428 428 THR THR B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 HIS 438 438 438 HIS HIS B . n 
B 1 439 VAL 439 439 439 VAL VAL B . n 
B 1 440 SER 440 440 440 SER SER B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 THR 442 442 442 THR THR B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 ILE 445 445 445 ILE ILE B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 PRO 449 449 449 PRO PRO B . n 
B 1 450 ALA 450 450 450 ALA ALA B . n 
B 1 451 VAL 451 451 451 VAL VAL B . n 
B 1 452 ARG 452 452 452 ARG ARG B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 LYS 456 456 456 LYS LYS B . n 
B 1 457 ALA 457 457 457 ALA ALA B . n 
B 1 458 MET 458 458 458 MET MET B . n 
B 1 459 LYS 459 459 459 LYS LYS B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 ILE 461 461 461 ILE ILE B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 MET 466 466 466 MET MET B . n 
B 1 467 ASN 467 467 467 ASN ASN B . n 
B 1 468 LEU 468 468 468 LEU LEU B . n 
B 1 469 HIS 469 469 469 HIS HIS B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 TYR 471 471 471 TYR TYR B . n 
B 1 472 LEU 472 472 472 LEU LEU B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 ASN 475 475 475 ASN ASN B . n 
B 1 476 GLY 476 476 476 GLY GLY B . n 
B 1 477 ILE 477 477 477 ILE ILE B . n 
B 1 478 ALA 478 478 478 ALA ALA B . n 
B 1 479 TYR 479 479 479 TYR TYR B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 SER 481 481 481 SER SER B . n 
B 1 482 PRO 482 482 482 PRO PRO B . n 
B 1 483 GLU 483 483 483 GLU GLU B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 PHE 487 487 487 PHE PHE B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 ASN 489 489 489 ASN ASN B . n 
B 1 490 THR 490 490 490 THR THR B . n 
B 1 491 PHE 491 491 491 PHE PHE B . n 
B 1 492 PHE 492 492 492 PHE PHE B . n 
B 1 493 MET 493 493 493 MET MET B . n 
B 1 494 MET 494 494 494 MET MET B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 ASN 496 496 496 ASN ASN B . n 
B 1 497 PHE 497 497 497 PHE PHE B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 SER 499 499 499 SER SER B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 GLN 501 501 501 GLN GLN B . n 
B 1 502 ARG 502 502 502 ARG ARG B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 ALA 504 504 504 ALA ALA B . n 
B 1 505 GLU 505 505 505 GLU GLU B . n 
B 1 506 ILE 506 506 506 ILE ILE B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 LYS 508 508 508 LYS LYS B . n 
B 1 509 GLU 509 509 509 GLU GLU B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 GLY 511 511 511 GLY GLY B . n 
B 1 512 GLU 512 512 512 GLU GLU B . n 
B 1 513 THR 513 513 513 THR THR B . n 
B 1 514 PHE 514 514 514 PHE PHE B . n 
B 1 515 ASP 515 515 515 ASP ASP B . n 
B 1 516 GLN 516 516 516 GLN GLN B . n 
B 1 517 TYR 517 517 517 TYR TYR B . n 
B 1 518 GLU 518 518 518 GLU GLU B . n 
B 1 519 GLY 519 519 519 GLY GLY B . n 
B 1 520 SER 520 520 520 SER SER B . n 
B 1 521 THR 521 521 521 THR THR B . n 
B 1 522 TYR 522 522 522 TYR TYR B . n 
B 1 523 ALA 523 523 523 ALA ALA B . n 
B 1 524 THR 524 524 524 THR THR B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 GLU 526 526 526 GLU GLU B . n 
B 1 527 TYR 527 527 527 TYR TYR B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 ASP 529 529 529 ASP ASP B . n 
B 1 530 LYS 530 530 530 LYS LYS B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 VAL 532 532 532 VAL VAL B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 THR 534 534 534 THR THR B . n 
B 1 535 ASP 535 535 535 ASP ASP B . n 
B 1 536 PHE 536 536 536 PHE PHE B . n 
B 1 537 SER 537 537 537 SER SER B . n 
B 1 538 PRO 538 538 538 PRO PRO B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 TYR 540 540 540 TYR TYR B . n 
B 1 541 GLU 541 541 541 GLU GLU B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 ILE 543 543 543 ILE ILE B . n 
B 1 544 ALA 544 544 544 ALA ALA B . n 
B 1 545 ASN 545 545 545 ASN ASN B . n 
B 1 546 LEU 546 546 546 LEU LEU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 GLU 548 548 548 GLU GLU B . n 
B 1 549 GLY 549 549 549 GLY GLY B . n 
B 1 550 MET 550 550 550 MET MET B . n 
B 1 551 HIS 551 551 551 HIS HIS B . n 
B 1 552 ILE 552 552 552 ILE ILE B . n 
B 1 553 PRO 553 553 553 PRO PRO B . n 
B 1 554 THR 554 554 554 THR THR B . n 
B 1 555 THR 555 555 555 THR THR B . n 
B 1 556 GLU 556 556 556 GLU GLU B . n 
B 1 557 ASP 557 557 557 ASP ASP B . n 
B 1 558 TRP 558 558 558 TRP TRP B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 LYS 560 560 560 LYS LYS B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 LYS 562 562 562 LYS LYS B . n 
B 1 563 ALA 563 563 563 ALA ALA B . n 
B 1 564 PHE 564 564 564 PHE PHE B . n 
B 1 565 VAL 565 565 565 VAL VAL B . n 
B 1 566 ALA 566 566 566 ALA ALA B . n 
B 1 567 GLU 567 567 567 GLU GLU B . n 
B 1 568 HIS 568 568 568 HIS HIS B . n 
B 1 569 GLY 569 569 569 GLY GLY B . n 
B 1 570 MET 570 570 570 MET MET B . n 
B 1 571 TYR 571 571 571 TYR TYR B . n 
B 1 572 HIS 572 572 572 HIS HIS B . n 
B 1 573 SER 573 573 573 SER SER B . n 
B 1 574 TYR 574 574 574 TYR TYR B . n 
B 1 575 ARG 575 575 575 ARG ARG B . n 
B 1 576 LEU 576 576 576 LEU LEU B . n 
B 1 577 CYS 577 577 577 CYS CYS B . n 
B 1 578 ILE 578 578 578 ILE ILE B . n 
B 1 579 ALA 579 579 579 ALA ALA B . n 
B 1 580 PRO 580 580 580 PRO PRO B . n 
B 1 581 THR 581 581 581 THR THR B . n 
B 1 582 GLY 582 582 582 GLY GLY B . n 
B 1 583 SER 583 583 583 SER SER B . n 
B 1 584 ILE 584 584 584 ILE ILE B . n 
B 1 585 SER 585 585 585 SER SER B . n 
B 1 586 TYR 586 586 586 TYR TYR B . n 
B 1 587 VAL 587 587 587 VAL VAL B . n 
B 1 588 GLN 588 588 588 GLN GLN B . n 
B 1 589 SER 589 589 589 SER SER B . n 
B 1 590 SER 590 590 590 SER SER B . n 
B 1 591 THR 591 591 591 THR THR B . n 
B 1 592 ALA 592 592 592 ALA ALA B . n 
B 1 593 SER 593 593 593 SER SER B . n 
B 1 594 VAL 594 594 594 VAL VAL B . n 
B 1 595 MET 595 595 595 MET MET B . n 
B 1 596 PRO 596 596 596 PRO PRO B . n 
B 1 597 ILE 597 597 597 ILE ILE B . n 
B 1 598 MET 598 598 598 MET MET B . n 
B 1 599 GLU 599 599 599 GLU GLU B . n 
B 1 600 ARG 600 600 600 ARG ARG B . n 
B 1 601 ILE 601 601 601 ILE ILE B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 GLU 603 603 603 GLU GLU B . n 
B 1 604 ARG 604 604 604 ARG ARG B . n 
B 1 605 THR 605 605 605 THR THR B . n 
B 1 606 TYR 606 606 606 TYR TYR B . n 
B 1 607 GLY 607 607 607 GLY GLY B . n 
B 1 608 ASN 608 608 608 ASN ASN B . n 
B 1 609 SER 609 609 609 SER SER B . n 
B 1 610 LYS 610 610 610 LYS LYS B . n 
B 1 611 THR 611 611 611 THR THR B . n 
B 1 612 TYR 612 612 612 TYR TYR B . n 
B 1 613 TYR 613 613 613 TYR TYR B . n 
B 1 614 PRO 614 614 614 PRO PRO B . n 
B 1 615 MET 615 615 615 MET MET B . n 
B 1 616 PRO 616 616 616 PRO PRO B . n 
B 1 617 GLY 617 617 617 GLY GLY B . n 
B 1 618 LEU 618 618 618 LEU LEU B . n 
B 1 619 ALA 619 619 619 ALA ALA B . n 
B 1 620 SER 620 620 620 SER SER B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 ASN 622 622 622 ASN ASN B . n 
B 1 623 TRP 623 623 623 TRP TRP B . n 
B 1 624 PHE 624 624 624 PHE PHE B . n 
B 1 625 PHE 625 625 625 PHE PHE B . n 
B 1 626 TYR 626 626 626 TYR TYR B . n 
B 1 627 LYS 627 627 627 LYS LYS B . n 
B 1 628 GLU 628 628 628 GLU GLU B . n 
B 1 629 ALA 629 629 629 ALA ALA B . n 
B 1 630 TYR 630 630 630 TYR TYR B . n 
B 1 631 ASP 631 631 631 ASP ASP B . n 
B 1 632 MET 632 632 632 MET MET B . n 
B 1 633 ASP 633 633 633 ASP ASP B . n 
B 1 634 MET 634 634 634 MET MET B . n 
B 1 635 PHE 635 635 635 PHE PHE B . n 
B 1 636 LYS 636 636 636 LYS LYS B . n 
B 1 637 VAL 637 637 637 VAL VAL B . n 
B 1 638 VAL 638 638 638 VAL VAL B . n 
B 1 639 ASP 639 639 639 ASP ASP B . n 
B 1 640 MET 640 640 640 MET MET B . n 
B 1 641 ILE 641 641 641 ILE ILE B . n 
B 1 642 ALA 642 642 642 ALA ALA B . n 
B 1 643 THR 643 643 643 THR THR B . n 
B 1 644 ILE 644 644 644 ILE ILE B . n 
B 1 645 GLN 645 645 645 GLN GLN B . n 
B 1 646 GLN 646 646 646 GLN GLN B . n 
B 1 647 HIS 647 647 647 HIS HIS B . n 
B 1 648 ILE 648 648 648 ILE ILE B . n 
B 1 649 ASP 649 649 649 ASP ASP B . n 
B 1 650 GLN 650 650 650 GLN GLN B . n 
B 1 651 GLY 651 651 651 GLY GLY B . n 
B 1 652 ILE 652 652 652 ILE ILE B . n 
B 1 653 SER 653 653 653 SER SER B . n 
B 1 654 PHE 654 654 654 PHE PHE B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 LEU 656 656 656 LEU LEU B . n 
B 1 657 PHE 657 657 657 PHE PHE B . n 
B 1 658 LEU 658 658 658 LEU LEU B . n 
B 1 659 LYS 659 659 659 LYS LYS B . n 
B 1 660 ASP 660 660 660 ASP ASP B . n 
B 1 661 THR 661 661 661 THR THR B . n 
B 1 662 MET 662 662 662 MET MET B . n 
B 1 663 THR 663 663 663 THR THR B . n 
B 1 664 THR 664 664 664 THR THR B . n 
B 1 665 ARG 665 665 665 ARG ARG B . n 
B 1 666 ASP 666 666 666 ASP ASP B . n 
B 1 667 LEU 667 667 667 LEU LEU B . n 
B 1 668 ASN 668 668 668 ASN ASN B . n 
B 1 669 ARG 669 669 669 ARG ARG B . n 
B 1 670 ILE 670 670 670 ILE ILE B . n 
B 1 671 ASP 671 671 671 ASP ASP B . n 
B 1 672 LEU 672 672 672 LEU LEU B . n 
B 1 673 TYR 673 673 673 TYR TYR B . n 
B 1 674 ALA 674 674 674 ALA ALA B . n 
B 1 675 HIS 675 675 675 HIS HIS B . n 
B 1 676 HIS 676 676 676 HIS HIS B . n 
B 1 677 ARG 677 677 677 ARG ARG B . n 
B 1 678 GLY 678 678 678 GLY GLY B . n 
B 1 679 ILE 679 679 679 ILE ILE B . n 
B 1 680 LYS 680 680 680 LYS LYS B . n 
B 1 681 THR 681 681 681 THR THR B . n 
B 1 682 ILE 682 682 682 ILE ILE B . n 
B 1 683 TYR 683 683 683 TYR TYR B . n 
B 1 684 TYR 684 684 684 TYR TYR B . n 
B 1 685 ALA 685 685 685 ALA ALA B . n 
B 1 686 ARG 686 686 686 ARG ARG B . n 
B 1 687 THR 687 687 687 THR THR B . n 
B 1 688 LYS 688 688 688 LYS LYS B . n 
B 1 689 ASP 689 689 ?   ?   ?   B . n 
B 1 690 THR 690 690 ?   ?   ?   B . n 
B 1 691 GLY 691 691 ?   ?   ?   B . n 
B 1 692 GLN 692 692 ?   ?   ?   B . n 
B 1 693 ASP 693 693 ?   ?   ?   B . n 
B 1 694 SER 694 694 ?   ?   ?   B . n 
B 1 695 CYS 695 695 ?   ?   ?   B . n 
B 1 696 LEU 696 696 ?   ?   ?   B . n 
B 1 697 SER 697 697 ?   ?   ?   B . n 
B 1 698 CYS 698 698 ?   ?   ?   B . n 
B 1 699 VAL 699 699 ?   ?   ?   B . n 
B 1 700 VAL 700 700 ?   ?   ?   B . n 
C 2 1   MET 1   -20 ?   ?   ?   C . n 
C 2 2   GLY 2   -19 ?   ?   ?   C . n 
C 2 3   SER 3   -18 ?   ?   ?   C . n 
C 2 4   SER 4   -17 ?   ?   ?   C . n 
C 2 5   HIS 5   -16 ?   ?   ?   C . n 
C 2 6   HIS 6   -15 ?   ?   ?   C . n 
C 2 7   HIS 7   -14 ?   ?   ?   C . n 
C 2 8   HIS 8   -13 ?   ?   ?   C . n 
C 2 9   HIS 9   -12 ?   ?   ?   C . n 
C 2 10  HIS 10  -11 ?   ?   ?   C . n 
C 2 11  SER 11  -10 ?   ?   ?   C . n 
C 2 12  SER 12  -9  ?   ?   ?   C . n 
C 2 13  GLY 13  -8  ?   ?   ?   C . n 
C 2 14  LEU 14  -7  ?   ?   ?   C . n 
C 2 15  VAL 15  -6  ?   ?   ?   C . n 
C 2 16  PRO 16  -5  ?   ?   ?   C . n 
C 2 17  ARG 17  -4  ?   ?   ?   C . n 
C 2 18  GLY 18  -3  ?   ?   ?   C . n 
C 2 19  SER 19  -2  ?   ?   ?   C . n 
C 2 20  HIS 20  -1  ?   ?   ?   C . n 
C 2 21  MET 21  0   ?   ?   ?   C . n 
C 2 22  MET 22  1   ?   ?   ?   C . n 
C 2 23  THR 23  2   ?   ?   ?   C . n 
C 2 24  LYS 24  3   ?   ?   ?   C . n 
C 2 25  ILE 25  4   ?   ?   ?   C . n 
C 2 26  TYR 26  5   ?   ?   ?   C . n 
C 2 27  ASP 27  6   ?   ?   ?   C . n 
C 2 28  ALA 28  7   ?   ?   ?   C . n 
C 2 29  ALA 29  8   ?   ?   ?   C . n 
C 2 30  ASN 30  9   ?   ?   ?   C . n 
C 2 31  TRP 31  10  ?   ?   ?   C . n 
C 2 32  SER 32  11  ?   ?   ?   C . n 
C 2 33  LYS 33  12  ?   ?   ?   C . n 
C 2 34  HIS 34  13  ?   ?   ?   C . n 
C 2 35  GLU 35  14  ?   ?   ?   C . n 
C 2 36  ASP 36  15  ?   ?   ?   C . n 
C 2 37  ASP 37  16  ?   ?   ?   C . n 
C 2 38  PHE 38  17  ?   ?   ?   C . n 
C 2 39  THR 39  18  ?   ?   ?   C . n 
C 2 40  GLN 40  19  ?   ?   ?   C . n 
C 2 41  MET 41  20  ?   ?   ?   C . n 
C 2 42  PHE 42  21  ?   ?   ?   C . n 
C 2 43  TYR 43  22  ?   ?   ?   C . n 
C 2 44  ASN 44  23  ?   ?   ?   C . n 
C 2 45  GLN 45  24  ?   ?   ?   C . n 
C 2 46  ASN 46  25  ?   ?   ?   C . n 
C 2 47  VAL 47  26  ?   ?   ?   C . n 
C 2 48  LYS 48  27  ?   ?   ?   C . n 
C 2 49  GLN 49  28  ?   ?   ?   C . n 
C 2 50  PHE 50  29  ?   ?   ?   C . n 
C 2 51  TRP 51  30  ?   ?   ?   C . n 
C 2 52  LEU 52  31  ?   ?   ?   C . n 
C 2 53  PRO 53  32  ?   ?   ?   C . n 
C 2 54  GLU 54  33  ?   ?   ?   C . n 
C 2 55  GLU 55  34  ?   ?   ?   C . n 
C 2 56  ILE 56  35  ?   ?   ?   C . n 
C 2 57  ALA 57  36  ?   ?   ?   C . n 
C 2 58  LEU 58  37  ?   ?   ?   C . n 
C 2 59  ASN 59  38  ?   ?   ?   C . n 
C 2 60  GLY 60  39  ?   ?   ?   C . n 
C 2 61  ASP 61  40  ?   ?   ?   C . n 
C 2 62  LEU 62  41  ?   ?   ?   C . n 
C 2 63  LEU 63  42  ?   ?   ?   C . n 
C 2 64  THR 64  43  ?   ?   ?   C . n 
C 2 65  TRP 65  44  ?   ?   ?   C . n 
C 2 66  LYS 66  45  ?   ?   ?   C . n 
C 2 67  TYR 67  46  ?   ?   ?   C . n 
C 2 68  LEU 68  47  ?   ?   ?   C . n 
C 2 69  GLY 69  48  ?   ?   ?   C . n 
C 2 70  LYS 70  49  ?   ?   ?   C . n 
C 2 71  ASN 71  50  ?   ?   ?   C . n 
C 2 72  GLU 72  51  ?   ?   ?   C . n 
C 2 73  GLN 73  52  ?   ?   ?   C . n 
C 2 74  ASP 74  53  ?   ?   ?   C . n 
C 2 75  THR 75  54  ?   ?   ?   C . n 
C 2 76  TYR 76  55  ?   ?   ?   C . n 
C 2 77  MET 77  56  ?   ?   ?   C . n 
C 2 78  LYS 78  57  ?   ?   ?   C . n 
C 2 79  VAL 79  58  ?   ?   ?   C . n 
C 2 80  LEU 80  59  ?   ?   ?   C . n 
C 2 81  ALA 81  60  ?   ?   ?   C . n 
C 2 82  GLY 82  61  ?   ?   ?   C . n 
C 2 83  LEU 83  62  ?   ?   ?   C . n 
C 2 84  THR 84  63  ?   ?   ?   C . n 
C 2 85  LEU 85  64  ?   ?   ?   C . n 
C 2 86  LEU 86  65  ?   ?   ?   C . n 
C 2 87  ASP 87  66  ?   ?   ?   C . n 
C 2 88  THR 88  67  ?   ?   ?   C . n 
C 2 89  GLU 89  68  ?   ?   ?   C . n 
C 2 90  GLN 90  69  ?   ?   ?   C . n 
C 2 91  GLY 91  70  ?   ?   ?   C . n 
C 2 92  ASN 92  71  ?   ?   ?   C . n 
C 2 93  THR 93  72  ?   ?   ?   C . n 
C 2 94  GLY 94  73  ?   ?   ?   C . n 
C 2 95  MET 95  74  ?   ?   ?   C . n 
C 2 96  PRO 96  75  ?   ?   ?   C . n 
C 2 97  ILE 97  76  ?   ?   ?   C . n 
C 2 98  VAL 98  77  ?   ?   ?   C . n 
C 2 99  ALA 99  78  ?   ?   ?   C . n 
C 2 100 GLU 100 79  ?   ?   ?   C . n 
C 2 101 HIS 101 80  ?   ?   ?   C . n 
C 2 102 VAL 102 81  ?   ?   ?   C . n 
C 2 103 ASP 103 82  ?   ?   ?   C . n 
C 2 104 GLY 104 83  ?   ?   ?   C . n 
C 2 105 HIS 105 84  ?   ?   ?   C . n 
C 2 106 GLN 106 85  ?   ?   ?   C . n 
C 2 107 ARG 107 86  ?   ?   ?   C . n 
C 2 108 LYS 108 87  ?   ?   ?   C . n 
C 2 109 ALA 109 88  ?   ?   ?   C . n 
C 2 110 VAL 110 89  ?   ?   ?   C . n 
C 2 111 LEU 111 90  ?   ?   ?   C . n 
C 2 112 ASN 112 91  ?   ?   ?   C . n 
C 2 113 PHE 113 92  ?   ?   ?   C . n 
C 2 114 MET 114 93  ?   ?   ?   C . n 
C 2 115 ALA 115 94  ?   ?   ?   C . n 
C 2 116 MET 116 95  ?   ?   ?   C . n 
C 2 117 MET 117 96  ?   ?   ?   C . n 
C 2 118 GLU 118 97  ?   ?   ?   C . n 
C 2 119 ASN 119 98  ?   ?   ?   C . n 
C 2 120 ALA 120 99  ?   ?   ?   C . n 
C 2 121 VAL 121 100 ?   ?   ?   C . n 
C 2 122 HIS 122 101 ?   ?   ?   C . n 
C 2 123 ALA 123 102 ?   ?   ?   C . n 
C 2 124 LYS 124 103 ?   ?   ?   C . n 
C 2 125 SER 125 104 ?   ?   ?   C . n 
C 2 126 TYR 126 105 ?   ?   ?   C . n 
C 2 127 SER 127 106 ?   ?   ?   C . n 
C 2 128 ASN 128 107 ?   ?   ?   C . n 
C 2 129 ILE 129 108 ?   ?   ?   C . n 
C 2 130 PHE 130 109 ?   ?   ?   C . n 
C 2 131 MET 131 110 ?   ?   ?   C . n 
C 2 132 THR 132 111 ?   ?   ?   C . n 
C 2 133 LEU 133 112 ?   ?   ?   C . n 
C 2 134 ALA 134 113 ?   ?   ?   C . n 
C 2 135 PRO 135 114 ?   ?   ?   C . n 
C 2 136 THR 136 115 ?   ?   ?   C . n 
C 2 137 GLU 137 116 ?   ?   ?   C . n 
C 2 138 THR 138 117 ?   ?   ?   C . n 
C 2 139 ILE 139 118 ?   ?   ?   C . n 
C 2 140 ASN 140 119 ?   ?   ?   C . n 
C 2 141 GLU 141 120 ?   ?   ?   C . n 
C 2 142 VAL 142 121 ?   ?   ?   C . n 
C 2 143 PHE 143 122 ?   ?   ?   C . n 
C 2 144 GLU 144 123 ?   ?   ?   C . n 
C 2 145 TRP 145 124 ?   ?   ?   C . n 
C 2 146 VAL 146 125 ?   ?   ?   C . n 
C 2 147 LYS 147 126 ?   ?   ?   C . n 
C 2 148 GLN 148 127 ?   ?   ?   C . n 
C 2 149 ASN 149 128 ?   ?   ?   C . n 
C 2 150 LYS 150 129 ?   ?   ?   C . n 
C 2 151 TYR 151 130 ?   ?   ?   C . n 
C 2 152 LEU 152 131 ?   ?   ?   C . n 
C 2 153 GLN 153 132 ?   ?   ?   C . n 
C 2 154 LYS 154 133 ?   ?   ?   C . n 
C 2 155 LYS 155 134 ?   ?   ?   C . n 
C 2 156 ALA 156 135 ?   ?   ?   C . n 
C 2 157 GLN 157 136 ?   ?   ?   C . n 
C 2 158 MET 158 137 ?   ?   ?   C . n 
C 2 159 ILE 159 138 ?   ?   ?   C . n 
C 2 160 VAL 160 139 ?   ?   ?   C . n 
C 2 161 GLY 161 140 ?   ?   ?   C . n 
C 2 162 LEU 162 141 ?   ?   ?   C . n 
C 2 163 TYR 163 142 ?   ?   ?   C . n 
C 2 164 LYS 164 143 ?   ?   ?   C . n 
C 2 165 ALA 165 144 ?   ?   ?   C . n 
C 2 166 ILE 166 145 ?   ?   ?   C . n 
C 2 167 GLN 167 146 ?   ?   ?   C . n 
C 2 168 LYS 168 147 ?   ?   ?   C . n 
C 2 169 ASP 169 148 ?   ?   ?   C . n 
C 2 170 ASP 170 149 ?   ?   ?   C . n 
C 2 171 GLU 171 150 ?   ?   ?   C . n 
C 2 172 ILE 172 151 ?   ?   ?   C . n 
C 2 173 SER 173 152 ?   ?   ?   C . n 
C 2 174 LEU 174 153 ?   ?   ?   C . n 
C 2 175 PHE 175 154 ?   ?   ?   C . n 
C 2 176 LYS 176 155 ?   ?   ?   C . n 
C 2 177 ALA 177 156 ?   ?   ?   C . n 
C 2 178 MET 178 157 ?   ?   ?   C . n 
C 2 179 VAL 179 158 ?   ?   ?   C . n 
C 2 180 ALA 180 159 ?   ?   ?   C . n 
C 2 181 SER 181 160 ?   ?   ?   C . n 
C 2 182 VAL 182 161 ?   ?   ?   C . n 
C 2 183 TYR 183 162 ?   ?   ?   C . n 
C 2 184 LEU 184 163 ?   ?   ?   C . n 
C 2 185 GLU 185 164 ?   ?   ?   C . n 
C 2 186 SER 186 165 ?   ?   ?   C . n 
C 2 187 PHE 187 166 ?   ?   ?   C . n 
C 2 188 LEU 188 167 ?   ?   ?   C . n 
C 2 189 PHE 189 168 ?   ?   ?   C . n 
C 2 190 TYR 190 169 ?   ?   ?   C . n 
C 2 191 SER 191 170 ?   ?   ?   C . n 
C 2 192 GLY 192 171 ?   ?   ?   C . n 
C 2 193 PHE 193 172 ?   ?   ?   C . n 
C 2 194 TYR 194 173 ?   ?   ?   C . n 
C 2 195 TYR 195 174 ?   ?   ?   C . n 
C 2 196 PRO 196 175 ?   ?   ?   C . n 
C 2 197 LEU 197 176 ?   ?   ?   C . n 
C 2 198 TYR 198 177 ?   ?   ?   C . n 
C 2 199 PHE 199 178 ?   ?   ?   C . n 
C 2 200 TYR 200 179 ?   ?   ?   C . n 
C 2 201 GLY 201 180 ?   ?   ?   C . n 
C 2 202 GLN 202 181 ?   ?   ?   C . n 
C 2 203 GLY 203 182 ?   ?   ?   C . n 
C 2 204 LYS 204 183 ?   ?   ?   C . n 
C 2 205 LEU 205 184 ?   ?   ?   C . n 
C 2 206 MET 206 185 ?   ?   ?   C . n 
C 2 207 GLN 207 186 ?   ?   ?   C . n 
C 2 208 SER 208 187 ?   ?   ?   C . n 
C 2 209 GLY 209 188 ?   ?   ?   C . n 
C 2 210 GLU 210 189 ?   ?   ?   C . n 
C 2 211 ILE 211 190 ?   ?   ?   C . n 
C 2 212 ILE 212 191 ?   ?   ?   C . n 
C 2 213 ASN 213 192 ?   ?   ?   C . n 
C 2 214 LEU 214 193 ?   ?   ?   C . n 
C 2 215 ILE 215 194 ?   ?   ?   C . n 
C 2 216 LEU 216 195 ?   ?   ?   C . n 
C 2 217 ARG 217 196 ?   ?   ?   C . n 
C 2 218 ASP 218 197 ?   ?   ?   C . n 
C 2 219 GLU 219 198 ?   ?   ?   C . n 
C 2 220 ALA 220 199 ?   ?   ?   C . n 
C 2 221 ILE 221 200 ?   ?   ?   C . n 
C 2 222 HIS 222 201 ?   ?   ?   C . n 
C 2 223 GLY 223 202 ?   ?   ?   C . n 
C 2 224 VAL 224 203 ?   ?   ?   C . n 
C 2 225 TYR 225 204 ?   ?   ?   C . n 
C 2 226 VAL 226 205 ?   ?   ?   C . n 
C 2 227 GLY 227 206 ?   ?   ?   C . n 
C 2 228 LEU 228 207 ?   ?   ?   C . n 
C 2 229 LEU 229 208 ?   ?   ?   C . n 
C 2 230 ALA 230 209 ?   ?   ?   C . n 
C 2 231 GLN 231 210 ?   ?   ?   C . n 
C 2 232 GLU 232 211 ?   ?   ?   C . n 
C 2 233 ILE 233 212 ?   ?   ?   C . n 
C 2 234 TYR 234 213 ?   ?   ?   C . n 
C 2 235 ASN 235 214 ?   ?   ?   C . n 
C 2 236 LYS 236 215 ?   ?   ?   C . n 
C 2 237 GLN 237 216 ?   ?   ?   C . n 
C 2 238 THR 238 217 ?   ?   ?   C . n 
C 2 239 GLU 239 218 ?   ?   ?   C . n 
C 2 240 GLU 240 219 ?   ?   ?   C . n 
C 2 241 LYS 241 220 ?   ?   ?   C . n 
C 2 242 LYS 242 221 ?   ?   ?   C . n 
C 2 243 ALA 243 222 ?   ?   ?   C . n 
C 2 244 GLU 244 223 ?   ?   ?   C . n 
C 2 245 LEU 245 224 ?   ?   ?   C . n 
C 2 246 ARG 246 225 ?   ?   ?   C . n 
C 2 247 GLU 247 226 ?   ?   ?   C . n 
C 2 248 PHE 248 227 ?   ?   ?   C . n 
C 2 249 ALA 249 228 ?   ?   ?   C . n 
C 2 250 ILE 250 229 ?   ?   ?   C . n 
C 2 251 ASP 251 230 ?   ?   ?   C . n 
C 2 252 LEU 252 231 ?   ?   ?   C . n 
C 2 253 LEU 253 232 ?   ?   ?   C . n 
C 2 254 ASN 254 233 ?   ?   ?   C . n 
C 2 255 GLN 255 234 ?   ?   ?   C . n 
C 2 256 LEU 256 235 ?   ?   ?   C . n 
C 2 257 TYR 257 236 ?   ?   ?   C . n 
C 2 258 GLU 258 237 ?   ?   ?   C . n 
C 2 259 ASN 259 238 ?   ?   ?   C . n 
C 2 260 GLU 260 239 ?   ?   ?   C . n 
C 2 261 LEU 261 240 ?   ?   ?   C . n 
C 2 262 GLU 262 241 ?   ?   ?   C . n 
C 2 263 TYR 263 242 ?   ?   ?   C . n 
C 2 264 THR 264 243 ?   ?   ?   C . n 
C 2 265 GLU 265 244 ?   ?   ?   C . n 
C 2 266 ASP 266 245 ?   ?   ?   C . n 
C 2 267 LEU 267 246 ?   ?   ?   C . n 
C 2 268 TYR 268 247 ?   ?   ?   C . n 
C 2 269 ASP 269 248 ?   ?   ?   C . n 
C 2 270 GLN 270 249 ?   ?   ?   C . n 
C 2 271 VAL 271 250 ?   ?   ?   C . n 
C 2 272 GLY 272 251 ?   ?   ?   C . n 
C 2 273 LEU 273 252 ?   ?   ?   C . n 
C 2 274 SER 274 253 ?   ?   ?   C . n 
C 2 275 HIS 275 254 ?   ?   ?   C . n 
C 2 276 ASP 276 255 ?   ?   ?   C . n 
C 2 277 VAL 277 256 ?   ?   ?   C . n 
C 2 278 LYS 278 257 ?   ?   ?   C . n 
C 2 279 LYS 279 258 ?   ?   ?   C . n 
C 2 280 PHE 280 259 ?   ?   ?   C . n 
C 2 281 ILE 281 260 ?   ?   ?   C . n 
C 2 282 ARG 282 261 ?   ?   ?   C . n 
C 2 283 TYR 283 262 ?   ?   ?   C . n 
C 2 284 ASN 284 263 ?   ?   ?   C . n 
C 2 285 ALA 285 264 ?   ?   ?   C . n 
C 2 286 ASN 286 265 ?   ?   ?   C . n 
C 2 287 LYS 287 266 ?   ?   ?   C . n 
C 2 288 ALA 288 267 ?   ?   ?   C . n 
C 2 289 LEU 289 268 ?   ?   ?   C . n 
C 2 290 MET 290 269 ?   ?   ?   C . n 
C 2 291 ASN 291 270 ?   ?   ?   C . n 
C 2 292 LEU 292 271 ?   ?   ?   C . n 
C 2 293 GLY 293 272 ?   ?   ?   C . n 
C 2 294 PHE 294 273 ?   ?   ?   C . n 
C 2 295 ASP 295 274 ?   ?   ?   C . n 
C 2 296 PRO 296 275 ?   ?   ?   C . n 
C 2 297 TYR 297 276 ?   ?   ?   C . n 
C 2 298 PHE 298 277 ?   ?   ?   C . n 
C 2 299 GLU 299 278 ?   ?   ?   C . n 
C 2 300 GLU 300 279 ?   ?   ?   C . n 
C 2 301 GLU 301 280 ?   ?   ?   C . n 
C 2 302 ASP 302 281 ?   ?   ?   C . n 
C 2 303 ILE 303 282 ?   ?   ?   C . n 
C 2 304 ASN 304 283 ?   ?   ?   C . n 
C 2 305 PRO 305 284 ?   ?   ?   C . n 
C 2 306 ILE 306 285 ?   ?   ?   C . n 
C 2 307 VAL 307 286 ?   ?   ?   C . n 
C 2 308 LEU 308 287 ?   ?   ?   C . n 
C 2 309 ASN 309 288 ?   ?   ?   C . n 
C 2 310 GLY 310 289 ?   ?   ?   C . n 
C 2 311 LEU 311 290 ?   ?   ?   C . n 
C 2 312 ASN 312 291 ?   ?   ?   C . n 
C 2 313 THR 313 292 ?   ?   ?   C . n 
C 2 314 LYS 314 293 ?   ?   ?   C . n 
C 2 315 THR 315 294 ?   ?   ?   C . n 
C 2 316 LYS 316 295 ?   ?   ?   C . n 
C 2 317 SER 317 296 ?   ?   ?   C . n 
C 2 318 HIS 318 297 ?   ?   ?   C . n 
C 2 319 ASP 319 298 ?   ?   ?   C . n 
C 2 320 PHE 320 299 ?   ?   ?   C . n 
C 2 321 PHE 321 300 ?   ?   ?   C . n 
C 2 322 SER 322 301 ?   ?   ?   C . n 
C 2 323 MET 323 302 ?   ?   ?   C . n 
C 2 324 LYS 324 303 ?   ?   ?   C . n 
C 2 325 GLY 325 304 ?   ?   ?   C . n 
C 2 326 ASN 326 305 ?   ?   ?   C . n 
C 2 327 GLY 327 306 ?   ?   ?   C . n 
C 2 328 TYR 328 307 ?   ?   ?   C . n 
C 2 329 LYS 329 308 ?   ?   ?   C . n 
C 2 330 LYS 330 309 ?   ?   ?   C . n 
C 2 331 ALA 331 310 ?   ?   ?   C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  ?   ?   ?   D . n 
D 2 38  PHE 38  17  ?   ?   ?   D . n 
D 2 39  THR 39  18  ?   ?   ?   D . n 
D 2 40  GLN 40  19  ?   ?   ?   D . n 
D 2 41  MET 41  20  ?   ?   ?   D . n 
D 2 42  PHE 42  21  ?   ?   ?   D . n 
D 2 43  TYR 43  22  ?   ?   ?   D . n 
D 2 44  ASN 44  23  ?   ?   ?   D . n 
D 2 45  GLN 45  24  ?   ?   ?   D . n 
D 2 46  ASN 46  25  ?   ?   ?   D . n 
D 2 47  VAL 47  26  ?   ?   ?   D . n 
D 2 48  LYS 48  27  ?   ?   ?   D . n 
D 2 49  GLN 49  28  ?   ?   ?   D . n 
D 2 50  PHE 50  29  ?   ?   ?   D . n 
D 2 51  TRP 51  30  ?   ?   ?   D . n 
D 2 52  LEU 52  31  ?   ?   ?   D . n 
D 2 53  PRO 53  32  ?   ?   ?   D . n 
D 2 54  GLU 54  33  ?   ?   ?   D . n 
D 2 55  GLU 55  34  ?   ?   ?   D . n 
D 2 56  ILE 56  35  ?   ?   ?   D . n 
D 2 57  ALA 57  36  ?   ?   ?   D . n 
D 2 58  LEU 58  37  ?   ?   ?   D . n 
D 2 59  ASN 59  38  ?   ?   ?   D . n 
D 2 60  GLY 60  39  ?   ?   ?   D . n 
D 2 61  ASP 61  40  ?   ?   ?   D . n 
D 2 62  LEU 62  41  ?   ?   ?   D . n 
D 2 63  LEU 63  42  ?   ?   ?   D . n 
D 2 64  THR 64  43  ?   ?   ?   D . n 
D 2 65  TRP 65  44  ?   ?   ?   D . n 
D 2 66  LYS 66  45  ?   ?   ?   D . n 
D 2 67  TYR 67  46  ?   ?   ?   D . n 
D 2 68  LEU 68  47  ?   ?   ?   D . n 
D 2 69  GLY 69  48  ?   ?   ?   D . n 
D 2 70  LYS 70  49  ?   ?   ?   D . n 
D 2 71  ASN 71  50  ?   ?   ?   D . n 
D 2 72  GLU 72  51  ?   ?   ?   D . n 
D 2 73  GLN 73  52  ?   ?   ?   D . n 
D 2 74  ASP 74  53  ?   ?   ?   D . n 
D 2 75  THR 75  54  ?   ?   ?   D . n 
D 2 76  TYR 76  55  ?   ?   ?   D . n 
D 2 77  MET 77  56  ?   ?   ?   D . n 
D 2 78  LYS 78  57  ?   ?   ?   D . n 
D 2 79  VAL 79  58  ?   ?   ?   D . n 
D 2 80  LEU 80  59  ?   ?   ?   D . n 
D 2 81  ALA 81  60  ?   ?   ?   D . n 
D 2 82  GLY 82  61  ?   ?   ?   D . n 
D 2 83  LEU 83  62  ?   ?   ?   D . n 
D 2 84  THR 84  63  ?   ?   ?   D . n 
D 2 85  LEU 85  64  ?   ?   ?   D . n 
D 2 86  LEU 86  65  ?   ?   ?   D . n 
D 2 87  ASP 87  66  ?   ?   ?   D . n 
D 2 88  THR 88  67  ?   ?   ?   D . n 
D 2 89  GLU 89  68  ?   ?   ?   D . n 
D 2 90  GLN 90  69  ?   ?   ?   D . n 
D 2 91  GLY 91  70  ?   ?   ?   D . n 
D 2 92  ASN 92  71  ?   ?   ?   D . n 
D 2 93  THR 93  72  ?   ?   ?   D . n 
D 2 94  GLY 94  73  ?   ?   ?   D . n 
D 2 95  MET 95  74  ?   ?   ?   D . n 
D 2 96  PRO 96  75  ?   ?   ?   D . n 
D 2 97  ILE 97  76  ?   ?   ?   D . n 
D 2 98  VAL 98  77  ?   ?   ?   D . n 
D 2 99  ALA 99  78  ?   ?   ?   D . n 
D 2 100 GLU 100 79  ?   ?   ?   D . n 
D 2 101 HIS 101 80  ?   ?   ?   D . n 
D 2 102 VAL 102 81  ?   ?   ?   D . n 
D 2 103 ASP 103 82  ?   ?   ?   D . n 
D 2 104 GLY 104 83  ?   ?   ?   D . n 
D 2 105 HIS 105 84  ?   ?   ?   D . n 
D 2 106 GLN 106 85  ?   ?   ?   D . n 
D 2 107 ARG 107 86  ?   ?   ?   D . n 
D 2 108 LYS 108 87  ?   ?   ?   D . n 
D 2 109 ALA 109 88  ?   ?   ?   D . n 
D 2 110 VAL 110 89  ?   ?   ?   D . n 
D 2 111 LEU 111 90  ?   ?   ?   D . n 
D 2 112 ASN 112 91  ?   ?   ?   D . n 
D 2 113 PHE 113 92  ?   ?   ?   D . n 
D 2 114 MET 114 93  ?   ?   ?   D . n 
D 2 115 ALA 115 94  ?   ?   ?   D . n 
D 2 116 MET 116 95  ?   ?   ?   D . n 
D 2 117 MET 117 96  ?   ?   ?   D . n 
D 2 118 GLU 118 97  ?   ?   ?   D . n 
D 2 119 ASN 119 98  ?   ?   ?   D . n 
D 2 120 ALA 120 99  ?   ?   ?   D . n 
D 2 121 VAL 121 100 ?   ?   ?   D . n 
D 2 122 HIS 122 101 ?   ?   ?   D . n 
D 2 123 ALA 123 102 ?   ?   ?   D . n 
D 2 124 LYS 124 103 ?   ?   ?   D . n 
D 2 125 SER 125 104 ?   ?   ?   D . n 
D 2 126 TYR 126 105 ?   ?   ?   D . n 
D 2 127 SER 127 106 ?   ?   ?   D . n 
D 2 128 ASN 128 107 ?   ?   ?   D . n 
D 2 129 ILE 129 108 ?   ?   ?   D . n 
D 2 130 PHE 130 109 ?   ?   ?   D . n 
D 2 131 MET 131 110 ?   ?   ?   D . n 
D 2 132 THR 132 111 ?   ?   ?   D . n 
D 2 133 LEU 133 112 ?   ?   ?   D . n 
D 2 134 ALA 134 113 ?   ?   ?   D . n 
D 2 135 PRO 135 114 ?   ?   ?   D . n 
D 2 136 THR 136 115 ?   ?   ?   D . n 
D 2 137 GLU 137 116 ?   ?   ?   D . n 
D 2 138 THR 138 117 ?   ?   ?   D . n 
D 2 139 ILE 139 118 ?   ?   ?   D . n 
D 2 140 ASN 140 119 ?   ?   ?   D . n 
D 2 141 GLU 141 120 ?   ?   ?   D . n 
D 2 142 VAL 142 121 ?   ?   ?   D . n 
D 2 143 PHE 143 122 ?   ?   ?   D . n 
D 2 144 GLU 144 123 ?   ?   ?   D . n 
D 2 145 TRP 145 124 ?   ?   ?   D . n 
D 2 146 VAL 146 125 ?   ?   ?   D . n 
D 2 147 LYS 147 126 ?   ?   ?   D . n 
D 2 148 GLN 148 127 ?   ?   ?   D . n 
D 2 149 ASN 149 128 ?   ?   ?   D . n 
D 2 150 LYS 150 129 ?   ?   ?   D . n 
D 2 151 TYR 151 130 ?   ?   ?   D . n 
D 2 152 LEU 152 131 ?   ?   ?   D . n 
D 2 153 GLN 153 132 ?   ?   ?   D . n 
D 2 154 LYS 154 133 ?   ?   ?   D . n 
D 2 155 LYS 155 134 ?   ?   ?   D . n 
D 2 156 ALA 156 135 ?   ?   ?   D . n 
D 2 157 GLN 157 136 ?   ?   ?   D . n 
D 2 158 MET 158 137 ?   ?   ?   D . n 
D 2 159 ILE 159 138 ?   ?   ?   D . n 
D 2 160 VAL 160 139 ?   ?   ?   D . n 
D 2 161 GLY 161 140 ?   ?   ?   D . n 
D 2 162 LEU 162 141 ?   ?   ?   D . n 
D 2 163 TYR 163 142 ?   ?   ?   D . n 
D 2 164 LYS 164 143 ?   ?   ?   D . n 
D 2 165 ALA 165 144 ?   ?   ?   D . n 
D 2 166 ILE 166 145 ?   ?   ?   D . n 
D 2 167 GLN 167 146 ?   ?   ?   D . n 
D 2 168 LYS 168 147 ?   ?   ?   D . n 
D 2 169 ASP 169 148 ?   ?   ?   D . n 
D 2 170 ASP 170 149 ?   ?   ?   D . n 
D 2 171 GLU 171 150 ?   ?   ?   D . n 
D 2 172 ILE 172 151 ?   ?   ?   D . n 
D 2 173 SER 173 152 ?   ?   ?   D . n 
D 2 174 LEU 174 153 ?   ?   ?   D . n 
D 2 175 PHE 175 154 ?   ?   ?   D . n 
D 2 176 LYS 176 155 ?   ?   ?   D . n 
D 2 177 ALA 177 156 ?   ?   ?   D . n 
D 2 178 MET 178 157 ?   ?   ?   D . n 
D 2 179 VAL 179 158 ?   ?   ?   D . n 
D 2 180 ALA 180 159 ?   ?   ?   D . n 
D 2 181 SER 181 160 ?   ?   ?   D . n 
D 2 182 VAL 182 161 ?   ?   ?   D . n 
D 2 183 TYR 183 162 ?   ?   ?   D . n 
D 2 184 LEU 184 163 ?   ?   ?   D . n 
D 2 185 GLU 185 164 ?   ?   ?   D . n 
D 2 186 SER 186 165 ?   ?   ?   D . n 
D 2 187 PHE 187 166 ?   ?   ?   D . n 
D 2 188 LEU 188 167 ?   ?   ?   D . n 
D 2 189 PHE 189 168 ?   ?   ?   D . n 
D 2 190 TYR 190 169 ?   ?   ?   D . n 
D 2 191 SER 191 170 ?   ?   ?   D . n 
D 2 192 GLY 192 171 ?   ?   ?   D . n 
D 2 193 PHE 193 172 ?   ?   ?   D . n 
D 2 194 TYR 194 173 ?   ?   ?   D . n 
D 2 195 TYR 195 174 ?   ?   ?   D . n 
D 2 196 PRO 196 175 ?   ?   ?   D . n 
D 2 197 LEU 197 176 ?   ?   ?   D . n 
D 2 198 TYR 198 177 ?   ?   ?   D . n 
D 2 199 PHE 199 178 ?   ?   ?   D . n 
D 2 200 TYR 200 179 ?   ?   ?   D . n 
D 2 201 GLY 201 180 ?   ?   ?   D . n 
D 2 202 GLN 202 181 ?   ?   ?   D . n 
D 2 203 GLY 203 182 ?   ?   ?   D . n 
D 2 204 LYS 204 183 ?   ?   ?   D . n 
D 2 205 LEU 205 184 ?   ?   ?   D . n 
D 2 206 MET 206 185 ?   ?   ?   D . n 
D 2 207 GLN 207 186 ?   ?   ?   D . n 
D 2 208 SER 208 187 ?   ?   ?   D . n 
D 2 209 GLY 209 188 ?   ?   ?   D . n 
D 2 210 GLU 210 189 ?   ?   ?   D . n 
D 2 211 ILE 211 190 ?   ?   ?   D . n 
D 2 212 ILE 212 191 ?   ?   ?   D . n 
D 2 213 ASN 213 192 ?   ?   ?   D . n 
D 2 214 LEU 214 193 ?   ?   ?   D . n 
D 2 215 ILE 215 194 ?   ?   ?   D . n 
D 2 216 LEU 216 195 ?   ?   ?   D . n 
D 2 217 ARG 217 196 ?   ?   ?   D . n 
D 2 218 ASP 218 197 ?   ?   ?   D . n 
D 2 219 GLU 219 198 ?   ?   ?   D . n 
D 2 220 ALA 220 199 ?   ?   ?   D . n 
D 2 221 ILE 221 200 ?   ?   ?   D . n 
D 2 222 HIS 222 201 ?   ?   ?   D . n 
D 2 223 GLY 223 202 ?   ?   ?   D . n 
D 2 224 VAL 224 203 ?   ?   ?   D . n 
D 2 225 TYR 225 204 ?   ?   ?   D . n 
D 2 226 VAL 226 205 ?   ?   ?   D . n 
D 2 227 GLY 227 206 ?   ?   ?   D . n 
D 2 228 LEU 228 207 ?   ?   ?   D . n 
D 2 229 LEU 229 208 ?   ?   ?   D . n 
D 2 230 ALA 230 209 ?   ?   ?   D . n 
D 2 231 GLN 231 210 ?   ?   ?   D . n 
D 2 232 GLU 232 211 ?   ?   ?   D . n 
D 2 233 ILE 233 212 ?   ?   ?   D . n 
D 2 234 TYR 234 213 ?   ?   ?   D . n 
D 2 235 ASN 235 214 ?   ?   ?   D . n 
D 2 236 LYS 236 215 ?   ?   ?   D . n 
D 2 237 GLN 237 216 ?   ?   ?   D . n 
D 2 238 THR 238 217 ?   ?   ?   D . n 
D 2 239 GLU 239 218 ?   ?   ?   D . n 
D 2 240 GLU 240 219 ?   ?   ?   D . n 
D 2 241 LYS 241 220 ?   ?   ?   D . n 
D 2 242 LYS 242 221 ?   ?   ?   D . n 
D 2 243 ALA 243 222 ?   ?   ?   D . n 
D 2 244 GLU 244 223 ?   ?   ?   D . n 
D 2 245 LEU 245 224 ?   ?   ?   D . n 
D 2 246 ARG 246 225 ?   ?   ?   D . n 
D 2 247 GLU 247 226 ?   ?   ?   D . n 
D 2 248 PHE 248 227 ?   ?   ?   D . n 
D 2 249 ALA 249 228 ?   ?   ?   D . n 
D 2 250 ILE 250 229 ?   ?   ?   D . n 
D 2 251 ASP 251 230 ?   ?   ?   D . n 
D 2 252 LEU 252 231 ?   ?   ?   D . n 
D 2 253 LEU 253 232 ?   ?   ?   D . n 
D 2 254 ASN 254 233 ?   ?   ?   D . n 
D 2 255 GLN 255 234 ?   ?   ?   D . n 
D 2 256 LEU 256 235 ?   ?   ?   D . n 
D 2 257 TYR 257 236 ?   ?   ?   D . n 
D 2 258 GLU 258 237 ?   ?   ?   D . n 
D 2 259 ASN 259 238 ?   ?   ?   D . n 
D 2 260 GLU 260 239 ?   ?   ?   D . n 
D 2 261 LEU 261 240 ?   ?   ?   D . n 
D 2 262 GLU 262 241 ?   ?   ?   D . n 
D 2 263 TYR 263 242 ?   ?   ?   D . n 
D 2 264 THR 264 243 ?   ?   ?   D . n 
D 2 265 GLU 265 244 ?   ?   ?   D . n 
D 2 266 ASP 266 245 ?   ?   ?   D . n 
D 2 267 LEU 267 246 ?   ?   ?   D . n 
D 2 268 TYR 268 247 ?   ?   ?   D . n 
D 2 269 ASP 269 248 ?   ?   ?   D . n 
D 2 270 GLN 270 249 ?   ?   ?   D . n 
D 2 271 VAL 271 250 ?   ?   ?   D . n 
D 2 272 GLY 272 251 ?   ?   ?   D . n 
D 2 273 LEU 273 252 ?   ?   ?   D . n 
D 2 274 SER 274 253 ?   ?   ?   D . n 
D 2 275 HIS 275 254 ?   ?   ?   D . n 
D 2 276 ASP 276 255 ?   ?   ?   D . n 
D 2 277 VAL 277 256 ?   ?   ?   D . n 
D 2 278 LYS 278 257 ?   ?   ?   D . n 
D 2 279 LYS 279 258 ?   ?   ?   D . n 
D 2 280 PHE 280 259 ?   ?   ?   D . n 
D 2 281 ILE 281 260 ?   ?   ?   D . n 
D 2 282 ARG 282 261 ?   ?   ?   D . n 
D 2 283 TYR 283 262 ?   ?   ?   D . n 
D 2 284 ASN 284 263 ?   ?   ?   D . n 
D 2 285 ALA 285 264 ?   ?   ?   D . n 
D 2 286 ASN 286 265 ?   ?   ?   D . n 
D 2 287 LYS 287 266 ?   ?   ?   D . n 
D 2 288 ALA 288 267 ?   ?   ?   D . n 
D 2 289 LEU 289 268 ?   ?   ?   D . n 
D 2 290 MET 290 269 ?   ?   ?   D . n 
D 2 291 ASN 291 270 ?   ?   ?   D . n 
D 2 292 LEU 292 271 ?   ?   ?   D . n 
D 2 293 GLY 293 272 ?   ?   ?   D . n 
D 2 294 PHE 294 273 ?   ?   ?   D . n 
D 2 295 ASP 295 274 ?   ?   ?   D . n 
D 2 296 PRO 296 275 ?   ?   ?   D . n 
D 2 297 TYR 297 276 ?   ?   ?   D . n 
D 2 298 PHE 298 277 ?   ?   ?   D . n 
D 2 299 GLU 299 278 ?   ?   ?   D . n 
D 2 300 GLU 300 279 ?   ?   ?   D . n 
D 2 301 GLU 301 280 ?   ?   ?   D . n 
D 2 302 ASP 302 281 ?   ?   ?   D . n 
D 2 303 ILE 303 282 ?   ?   ?   D . n 
D 2 304 ASN 304 283 ?   ?   ?   D . n 
D 2 305 PRO 305 284 ?   ?   ?   D . n 
D 2 306 ILE 306 285 ?   ?   ?   D . n 
D 2 307 VAL 307 286 ?   ?   ?   D . n 
D 2 308 LEU 308 287 ?   ?   ?   D . n 
D 2 309 ASN 309 288 ?   ?   ?   D . n 
D 2 310 GLY 310 289 ?   ?   ?   D . n 
D 2 311 LEU 311 290 ?   ?   ?   D . n 
D 2 312 ASN 312 291 ?   ?   ?   D . n 
D 2 313 THR 313 292 ?   ?   ?   D . n 
D 2 314 LYS 314 293 ?   ?   ?   D . n 
D 2 315 THR 315 294 ?   ?   ?   D . n 
D 2 316 LYS 316 295 ?   ?   ?   D . n 
D 2 317 SER 317 296 ?   ?   ?   D . n 
D 2 318 HIS 318 297 ?   ?   ?   D . n 
D 2 319 ASP 319 298 ?   ?   ?   D . n 
D 2 320 PHE 320 299 ?   ?   ?   D . n 
D 2 321 PHE 321 300 ?   ?   ?   D . n 
D 2 322 SER 322 301 ?   ?   ?   D . n 
D 2 323 MET 323 302 ?   ?   ?   D . n 
D 2 324 LYS 324 303 ?   ?   ?   D . n 
D 2 325 GLY 325 304 ?   ?   ?   D . n 
D 2 326 ASN 326 305 ?   ?   ?   D . n 
D 2 327 GLY 327 306 ?   ?   ?   D . n 
D 2 328 TYR 328 307 ?   ?   ?   D . n 
D 2 329 LYS 329 308 ?   ?   ?   D . n 
D 2 330 LYS 330 309 ?   ?   ?   D . n 
D 2 331 ALA 331 310 ?   ?   ?   D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
E 3 1   MET 1   1   ?   ?   ?   E . n 
E 3 2   ALA 2   2   ?   ?   ?   E . n 
E 3 3   ILE 3   3   ?   ?   ?   E . n 
E 3 4   VAL 4   4   ?   ?   ?   E . n 
E 3 5   LYS 5   5   ?   ?   ?   E . n 
E 3 6   ALA 6   6   ?   ?   ?   E . n 
E 3 7   THR 7   7   ?   ?   ?   E . n 
E 3 8   ASP 8   8   ?   ?   ?   E . n 
E 3 9   GLN 9   9   ?   ?   ?   E . n 
E 3 10  SER 10  10  ?   ?   ?   E . n 
E 3 11  PHE 11  11  ?   ?   ?   E . n 
E 3 12  SER 12  12  ?   ?   ?   E . n 
E 3 13  ALA 13  13  ?   ?   ?   E . n 
E 3 14  GLU 14  14  ?   ?   ?   E . n 
E 3 15  THR 15  15  ?   ?   ?   E . n 
E 3 16  SER 16  16  ?   ?   ?   E . n 
E 3 17  GLU 17  17  ?   ?   ?   E . n 
E 3 18  GLY 18  18  ?   ?   ?   E . n 
E 3 19  VAL 19  19  19  VAL VAL E . n 
E 3 20  VAL 20  20  20  VAL VAL E . n 
E 3 21  LEU 21  21  21  LEU LEU E . n 
E 3 22  ALA 22  22  22  ALA ALA E . n 
E 3 23  ASP 23  23  23  ASP ASP E . n 
E 3 24  PHE 24  24  24  PHE PHE E . n 
E 3 25  TRP 25  25  25  TRP TRP E . n 
E 3 26  ALA 26  26  26  ALA ALA E . n 
E 3 27  PRO 27  27  27  PRO PRO E . n 
E 3 28  TRP 28  28  28  TRP TRP E . n 
E 3 29  CYS 29  29  29  CYS CYS E . n 
E 3 30  GLY 30  30  30  GLY GLY E . n 
E 3 31  PRO 31  31  31  PRO PRO E . n 
E 3 32  CYS 32  32  32  CYS CYS E . n 
E 3 33  LYS 33  33  33  LYS LYS E . n 
E 3 34  MET 34  34  34  MET MET E . n 
E 3 35  ILE 35  35  35  ILE ILE E . n 
E 3 36  ALA 36  36  36  ALA ALA E . n 
E 3 37  PRO 37  37  37  PRO PRO E . n 
E 3 38  VAL 38  38  38  VAL VAL E . n 
E 3 39  LEU 39  39  39  LEU LEU E . n 
E 3 40  GLU 40  40  40  GLU GLU E . n 
E 3 41  GLU 41  41  41  GLU GLU E . n 
E 3 42  LEU 42  42  42  LEU LEU E . n 
E 3 43  ASP 43  43  43  ASP ASP E . n 
E 3 44  GLN 44  44  44  GLN GLN E . n 
E 3 45  GLU 45  45  45  GLU GLU E . n 
E 3 46  MET 46  46  46  MET MET E . n 
E 3 47  GLY 47  47  47  GLY GLY E . n 
E 3 48  ASP 48  48  48  ASP ASP E . n 
E 3 49  LYS 49  49  49  LYS LYS E . n 
E 3 50  LEU 50  50  50  LEU LEU E . n 
E 3 51  LYS 51  51  51  LYS LYS E . n 
E 3 52  ILE 52  52  52  ILE ILE E . n 
E 3 53  VAL 53  53  53  VAL VAL E . n 
E 3 54  LYS 54  54  54  LYS LYS E . n 
E 3 55  ILE 55  55  55  ILE ILE E . n 
E 3 56  ASP 56  56  56  ASP ASP E . n 
E 3 57  VAL 57  57  57  VAL VAL E . n 
E 3 58  ASP 58  58  58  ASP ASP E . n 
E 3 59  GLU 59  59  59  GLU GLU E . n 
E 3 60  ASN 60  60  60  ASN ASN E . n 
E 3 61  GLN 61  61  61  GLN GLN E . n 
E 3 62  GLU 62  62  62  GLU GLU E . n 
E 3 63  THR 63  63  63  THR THR E . n 
E 3 64  ALA 64  64  64  ALA ALA E . n 
E 3 65  GLY 65  65  65  GLY GLY E . n 
E 3 66  LYS 66  66  66  LYS LYS E . n 
E 3 67  TYR 67  67  67  TYR TYR E . n 
E 3 68  GLY 68  68  68  GLY GLY E . n 
E 3 69  VAL 69  69  69  VAL VAL E . n 
E 3 70  MET 70  70  70  MET MET E . n 
E 3 71  SER 71  71  71  SER SER E . n 
E 3 72  ILE 72  72  72  ILE ILE E . n 
E 3 73  PRO 73  73  73  PRO PRO E . n 
E 3 74  THR 74  74  74  THR THR E . n 
E 3 75  LEU 75  75  75  LEU LEU E . n 
E 3 76  LEU 76  76  76  LEU LEU E . n 
E 3 77  VAL 77  77  77  VAL VAL E . n 
E 3 78  LEU 78  78  78  LEU LEU E . n 
E 3 79  LYS 79  79  79  LYS LYS E . n 
E 3 80  ASP 80  80  80  ASP ASP E . n 
E 3 81  GLY 81  81  81  GLY GLY E . n 
E 3 82  GLU 82  82  82  GLU GLU E . n 
E 3 83  VAL 83  83  83  VAL VAL E . n 
E 3 84  VAL 84  84  84  VAL VAL E . n 
E 3 85  GLU 85  85  85  GLU GLU E . n 
E 3 86  THR 86  86  86  THR THR E . n 
E 3 87  SER 87  87  87  SER SER E . n 
E 3 88  VAL 88  88  88  VAL VAL E . n 
E 3 89  GLY 89  89  89  GLY GLY E . n 
E 3 90  PHE 90  90  90  PHE PHE E . n 
E 3 91  LYS 91  91  91  LYS LYS E . n 
E 3 92  PRO 92  92  92  PRO PRO E . n 
E 3 93  LYS 93  93  93  LYS LYS E . n 
E 3 94  GLU 94  94  94  GLU GLU E . n 
E 3 95  ALA 95  95  95  ALA ALA E . n 
E 3 96  LEU 96  96  96  LEU LEU E . n 
E 3 97  GLN 97  97  97  GLN GLN E . n 
E 3 98  GLU 98  98  98  GLU GLU E . n 
E 3 99  LEU 99  99  99  LEU LEU E . n 
E 3 100 VAL 100 100 100 VAL VAL E . n 
E 3 101 ASN 101 101 101 ASN ASN E . n 
E 3 102 LYS 102 102 102 LYS LYS E . n 
E 3 103 HIS 103 103 103 HIS HIS E . n 
E 3 104 LEU 104 104 104 LEU LEU E . 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 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 TTP ? ? TTP ? ? '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 
F 4 TTP 1 801 801 TTP TTP A . 
G 5 MG  1 802 802 MG  MG  A . 
H 6 ATP 1 803 803 ATP ATP A . 
I 7 GDP 1 804 804 GDP GDP A . 
J 5 MG  1 801 801 MG  MG  B . 
K 4 TTP 1 802 802 TTP TTP B . 
L 6 ATP 1 803 803 ATP ATP B . 
M 7 GDP 1 804 804 GDP GDP B . 
# 
_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                   9BXT 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BXT 
_struct.title                        
'TrxA focus-classified model for pre-reduction condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BXT 
_struct_keywords.text            'Ribonucleotide Reductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 5 ? 
K N N 4 ? 
L N N 6 ? 
M N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RIR1_BACSU P50620 ? 1 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
1 
2 UNP RIR2_BACSU P50621 ? 2 
;MTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVLAGLTLLDTEQGNTGMPIVAEH
VDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIVGLYKAIQKDDEISLFKAMVAS
VYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEEKKAELREFAIDLLNQLYENEL
EYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDFFSMKGNGYKKATVEPLKDDDF
YFEDEKEQI
;
1 
3 UNP THIO_BACSU P14949 ? 3 
;MAIVKATDQSFSAETSEGVVLADFWAPWCGPCKMIAPVLEELDQEMGDKLKIVKIDVDENQETAGKYGVMSIPTLLVLKD
GEVVETSVGFKPKEALQELVNKHL
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BXT A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BXT B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BXT C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BXT D 22 ? 350 ? P50621 1 ? 329 ? 1 329 
5 3 9BXT E 1  ? 104 ? P14949 1 ? 104 ? 1 104 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
3 9BXT MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BXT GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BXT SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BXT SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BXT HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BXT HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BXT HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BXT HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BXT HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BXT HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BXT SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BXT SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BXT GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BXT LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BXT VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BXT PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BXT ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BXT GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BXT SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BXT HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BXT MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BXT MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BXT GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BXT SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BXT SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BXT HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BXT HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BXT HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BXT HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BXT HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BXT HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BXT SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BXT SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BXT GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BXT LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BXT VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BXT PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BXT ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BXT GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BXT SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BXT HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BXT MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? ASN A 14  ? PRO A 7   ASN A 14  1 ? 8  
HELX_P HELX_P2  AA2 GLU A 15  ? MET A 17  ? GLU A 15  MET A 17  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 27  ? TYR A 40  ? ASP A 27  TYR A 40  1 ? 14 
HELX_P HELX_P4  AA4 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P5  AA5 GLU A 65  ? LEU A 71  ? GLU A 65  LEU A 71  1 ? 7  
HELX_P HELX_P6  AA6 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P7  AA7 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P8  AA8 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P9  AA9 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P10 AB1 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P11 AB2 SER A 178 ? LYS A 194 ? SER A 178 LYS A 194 1 ? 17 
HELX_P HELX_P12 AB3 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P13 AB4 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P14 AB5 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P15 AB6 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P16 AB7 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P17 AB8 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P18 AB9 ASP A 318 ? ASP A 328 ? ASP A 318 ASP A 328 1 ? 11 
HELX_P HELX_P19 AC1 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P20 AC2 GLN A 361 ? VAL A 367 ? GLN A 361 VAL A 367 1 ? 7  
HELX_P HELX_P21 AC3 ILE A 416 ? HIS A 422 ? ILE A 416 HIS A 422 1 ? 7  
HELX_P HELX_P22 AC4 SER A 424 ? THR A 443 ? SER A 424 THR A 443 1 ? 20 
HELX_P HELX_P23 AC5 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P24 AC6 ASN A 467 ? ASN A 475 ? ASN A 467 ASN A 475 1 ? 9  
HELX_P HELX_P25 AC7 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P26 AC8 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P27 AC9 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P28 AD1 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P29 AD2 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P30 AD3 GLY A 582 ? GLN A 588 ? GLY A 582 GLN A 588 1 ? 7  
HELX_P HELX_P31 AD4 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P32 AD5 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P33 AD6 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P34 AD7 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P35 AD8 ASP B 27  ? TYR B 40  ? ASP B 27  TYR B 40  1 ? 14 
HELX_P HELX_P36 AD9 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P37 AE1 GLU B 65  ? LEU B 71  ? GLU B 65  LEU B 71  1 ? 7  
HELX_P HELX_P38 AE2 SER B 73  ? ALA B 86  ? SER B 73  ALA B 86  1 ? 14 
HELX_P HELX_P39 AE3 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P40 AE4 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P41 AE5 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P42 AE6 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P43 AE7 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P44 AE8 LYS B 221 ? ALA B 237 ? LYS B 221 ALA B 237 1 ? 17 
HELX_P HELX_P45 AE9 ASP B 238 ? GLN B 242 ? ASP B 238 GLN B 242 5 ? 5  
HELX_P HELX_P46 AF1 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P47 AF2 PRO B 285 ? ASP B 295 ? PRO B 285 ASP B 295 1 ? 11 
HELX_P HELX_P48 AF3 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P49 AF4 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 318 ? ASP B 328 ? ASP B 318 ASP B 328 1 ? 11 
HELX_P HELX_P51 AF6 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P52 AF7 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P53 AF8 ILE B 416 ? HIS B 422 ? ILE B 416 HIS B 422 1 ? 7  
HELX_P HELX_P54 AF9 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P55 AG1 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P56 AG2 ASN B 467 ? ASN B 475 ? ASN B 467 ASN B 475 1 ? 9  
HELX_P HELX_P57 AG3 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P58 AG4 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P59 AG5 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P60 AG6 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P61 AG7 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P62 AG8 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P63 AG9 GLU B 628 ? MET B 632 ? GLU B 628 MET B 632 5 ? 5  
HELX_P HELX_P64 AH1 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P65 AH2 THR B 663 ? GLY B 678 ? THR B 663 GLY B 678 1 ? 16 
HELX_P HELX_P66 AH3 LYS C 337 ? PHE C 341 ? LYS C 316 PHE C 320 5 ? 5  
HELX_P HELX_P67 AH4 CYS E 29  ? GLY E 47  ? CYS E 29  GLY E 47  1 ? 19 
HELX_P HELX_P68 AH5 ASN E 60  ? TYR E 67  ? ASN E 60  TYR E 67  1 ? 8  
HELX_P HELX_P69 AH6 PRO E 92  ? LYS E 102 ? PRO E 92  LYS E 102 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 170 SG  ? ? ? 1_555 A CYS 409 SG  ? ? A CYS 170 A CYS 409 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf2 disulf ? ? B CYS 170 SG  ? ? ? 1_555 B CYS 409 SG  ? ? B CYS 170 B CYS 409 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? E CYS 29  SG  ? ? ? 1_555 E CYS 32  SG  ? ? E CYS 29  E CYS 32  1_555 ? ? ? ? ? ? ? 2.661 ? ? 
metalc1 metalc ? ? F TTP .   O2A ? ? ? 1_555 G MG  .   MG  ? ? A TTP 801 A MG  802 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc2 metalc ? ? F TTP .   O1B ? ? ? 1_555 G MG  .   MG  ? ? A TTP 801 A MG  802 1_555 ? ? ? ? ? ? ? 2.914 ? ? 
metalc3 metalc ? ? J MG  .   MG  ? ? ? 1_555 K TTP .   O3G ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc4 metalc ? ? J MG  .   MG  ? ? ? 1_555 K TTP .   O2A ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc5 metalc ? ? J MG  .   MG  ? ? ? 1_555 K TTP .   O1B ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.882 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O2A ? F TTP . ? A TTP 801 ? 1_555 MG ? G MG . ? A MG 802 ? 1_555 O1B ? F TTP . ? A TTP 801 ? 1_555 62.2 ? 
2 O3G ? K TTP . ? B TTP 802 ? 1_555 MG ? J MG . ? B MG 801 ? 1_555 O2A ? K TTP . ? B TTP 802 ? 1_555 92.1 ? 
3 O3G ? K TTP . ? B TTP 802 ? 1_555 MG ? J MG . ? B MG 801 ? 1_555 O1B ? K TTP . ? B TTP 802 ? 1_555 61.2 ? 
4 O2A ? K TTP . ? B TTP 802 ? 1_555 MG ? J MG . ? B MG 801 ? 1_555 O1B ? K TTP . ? B TTP 802 ? 1_555 63.4 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 170 ? CYS A 409 ? CYS A 170 ? 1_555 CYS A 409 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 170 ? CYS B 409 ? CYS B 170 ? 1_555 CYS B 409 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS E 29  ? CYS E 32  ? CYS E 29  ? 1_555 CYS E 32  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 1.78  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 2.55  
3 ILE 72  E . ? ILE 72  E PRO 73  E ? PRO 73  E 1 -5.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 8 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA7 6 7 ? parallel      
AA7 7 8 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 LEU A 411 ? ASN A 415 ? LEU A 411 ASN A 415 
AA1 3 GLY A 462 ? MET A 466 ? GLY A 462 MET A 466 
AA2 1 ILE A 407 ? SER A 408 ? ILE A 407 SER A 408 
AA2 2 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 3 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 4 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 5 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 6 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 7 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LYS A 659 ? THR A 655 LYS A 659 
AA5 2 TYR A 684 ? LYS A 688 ? TYR A 684 LYS A 688 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ILE B 407 ? ASN B 415 ? ILE B 407 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA7 2 ILE B 407 ? ASN B 415 ? ILE B 407 ASN B 415 
AA7 3 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 4 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 5 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 6 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 7 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 8 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? THR B 605 ? ILE B 601 THR B 605 
AA9 2 LYS B 610 ? PRO B 614 ? LYS B 610 PRO B 614 
AB1 1 THR B 655 ? LYS B 659 ? THR B 655 LYS B 659 
AB1 2 TYR B 684 ? LYS B 688 ? TYR B 684 LYS B 688 
AB2 1 LYS E 51  ? ASP E 56  ? LYS E 51  ASP E 56  
AB2 2 VAL E 20  ? TRP E 25  ? VAL E 20  TRP E 25  
AB2 3 THR E 74  ? LYS E 79  ? THR E 74  LYS E 79  
AB2 4 GLU E 82  ? VAL E 88  ? GLU E 82  VAL E 88  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N LEU A 414 ? N LEU A 414 O MET A 466 ? O MET A 466 
AA2 1 2 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 2 3 N PHE A 171 ? N PHE A 171 O SER A 200 ? O SER A 200 
AA2 3 4 N LEU A 201 ? N LEU A 201 O TYR A 250 ? O TYR A 250 
AA2 4 5 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA2 5 6 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 6 7 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA4 1 2 N ARG A 604 ? N ARG A 604 O THR A 611 ? O THR A 611 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA7 2 3 O ILE B 407 ? O ILE B 407 N LEU B 172 ? N LEU B 172 
AA7 3 4 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 4 5 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA7 5 6 N ALA B 249 ? N ALA B 249 O SER B 279 ? O SER B 279 
AA7 6 7 N ILE B 284 ? N ILE B 284 O MET B 359 ? O MET B 359 
AA7 7 8 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB1 1 2 N LEU B 656 ? N LEU B 656 O TYR B 684 ? O TYR B 684 
AB2 1 2 O VAL E 53  ? O VAL E 53  N ASP E 23  ? N ASP E 23  
AB2 2 3 N ALA E 22  ? N ALA E 22  O LEU E 76  ? O LEU E 76  
AB2 3 4 N LEU E 75  ? N LEU E 75  O SER E 87  ? O SER E 87  
# 
_pdbx_entry_details.entry_id                   9BXT 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B PRO 616 ? ? OH B TYR 626 ? ? 2.13 
2 1 O A PRO 616 ? ? OH A TYR 626 ? ? 2.15 
3 1 O A GLU 119 ? ? OG A SER 123 ? ? 2.18 
# 
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 MET A 240 ? ? 73.46  -7.62   
2 1 SER A 593 ? ? 61.31  -155.42 
3 1 ASN B 131 ? ? 60.22  61.13   
4 1 ASP B 215 ? ? 71.81  -3.83   
5 1 ASP B 238 ? ? -97.25 30.68   
6 1 MET B 240 ? ? 59.39  2.73    
7 1 SER B 593 ? ? 57.30  -159.13 
8 1 ASP D 317 ? ? 62.23  172.19  
9 1 ASP D 318 ? ? 68.64  -4.94   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BXT 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_em_3d_fitting_list.pdb_entry_id 
_em_3d_fitting_list.pdb_chain_id 
_em_3d_fitting_list.pdb_chain_residue_range 
_em_3d_fitting_list.details 
_em_3d_fitting_list.chain_id 
_em_3d_fitting_list.chain_residue_range 
_em_3d_fitting_list.source_name 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 9BXC ? ? 'Rigid-body docking of consensus model 9BXC containing alpha subunits and beta C-terminal tails' ? ?      PDB       
'experimental model' 9BXC 1 
2 1 .    . . 'Rigid-body docking of residues 19-104 from AF2 prediction of Uniprot entry P14949'              ? 19-104 AlphaFold 
'in silico model'    ?    ? 
# 
_em_3d_reconstruction.entry_id                    9BXT 
_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                  2.88 
_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               171000 
_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       '50 mM HEPES, 150 mM NaCl, 15 mM MgCl2, 5% (w/v) glycerol' 
_em_buffer.pH            7.6 
# 
_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                 'Bacillus subtilis ribonucleotide reductase complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_imaging.entry_id                        9BXT 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             'COMA FREE' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_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              9BXT 
_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   298 
_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                9BXT 
_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              9BXT 
_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 SER 2   ? A SER 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A ASP 689 ? A ASP 689 
7   1 Y 1 A THR 690 ? A THR 690 
8   1 Y 1 A GLY 691 ? A GLY 691 
9   1 Y 1 A GLN 692 ? A GLN 692 
10  1 Y 1 A ASP 693 ? A ASP 693 
11  1 Y 1 A SER 694 ? A SER 694 
12  1 Y 1 A CYS 695 ? A CYS 695 
13  1 Y 1 A LEU 696 ? A LEU 696 
14  1 Y 1 A SER 697 ? A SER 697 
15  1 Y 1 A CYS 698 ? A CYS 698 
16  1 Y 1 A VAL 699 ? A VAL 699 
17  1 Y 1 A VAL 700 ? A VAL 700 
18  1 Y 1 B MET 1   ? B MET 1   
19  1 Y 1 B SER 2   ? B SER 2   
20  1 Y 1 B GLN 3   ? B GLN 3   
21  1 Y 1 B ASN 4   ? B ASN 4   
22  1 Y 1 B GLN 5   ? B GLN 5   
23  1 Y 1 B ASP 689 ? B ASP 689 
24  1 Y 1 B THR 690 ? B THR 690 
25  1 Y 1 B GLY 691 ? B GLY 691 
26  1 Y 1 B GLN 692 ? B GLN 692 
27  1 Y 1 B ASP 693 ? B ASP 693 
28  1 Y 1 B SER 694 ? B SER 694 
29  1 Y 1 B CYS 695 ? B CYS 695 
30  1 Y 1 B LEU 696 ? B LEU 696 
31  1 Y 1 B SER 697 ? B SER 697 
32  1 Y 1 B CYS 698 ? B CYS 698 
33  1 Y 1 B VAL 699 ? B VAL 699 
34  1 Y 1 B VAL 700 ? B VAL 700 
35  1 Y 1 C MET -20 ? C MET 1   
36  1 Y 1 C GLY -19 ? C GLY 2   
37  1 Y 1 C SER -18 ? C SER 3   
38  1 Y 1 C SER -17 ? C SER 4   
39  1 Y 1 C HIS -16 ? C HIS 5   
40  1 Y 1 C HIS -15 ? C HIS 6   
41  1 Y 1 C HIS -14 ? C HIS 7   
42  1 Y 1 C HIS -13 ? C HIS 8   
43  1 Y 1 C HIS -12 ? C HIS 9   
44  1 Y 1 C HIS -11 ? C HIS 10  
45  1 Y 1 C SER -10 ? C SER 11  
46  1 Y 1 C SER -9  ? C SER 12  
47  1 Y 1 C GLY -8  ? C GLY 13  
48  1 Y 1 C LEU -7  ? C LEU 14  
49  1 Y 1 C VAL -6  ? C VAL 15  
50  1 Y 1 C PRO -5  ? C PRO 16  
51  1 Y 1 C ARG -4  ? C ARG 17  
52  1 Y 1 C GLY -3  ? C GLY 18  
53  1 Y 1 C SER -2  ? C SER 19  
54  1 Y 1 C HIS -1  ? C HIS 20  
55  1 Y 1 C MET 0   ? C MET 21  
56  1 Y 1 C MET 1   ? C MET 22  
57  1 Y 1 C THR 2   ? C THR 23  
58  1 Y 1 C LYS 3   ? C LYS 24  
59  1 Y 1 C ILE 4   ? C ILE 25  
60  1 Y 1 C TYR 5   ? C TYR 26  
61  1 Y 1 C ASP 6   ? C ASP 27  
62  1 Y 1 C ALA 7   ? C ALA 28  
63  1 Y 1 C ALA 8   ? C ALA 29  
64  1 Y 1 C ASN 9   ? C ASN 30  
65  1 Y 1 C TRP 10  ? C TRP 31  
66  1 Y 1 C SER 11  ? C SER 32  
67  1 Y 1 C LYS 12  ? C LYS 33  
68  1 Y 1 C HIS 13  ? C HIS 34  
69  1 Y 1 C GLU 14  ? C GLU 35  
70  1 Y 1 C ASP 15  ? C ASP 36  
71  1 Y 1 C ASP 16  ? C ASP 37  
72  1 Y 1 C PHE 17  ? C PHE 38  
73  1 Y 1 C THR 18  ? C THR 39  
74  1 Y 1 C GLN 19  ? C GLN 40  
75  1 Y 1 C MET 20  ? C MET 41  
76  1 Y 1 C PHE 21  ? C PHE 42  
77  1 Y 1 C TYR 22  ? C TYR 43  
78  1 Y 1 C ASN 23  ? C ASN 44  
79  1 Y 1 C GLN 24  ? C GLN 45  
80  1 Y 1 C ASN 25  ? C ASN 46  
81  1 Y 1 C VAL 26  ? C VAL 47  
82  1 Y 1 C LYS 27  ? C LYS 48  
83  1 Y 1 C GLN 28  ? C GLN 49  
84  1 Y 1 C PHE 29  ? C PHE 50  
85  1 Y 1 C TRP 30  ? C TRP 51  
86  1 Y 1 C LEU 31  ? C LEU 52  
87  1 Y 1 C PRO 32  ? C PRO 53  
88  1 Y 1 C GLU 33  ? C GLU 54  
89  1 Y 1 C GLU 34  ? C GLU 55  
90  1 Y 1 C ILE 35  ? C ILE 56  
91  1 Y 1 C ALA 36  ? C ALA 57  
92  1 Y 1 C LEU 37  ? C LEU 58  
93  1 Y 1 C ASN 38  ? C ASN 59  
94  1 Y 1 C GLY 39  ? C GLY 60  
95  1 Y 1 C ASP 40  ? C ASP 61  
96  1 Y 1 C LEU 41  ? C LEU 62  
97  1 Y 1 C LEU 42  ? C LEU 63  
98  1 Y 1 C THR 43  ? C THR 64  
99  1 Y 1 C TRP 44  ? C TRP 65  
100 1 Y 1 C LYS 45  ? C LYS 66  
101 1 Y 1 C TYR 46  ? C TYR 67  
102 1 Y 1 C LEU 47  ? C LEU 68  
103 1 Y 1 C GLY 48  ? C GLY 69  
104 1 Y 1 C LYS 49  ? C LYS 70  
105 1 Y 1 C ASN 50  ? C ASN 71  
106 1 Y 1 C GLU 51  ? C GLU 72  
107 1 Y 1 C GLN 52  ? C GLN 73  
108 1 Y 1 C ASP 53  ? C ASP 74  
109 1 Y 1 C THR 54  ? C THR 75  
110 1 Y 1 C TYR 55  ? C TYR 76  
111 1 Y 1 C MET 56  ? C MET 77  
112 1 Y 1 C LYS 57  ? C LYS 78  
113 1 Y 1 C VAL 58  ? C VAL 79  
114 1 Y 1 C LEU 59  ? C LEU 80  
115 1 Y 1 C ALA 60  ? C ALA 81  
116 1 Y 1 C GLY 61  ? C GLY 82  
117 1 Y 1 C LEU 62  ? C LEU 83  
118 1 Y 1 C THR 63  ? C THR 84  
119 1 Y 1 C LEU 64  ? C LEU 85  
120 1 Y 1 C LEU 65  ? C LEU 86  
121 1 Y 1 C ASP 66  ? C ASP 87  
122 1 Y 1 C THR 67  ? C THR 88  
123 1 Y 1 C GLU 68  ? C GLU 89  
124 1 Y 1 C GLN 69  ? C GLN 90  
125 1 Y 1 C GLY 70  ? C GLY 91  
126 1 Y 1 C ASN 71  ? C ASN 92  
127 1 Y 1 C THR 72  ? C THR 93  
128 1 Y 1 C GLY 73  ? C GLY 94  
129 1 Y 1 C MET 74  ? C MET 95  
130 1 Y 1 C PRO 75  ? C PRO 96  
131 1 Y 1 C ILE 76  ? C ILE 97  
132 1 Y 1 C VAL 77  ? C VAL 98  
133 1 Y 1 C ALA 78  ? C ALA 99  
134 1 Y 1 C GLU 79  ? C GLU 100 
135 1 Y 1 C HIS 80  ? C HIS 101 
136 1 Y 1 C VAL 81  ? C VAL 102 
137 1 Y 1 C ASP 82  ? C ASP 103 
138 1 Y 1 C GLY 83  ? C GLY 104 
139 1 Y 1 C HIS 84  ? C HIS 105 
140 1 Y 1 C GLN 85  ? C GLN 106 
141 1 Y 1 C ARG 86  ? C ARG 107 
142 1 Y 1 C LYS 87  ? C LYS 108 
143 1 Y 1 C ALA 88  ? C ALA 109 
144 1 Y 1 C VAL 89  ? C VAL 110 
145 1 Y 1 C LEU 90  ? C LEU 111 
146 1 Y 1 C ASN 91  ? C ASN 112 
147 1 Y 1 C PHE 92  ? C PHE 113 
148 1 Y 1 C MET 93  ? C MET 114 
149 1 Y 1 C ALA 94  ? C ALA 115 
150 1 Y 1 C MET 95  ? C MET 116 
151 1 Y 1 C MET 96  ? C MET 117 
152 1 Y 1 C GLU 97  ? C GLU 118 
153 1 Y 1 C ASN 98  ? C ASN 119 
154 1 Y 1 C ALA 99  ? C ALA 120 
155 1 Y 1 C VAL 100 ? C VAL 121 
156 1 Y 1 C HIS 101 ? C HIS 122 
157 1 Y 1 C ALA 102 ? C ALA 123 
158 1 Y 1 C LYS 103 ? C LYS 124 
159 1 Y 1 C SER 104 ? C SER 125 
160 1 Y 1 C TYR 105 ? C TYR 126 
161 1 Y 1 C SER 106 ? C SER 127 
162 1 Y 1 C ASN 107 ? C ASN 128 
163 1 Y 1 C ILE 108 ? C ILE 129 
164 1 Y 1 C PHE 109 ? C PHE 130 
165 1 Y 1 C MET 110 ? C MET 131 
166 1 Y 1 C THR 111 ? C THR 132 
167 1 Y 1 C LEU 112 ? C LEU 133 
168 1 Y 1 C ALA 113 ? C ALA 134 
169 1 Y 1 C PRO 114 ? C PRO 135 
170 1 Y 1 C THR 115 ? C THR 136 
171 1 Y 1 C GLU 116 ? C GLU 137 
172 1 Y 1 C THR 117 ? C THR 138 
173 1 Y 1 C ILE 118 ? C ILE 139 
174 1 Y 1 C ASN 119 ? C ASN 140 
175 1 Y 1 C GLU 120 ? C GLU 141 
176 1 Y 1 C VAL 121 ? C VAL 142 
177 1 Y 1 C PHE 122 ? C PHE 143 
178 1 Y 1 C GLU 123 ? C GLU 144 
179 1 Y 1 C TRP 124 ? C TRP 145 
180 1 Y 1 C VAL 125 ? C VAL 146 
181 1 Y 1 C LYS 126 ? C LYS 147 
182 1 Y 1 C GLN 127 ? C GLN 148 
183 1 Y 1 C ASN 128 ? C ASN 149 
184 1 Y 1 C LYS 129 ? C LYS 150 
185 1 Y 1 C TYR 130 ? C TYR 151 
186 1 Y 1 C LEU 131 ? C LEU 152 
187 1 Y 1 C GLN 132 ? C GLN 153 
188 1 Y 1 C LYS 133 ? C LYS 154 
189 1 Y 1 C LYS 134 ? C LYS 155 
190 1 Y 1 C ALA 135 ? C ALA 156 
191 1 Y 1 C GLN 136 ? C GLN 157 
192 1 Y 1 C MET 137 ? C MET 158 
193 1 Y 1 C ILE 138 ? C ILE 159 
194 1 Y 1 C VAL 139 ? C VAL 160 
195 1 Y 1 C GLY 140 ? C GLY 161 
196 1 Y 1 C LEU 141 ? C LEU 162 
197 1 Y 1 C TYR 142 ? C TYR 163 
198 1 Y 1 C LYS 143 ? C LYS 164 
199 1 Y 1 C ALA 144 ? C ALA 165 
200 1 Y 1 C ILE 145 ? C ILE 166 
201 1 Y 1 C GLN 146 ? C GLN 167 
202 1 Y 1 C LYS 147 ? C LYS 168 
203 1 Y 1 C ASP 148 ? C ASP 169 
204 1 Y 1 C ASP 149 ? C ASP 170 
205 1 Y 1 C GLU 150 ? C GLU 171 
206 1 Y 1 C ILE 151 ? C ILE 172 
207 1 Y 1 C SER 152 ? C SER 173 
208 1 Y 1 C LEU 153 ? C LEU 174 
209 1 Y 1 C PHE 154 ? C PHE 175 
210 1 Y 1 C LYS 155 ? C LYS 176 
211 1 Y 1 C ALA 156 ? C ALA 177 
212 1 Y 1 C MET 157 ? C MET 178 
213 1 Y 1 C VAL 158 ? C VAL 179 
214 1 Y 1 C ALA 159 ? C ALA 180 
215 1 Y 1 C SER 160 ? C SER 181 
216 1 Y 1 C VAL 161 ? C VAL 182 
217 1 Y 1 C TYR 162 ? C TYR 183 
218 1 Y 1 C LEU 163 ? C LEU 184 
219 1 Y 1 C GLU 164 ? C GLU 185 
220 1 Y 1 C SER 165 ? C SER 186 
221 1 Y 1 C PHE 166 ? C PHE 187 
222 1 Y 1 C LEU 167 ? C LEU 188 
223 1 Y 1 C PHE 168 ? C PHE 189 
224 1 Y 1 C TYR 169 ? C TYR 190 
225 1 Y 1 C SER 170 ? C SER 191 
226 1 Y 1 C GLY 171 ? C GLY 192 
227 1 Y 1 C PHE 172 ? C PHE 193 
228 1 Y 1 C TYR 173 ? C TYR 194 
229 1 Y 1 C TYR 174 ? C TYR 195 
230 1 Y 1 C PRO 175 ? C PRO 196 
231 1 Y 1 C LEU 176 ? C LEU 197 
232 1 Y 1 C TYR 177 ? C TYR 198 
233 1 Y 1 C PHE 178 ? C PHE 199 
234 1 Y 1 C TYR 179 ? C TYR 200 
235 1 Y 1 C GLY 180 ? C GLY 201 
236 1 Y 1 C GLN 181 ? C GLN 202 
237 1 Y 1 C GLY 182 ? C GLY 203 
238 1 Y 1 C LYS 183 ? C LYS 204 
239 1 Y 1 C LEU 184 ? C LEU 205 
240 1 Y 1 C MET 185 ? C MET 206 
241 1 Y 1 C GLN 186 ? C GLN 207 
242 1 Y 1 C SER 187 ? C SER 208 
243 1 Y 1 C GLY 188 ? C GLY 209 
244 1 Y 1 C GLU 189 ? C GLU 210 
245 1 Y 1 C ILE 190 ? C ILE 211 
246 1 Y 1 C ILE 191 ? C ILE 212 
247 1 Y 1 C ASN 192 ? C ASN 213 
248 1 Y 1 C LEU 193 ? C LEU 214 
249 1 Y 1 C ILE 194 ? C ILE 215 
250 1 Y 1 C LEU 195 ? C LEU 216 
251 1 Y 1 C ARG 196 ? C ARG 217 
252 1 Y 1 C ASP 197 ? C ASP 218 
253 1 Y 1 C GLU 198 ? C GLU 219 
254 1 Y 1 C ALA 199 ? C ALA 220 
255 1 Y 1 C ILE 200 ? C ILE 221 
256 1 Y 1 C HIS 201 ? C HIS 222 
257 1 Y 1 C GLY 202 ? C GLY 223 
258 1 Y 1 C VAL 203 ? C VAL 224 
259 1 Y 1 C TYR 204 ? C TYR 225 
260 1 Y 1 C VAL 205 ? C VAL 226 
261 1 Y 1 C GLY 206 ? C GLY 227 
262 1 Y 1 C LEU 207 ? C LEU 228 
263 1 Y 1 C LEU 208 ? C LEU 229 
264 1 Y 1 C ALA 209 ? C ALA 230 
265 1 Y 1 C GLN 210 ? C GLN 231 
266 1 Y 1 C GLU 211 ? C GLU 232 
267 1 Y 1 C ILE 212 ? C ILE 233 
268 1 Y 1 C TYR 213 ? C TYR 234 
269 1 Y 1 C ASN 214 ? C ASN 235 
270 1 Y 1 C LYS 215 ? C LYS 236 
271 1 Y 1 C GLN 216 ? C GLN 237 
272 1 Y 1 C THR 217 ? C THR 238 
273 1 Y 1 C GLU 218 ? C GLU 239 
274 1 Y 1 C GLU 219 ? C GLU 240 
275 1 Y 1 C LYS 220 ? C LYS 241 
276 1 Y 1 C LYS 221 ? C LYS 242 
277 1 Y 1 C ALA 222 ? C ALA 243 
278 1 Y 1 C GLU 223 ? C GLU 244 
279 1 Y 1 C LEU 224 ? C LEU 245 
280 1 Y 1 C ARG 225 ? C ARG 246 
281 1 Y 1 C GLU 226 ? C GLU 247 
282 1 Y 1 C PHE 227 ? C PHE 248 
283 1 Y 1 C ALA 228 ? C ALA 249 
284 1 Y 1 C ILE 229 ? C ILE 250 
285 1 Y 1 C ASP 230 ? C ASP 251 
286 1 Y 1 C LEU 231 ? C LEU 252 
287 1 Y 1 C LEU 232 ? C LEU 253 
288 1 Y 1 C ASN 233 ? C ASN 254 
289 1 Y 1 C GLN 234 ? C GLN 255 
290 1 Y 1 C LEU 235 ? C LEU 256 
291 1 Y 1 C TYR 236 ? C TYR 257 
292 1 Y 1 C GLU 237 ? C GLU 258 
293 1 Y 1 C ASN 238 ? C ASN 259 
294 1 Y 1 C GLU 239 ? C GLU 260 
295 1 Y 1 C LEU 240 ? C LEU 261 
296 1 Y 1 C GLU 241 ? C GLU 262 
297 1 Y 1 C TYR 242 ? C TYR 263 
298 1 Y 1 C THR 243 ? C THR 264 
299 1 Y 1 C GLU 244 ? C GLU 265 
300 1 Y 1 C ASP 245 ? C ASP 266 
301 1 Y 1 C LEU 246 ? C LEU 267 
302 1 Y 1 C TYR 247 ? C TYR 268 
303 1 Y 1 C ASP 248 ? C ASP 269 
304 1 Y 1 C GLN 249 ? C GLN 270 
305 1 Y 1 C VAL 250 ? C VAL 271 
306 1 Y 1 C GLY 251 ? C GLY 272 
307 1 Y 1 C LEU 252 ? C LEU 273 
308 1 Y 1 C SER 253 ? C SER 274 
309 1 Y 1 C HIS 254 ? C HIS 275 
310 1 Y 1 C ASP 255 ? C ASP 276 
311 1 Y 1 C VAL 256 ? C VAL 277 
312 1 Y 1 C LYS 257 ? C LYS 278 
313 1 Y 1 C LYS 258 ? C LYS 279 
314 1 Y 1 C PHE 259 ? C PHE 280 
315 1 Y 1 C ILE 260 ? C ILE 281 
316 1 Y 1 C ARG 261 ? C ARG 282 
317 1 Y 1 C TYR 262 ? C TYR 283 
318 1 Y 1 C ASN 263 ? C ASN 284 
319 1 Y 1 C ALA 264 ? C ALA 285 
320 1 Y 1 C ASN 265 ? C ASN 286 
321 1 Y 1 C LYS 266 ? C LYS 287 
322 1 Y 1 C ALA 267 ? C ALA 288 
323 1 Y 1 C LEU 268 ? C LEU 289 
324 1 Y 1 C MET 269 ? C MET 290 
325 1 Y 1 C ASN 270 ? C ASN 291 
326 1 Y 1 C LEU 271 ? C LEU 292 
327 1 Y 1 C GLY 272 ? C GLY 293 
328 1 Y 1 C PHE 273 ? C PHE 294 
329 1 Y 1 C ASP 274 ? C ASP 295 
330 1 Y 1 C PRO 275 ? C PRO 296 
331 1 Y 1 C TYR 276 ? C TYR 297 
332 1 Y 1 C PHE 277 ? C PHE 298 
333 1 Y 1 C GLU 278 ? C GLU 299 
334 1 Y 1 C GLU 279 ? C GLU 300 
335 1 Y 1 C GLU 280 ? C GLU 301 
336 1 Y 1 C ASP 281 ? C ASP 302 
337 1 Y 1 C ILE 282 ? C ILE 303 
338 1 Y 1 C ASN 283 ? C ASN 304 
339 1 Y 1 C PRO 284 ? C PRO 305 
340 1 Y 1 C ILE 285 ? C ILE 306 
341 1 Y 1 C VAL 286 ? C VAL 307 
342 1 Y 1 C LEU 287 ? C LEU 308 
343 1 Y 1 C ASN 288 ? C ASN 309 
344 1 Y 1 C GLY 289 ? C GLY 310 
345 1 Y 1 C LEU 290 ? C LEU 311 
346 1 Y 1 C ASN 291 ? C ASN 312 
347 1 Y 1 C THR 292 ? C THR 313 
348 1 Y 1 C LYS 293 ? C LYS 314 
349 1 Y 1 C THR 294 ? C THR 315 
350 1 Y 1 C LYS 295 ? C LYS 316 
351 1 Y 1 C SER 296 ? C SER 317 
352 1 Y 1 C HIS 297 ? C HIS 318 
353 1 Y 1 C ASP 298 ? C ASP 319 
354 1 Y 1 C PHE 299 ? C PHE 320 
355 1 Y 1 C PHE 300 ? C PHE 321 
356 1 Y 1 C SER 301 ? C SER 322 
357 1 Y 1 C MET 302 ? C MET 323 
358 1 Y 1 C LYS 303 ? C LYS 324 
359 1 Y 1 C GLY 304 ? C GLY 325 
360 1 Y 1 C ASN 305 ? C ASN 326 
361 1 Y 1 C GLY 306 ? C GLY 327 
362 1 Y 1 C TYR 307 ? C TYR 328 
363 1 Y 1 C LYS 308 ? C LYS 329 
364 1 Y 1 C LYS 309 ? C LYS 330 
365 1 Y 1 C ALA 310 ? C ALA 331 
366 1 Y 1 C GLU 323 ? C GLU 344 
367 1 Y 1 C ASP 324 ? C ASP 345 
368 1 Y 1 C GLU 325 ? C GLU 346 
369 1 Y 1 C LYS 326 ? C LYS 347 
370 1 Y 1 C GLU 327 ? C GLU 348 
371 1 Y 1 C GLN 328 ? C GLN 349 
372 1 Y 1 C ILE 329 ? C ILE 350 
373 1 Y 1 D MET -20 ? D MET 1   
374 1 Y 1 D GLY -19 ? D GLY 2   
375 1 Y 1 D SER -18 ? D SER 3   
376 1 Y 1 D SER -17 ? D SER 4   
377 1 Y 1 D HIS -16 ? D HIS 5   
378 1 Y 1 D HIS -15 ? D HIS 6   
379 1 Y 1 D HIS -14 ? D HIS 7   
380 1 Y 1 D HIS -13 ? D HIS 8   
381 1 Y 1 D HIS -12 ? D HIS 9   
382 1 Y 1 D HIS -11 ? D HIS 10  
383 1 Y 1 D SER -10 ? D SER 11  
384 1 Y 1 D SER -9  ? D SER 12  
385 1 Y 1 D GLY -8  ? D GLY 13  
386 1 Y 1 D LEU -7  ? D LEU 14  
387 1 Y 1 D VAL -6  ? D VAL 15  
388 1 Y 1 D PRO -5  ? D PRO 16  
389 1 Y 1 D ARG -4  ? D ARG 17  
390 1 Y 1 D GLY -3  ? D GLY 18  
391 1 Y 1 D SER -2  ? D SER 19  
392 1 Y 1 D HIS -1  ? D HIS 20  
393 1 Y 1 D MET 0   ? D MET 21  
394 1 Y 1 D MET 1   ? D MET 22  
395 1 Y 1 D THR 2   ? D THR 23  
396 1 Y 1 D LYS 3   ? D LYS 24  
397 1 Y 1 D ILE 4   ? D ILE 25  
398 1 Y 1 D TYR 5   ? D TYR 26  
399 1 Y 1 D ASP 6   ? D ASP 27  
400 1 Y 1 D ALA 7   ? D ALA 28  
401 1 Y 1 D ALA 8   ? D ALA 29  
402 1 Y 1 D ASN 9   ? D ASN 30  
403 1 Y 1 D TRP 10  ? D TRP 31  
404 1 Y 1 D SER 11  ? D SER 32  
405 1 Y 1 D LYS 12  ? D LYS 33  
406 1 Y 1 D HIS 13  ? D HIS 34  
407 1 Y 1 D GLU 14  ? D GLU 35  
408 1 Y 1 D ASP 15  ? D ASP 36  
409 1 Y 1 D ASP 16  ? D ASP 37  
410 1 Y 1 D PHE 17  ? D PHE 38  
411 1 Y 1 D THR 18  ? D THR 39  
412 1 Y 1 D GLN 19  ? D GLN 40  
413 1 Y 1 D MET 20  ? D MET 41  
414 1 Y 1 D PHE 21  ? D PHE 42  
415 1 Y 1 D TYR 22  ? D TYR 43  
416 1 Y 1 D ASN 23  ? D ASN 44  
417 1 Y 1 D GLN 24  ? D GLN 45  
418 1 Y 1 D ASN 25  ? D ASN 46  
419 1 Y 1 D VAL 26  ? D VAL 47  
420 1 Y 1 D LYS 27  ? D LYS 48  
421 1 Y 1 D GLN 28  ? D GLN 49  
422 1 Y 1 D PHE 29  ? D PHE 50  
423 1 Y 1 D TRP 30  ? D TRP 51  
424 1 Y 1 D LEU 31  ? D LEU 52  
425 1 Y 1 D PRO 32  ? D PRO 53  
426 1 Y 1 D GLU 33  ? D GLU 54  
427 1 Y 1 D GLU 34  ? D GLU 55  
428 1 Y 1 D ILE 35  ? D ILE 56  
429 1 Y 1 D ALA 36  ? D ALA 57  
430 1 Y 1 D LEU 37  ? D LEU 58  
431 1 Y 1 D ASN 38  ? D ASN 59  
432 1 Y 1 D GLY 39  ? D GLY 60  
433 1 Y 1 D ASP 40  ? D ASP 61  
434 1 Y 1 D LEU 41  ? D LEU 62  
435 1 Y 1 D LEU 42  ? D LEU 63  
436 1 Y 1 D THR 43  ? D THR 64  
437 1 Y 1 D TRP 44  ? D TRP 65  
438 1 Y 1 D LYS 45  ? D LYS 66  
439 1 Y 1 D TYR 46  ? D TYR 67  
440 1 Y 1 D LEU 47  ? D LEU 68  
441 1 Y 1 D GLY 48  ? D GLY 69  
442 1 Y 1 D LYS 49  ? D LYS 70  
443 1 Y 1 D ASN 50  ? D ASN 71  
444 1 Y 1 D GLU 51  ? D GLU 72  
445 1 Y 1 D GLN 52  ? D GLN 73  
446 1 Y 1 D ASP 53  ? D ASP 74  
447 1 Y 1 D THR 54  ? D THR 75  
448 1 Y 1 D TYR 55  ? D TYR 76  
449 1 Y 1 D MET 56  ? D MET 77  
450 1 Y 1 D LYS 57  ? D LYS 78  
451 1 Y 1 D VAL 58  ? D VAL 79  
452 1 Y 1 D LEU 59  ? D LEU 80  
453 1 Y 1 D ALA 60  ? D ALA 81  
454 1 Y 1 D GLY 61  ? D GLY 82  
455 1 Y 1 D LEU 62  ? D LEU 83  
456 1 Y 1 D THR 63  ? D THR 84  
457 1 Y 1 D LEU 64  ? D LEU 85  
458 1 Y 1 D LEU 65  ? D LEU 86  
459 1 Y 1 D ASP 66  ? D ASP 87  
460 1 Y 1 D THR 67  ? D THR 88  
461 1 Y 1 D GLU 68  ? D GLU 89  
462 1 Y 1 D GLN 69  ? D GLN 90  
463 1 Y 1 D GLY 70  ? D GLY 91  
464 1 Y 1 D ASN 71  ? D ASN 92  
465 1 Y 1 D THR 72  ? D THR 93  
466 1 Y 1 D GLY 73  ? D GLY 94  
467 1 Y 1 D MET 74  ? D MET 95  
468 1 Y 1 D PRO 75  ? D PRO 96  
469 1 Y 1 D ILE 76  ? D ILE 97  
470 1 Y 1 D VAL 77  ? D VAL 98  
471 1 Y 1 D ALA 78  ? D ALA 99  
472 1 Y 1 D GLU 79  ? D GLU 100 
473 1 Y 1 D HIS 80  ? D HIS 101 
474 1 Y 1 D VAL 81  ? D VAL 102 
475 1 Y 1 D ASP 82  ? D ASP 103 
476 1 Y 1 D GLY 83  ? D GLY 104 
477 1 Y 1 D HIS 84  ? D HIS 105 
478 1 Y 1 D GLN 85  ? D GLN 106 
479 1 Y 1 D ARG 86  ? D ARG 107 
480 1 Y 1 D LYS 87  ? D LYS 108 
481 1 Y 1 D ALA 88  ? D ALA 109 
482 1 Y 1 D VAL 89  ? D VAL 110 
483 1 Y 1 D LEU 90  ? D LEU 111 
484 1 Y 1 D ASN 91  ? D ASN 112 
485 1 Y 1 D PHE 92  ? D PHE 113 
486 1 Y 1 D MET 93  ? D MET 114 
487 1 Y 1 D ALA 94  ? D ALA 115 
488 1 Y 1 D MET 95  ? D MET 116 
489 1 Y 1 D MET 96  ? D MET 117 
490 1 Y 1 D GLU 97  ? D GLU 118 
491 1 Y 1 D ASN 98  ? D ASN 119 
492 1 Y 1 D ALA 99  ? D ALA 120 
493 1 Y 1 D VAL 100 ? D VAL 121 
494 1 Y 1 D HIS 101 ? D HIS 122 
495 1 Y 1 D ALA 102 ? D ALA 123 
496 1 Y 1 D LYS 103 ? D LYS 124 
497 1 Y 1 D SER 104 ? D SER 125 
498 1 Y 1 D TYR 105 ? D TYR 126 
499 1 Y 1 D SER 106 ? D SER 127 
500 1 Y 1 D ASN 107 ? D ASN 128 
501 1 Y 1 D ILE 108 ? D ILE 129 
502 1 Y 1 D PHE 109 ? D PHE 130 
503 1 Y 1 D MET 110 ? D MET 131 
504 1 Y 1 D THR 111 ? D THR 132 
505 1 Y 1 D LEU 112 ? D LEU 133 
506 1 Y 1 D ALA 113 ? D ALA 134 
507 1 Y 1 D PRO 114 ? D PRO 135 
508 1 Y 1 D THR 115 ? D THR 136 
509 1 Y 1 D GLU 116 ? D GLU 137 
510 1 Y 1 D THR 117 ? D THR 138 
511 1 Y 1 D ILE 118 ? D ILE 139 
512 1 Y 1 D ASN 119 ? D ASN 140 
513 1 Y 1 D GLU 120 ? D GLU 141 
514 1 Y 1 D VAL 121 ? D VAL 142 
515 1 Y 1 D PHE 122 ? D PHE 143 
516 1 Y 1 D GLU 123 ? D GLU 144 
517 1 Y 1 D TRP 124 ? D TRP 145 
518 1 Y 1 D VAL 125 ? D VAL 146 
519 1 Y 1 D LYS 126 ? D LYS 147 
520 1 Y 1 D GLN 127 ? D GLN 148 
521 1 Y 1 D ASN 128 ? D ASN 149 
522 1 Y 1 D LYS 129 ? D LYS 150 
523 1 Y 1 D TYR 130 ? D TYR 151 
524 1 Y 1 D LEU 131 ? D LEU 152 
525 1 Y 1 D GLN 132 ? D GLN 153 
526 1 Y 1 D LYS 133 ? D LYS 154 
527 1 Y 1 D LYS 134 ? D LYS 155 
528 1 Y 1 D ALA 135 ? D ALA 156 
529 1 Y 1 D GLN 136 ? D GLN 157 
530 1 Y 1 D MET 137 ? D MET 158 
531 1 Y 1 D ILE 138 ? D ILE 159 
532 1 Y 1 D VAL 139 ? D VAL 160 
533 1 Y 1 D GLY 140 ? D GLY 161 
534 1 Y 1 D LEU 141 ? D LEU 162 
535 1 Y 1 D TYR 142 ? D TYR 163 
536 1 Y 1 D LYS 143 ? D LYS 164 
537 1 Y 1 D ALA 144 ? D ALA 165 
538 1 Y 1 D ILE 145 ? D ILE 166 
539 1 Y 1 D GLN 146 ? D GLN 167 
540 1 Y 1 D LYS 147 ? D LYS 168 
541 1 Y 1 D ASP 148 ? D ASP 169 
542 1 Y 1 D ASP 149 ? D ASP 170 
543 1 Y 1 D GLU 150 ? D GLU 171 
544 1 Y 1 D ILE 151 ? D ILE 172 
545 1 Y 1 D SER 152 ? D SER 173 
546 1 Y 1 D LEU 153 ? D LEU 174 
547 1 Y 1 D PHE 154 ? D PHE 175 
548 1 Y 1 D LYS 155 ? D LYS 176 
549 1 Y 1 D ALA 156 ? D ALA 177 
550 1 Y 1 D MET 157 ? D MET 178 
551 1 Y 1 D VAL 158 ? D VAL 179 
552 1 Y 1 D ALA 159 ? D ALA 180 
553 1 Y 1 D SER 160 ? D SER 181 
554 1 Y 1 D VAL 161 ? D VAL 182 
555 1 Y 1 D TYR 162 ? D TYR 183 
556 1 Y 1 D LEU 163 ? D LEU 184 
557 1 Y 1 D GLU 164 ? D GLU 185 
558 1 Y 1 D SER 165 ? D SER 186 
559 1 Y 1 D PHE 166 ? D PHE 187 
560 1 Y 1 D LEU 167 ? D LEU 188 
561 1 Y 1 D PHE 168 ? D PHE 189 
562 1 Y 1 D TYR 169 ? D TYR 190 
563 1 Y 1 D SER 170 ? D SER 191 
564 1 Y 1 D GLY 171 ? D GLY 192 
565 1 Y 1 D PHE 172 ? D PHE 193 
566 1 Y 1 D TYR 173 ? D TYR 194 
567 1 Y 1 D TYR 174 ? D TYR 195 
568 1 Y 1 D PRO 175 ? D PRO 196 
569 1 Y 1 D LEU 176 ? D LEU 197 
570 1 Y 1 D TYR 177 ? D TYR 198 
571 1 Y 1 D PHE 178 ? D PHE 199 
572 1 Y 1 D TYR 179 ? D TYR 200 
573 1 Y 1 D GLY 180 ? D GLY 201 
574 1 Y 1 D GLN 181 ? D GLN 202 
575 1 Y 1 D GLY 182 ? D GLY 203 
576 1 Y 1 D LYS 183 ? D LYS 204 
577 1 Y 1 D LEU 184 ? D LEU 205 
578 1 Y 1 D MET 185 ? D MET 206 
579 1 Y 1 D GLN 186 ? D GLN 207 
580 1 Y 1 D SER 187 ? D SER 208 
581 1 Y 1 D GLY 188 ? D GLY 209 
582 1 Y 1 D GLU 189 ? D GLU 210 
583 1 Y 1 D ILE 190 ? D ILE 211 
584 1 Y 1 D ILE 191 ? D ILE 212 
585 1 Y 1 D ASN 192 ? D ASN 213 
586 1 Y 1 D LEU 193 ? D LEU 214 
587 1 Y 1 D ILE 194 ? D ILE 215 
588 1 Y 1 D LEU 195 ? D LEU 216 
589 1 Y 1 D ARG 196 ? D ARG 217 
590 1 Y 1 D ASP 197 ? D ASP 218 
591 1 Y 1 D GLU 198 ? D GLU 219 
592 1 Y 1 D ALA 199 ? D ALA 220 
593 1 Y 1 D ILE 200 ? D ILE 221 
594 1 Y 1 D HIS 201 ? D HIS 222 
595 1 Y 1 D GLY 202 ? D GLY 223 
596 1 Y 1 D VAL 203 ? D VAL 224 
597 1 Y 1 D TYR 204 ? D TYR 225 
598 1 Y 1 D VAL 205 ? D VAL 226 
599 1 Y 1 D GLY 206 ? D GLY 227 
600 1 Y 1 D LEU 207 ? D LEU 228 
601 1 Y 1 D LEU 208 ? D LEU 229 
602 1 Y 1 D ALA 209 ? D ALA 230 
603 1 Y 1 D GLN 210 ? D GLN 231 
604 1 Y 1 D GLU 211 ? D GLU 232 
605 1 Y 1 D ILE 212 ? D ILE 233 
606 1 Y 1 D TYR 213 ? D TYR 234 
607 1 Y 1 D ASN 214 ? D ASN 235 
608 1 Y 1 D LYS 215 ? D LYS 236 
609 1 Y 1 D GLN 216 ? D GLN 237 
610 1 Y 1 D THR 217 ? D THR 238 
611 1 Y 1 D GLU 218 ? D GLU 239 
612 1 Y 1 D GLU 219 ? D GLU 240 
613 1 Y 1 D LYS 220 ? D LYS 241 
614 1 Y 1 D LYS 221 ? D LYS 242 
615 1 Y 1 D ALA 222 ? D ALA 243 
616 1 Y 1 D GLU 223 ? D GLU 244 
617 1 Y 1 D LEU 224 ? D LEU 245 
618 1 Y 1 D ARG 225 ? D ARG 246 
619 1 Y 1 D GLU 226 ? D GLU 247 
620 1 Y 1 D PHE 227 ? D PHE 248 
621 1 Y 1 D ALA 228 ? D ALA 249 
622 1 Y 1 D ILE 229 ? D ILE 250 
623 1 Y 1 D ASP 230 ? D ASP 251 
624 1 Y 1 D LEU 231 ? D LEU 252 
625 1 Y 1 D LEU 232 ? D LEU 253 
626 1 Y 1 D ASN 233 ? D ASN 254 
627 1 Y 1 D GLN 234 ? D GLN 255 
628 1 Y 1 D LEU 235 ? D LEU 256 
629 1 Y 1 D TYR 236 ? D TYR 257 
630 1 Y 1 D GLU 237 ? D GLU 258 
631 1 Y 1 D ASN 238 ? D ASN 259 
632 1 Y 1 D GLU 239 ? D GLU 260 
633 1 Y 1 D LEU 240 ? D LEU 261 
634 1 Y 1 D GLU 241 ? D GLU 262 
635 1 Y 1 D TYR 242 ? D TYR 263 
636 1 Y 1 D THR 243 ? D THR 264 
637 1 Y 1 D GLU 244 ? D GLU 265 
638 1 Y 1 D ASP 245 ? D ASP 266 
639 1 Y 1 D LEU 246 ? D LEU 267 
640 1 Y 1 D TYR 247 ? D TYR 268 
641 1 Y 1 D ASP 248 ? D ASP 269 
642 1 Y 1 D GLN 249 ? D GLN 270 
643 1 Y 1 D VAL 250 ? D VAL 271 
644 1 Y 1 D GLY 251 ? D GLY 272 
645 1 Y 1 D LEU 252 ? D LEU 273 
646 1 Y 1 D SER 253 ? D SER 274 
647 1 Y 1 D HIS 254 ? D HIS 275 
648 1 Y 1 D ASP 255 ? D ASP 276 
649 1 Y 1 D VAL 256 ? D VAL 277 
650 1 Y 1 D LYS 257 ? D LYS 278 
651 1 Y 1 D LYS 258 ? D LYS 279 
652 1 Y 1 D PHE 259 ? D PHE 280 
653 1 Y 1 D ILE 260 ? D ILE 281 
654 1 Y 1 D ARG 261 ? D ARG 282 
655 1 Y 1 D TYR 262 ? D TYR 283 
656 1 Y 1 D ASN 263 ? D ASN 284 
657 1 Y 1 D ALA 264 ? D ALA 285 
658 1 Y 1 D ASN 265 ? D ASN 286 
659 1 Y 1 D LYS 266 ? D LYS 287 
660 1 Y 1 D ALA 267 ? D ALA 288 
661 1 Y 1 D LEU 268 ? D LEU 289 
662 1 Y 1 D MET 269 ? D MET 290 
663 1 Y 1 D ASN 270 ? D ASN 291 
664 1 Y 1 D LEU 271 ? D LEU 292 
665 1 Y 1 D GLY 272 ? D GLY 293 
666 1 Y 1 D PHE 273 ? D PHE 294 
667 1 Y 1 D ASP 274 ? D ASP 295 
668 1 Y 1 D PRO 275 ? D PRO 296 
669 1 Y 1 D TYR 276 ? D TYR 297 
670 1 Y 1 D PHE 277 ? D PHE 298 
671 1 Y 1 D GLU 278 ? D GLU 299 
672 1 Y 1 D GLU 279 ? D GLU 300 
673 1 Y 1 D GLU 280 ? D GLU 301 
674 1 Y 1 D ASP 281 ? D ASP 302 
675 1 Y 1 D ILE 282 ? D ILE 303 
676 1 Y 1 D ASN 283 ? D ASN 304 
677 1 Y 1 D PRO 284 ? D PRO 305 
678 1 Y 1 D ILE 285 ? D ILE 306 
679 1 Y 1 D VAL 286 ? D VAL 307 
680 1 Y 1 D LEU 287 ? D LEU 308 
681 1 Y 1 D ASN 288 ? D ASN 309 
682 1 Y 1 D GLY 289 ? D GLY 310 
683 1 Y 1 D LEU 290 ? D LEU 311 
684 1 Y 1 D ASN 291 ? D ASN 312 
685 1 Y 1 D THR 292 ? D THR 313 
686 1 Y 1 D LYS 293 ? D LYS 314 
687 1 Y 1 D THR 294 ? D THR 315 
688 1 Y 1 D LYS 295 ? D LYS 316 
689 1 Y 1 D SER 296 ? D SER 317 
690 1 Y 1 D HIS 297 ? D HIS 318 
691 1 Y 1 D ASP 298 ? D ASP 319 
692 1 Y 1 D PHE 299 ? D PHE 320 
693 1 Y 1 D PHE 300 ? D PHE 321 
694 1 Y 1 D SER 301 ? D SER 322 
695 1 Y 1 D MET 302 ? D MET 323 
696 1 Y 1 D LYS 303 ? D LYS 324 
697 1 Y 1 D GLY 304 ? D GLY 325 
698 1 Y 1 D ASN 305 ? D ASN 326 
699 1 Y 1 D GLY 306 ? D GLY 327 
700 1 Y 1 D TYR 307 ? D TYR 328 
701 1 Y 1 D LYS 308 ? D LYS 329 
702 1 Y 1 D LYS 309 ? D LYS 330 
703 1 Y 1 D ALA 310 ? D ALA 331 
704 1 Y 1 D GLU 323 ? D GLU 344 
705 1 Y 1 D ASP 324 ? D ASP 345 
706 1 Y 1 D GLU 325 ? D GLU 346 
707 1 Y 1 D LYS 326 ? D LYS 347 
708 1 Y 1 D GLU 327 ? D GLU 348 
709 1 Y 1 D GLN 328 ? D GLN 349 
710 1 Y 1 D ILE 329 ? D ILE 350 
711 1 Y 1 E MET 1   ? E MET 1   
712 1 Y 1 E ALA 2   ? E ALA 2   
713 1 Y 1 E ILE 3   ? E ILE 3   
714 1 Y 1 E VAL 4   ? E VAL 4   
715 1 Y 1 E LYS 5   ? E LYS 5   
716 1 Y 1 E ALA 6   ? E ALA 6   
717 1 Y 1 E THR 7   ? E THR 7   
718 1 Y 1 E ASP 8   ? E ASP 8   
719 1 Y 1 E GLN 9   ? E GLN 9   
720 1 Y 1 E SER 10  ? E SER 10  
721 1 Y 1 E PHE 11  ? E PHE 11  
722 1 Y 1 E SER 12  ? E SER 12  
723 1 Y 1 E ALA 13  ? E ALA 13  
724 1 Y 1 E GLU 14  ? E GLU 14  
725 1 Y 1 E THR 15  ? E THR 15  
726 1 Y 1 E SER 16  ? E SER 16  
727 1 Y 1 E GLU 17  ? E GLU 17  
728 1 Y 1 E GLY 18  ? E GLY 18  
# 
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  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GDP PB     P  N N 135 
GDP O1B    O  N N 136 
GDP O2B    O  N N 137 
GDP O3B    O  N N 138 
GDP O3A    O  N N 139 
GDP PA     P  N N 140 
GDP O1A    O  N N 141 
GDP O2A    O  N N 142 
GDP "O5'"  O  N N 143 
GDP "C5'"  C  N N 144 
GDP "C4'"  C  N R 145 
GDP "O4'"  O  N N 146 
GDP "C3'"  C  N S 147 
GDP "O3'"  O  N N 148 
GDP "C2'"  C  N R 149 
GDP "O2'"  O  N N 150 
GDP "C1'"  C  N R 151 
GDP N9     N  Y N 152 
GDP C8     C  Y N 153 
GDP N7     N  Y N 154 
GDP C5     C  Y N 155 
GDP C6     C  N N 156 
GDP O6     O  N N 157 
GDP N1     N  N N 158 
GDP C2     C  N N 159 
GDP N2     N  N N 160 
GDP N3     N  N N 161 
GDP C4     C  Y N 162 
GDP HOB2   H  N N 163 
GDP HOB3   H  N N 164 
GDP HOA2   H  N N 165 
GDP "H5'"  H  N N 166 
GDP "H5''" H  N N 167 
GDP "H4'"  H  N N 168 
GDP "H3'"  H  N N 169 
GDP "HO3'" H  N N 170 
GDP "H2'"  H  N N 171 
GDP "HO2'" H  N N 172 
GDP "H1'"  H  N N 173 
GDP H8     H  N N 174 
GDP HN1    H  N N 175 
GDP HN21   H  N N 176 
GDP HN22   H  N N 177 
GLN N      N  N N 178 
GLN CA     C  N S 179 
GLN C      C  N N 180 
GLN O      O  N N 181 
GLN CB     C  N N 182 
GLN CG     C  N N 183 
GLN CD     C  N N 184 
GLN OE1    O  N N 185 
GLN NE2    N  N N 186 
GLN OXT    O  N N 187 
GLN H      H  N N 188 
GLN H2     H  N N 189 
GLN HA     H  N N 190 
GLN HB2    H  N N 191 
GLN HB3    H  N N 192 
GLN HG2    H  N N 193 
GLN HG3    H  N N 194 
GLN HE21   H  N N 195 
GLN HE22   H  N N 196 
GLN HXT    H  N N 197 
GLU N      N  N N 198 
GLU CA     C  N S 199 
GLU C      C  N N 200 
GLU O      O  N N 201 
GLU CB     C  N N 202 
GLU CG     C  N N 203 
GLU CD     C  N N 204 
GLU OE1    O  N N 205 
GLU OE2    O  N N 206 
GLU OXT    O  N N 207 
GLU H      H  N N 208 
GLU H2     H  N N 209 
GLU HA     H  N N 210 
GLU HB2    H  N N 211 
GLU HB3    H  N N 212 
GLU HG2    H  N N 213 
GLU HG3    H  N N 214 
GLU HE2    H  N N 215 
GLU HXT    H  N N 216 
GLY N      N  N N 217 
GLY CA     C  N N 218 
GLY C      C  N N 219 
GLY O      O  N N 220 
GLY OXT    O  N N 221 
GLY H      H  N N 222 
GLY H2     H  N N 223 
GLY HA2    H  N N 224 
GLY HA3    H  N N 225 
GLY HXT    H  N N 226 
HIS N      N  N N 227 
HIS CA     C  N S 228 
HIS C      C  N N 229 
HIS O      O  N N 230 
HIS CB     C  N N 231 
HIS CG     C  Y N 232 
HIS ND1    N  Y N 233 
HIS CD2    C  Y N 234 
HIS CE1    C  Y N 235 
HIS NE2    N  Y N 236 
HIS OXT    O  N N 237 
HIS H      H  N N 238 
HIS H2     H  N N 239 
HIS HA     H  N N 240 
HIS HB2    H  N N 241 
HIS HB3    H  N N 242 
HIS HD1    H  N N 243 
HIS HD2    H  N N 244 
HIS HE1    H  N N 245 
HIS HE2    H  N N 246 
HIS HXT    H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
MG  MG     MG N N 337 
PHE N      N  N N 338 
PHE CA     C  N S 339 
PHE C      C  N N 340 
PHE O      O  N N 341 
PHE CB     C  N N 342 
PHE CG     C  Y N 343 
PHE CD1    C  Y N 344 
PHE CD2    C  Y N 345 
PHE CE1    C  Y N 346 
PHE CE2    C  Y N 347 
PHE CZ     C  Y N 348 
PHE OXT    O  N N 349 
PHE H      H  N N 350 
PHE H2     H  N N 351 
PHE HA     H  N N 352 
PHE HB2    H  N N 353 
PHE HB3    H  N N 354 
PHE HD1    H  N N 355 
PHE HD2    H  N N 356 
PHE HE1    H  N N 357 
PHE HE2    H  N N 358 
PHE HZ     H  N N 359 
PHE HXT    H  N N 360 
PRO N      N  N N 361 
PRO CA     C  N S 362 
PRO C      C  N N 363 
PRO O      O  N N 364 
PRO CB     C  N N 365 
PRO CG     C  N N 366 
PRO CD     C  N N 367 
PRO OXT    O  N N 368 
PRO H      H  N N 369 
PRO HA     H  N N 370 
PRO HB2    H  N N 371 
PRO HB3    H  N N 372 
PRO HG2    H  N N 373 
PRO HG3    H  N N 374 
PRO HD2    H  N N 375 
PRO HD3    H  N N 376 
PRO HXT    H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TTP PA     P  N S 436 
TTP O1A    O  N N 437 
TTP O2A    O  N N 438 
TTP O3A    O  N N 439 
TTP PB     P  N S 440 
TTP O1B    O  N N 441 
TTP O2B    O  N N 442 
TTP O3B    O  N N 443 
TTP PG     P  N N 444 
TTP O1G    O  N N 445 
TTP O2G    O  N N 446 
TTP O3G    O  N N 447 
TTP "O5'"  O  N N 448 
TTP "C5'"  C  N N 449 
TTP "C4'"  C  N R 450 
TTP "O4'"  O  N N 451 
TTP "C3'"  C  N S 452 
TTP "O3'"  O  N N 453 
TTP "C2'"  C  N N 454 
TTP "C1'"  C  N R 455 
TTP N1     N  N N 456 
TTP C2     C  N N 457 
TTP O2     O  N N 458 
TTP N3     N  N N 459 
TTP C4     C  N N 460 
TTP O4     O  N N 461 
TTP C5     C  N N 462 
TTP C5M    C  N N 463 
TTP C6     C  N N 464 
TTP HOA2   H  N N 465 
TTP HOB2   H  N N 466 
TTP HOG2   H  N N 467 
TTP HOG3   H  N N 468 
TTP "H5'1" H  N N 469 
TTP "H5'2" H  N N 470 
TTP "H4'"  H  N N 471 
TTP "H3'"  H  N N 472 
TTP "HO3'" H  N N 473 
TTP "H2'1" H  N N 474 
TTP "H2'2" H  N N 475 
TTP "H1'"  H  N N 476 
TTP HN3    H  N N 477 
TTP HM51   H  N N 478 
TTP HM52   H  N N 479 
TTP HM53   H  N N 480 
TTP H6     H  N N 481 
TYR N      N  N N 482 
TYR CA     C  N S 483 
TYR C      C  N N 484 
TYR O      O  N N 485 
TYR CB     C  N N 486 
TYR CG     C  Y N 487 
TYR CD1    C  Y N 488 
TYR CD2    C  Y N 489 
TYR CE1    C  Y N 490 
TYR CE2    C  Y N 491 
TYR CZ     C  Y N 492 
TYR OH     O  N N 493 
TYR OXT    O  N N 494 
TYR H      H  N N 495 
TYR H2     H  N N 496 
TYR HA     H  N N 497 
TYR HB2    H  N N 498 
TYR HB3    H  N N 499 
TYR HD1    H  N N 500 
TYR HD2    H  N N 501 
TYR HE1    H  N N 502 
TYR HE2    H  N N 503 
TYR HH     H  N N 504 
TYR HXT    H  N N 505 
VAL N      N  N N 506 
VAL CA     C  N S 507 
VAL C      C  N N 508 
VAL O      O  N N 509 
VAL CB     C  N N 510 
VAL CG1    C  N N 511 
VAL CG2    C  N N 512 
VAL OXT    O  N N 513 
VAL H      H  N N 514 
VAL H2     H  N N 515 
VAL HA     H  N N 516 
VAL HB     H  N N 517 
VAL HG11   H  N N 518 
VAL HG12   H  N N 519 
VAL HG13   H  N N 520 
VAL HG21   H  N N 521 
VAL HG22   H  N N 522 
VAL HG23   H  N N 523 
VAL HXT    H  N N 524 
# 
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  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GDP PB    O1B    doub N N 132 
GDP PB    O2B    sing N N 133 
GDP PB    O3B    sing N N 134 
GDP PB    O3A    sing N N 135 
GDP O2B   HOB2   sing N N 136 
GDP O3B   HOB3   sing N N 137 
GDP O3A   PA     sing N N 138 
GDP PA    O1A    doub N N 139 
GDP PA    O2A    sing N N 140 
GDP PA    "O5'"  sing N N 141 
GDP O2A   HOA2   sing N N 142 
GDP "O5'" "C5'"  sing N N 143 
GDP "C5'" "C4'"  sing N N 144 
GDP "C5'" "H5'"  sing N N 145 
GDP "C5'" "H5''" sing N N 146 
GDP "C4'" "O4'"  sing N N 147 
GDP "C4'" "C3'"  sing N N 148 
GDP "C4'" "H4'"  sing N N 149 
GDP "O4'" "C1'"  sing N N 150 
GDP "C3'" "O3'"  sing N N 151 
GDP "C3'" "C2'"  sing N N 152 
GDP "C3'" "H3'"  sing N N 153 
GDP "O3'" "HO3'" sing N N 154 
GDP "C2'" "O2'"  sing N N 155 
GDP "C2'" "C1'"  sing N N 156 
GDP "C2'" "H2'"  sing N N 157 
GDP "O2'" "HO2'" sing N N 158 
GDP "C1'" N9     sing N N 159 
GDP "C1'" "H1'"  sing N N 160 
GDP N9    C8     sing Y N 161 
GDP N9    C4     sing Y N 162 
GDP C8    N7     doub Y N 163 
GDP C8    H8     sing N N 164 
GDP N7    C5     sing Y N 165 
GDP C5    C6     sing N N 166 
GDP C5    C4     doub Y N 167 
GDP C6    O6     doub N N 168 
GDP C6    N1     sing N N 169 
GDP N1    C2     sing N N 170 
GDP N1    HN1    sing N N 171 
GDP C2    N2     sing N N 172 
GDP C2    N3     doub N N 173 
GDP N2    HN21   sing N N 174 
GDP N2    HN22   sing N N 175 
GDP N3    C4     sing N N 176 
GLN N     CA     sing N N 177 
GLN N     H      sing N N 178 
GLN N     H2     sing N N 179 
GLN CA    C      sing N N 180 
GLN CA    CB     sing N N 181 
GLN CA    HA     sing N N 182 
GLN C     O      doub N N 183 
GLN C     OXT    sing N N 184 
GLN CB    CG     sing N N 185 
GLN CB    HB2    sing N N 186 
GLN CB    HB3    sing N N 187 
GLN CG    CD     sing N N 188 
GLN CG    HG2    sing N N 189 
GLN CG    HG3    sing N N 190 
GLN CD    OE1    doub N N 191 
GLN CD    NE2    sing N N 192 
GLN NE2   HE21   sing N N 193 
GLN NE2   HE22   sing N N 194 
GLN OXT   HXT    sing N N 195 
GLU N     CA     sing N N 196 
GLU N     H      sing N N 197 
GLU N     H2     sing N N 198 
GLU CA    C      sing N N 199 
GLU CA    CB     sing N N 200 
GLU CA    HA     sing N N 201 
GLU C     O      doub N N 202 
GLU C     OXT    sing N N 203 
GLU CB    CG     sing N N 204 
GLU CB    HB2    sing N N 205 
GLU CB    HB3    sing N N 206 
GLU CG    CD     sing N N 207 
GLU CG    HG2    sing N N 208 
GLU CG    HG3    sing N N 209 
GLU CD    OE1    doub N N 210 
GLU CD    OE2    sing N N 211 
GLU OE2   HE2    sing N N 212 
GLU OXT   HXT    sing N N 213 
GLY N     CA     sing N N 214 
GLY N     H      sing N N 215 
GLY N     H2     sing N N 216 
GLY CA    C      sing N N 217 
GLY CA    HA2    sing N N 218 
GLY CA    HA3    sing N N 219 
GLY C     O      doub N N 220 
GLY C     OXT    sing N N 221 
GLY OXT   HXT    sing N N 222 
HIS N     CA     sing N N 223 
HIS N     H      sing N N 224 
HIS N     H2     sing N N 225 
HIS CA    C      sing N N 226 
HIS CA    CB     sing N N 227 
HIS CA    HA     sing N N 228 
HIS C     O      doub N N 229 
HIS C     OXT    sing N N 230 
HIS CB    CG     sing N N 231 
HIS CB    HB2    sing N N 232 
HIS CB    HB3    sing N N 233 
HIS CG    ND1    sing Y N 234 
HIS CG    CD2    doub Y N 235 
HIS ND1   CE1    doub Y N 236 
HIS ND1   HD1    sing N N 237 
HIS CD2   NE2    sing Y N 238 
HIS CD2   HD2    sing N N 239 
HIS CE1   NE2    sing Y N 240 
HIS CE1   HE1    sing N N 241 
HIS NE2   HE2    sing N N 242 
HIS OXT   HXT    sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
THR N     CA     sing N N 382 
THR N     H      sing N N 383 
THR N     H2     sing N N 384 
THR CA    C      sing N N 385 
THR CA    CB     sing N N 386 
THR CA    HA     sing N N 387 
THR C     O      doub N N 388 
THR C     OXT    sing N N 389 
THR CB    OG1    sing N N 390 
THR CB    CG2    sing N N 391 
THR CB    HB     sing N N 392 
THR OG1   HG1    sing N N 393 
THR CG2   HG21   sing N N 394 
THR CG2   HG22   sing N N 395 
THR CG2   HG23   sing N N 396 
THR OXT   HXT    sing N N 397 
TRP N     CA     sing N N 398 
TRP N     H      sing N N 399 
TRP N     H2     sing N N 400 
TRP CA    C      sing N N 401 
TRP CA    CB     sing N N 402 
TRP CA    HA     sing N N 403 
TRP C     O      doub N N 404 
TRP C     OXT    sing N N 405 
TRP CB    CG     sing N N 406 
TRP CB    HB2    sing N N 407 
TRP CB    HB3    sing N N 408 
TRP CG    CD1    doub Y N 409 
TRP CG    CD2    sing Y N 410 
TRP CD1   NE1    sing Y N 411 
TRP CD1   HD1    sing N N 412 
TRP CD2   CE2    doub Y N 413 
TRP CD2   CE3    sing Y N 414 
TRP NE1   CE2    sing Y N 415 
TRP NE1   HE1    sing N N 416 
TRP CE2   CZ2    sing Y N 417 
TRP CE3   CZ3    doub Y N 418 
TRP CE3   HE3    sing N N 419 
TRP CZ2   CH2    doub Y N 420 
TRP CZ2   HZ2    sing N N 421 
TRP CZ3   CH2    sing Y N 422 
TRP CZ3   HZ3    sing N N 423 
TRP CH2   HH2    sing N N 424 
TRP OXT   HXT    sing N N 425 
TTP PA    O1A    doub N N 426 
TTP PA    O2A    sing N N 427 
TTP PA    O3A    sing N N 428 
TTP PA    "O5'"  sing N N 429 
TTP O2A   HOA2   sing N N 430 
TTP O3A   PB     sing N N 431 
TTP PB    O1B    doub N N 432 
TTP PB    O2B    sing N N 433 
TTP PB    O3B    sing N N 434 
TTP O2B   HOB2   sing N N 435 
TTP O3B   PG     sing N N 436 
TTP PG    O1G    doub N N 437 
TTP PG    O2G    sing N N 438 
TTP PG    O3G    sing N N 439 
TTP O2G   HOG2   sing N N 440 
TTP O3G   HOG3   sing N N 441 
TTP "O5'" "C5'"  sing N N 442 
TTP "C5'" "C4'"  sing N N 443 
TTP "C5'" "H5'1" sing N N 444 
TTP "C5'" "H5'2" sing N N 445 
TTP "C4'" "O4'"  sing N N 446 
TTP "C4'" "C3'"  sing N N 447 
TTP "C4'" "H4'"  sing N N 448 
TTP "O4'" "C1'"  sing N N 449 
TTP "C3'" "O3'"  sing N N 450 
TTP "C3'" "C2'"  sing N N 451 
TTP "C3'" "H3'"  sing N N 452 
TTP "O3'" "HO3'" sing N N 453 
TTP "C2'" "C1'"  sing N N 454 
TTP "C2'" "H2'1" sing N N 455 
TTP "C2'" "H2'2" sing N N 456 
TTP "C1'" N1     sing N N 457 
TTP "C1'" "H1'"  sing N N 458 
TTP N1    C2     sing N N 459 
TTP N1    C6     sing N N 460 
TTP C2    O2     doub N N 461 
TTP C2    N3     sing N N 462 
TTP N3    C4     sing N N 463 
TTP N3    HN3    sing N N 464 
TTP C4    O4     doub N N 465 
TTP C4    C5     sing N N 466 
TTP C5    C5M    sing N N 467 
TTP C5    C6     doub N N 468 
TTP C5M   HM51   sing N N 469 
TTP C5M   HM52   sing N N 470 
TTP C5M   HM53   sing N N 471 
TTP C6    H6     sing N N 472 
TYR N     CA     sing N N 473 
TYR N     H      sing N N 474 
TYR N     H2     sing N N 475 
TYR CA    C      sing N N 476 
TYR CA    CB     sing N N 477 
TYR CA    HA     sing N N 478 
TYR C     O      doub N N 479 
TYR C     OXT    sing N N 480 
TYR CB    CG     sing N N 481 
TYR CB    HB2    sing N N 482 
TYR CB    HB3    sing N N 483 
TYR CG    CD1    doub Y N 484 
TYR CG    CD2    sing Y N 485 
TYR CD1   CE1    sing Y N 486 
TYR CD1   HD1    sing N N 487 
TYR CD2   CE2    doub Y N 488 
TYR CD2   HD2    sing N N 489 
TYR CE1   CZ     doub Y N 490 
TYR CE1   HE1    sing N N 491 
TYR CE2   CZ     sing Y N 492 
TYR CE2   HE2    sing N N 493 
TYR CZ    OH     sing N N 494 
TYR OH    HH     sing N N 495 
TYR OXT   HXT    sing N N 496 
VAL N     CA     sing N N 497 
VAL N     H      sing N N 498 
VAL N     H2     sing N N 499 
VAL CA    C      sing N N 500 
VAL CA    CB     sing N N 501 
VAL CA    HA     sing N N 502 
VAL C     O      doub N N 503 
VAL C     OXT    sing N N 504 
VAL CB    CG1    sing N N 505 
VAL CB    CG2    sing N N 506 
VAL CB    HB     sing N N 507 
VAL CG1   HG11   sing N N 508 
VAL CG1   HG12   sing N N 509 
VAL CG1   HG13   sing N N 510 
VAL CG2   HG21   sing N N 511 
VAL CG2   HG22   sing N N 512 
VAL CG2   HG23   sing N N 513 
VAL OXT   HXT    sing N N 514 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-22 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BXT 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              
'TrxA focus-classified model for pre-reduction condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_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          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_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          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_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         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
MASKING                    ? 3  ? ? ? ?               ? 
'CTF CORRECTION'           ? 4  1 ? ? ?               ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?               ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?               ? 
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF ChimeraX' ? 
OTHER                      ? 8  ? ? ? ?               ? 
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? cryoSPARC       ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? cryoSPARC       ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? cryoSPARC       ? 
'MODEL REFINEMENT'         ? 13 ? 1 ? ?               ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' MCB-1942668 1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1719875 2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
1 'experimental model' PDB       9BXC 
2 'in silico model'    AlphaFold ?    
# 
_atom_sites.entry_id                    9BXT 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 104.792 114.061 98.366  1.00 66.72  ? 6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.915 114.906 97.987  1.00 69.66  ? 6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.479 115.925 96.936  1.00 71.51  ? 6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.567 115.662 96.151  1.00 68.97  ? 6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 107.105 114.059 97.483  1.00 70.94  ? 6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 107.427 112.956 98.479  1.00 69.01  ? 6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 106.806 113.470 96.114  1.00 68.04  ? 6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.112 117.096 96.935  1.00 67.79  ? 7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.782 118.107 95.927  1.00 62.41  ? 7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.220 117.674 94.539  1.00 61.32  ? 7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.122 116.848 94.375  1.00 65.31  ? 7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.558 119.345 96.395  1.00 60.86  ? 7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.904 119.069 97.831  1.00 60.79  ? 7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 107.107 117.594 97.898  1.00 63.21  ? 7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.558 118.243 93.529  1.00 62.02  ? 8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.849 117.870 92.149  1.00 62.33  ? 8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.281 118.203 91.757  1.00 63.56  ? 8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.949 117.395 91.103  1.00 63.71  ? 8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.874 118.565 91.196  1.00 60.47  ? 8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.890 118.000 89.785  1.00 62.20  ? 8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.053 118.843 88.839  1.00 65.94  ? 8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.518 118.680 87.401  1.00 63.30  ? 8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 103.374 118.591 86.451  1.00 59.19  ? 8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.769 119.385 92.139  1.00 64.75  ? 9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.133 119.764 91.788  1.00 61.30  ? 9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.160 118.890 92.495  1.00 61.23  ? 9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.164 118.498 91.890  1.00 64.30  ? 9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.376 121.235 92.118  1.00 61.40  ? 9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.050 121.622 93.528  1.00 57.27  ? 9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.896 121.601 94.596  1.00 54.61  ? 9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.796 122.106 94.022  1.00 60.05  ? 9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.247 122.034 95.725  1.00 54.53  ? 9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.955 122.350 95.400  1.00 58.13  ? 9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.551 122.351 93.434  1.00 59.35  ? 9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.920 122.827 96.198  1.00 58.79  ? 9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.525 122.824 94.229  1.00 62.76  ? 9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.716 123.057 95.595  1.00 64.17  ? 9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.930 118.580 93.771  1.00 65.25  ? 10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.842 117.702 94.497  1.00 63.67  ? 10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.819 116.304 93.895  1.00 64.56  ? 10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.864 115.663 93.733  1.00 68.99  ? 10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.491 117.687 95.994  1.00 63.24  ? 10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.797 119.050 96.617  1.00 67.19  ? 10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 111.251 116.585 96.710  1.00 64.71  ? 10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.774 119.064 98.125  1.00 66.28  ? 10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.627 115.816 93.538  1.00 69.43  ? 11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.517 114.506 92.907  1.00 66.39  ? 11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 110.260 114.470 91.578  1.00 67.07  ? 11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.939 113.486 91.264  1.00 69.00  ? 11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.044 114.143 92.716  1.00 68.48  ? 11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.751 113.299 91.488  1.00 72.19  ? 11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.302 113.389 91.056  1.00 71.26  ? 11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.394 113.389 91.887  1.00 67.89  ? 11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 106.077 113.467 89.750  1.00 67.31  ? 11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.147 115.539 90.785  1.00 67.51  ? 12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.887 115.609 89.528  1.00 67.61  ? 12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.388 115.676 89.777  1.00 68.28  ? 12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.179 115.132 88.998  1.00 70.50  ? 12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.424 116.817 88.715  1.00 65.54  ? 12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.286 116.576 87.721  1.00 66.51  ? 12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.726 117.897 87.217  1.00 68.14  ? 12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.761 115.716 86.564  1.00 68.34  ? 12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.799 116.348 90.854  1.00 69.12  ? 13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.216 116.415 91.190  1.00 67.70  ? 13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.762 115.043 91.564  1.00 71.07  ? 13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 115.921 114.728 91.274  1.00 74.62  ? 13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.441 117.412 92.327  1.00 67.02  ? 13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.864 117.394 92.846  1.00 68.16  ? 13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.183 116.675 93.792  1.00 67.67  ? 13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.730 118.186 92.226  1.00 72.73  ? 13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.943 114.212 92.213  1.00 72.31  ? 14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.378 112.867 92.570  1.00 71.85  ? 14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.549 111.959 91.360  1.00 72.74  ? 14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 115.138 110.882 91.497  1.00 77.20  ? 14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.397 112.232 93.555  1.00 72.41  ? 14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.160 113.092 94.778  1.00 73.92  ? 14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 112.019 113.321 95.179  1.00 76.55  ? 14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 114.240 113.579 95.376  1.00 73.37  ? 14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.057 112.359 90.188  1.00 75.68  ? 15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.268 111.587 88.971  1.00 78.54  ? 15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.653 111.794 88.376  1.00 78.61  ? 15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.976 111.160 87.366  1.00 78.66  ? 15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.200 111.931 87.930  1.00 77.92  ? 15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.818 112.153 88.514  1.00 79.59  ? 15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.735 111.420 87.748  1.00 81.39  ? 15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 111.070 110.711 86.776  1.00 78.74  ? 15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.550 111.551 88.120  1.00 80.39  ? 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.469 112.670 88.968  1.00 78.78  ? 16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.853 112.814 88.528  1.00 79.04  ? 16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.607 111.508 88.739  1.00 77.00  ? 16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.335 111.038 87.857  1.00 78.29  ? 16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.532 113.982 89.268  1.00 80.76  ? 16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.900 115.319 88.870  1.00 74.37  ? 16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 120.029 113.988 89.000  1.00 79.12  ? 16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.434 115.902 87.586  1.00 74.11  ? 16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.431 110.895 89.911  1.00 78.29  ? 17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 119.128 109.659 90.244  1.00 80.32  ? 17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.454 108.417 89.678  1.00 80.53  ? 17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 119.074 107.347 89.675  1.00 79.82  ? 17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 119.257 109.523 91.762  1.00 79.64  ? 17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.672 110.805 92.458  1.00 80.88  ? 17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 121.409 111.201 92.191  1.00 92.51  ? 17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.192 110.149 93.410  1.00 81.01  ? 17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 117.213 108.519 89.206  1.00 80.80  ? 18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.568 107.396 88.538  1.00 81.52  ? 18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.206 107.262 87.162  1.00 82.75  ? 18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 116.985 108.092 86.274  1.00 83.07  ? 18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 115.041 107.577 88.451  1.00 81.00  ? 18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 114.398 107.272 89.805  1.00 79.90  ? 18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.449 106.662 87.390  1.00 79.43  ? 18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 113.384 108.297 90.252  1.00 80.83  ? 18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 118.023 106.227 86.990  1.00 85.59  ? 19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.852 106.100 85.801  1.00 84.68  ? 19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 118.115 105.332 84.713  1.00 86.89  ? 19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.644 104.212 84.939  1.00 87.36  ? 19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 120.163 105.398 86.149  1.00 84.19  ? 19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 121.198 106.308 86.791  1.00 83.60  ? 19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.614 105.967 86.375  1.00 86.31  ? 19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 123.016 106.215 85.240  1.00 87.08  ? 19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.380 105.396 87.297  1.00 84.26  ? 19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 118.015 105.937 83.534  1.00 91.62  ? 20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.448 105.296 82.356  1.00 92.85  ? 20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.516 105.227 81.275  1.00 93.61  ? 20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 119.220 106.213 81.030  1.00 90.03  ? 20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.206 106.044 81.857  1.00 91.33  ? 20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 116.440 107.501 81.498  1.00 92.56  ? 20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.583 107.925 80.318  1.00 93.30  ? 20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 115.991 107.188 79.054  1.00 92.94  ? 20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.461 107.257 78.836  1.00 92.57  ? 20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.648 104.054 80.652  1.00 94.77  ? 21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.672 103.796 79.639  1.00 95.05  ? 21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 121.078 104.024 80.194  1.00 94.89  ? 21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.997 104.399 79.461  1.00 92.13  ? 21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 119.438 104.644 78.383  1.00 95.60  ? 21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 120.166 104.103 77.166  1.00 95.15  ? 21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 119.720 103.075 76.613  1.00 93.81  ? 21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 121.181 104.707 76.759  1.00 94.95  ? 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 121.254 103.802 81.495  1.00 90.47  ? 22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.557 103.936 82.111  1.00 88.25  ? 22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 123.031 105.353 82.332  1.00 88.35  ? 22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 124.191 105.549 82.703  1.00 86.80  ? 22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 122.175 106.350 82.117  1.00 88.20  ? 23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.546 107.751 82.253  1.00 85.56  ? 23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.592 108.450 83.210  1.00 85.99  ? 23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.391 108.161 83.227  1.00 86.88  ? 23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.531 108.465 80.896  1.00 85.01  ? 23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 122.866 107.575 79.710  1.00 89.09  ? 23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 124.330 107.170 79.706  1.00 88.31  ? 23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 125.219 108.313 79.257  1.00 86.05  ? 23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.564 109.145 78.210  1.00 84.85  ? 23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 122.132 109.369 84.007  1.00 77.81  ? 24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.302 110.176 84.889  1.00 75.23  ? 24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.394 111.086 84.072  1.00 77.80  ? 24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 120.785 111.600 83.020  1.00 76.42  ? 24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.172 111.012 85.826  1.00 71.96  ? 24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.851 110.214 86.902  1.00 73.01  ? 24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.222 109.978 88.110  1.00 74.68  ? 24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 124.122 109.702 86.704  1.00 73.70  ? 24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.844 109.247 89.102  1.00 75.09  ? 24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.749 108.967 87.692  1.00 76.12  ? 24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 124.108 108.742 88.893  1.00 76.08  ? 24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.171 111.286 84.562  1.00 79.47  ? 25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.195 112.141 83.885  1.00 76.36  ? 25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.433 113.596 84.290  1.00 78.93  ? 25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.666 114.211 85.034  1.00 81.94  ? 25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.776 111.697 84.209  1.00 79.51  ? 25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.443 110.290 83.756  1.00 78.54  ? 25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 115.025 109.891 84.106  1.00 79.43  ? 25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.087 110.171 83.360  1.00 78.44  ? 25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.860 109.236 85.248  1.00 80.41  ? 25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.532 114.150 83.772  1.00 75.07  ? 26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 119.902 115.519 84.114  1.00 70.70  ? 26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.907 116.529 83.558  1.00 69.40  ? 26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.733 117.608 84.136  1.00 67.68  ? 26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.311 115.821 83.607  1.00 68.80  ? 26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.393 115.122 84.378  1.00 67.51  ? 26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.421 115.178 85.760  1.00 66.67  ? 26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.378 114.404 83.721  1.00 66.25  ? 26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.413 114.535 86.473  1.00 68.39  ? 26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.373 113.759 84.429  1.00 66.67  ? 26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.390 113.825 85.806  1.00 70.25  ? 26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.248 116.203 82.444  1.00 78.17  ? 27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.254 117.107 81.876  1.00 78.01  ? 27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.027 117.252 82.764  1.00 79.28  ? 27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.263 118.208 82.593  1.00 78.41  ? 27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.835 116.624 80.487  1.00 78.82  ? 27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.917 117.718 79.441  1.00 82.43  ? 27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 117.204 118.876 79.812  1.00 80.15  ? 27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.693 117.422 78.249  1.00 80.62  ? 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.817 116.326 83.703  1.00 75.78  ? 28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.705 116.446 84.639  1.00 76.00  ? 28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.858 117.641 85.569  1.00 76.71  ? 28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.860 118.102 86.133  1.00 78.00  ? 28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.569 115.166 85.465  1.00 74.64  ? 28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 113.992 113.986 84.701  1.00 77.78  ? 28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.480 113.928 84.831  1.00 78.18  ? 28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 111.835 113.429 83.551  1.00 76.83  ? 28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 112.190 114.278 82.380  1.00 75.56  ? 28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.082 118.145 85.747  1.00 72.97  ? 29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.293 119.259 86.666  1.00 71.75  ? 29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.623 120.532 86.167  1.00 69.87  ? 29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.027 121.269 86.956  1.00 70.97  ? 29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.787 119.485 86.885  1.00 71.70  ? 29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 118.121 119.799 88.330  1.00 71.39  ? 29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.365 119.364 89.224  1.00 69.88  ? 29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.143 120.474 88.573  1.00 70.82  ? 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.702 120.806 84.861  1.00 73.26  ? 30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 115.026 121.980 84.315  1.00 73.11  ? 30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.517 121.873 84.496  1.00 76.35  ? 30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.849 122.859 84.841  1.00 77.75  ? 30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.378 122.149 82.837  1.00 72.92  ? 30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 116.861 122.338 82.572  1.00 76.28  ? 30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 117.158 122.329 81.081  1.00 77.87  ? 30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 118.642 122.127 80.816  1.00 78.01  ? 30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 118.887 121.454 79.511  1.00 76.63  ? 30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.961 120.681 84.266  1.00 73.60  ? 31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.558 120.445 84.581  1.00 71.97  ? 31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.281 120.681 86.057  1.00 71.56  ? 31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.202 121.166 86.416  1.00 71.79  ? 31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.163 119.021 84.191  1.00 72.37  ? 31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.799 118.855 82.727  1.00 75.11  ? 31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.346 117.570 82.138  1.00 77.98  ? 31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.010 116.487 82.658  1.00 78.82  ? 31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 112.113 117.645 81.156  1.00 73.53  ? 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.243 120.353 86.924  1.00 62.95  ? 32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 112.074 120.623 88.346  1.00 61.92  ? 32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.995 122.120 88.621  1.00 64.23  ? 32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 111.175 122.556 89.433  1.00 65.53  ? 32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.207 119.983 89.146  1.00 63.51  ? 32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.829 122.925 87.954  1.00 64.37  ? 33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.752 124.376 88.133  1.00 60.08  ? 33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.406 124.897 87.652  1.00 60.57  ? 33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.772 125.733 88.308  1.00 64.66  ? 33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.907 125.088 87.403  1.00 61.97  ? 33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.735 126.596 87.501  1.00 61.90  ? 33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 115.240 124.675 87.959  1.00 63.28  ? 33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.963 124.430 86.482  1.00 64.58  ? 34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.689 124.896 85.940  1.00 65.81  ? 34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.537 124.550 86.876  1.00 68.41  ? 34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.680 125.395 87.166  1.00 70.74  ? 34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.461 124.294 84.554  1.00 69.17  ? 34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.640 125.158 83.649  1.00 69.74  ? 34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.400 125.644 84.008  1.00 71.06  ? 34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.879 125.623 82.400  1.00 69.83  ? 34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.912 126.371 83.019  1.00 71.98  ? 34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.790 126.374 82.031  1.00 71.75  ? 34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.509 123.309 87.367  1.00 66.93  ? 35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.458 122.894 88.289  1.00 62.76  ? 35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.522 123.691 89.584  1.00 63.12  ? 35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.497 124.168 90.082  1.00 67.50  ? 35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.571 121.396 88.570  1.00 63.01  ? 35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.786 121.025 89.688  1.00 67.11  ? 35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.726 123.850 90.142  1.00 60.24  ? 36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.892 124.617 91.370  1.00 59.27  ? 36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.329 126.017 91.214  1.00 56.73  ? 36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.485 126.451 92.006  1.00 58.27  ? 36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.373 124.674 91.747  1.00 56.27  ? 36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.665 125.419 93.028  1.00 53.87  ? 36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.090 125.030 94.229  1.00 58.68  ? 36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.521 126.512 93.037  1.00 55.82  ? 36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.361 125.707 95.401  1.00 57.16  ? 36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.794 127.195 94.202  1.00 59.96  ? 36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.212 126.789 95.382  1.00 59.40  ? 36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.481 127.468 96.548  1.00 60.34  ? 36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.750 126.725 90.166  1.00 60.59  ? 37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.262 128.080 89.956  1.00 61.03  ? 37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.750 128.093 89.797  1.00 67.33  ? 37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 106.043 128.676 90.624  1.00 69.93  ? 37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.958 128.710 88.751  1.00 60.48  ? 37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.181 129.495 89.119  1.00 65.70  ? 37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 111.414 128.877 89.205  1.00 65.49  ? 37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 110.091 130.845 89.405  1.00 64.10  ? 37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 112.537 129.594 89.556  1.00 62.74  ? 37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 111.211 131.567 89.755  1.00 65.75  ? 37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.436 130.941 89.830  1.00 64.68  ? 37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.235 127.357 88.806  1.00 70.51  ? 38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.819 127.441 88.456  1.00 69.40  ? 38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.934 127.076 89.644  1.00 68.49  ? 38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.908 127.723 89.889  1.00 70.02  ? 38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.525 126.552 87.233  1.00 68.13  ? 38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 103.029 126.330 87.073  1.00 71.66  ? 38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 105.112 127.173 85.978  1.00 64.15  ? 38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.316 126.055 90.413  1.00 65.82  ? 39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.436 125.547 91.456  1.00 70.26  ? 39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.634 126.209 92.813  1.00 72.31  ? 39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.703 126.195 93.626  1.00 74.80  ? 39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.617 124.033 91.601  1.00 69.32  ? 39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.557 123.309 90.270  1.00 72.92  ? 39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.878 123.809 89.349  1.00 72.15  ? 39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.187 122.238 90.145  1.00 74.82  ? 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.804 126.785 93.093  1.00 67.09  ? 40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.064 127.380 94.396  1.00 67.39  ? 40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.357 128.869 94.310  1.00 72.44  ? 40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.715 129.665 95.006  1.00 73.70  ? 40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.239 126.643 95.062  1.00 61.70  ? 40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.446 126.938 96.533  1.00 63.55  ? 40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.445 127.514 97.301  1.00 66.16  ? 40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.648 126.632 97.152  1.00 67.06  ? 40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.640 127.778 98.644  1.00 70.26  ? 40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.854 126.892 98.491  1.00 68.13  ? 40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.847 127.466 99.233  1.00 72.19  ? 40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 107.047 127.727 100.568 1.00 70.60  ? 40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.293 129.272 93.451  1.00 64.93  ? 41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.801 130.636 93.488  1.00 59.65  ? 41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.785 131.603 92.903  1.00 62.39  ? 41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.329 132.529 93.581  1.00 68.97  ? 41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.150 130.716 92.749  1.00 62.86  ? 41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.189 129.821 93.429  1.00 63.14  ? 41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.645 132.147 92.689  1.00 61.63  ? 41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.317 130.050 94.913  1.00 58.66  ? 41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.387 131.381 91.647  1.00 61.71  ? 42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.437 132.279 91.000  1.00 67.21  ? 42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.135 132.378 91.781  1.00 70.80  ? 42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.454 133.410 91.727  1.00 70.10  ? 42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.167 131.812 89.571  1.00 66.63  ? 42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.426 131.745 88.732  1.00 68.49  ? 42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.459 132.302 89.101  1.00 71.56  ? 42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.346 131.060 87.597  1.00 70.03  ? 42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.770 131.322 92.509  1.00 72.76  ? 43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.584 131.375 93.353  1.00 70.78  ? 43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.825 132.149 94.644  1.00 71.92  ? 43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.933 132.875 95.096  1.00 72.54  ? 43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.105 129.958 93.673  1.00 69.36  ? 43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.245 128.981 92.519  1.00 71.62  ? 43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.541 129.457 91.264  1.00 75.15  ? 43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 99.397  129.907 91.312  1.00 72.70  ? 43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 101.227 129.365 90.131  1.00 76.02  ? 43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.009 132.016 95.250  1.00 67.05  ? 44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.282 132.617 96.550  1.00 68.17  ? 44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.246 133.799 96.480  1.00 66.87  ? 44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.979 134.048 97.442  1.00 69.42  ? 44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 103.811 131.568 97.531  1.00 65.30  ? 44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.944 130.325 97.586  1.00 70.11  ? 44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 102.152 130.063 96.685  1.00 71.14  ? 44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.076 129.564 98.665  1.00 70.45  ? 44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.267 134.529 95.369  1.00 62.86  ? 45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.935 135.824 95.308  1.00 66.54  ? 45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.893 136.930 95.243  1.00 67.01  ? 45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.973 136.877 94.419  1.00 66.99  ? 45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.883 135.931 94.110  1.00 65.65  ? 45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 105.158 135.733 92.889  1.00 65.48  ? 45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 107.035 134.949 94.228  1.00 68.25  ? 45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.041 137.926 96.114  1.00 64.32  ? 46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.119 139.055 96.131  1.00 63.06  ? 46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.327 139.871 94.863  1.00 64.94  ? 46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.433 140.355 94.594  1.00 65.60  ? 46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.324 139.914 97.384  1.00 61.48  ? 46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.234 140.967 97.488  1.00 66.10  ? 46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.352 139.044 98.625  1.00 62.35  ? 46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.266 140.025 94.078  1.00 69.39  ? 47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.316 140.780 92.837  1.00 71.29  ? 47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.531 142.072 93.000  1.00 74.11  ? 47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.411 142.070 93.522  1.00 73.57  ? 47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.755 139.969 91.665  1.00 72.33  ? 47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 101.925 140.638 90.331  1.00 76.19  ? 47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.189 140.854 89.806  1.00 73.04  ? 47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.822 141.053 89.603  1.00 73.31  ? 47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 103.350 141.471 88.580  1.00 71.76  ? 47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 100.977 141.670 88.376  1.00 71.80  ? 47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 102.242 141.879 87.864  1.00 70.80  ? 47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.126 143.172 92.551  1.00 70.03  ? 48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.534 144.494 92.660  1.00 67.26  ? 48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.192 145.015 91.272  1.00 69.74  ? 48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.756 144.571 90.268  1.00 70.05  ? 48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.477 145.469 93.375  1.00 66.66  ? 48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.918 145.003 94.736  1.00 70.56  ? 48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 103.969 144.111 94.878  1.00 68.43  ? 48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 102.288 145.471 95.877  1.00 71.78  ? 48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 104.375 143.691 96.130  1.00 64.36  ? 48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 102.689 145.053 97.130  1.00 69.40  ? 48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.735 144.162 97.256  1.00 65.20  ? 48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.250 145.961 91.228  1.00 75.54  ? 49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.782  146.487 89.950  1.00 78.28  ? 49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.904 147.159 89.170  1.00 78.31  ? 49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.882 147.170 87.933  1.00 79.18  ? 49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.633  147.470 90.179  1.00 77.63  ? 49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.367  146.821 90.649  1.00 80.66  ? 49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.334  145.547 91.173  1.00 79.67  ? 49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.092  147.274 90.679  1.00 79.58  ? 49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.091  145.241 91.503  1.00 76.12  ? 49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.319  146.272 91.214  1.00 77.40  ? 49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.889 147.719 89.867  1.00 70.90  ? 50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.035 148.340 89.223  1.00 71.44  ? 50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.200 148.361 90.204  1.00 71.71  ? 50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.045 148.070 91.392  1.00 72.46  ? 50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.696 149.746 88.705  1.00 70.91  ? 50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.379 150.733 89.819  1.00 72.53  ? 50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.362 150.384 90.998  1.00 70.49  ? 50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 102.126 151.980 89.440  1.00 73.66  ? 50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.382 148.699 89.683  1.00 62.49  ? 51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.568 148.762 90.530  1.00 64.61  ? 51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.450 149.856 91.581  1.00 67.05  ? 51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.028 149.737 92.667  1.00 67.75  ? 51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.814 148.979 89.673  1.00 64.87  ? 51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.156 149.041 90.403  1.00 63.01  ? 51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.387 147.779 91.216  1.00 61.20  ? 51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.288 149.265 89.419  1.00 65.27  ? 51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.712 150.927 91.280  1.00 67.15  ? 52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.538 152.003 92.250  1.00 65.44  ? 52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.833 151.505 93.505  1.00 67.82  ? 52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.257 151.808 94.627  1.00 67.18  ? 52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 104.756 153.154 91.618  1.00 67.04  ? 52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.619 154.378 92.504  1.00 68.15  ? 52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.976 154.867 92.977  1.00 71.57  ? 52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.857 156.191 93.710  1.00 68.13  ? 52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 105.907 157.342 92.769  1.00 65.10  ? 52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.759 150.731 93.332  1.00 75.56  ? 53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.041 150.195 94.484  1.00 74.41  ? 53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.918 149.240 95.280  1.00 72.61  ? 53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.892 149.250 96.516  1.00 72.21  ? 53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.761 149.496 94.026  1.00 73.63  ? 53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.803 149.154 95.154  1.00 73.46  ? 53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.647  148.290 94.695  1.00 77.58  ? 53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.628  147.901 93.507  1.00 78.00  ? 53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 98.756  147.999 95.519  1.00 75.50  ? 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.704 148.411 94.592  1.00 66.68  ? 54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.591 147.483 95.286  1.00 68.35  ? 54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.638 148.228 96.103  1.00 62.93  ? 54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.898 147.887 97.263  1.00 65.14  ? 54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.265 146.550 94.280  1.00 67.52  ? 54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.369 145.706 94.882  1.00 64.73  ? 54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.902 144.701 93.883  1.00 64.15  ? 54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.767 143.660 94.564  1.00 64.59  ? 54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.873 142.417 93.755  1.00 68.72  ? 54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.255 149.250 95.508  1.00 62.77  ? 55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.267 150.019 96.223  1.00 63.12  ? 55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.663 150.748 97.415  1.00 67.05  ? 55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.260 150.779 98.498  1.00 69.94  ? 55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.941 151.008 95.273  1.00 65.17  ? 55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.847 150.403 94.199  1.00 66.38  ? 55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.379 151.492 93.286  1.00 63.80  ? 55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.988 149.618 94.827  1.00 62.41  ? 55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.478 151.338 97.239  1.00 71.43  ? 56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.822 152.009 98.356  1.00 68.85  ? 56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.490 151.025 99.470  1.00 68.23  ? 56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.697 151.323 100.651 1.00 67.72  ? 56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.562 152.724 97.871  1.00 69.78  ? 56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 104.868 153.857 96.912  1.00 74.08  ? 56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 103.975 154.700 96.680  1.00 73.49  ? 56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 106.004 153.909 96.395  1.00 72.11  ? 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.989 149.841 99.112  1.00 67.84  ? 57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.673 148.831 100.116 1.00 67.33  ? 57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.922 148.388 100.864 1.00 69.48  ? 57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.888 148.199 102.085 1.00 74.85  ? 57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.988 147.636 99.448  1.00 65.24  ? 57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.744 146.452 100.360 1.00 65.88  ? 57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 104.705 145.462 100.522 1.00 67.72  ? 57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 102.548 146.321 101.052 1.00 69.82  ? 57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 104.486 144.381 101.351 1.00 72.32  ? 57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 102.319 145.242 101.882 1.00 69.94  ? 57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.291 144.275 102.028 1.00 70.05  ? 57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.069 143.199 102.856 1.00 66.45  ? 57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.035 148.216 100.150 1.00 63.51  ? 58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.243 147.702 100.787 1.00 59.58  ? 58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.916 148.748 101.668 1.00 60.28  ? 58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.393 148.420 102.760 1.00 60.12  ? 58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.207 147.179 99.722  1.00 56.97  ? 58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.721 145.897 99.040  1.00 56.82  ? 58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.535 145.584 97.800  1.00 60.15  ? 58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.756 144.730 100.009 1.00 59.63  ? 58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.970 150.007 101.226 1.00 65.42  ? 59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.556 151.047 102.067 1.00 65.61  ? 59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.654 151.359 103.256 1.00 69.37  ? 59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.129 151.512 104.387 1.00 68.17  ? 59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.865 152.310 101.244 1.00 61.68  ? 59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.680 153.281 102.072 1.00 64.31  ? 59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.643 151.946 99.998  1.00 63.97  ? 59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.343 151.467 103.022 1.00 72.71  ? 60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.423 151.832 104.096 1.00 71.85  ? 60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.369 150.761 105.178 1.00 71.74  ? 60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.324 151.081 106.372 1.00 72.42  ? 60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 105.030 152.091 103.523 1.00 73.40  ? 60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.873 153.459 102.878 1.00 73.82  ? 60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.596 153.580 102.071 1.00 77.52  ? 60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.798 152.620 102.071 1.00 75.44  ? 60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.393 154.634 101.433 1.00 74.47  ? 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.371 149.487 104.787 1.00 67.28  ? 61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.317 148.385 105.740 1.00 67.10  ? 61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.678 148.046 106.336 1.00 69.26  ? 61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.842 146.950 106.887 1.00 68.85  ? 61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.710 147.144 105.081 1.00 68.44  ? 61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.259 147.344 104.696 1.00 73.92  ? 61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.822 148.464 104.432 1.00 70.54  ? 61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.499 146.256 104.670 1.00 73.50  ? 61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.644 148.960 106.228 1.00 67.15  ? 62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.972 148.799 106.824 1.00 66.85  ? 62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.676 147.549 106.301 1.00 66.69  ? 62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.402 146.871 107.030 1.00 67.55  ? 62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.893 148.779 108.354 1.00 68.40  ? 62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.013 149.870 108.955 1.00 69.84  ? 62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.273 151.241 108.358 1.00 70.57  ? 62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.418 151.673 108.238 1.00 69.93  ? 62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 108.203 151.933 107.981 1.00 68.76  ? 62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.457 147.239 105.023 1.00 67.83  ? 63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.220 146.189 104.360 1.00 64.88  ? 63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.455 146.734 103.664 1.00 66.27  ? 63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.489 146.058 103.631 1.00 68.94  ? 63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.348 145.451 103.339 1.00 61.75  ? 63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.313 144.533 103.947 1.00 66.95  ? 63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.684 143.496 104.792 1.00 63.36  ? 63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.964 144.695 103.663 1.00 66.47  ? 63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.739 142.653 105.344 1.00 63.44  ? 63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 107.013 143.858 104.210 1.00 66.11  ? 63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.405 142.839 105.050 1.00 68.41  ? 63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.458 142.003 105.595 1.00 70.80  ? 63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.371 147.941 103.112 1.00 59.32  ? 64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.488 148.592 102.447 1.00 53.96  ? 64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.855 149.876 103.173 1.00 58.38  ? 64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.015 150.503 103.827 1.00 60.18  ? 64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.161 148.925 100.988 1.00 54.71  ? 64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.185 147.746 100.051 1.00 55.06  ? 64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.674 146.514 100.461 1.00 55.75  ? 64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.727 147.870 98.749  1.00 56.55  ? 64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.698 145.437 99.600  1.00 54.81  ? 64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.749 146.804 97.883  1.00 55.68  ? 64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.234 145.589 98.312  1.00 56.18  ? 64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.251 144.527 97.441  1.00 57.03  ? 64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.121 150.258 103.058 1.00 65.93  ? 65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.547 151.582 103.486 1.00 66.73  ? 65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.111 152.615 102.456 1.00 66.51  ? 65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.089 152.343 101.253 1.00 64.79  ? 65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.062 151.628 103.673 1.00 64.59  ? 65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.593 150.615 104.672 1.00 63.23  ? 65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.105 150.627 104.761 1.00 69.66  ? 65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.762 150.717 103.703 1.00 71.91  ? 65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.638 150.543 105.888 1.00 67.13  ? 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.756 153.803 102.935 1.00 69.54  ? 66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.310 154.877 102.061 1.00 70.69  ? 66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.474 155.711 101.537 1.00 71.36  ? 66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.381 156.260 100.434 1.00 71.35  ? 66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.310 155.773 102.820 1.00 70.89  ? 66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.798 157.095 102.174 1.00 72.52  ? 66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 112.702 157.126 100.643 1.00 76.33  ? 66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 112.654 156.066 99.982  1.00 73.46  ? 66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.666 158.245 100.089 1.00 75.88  ? 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.584 155.773 102.277 1.00 70.95  ? 67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.684 156.660 101.907 1.00 71.50  ? 67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.298 156.277 100.565 1.00 73.01  ? 67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.612 157.154 99.752  1.00 72.60  ? 67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.746 156.659 103.008 1.00 71.43  ? 67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 119.128 155.276 103.521 1.00 74.75  ? 67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 120.340 154.703 102.810 1.00 76.28  ? 67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 121.177 155.495 102.329 1.00 72.00  ? 67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 120.453 153.461 102.731 1.00 73.97  ? 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.479 154.980 100.307 1.00 65.57  ? 68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.137 154.576 99.069  1.00 63.02  ? 68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.211 154.686 97.864  1.00 66.29  ? 68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.682 154.951 96.753  1.00 68.48  ? 68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.690 153.152 99.198  1.00 64.99  ? 68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.725 152.073 98.796  1.00 63.63  ? 68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.727 151.656 99.659  1.00 62.08  ? 68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.835 151.457 97.561  1.00 61.70  ? 68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 116.846 150.657 99.288  1.00 61.38  ? 68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 117.959 150.458 97.186  1.00 62.94  ? 68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 116.966 150.056 98.052  1.00 62.55  ? 68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 116.905 154.488 98.053  1.00 66.22  ? 69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 115.959 154.669 96.958  1.00 65.11  ? 69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.663 156.135 96.675  1.00 66.42  ? 69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.229 156.462 95.565  1.00 66.49  ? 69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.651 153.934 97.253  1.00 64.57  ? 69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.654 152.423 97.012  1.00 64.20  ? 69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.377 151.788 97.535  1.00 61.55  ? 69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.847 152.111 95.538  1.00 62.20  ? 69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 115.885 157.021 97.650  1.00 68.32  ? 70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.640 158.442 97.439  1.00 68.97  ? 70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.670 159.076 96.513  1.00 69.44  ? 70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.417 160.157 95.974  1.00 68.63  ? 70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.626 159.177 98.779  1.00 68.47  ? 70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.763 158.839 99.555  1.00 68.83  ? 70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.821 158.429 96.318  1.00 62.51  ? 71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.840 158.952 95.420  1.00 61.51  ? 71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.459 158.816 93.953  1.00 63.84  ? 71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.137 159.399 93.100  1.00 64.57  ? 71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.173 158.248 95.674  1.00 62.15  ? 71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.505 157.932 97.133  1.00 66.89  ? 71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.655 156.943 97.219  1.00 63.36  ? 71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 120.831 159.205 97.896  1.00 64.54  ? 71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.404 158.068 93.640  1.00 59.40  ? 72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 116.954 157.860 92.272  1.00 59.47  ? 72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.522 158.344 92.118  1.00 59.98  ? 72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.697 158.174 93.021  1.00 63.12  ? 72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.016 156.380 91.874  1.00 60.16  ? 72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.313 155.678 92.195  1.00 55.39  ? 72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.519 155.094 93.437  1.00 56.43  ? 72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.321 155.577 91.247  1.00 54.30  ? 72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.697 154.448 93.732  1.00 55.37  ? 72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.502 154.928 91.533  1.00 57.19  ? 72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.684 154.367 92.777  1.00 55.91  ? 72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 121.858 153.721 93.072  1.00 56.83  ? 72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.230 158.949 90.971  1.00 65.85  ? 73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 113.845 159.162 90.589  1.00 67.16  ? 73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.200 157.821 90.253  1.00 69.51  ? 73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 113.879 156.833 89.961  1.00 69.02  ? 73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 113.753 160.113 89.395  1.00 65.32  ? 73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.175 159.476 88.202  1.00 68.74  ? 73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 111.867 157.786 90.309  1.00 69.15  ? 74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.172 156.527 90.058  1.00 68.43  ? 74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.395 156.038 88.632  1.00 70.99  ? 74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.360 154.830 88.373  1.00 75.00  ? 74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 109.677 156.660 90.336  1.00 68.78  ? 74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 108.912 155.401 90.063  1.00 71.46  ? 74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.178 154.251 90.786  1.00 67.44  ? 74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 107.953 155.354 89.066  1.00 72.35  ? 74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.491 153.083 90.534  1.00 70.91  ? 74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.260 154.187 88.810  1.00 70.73  ? 74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.532 153.050 89.543  1.00 71.83  ? 74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.617 156.958 87.691  1.00 75.02  ? 75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 111.919 156.547 86.323  1.00 76.15  ? 75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.211 155.745 86.271  1.00 77.43  ? 75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.293 154.723 85.577  1.00 78.61  ? 75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.007 157.775 85.412  1.00 76.17  ? 75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.779 158.729 85.331  1.00 77.98  ? 75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.374 158.112 85.496  1.00 82.17  ? 75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.188 156.876 85.509  1.00 78.77  ? 75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.423 158.910 85.623  1.00 80.90  ? 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.228 156.189 87.008  1.00 69.46  ? 76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.503 155.479 87.036  1.00 65.84  ? 76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.353 154.092 87.652  1.00 67.97  ? 76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 115.901 153.112 87.134  1.00 75.21  ? 76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.529 156.309 87.801  1.00 69.32  ? 76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.686 157.703 87.224  1.00 73.27  ? 76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.852 157.815 85.992  1.00 71.86  ? 76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 116.641 158.684 87.997  1.00 71.55  ? 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.604 153.990 88.753  1.00 57.07  ? 77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.388 152.695 89.395  1.00 59.61  ? 77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.620 151.760 88.469  1.00 62.08  ? 77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.934 150.568 88.362  1.00 60.45  ? 77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.665 152.882 90.739  1.00 61.31  ? 77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.463 153.815 91.649  1.00 61.86  ? 77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.449 151.543 91.414  1.00 60.49  ? 77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 113.689 154.298 92.853  1.00 62.42  ? 77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.591 152.282 87.799  1.00 68.30  ? 78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.821 151.461 86.870  1.00 65.07  ? 78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.684 150.987 85.709  1.00 68.29  ? 78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.578 149.833 85.281  1.00 72.63  ? 78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.609 152.243 86.365  1.00 68.08  ? 78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.672 151.444 85.478  1.00 70.61  ? 78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.481 152.288 85.063  1.00 70.68  ? 78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.708 151.642 83.929  1.00 72.74  ? 78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.833 152.629 83.240  1.00 70.87  ? 78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.549 151.861 85.185  1.00 67.80  ? 79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.452 151.449 84.115  1.00 68.18  ? 79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.424 150.378 84.595  1.00 66.03  ? 79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.731 149.433 83.860  1.00 69.83  ? 79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.212 152.658 83.569  1.00 67.31  ? 79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.385 153.541 82.651  1.00 70.11  ? 79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 113.782 152.770 81.493  1.00 74.60  ? 79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 114.541 152.098 80.764  1.00 74.15  ? 79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 112.548 152.836 81.310  1.00 70.66  ? 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.918 150.509 85.828  1.00 54.52  ? 80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.817 149.499 86.382  1.00 52.38  ? 80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.110 148.154 86.497  1.00 61.58  ? 80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.659 147.108 86.121  1.00 63.64  ? 80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.365 149.977 87.740  1.00 53.36  ? 80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.926 148.814 88.534  1.00 53.54  ? 80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.424 151.044 87.532  1.00 57.32  ? 80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.877 148.158 87.009  1.00 61.63  ? 81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.127 146.912 87.142  1.00 55.69  ? 81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.807 146.309 85.779  1.00 54.34  ? 81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.835 145.085 85.615  1.00 61.52  ? 81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.850 147.146 87.946  1.00 53.50  ? 81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 113.049 147.071 89.434  1.00 52.19  ? 81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.789 148.034 90.097  1.00 54.25  ? 81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.495 146.038 90.171  1.00 55.99  ? 81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.973 147.970 91.464  1.00 56.05  ? 81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.677 145.969 91.540  1.00 53.30  ? 81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.417 146.935 92.186  1.00 51.27  ? 81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.495 147.151 84.790  1.00 54.52  ? 82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.295 146.658 83.431  1.00 56.86  ? 82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.565 146.014 82.893  1.00 57.81  ? 82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.508 144.975 82.226  1.00 61.20  ? 82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.849 147.800 82.517  1.00 61.40  ? 82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.433 148.292 82.757  1.00 62.19  ? 82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.413 147.348 82.149  1.00 62.40  ? 82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.431 148.096 81.264  1.00 63.22  ? 82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.873 148.120 79.843  1.00 60.09  ? 82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.720 146.624 83.169  1.00 54.02  ? 83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.988 146.041 82.750  1.00 56.19  ? 83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.204 144.679 83.395  1.00 57.46  ? 83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.700 143.749 82.750  1.00 58.02  ? 83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.139 146.988 83.093  1.00 54.57  ? 83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.869 148.286 82.550  1.00 58.50  ? 83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.448 146.470 82.515  1.00 54.62  ? 83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.842 144.545 84.674  1.00 48.39  ? 84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.965 143.249 85.334  1.00 48.21  ? 84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.052 142.210 84.697  1.00 56.29  ? 84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.467 141.070 84.460  1.00 61.75  ? 84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.660 143.386 86.824  1.00 48.63  ? 84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.808 142.586 84.403  1.00 57.71  ? 85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.849 141.663 83.813  1.00 50.10  ? 85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.992 141.528 82.304  1.00 52.76  ? 85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.414 140.601 81.726  1.00 58.41  ? 85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.420 142.097 84.156  1.00 52.12  ? 85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.009 141.771 85.574  1.00 54.06  ? 85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 112.280 142.645 86.618  1.00 53.50  ? 85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.352 140.585 85.870  1.00 56.13  ? 85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.904 142.349 87.914  1.00 53.57  ? 85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.975 140.279 87.163  1.00 58.55  ? 85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.254 141.164 88.180  1.00 57.75  ? 85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.878 140.862 89.468  1.00 54.84  ? 85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.740 142.421 81.650  1.00 54.10  ? 86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.962 142.280 80.215  1.00 56.05  ? 86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.806 141.053 79.896  1.00 58.53  ? 86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.665 140.468 78.816  1.00 58.96  ? 86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.627 143.535 79.652  1.00 51.34  ? 86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.686 140.654 80.817  1.00 55.82  ? 87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.506 139.469 80.596  1.00 53.23  ? 87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.663 138.201 80.553  1.00 54.26  ? 87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.020 137.246 79.853  1.00 52.58  ? 87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.577 139.369 81.684  1.00 53.65  ? 87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.258 138.013 81.784  1.00 55.54  ? 87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.702 138.078 81.324  1.00 52.08  ? 87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 121.317 136.691 81.246  1.00 48.22  ? 87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 121.577 136.122 82.597  1.00 46.21  ? 87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.537 138.186 81.269  1.00 63.24  ? 88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.684 137.006 81.396  1.00 62.95  ? 88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.477 135.838 81.985  1.00 57.74  ? 88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.515 134.731 81.443  1.00 57.73  ? 88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.053 136.631 80.051  1.00 60.55  ? 88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.227 137.746 79.424  1.00 59.50  ? 88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 111.900 137.940 80.143  1.00 59.22  ? 88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 111.004 136.710 80.051  1.00 62.60  ? 88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 111.246 135.890 78.828  1.00 64.15  ? 88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.125 136.118 83.113  1.00 52.49  ? 89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.957 135.124 83.773  1.00 53.02  ? 89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.121 133.937 84.227  1.00 54.18  ? 89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.054 134.097 84.825  1.00 56.99  ? 89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.675 135.746 84.971  1.00 51.82  ? 89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.478 134.762 85.775  1.00 51.52  ? 89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.757 134.409 85.383  1.00 49.34  ? 89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.953 134.191 86.921  1.00 48.04  ? 89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.496 133.505 86.118  1.00 48.49  ? 89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.688 133.285 87.659  1.00 49.20  ? 89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.960 132.943 87.258  1.00 50.65  ? 89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.616 132.736 83.939  1.00 54.83  ? 90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.974 131.501 84.363  1.00 54.63  ? 90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.983 130.663 85.131  1.00 54.63  ? 90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.109 130.463 84.664  1.00 54.14  ? 90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.429 130.713 83.168  1.00 54.30  ? 90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.489 131.505 82.276  1.00 53.78  ? 90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.042 131.324 82.699  1.00 54.92  ? 90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.498 132.534 83.302  1.00 54.32  ? 90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.053 133.578 82.617  1.00 57.36  ? 90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.060 133.590 81.295  1.00 57.57  ? 90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.589 134.636 83.276  1.00 60.49  ? 90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.583 130.188 86.299  1.00 51.80  ? 91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.436 129.306 87.081  1.00 50.49  ? 91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.598 127.982 86.349  1.00 56.03  ? 91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.593 127.375 85.958  1.00 57.82  ? 91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.838 129.082 88.466  1.00 50.53  ? 91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.981 130.260 89.386  1.00 53.25  ? 91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.180 130.510 90.032  1.00 57.90  ? 91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.917 131.116 89.607  1.00 53.38  ? 91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.314 131.590 90.881  1.00 49.31  ? 91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.046 132.198 90.455  1.00 52.40  ? 91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.245 132.435 91.092  1.00 48.81  ? 91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.825 127.496 86.136  1.00 56.19  ? 92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 119.012 126.245 85.397  1.00 55.30  ? 92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.916 124.988 86.246  1.00 58.02  ? 92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.859 123.886 85.680  1.00 58.52  ? 92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.427 126.409 84.820  1.00 57.88  ? 92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.126 127.386 85.757  1.00 56.29  ? 92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.097 127.997 86.679  1.00 54.70  ? 92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.899 125.117 87.569  1.00 54.09  ? 93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.735 123.985 88.465  1.00 53.39  ? 93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.718 124.352 89.533  1.00 56.13  ? 93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.603 125.515 89.927  1.00 56.67  ? 93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 120.064 123.576 89.113  1.00 54.88  ? 93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.881 122.502 90.018  1.00 58.12  ? 93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.970 123.346 89.991  1.00 60.21  ? 94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.956 123.589 91.011  1.00 54.98  ? 94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.585 124.053 92.317  1.00 59.01  ? 94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.003 124.870 93.039  1.00 62.20  ? 94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.121 122.329 91.238  1.00 57.51  ? 94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.469 122.276 92.587  1.00 58.85  ? 94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.409 123.110 92.892  1.00 58.08  ? 94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.921 121.399 93.556  1.00 58.43  ? 94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.816 123.070 94.135  1.00 58.52  ? 94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.327 121.354 94.799  1.00 57.22  ? 94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.273 122.190 95.088  1.00 54.79  ? 94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.773 123.536 92.640  1.00 52.98  ? 95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.414 123.888 93.901  1.00 50.33  ? 95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.781 125.366 93.956  1.00 51.68  ? 95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.737 125.970 95.030  1.00 57.51  ? 95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.653 123.018 94.114  1.00 54.45  ? 95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.431 123.293 95.394  1.00 59.50  ? 95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.500 123.129 96.932  1.00 72.89  ? 95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.475 121.700 96.598  1.00 55.77  ? 95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.128 125.964 92.815  1.00 47.09  ? 96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.432 127.393 92.782  1.00 42.04  ? 96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.223 128.222 93.199  1.00 48.39  ? 96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.315 129.085 94.085  1.00 52.17  ? 96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.891 127.787 91.380  1.00 44.10  ? 96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.830 126.857 90.873  1.00 49.91  ? 96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.079 127.972 92.560  1.00 53.90  ? 97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.860 128.694 92.902  1.00 47.90  ? 97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.433 128.403 94.332  1.00 48.46  ? 97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.965 129.301 95.041  1.00 55.47  ? 97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.745 128.331 91.923  1.00 47.02  ? 97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.574 127.151 94.770  1.00 47.28  ? 98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.213 126.801 96.140  1.00 48.28  ? 98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.054 127.585 97.140  1.00 53.99  ? 98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.523 128.172 98.089  1.00 63.78  ? 98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.374 125.296 96.352  1.00 55.95  ? 98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.116 124.849 97.762  1.00 57.35  ? 98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.822 124.645 98.210  1.00 58.48  ? 98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.166 124.625 98.637  1.00 57.23  ? 98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.579 124.233 99.505  1.00 58.44  ? 98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.929 124.213 99.933  1.00 59.95  ? 98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.634 124.016 100.367 1.00 60.44  ? 98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.371 127.630 96.924  1.00 54.49  ? 99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.246 128.398 97.803  1.00 51.60  ? 99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.873 129.871 97.811  1.00 54.79  ? 99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.753 130.480 98.880  1.00 57.82  ? 99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.707 128.221 97.387  1.00 49.54  ? 99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.516 127.353 98.329  1.00 54.36  ? 99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.779 126.096 98.721  1.00 53.57  ? 99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.494 125.395 99.859  1.00 56.13  ? 99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.546 126.240 101.084 1.00 53.98  ? 99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.680 130.468 96.633  1.00 48.14  ? 100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.384 131.896 96.616  1.00 42.45  ? 100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.062 132.191 97.311  1.00 49.82  ? 100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 115.995 133.040 98.205  1.00 56.82  ? 100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.358 132.450 95.195  1.00 42.04  ? 100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.984 133.903 95.146  1.00 43.18  ? 100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.908 134.876 95.481  1.00 48.81  ? 100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.699 134.293 94.816  1.00 50.36  ? 100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.568 136.211 95.462  1.00 50.77  ? 100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.352 135.628 94.799  1.00 48.24  ? 100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.288 136.588 95.122  1.00 48.20  ? 100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.002 131.478 96.937  1.00 52.60  ? 101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.676 131.768 97.456  1.00 49.65  ? 101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.435 131.186 98.840  1.00 47.88  ? 101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.336 131.350 99.376  1.00 59.76  ? 101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.615 131.267 96.475  1.00 48.12  ? 101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.548 132.094 95.211  1.00 44.61  ? 101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.913 133.327 95.199  1.00 50.26  ? 101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 113.138 131.651 94.037  1.00 47.21  ? 101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.856 134.089 94.051  1.00 45.31  ? 101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.087 132.407 92.885  1.00 51.60  ? 101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.444 133.624 92.897  1.00 48.81  ? 101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.391 134.380 91.749  1.00 51.72  ? 101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.420 130.507 99.426  1.00 50.37  ? 102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.341 130.118 100.825 1.00 55.39  ? 102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.248 130.928 101.738 1.00 59.23  ? 102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 114.925 131.083 102.918 1.00 59.21  ? 102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.681 128.631 100.985 1.00 57.17  ? 102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.480 127.734 100.762 1.00 60.76  ? 102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.696 127.945 99.837  1.00 59.99  ? 102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.327 126.729 101.616 1.00 57.12  ? 102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.367 131.450 101.235 1.00 62.73  ? 103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.325 132.176 102.058 1.00 60.40  ? 103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.396 133.661 101.734 1.00 56.92  ? 103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.338 134.493 102.644 1.00 62.08  ? 103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.724 131.556 101.908 1.00 63.54  ? 103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.758 130.082 102.267 1.00 67.10  ? 103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.690 129.506 102.561 1.00 62.03  ? 103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 119.860 129.495 102.252 1.00 68.03  ? 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.519 134.021 100.455 1.00 47.63  ? 104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.848 135.386 100.073 1.00 52.91  ? 104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.674 136.188 99.537  1.00 51.23  ? 104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.756 137.420 99.510  1.00 56.16  ? 104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.970 135.384 99.024  1.00 53.43  ? 104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.162 134.554 99.435  1.00 54.83  ? 104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.136 135.071 100.279 1.00 52.18  ? 104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.311 133.248 98.987  1.00 51.37  ? 104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.222 134.312 100.662 1.00 52.80  ? 104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.395 132.483 99.365  1.00 51.47  ? 104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.347 133.019 100.203 1.00 55.27  ? 104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.431 132.263 100.582 1.00 57.83  ? 104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.597 135.537 99.111  1.00 56.96  ? 105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.425 136.269 98.649  1.00 54.57  ? 105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.697 136.887 99.835  1.00 59.98  ? 105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.496 136.234 100.863 1.00 62.01  ? 105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.488 135.347 97.875  1.00 48.27  ? 105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.308 138.151 99.693  1.00 57.99  ? 106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.582 138.830 100.757 1.00 54.86  ? 106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.178 138.259 100.880 1.00 54.18  ? 106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.469 138.099 99.881  1.00 53.89  ? 106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.524 140.333 100.490 1.00 56.44  ? 106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.806 141.189 101.534 1.00 55.52  ? 106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.562 141.175 102.851 1.00 56.47  ? 106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.633 142.610 101.028 1.00 55.26  ? 106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.777 137.948 102.108 1.00 63.76  ? 107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.460 137.408 102.397 1.00 63.89  ? 107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.707 138.352 103.323 1.00 65.62  ? 107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.294 139.221 103.973 1.00 64.53  ? 107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.554 136.017 103.036 1.00 60.02  ? 107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.992 134.921 102.083 1.00 60.07  ? 107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.347 133.656 102.840 1.00 65.84  ? 107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.891 132.590 101.908 1.00 61.86  ? 107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.603 131.515 102.652 1.00 62.14  ? 107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.390 138.172 103.370 1.00 71.88  ? 108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.560 138.961 104.262 1.00 73.53  ? 108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.878 138.632 105.718 1.00 74.55  ? 108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.524 137.627 106.030 1.00 76.81  ? 108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.078 138.715 103.975 1.00 75.30  ? 108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.824 137.305 103.949 1.00 74.91  ? 108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.688 139.318 102.635 1.00 71.12  ? 108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.419 139.506 106.618 1.00 75.29  ? 109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.724 139.351 108.037 1.00 75.81  ? 109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.207 138.038 108.609 1.00 77.24  ? 109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 106.745 137.561 109.614 1.00 74.92  ? 109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.150 140.528 108.828 1.00 73.95  ? 109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.946 141.802 108.637 1.00 75.42  ? 109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.150 141.762 108.387 1.00 75.86  ? 109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.277 142.943 108.750 1.00 74.94  ? 109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.183 137.444 108.002 1.00 79.56  ? 110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 104.683 136.141 108.415 1.00 80.92  ? 110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.297 134.995 107.621 1.00 80.94  ? 110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 104.922 133.839 107.839 1.00 80.15  ? 110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.157 136.097 108.293 1.00 81.51  ? 110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.659 136.674 106.985 1.00 83.04  ? 110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.382 137.497 106.388 1.00 81.63  ? 110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.545 136.308 106.555 1.00 81.73  ? 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.220 135.289 106.705 1.00 74.90  ? 111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 106.950 134.310 105.903 1.00 76.64  ? 111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.041 133.459 105.024 1.00 75.93  ? 111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.497 132.460 104.455 1.00 73.11  ? 111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 107.819 133.400 106.781 1.00 75.20  ? 111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.313 133.582 106.578 1.00 74.94  ? 111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.883 134.592 107.560 1.00 76.08  ? 111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 111.403 134.586 107.540 1.00 76.57  ? 111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 111.975 135.515 108.553 1.00 75.14  ? 111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 104.764 133.822 104.897 1.00 80.28  ? 112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 103.848 133.023 104.090 1.00 82.11  ? 112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.066 133.257 102.600 1.00 79.99  ? 112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 103.943 132.327 101.795 1.00 79.24  ? 112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.402 133.332 104.477 1.00 79.85  ? 112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.028 132.887 105.882 1.00 80.96  ? 112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 100.576 133.212 106.193 1.00 82.65  ? 112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 100.201 132.775 107.599 1.00 80.89  ? 112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 98.796  133.136 107.933 1.00 78.71  ? 112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.389 134.488 102.216 1.00 72.00  ? 113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.519 134.870 100.819 1.00 68.47  ? 113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.942 135.338 100.538 1.00 66.19  ? 113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.771 135.472 101.442 1.00 69.19  ? 113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.514 135.970 100.458 1.00 67.49  ? 113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.428 135.534 99.485  1.00 64.80  ? 113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.721 134.282 99.976  1.00 66.61  ? 113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.770 133.733 98.926  1.00 69.46  ? 113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 99.859  132.698 99.487  1.00 67.71  ? 113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.220 135.587 99.260  1.00 58.80  ? 114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.532 136.026 98.795  1.00 61.39  ? 114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.388 137.419 98.200  1.00 57.80  ? 114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.518 137.652 97.353  1.00 57.68  ? 114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.123 135.046 97.768  1.00 60.33  ? 114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.496 133.726 98.440  1.00 60.35  ? 114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.337 135.651 97.087  1.00 55.94  ? 114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.678 132.585 97.472  1.00 56.70  ? 114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.233 138.345 98.647  1.00 54.69  ? 115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.183 139.720 98.170  1.00 54.43  ? 115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.186 140.019 97.067  1.00 55.91  ? 115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.932 140.900 96.240  1.00 54.84  ? 115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.417 140.693 99.330  1.00 56.27  ? 115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.324 140.746 100.396 1.00 53.72  ? 115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.832 141.434 101.649 1.00 55.33  ? 115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.090 141.451 99.857  1.00 54.10  ? 115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.313 139.314 97.026  1.00 60.63  ? 116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.391 139.605 96.091  1.00 56.57  ? 116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.621 138.432 95.151  1.00 56.52  ? 116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.740 137.286 95.596  1.00 61.89  ? 116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.689 139.922 96.834  1.00 54.02  ? 116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.991 141.397 96.964  1.00 57.46  ? 116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.238 141.655 97.780  1.00 60.30  ? 116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.829 140.678 98.286  1.00 57.63  ? 116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.631 142.831 97.914  1.00 62.88  ? 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.688 138.725 93.855  1.00 49.00  ? 117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.207 137.780 92.883  1.00 49.83  ? 117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.729 137.894 92.835  1.00 51.44  ? 117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.342 138.678 93.567  1.00 59.75  ? 117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.591 138.034 91.510  1.00 51.94  ? 117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.139 137.608 91.381  1.00 56.69  ? 117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.789 137.315 89.929  1.00 61.79  ? 117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 108.534 136.584 89.795  1.00 62.59  ? 117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.380 135.298 90.080  1.00 58.89  ? 117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 109.388 134.558 90.509  1.00 55.34  ? 117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 107.183 134.739 89.926  1.00 58.32  ? 117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.360 137.102 91.969  1.00 46.11  ? 118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.797 137.248 91.766  1.00 43.33  ? 118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.114 138.577 91.095  1.00 46.78  ? 118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.031 139.297 91.511  1.00 52.79  ? 118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.336 136.077 90.945  1.00 46.15  ? 118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.840 135.943 90.991  1.00 44.20  ? 118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.511 135.876 92.201  1.00 40.47  ? 118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.586 135.878 89.824  1.00 44.87  ? 118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.883 135.753 92.249  1.00 41.65  ? 118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.959 135.749 89.862  1.00 42.77  ? 118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.603 135.689 91.078  1.00 45.32  ? 118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.972 135.564 91.124  1.00 47.93  ? 118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.349 138.925 90.062  1.00 50.73  ? 119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.500 140.194 89.366  1.00 45.34  ? 119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.151 141.389 90.241  1.00 46.09  ? 119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.518 142.514 89.889  1.00 54.22  ? 119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.631 140.197 88.109  1.00 49.76  ? 119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.253 139.476 86.927  1.00 50.52  ? 119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.526 138.192 86.576  1.00 56.29  ? 119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.261 137.387 87.494  1.00 54.07  ? 119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.223 137.986 85.382  1.00 58.32  ? 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.455 141.180 91.355  1.00 50.00  ? 120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.145 142.236 92.311  1.00 49.25  ? 120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.240 142.438 93.342  1.00 46.51  ? 120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.644 143.575 93.596  1.00 54.51  ? 120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.830 141.927 93.031  1.00 48.84  ? 120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.620 142.183 92.163  1.00 56.66  ? 120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.719 143.016 91.240  1.00 58.94  ? 120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.571 141.549 92.399  1.00 60.37  ? 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.733 141.350 93.938  1.00 40.92  ? 121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.879 141.447 94.833  1.00 37.23  ? 121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.101 141.991 94.109  1.00 42.90  ? 121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.815 142.840 94.654  1.00 52.27  ? 121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.181 140.078 95.442  1.00 36.97  ? 121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.406 140.037 96.337  1.00 38.74  ? 121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.038 140.229 97.796  1.00 37.84  ? 121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.793 141.316 98.407  1.00 41.77  ? 121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.293 142.509 98.698  1.00 42.18  ? 121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.032 142.812 98.443  1.00 43.60  ? 121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.080 143.421 99.259  1.00 44.13  ? 121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.349 141.531 92.882  1.00 43.63  ? 122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.487 142.034 92.120  1.00 39.47  ? 122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.319 143.516 91.811  1.00 41.68  ? 122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.275 144.291 91.916  1.00 51.28  ? 122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.677 141.195 90.843  1.00 40.29  ? 122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.549 139.978 91.147  1.00 37.20  ? 122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.292 142.027 89.728  1.00 38.53  ? 122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.798 139.104 89.955  1.00 44.82  ? 122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.109 143.936 91.434  1.00 41.17  ? 123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.873 145.350 91.156  1.00 35.13  ? 123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.087 146.202 92.399  1.00 39.44  ? 123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.680 147.283 92.323  1.00 50.84  ? 123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.459 145.557 90.616  1.00 40.35  ? 123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.137 144.585 89.644  1.00 44.95  ? 123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.609 145.734 93.552  1.00 42.38  ? 124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.768 146.503 94.783  1.00 40.38  ? 124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.239 146.592 95.172  1.00 40.52  ? 124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.724 147.656 95.579  1.00 51.27  ? 124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.911 145.890 95.904  1.00 46.43  ? 124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.437 146.213 95.664  1.00 43.54  ? 124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.351 146.403 97.263  1.00 43.69  ? 124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.164 147.686 95.458  1.00 43.41  ? 124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.976 145.486 95.042  1.00 39.41  ? 125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.402 145.502 95.355  1.00 37.08  ? 125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.146 146.445 94.417  1.00 38.85  ? 125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.034 147.194 94.842  1.00 53.36  ? 125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.974 144.072 95.303  1.00 38.78  ? 125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.478 144.098 95.422  1.00 42.18  ? 125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.380 143.226 96.413  1.00 40.75  ? 125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.794 146.429 93.129  1.00 31.16  ? 126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.432 147.327 92.169  1.00 31.57  ? 126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.128 148.786 92.480  1.00 38.46  ? 126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.016 149.644 92.393  1.00 48.53  ? 126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.978 146.981 90.756  1.00 39.02  ? 126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.876 149.089 92.829  1.00 42.77  ? 127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.514 150.457 93.179  1.00 39.35  ? 127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.249 150.911 94.430  1.00 42.08  ? 127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.639 152.079 94.542  1.00 52.63  ? 127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.003 150.568 93.372  1.00 38.11  ? 127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.152 150.468 92.107  1.00 43.92  ? 127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.693 150.277 92.471  1.00 48.60  ? 127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.334 151.699 91.239  1.00 43.29  ? 127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.442 150.004 95.388  1.00 36.55  ? 128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.246 150.338 96.556  1.00 37.87  ? 128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.689 150.626 96.157  1.00 42.87  ? 128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.282 151.614 96.601  1.00 46.01  ? 128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.181 149.203 97.580  1.00 35.50  ? 128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.160 149.353 98.708  1.00 46.67  ? 128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.860 150.157 99.794  1.00 49.88  ? 128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.375 148.691 98.685  1.00 41.51  ? 128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.756 150.302 100.833 1.00 50.12  ? 128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.274 148.834 99.721  1.00 39.63  ? 128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.964 149.640 100.796 1.00 46.89  ? 128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.261 149.776 95.299  1.00 41.64  ? 129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.662 149.928 94.915  1.00 33.06  ? 129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.906 151.235 94.174  1.00 38.74  ? 129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.911 151.915 94.414  1.00 46.72  ? 129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.103 148.752 94.044  1.00 32.71  ? 129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.357 147.487 94.803  1.00 35.58  ? 129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.524 147.504 96.175  1.00 37.84  ? 129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.453 146.278 94.136  1.00 35.24  ? 129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.763 146.337 96.868  1.00 41.79  ? 129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.698 145.111 94.823  1.00 37.80  ? 129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.850 145.139 96.192  1.00 42.35  ? 129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.007 151.600 93.259  1.00 46.37  ? 130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.272 152.733 92.380  1.00 46.90  ? 130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.272 154.060 93.127  1.00 56.10  ? 130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.033 154.967 92.769  1.00 59.83  ? 130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.253 152.767 91.247  1.00 46.79  ? 130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.427 154.199 94.149  1.00 56.27  ? 131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.348 155.410 94.966  1.00 53.83  ? 131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 123.996 156.633 94.115  1.00 54.23  ? 131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.756 157.597 94.010  1.00 58.92  ? 131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 125.652 155.633 95.742  1.00 52.04  ? 131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.413 155.978 97.198  1.00 58.61  ? 131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.594 155.353 97.870  1.00 57.28  ? 131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.130 156.980 97.693  1.00 56.71  ? 131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 122.816 156.573 93.500  1.00 53.63  ? 132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.270 157.686 92.752  1.00 58.34  ? 132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.575 157.686 91.268  1.00 58.50  ? 132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.015 158.518 90.543  1.00 59.18  ? 132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.434 156.790 90.793  1.00 58.61  ? 133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 123.810 156.745 89.386  1.00 61.08  ? 133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 122.938 155.725 88.660  1.00 63.70  ? 133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 122.935 154.542 89.012  1.00 62.89  ? 133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.290 156.396 89.237  1.00 61.07  ? 133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 125.861 156.821 87.898  1.00 64.72  ? 133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.072 157.065 86.960  1.00 64.85  ? 133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.101 156.910 87.783  1.00 60.49  ? 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.199 156.185 87.648  1.00 61.47  ? 134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.333 155.278 86.901  1.00 58.57  ? 134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.138 154.361 85.988  1.00 63.71  ? 134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 121.870 153.155 85.920  1.00 67.85  ? 134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.311 156.072 86.089  1.00 64.23  ? 134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.735 157.094 86.911  1.00 64.29  ? 134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.211 155.156 85.578  1.00 64.82  ? 134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.122 154.912 85.274  1.00 63.86  ? 135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 123.937 154.093 84.382  1.00 62.88  ? 135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.751 153.070 85.164  1.00 61.66  ? 135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 124.875 151.913 84.745  1.00 66.42  ? 135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 124.852 154.981 83.540  1.00 62.04  ? 135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.163 155.653 82.363  1.00 62.70  ? 135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 122.913 154.920 81.915  1.00 70.95  ? 135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.042 153.891 81.218  1.00 70.28  ? 135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.800 155.373 82.257  1.00 70.18  ? 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.311 153.478 86.303  1.00 50.56  ? 136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.045 152.535 87.141  1.00 51.73  ? 136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.120 151.459 87.694  1.00 54.87  ? 136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.510 150.292 87.808  1.00 56.03  ? 136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.748 153.280 88.275  1.00 57.03  ? 136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 127.726 152.436 89.069  1.00 54.87  ? 136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.045 152.275 88.333  1.00 54.33  ? 136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.119 151.718 89.253  1.00 55.87  ? 136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.478 151.835 88.655  1.00 56.17  ? 136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 123.886 151.833 88.045  1.00 57.39  ? 137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.923 150.847 88.524  1.00 51.84  ? 137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.578 149.839 87.437  1.00 48.70  ? 137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.472 148.638 87.705  1.00 50.64  ? 137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.663 151.544 89.030  1.00 48.76  ? 137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.399 150.309 86.200  1.00 49.38  ? 138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.129 149.391 85.099  1.00 51.94  ? 138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.331 148.496 84.820  1.00 54.32  ? 138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.170 147.317 84.488  1.00 55.04  ? 138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.731 150.169 83.847  1.00 54.53  ? 138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.410 150.908 83.976  1.00 54.40  ? 138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 119.777 151.146 82.618  1.00 52.91  ? 138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.660 152.630 82.315  1.00 58.21  ? 138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 118.458 152.933 81.492  1.00 55.62  ? 138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.543 149.041 84.943  1.00 54.42  ? 139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.740 148.221 84.777  1.00 48.76  ? 139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.815 147.136 85.844  1.00 47.64  ? 139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.159 145.988 85.549  1.00 63.05  ? 139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.988 149.100 84.816  1.00 51.62  ? 139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.338 149.739 83.485  1.00 52.37  ? 139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.333 150.873 83.627  1.00 60.11  ? 139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 129.344 150.692 84.338  1.00 57.05  ? 139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 128.104 151.946 83.031  1.00 58.39  ? 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.494 147.483 87.093  1.00 36.63  ? 140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.476 146.489 88.162  1.00 37.46  ? 140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.394 145.442 87.927  1.00 41.51  ? 140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.594 144.256 88.214  1.00 40.71  ? 140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.267 147.176 89.508  1.00 44.82  ? 140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.525 147.734 90.119  1.00 42.42  ? 140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.634 146.927 90.329  1.00 42.52  ? 140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.605 149.067 90.489  1.00 39.98  ? 140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.785 147.435 90.887  1.00 42.23  ? 140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.750 149.582 91.048  1.00 44.68  ? 140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.836 148.764 91.246  1.00 44.87  ? 140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.978 149.281 91.804  1.00 46.73  ? 140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.233 145.871 87.428  1.00 49.54  ? 141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.161 144.936 87.101  1.00 44.51  ? 141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.611 143.960 86.024  1.00 44.79  ? 141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.367 142.754 86.119  1.00 56.08  ? 141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.897 145.705 86.675  1.00 43.77  ? 141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.044 144.852 85.770  1.00 45.05  ? 141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.101 146.104 87.892  1.00 46.75  ? 141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.267 144.466 84.979  1.00 42.78  ? 142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.788 143.583 83.941  1.00 44.29  ? 142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.848 142.646 84.504  1.00 47.12  ? 142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.919 141.473 84.123  1.00 56.27  ? 142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.355 144.406 82.786  1.00 47.80  ? 142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.274 144.983 81.898  1.00 52.30  ? 142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.343 144.284 81.500  1.00 47.77  ? 142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.390 146.267 81.581  1.00 46.47  ? 142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.683 143.152 85.412  1.00 42.95  ? 143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.737 142.337 86.003  1.00 39.84  ? 143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.167 141.191 86.828  1.00 42.41  ? 143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.675 140.065 86.773  1.00 51.18  ? 143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.639 143.220 86.864  1.00 44.36  ? 143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.946 142.616 87.365  1.00 42.38  ? 143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.942 142.546 86.231  1.00 46.65  ? 143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.490 143.449 88.510  1.00 41.85  ? 143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.115 141.456 87.600  1.00 40.58  ? 144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.573 140.444 88.500  1.00 33.99  ? 144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.553 139.526 87.838  1.00 38.82  ? 144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.468 138.348 88.203  1.00 44.98  ? 144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.942 141.109 89.727  1.00 39.89  ? 144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.954 141.568 90.763  1.00 37.04  ? 144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.188 142.249 92.242  1.00 52.15  ? 144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.640 143.837 91.631  1.00 42.51  ? 144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.774 140.027 86.879  1.00 37.76  ? 145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.797 139.175 86.210  1.00 35.53  ? 145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.475 138.277 85.183  1.00 42.76  ? 145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.965 137.197 84.866  1.00 51.15  ? 145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.676 140.021 85.581  1.00 38.26  ? 145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.375 139.220 85.527  1.00 42.13  ? 145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.064 140.506 84.192  1.00 40.14  ? 145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.843 138.828 86.884  1.00 40.25  ? 145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.624 138.696 84.649  1.00 40.71  ? 146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.482 137.779 83.912  1.00 37.61  ? 146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.204 136.818 84.840  1.00 39.79  ? 146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.860 135.889 84.357  1.00 46.04  ? 146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.503 138.553 83.077  1.00 35.83  ? 146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.861 139.344 81.957  1.00 39.77  ? 146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.756 139.034 81.518  1.00 43.56  ? 146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.553 140.375 81.491  1.00 44.28  ? 146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.102 137.036 86.152  1.00 40.38  ? 147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.753 136.211 87.164  1.00 36.46  ? 147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.266 136.201 86.988  1.00 42.92  ? 147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.926 135.202 87.274  1.00 52.40  ? 147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.196 134.785 87.163  1.00 38.61  ? 147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.771 134.689 87.675  1.00 36.90  ? 147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.433 133.316 88.206  1.00 43.29  ? 147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.693 133.181 89.180  1.00 42.88  ? 147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.974 132.285 87.569  1.00 47.46  ? 147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.824 137.312 86.503  1.00 42.09  ? 148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.273 137.443 86.423  1.00 42.04  ? 148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.882 137.689 87.797  1.00 39.20  ? 148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.933 137.129 88.124  1.00 44.02  ? 148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.645 138.578 85.470  1.00 36.24  ? 148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.265 138.328 84.024  1.00 43.53  ? 148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.400 139.570 83.167  1.00 47.67  ? 148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.444 140.371 83.125  1.00 52.30  ? 148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.463 139.747 82.538  1.00 50.22  ? 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.231 138.515 88.610  1.00 31.08  ? 149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.706 138.859 89.941  1.00 32.13  ? 149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.600 138.608 90.951  1.00 35.75  ? 149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.430 138.905 90.693  1.00 47.24  ? 149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.157 140.320 90.003  1.00 37.22  ? 149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.327 140.861 91.403  1.00 32.41  ? 149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.349 140.410 92.224  1.00 31.47  ? 149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.467 141.830 91.901  1.00 29.17  ? 149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.509 140.906 93.500  1.00 35.46  ? 149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.618 142.330 93.176  1.00 38.27  ? 149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.641 141.865 93.972  1.00 40.87  ? 149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.793 142.361 95.245  1.00 36.60  ? 149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.976 138.056 92.097  1.00 27.97  ? 150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.026 137.752 93.165  1.00 21.36  ? 150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.443 138.449 94.449  1.00 28.52  ? 150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.474 138.079 95.043  1.00 38.66  ? 150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.934 136.244 93.387  1.00 32.95  ? 150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.027 135.836 94.534  1.00 34.08  ? 150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.632 136.418 94.418  1.00 34.67  ? 150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.878 136.078 93.507  1.00 28.52  ? 150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.280 137.295 95.348  1.00 34.58  ? 150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.704 139.456 94.911  1.00 30.88  ? 151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.986 140.025 96.232  1.00 26.83  ? 151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.837 138.969 97.314  1.00 28.69  ? 151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.048 138.030 97.189  1.00 36.64  ? 151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.934 141.131 96.377  1.00 32.10  ? 151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.525 141.456 94.984  1.00 33.54  ? 151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.626 140.176 94.214  1.00 33.58  ? 151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.622 139.123 98.376  1.00 29.24  ? 152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.622 138.150 99.457  1.00 20.67  ? 152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.226 138.007 100.059 1.00 33.93  ? 152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.340 138.839 99.852  1.00 37.50  ? 152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.618 138.555 100.542 1.00 28.63  ? 152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.190 139.726 101.214 1.00 38.91  ? 152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.037 136.920 100.805 1.00 43.31  ? 153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.744 136.652 101.433 1.00 39.14  ? 153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.246 137.806 102.294 1.00 41.71  ? 153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.076 138.191 102.142 1.00 39.74  ? 153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.827 135.346 102.236 1.00 43.31  ? 153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.879 134.232 101.338 1.00 43.39  ? 153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.622 135.199 103.152 1.00 39.39  ? 153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.045 138.409 103.187 1.00 37.15  ? 154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.542 139.597 103.898 1.00 29.79  ? 154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.186 140.741 102.969 1.00 29.24  ? 154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.132 141.368 103.134 1.00 37.23  ? 154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.706 139.961 104.830 1.00 30.82  ? 154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.450 138.695 105.012 1.00 32.91  ? 154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.379 138.019 103.682 1.00 33.07  ? 154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.033 141.019 101.975 1.00 25.25  ? 155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.782 142.141 101.076 1.00 22.98  ? 155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.578 141.873 100.183 1.00 31.88  ? 155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.707 142.734 100.026 1.00 46.21  ? 155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 127.021 142.427 100.231 1.00 35.04  ? 155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.169 142.540 101.081 1.00 34.88  ? 155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.842 143.717 99.453  1.00 29.35  ? 155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.514 140.683 99.584  1.00 37.16  ? 156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.384 140.354 98.721  1.00 34.28  ? 156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.081 140.322 99.511  1.00 38.87  ? 156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.042 140.789 99.030  1.00 43.70  ? 156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.628 139.015 98.026  1.00 36.19  ? 156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.782 138.799 96.805  1.00 37.21  ? 156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.761 139.739 95.789  1.00 40.07  ? 156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.016 137.656 96.669  1.00 35.87  ? 156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.987 139.545 94.663  1.00 38.64  ? 156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.240 137.455 95.545  1.00 38.12  ? 156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.226 138.402 94.541  1.00 42.91  ? 156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.120 139.776 100.726 1.00 43.37  ? 157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.913 139.650 101.536 1.00 36.20  ? 157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.415 141.005 102.023 1.00 40.04  ? 157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.225 141.318 101.902 1.00 47.20  ? 157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.187 138.723 102.721 1.00 42.35  ? 157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 119.993 138.245 103.547 1.00 44.29  ? 157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.339 137.051 102.892 1.00 41.86  ? 157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.430 137.907 104.962 1.00 44.92  ? 157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.307 141.825 102.576 1.00 38.49  ? 158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.902 142.984 103.361 1.00 37.06  ? 158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 121.023 144.311 102.625 1.00 38.82  ? 158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.772 145.356 103.231 1.00 49.13  ? 158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.723 143.042 104.653 1.00 40.27  ? 158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.660 141.752 105.442 1.00 42.62  ? 158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.595 141.153 105.586 1.00 46.42  ? 158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.803 141.314 105.952 1.00 44.63  ? 158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.398 144.311 101.348 1.00 34.04  ? 159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.548 145.566 100.622 1.00 33.19  ? 159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.184 146.204 100.395 1.00 42.88  ? 159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.317 145.616 99.742  1.00 50.84  ? 159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.256 145.338 99.291  1.00 39.48  ? 159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.996 147.406 100.931 1.00 57.76  ? 160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.760 148.133 100.734 1.00 57.58  ? 160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.583 147.646 101.547 1.00 52.96  ? 160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.443 147.995 101.221 1.00 55.86  ? 160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.816 146.854 102.589 1.00 50.51  ? 161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.757 146.345 103.448 1.00 55.44  ? 161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.892 146.957 104.834 1.00 58.77  ? 161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.005 147.136 105.336 1.00 59.41  ? 161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.803 144.817 103.540 1.00 50.22  ? 161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 115.823 144.111 102.620 1.00 54.61  ? 161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.450 142.892 101.971 1.00 54.87  ? 161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.389 141.721 102.838 1.00 55.19  ? 161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.317 140.470 102.406 1.00 57.30  ? 161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.295 140.185 101.114 1.00 54.50  ? 161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.266 139.479 103.291 1.00 57.17  ? 161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.754 147.290 105.447 1.00 65.77  ? 162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.778 147.877 106.783 1.00 68.05  ? 162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.002 146.816 107.854 1.00 68.39  ? 162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 116.812 147.007 108.767 1.00 63.41  ? 162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.481 148.642 107.049 1.00 67.36  ? 162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.643 149.795 108.025 1.00 65.11  ? 162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.491 150.777 107.923 1.00 66.62  ? 162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.702 151.761 106.785 1.00 67.10  ? 162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 112.420 152.124 106.122 1.00 67.07  ? 162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.292 145.690 107.760 1.00 69.23  ? 163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.472 144.579 108.694 1.00 69.64  ? 163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.695 143.774 108.252 1.00 73.04  ? 163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.625 142.840 107.451 1.00 71.12  ? 163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.214 143.724 108.759 1.00 71.46  ? 163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 114.367 142.432 109.546 1.00 71.69  ? 163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 113.646 142.512 110.879 1.00 72.16  ? 163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 112.205 142.654 110.713 1.00 71.90  ? 163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 111.356 141.638 110.633 1.00 70.44  ? 163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 111.771 140.384 110.695 1.00 69.91  ? 163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 110.058 141.886 110.484 1.00 68.37  ? 163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.848 144.175 108.786 1.00 60.54  ? 164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.114 143.625 108.323 1.00 59.45  ? 164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.125 143.494 109.452 1.00 62.51  ? 164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 119.794 143.679 110.628 1.00 59.85  ? 164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.704 144.512 107.227 1.00 57.71  ? 164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 119.764 145.978 107.623 1.00 56.40  ? 164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.024 146.654 107.115 1.00 56.97  ? 164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 120.984 146.902 105.679 1.00 55.69  ? 164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 121.835 147.688 105.034 1.00 59.33  ? 164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 122.809 148.319 105.667 1.00 56.20  ? 164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 121.704 147.844 103.720 1.00 57.50  ? 164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.362 143.177 109.088 1.00 57.81  ? 165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.490 143.246 109.991 1.00 53.45  ? 165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.541 144.173 109.419 1.00 54.62  ? 165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.288 145.366 109.231 1.00 55.63  ? 165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.722 143.637 109.137 1.00 56.59  ? 166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.765 144.362 108.431 1.00 55.14  ? 166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.098 143.652 107.125 1.00 53.08  ? 166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.985 142.428 107.016 1.00 49.55  ? 166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.026 144.500 109.289 1.00 52.01  ? 166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.646 145.890 109.265 1.00 54.69  ? 166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.707 146.964 109.779 1.00 56.79  ? 166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 125.938 146.685 110.722 1.00 56.78  ? 166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.738 148.090 109.239 1.00 58.58  ? 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.510 144.438 106.130 1.00 36.62  ? 167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.988 143.880 104.874 1.00 32.98  ? 167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.386 143.295 104.993 1.00 40.57  ? 167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.863 142.665 104.043 1.00 40.53  ? 167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 126.977 144.948 103.780 1.00 33.84  ? 167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.689 145.752 103.612 1.00 33.48  ? 167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.841 146.742 102.481 1.00 34.30  ? 167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.517 144.831 103.353 1.00 34.38  ? 167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.046 143.495 106.125 1.00 40.79  ? 168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.394 142.989 106.342 1.00 30.27  ? 168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.323 141.535 106.788 1.00 41.90  ? 168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.559 141.180 107.692 1.00 44.04  ? 168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.127 143.863 107.371 1.00 38.54  ? 168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.499 143.313 107.644 1.00 45.29  ? 168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.223 145.290 106.866 1.00 45.95  ? 168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 131.124 140.686 106.145 1.00 46.49  ? 169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 131.107 139.253 106.404 1.00 52.33  ? 169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.992 138.848 107.577 1.00 52.73  ? 169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.671 137.891 108.289 1.00 51.45  ? 169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 131.543 138.490 105.150 1.00 44.38  ? 169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 130.681 138.764 104.059 1.00 48.27  ? 169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 133.098 139.555 107.799 1.00 42.47  ? 170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.102 139.115 108.755 1.00 39.49  ? 170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.390 140.240 109.726 1.00 43.84  ? 170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 134.165 141.412 109.423 1.00 49.87  ? 170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.429 138.752 108.091 1.00 45.38  ? 170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.371 137.537 106.806 1.00 60.31  ? 170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 134.928 139.872 110.881 1.00 33.56  ? 171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.489 140.833 111.815 1.00 23.03  ? 171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 136.685 140.193 112.495 1.00 26.64  ? 171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.538 139.206 113.220 1.00 42.05  ? 171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.448 141.279 112.841 1.00 30.32  ? 171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.199 141.836 112.225 1.00 28.98  ? 171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.173 143.128 111.731 1.00 25.35  ? 171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.057 141.061 112.120 1.00 29.55  ? 171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.031 143.638 111.155 1.00 19.46  ? 171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 130.911 141.569 111.545 1.00 31.25  ? 171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 130.898 142.859 111.063 1.00 27.00  ? 171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 137.865 140.749 112.253 1.00 23.07  ? 172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.105 140.234 112.813 1.00 23.55  ? 172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.560 141.187 113.908 1.00 19.85  ? 172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.946 142.324 113.625 1.00 24.09  ? 172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.178 140.087 111.735 1.00 25.66  ? 172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.006 138.971 110.703 1.00 11.99  ? 172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.062 139.386 109.587 1.00 26.30  ? 172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.356 138.578 110.139 1.00 16.11  ? 172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.521 140.716 115.151 1.00 26.27  ? 173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 139.766 141.551 116.316 1.00 31.70  ? 173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.096 141.187 116.956 1.00 32.42  ? 173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.394 140.008 117.166 1.00 41.36  ? 173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 138.646 141.400 117.348 1.00 29.35  ? 173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.210 141.621 116.879 1.00 29.95  ? 173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.261 141.461 118.050 1.00 33.20  ? 173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.051 142.988 116.239 1.00 33.44  ? 173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 141.891 142.205 117.261 1.00 37.02  ? 174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.112 142.033 118.032 1.00 32.19  ? 174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 142.789 142.206 119.510 1.00 33.26  ? 174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.221 143.227 119.910 1.00 43.67  ? 174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.172 143.044 117.597 1.00 39.00  ? 174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 144.725 142.815 116.206 1.00 35.21  ? 174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 145.992 141.992 116.216 1.00 37.13  ? 174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 146.475 141.656 117.316 1.00 41.17  ? 174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 146.511 141.684 115.122 1.00 43.40  ? 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.147 141.211 120.314 1.00 30.39  ? 175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 142.870 141.216 121.746 1.00 32.13  ? 175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.180 141.467 122.477 1.00 33.42  ? 175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.108 140.652 122.401 1.00 34.99  ? 175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.221 139.901 122.204 1.00 28.13  ? 175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 141.655 140.052 123.604 1.00 31.11  ? 175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.139 139.479 121.230 1.00 27.19  ? 175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.256 142.590 123.184 1.00 31.56  ? 176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.450 142.929 123.936 1.00 30.74  ? 176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 145.456 142.206 125.281 1.00 34.50  ? 176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 144.441 141.676 125.741 1.00 33.67  ? 176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 145.548 144.440 124.133 1.00 27.22  ? 176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 146.978 144.932 124.152 1.00 31.93  ? 176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 147.900 144.176 124.447 1.00 34.32  ? 176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.169 146.206 123.833 1.00 35.81  ? 176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 146.624 142.197 125.919 1.00 40.63  ? 177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 146.831 141.442 127.156 1.00 33.48  ? 177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 146.427 142.293 128.362 1.00 39.42  ? 177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.253 142.817 129.111 1.00 46.07  ? 177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.277 140.980 127.254 1.00 34.82  ? 177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 148.501 140.002 128.385 1.00 44.67  ? 177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 147.604 139.171 128.639 1.00 49.21  ? 177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 149.576 140.060 129.015 1.00 44.18  ? 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.114 142.419 128.540 1.00 32.98  ? 178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 144.563 143.118 129.691 1.00 33.54  ? 178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.124 142.676 129.893 1.00 34.57  ? 178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 142.464 142.227 128.954 1.00 43.93  ? 178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 144.640 144.640 129.522 1.00 36.70  ? 178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 143.440 145.154 128.976 1.00 41.88  ? 178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 142.648 142.798 131.135 1.00 34.87  ? 179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.258 142.458 131.422 1.00 31.19  ? 179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.305 143.434 130.750 1.00 27.59  ? 179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.233 143.039 130.282 1.00 31.60  ? 179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.013 142.428 132.930 1.00 41.10  ? 179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 139.601 142.005 133.341 1.00 35.17  ? 179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 139.322 140.575 132.906 1.00 29.89  ? 179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 139.382 142.174 134.834 1.00 34.08  ? 179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 140.669 144.718 130.708 1.00 36.80  ? 180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 139.850 145.691 129.993 1.00 35.66  ? 180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 139.790 145.365 128.508 1.00 35.23  ? 180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 138.719 145.425 127.892 1.00 40.41  ? 180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 140.401 147.100 130.208 1.00 35.20  ? 180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.888 147.324 131.624 1.00 39.59  ? 180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 141.807 146.651 132.090 1.00 46.65  ? 180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 140.277 148.275 132.315 1.00 41.66  ? 180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 140.931 145.001 127.920 1.00 39.97  ? 181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 140.959 144.653 126.504 1.00 31.64  ? 181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.183 143.371 126.233 1.00 35.85  ? 181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.520 143.253 125.200 1.00 42.46  ? 181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.402 144.522 126.026 1.00 39.44  ? 181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.116 145.857 125.964 1.00 45.59  ? 181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 142.690 146.721 125.171 1.00 44.72  ? 181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.101 146.046 126.708 1.00 47.23  ? 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.237 142.407 127.152 1.00 30.44  ? 182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.490 141.166 126.968 1.00 25.33  ? 182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 137.991 141.417 127.093 1.00 28.63  ? 182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.187 140.872 126.327 1.00 31.42  ? 182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 139.984 140.104 127.965 1.00 26.21  ? 182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.291 139.490 127.465 1.00 28.92  ? 182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 138.935 139.025 128.181 1.00 28.60  ? 182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.079 138.785 128.530 1.00 27.69  ? 182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 137.592 142.251 128.057 1.00 29.47  ? 183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.185 142.608 128.196 1.00 27.44  ? 183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 135.682 143.339 126.959 1.00 35.68  ? 183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 134.574 143.075 126.477 1.00 37.04  ? 183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 135.988 143.471 129.441 1.00 30.40  ? 183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 136.633 142.902 130.565 1.00 37.10  ? 183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 136.486 144.264 126.431 1.00 35.02  ? 184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.114 144.937 125.195 1.00 28.91  ? 184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.082 143.971 124.020 1.00 34.24  ? 184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.263 144.137 123.114 1.00 42.06  ? 184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.072 146.092 124.910 1.00 31.00  ? 184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.568 147.052 123.849 1.00 37.37  ? 184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 135.120 147.440 124.086 1.00 34.56  ? 184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.999 148.670 124.857 1.00 40.84  ? 184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 133.861 149.323 125.047 1.00 42.98  ? 184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 132.719 148.883 124.544 1.00 42.11  ? 184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 133.869 150.447 125.756 1.00 36.07  ? 184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 136.957 142.965 124.012 1.00 35.31  ? 185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 136.902 141.949 122.968 1.00 25.51  ? 185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.591 141.182 123.023 1.00 31.51  ? 185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 134.971 140.931 121.986 1.00 38.23  ? 185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.088 140.995 123.098 1.00 26.34  ? 185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.146 140.813 124.226 1.00 33.32  ? 186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 133.859 140.132 124.371 1.00 34.20  ? 186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 132.725 141.035 123.895 1.00 32.27  ? 186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 131.830 140.607 123.151 1.00 33.66  ? 186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 133.641 139.689 125.829 1.00 30.46  ? 186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 134.833 138.878 126.336 1.00 30.36  ? 186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.358 138.889 125.960 1.00 29.49  ? 186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.014 137.565 125.636 1.00 35.86  ? 186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 132.753 142.302 124.316 1.00 35.11  ? 187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 131.704 143.242 123.936 1.00 29.83  ? 187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.641 143.417 122.423 1.00 36.82  ? 187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.564 143.351 121.822 1.00 43.73  ? 187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 131.938 144.588 124.622 1.00 38.17  ? 187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.110 145.706 124.017 1.00 48.03  ? 187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 129.877 145.544 123.904 1.00 42.95  ? 187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 131.693 146.748 123.650 1.00 45.69  ? 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 132.795 143.632 121.792 1.00 35.25  ? 188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 132.841 143.856 120.353 1.00 35.72  ? 188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.466 142.586 119.601 1.00 35.60  ? 188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 131.798 142.640 118.563 1.00 43.20  ? 188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.230 144.382 119.949 1.00 33.86  ? 188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.483 145.751 120.580 1.00 38.62  ? 188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.349 144.499 118.452 1.00 35.75  ? 188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 135.877 146.277 120.345 1.00 36.81  ? 188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 132.871 141.422 120.117 1.00 29.14  ? 189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.495 140.163 119.489 1.00 20.59  ? 189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 130.983 139.992 119.482 1.00 25.47  ? 189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.398 139.605 118.467 1.00 37.10  ? 189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.166 138.996 120.212 1.00 28.37  ? 189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.566 139.189 120.298 1.00 40.45  ? 189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.329 140.294 120.606 1.00 34.99  ? 190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 128.872 140.193 120.645 1.00 28.54  ? 190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.217 141.237 119.746 1.00 29.87  ? 190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.235 140.940 119.052 1.00 38.35  ? 190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.371 140.326 122.081 1.00 35.04  ? 190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.845 139.214 122.995 1.00 34.89  ? 190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 127.882 139.072 124.511 1.00 41.08  ? 190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 127.904 140.765 125.082 1.00 31.97  ? 190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 128.751 142.462 119.736 1.00 34.35  ? 191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.139 143.531 118.949 1.00 39.39  ? 191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.321 143.299 117.455 1.00 36.43  ? 191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.572 143.848 116.639 1.00 37.99  ? 191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 128.721 144.885 119.355 1.00 31.68  ? 191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 128.367 145.315 120.768 1.00 35.13  ? 191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 126.927 145.762 120.907 1.00 38.88  ? 191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 126.178 145.810 119.932 1.00 44.26  ? 191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.527 146.080 122.130 1.00 37.17  ? 191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.328 142.517 117.073 1.00 36.28  ? 192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.506 142.200 115.662 1.00 29.05  ? 192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.831 140.890 115.282 1.00 37.71  ? 192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.504 140.688 114.107 1.00 48.95  ? 192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 130.995 142.164 115.321 1.00 28.85  ? 192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 131.690 143.517 115.496 1.00 35.08  ? 192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.189 143.383 115.338 1.00 33.57  ? 192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.134 144.543 114.522 1.00 28.68  ? 192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.615 139.993 116.247 1.00 36.42  ? 193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 127.825 138.798 115.985 1.00 31.13  ? 193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.344 139.113 115.849 1.00 40.29  ? 193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.666 138.484 115.031 1.00 48.74  ? 193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.037 137.770 117.093 1.00 35.11  ? 193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 129.368 137.808 117.569 1.00 37.30  ? 193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 125.827 140.069 116.623 1.00 41.25  ? 194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.457 140.520 116.425 1.00 40.20  ? 194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.251 141.170 115.065 1.00 49.73  ? 194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.109 141.255 114.599 1.00 52.14  ? 194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.042 141.502 117.526 1.00 31.97  ? 194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 124.811 142.806 117.511 1.00 37.84  ? 194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.897 144.018 117.610 1.00 46.81  ? 194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.880 143.873 118.727 1.00 46.95  ? 194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 121.873 144.968 118.704 1.00 40.76  ? 194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.323 141.630 114.425 1.00 47.47  ? 195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.263 142.163 113.074 1.00 41.52  ? 195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.276 141.069 112.014 1.00 46.41  ? 195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.978 141.350 110.849 1.00 56.60  ? 195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.431 143.125 112.836 1.00 39.44  ? 195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.383 144.427 113.638 1.00 48.38  ? 195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.575 145.310 113.307 1.00 46.77  ? 195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.072 145.163 113.408 1.00 46.71  ? 195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.615 139.837 112.386 1.00 35.74  ? 196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.564 138.723 111.462 1.00 37.02  ? 196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.920 138.195 111.041 1.00 43.36  ? 196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.086 136.987 110.848 1.00 44.86  ? 196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.895 139.087 110.893 1.00 41.48  ? 197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.197 138.674 110.408 1.00 42.26  ? 197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 129.955 137.834 111.419 1.00 37.65  ? 197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.834 138.007 112.631 1.00 26.92  ? 197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.752 136.903 110.897 1.00 28.17  ? 198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.603 136.104 111.755 1.00 25.37  ? 198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 132.769 136.908 112.298 1.00 28.42  ? 198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.287 137.816 111.650 1.00 38.94  ? 198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.187 136.564 113.513 1.00 34.89  ? 199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.221 137.305 114.224 1.00 24.40  ? 199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.392 136.376 114.506 1.00 22.12  ? 199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.207 135.282 115.046 1.00 34.72  ? 199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 133.687 137.912 115.535 1.00 19.09  ? 199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 134.792 138.655 116.263 1.00 20.06  ? 199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.516 138.835 115.254 1.00 30.25  ? 199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.593 136.814 114.142 1.00 22.12  ? 200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 137.826 136.107 114.448 1.00 3.29   ? 200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.680 136.961 115.372 1.00 19.27  ? 200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 138.783 138.178 115.186 1.00 27.48  ? 200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.604 135.774 113.174 1.00 15.35  ? 200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.693 134.914 113.452 1.00 21.04  ? 200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.284 136.328 116.371 1.00 31.41  ? 201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.058 137.034 117.380 1.00 19.40  ? 201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.469 136.472 117.458 1.00 16.30  ? 201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.665 135.254 117.451 1.00 32.37  ? 201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.379 136.947 118.746 1.00 24.50  ? 201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 137.982 137.568 118.782 1.00 24.63  ? 201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 136.913 136.489 118.819 1.00 21.27  ? 201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 137.844 138.515 119.960 1.00 27.31  ? 201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.447 137.372 117.528 1.00 18.44  ? 202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 143.846 137.000 117.701 1.00 22.31  ? 202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.147 136.969 119.193 1.00 27.20  ? 202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.142 138.011 119.857 1.00 41.49  ? 202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 144.760 137.984 116.975 1.00 25.32  ? 202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.195 137.507 116.913 1.00 19.89  ? 202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.476 136.322 117.084 1.00 27.97  ? 202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.114 138.433 116.667 1.00 22.21  ? 202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.408 135.777 119.721 1.00 19.68  ? 203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 144.658 135.592 121.143 1.00 24.76  ? 203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.133 135.389 121.460 1.00 22.87  ? 203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.468 135.027 122.592 1.00 26.12  ? 203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 143.841 134.412 121.668 1.00 22.64  ? 203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.339 134.448 121.381 1.00 24.77  ? 203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 141.626 133.370 122.169 1.00 23.19  ? 203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 141.749 135.814 121.693 1.00 27.85  ? 203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.023 135.617 120.490 1.00 20.36  ? 204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.445 135.392 120.715 1.00 18.22  ? 204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.054 136.416 121.661 1.00 36.67  ? 204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.079 136.128 122.288 1.00 34.82  ? 204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.196 135.405 119.385 1.00 22.40  ? 204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 148.684 134.425 118.500 1.00 36.41  ? 204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 148.458 137.600 121.776 1.00 43.80  ? 205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 148.943 138.608 122.708 1.00 30.22  ? 205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 148.560 138.317 124.150 1.00 29.78  ? 205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.253 138.778 125.063 1.00 37.63  ? 205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 148.414 139.988 122.317 1.00 27.66  ? 205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 148.983 140.503 121.018 1.00 31.72  ? 205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 148.360 141.823 120.636 1.00 35.84  ? 205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.122 142.458 119.498 1.00 38.55  ? 205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.181 141.564 118.312 1.00 32.09  ? 205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 147.477 137.578 124.373 1.00 30.34  ? 206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.094 137.202 125.724 1.00 24.34  ? 206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.173 136.333 126.354 1.00 27.86  ? 206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 148.670 135.387 125.738 1.00 35.48  ? 206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 145.763 136.452 125.709 1.00 25.50  ? 206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 144.619 137.127 124.956 1.00 30.35  ? 206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 143.400 136.230 124.948 1.00 29.33  ? 206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 144.296 138.465 125.585 1.00 31.71  ? 206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 148.534 136.660 127.590 1.00 33.81  ? 207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 149.563 135.899 128.276 1.00 37.09  ? 207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.042 134.514 128.648 1.00 42.53  ? 207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 147.840 134.295 128.828 1.00 44.22  ? 207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.054 136.657 129.510 1.00 37.63  ? 207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.015 136.883 130.585 1.00 37.32  ? 207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 149.574 137.772 131.686 1.00 39.16  ? 207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 149.702 139.161 131.265 1.00 38.29  ? 207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 149.550 140.203 132.071 1.00 34.64  ? 207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 149.297 140.048 133.360 1.00 42.66  ? 207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 149.651 141.430 131.572 1.00 36.38  ? 207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 149.970 133.569 128.756 1.00 42.87  ? 208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 149.639 132.160 128.879 1.00 39.07  ? 208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 149.146 131.825 130.284 1.00 44.15  ? 208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 149.072 132.678 131.172 1.00 50.70  ? 208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.849 131.304 128.510 1.00 41.81  ? 208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.790 130.559 130.480 1.00 46.33  ? 209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 148.375 130.079 131.789 1.00 43.67  ? 209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 149.570 130.006 132.728 1.00 54.35  ? 209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 150.659 129.569 132.344 1.00 54.74  ? 209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 147.712 128.709 131.660 1.00 44.89  ? 209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.047 128.204 132.927 1.00 51.27  ? 209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 146.165 127.002 132.632 1.00 51.41  ? 209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 146.958 125.707 132.682 1.00 52.02  ? 209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.078 125.773 133.659 1.00 54.79  ? 209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.363 130.435 133.969 1.00 53.77  ? 210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 150.442 130.485 134.929 1.00 53.92  ? 210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 151.274 131.744 134.891 1.00 53.68  ? 210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 152.346 131.777 135.506 1.00 58.85  ? 210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.825 132.777 134.187 1.00 46.79  ? 211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 151.525 134.050 134.152 1.00 46.57  ? 211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.068 134.940 135.303 1.00 53.48  ? 211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.143 134.615 136.048 1.00 55.42  ? 211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 151.301 134.762 132.819 1.00 46.67  ? 211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 151.934 134.069 131.630 1.00 47.72  ? 211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 152.917 134.959 130.901 1.00 54.37  ? 211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 153.708 135.647 131.579 1.00 57.40  ? 211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 152.895 134.979 129.653 1.00 51.62  ? 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 151.737 136.082 135.436 1.00 51.17  ? 212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 151.498 136.975 136.559 1.00 47.30  ? 212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 150.519 138.082 136.193 1.00 49.04  ? 212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 150.564 138.635 135.091 1.00 56.41  ? 212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 152.816 137.585 137.037 1.00 50.07  ? 212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 149.627 138.400 137.129 1.00 47.92  ? 213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 148.740 139.554 137.030 1.00 50.03  ? 213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 149.129 140.511 138.146 1.00 53.85  ? 213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 148.783 140.289 139.313 1.00 60.94  ? 213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 147.261 139.159 137.134 1.00 48.42  ? 213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 146.944 137.990 136.206 1.00 53.39  ? 213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 146.370 140.347 136.805 1.00 46.69  ? 213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 145.654 137.280 136.547 1.00 51.68  ? 213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 149.844 141.581 137.791 1.00 57.42  ? 214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 150.364 142.546 138.761 1.00 59.25  ? 214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 151.243 141.856 139.804 1.00 64.81  ? 214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 150.897 141.769 140.982 1.00 67.66  ? 214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 149.236 143.337 139.429 1.00 59.52  ? 214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 149.206 144.813 139.054 1.00 56.69  ? 214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 147.957 145.526 139.573 1.00 61.00  ? 214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 147.097 144.629 140.453 1.00 60.36  ? 214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 145.959 144.041 139.698 1.00 59.73  ? 214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 152.367 141.313 139.332 1.00 66.42  ? 215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 153.484 140.811 140.133 1.00 70.80  ? 215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.128 139.664 141.077 1.00 71.24  ? 215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 153.956 139.269 141.905 1.00 70.31  ? 215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.163 141.985 140.876 1.00 67.86  ? 215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 153.509 142.365 142.222 1.00 69.82  ? 215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 152.719 141.609 142.825 1.00 68.79  ? 215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.805 143.484 142.688 1.00 69.31  ? 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 151.920 139.117 140.971 1.00 66.39  ? 216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.576 137.896 141.695 1.00 67.47  ? 216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 151.608 136.742 140.695 1.00 72.63  ? 216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.008 136.815 139.621 1.00 75.74  ? 216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.222 138.009 142.413 1.00 70.06  ? 216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.037 137.968 141.447 1.00 66.09  ? 216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.097 136.929 143.478 1.00 71.77  ? 216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.349 135.689 141.026 1.00 72.47  ? 217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 152.719 134.693 140.031 1.00 71.25  ? 217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 151.664 133.592 139.925 1.00 71.37  ? 217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 150.844 133.383 140.825 1.00 72.17  ? 217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.091 134.111 140.359 1.00 73.12  ? 217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.117 135.165 140.731 1.00 72.75  ? 217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 155.935 135.625 139.544 1.00 73.66  ? 217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.690 134.805 138.982 1.00 73.87  ? 217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 155.819 136.811 139.169 1.00 70.10  ? 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 151.700 132.877 138.796 1.00 67.93  ? 218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.797 131.769 138.503 1.00 67.59  ? 218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.341 132.177 138.667 1.00 68.59  ? 218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.542 131.436 139.248 1.00 67.81  ? 218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.112 130.564 139.391 1.00 65.64  ? 218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 150.937 129.248 138.664 1.00 68.85  ? 218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 149.861 128.650 138.689 1.00 71.77  ? 218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 151.994 128.790 138.004 1.00 66.64  ? 218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.986 133.352 138.154 1.00 58.44  ? 219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 147.662 133.920 138.361 1.00 57.02  ? 219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 146.740 133.736 137.162 1.00 55.71  ? 219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 145.535 133.527 137.333 1.00 55.67  ? 219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 147.785 135.409 138.708 1.00 58.05  ? 219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.276 133.814 135.948 1.00 55.07  ? 220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 146.444 133.708 134.759 1.00 52.28  ? 220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.960 132.278 134.561 1.00 53.41  ? 220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 146.642 131.317 134.922 1.00 55.39  ? 220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 147.220 134.155 133.524 1.00 48.01  ? 220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.435 133.406 133.432 1.00 59.17  ? 220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.561 135.618 133.631 1.00 46.94  ? 220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 144.772 132.143 133.978 1.00 52.63  ? 221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.265 130.850 133.548 1.00 57.53  ? 221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 144.462 130.621 132.055 1.00 58.30  ? 221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.933 129.646 131.512 1.00 55.74  ? 221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 142.788 130.707 133.916 1.00 57.94  ? 221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.901 131.836 133.435 1.00 56.10  ? 221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 140.452 131.584 133.818 1.00 57.29  ? 221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.325 131.166 135.274 1.00 55.07  ? 221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 140.889 132.190 136.198 1.00 53.90  ? 221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.206 131.496 131.388 1.00 55.41  ? 222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 145.581 131.309 130.002 1.00 50.67  ? 222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 144.552 131.861 129.038 1.00 48.97  ? 222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 143.561 132.496 129.411 1.00 51.89  ? 222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.815 131.603 127.754 1.00 46.37  ? 223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.882 131.996 126.704 1.00 47.85  ? 223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 142.665 131.091 126.639 1.00 45.06  ? 223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 141.697 131.428 125.953 1.00 48.52  ? 223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 144.569 132.017 125.325 1.00 40.60  ? 223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 145.906 132.733 125.408 1.00 38.64  ? 223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.747 130.603 124.794 1.00 39.88  ? 223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.683 129.954 127.339 1.00 43.63  ? 224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.545 129.041 127.307 1.00 40.15  ? 224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.341 129.655 128.013 1.00 46.43  ? 224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.195 129.473 127.586 1.00 49.73  ? 224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 141.937 127.682 127.913 1.00 45.55  ? 224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 140.730 126.761 127.992 1.00 44.10  ? 224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.042 127.041 127.091 1.00 44.99  ? 224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.574 130.391 129.101 1.00 39.75  ? 225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 139.478 131.108 129.736 1.00 35.60  ? 225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.881 132.168 128.830 1.00 38.03  ? 225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 137.661 132.351 128.785 1.00 46.70  ? 225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 139.735 132.881 128.093 1.00 28.01  ? 226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.243 133.864 127.137 1.00 32.38  ? 226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 138.476 133.183 126.012 1.00 36.65  ? 226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 137.489 133.730 125.510 1.00 38.19  ? 226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.408 134.711 126.596 1.00 34.37  ? 226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 139.876 135.891 125.799 1.00 37.05  ? 226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.283 135.187 127.741 1.00 38.47  ? 226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.905 131.988 125.594 1.00 40.23  ? 227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.138 131.240 124.603 1.00 34.85  ? 227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.791 130.804 125.157 1.00 36.64  ? 227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.798 130.788 124.427 1.00 42.87  ? 227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.925 130.029 124.104 1.00 33.28  ? 227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.259 130.366 123.487 1.00 28.10  ? 227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.884 129.027 122.469 1.00 46.81  ? 227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 141.001 127.722 123.681 1.00 46.72  ? 227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.735 130.432 126.436 1.00 33.96  ? 228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.453 130.121 127.061 1.00 36.30  ? 228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 134.529 131.330 127.022 1.00 38.57  ? 228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.348 131.224 126.657 1.00 47.46  ? 228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.669 129.685 128.506 1.00 39.36  ? 228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 135.856 128.206 128.720 1.00 40.54  ? 228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.027 127.984 129.650 1.00 48.43  ? 228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 136.755 126.850 130.606 1.00 46.86  ? 228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 137.872 126.661 131.572 1.00 49.02  ? 228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.057 132.494 127.408 1.00 24.10  ? 229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.262 133.717 127.393 1.00 23.31  ? 229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 133.788 134.050 125.985 1.00 28.44  ? 229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 132.622 134.405 125.784 1.00 35.93  ? 229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.071 134.877 127.970 1.00 36.33  ? 229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 135.265 134.935 129.483 1.00 27.49  ? 229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 136.397 135.885 129.817 1.00 28.47  ? 229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 133.982 135.374 130.158 1.00 31.32  ? 229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 134.676 133.935 124.996 1.00 31.61  ? 230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.305 134.226 123.617 1.00 26.33  ? 230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.276 133.230 123.097 1.00 33.87  ? 230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.345 133.611 122.382 1.00 46.53  ? 230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.549 134.221 122.732 1.00 33.72  ? 230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.447 135.449 122.850 1.00 38.56  ? 230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 137.770 135.209 122.146 1.00 37.73  ? 230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 135.745 136.667 122.280 1.00 33.36  ? 230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.429 131.952 123.445 1.00 36.57  ? 231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 132.489 130.936 122.995 1.00 35.10  ? 231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.100 131.186 123.561 1.00 40.75  ? 231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.101 131.092 122.840 1.00 48.50  ? 231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.999 129.551 123.392 1.00 34.51  ? 231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.911 128.502 123.384 1.00 52.62  ? 231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 131.488 128.092 122.284 1.00 55.46  ? 231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.488 128.075 124.479 1.00 50.80  ? 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.016 131.535 124.845 1.00 37.11  ? 232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 129.708 131.824 125.423 1.00 36.47  ? 232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.152 133.152 124.927 1.00 36.40  ? 232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 127.931 133.316 124.838 1.00 50.84  ? 232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.800 131.801 126.942 1.00 36.74  ? 232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 129.985 130.403 127.477 1.00 48.94  ? 232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 129.017 129.710 127.787 1.00 49.31  ? 232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 131.235 129.964 127.555 1.00 47.33  ? 232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.026 134.105 124.594 1.00 28.70  ? 233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 129.572 135.352 123.991 1.00 25.03  ? 233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 128.972 135.115 122.611 1.00 32.55  ? 233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 127.952 135.716 122.258 1.00 41.84  ? 233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 130.733 136.340 123.911 1.00 27.45  ? 233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 129.597 134.243 121.817 1.00 38.88  ? 234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.067 133.938 120.492 1.00 35.22  ? 234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 127.812 133.084 120.589 1.00 40.30  ? 234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 126.905 133.208 119.756 1.00 40.95  ? 234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.130 133.243 119.643 1.00 31.07  ? 234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.234 134.152 119.192 1.00 34.73  ? 234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 130.951 135.323 118.516 1.00 40.10  ? 234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.556 133.833 119.435 1.00 30.28  ? 234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 131.965 136.160 118.100 1.00 34.88  ? 234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.573 134.669 119.025 1.00 32.29  ? 234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.277 135.830 118.356 1.00 32.08  ? 234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 127.741 132.208 121.593 1.00 41.56  ? 235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.513 131.458 121.831 1.00 39.21  ? 235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.372 132.387 122.223 1.00 43.24  ? 235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.229 132.187 121.799 1.00 46.55  ? 235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.738 130.405 122.914 1.00 37.77  ? 235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.425 128.990 122.469 1.00 49.67  ? 235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.179 128.073 123.657 1.00 47.66  ? 235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.191 128.219 124.696 1.00 48.57  ? 235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.440 127.784 124.597 1.00 46.85  ? 235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 128.873 127.164 123.512 1.00 45.69  ? 235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.275 127.973 125.615 1.00 39.13  ? 235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 125.661 133.404 123.037 1.00 38.68  ? 236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 124.621 134.348 123.430 1.00 43.00  ? 236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.151 135.176 122.240 1.00 44.24  ? 236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 122.948 135.400 122.069 1.00 47.40  ? 236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.130 135.254 124.549 1.00 36.16  ? 236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.061 136.143 125.132 1.00 40.07  ? 236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.089 135.624 125.973 1.00 39.19  ? 236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.023 137.501 124.845 1.00 32.93  ? 236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.110 136.425 126.511 1.00 41.61  ? 236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.044 138.313 125.380 1.00 32.30  ? 236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.091 137.767 126.212 1.00 37.28  ? 236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.111 138.563 126.751 1.00 38.00  ? 236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.084 135.643 121.415 1.00 43.85  ? 237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 124.745 136.377 120.196 1.00 46.92  ? 237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.564 135.405 119.028 1.00 56.79  ? 237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.318 135.393 118.056 1.00 59.08  ? 237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 125.810 137.424 119.896 1.00 40.92  ? 237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.532 134.571 119.150 1.00 68.59  ? 238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.261 133.512 118.189 1.00 67.54  ? 238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.355 133.951 117.050 1.00 73.03  ? 238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 121.886 133.089 116.297 1.00 78.27  ? 238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 122.648 132.303 118.898 1.00 72.35  ? 238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 123.624 131.156 119.035 1.00 71.53  ? 238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 124.693 131.207 118.393 1.00 72.34  ? 238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 123.325 130.207 119.790 1.00 67.74  ? 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.095 135.253 116.911 1.00 82.10  ? 239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.344 135.791 115.776 1.00 85.28  ? 239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.984 135.106 115.639 1.00 87.36  ? 239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.636 134.581 114.580 1.00 86.05  ? 239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 122.156 135.656 114.484 1.00 84.47  ? 239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 123.598 136.114 114.618 1.00 81.42  ? 239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 124.467 135.671 113.457 1.00 83.87  ? 239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.011 135.598 112.316 1.00 86.40  ? 239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 125.728 135.370 113.745 1.00 80.93  ? 239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 119.229 135.087 116.742 1.00 96.05  ? 240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.923 134.442 116.879 1.00 98.05  ? 240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.033 132.921 116.946 1.00 100.04 ? 240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.045 132.249 117.270 1.00 99.76  ? 240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.966 134.844 115.741 1.00 99.56  ? 240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.577 134.221 115.753 1.00 100.22 ? 240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 114.212 135.359 115.510 1.00 106.16 ? 240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.861 134.191 115.398 1.00 97.95  ? 240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.215 132.356 116.724 1.00 101.55 ? 241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.338 130.933 116.507 1.00 100.43 ? 241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.108 130.513 115.074 1.00 102.44 ? 241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 119.330 129.341 114.745 1.00 100.72 ? 241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 118.674 131.438 114.213 1.00 110.61 ? 242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.506 131.133 112.796 1.00 111.49 ? 242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 119.832 130.728 112.172 1.00 110.88 ? 242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 119.898 129.766 111.397 1.00 107.14 ? 242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 117.920 132.347 112.076 1.00 109.54 ? 242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.453 132.605 112.377 1.00 108.59 ? 242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.938 133.868 111.716 1.00 109.92 ? 242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.646 134.508 110.938 1.00 111.68 ? 242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.702 134.240 112.030 1.00 107.65 ? 242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 120.897 131.456 112.496 1.00 101.12 ? 243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.261 131.045 112.194 1.00 100.78 ? 243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.068 131.206 113.470 1.00 99.61  ? 243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.174 132.316 113.998 1.00 96.91  ? 243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 122.866 131.876 111.058 1.00 98.02  ? 243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.382 131.819 111.006 1.00 98.29  ? 243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 124.862 130.463 110.518 1.00 100.88 ? 243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 126.310 130.328 110.607 1.00 100.52 ? 243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 127.129 130.322 109.564 1.00 99.09  ? 243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 126.674 130.449 108.328 1.00 96.53  ? 243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 128.436 130.188 109.768 1.00 97.90  ? 243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.626 130.103 113.965 1.00 88.50  ? 244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.315 130.127 115.247 1.00 88.29  ? 244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.519 131.057 115.193 1.00 86.89  ? 244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.191 131.174 114.166 1.00 83.98  ? 244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.756 128.716 115.638 1.00 85.37  ? 244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.636 127.850 116.191 1.00 86.20  ? 244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.139 126.525 116.728 1.00 86.56  ? 244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.030 125.904 116.148 1.00 84.86  ? 244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.566 126.083 117.842 1.00 84.76  ? 244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 125.780 131.732 116.312 1.00 70.64  ? 245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 126.911 132.632 116.406 1.00 65.45  ? 245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.227 131.918 116.188 1.00 64.11  ? 245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.624 131.067 116.990 1.00 62.19  ? 245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 128.912 132.258 115.101 1.00 57.70  ? 246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.154 131.605 114.715 1.00 56.45  ? 246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.316 132.552 114.965 1.00 53.24  ? 246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.292 133.705 114.523 1.00 47.83  ? 246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.118 131.184 113.246 1.00 55.55  ? 246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.137 130.187 113.024 1.00 62.30  ? 246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.324 132.065 115.671 1.00 32.67  ? 247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 133.493 132.866 115.972 1.00 18.38  ? 247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 134.747 132.026 115.897 1.00 19.45  ? 247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 134.729 130.819 116.147 1.00 36.87  ? 247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 135.846 132.683 115.543 1.00 22.12  ? 248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.141 132.034 115.430 1.00 21.89  ? 248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.105 132.620 116.448 1.00 18.86  ? 248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 137.983 133.780 116.852 1.00 26.19  ? 248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 137.724 132.184 114.022 1.00 18.58  ? 248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.061 131.798 116.867 1.00 20.85  ? 249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.146 132.226 117.737 1.00 12.54  ? 249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.454 131.747 117.133 1.00 12.34  ? 249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.589 130.567 116.796 1.00 28.01  ? 249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.977 131.677 119.157 1.00 23.96  ? 249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.409 132.657 116.987 1.00 11.89  ? 250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 143.697 132.347 116.389 1.00 17.51  ? 250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 144.800 132.502 117.424 1.00 13.05  ? 250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 144.788 133.442 118.224 1.00 24.98  ? 250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 143.976 133.247 115.186 1.00 22.60  ? 250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.508 132.670 113.871 1.00 22.65  ? 250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.167 132.686 113.522 1.00 14.66  ? 250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.411 132.108 112.979 1.00 20.26  ? 250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.735 132.158 112.324 1.00 7.06   ? 250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.988 131.577 111.779 1.00 24.57  ? 250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.651 131.606 111.456 1.00 21.53  ? 250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.225 131.080 110.259 1.00 25.20  ? 250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 145.749 131.572 117.407 1.00 14.43  ? 251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 146.867 131.594 118.338 1.00 20.26  ? 251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.140 131.220 117.599 1.00 25.15  ? 251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.143 130.273 116.808 1.00 32.19  ? 251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 146.639 130.632 119.507 1.00 32.54  ? 251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.529 130.866 120.726 1.00 17.93  ? 251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.038 132.059 121.508 1.00 21.81  ? 251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 147.585 129.637 121.605 1.00 22.04  ? 251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.212 131.963 117.858 1.00 34.02  ? 252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.508 131.613 117.299 1.00 30.78  ? 252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 150.974 130.279 117.864 1.00 29.46  ? 252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 150.762 129.976 119.041 1.00 35.94  ? 252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.529 132.707 117.603 1.00 23.99  ? 252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 152.676 132.724 116.616 1.00 34.95  ? 252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 153.533 131.843 116.629 1.00 43.19  ? 252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 152.696 133.727 115.749 1.00 32.75  ? 252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 151.601 129.465 117.011 1.00 27.12  ? 253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.047 128.149 117.445 1.00 28.93  ? 253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.171 128.241 118.469 1.00 36.88  ? 253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.427 127.271 119.192 1.00 43.44  ? 253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.473 127.299 116.235 1.00 28.66  ? 253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 152.423 125.812 116.589 1.00 27.07  ? 253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.858 127.699 115.759 1.00 32.82  ? 253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.148 124.914 115.419 1.00 34.05  ? 253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 153.846 129.382 118.559 1.00 37.46  ? 254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 154.877 129.594 119.564 1.00 31.18  ? 254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.320 130.142 120.870 1.00 35.36  ? 254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.079 130.310 121.829 1.00 45.76  ? 254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 155.959 130.527 119.017 1.00 34.54  ? 254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 156.918 129.849 118.087 1.00 40.43  ? 254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 157.814 128.909 118.563 1.00 39.74  ? 254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 156.912 130.133 116.733 1.00 43.79  ? 254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 158.694 128.278 117.714 1.00 41.65  ? 254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 157.790 129.502 115.877 1.00 45.63  ? 254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 158.683 128.574 116.369 1.00 45.65  ? 254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.023 130.434 120.922 1.00 34.34  ? 255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.377 130.767 122.181 1.00 24.19  ? 255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 152.407 129.559 123.107 1.00 36.86  ? 255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 152.240 128.418 122.669 1.00 47.67  ? 255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 150.937 131.215 121.927 1.00 31.27  ? 255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.295 131.912 123.086 1.00 34.27  ? 255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 149.977 131.268 124.262 1.00 36.92  ? 255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 149.892 133.194 123.240 1.00 31.12  ? 255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.415 132.126 125.094 1.00 26.15  ? 255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 149.351 133.302 124.498 1.00 21.46  ? 255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 152.630 129.814 124.396 1.00 43.25  ? 256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.755 128.723 125.355 1.00 42.06  ? 256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.473 127.903 125.442 1.00 43.83  ? 256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.521 126.673 125.558 1.00 47.69  ? 256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.136 129.281 126.723 1.00 44.24  ? 256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.108 128.419 127.490 1.00 48.63  ? 256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.375 127.327 128.235 1.00 47.04  ? 256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.017 127.718 128.593 1.00 49.92  ? 256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.190 126.974 129.315 1.00 51.43  ? 256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 151.552 125.785 129.769 1.00 48.85  ? 256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 149.972 127.432 129.586 1.00 48.57  ? 256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.326 128.559 125.378 1.00 40.46  ? 257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.029 127.893 125.467 1.00 33.25  ? 257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.657 127.134 124.215 1.00 39.83  ? 257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.487 126.749 124.133 1.00 44.16  ? 257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.936 128.915 125.779 1.00 38.18  ? 257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.989 129.404 127.205 1.00 47.43  ? 257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 148.724 128.801 128.015 1.00 52.83  ? 257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 147.292 130.389 127.517 1.00 53.19  ? 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.564 126.901 123.264 1.00 45.46  ? 258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.172 126.293 121.995 1.00 43.60  ? 258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.656 124.875 122.211 1.00 43.59  ? 258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.731 124.427 121.524 1.00 48.92  ? 258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.344 126.335 120.994 1.00 41.06  ? 258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.872 125.905 119.605 1.00 37.84  ? 258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.513 125.480 121.467 1.00 36.04  ? 258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.757 126.766 119.062 1.00 33.24  ? 258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.237 124.145 123.166 1.00 46.09  ? 259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 148.767 122.790 123.436 1.00 41.31  ? 259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.379 122.803 124.064 1.00 43.67  ? 259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.507 122.023 123.668 1.00 48.03  ? 259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 149.761 122.055 124.333 1.00 48.72  ? 259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 150.939 121.497 123.560 1.00 48.93  ? 259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 150.769 120.703 122.635 1.00 47.41  ? 259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.143 121.908 123.938 1.00 44.40  ? 259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.155 123.683 125.044 1.00 42.07  ? 260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 145.820 123.825 125.614 1.00 39.92  ? 260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 144.855 124.446 124.614 1.00 36.51  ? 260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 143.651 124.168 124.658 1.00 41.64  ? 260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 145.880 124.664 126.889 1.00 41.86  ? 260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 146.896 124.140 127.882 1.00 48.61  ? 260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 148.061 123.932 127.486 1.00 51.89  ? 260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 146.529 123.933 129.058 1.00 46.67  ? 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.364 125.292 123.716 1.00 41.35  ? 261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.538 125.854 122.653 1.00 39.29  ? 261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 143.994 124.756 121.748 1.00 28.40  ? 261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.822 124.786 121.358 1.00 31.44  ? 261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.369 126.861 121.857 1.00 40.36  ? 261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.647 127.494 120.707 1.00 36.37  ? 261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.851 128.607 120.907 1.00 30.43  ? 261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.795 127.005 119.422 1.00 37.35  ? 261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.195 129.204 119.852 1.00 29.94  ? 261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.142 127.599 118.365 1.00 34.49  ? 261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.344 128.701 118.582 1.00 33.68  ? 261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 144.835 123.778 121.410 1.00 35.42  ? 262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.403 122.647 120.596 1.00 39.31  ? 262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.600 121.632 121.398 1.00 44.86  ? 262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 142.744 120.942 120.832 1.00 42.92  ? 262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.618 121.963 119.971 1.00 38.80  ? 262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.467 122.822 119.040 1.00 33.34  ? 262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.755 122.104 118.689 1.00 32.96  ? 262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 145.679 123.160 117.796 1.00 39.11  ? 262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 143.862 121.520 122.703 1.00 52.97  ? 263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.186 120.524 123.525 1.00 44.79  ? 263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.689 120.772 123.635 1.00 48.85  ? 263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 140.950 119.855 124.009 1.00 62.87  ? 263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 143.800 120.490 124.925 1.00 53.07  ? 263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.080 119.682 124.985 1.00 58.89  ? 263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.262 118.786 124.135 1.00 61.27  ? 263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 145.906 119.942 125.886 1.00 54.12  ? 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.225 121.981 123.325 1.00 44.07  ? 264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 139.807 122.293 123.442 1.00 47.06  ? 264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 138.978 121.714 122.304 1.00 52.14  ? 264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 137.754 121.617 122.438 1.00 49.98  ? 264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 139.605 123.807 123.505 1.00 49.16  ? 264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.089 124.408 122.298 1.00 50.39  ? 264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.362 124.385 124.687 1.00 50.46  ? 264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.607 121.334 121.196 1.00 53.17  ? 265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 138.905 120.723 120.077 1.00 53.48  ? 265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 138.924 119.202 120.117 1.00 52.02  ? 265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.341 118.568 119.232 1.00 50.25  ? 265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.498 121.206 118.751 1.00 50.88  ? 265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.033 122.587 118.342 1.00 49.84  ? 265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.531 122.724 118.491 1.00 50.50  ? 265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.060 124.091 118.050 1.00 48.98  ? 265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.648 124.343 118.440 1.00 50.33  ? 265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.580 118.605 121.107 1.00 57.62  ? 266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 139.567 117.157 121.239 1.00 56.18  ? 266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.184 116.676 121.655 1.00 62.31  ? 266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.508 117.309 122.473 1.00 64.71  ? 266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 140.611 116.705 122.259 1.00 57.44  ? 266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.042 116.797 121.762 1.00 60.55  ? 266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.077 116.760 122.889 1.00 60.18  ? 266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 142.874 115.606 123.871 1.00 61.19  ? 266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 141.887 115.883 124.957 1.00 62.68  ? 266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 137.756 115.552 121.079 1.00 67.79  ? 267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 136.474 114.972 121.463 1.00 67.49  ? 267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.532 114.463 122.897 1.00 66.44  ? 267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.561 114.582 123.654 1.00 66.16  ? 267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.070 113.858 120.479 1.00 69.73  ? 267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 136.137 114.364 119.038 1.00 68.62  ? 267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 134.673 113.348 120.792 1.00 68.73  ? 267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 137.338 113.862 118.269 1.00 66.75  ? 267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 137.672 113.896 123.295 1.00 68.91  ? 268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 137.851 113.406 124.656 1.00 72.66  ? 268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 137.982 114.528 125.678 1.00 72.21  ? 268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 137.973 114.246 126.881 1.00 69.20  ? 268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.081 112.501 124.728 1.00 70.15  ? 268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.250 113.195 124.326 1.00 66.44  ? 268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.114 115.778 125.236 1.00 78.13  ? 269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.266 116.887 126.167 1.00 76.46  ? 269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.021 117.043 127.028 1.00 77.89  ? 269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.890 116.914 126.550 1.00 74.96  ? 269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.543 118.184 125.406 1.00 72.65  ? 269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.237 117.322 128.310 1.00 83.25  ? 270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.138 117.492 129.245 1.00 82.00  ? 270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 135.393 118.797 128.972 1.00 80.80  ? 270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 135.902 119.713 128.321 1.00 82.61  ? 270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 136.655 117.468 130.683 1.00 82.97  ? 270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 137.821 118.413 130.897 1.00 83.11  ? 270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 137.584 119.630 131.042 1.00 80.82  ? 270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 138.975 117.938 130.922 1.00 82.31  ? 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.163 118.869 129.487 1.00 84.26  ? 271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.345 120.063 129.315 1.00 85.69  ? 271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 133.930 121.276 130.025 1.00 86.39  ? 271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.515 122.405 129.741 1.00 84.99  ? 271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 131.924 119.805 129.820 1.00 84.29  ? 271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.263 118.567 129.230 1.00 85.69  ? 271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.433 118.469 127.726 1.00 88.52  ? 271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 131.179 119.474 127.028 1.00 88.19  ? 271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.820 117.385 127.240 1.00 85.56  ? 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 134.879 121.071 130.938 1.00 81.05  ? 272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.507 122.170 131.655 1.00 80.45  ? 272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.587 122.865 130.832 1.00 82.19  ? 272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.087 123.913 131.252 1.00 81.84  ? 272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.084 121.648 132.980 1.00 80.26  ? 272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 136.726 122.737 133.820 1.00 82.55  ? 272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 137.947 122.963 133.676 1.00 80.20  ? 272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 136.009 123.368 134.625 1.00 79.50  ? 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 136.952 122.323 129.671 1.00 76.28  ? 273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 137.959 122.950 128.822 1.00 74.78  ? 273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.419 123.108 127.403 1.00 73.21  ? 273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 137.869 123.978 126.650 1.00 73.79  ? 273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.269 122.138 128.834 1.00 75.56  ? 273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 139.054 120.756 128.231 1.00 75.96  ? 273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.385 122.885 128.112 1.00 72.68  ? 273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.433 122.292 127.042 1.00 71.10  ? 274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 135.978 122.229 125.658 1.00 72.14  ? 274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.185 123.475 125.278 1.00 71.25  ? 274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.348 123.954 126.047 1.00 72.11  ? 274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.130 120.975 125.443 1.00 73.63  ? 274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.191 121.048 124.249 1.00 70.68  ? 274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.929 119.670 123.656 1.00 73.18  ? 274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.784 119.375 122.509 1.00 75.51  ? 274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 134.767 120.035 121.357 1.00 74.45  ? 274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 133.918 121.025 121.135 1.00 71.99  ? 274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 135.618 119.683 120.397 1.00 72.22  ? 274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.458 123.997 124.083 1.00 61.07  ? 275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 134.678 125.074 123.485 1.00 62.16  ? 275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 133.993 124.527 122.240 1.00 63.91  ? 275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.566 123.726 121.492 1.00 67.35  ? 275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.545 126.306 123.142 1.00 57.23  ? 275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.958 127.033 124.412 1.00 57.07  ? 275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.767 125.896 122.340 1.00 62.68  ? 275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 132.754 124.957 122.023 1.00 59.43  ? 276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 131.929 124.411 120.951 1.00 60.39  ? 276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.716 125.369 119.792 1.00 56.70  ? 276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.941 124.991 118.640 1.00 59.56  ? 276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.563 123.983 121.507 1.00 64.65  ? 276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.621 123.355 122.889 1.00 65.03  ? 276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.782 121.846 122.804 1.00 61.40  ? 276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.380 121.177 124.108 1.00 62.71  ? 276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.563 122.083 125.275 1.00 61.82  ? 276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.286 126.600 120.059 1.00 50.10  ? 277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.992 127.555 118.999 1.00 49.81  ? 277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.205 128.364 118.565 1.00 48.43  ? 277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.073 129.223 117.688 1.00 52.46  ? 277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.882 128.516 119.441 1.00 52.58  ? 277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.342 129.301 120.548 1.00 47.84  ? 277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.642 127.741 119.853 1.00 50.86  ? 277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.373 128.117 119.149 1.00 43.76  ? 278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.588 128.858 118.823 1.00 39.42  ? 278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.478 127.990 117.945 1.00 35.22  ? 278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.109 127.046 118.424 1.00 41.41  ? 278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.319 129.290 120.089 1.00 36.69  ? 278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.172 130.546 119.924 1.00 30.11  ? 278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.313 131.715 119.510 1.00 32.01  ? 278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.919 130.860 121.201 1.00 37.91  ? 278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.528 128.315 116.657 1.00 25.83  ? 279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.520 127.713 115.781 1.00 27.42  ? 279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.910 128.189 116.178 1.00 27.93  ? 279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.084 129.286 116.714 1.00 43.23  ? 279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.233 128.073 114.326 1.00 29.47  ? 279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.056 127.436 113.866 1.00 37.19  ? 279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.910 127.352 115.923 1.00 24.15  ? 280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.274 127.661 116.324 1.00 28.57  ? 280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.183 127.620 115.106 1.00 33.64  ? 280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.004 126.808 114.194 1.00 41.22  ? 280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.789 126.709 117.427 1.00 28.04  ? 280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.931 125.281 116.904 1.00 29.95  ? 280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.879 126.756 118.644 1.00 35.95  ? 280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 141.994 124.483 117.621 1.00 27.69  ? 280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.145 128.530 115.085 1.00 21.97  ? 281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.173 128.528 114.063 1.00 6.75   ? 281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.536 128.681 114.701 1.00 14.92  ? 281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 144.685 129.301 115.755 1.00 31.34  ? 281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.538 128.100 114.049 1.00 24.37  ? 282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.911 128.118 114.539 1.00 19.64  ? 282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 147.782 128.825 113.514 1.00 19.95  ? 282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 147.788 128.456 112.334 1.00 33.68  ? 282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.434 126.699 114.821 1.00 23.70  ? 282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.939 126.716 114.992 1.00 29.68  ? 282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.777 126.146 116.066 1.00 30.33  ? 282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.513 129.838 113.966 1.00 18.04  ? 283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.413 130.607 113.119 1.00 18.99  ? 283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 150.808 130.020 113.266 1.00 25.11  ? 283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.382 130.028 114.361 1.00 35.65  ? 283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.391 132.097 113.490 1.00 19.35  ? 283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.149 132.907 112.464 1.00 21.34  ? 283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 147.959 132.582 113.612 1.00 23.94  ? 283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.354 129.509 112.169 1.00 28.11  ? 284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 152.624 128.792 112.172 1.00 32.32  ? 284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 153.646 129.635 111.415 1.00 35.53  ? 284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.588 129.715 110.179 1.00 42.17  ? 284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.487 127.398 111.547 1.00 31.55  ? 284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.365 126.614 112.231 1.00 26.11  ? 284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.803 126.644 111.639 1.00 33.27  ? 284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.315 125.158 111.839 1.00 30.54  ? 284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 154.590 130.277 112.097 1.00 36.76  ? 285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 155.697 130.924 111.389 1.00 39.57  ? 285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 156.623 129.889 110.770 1.00 42.05  ? 285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 156.587 128.702 111.100 1.00 44.81  ? 285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.410 131.724 112.487 1.00 39.74  ? 285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.442 131.777 113.632 1.00 38.43  ? 285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 154.648 130.519 113.546 1.00 35.90  ? 285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.462 130.361 109.843 1.00 52.04  ? 286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.420 129.468 109.200 1.00 48.90  ? 286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.391 128.868 110.205 1.00 53.63  ? 286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.956 127.797 109.958 1.00 56.54  ? 286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.194 130.213 108.110 1.00 48.92  ? 286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.609 130.001 106.730 1.00 57.36  ? 286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.439 129.577 106.637 1.00 58.52  ? 286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.319 130.261 105.737 1.00 58.10  ? 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 159.602 129.542 111.340 1.00 54.58  ? 287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.534 129.038 112.342 1.00 50.33  ? 287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.075 127.700 112.906 1.00 53.49  ? 287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.893 126.803 113.133 1.00 64.19  ? 287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 160.704 130.061 113.464 1.00 50.46  ? 287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 161.842 129.743 114.414 1.00 46.88  ? 287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.120 129.450 113.649 1.00 55.48  ? 287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.302 129.282 114.584 1.00 57.12  ? 287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 165.585 129.184 113.840 1.00 53.25  ? 287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 158.771 127.550 113.150 1.00 45.52  ? 288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.260 126.277 113.648 1.00 44.13  ? 288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.476 125.161 112.634 1.00 46.73  ? 288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.832 124.036 113.003 1.00 52.11  ? 288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.779 126.402 113.999 1.00 43.30  ? 288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.199 125.161 114.615 1.00 46.97  ? 288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.322 124.927 115.974 1.00 48.86  ? 288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.536 124.227 113.837 1.00 46.04  ? 288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.794 123.786 116.544 1.00 52.23  ? 288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.007 123.084 114.402 1.00 43.89  ? 288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.135 122.864 115.756 1.00 50.49  ? 288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.256 125.453 111.351 1.00 53.15  ? 289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.465 124.446 110.317 1.00 52.77  ? 289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.938 124.072 110.228 1.00 52.26  ? 289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.285 122.901 110.033 1.00 58.74  ? 289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.919 124.948 108.968 1.00 54.67  ? 289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.115 123.896 107.889 1.00 51.62  ? 289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.450 125.318 109.100 1.00 49.39  ? 289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.830 125.056 110.372 1.00 54.63  ? 290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.259 124.759 110.392 1.00 52.89  ? 290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.623 123.880 111.580 1.00 51.88  ? 290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.382 122.915 111.437 1.00 62.15  ? 290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.067 126.057 110.418 1.00 52.29  ? 290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 162.869 126.939 109.198 1.00 57.89  ? 290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 163.537 128.293 109.344 1.00 61.58  ? 290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 164.416 128.433 110.220 1.00 59.54  ? 290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 163.181 129.217 108.583 1.00 61.50  ? 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.089 124.195 112.762 1.00 46.70  ? 291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.384 123.396 113.948 1.00 51.40  ? 291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 161.878 121.969 113.790 1.00 56.20  ? 291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.557 121.013 114.184 1.00 57.94  ? 291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.770 124.044 115.188 1.00 46.77  ? 291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.335 125.400 115.606 1.00 49.36  ? 291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.390 126.089 116.572 1.00 49.28  ? 291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.716 125.239 116.220 1.00 51.05  ? 291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.681 121.804 113.223 1.00 54.54  ? 292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.159 120.468 112.970 1.00 46.98  ? 292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 160.992 119.724 111.936 1.00 48.76  ? 292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.174 118.507 112.048 1.00 55.11  ? 292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.702 120.552 112.517 1.00 49.81  ? 292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.500 120.434 110.925 1.00 57.21  ? 293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.262 119.786 109.861 1.00 58.11  ? 293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.553 119.171 110.387 1.00 64.27  ? 293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 163.905 118.046 110.013 1.00 66.23  ? 293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.555 120.794 108.751 1.00 58.59  ? 293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.439 120.267 107.637 1.00 60.70  ? 293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.850 121.391 106.704 1.00 63.81  ? 293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.692 122.136 106.222 1.00 67.15  ? 293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.598 123.459 106.221 1.00 65.34  ? 293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.582 124.221 106.670 1.00 64.51  ? 293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.490 124.030 105.761 1.00 58.87  ? 293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.271 119.883 111.252 1.00 65.65  ? 294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.526 119.388 111.802 1.00 64.92  ? 294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.332 118.495 113.020 1.00 67.57  ? 294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.323 117.989 113.559 1.00 69.82  ? 294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.449 120.557 112.166 1.00 64.13  ? 294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.274 121.789 111.299 1.00 67.64  ? 294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.042 121.700 109.995 1.00 70.28  ? 294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 167.859 120.767 109.846 1.00 67.43  ? 294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.827 122.563 109.118 1.00 70.16  ? 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.089 118.292 113.461 1.00 67.05  ? 295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 163.777 117.421 114.595 1.00 67.88  ? 295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.514 117.862 115.857 1.00 72.61  ? 295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 164.960 117.039 116.660 1.00 73.47  ? 295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.081 115.956 114.269 1.00 68.18  ? 295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.208 114.988 115.045 1.00 72.36  ? 295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.811 115.317 116.183 1.00 71.15  ? 295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 162.917 113.895 114.516 1.00 70.59  ? 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.651 119.172 116.030 1.00 70.20  ? 296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.255 119.743 117.223 1.00 67.87  ? 296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.168 120.259 118.156 1.00 65.19  ? 296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.097 120.683 117.716 1.00 64.46  ? 296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.218 120.878 116.866 1.00 69.98  ? 296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 165.825 121.662 115.626 1.00 69.12  ? 296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 166.715 122.881 115.433 1.00 67.28  ? 296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.188 122.534 115.588 1.00 68.52  ? 296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 168.611 121.439 114.671 1.00 67.49  ? 296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.453 120.209 119.456 1.00 66.01  ? 297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 163.480 120.629 120.455 1.00 64.34  ? 297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.104 122.093 120.264 1.00 65.31  ? 297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 163.972 122.956 120.103 1.00 63.50  ? 297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.041 120.405 121.859 1.00 64.59  ? 297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.805 122.367 120.282 1.00 56.29  ? 298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.283 123.719 120.160 1.00 56.82  ? 298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.854 124.245 121.522 1.00 60.58  ? 298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 160.781 123.508 122.508 1.00 64.04  ? 298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.104 123.764 119.185 1.00 54.96  ? 298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.567 125.543 121.565 1.00 51.24  ? 299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.164 126.219 122.789 1.00 47.17  ? 299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.916 127.044 122.524 1.00 44.21  ? 299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.865 127.801 121.550 1.00 53.55  ? 299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.286 127.118 123.316 1.00 47.06  ? 299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.428 126.367 123.957 1.00 47.12  ? 299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 163.671 126.305 123.347 1.00 50.86  ? 299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 162.266 125.731 125.179 1.00 51.33  ? 299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 164.720 125.623 123.931 1.00 50.70  ? 299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 163.308 125.046 125.771 1.00 55.72  ? 299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.533 124.995 125.142 1.00 54.71  ? 299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.575 124.315 125.727 1.00 53.74  ? 299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.916 126.899 123.389 1.00 42.26  ? 300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.750 127.772 123.397 1.00 46.12  ? 300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.935 128.784 124.516 1.00 47.85  ? 300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 157.240 128.415 125.657 1.00 52.53  ? 300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.443 126.976 123.564 1.00 45.57  ? 300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.117 126.228 122.285 1.00 45.31  ? 300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.542 126.008 124.733 1.00 48.11  ? 300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 156.769 130.060 124.193 1.00 41.61  ? 301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.143 131.139 125.089 1.00 39.14  ? 301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 155.922 131.735 125.775 1.00 45.44  ? 301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 154.816 131.738 125.228 1.00 49.04  ? 301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 157.889 132.234 124.327 1.00 41.19  ? 301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.026 131.722 123.494 1.00 43.92  ? 301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.233 131.387 124.080 1.00 43.76  ? 301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 158.883 131.568 122.127 1.00 39.52  ? 301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.279 130.912 123.316 1.00 46.22  ? 301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 159.926 131.094 121.359 1.00 43.71  ? 301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.126 130.767 121.955 1.00 50.17  ? 301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.136 132.237 126.983 1.00 49.04  ? 302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.101 132.987 127.678 1.00 49.11  ? 302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.089 134.415 127.147 1.00 47.55  ? 302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.096 135.120 127.279 1.00 47.18  ? 302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 155.350 132.978 129.180 1.00 45.31  ? 302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 155.101 131.639 129.842 1.00 41.41  ? 302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.023 130.608 129.739 1.00 43.88  ? 302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.946 131.408 130.574 1.00 44.96  ? 302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.803 129.387 130.346 1.00 48.18  ? 302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.716 130.191 131.184 1.00 49.00  ? 302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.647 129.183 131.066 1.00 50.58  ? 302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 154.422 127.969 131.670 1.00 47.96  ? 302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 153.994 134.870 126.531 1.00 41.55  ? 303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.027 136.178 125.852 1.00 42.41  ? 303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.330 137.352 126.768 1.00 45.17  ? 303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.001 138.301 126.343 1.00 51.05  ? 303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 152.620 136.287 125.247 1.00 40.62  ? 303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.132 134.888 125.162 1.00 41.42  ? 303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 152.712 134.177 126.339 1.00 34.19  ? 303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 153.857 137.321 128.014 1.00 45.96  ? 304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.027 138.482 128.878 1.00 43.51  ? 304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 155.465 138.646 129.344 1.00 45.91  ? 304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 155.913 139.776 129.550 1.00 52.70  ? 304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.093 138.397 130.085 1.00 47.92  ? 304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.064 139.645 130.909 1.00 51.99  ? 304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.585 139.709 132.183 1.00 50.50  ? 304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 152.593 140.883 130.632 1.00 48.43  ? 304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.424 140.930 132.661 1.00 50.74  ? 304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 152.826 141.663 131.740 1.00 50.72  ? 304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 156.202 137.548 129.513 1.00 45.58  ? 305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 157.622 137.667 129.829 1.00 39.88  ? 305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 158.374 138.350 128.695 1.00 46.02  ? 305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.224 139.217 128.934 1.00 55.74  ? 305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 158.215 136.289 130.115 1.00 43.55  ? 305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.326 135.552 128.892 1.00 51.15  ? 305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 157.330 135.524 131.082 1.00 48.27  ? 305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.056 137.987 127.451 1.00 46.36  ? 306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 158.673 138.638 126.299 1.00 45.29  ? 306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.277 140.106 126.239 1.00 46.53  ? 306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.103 140.973 125.935 1.00 53.51  ? 306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.298 137.895 125.004 1.00 45.68  ? 306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 158.925 136.504 124.994 1.00 42.35  ? 306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 158.731 138.688 123.781 1.00 50.26  ? 306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.526 135.676 123.811 1.00 43.21  ? 306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.006 140.410 126.516 1.00 43.34  ? 307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 156.568 141.802 126.504 1.00 46.45  ? 307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.293 142.618 127.568 1.00 50.48  ? 307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 157.681 143.766 127.324 1.00 53.16  ? 307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.056 141.882 126.705 1.00 42.25  ? 307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 154.495 143.274 126.530 1.00 45.38  ? 307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.192 143.766 125.269 1.00 45.03  ? 307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.273 144.097 127.625 1.00 48.72  ? 307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 153.683 145.038 125.103 1.00 44.87  ? 307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 153.763 145.370 127.468 1.00 51.57  ? 307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 153.470 145.835 126.204 1.00 52.53  ? 307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 152.961 147.103 126.043 1.00 53.93  ? 307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 157.475 142.045 128.757 1.00 47.92  ? 308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.198 142.740 129.816 1.00 47.44  ? 308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 159.660 142.949 129.442 1.00 50.73  ? 308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.228 144.016 129.697 1.00 53.96  ? 308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.089 141.955 131.123 1.00 50.07  ? 308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 156.726 142.031 131.786 1.00 48.88  ? 308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 156.799 141.587 133.237 1.00 51.83  ? 308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 157.416 140.202 133.359 1.00 51.61  ? 308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 156.392 139.151 133.603 1.00 51.52  ? 308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.286 141.938 128.836 1.00 47.74  ? 309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 161.715 142.022 128.550 1.00 50.32  ? 309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.007 142.964 127.388 1.00 54.83  ? 309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 162.951 143.760 127.450 1.00 54.67  ? 309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.269 140.629 128.261 1.00 49.58  ? 309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 163.680 140.634 127.704 1.00 58.34  ? 309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 164.724 140.949 128.754 1.00 59.50  ? 309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 164.394 140.900 129.957 1.00 60.92  ? 309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 165.877 141.246 128.377 1.00 53.24  ? 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.212 142.893 126.320 1.00 53.16  ? 310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 161.500 143.614 125.089 1.00 49.98  ? 310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 160.571 144.789 124.830 1.00 48.54  ? 310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 160.834 145.569 123.908 1.00 46.99  ? 310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.434 142.655 123.892 1.00 48.82  ? 310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.499 141.582 123.904 1.00 50.57  ? 310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 163.777 141.841 123.428 1.00 50.92  ? 310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.227 140.312 124.392 1.00 49.45  ? 310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 164.753 140.863 123.438 1.00 52.11  ? 310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.197 139.329 124.407 1.00 49.01  ? 310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.457 139.610 123.928 1.00 52.88  ? 310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.427 138.635 123.940 1.00 53.92  ? 310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 159.501 144.943 125.606 1.00 46.04  ? 311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 158.572 146.029 125.371 1.00 46.32  ? 311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 157.664 145.843 124.179 1.00 46.96  ? 311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 156.963 146.786 123.801 1.00 51.54  ? 311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 157.654 144.657 123.574 1.00 51.41  ? 312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 156.837 144.387 122.403 1.00 53.06  ? 312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.182 143.023 122.549 1.00 52.11  ? 312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 156.711 142.131 123.217 1.00 55.14  ? 312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 157.666 144.439 121.114 1.00 49.61  ? 312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 156.936 145.044 119.928 1.00 55.63  ? 312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 157.808 145.129 118.694 1.00 61.63  ? 312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 157.309 145.125 117.568 1.00 60.79  ? 312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 159.117 145.205 118.896 1.00 53.23  ? 312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.023 142.871 121.915 1.00 44.86  ? 313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.294 141.614 121.980 1.00 44.51  ? 313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.022 140.525 121.201 1.00 49.52  ? 313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 155.810 140.798 120.294 1.00 53.93  ? 313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 152.877 141.790 121.436 1.00 41.57  ? 313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 151.998 142.634 122.304 1.00 47.42  ? 313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 151.479 142.183 123.497 1.00 49.63  ? 313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 151.546 143.902 122.152 1.00 45.05  ? 313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 150.745 143.136 124.044 1.00 46.76  ? 313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 150.770 144.189 123.248 1.00 46.04  ? 313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 154.745 139.272 121.572 1.00 49.35  ? 314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 155.413 138.139 120.940 1.00 48.33  ? 314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.099 138.062 119.450 1.00 52.70  ? 314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 155.981 137.751 118.640 1.00 56.37  ? 314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.012 136.841 121.641 1.00 53.32  ? 314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 155.929 135.665 121.359 1.00 46.89  ? 314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 155.055 134.089 121.332 1.00 56.39  ? 314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 153.612 134.512 120.361 1.00 50.12  ? 314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 153.855 138.339 119.067 1.00 44.69  ? 315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.433 138.228 117.677 1.00 44.89  ? 315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 153.756 139.463 116.840 1.00 50.95  ? 315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.566 139.427 115.620 1.00 58.40  ? 315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 151.933 137.923 117.605 1.00 44.85  ? 315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.103 138.876 118.435 1.00 48.85  ? 315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 151.681 139.575 119.291 1.00 48.42  ? 315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 149.872 138.928 118.229 1.00 48.23  ? 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.234 140.548 117.452 1.00 43.19  ? 316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.755 141.685 116.703 1.00 48.14  ? 316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.230 141.555 116.352 1.00 53.55  ? 316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.766 142.439 115.674 1.00 54.18  ? 316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.544 142.994 117.478 1.00 47.78  ? 316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.252 143.763 117.178 1.00 50.51  ? 316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 151.963 142.997 117.421 1.00 54.35  ? 316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 150.891 143.611 117.243 1.00 51.25  ? 316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 151.999 141.815 117.813 1.00 58.64  ? 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 156.897 140.494 116.789 1.00 52.50  ? 317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.316 140.307 116.527 1.00 53.88  ? 317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.527 139.120 115.600 1.00 54.46  ? 317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.868 138.084 115.738 1.00 49.58  ? 317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.084 140.100 117.832 1.00 54.88  ? 317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 158.651 141.034 118.947 1.00 52.46  ? 317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 159.583 140.820 120.470 1.00 53.64  ? 317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 160.696 142.218 120.371 1.00 54.32  ? 317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.448 139.278 114.650 1.00 58.61  ? 318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 159.773 138.213 113.710 1.00 58.95  ? 318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.381 137.030 114.448 1.00 57.28  ? 318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.512 137.112 114.938 1.00 57.68  ? 318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 160.732 138.718 112.631 1.00 58.63  ? 318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 160.363 138.225 111.245 1.00 63.51  ? 318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.217 136.997 111.069 1.00 62.91  ? 318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 160.224 139.064 110.332 1.00 62.11  ? 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 159.637 135.926 114.536 1.00 51.99  ? 319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.126 134.773 115.282 1.00 46.47  ? 319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.317 134.120 114.592 1.00 49.41  ? 319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.181 133.554 115.267 1.00 53.87  ? 319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.002 133.759 115.484 1.00 48.02  ? 319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.384 132.588 116.370 1.00 51.04  ? 319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 159.199 132.938 118.129 1.00 56.09  ? 319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 157.693 133.904 118.128 1.00 52.76  ? 319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.395 134.209 113.262 1.00 59.20  ? 320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.545 133.655 112.555 1.00 59.42  ? 320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 163.840 134.336 112.973 1.00 56.08  ? 320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 164.918 133.742 112.860 1.00 57.03  ? 320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.345 133.779 111.045 1.00 55.59  ? 320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.190 132.943 110.541 1.00 57.79  ? 320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.139 132.867 111.175 1.00 57.02  ? 320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 161.381 132.307 109.392 1.00 59.67  ? 320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 163.756 135.574 113.452 1.00 56.09  ? 321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 164.912 136.320 113.929 1.00 55.81  ? 321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.043 136.308 115.446 1.00 57.86  ? 321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.161 136.233 115.965 1.00 56.98  ? 321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 164.838 137.770 113.438 1.00 55.71  ? 321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 165.956 138.664 113.945 1.00 61.65  ? 321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 165.444 139.988 114.476 1.00 64.39  ? 321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.215 140.204 114.454 1.00 61.03  ? 321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 166.272 140.814 114.918 1.00 60.61  ? 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 163.928 136.367 116.168 1.00 56.90  ? 322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 163.947 136.541 117.614 1.00 53.17  ? 322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 163.740 135.248 118.391 1.00 54.44  ? 322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 163.718 135.289 119.623 1.00 61.15  ? 322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 162.887 137.565 118.031 1.00 52.09  ? 322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.290 139.003 117.755 1.00 59.52  ? 322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 163.610 139.950 119.253 1.00 69.90  ? 322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 163.786 141.597 118.573 1.00 60.30  ? 322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 163.593 134.106 117.716 1.00 47.97  ? 323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.417 132.849 118.437 1.00 44.70  ? 323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 164.657 132.515 119.257 1.00 48.75  ? 323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 164.558 132.136 120.430 1.00 53.08  ? 323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.096 131.721 117.456 1.00 51.91  ? 323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.035 130.348 118.092 1.00 49.90  ? 323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 161.866 129.884 118.676 1.00 46.38  ? 323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.146 129.515 118.101 1.00 50.11  ? 323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 161.806 128.633 119.258 1.00 44.79  ? 323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.095 128.264 118.678 1.00 48.82  ? 323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.923 127.828 119.255 1.00 50.01  ? 323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.871 126.582 119.831 1.00 50.76  ? 323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 165.838 132.659 118.653 1.00 55.34  ? 324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.076 132.403 119.381 1.00 54.77  ? 324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.251 133.391 120.527 1.00 55.87  ? 324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 167.684 133.014 121.623 1.00 58.95  ? 324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.266 132.467 118.427 1.00 56.09  ? 324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.175 131.443 117.314 1.00 61.68  ? 324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 167.813 130.283 117.602 1.00 60.57  ? 324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.461 131.797 116.151 1.00 61.87  ? 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 166.912 134.661 120.294 1.00 51.66  ? 325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.015 135.661 121.351 1.00 47.22  ? 325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.103 135.317 122.521 1.00 51.55  ? 325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 166.489 135.471 123.684 1.00 59.23  ? 325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 166.681 137.045 120.796 1.00 52.89  ? 325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 167.455 137.409 119.542 1.00 52.78  ? 325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 167.443 138.908 119.302 1.00 53.42  ? 325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.759 139.377 118.706 1.00 52.71  ? 325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 169.916 138.628 119.267 1.00 50.36  ? 325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 164.885 134.856 122.230 1.00 50.93  ? 326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 163.985 134.418 123.292 1.00 49.74  ? 326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 164.544 133.206 124.025 1.00 52.17  ? 326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.450 133.116 125.254 1.00 54.54  ? 326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 162.605 134.096 122.717 1.00 51.57  ? 326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 161.910 135.271 122.091 1.00 49.99  ? 326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.246 136.567 122.442 1.00 52.70  ? 326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 160.915 135.076 121.149 1.00 46.76  ? 326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 161.605 137.643 121.864 1.00 56.62  ? 326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.270 136.149 120.568 1.00 48.50  ? 326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 160.615 137.433 120.927 1.00 55.17  ? 326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.123 132.257 123.284 1.00 56.07  ? 327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 165.592 131.017 123.896 1.00 55.65  ? 327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 166.773 131.279 124.824 1.00 60.15  ? 327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 166.811 130.778 125.955 1.00 64.49  ? 327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 165.941 129.985 122.810 1.00 53.38  ? 327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 166.737 128.835 123.402 1.00 54.37  ? 327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 164.674 129.467 122.155 1.00 49.32  ? 327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 167.746 132.070 124.377 1.00 57.33  ? 328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 168.900 132.374 125.216 1.00 58.25  ? 328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 168.646 133.516 126.191 1.00 59.22  ? 328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.607 134.060 126.743 1.00 62.41  ? 328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.127 132.694 124.356 1.00 60.59  ? 328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.180 131.877 123.080 1.00 63.26  ? 328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.150 130.631 123.168 1.00 62.56  ? 328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 170.285 132.478 121.991 1.00 62.05  ? 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 167.389 133.892 126.415 1.00 55.78  ? 329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.065 134.952 127.359 1.00 57.27  ? 329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 166.556 134.333 128.654 1.00 57.88  ? 329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 165.466 133.747 128.659 1.00 55.17  ? 329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.014 135.880 126.773 1.00 53.42  ? 329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.011 137.250 127.422 1.00 54.11  ? 329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 165.446 138.196 126.879 1.00 53.64  ? 329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.642 137.364 128.581 1.00 62.61  ? 329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 167.300 134.428 129.760 1.00 62.99  ? 330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 166.814 133.833 131.014 1.00 62.85  ? 330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 165.570 134.507 131.565 1.00 64.78  ? 330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 164.827 133.878 132.327 1.00 68.29  ? 330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.011 133.991 131.961 1.00 63.54  ? 330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 168.739 135.179 131.437 1.00 61.98  ? 330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 168.586 135.125 129.940 1.00 61.73  ? 330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 165.316 135.763 131.204 1.00 54.42  ? 331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.133 136.467 131.681 1.00 55.21  ? 331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 162.894 136.169 130.848 1.00 55.88  ? 331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 161.820 136.701 131.151 1.00 55.06  ? 331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 164.395 137.975 131.715 1.00 56.05  ? 331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 165.515 138.375 132.662 1.00 56.81  ? 331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 165.793 139.875 132.615 1.00 56.29  ? 331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 166.421 140.347 131.381 1.00 59.81  ? 331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 167.497 139.826 130.801 1.00 58.33  ? 331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 168.178 138.833 131.352 1.00 59.40  ? 331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 167.918 140.335 129.647 1.00 52.80  ? 331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.014 135.345 129.812 1.00 53.36  ? 332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 161.881 134.909 129.003 1.00 50.31  ? 332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 161.525 133.489 129.423 1.00 54.69  ? 332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 162.375 132.592 129.391 1.00 57.71  ? 332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.203 134.982 127.503 1.00 48.36  ? 332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.182 134.194 126.703 1.00 49.40  ? 332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.246 136.428 127.041 1.00 50.09  ? 332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 160.272 133.283 129.822 1.00 54.16  ? 333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.831 131.979 130.298 1.00 47.71  ? 333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 159.322 131.126 129.143 1.00 47.73  ? 333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 158.632 131.616 128.245 1.00 54.63  ? 333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.740 132.136 131.356 1.00 49.14  ? 333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 158.536 130.903 132.221 1.00 51.63  ? 333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.349 131.070 133.155 1.00 52.16  ? 333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.088 129.799 133.948 1.00 52.79  ? 333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 155.944 129.956 134.889 1.00 57.06  ? 333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.671 129.841 129.173 1.00 51.59  ? 334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 159.284 128.909 128.124 1.00 53.85  ? 334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 159.377 127.488 128.659 1.00 55.58  ? 334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.947 127.242 129.725 1.00 57.43  ? 334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 160.171 129.064 126.884 1.00 51.31  ? 334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.620 128.677 127.125 1.00 53.31  ? 334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.567 129.442 126.222 1.00 57.26  ? 334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 163.042 130.722 126.882 1.00 53.92  ? 334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 164.318 130.525 127.621 1.00 47.38  ? 334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.798 126.550 127.908 1.00 59.69  ? 335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 158.972 125.127 128.168 1.00 63.64  ? 335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.322 124.425 126.865 1.00 59.43  ? 335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.772 124.758 125.811 1.00 58.42  ? 335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.722 124.480 128.772 1.00 61.84  ? 335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.402 125.085 128.341 1.00 63.11  ? 335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 155.245 124.560 129.168 1.00 64.63  ? 335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 154.153 124.344 128.601 1.00 57.49  ? 335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.428 124.356 130.386 1.00 63.13  ? 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.232 123.458 126.944 1.00 60.25  ? 336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.597 122.667 125.777 1.00 56.66  ? 336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.400 121.876 125.263 1.00 56.95  ? 336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.646 121.282 126.038 1.00 58.89  ? 336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.747 121.723 126.128 1.00 58.75  ? 336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.167 120.786 125.008 1.00 61.35  ? 336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 161.728 119.360 125.309 1.00 61.47  ? 336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 162.204 118.386 124.246 1.00 62.02  ? 336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 161.272 117.235 124.099 1.00 60.25  ? 336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.225 121.877 123.941 1.00 55.28  ? 337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.219 121.063 123.273 1.00 60.60  ? 337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 158.876 120.356 122.095 1.00 62.84  ? 337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.019 120.633 121.729 1.00 62.09  ? 337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.005 121.885 122.790 1.00 54.90  ? 337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.438 122.914 121.745 1.00 56.07  ? 337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.303 122.550 123.963 1.00 57.36  ? 337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.397 123.176 120.682 1.00 56.36  ? 337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.130 119.430 121.500 1.00 60.63  ? 338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.577 118.729 120.303 1.00 59.39  ? 338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 157.810 119.263 119.102 1.00 58.29  ? 338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.599 119.019 118.992 1.00 61.39  ? 338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.366 117.222 120.447 1.00 58.87  ? 338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.214 116.419 119.482 1.00 59.93  ? 338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.217 116.673 118.278 1.00 62.43  ? 338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 159.937 115.437 120.006 1.00 60.53  ? 338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.453 119.999 118.192 1.00 51.83  ? 339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.714 120.553 117.046 1.00 53.63  ? 339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.089 119.497 116.154 1.00 54.73  ? 339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 155.998 119.720 115.617 1.00 55.99  ? 339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.782 121.366 116.302 1.00 50.50  ? 339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.074 120.754 116.709 1.00 54.07  ? 339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 159.892 120.300 118.124 1.00 50.72  ? 339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 157.744 118.347 115.978 1.00 54.45  ? 340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.153 117.284 115.170 1.00 50.36  ? 340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 155.962 116.654 115.879 1.00 53.60  ? 340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 154.965 116.302 115.239 1.00 56.66  ? 340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.205 116.230 114.834 1.00 51.42  ? 340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.070 116.601 113.646 1.00 50.52  ? 340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 159.985 115.464 113.236 1.00 50.38  ? 340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 160.749 115.803 112.043 1.00 53.48  ? 340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.772 115.099 111.581 1.00 56.22  ? 340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 162.179 113.994 112.184 1.00 56.95  ? 340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.404 115.514 110.487 1.00 54.64  ? 340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.043 116.507 117.203 1.00 56.20  ? 341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 154.893 116.026 117.958 1.00 57.12  ? 341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 153.737 117.012 117.875 1.00 56.57  ? 341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.573 116.609 117.784 1.00 56.65  ? 341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.281 115.774 119.414 1.00 58.56  ? 341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.073 114.342 119.871 1.00 59.30  ? 341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.069 113.402 119.215 1.00 64.63  ? 341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.336 112.185 120.085 1.00 61.80  ? 341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.645 111.551 119.767 1.00 57.83  ? 341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.036 118.313 117.896 1.00 51.88  ? 342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 152.982 119.312 117.750 1.00 49.92  ? 342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.378 119.279 116.350 1.00 50.87  ? 342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.167 119.465 116.188 1.00 54.91  ? 342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.528 120.703 118.073 1.00 47.62  ? 342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.490 121.805 118.292 1.00 49.82  ? 342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.350 121.306 119.161 1.00 47.97  ? 342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.138 123.028 118.914 1.00 53.49  ? 342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.201 119.040 115.328 1.00 47.74  ? 343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.676 118.900 113.972 1.00 44.81  ? 343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.775 117.676 113.854 1.00 50.71  ? 343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.720 117.730 113.211 1.00 55.42  ? 343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 153.826 118.815 112.970 1.00 49.70  ? 343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.240 120.119 112.287 1.00 51.32  ? 343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.281 119.846 111.216 1.00 49.07  ? 343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.030 120.823 111.698 1.00 48.88  ? 343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.180 116.560 114.462 1.00 53.17  ? 344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.339 115.367 114.457 1.00 50.18  ? 344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.044 115.605 115.224 1.00 52.05  ? 344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 148.982 115.105 114.836 1.00 57.13  ? 344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.107 114.185 115.047 1.00 54.48  ? 344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 152.878 113.375 114.016 1.00 54.94  ? 344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.271 113.009 114.486 1.00 60.13  ? 344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.431 112.683 115.681 1.00 60.52  ? 344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.207 113.050 113.661 1.00 57.23  ? 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.117 116.361 116.323 1.00 46.26  ? 345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 148.910 116.718 117.059 1.00 49.20  ? 345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 147.979 117.566 116.205 1.00 50.82  ? 345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 146.761 117.362 116.212 1.00 56.04  ? 345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.280 117.454 118.347 1.00 45.54  ? 345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.092 117.827 119.215 1.00 44.89  ? 345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.495 118.789 120.318 1.00 49.33  ? 345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.457 118.823 121.426 1.00 52.67  ? 345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 146.072 118.824 120.883 1.00 55.89  ? 345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.539 118.517 115.455 1.00 44.59  ? 346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.736 119.307 114.528 1.00 41.14  ? 346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.072 118.415 113.490 1.00 46.89  ? 346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 145.880 118.560 113.196 1.00 50.01  ? 346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.610 120.357 113.840 1.00 41.85  ? 346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.193 121.504 114.663 1.00 45.02  ? 346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.220 122.253 113.838 1.00 46.42  ? 346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.097 122.439 115.114 1.00 45.34  ? 346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.837 117.479 112.924 1.00 45.14  ? 347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.296 116.608 111.886 1.00 40.46  ? 347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.169 115.737 112.423 1.00 50.44  ? 347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.129 115.586 111.772 1.00 54.82  ? 347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.408 115.742 111.295 1.00 41.93  ? 347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.346 115.167 113.617 1.00 51.19  ? 348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.296 114.314 114.165 1.00 50.05  ? 348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.089 115.130 114.612 1.00 53.93  ? 348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 142.954 114.657 114.498 1.00 54.64  ? 348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 145.838 113.453 115.310 1.00 50.95  ? 348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.424 113.879 116.710 1.00 55.08  ? 348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 146.111 112.801 117.984 1.00 69.17  ? 348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.669 113.609 118.337 1.00 54.37  ? 348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.302 116.358 115.089 1.00 46.48  ? 349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.176 117.218 115.433 1.00 42.39  ? 349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.368 117.582 114.195 1.00 39.92  ? 349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.132 117.612 114.240 1.00 37.93  ? 349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.679 118.475 116.142 1.00 42.84  ? 349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.809 119.024 117.273 1.00 43.75  ? 349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 143.211 118.402 118.598 1.00 45.48  ? 349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 142.907 120.538 117.337 1.00 44.07  ? 349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.048 117.861 113.078 1.00 40.65  ? 350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.337 118.158 111.839 1.00 41.75  ? 350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.646 116.922 111.277 1.00 48.62  ? 350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.571 117.034 110.678 1.00 51.02  ? 350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.295 118.751 110.806 1.00 40.93  ? 350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 143.989 120.020 111.268 1.00 44.36  ? 350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.699 120.722 110.126 1.00 42.34  ? 350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 143.814 121.653 109.435 1.00 44.36  ? 350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.798 121.839 108.124 1.00 45.43  ? 350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 144.607 121.169 107.320 1.00 46.95  ? 350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 142.946 122.719 107.605 1.00 44.49  ? 350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.247 115.743 111.445 1.00 49.57  ? 351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.578 114.517 111.027 1.00 49.85  ? 351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.318 114.269 111.848 1.00 50.75  ? 351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.280 113.877 111.304 1.00 58.04  ? 351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.537 113.333 111.143 1.00 52.52  ? 351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.668 113.509 110.308 1.00 54.17  ? 351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.391 114.495 113.161 1.00 52.67  ? 352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.263 114.200 114.037 1.00 51.84  ? 352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.142 115.224 113.902 1.00 52.54  ? 352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 136.963 114.852 113.884 1.00 56.31  ? 352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.739 114.123 115.488 1.00 56.46  ? 352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.558 112.885 115.809 1.00 58.96  ? 352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 141.258 112.981 117.150 1.00 60.31  ? 352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.152 114.041 117.803 1.00 56.59  ? 352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 141.912 111.996 117.552 1.00 61.96  ? 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.477 116.513 113.810 1.00 53.72  ? 353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.465 117.560 113.843 1.00 52.97  ? 353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.592 118.611 112.747 1.00 47.41  ? 353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.705 119.465 112.644 1.00 47.75  ? 353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.482 118.275 115.203 1.00 51.45  ? 353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 138.701 118.968 115.400 1.00 49.41  ? 353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.645 118.584 111.936 1.00 42.98  ? 354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.842 119.598 110.923 1.00 38.89  ? 354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.516 120.862 111.405 1.00 41.57  ? 354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.777 121.754 110.589 1.00 43.87  ? 354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 139.809 120.965 112.696 1.00 43.21  ? 355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.467 122.100 113.315 1.00 38.39  ? 355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 141.890 121.725 113.717 1.00 39.09  ? 355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.175 120.554 113.974 1.00 45.41  ? 355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.693 122.567 114.554 1.00 40.64  ? 355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.348 123.175 114.236 1.00 39.49  ? 355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.242 124.262 113.383 1.00 34.95  ? 355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.185 122.659 114.788 1.00 48.30  ? 355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.015 124.819 113.089 1.00 40.49  ? 355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 135.954 123.211 114.501 1.00 48.97  ? 355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 135.875 124.291 113.651 1.00 44.91  ? 355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.650 124.845 113.360 1.00 44.69  ? 355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.809 122.693 113.799 1.00 33.57  ? 356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.653 124.136 113.586 1.00 34.79  ? 356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.873 124.581 112.148 1.00 34.98  ? 356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.366 123.823 111.319 1.00 39.53  ? 356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.737 124.716 114.496 1.00 37.74  ? 356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.846 123.719 114.355 1.00 33.05  ? 356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.166 122.372 114.275 1.00 26.62  ? 356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.507 125.818 111.832 1.00 31.93  ? 357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.976 126.436 110.601 1.00 23.70  ? 357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.474 126.689 110.708 1.00 32.91  ? 357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.961 127.196 111.723 1.00 41.83  ? 357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.241 127.750 110.336 1.00 27.15  ? 357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.746 127.717 110.582 1.00 23.61  ? 357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.000 126.582 110.306 1.00 21.07  ? 357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.082 128.826 111.085 1.00 30.12  ? 357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.641 126.547 110.522 1.00 27.98  ? 357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.722 128.801 111.310 1.00 33.41  ? 357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.006 127.658 111.025 1.00 35.49  ? 357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.648 127.624 111.241 1.00 37.31  ? 357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.208 126.336 109.661 1.00 32.30  ? 358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.659 126.464 109.648 1.00 29.30  ? 358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.023 127.703 108.844 1.00 36.03  ? 358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.733 127.782 107.645 1.00 42.98  ? 358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.330 125.211 109.068 1.00 31.51  ? 358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.875 123.963 109.827 1.00 36.58  ? 358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.838 125.345 109.123 1.00 33.51  ? 358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.264 123.960 111.286 1.00 34.02  ? 358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.658 128.671 109.502 1.00 22.88  ? 359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.091 129.912 108.868 1.00 12.88  ? 359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.612 129.947 108.872 1.00 20.19  ? 359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.233 130.025 109.936 1.00 36.10  ? 359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.515 131.129 109.587 1.00 17.18  ? 359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 147.332 132.340 108.691 1.00 22.89  ? 359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.383 133.908 109.573 1.00 37.14  ? 359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.072 134.407 109.270 1.00 21.96  ? 359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.210 129.890 107.686 1.00 26.81  ? 360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.661 129.975 107.544 1.00 20.30  ? 360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.037 131.449 107.508 1.00 32.47  ? 360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 151.948 132.100 106.465 1.00 45.01  ? 360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.120 129.242 106.291 1.00 23.80  ? 360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.738 127.791 106.271 1.00 36.51  ? 360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.209 126.924 107.242 1.00 39.62  ? 360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.898 127.296 105.289 1.00 30.92  ? 360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.855 125.590 107.228 1.00 30.23  ? 360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.542 125.965 105.271 1.00 28.68  ? 360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.020 125.110 106.241 1.00 31.58  ? 360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.469 131.976 108.657 1.00 29.57  ? 361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.643 133.419 108.803 1.00 31.93  ? 361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.676 133.966 107.829 1.00 37.87  ? 361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.470 135.026 107.226 1.00 42.76  ? 361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.035 133.757 110.241 1.00 34.21  ? 361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 152.420 135.043 110.758 1.00 26.87  ? 361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.106 135.561 112.003 1.00 38.98  ? 361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.571 134.786 112.838 1.00 41.59  ? 361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 153.163 136.880 112.141 1.00 41.95  ? 361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 154.798 133.264 107.661 1.00 37.21  ? 362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 155.835 133.764 106.768 1.00 34.19  ? 362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.417 133.665 105.308 1.00 35.39  ? 362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 155.842 134.486 104.490 1.00 45.61  ? 362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.142 133.011 107.005 1.00 38.85  ? 362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.777 133.358 108.337 1.00 49.29  ? 362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.191 133.016 109.385 1.00 43.51  ? 362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 158.862 133.975 108.337 1.00 51.86  ? 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.591 132.675 104.960 1.00 39.73  ? 363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.033 132.626 103.612 1.00 29.56  ? 363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.127 133.822 103.356 1.00 25.40  ? 363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.102 134.368 102.247 1.00 37.36  ? 363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.265 131.320 103.406 1.00 23.09  ? 363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.176 130.150 103.113 1.00 24.33  ? 363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.373 130.320 102.887 1.00 30.46  ? 363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.612 128.950 103.110 1.00 29.72  ? 363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.368 134.235 104.371 1.00 18.85  ? 364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.513 135.410 104.237 1.00 28.75  ? 364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.354 136.675 104.132 1.00 34.22  ? 364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.117 137.530 103.271 1.00 28.52  ? 364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.532 135.494 105.418 1.00 16.93  ? 364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.577 136.641 105.212 1.00 21.27  ? 364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.781 134.188 105.578 1.00 24.12  ? 364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.346 136.815 105.009 1.00 32.74  ? 365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.114 138.046 105.120 1.00 20.64  ? 365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.259 138.139 104.120 1.00 28.27  ? 365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.856 139.212 103.987 1.00 35.21  ? 365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.663 138.190 106.541 1.00 21.90  ? 365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.566 138.247 107.582 1.00 24.83  ? 365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.737 139.156 107.578 1.00 25.36  ? 365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.552 137.270 108.480 1.00 28.38  ? 365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.583 137.049 103.422 1.00 32.58  ? 366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.610 137.117 102.387 1.00 32.02  ? 366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.160 137.994 101.226 1.00 37.67  ? 366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 156.977 138.687 100.610 1.00 36.27  ? 366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 156.956 135.712 101.899 1.00 33.41  ? 366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 158.120 135.650 100.923 1.00 39.73  ? 366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 158.122 134.351 100.123 1.00 44.54  ? 366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 157.534 133.185 100.910 1.00 39.40  ? 366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 158.365 132.819 102.091 1.00 34.85  ? 366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 154.866 137.976 100.917 1.00 37.37  ? 367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.302 138.753 99.824  1.00 30.32  ? 367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.232 139.723 100.323 1.00 30.34  ? 367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.410 140.192 99.545  1.00 36.14  ? 367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.748 137.831 98.722  1.00 29.36  ? 367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.887 137.198 97.941  1.00 30.39  ? 367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.862 136.761 99.331  1.00 24.15  ? 367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.236 140.027 101.618 1.00 26.05  ? 368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.285 140.978 102.180 1.00 15.37  ? 368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.733 142.394 101.842 1.00 21.56  ? 368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 153.864 142.785 102.147 1.00 31.52  ? 368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.169 140.793 103.691 1.00 21.23  ? 368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.195 141.725 104.338 1.00 17.75  ? 368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.380 142.230 105.606 1.00 21.83  ? 368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.027 142.246 103.894 1.00 20.53  ? 368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.368 143.022 105.915 1.00 22.13  ? 368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.534 143.048 104.893 1.00 23.77  ? 368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.844 143.158 101.210 1.00 22.93  ? 369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.188 144.496 100.748 1.00 24.95  ? 369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.255 145.519 101.872 1.00 32.14  ? 369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.981 146.511 101.742 1.00 39.74  ? 369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.179 144.959 99.698  1.00 28.63  ? 369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.533 145.305 102.966 1.00 30.55  ? 370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.387 146.294 104.027 1.00 26.04  ? 370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.076 145.852 105.314 1.00 27.79  ? 370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.541 146.019 106.411 1.00 38.51  ? 370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 149.913 146.590 104.282 1.00 24.77  ? 370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.194 147.075 103.039 1.00 27.53  ? 370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.613 148.040 102.405 1.00 42.47  ? 370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.109 146.401 102.680 1.00 26.03  ? 370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.274 145.275 105.191 1.00 24.97  ? 371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.044 144.897 106.369 1.00 25.12  ? 371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.455 146.103 107.203 1.00 27.68  ? 371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 154.680 145.959 108.409 1.00 23.32  ? 371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.289 144.108 105.958 1.00 20.88  ? 371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.008 142.634 105.774 1.00 27.47  ? 371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.061 142.095 106.342 1.00 29.37  ? 371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.837 141.970 104.978 1.00 26.24  ? 371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.568 147.282 106.587 1.00 38.99  ? 372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 154.894 148.485 107.345 1.00 35.06  ? 372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 153.786 148.831 108.333 1.00 35.57  ? 372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.063 149.232 109.468 1.00 35.89  ? 372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.147 149.651 106.390 1.00 30.59  ? 372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 153.927 150.094 105.647 1.00 34.48  ? 372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.268 149.284 104.749 1.00 35.33  ? 372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.240 151.260 105.677 1.00 36.95  ? 372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.228 149.931 104.256 1.00 35.70  ? 372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.191 151.133 104.801 1.00 40.14  ? 372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.526 148.693 107.913 1.00 32.39  ? 373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.408 148.915 108.827 1.00 34.02  ? 373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.438 147.887 109.947 1.00 36.92  ? 373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 151.399 148.228 111.135 1.00 43.02  ? 373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.074 148.868 108.061 1.00 25.32  ? 373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.008 149.993 107.030 1.00 29.91  ? 373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 148.902 148.948 109.024 1.00 29.32  ? 373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 148.824 149.896 106.100 1.00 32.87  ? 373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.530 146.610 109.576 1.00 22.05  ? 374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 151.625 145.500 110.513 1.00 21.72  ? 374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 151.822 144.205 109.739 1.00 32.62  ? 374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.407 144.102 108.581 1.00 33.80  ? 374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.373 145.404 111.386 1.00 34.79  ? 374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 150.120 144.064 111.767 1.00 30.91  ? 374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.454 143.218 110.357 1.00 36.02  ? 375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.484 141.890 109.771 1.00 20.46  ? 375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.163 141.183 110.041 1.00 25.57  ? 375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.479 141.458 111.030 1.00 32.14  ? 375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.653 141.078 110.329 1.00 21.71  ? 375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 154.893 141.115 109.452 1.00 29.02  ? 375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.161 141.144 110.283 1.00 36.07  ? 375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.398 141.151 109.399 1.00 32.70  ? 375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 157.422 139.991 108.467 1.00 32.79  ? 375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.799 140.272 109.144 1.00 29.54  ? 376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.546 139.535 109.274 1.00 24.73  ? 376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.732 138.488 110.366 1.00 24.26  ? 376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.451 137.505 110.183 1.00 33.28  ? 376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.130 138.890 107.950 1.00 22.14  ? 376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.787 138.199 108.102 1.00 29.21  ? 376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.074 139.931 106.849 1.00 13.12  ? 376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.080 138.701 111.507 1.00 23.44  ? 377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.237 137.819 112.653 1.00 18.92  ? 377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.176 136.733 112.726 1.00 24.47  ? 377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.397 135.719 113.396 1.00 32.91  ? 377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.209 138.631 113.951 1.00 31.77  ? 377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.260 139.722 114.022 1.00 33.89  ? 377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.693 140.980 114.646 1.00 24.82  ? 377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.551 142.186 114.325 1.00 32.39  ? 377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.866 143.459 114.672 1.00 37.61  ? 377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.039 136.917 112.064 1.00 26.90  ? 378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 145.945 135.961 112.155 1.00 9.20   ? 378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.007 136.159 110.976 1.00 14.36  ? 378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.057 137.177 110.280 1.00 21.46  ? 378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.190 136.095 113.484 1.00 12.66  ? 378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.367 137.348 113.603 1.00 16.08  ? 378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 144.938 138.597 113.424 1.00 20.12  ? 378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.024 137.275 113.919 1.00 14.45  ? 378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.184 139.741 113.542 1.00 16.21  ? 378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.267 138.419 114.040 1.00 21.65  ? 378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 142.849 139.653 113.852 1.00 17.40  ? 378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.152 135.168 110.760 1.00 17.25  ? 379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.188 135.160 109.670 1.00 1.83   ? 379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 141.771 135.207 110.234 1.00 11.86  ? 379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.560 135.324 111.443 1.00 28.06  ? 379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.383 133.933 108.777 1.00 12.93  ? 379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 142.804 134.140 107.502 1.00 30.00  ? 379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.793 135.113 109.338 1.00 16.09  ? 380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.393 135.250 109.704 1.00 21.01  ? 380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.787 133.883 110.021 1.00 33.28  ? 380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.487 132.872 110.130 1.00 38.03  ? 380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.624 135.961 108.594 1.00 18.61  ? 380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.626 135.186 107.297 1.00 21.63  ? 380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.651 134.647 106.887 1.00 34.31  ? 380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.474 135.125 106.643 1.00 24.53  ? 380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.462 133.849 110.178 1.00 34.03  ? 381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.766 132.602 110.473 1.00 32.24  ? 381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.818 131.635 109.297 1.00 27.90  ? 381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.823 130.415 109.500 1.00 36.08  ? 381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.319 132.901 110.861 1.00 27.81  ? 381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.359 131.735 111.095 1.00 33.57  ? 381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.767 130.921 112.309 1.00 32.27  ? 381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 132.940 132.253 111.243 1.00 34.66  ? 381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.862 132.150 108.072 1.00 29.71  ? 382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 136.962 131.322 106.880 1.00 18.44  ? 382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.406 131.086 106.460 1.00 22.94  ? 382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.645 130.432 105.440 1.00 31.15  ? 382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.177 131.957 105.731 1.00 31.16  ? 382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.395 132.055 106.009 1.00 38.20  ? 382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.366 131.603 107.228 1.00 25.78  ? 383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.792 131.371 106.994 1.00 17.84  ? 383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.212 131.798 105.589 1.00 25.71  ? 383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 141.952 131.092 104.903 1.00 36.10  ? 383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.159 129.909 107.251 1.00 31.38  ? 383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.561 129.752 107.384 1.00 40.59  ? 383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.727 132.957 105.149 1.00 24.06  ? 384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.092 133.489 103.840 1.00 19.14  ? 384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.410 134.977 103.829 1.00 24.26  ? 384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 141.927 135.462 102.817 1.00 42.46  ? 384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 139.985 133.193 102.811 1.00 23.03  ? 384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 138.548 133.383 103.294 1.00 30.31  ? 384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.135 134.832 103.436 1.00 32.79  ? 384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.813 135.706 102.864 1.00 31.29  ? 384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.128 135.098 104.125 1.00 31.87  ? 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.122 135.714 104.896 1.00 21.27  ? 385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.466 137.129 104.978 1.00 13.80  ? 385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.792 137.269 105.710 1.00 22.49  ? 385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 142.962 136.748 106.817 1.00 36.86  ? 385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.361 137.934 105.674 1.00 11.38  ? 385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.931 139.207 106.257 1.00 10.58  ? 385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.291 138.279 104.677 1.00 23.36  ? 385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.737 137.969 105.085 1.00 23.20  ? 386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.088 138.149 105.612 1.00 11.99  ? 386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.458 139.620 105.455 1.00 18.10  ? 386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.964 140.037 104.410 1.00 10.34  ? 386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.063 137.237 104.894 1.00 7.75   ? 386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.748 135.755 105.066 1.00 7.13   ? 386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.603 134.937 104.146 1.00 11.86  ? 386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.958 135.332 106.507 1.00 23.27  ? 386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.205 140.401 106.501 1.00 26.62  ? 387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.394 141.841 106.463 1.00 14.02  ? 387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.175 142.301 107.685 1.00 23.71  ? 387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.191 141.643 108.727 1.00 35.18  ? 387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.050 142.571 106.397 1.00 12.85  ? 387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.172 142.130 105.247 1.00 20.73  ? 387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.027 143.080 105.004 1.00 20.78  ? 387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 141.992 144.173 105.563 1.00 32.66  ? 387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.081 142.670 104.170 1.00 17.54  ? 387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 146.834 143.448 107.535 1.00 19.40  ? 388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.556 144.049 108.645 1.00 21.00  ? 388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.583 144.541 109.708 1.00 28.28  ? 388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.559 145.158 109.399 1.00 34.04  ? 388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.421 145.206 108.153 1.00 27.59  ? 388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 146.909 144.268 110.968 1.00 24.00  ? 389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.071 144.673 112.085 1.00 20.71  ? 389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 146.942 145.234 113.194 1.00 25.15  ? 389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.033 144.720 113.459 1.00 38.63  ? 389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.240 143.500 112.615 1.00 30.46  ? 389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.067 142.395 112.933 1.00 34.17  ? 389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.453 146.286 113.842 1.00 29.44  ? 390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.118 146.896 114.983 1.00 29.77  ? 390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.230 146.723 116.204 1.00 33.00  ? 390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.025 146.986 116.141 1.00 38.15  ? 390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.401 148.379 114.733 1.00 29.07  ? 390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.393 148.640 113.615 1.00 29.82  ? 390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 148.600 150.116 113.356 1.00 35.71  ? 390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 147.925 150.962 113.943 1.00 33.78  ? 390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 149.535 150.437 112.470 1.00 29.56  ? 390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 146.823 146.272 117.310 1.00 38.54  ? 391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.043 146.028 118.514 1.00 37.17  ? 391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.550 147.349 119.089 1.00 46.52  ? 391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.179 148.405 118.929 1.00 36.41  ? 391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 146.862 145.235 119.548 1.00 32.09  ? 391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 147.791 146.154 120.327 1.00 33.76  ? 391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 145.936 144.485 120.490 1.00 32.65  ? 391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.397 147.295 119.747 1.00 48.12  ? 392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 143.806 148.450 120.402 1.00 35.19  ? 392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.000 148.320 121.903 1.00 44.38  ? 392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 143.641 147.295 122.493 1.00 50.91  ? 392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.319 148.573 120.069 1.00 36.41  ? 392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.113 148.624 118.671 1.00 40.25  ? 392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.570 149.354 122.516 1.00 48.57  ? 393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 144.770 149.383 123.960 1.00 46.29  ? 393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.540 150.023 124.586 1.00 48.67  ? 393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.477 151.243 124.758 1.00 51.40  ? 393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.043 150.142 124.315 1.00 54.05  ? 393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.223 150.210 125.719 1.00 55.50  ? 393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.553 149.198 124.925 1.00 45.12  ? 394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.336 149.680 125.568 1.00 42.82  ? 394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 141.631 149.898 127.045 1.00 47.49  ? 394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 141.874 148.942 127.788 1.00 49.71  ? 394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.194 148.689 125.368 1.00 43.13  ? 394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 139.806 148.477 123.922 1.00 42.85  ? 394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.200 149.489 123.189 1.00 41.88  ? 394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.050 147.268 123.288 1.00 43.06  ? 394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.845 149.300 121.867 1.00 44.00  ? 394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 139.697 147.069 121.968 1.00 43.08  ? 394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.097 148.088 121.263 1.00 48.99  ? 394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.746 147.891 119.946 1.00 53.38  ? 394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.614 151.156 127.468 1.00 51.08  ? 395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 141.980 151.536 128.822 1.00 52.75  ? 395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 140.755 151.512 129.724 1.00 55.82  ? 395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 139.638 151.247 129.270 1.00 48.44  ? 395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 142.614 152.927 128.843 1.00 50.86  ? 395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 141.610 153.913 128.578 1.00 54.84  ? 395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 143.701 153.024 127.786 1.00 49.58  ? 395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 140.978 151.775 131.010 1.00 55.34  ? 396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 139.899 151.862 131.985 1.00 49.97  ? 396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 138.886 152.929 131.586 1.00 50.39  ? 396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.177 153.783 130.741 1.00 55.74  ? 396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.468 152.157 133.374 1.00 50.16  ? 396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.550 151.174 133.780 1.00 56.17  ? 396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 142.630 151.183 133.151 1.00 58.30  ? 396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 141.324 150.393 134.728 1.00 51.38  ? 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 137.689 152.873 132.171 1.00 48.18  ? 397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.661 153.880 131.935 1.00 46.83  ? 397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.197 155.276 132.226 1.00 48.74  ? 397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 138.238 155.433 132.867 1.00 52.92  ? 397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.429 153.567 132.795 1.00 48.35  ? 397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.156 154.278 132.378 1.00 49.77  ? 397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.861 155.554 132.842 1.00 49.14  ? 397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 133.264 153.680 131.499 1.00 46.43  ? 397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.708 156.204 132.460 1.00 46.85  ? 397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 132.108 154.326 131.108 1.00 46.39  ? 397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 131.835 155.587 131.593 1.00 50.26  ? 397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 130.684 156.230 131.204 1.00 51.26  ? 397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 136.507 156.281 131.667 1.00 54.15  ? 398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 136.850 157.708 131.670 1.00 57.38  ? 398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 138.344 157.934 131.446 1.00 56.19  ? 398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 138.922 158.918 131.921 1.00 52.95  ? 398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 136.320 158.434 132.927 1.00 56.74  ? 398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 137.161 158.223 134.178 1.00 58.91  ? 398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 137.398 159.215 134.898 1.00 56.66  ? 398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 137.513 157.084 134.510 1.00 53.68  ? 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 138.962 157.031 130.687 1.00 59.08  ? 399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 140.312 157.195 130.172 1.00 55.57  ? 399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.278 156.945 128.672 1.00 56.51  ? 399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.592 156.030 128.208 1.00 55.05  ? 399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 141.297 156.231 130.847 1.00 54.99  ? 399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.198 156.873 131.888 1.00 58.24  ? 399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.265 155.918 132.384 1.00 61.15  ? 399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 143.346 154.796 131.845 1.00 61.27  ? 399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.023 156.288 133.306 1.00 60.16  ? 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.006 157.764 127.917 1.00 57.34  ? 400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 140.991 157.643 126.464 1.00 59.37  ? 400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.651 156.338 126.032 1.00 60.78  ? 400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 142.733 155.987 126.511 1.00 59.28  ? 400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.700 158.833 125.822 1.00 57.31  ? 400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.051 159.312 124.529 1.00 61.05  ? 400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 139.627 159.793 124.733 1.00 63.45  ? 400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 138.754 159.448 123.908 1.00 61.86  ? 400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.381 160.512 125.724 1.00 60.98  ? 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 140.993 155.620 125.128 1.00 54.45  ? 401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.504 154.355 124.624 1.00 50.67  ? 401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.363 154.576 123.386 1.00 54.99  ? 401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.115 155.477 122.582 1.00 55.91  ? 401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.361 153.397 124.287 1.00 50.86  ? 401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.292 153.360 125.357 1.00 59.36  ? 401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 139.646 153.305 126.553 1.00 62.18  ? 401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.096 153.379 125.001 1.00 55.32  ? 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.381 153.732 123.239 1.00 56.65  ? 402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.237 153.731 122.058 1.00 51.08  ? 402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.637 152.768 121.039 1.00 51.73  ? 402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 143.715 151.548 121.209 1.00 59.53  ? 402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.665 153.334 122.422 1.00 50.35  ? 402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.429 154.404 123.183 1.00 54.11  ? 402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 146.388 154.199 124.685 1.00 58.93  ? 402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 146.935 153.182 125.161 1.00 55.86  ? 402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 145.807 155.051 125.388 1.00 57.12  ? 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.044 153.314 119.986 1.00 37.92  ? 403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.312 152.523 119.004 1.00 39.80  ? 403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.267 152.074 117.906 1.00 45.52  ? 403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 143.978 152.893 117.312 1.00 47.64  ? 403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.138 153.325 118.420 1.00 37.70  ? 403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.107 153.624 119.510 1.00 42.64  ? 403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.497 152.574 117.271 1.00 40.57  ? 403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.717 152.414 120.327 1.00 39.91  ? 403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.282 150.775 117.639 1.00 36.90  ? 404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.101 150.176 116.608 1.00 29.50  ? 404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.327 149.908 115.336 1.00 38.36  ? 404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.383 150.628 114.989 1.00 48.44  ? 404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 143.730 148.856 114.626 1.00 36.03  ? 405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.123 148.476 113.354 1.00 19.61  ? 405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.590 147.054 113.469 1.00 31.88  ? 405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.330 146.138 113.841 1.00 39.06  ? 405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.133 148.588 112.213 1.00 28.40  ? 405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.722 149.973 111.944 1.00 31.09  ? 405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 145.809 149.890 110.887 1.00 23.72  ? 405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.641 150.948 111.522 1.00 31.01  ? 405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.312 146.870 113.147 1.00 37.31  ? 406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.685 145.558 113.114 1.00 30.46  ? 406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.075 145.310 111.741 1.00 34.52  ? 406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.428 146.192 111.168 1.00 41.36  ? 406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.616 145.425 114.201 1.00 34.59  ? 406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.211 145.220 115.580 1.00 38.76  ? 406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.432 144.979 115.672 1.00 37.99  ? 406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.455 145.291 116.572 1.00 43.01  ? 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.263 144.098 111.234 1.00 29.33  ? 407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 139.978 143.788 109.837 1.00 25.04  ? 407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 138.500 143.458 109.672 1.00 24.36  ? 407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 137.857 142.947 110.596 1.00 40.88  ? 407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 140.868 142.630 109.363 1.00 26.52  ? 407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.340 142.960 109.615 1.00 19.18  ? 407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 140.638 142.333 107.904 1.00 28.22  ? 407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.138 141.797 110.145 1.00 26.75  ? 407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 137.957 143.754 108.492 1.00 31.53  ? 408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 136.580 143.447 108.139 1.00 38.59  ? 408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 136.508 142.940 106.703 1.00 44.09  ? 408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.300 143.342 105.846 1.00 46.22  ? 408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 135.686 144.682 108.307 1.00 36.93  ? 408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.463 145.322 107.064 1.00 46.03  ? 408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 135.548 142.051 106.446 1.00 46.28  ? 409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 135.321 141.472 105.125 1.00 47.05  ? 409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 134.323 142.312 104.341 1.00 49.13  ? 409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 133.154 142.415 104.728 1.00 53.04  ? 409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 134.795 140.038 105.218 1.00 51.50  ? 409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 135.992 138.685 105.257 1.00 66.08  ? 409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.774 142.887 103.234 1.00 38.40  ? 410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.883 143.395 102.193 1.00 27.49  ? 410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.026 142.435 101.018 1.00 36.56  ? 410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.871 142.632 100.141 1.00 46.78  ? 410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 134.231 144.830 101.814 1.00 33.49  ? 410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 134.479 145.706 103.026 1.00 48.11  ? 410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 133.544 146.124 103.705 1.00 46.72  ? 410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 135.747 145.987 103.303 1.00 46.83  ? 410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.203 141.391 101.008 1.00 29.92  ? 411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.408 140.251 100.129 1.00 22.76  ? 411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.521 140.307 98.894  1.00 28.15  ? 411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.395 140.809 98.926  1.00 39.75  ? 411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.151 138.936 100.866 1.00 26.22  ? 411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 134.015 138.658 102.089 1.00 28.26  ? 411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.947 137.191 102.468 1.00 34.13  ? 411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.440 139.074 101.806 1.00 33.91  ? 411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.057 139.777 97.802  1.00 23.63  ? 412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.300 139.571 96.586  1.00 16.20  ? 412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.021 138.563 95.728  1.00 22.73  ? 412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.253 138.492 95.735  1.00 43.32  ? 412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.253 137.775 94.986  1.00 28.26  ? 413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.800 136.652 94.241  1.00 20.28  ? 413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.536 136.816 92.755  1.00 25.99  ? 413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.433 137.190 92.345  1.00 38.51  ? 413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.207 135.327 94.728  1.00 26.77  ? 413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.669 135.013 96.029  1.00 31.40  ? 413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.558 136.539 91.953  1.00 30.61  ? 414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.412 136.454 90.511  1.00 26.96  ? 414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.055 135.030 90.118  1.00 36.71  ? 414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.675 134.070 90.586  1.00 40.98  ? 414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.699 136.875 89.802  1.00 27.33  ? 414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.328 138.204 90.208  1.00 37.49  ? 414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.548 138.476 89.354  1.00 36.38  ? 414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.316 139.324 90.065  1.00 35.99  ? 414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.051 134.895 89.260  1.00 43.78  ? 415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.707 133.602 88.680  1.00 39.54  ? 415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.600 133.406 87.465  1.00 38.47  ? 415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.364 133.993 86.408  1.00 42.77  ? 415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.232 133.548 88.307  1.00 34.86  ? 415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.734 132.136 88.117  1.00 45.77  ? 415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 129.567 131.394 89.079  1.00 47.22  ? 415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 129.503 131.752 86.869  1.00 44.99  ? 415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.627 132.568 87.616  1.00 30.24  ? 416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.638 132.424 86.573  1.00 31.95  ? 416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.002 131.960 85.269  1.00 37.16  ? 416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.363 132.431 84.182  1.00 40.33  ? 416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.748 131.466 87.043  1.00 32.51  ? 416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.500 132.077 88.225  1.00 26.92  ? 416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.705 131.166 85.912  1.00 31.70  ? 416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.480 131.140 88.880  1.00 29.25  ? 416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.031 131.048 85.356  1.00 41.47  ? 417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.346 130.573 84.158  1.00 40.85  ? 417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.658 131.718 83.426  1.00 40.91  ? 417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.902 131.942 82.235  1.00 50.33  ? 417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.334 129.491 84.535  1.00 37.93  ? 417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.462 128.894 83.428  1.00 38.66  ? 417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 131.288 128.494 82.217  1.00 37.21  ? 417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.679 127.709 83.958  1.00 45.11  ? 417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.820 132.479 84.132  1.00 43.21  ? 418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.088 133.558 83.480  1.00 44.74  ? 418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.985 134.750 83.180  1.00 45.14  ? 418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.708 135.511 82.247  1.00 46.73  ? 418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.899 133.982 84.340  1.00 42.48  ? 418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.764 132.980 84.294  1.00 49.79  ? 418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.445 132.435 83.238  1.00 52.89  ? 418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.145 132.732 85.441  1.00 47.80  ? 418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.053 134.935 83.958  1.00 46.25  ? 419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.998 136.008 83.671  1.00 43.18  ? 419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.724 135.745 82.359  1.00 46.71  ? 419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.883 136.649 81.530  1.00 50.52  ? 419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.984 136.183 84.841  1.00 36.84  ? 419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.251 136.874 84.375  1.00 43.55  ? 419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.338 136.975 85.959  1.00 43.76  ? 419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.166 134.504 82.138  1.00 48.13  ? 420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.935 134.212 80.937  1.00 47.35  ? 420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.060 133.899 79.730  1.00 47.43  ? 420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 134.533 134.026 78.597  1.00 53.21  ? 420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.905 133.057 81.187  1.00 45.50  ? 420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 137.134 133.474 81.974  1.00 44.82  ? 420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 138.575 133.780 80.937  1.00 60.55  ? 420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.739 132.224 80.079  1.00 51.75  ? 420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.805 133.489 79.936  1.00 55.78  ? 421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.893 133.351 78.805  1.00 56.07  ? 421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.583 134.706 78.185  1.00 55.45  ? 421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 131.471 134.827 76.959  1.00 52.55  ? 421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.604 132.651 79.236  1.00 47.71  ? 421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.759 131.163 79.502  1.00 54.02  ? 421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.436 130.483 79.792  1.00 61.89  ? 421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.721 130.939 80.710  1.00 57.01  ? 421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 129.112 129.492 79.105  1.00 58.03  ? 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.442 135.739 79.016  1.00 50.73  ? 422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.168 137.083 78.527  1.00 51.14  ? 422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.424 137.831 78.105  1.00 54.53  ? 422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.308 138.944 77.579  1.00 52.42  ? 422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.429 137.890 79.597  1.00 46.73  ? 422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.045 137.395 79.880  1.00 54.30  ? 422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.783 136.413 80.811  1.00 56.69  ? 422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.848 137.747 79.357  1.00 53.20  ? 422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.483 136.181 80.847  1.00 53.24  ? 422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.893 136.977 79.974  1.00 52.53  ? 422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.607 137.251 78.320  1.00 61.16  ? 423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.879 137.882 77.965  1.00 57.03  ? 423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.999 139.269 78.589  1.00 60.88  ? 423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.417 140.234 77.946  1.00 62.14  ? 423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.054 137.953 76.446  1.00 54.05  ? 423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 134.789 136.645 75.721  1.00 58.77  ? 423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.985 135.714 75.804  1.00 63.42  ? 423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.576 134.266 75.592  1.00 63.27  ? 423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.242 133.351 76.559  1.00 60.10  ? 423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.627 139.370 79.862  1.00 48.30  ? 424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.559 140.643 80.571  1.00 48.06  ? 424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.256 140.546 81.919  1.00 46.97  ? 424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.700 140.906 82.958  1.00 48.86  ? 424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.114 141.092 80.752  1.00 52.60  ? 424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.489 140.375 81.802  1.00 52.10  ? 424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.489 140.036 81.927  1.00 48.43  ? 425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.264 140.004 83.164  1.00 40.63  ? 425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.491 141.420 83.678  1.00 44.54  ? 425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.279 141.713 84.860  1.00 48.54  ? 425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.597 139.265 82.949  1.00 44.92  ? 425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.363 137.764 82.788  1.00 47.31  ? 425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.544 139.525 84.110  1.00 43.91  ? 425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.619 136.990 82.475  1.00 44.56  ? 425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.904 142.325 82.789  1.00 44.98  ? 426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.204 143.694 83.198  1.00 39.79  ? 426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.968 144.395 83.744  1.00 40.68  ? 426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.994 144.956 84.847  1.00 49.42  ? 426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.779 144.473 82.016  1.00 44.09  ? 426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.774 145.979 82.202  1.00 48.51  ? 426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.386 146.710 81.025  1.00 53.29  ? 426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.641 146.061 79.988  1.00 46.60  ? 426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.612 147.933 81.135  1.00 57.06  ? 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.874 144.376 82.979  1.00 40.37  ? 427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.665 145.079 83.391  1.00 38.78  ? 427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.101 144.498 84.680  1.00 38.77  ? 427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.711 145.243 85.588  1.00 45.95  ? 427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.627 145.025 82.270  1.00 47.27  ? 427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 132.283 145.643 82.615  1.00 47.18  ? 427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 131.159 144.947 81.866  1.00 49.35  ? 427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 130.548 143.826 82.690  1.00 51.66  ? 427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 129.357 144.291 83.452  1.00 49.15  ? 427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.060 143.168 84.784  1.00 39.88  ? 428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.535 142.539 85.991  1.00 30.36  ? 428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.393 142.866 87.203  1.00 39.87  ? 428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.866 143.198 88.270  1.00 45.21  ? 428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.438 141.027 85.806  1.00 33.83  ? 428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.689 140.735 84.621  1.00 43.86  ? 428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.751 140.391 87.000  1.00 41.47  ? 428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.719 142.787 87.061  1.00 37.64  ? 429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.600 143.064 88.191  1.00 31.37  ? 429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.464 144.514 88.631  1.00 38.36  ? 429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.393 144.808 89.829  1.00 42.88  ? 429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.057 142.710 87.842  1.00 35.36  ? 429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.001 143.292 88.874  1.00 36.77  ? 429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.234 141.207 87.773  1.00 40.32  ? 429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.404 145.444 87.675  1.00 42.83  ? 430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.304 146.854 88.036  1.00 37.27  ? 430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.963 147.175 88.688  1.00 37.34  ? 430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.912 147.904 89.687  1.00 46.39  ? 430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.536 147.727 86.804  1.00 38.77  ? 430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.950 147.626 86.254  1.00 38.32  ? 430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.277 148.774 85.322  1.00 41.66  ? 430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.748 148.763 84.945  1.00 46.20  ? 430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.102 149.900 84.055  1.00 44.83  ? 430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.865 146.638 88.147  1.00 42.49  ? 431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.559 146.888 88.749  1.00 34.34  ? 431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.454 146.254 90.132  1.00 37.12  ? 431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.877 146.848 91.050  1.00 44.19  ? 431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.452 146.372 87.833  1.00 37.45  ? 431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.962 147.341 86.758  1.00 42.90  ? 431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 130.102 146.616 85.740  1.00 41.46  ? 431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.193 148.491 87.386  1.00 41.64  ? 431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.006 145.051 90.299  1.00 30.95  ? 432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.020 144.414 91.609  1.00 29.45  ? 432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.849 145.215 92.602  1.00 38.61  ? 432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.472 145.348 93.771  1.00 43.73  ? 432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.558 142.991 91.486  1.00 36.79  ? 432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.990 145.747 92.157  1.00 41.15  ? 433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.808 146.585 93.024  1.00 34.22  ? 433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.054 147.840 93.440  1.00 34.01  ? 433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.110 148.248 94.605  1.00 40.59  ? 433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.113 146.947 92.316  1.00 38.74  ? 433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.794 145.750 91.924  1.00 36.89  ? 433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.014 147.759 93.231  1.00 36.54  ? 433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.334 148.460 92.502  1.00 30.02  ? 434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.537 149.636 92.842  1.00 36.98  ? 434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.438 149.294 93.843  1.00 41.44  ? 434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.195 150.048 94.795  1.00 42.71  ? 434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.939 150.247 91.577  1.00 40.54  ? 434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.986 150.868 90.678  1.00 49.57  ? 434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 134.974 151.417 91.207  1.00 49.97  ? 434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.822 150.807 89.441  1.00 46.51  ? 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.759 148.161 93.643  1.00 35.77  ? 435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.702 147.757 94.567  1.00 25.23  ? 435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.256 147.475 95.958  1.00 30.34  ? 435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.654 147.865 96.964  1.00 41.76  ? 435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.974 146.529 94.026  1.00 31.48  ? 435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.802 145.382 94.079  1.00 35.44  ? 435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.400 146.794 96.032  1.00 34.65  ? 436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.007 146.509 97.327  1.00 23.11  ? 436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.497 147.785 97.998  1.00 24.36  ? 436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.424 147.915 99.225  1.00 34.03  ? 436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.149 145.512 97.156  1.00 33.75  ? 436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.712 144.124 96.695  1.00 25.12  ? 436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.909 143.263 96.342  1.00 24.83  ? 436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.864 143.474 97.762  1.00 26.30  ? 436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.995 148.739 97.208  1.00 34.22  ? 437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.370 150.038 97.752  1.00 31.21  ? 437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.161 150.750 98.339  1.00 39.59  ? 437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.244 151.346 99.418  1.00 47.99  ? 437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.012 150.892 96.660  1.00 23.89  ? 437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.117 150.182 96.089  1.00 37.11  ? 437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.504 152.207 97.231  1.00 32.70  ? 437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.026 150.698 97.639  1.00 35.84  ? 438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.805 151.299 98.164  1.00 33.70  ? 438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.365 150.620 99.454  1.00 29.84  ? 438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 129.938 151.288 100.403 1.00 45.02  ? 438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.691 151.230 97.121  1.00 40.01  ? 438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.419 151.880 97.562  1.00 36.47  ? 438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 127.444 151.205 98.262  1.00 40.15  ? 438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.964 153.146 97.408  1.00 34.94  ? 438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.441 152.025 98.519  1.00 42.67  ? 438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.732 153.209 98.011  1.00 46.21  ? 438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.452 149.289 99.504  1.00 25.76  ? 439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.074 148.564 100.715 1.00 27.84  ? 439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.974 148.960 101.879 1.00 35.99  ? 439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.503 149.178 103.002 1.00 43.35  ? 439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.111 147.044 100.465 1.00 30.94  ? 439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.912 146.284 101.766 1.00 30.37  ? 439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.051 146.652 99.460  1.00 30.47  ? 439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.282 149.056 101.630 1.00 40.52  ? 440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.209 149.457 102.684 1.00 36.96  ? 440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.935 150.880 103.153 1.00 36.93  ? 440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.964 151.161 104.357 1.00 41.93  ? 440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.649 149.321 102.190 1.00 34.95  ? 440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.573 149.536 103.242 1.00 41.88  ? 440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.670 151.794 102.216 1.00 36.29  ? 441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.429 153.185 102.582 1.00 37.07  ? 441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.139 153.341 103.379 1.00 44.31  ? 441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.103 154.075 104.373 1.00 51.03  ? 441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.390 154.057 101.329 1.00 37.28  ? 441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.748 154.578 100.896 1.00 44.71  ? 441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.855 154.746 99.395  1.00 50.92  ? 441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 132.811 154.679 98.712  1.00 49.84  ? 441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.982 154.949 98.898  1.00 46.61  ? 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.071 152.660 102.964 1.00 42.55  ? 442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.788 152.797 103.641 1.00 43.36  ? 442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.724 152.044 104.963 1.00 44.13  ? 442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.753 152.219 105.707 1.00 48.14  ? 442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.651 152.323 102.733 1.00 45.07  ? 442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.884 150.966 102.338 1.00 45.37  ? 442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.558 153.205 101.501 1.00 43.50  ? 442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.719 151.220 105.271 1.00 45.44  ? 443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.752 150.518 106.548 1.00 49.28  ? 443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.236 151.471 107.632 1.00 51.24  ? 443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.319 152.055 107.518 1.00 54.11  ? 443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.657 149.291 106.467 1.00 50.95  ? 443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.003 148.262 105.716 1.00 53.02  ? 443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.970 148.773 107.861 1.00 48.71  ? 443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.431 151.634 108.680 1.00 60.79  ? 444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 129.780 152.488 109.816 1.00 61.29  ? 444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.330 151.758 111.076 1.00 60.93  ? 444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.150 151.801 111.438 1.00 63.78  ? 444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.129 153.862 109.701 1.00 62.68  ? 444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 129.794 154.897 110.586 1.00 65.64  ? 444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 131.018 155.102 110.449 1.00 60.33  ? 444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 129.092 155.509 111.418 1.00 68.02  ? 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.267 151.088 111.735 1.00 50.34  ? 445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 129.981 150.292 112.922 1.00 55.39  ? 445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.430 151.097 114.132 1.00 57.74  ? 445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.620 151.383 114.298 1.00 56.60  ? 445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 130.669 148.923 112.862 1.00 53.99  ? 445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 129.901 147.996 111.923 1.00 53.85  ? 445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 130.738 148.302 114.242 1.00 54.33  ? 445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.677 146.784 111.504 1.00 49.61  ? 445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.472 151.471 114.980 1.00 67.70  ? 446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.744 152.388 116.078 1.00 68.46  ? 446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.235 151.686 117.337 1.00 63.19  ? 446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 130.952 152.304 118.129 1.00 60.22  ? 446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.493 153.213 116.407 1.00 65.68  ? 446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.172 152.441 116.413 1.00 65.62  ? 446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.534 152.356 115.027 1.00 65.06  ? 446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.610 153.615 114.295 1.00 70.56  ? 446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 125.861 154.680 114.546 1.00 68.83  ? 446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 124.950 154.674 115.505 1.00 63.58  ? 446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 126.026 155.777 113.811 1.00 66.78  ? 446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 129.876 150.422 117.540 1.00 53.70  ? 447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.253 149.707 118.751 1.00 49.54  ? 447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.599 149.005 118.637 1.00 50.22  ? 447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.083 148.458 119.634 1.00 52.45  ? 447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.171 148.690 119.120 1.00 50.40  ? 447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.234 149.205 120.192 1.00 54.38  ? 447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 128.638 149.412 121.335 1.00 56.80  ? 447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 126.977 149.418 119.826 1.00 47.99  ? 447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.211 149.006 117.458 1.00 53.71  ? 448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.560 148.473 117.264 1.00 49.18  ? 448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.455 149.604 116.782 1.00 48.65  ? 448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.440 149.944 115.585 1.00 44.00  ? 448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.561 147.318 116.267 1.00 44.53  ? 448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.242 150.219 117.665 1.00 43.57  ? 449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.021 151.399 117.267 1.00 38.96  ? 449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.151 151.064 116.311 1.00 42.31  ? 449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.364 151.766 115.318 1.00 42.81  ? 449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.562 151.932 118.602 1.00 40.91  ? 449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 135.846 151.156 119.674 1.00 46.12  ? 449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.477 149.853 119.067 1.00 37.53  ? 449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 137.886 149.990 116.609 1.00 40.22  ? 450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 138.999 149.595 115.754 1.00 29.24  ? 450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.513 149.131 114.387 1.00 37.35  ? 450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.144 149.428 113.367 1.00 40.84  ? 450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 139.820 148.503 116.434 1.00 38.46  ? 450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.396 148.403 114.346 1.00 45.06  ? 451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 136.846 147.952 113.069 1.00 35.02  ? 451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.468 149.148 112.206 1.00 35.92  ? 451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.793 149.205 111.015 1.00 42.67  ? 451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.641 147.021 113.301 1.00 33.21  ? 451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.763 146.963 112.063 1.00 39.06  ? 451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.105 145.630 113.686 1.00 33.49  ? 451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 135.782 150.127 112.800 1.00 36.86  ? 452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.381 151.317 112.058 1.00 38.91  ? 452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.592 152.119 111.595 1.00 37.69  ? 452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.639 152.589 110.451 1.00 43.84  ? 452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.461 152.174 112.927 1.00 35.25  ? 452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.132 153.540 112.362 1.00 40.12  ? 452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.682 154.476 113.467 1.00 39.17  ? 452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 132.232 154.624 113.495 1.00 51.24  ? 452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 131.570 155.358 114.378 1.00 52.08  ? 452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 132.199 156.039 115.322 1.00 44.60  ? 452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 130.243 155.410 114.313 1.00 48.87  ? 452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.586 152.280 112.473 1.00 35.47  ? 453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 138.781 153.033 112.111 1.00 32.91  ? 453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.533 152.362 110.969 1.00 38.11  ? 453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 139.975 153.034 110.030 1.00 46.97  ? 453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.686 153.194 113.334 1.00 33.22  ? 453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.164 153.274 113.006 1.00 33.43  ? 453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 141.885 154.246 113.919 1.00 33.88  ? 453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.215 154.570 113.416 1.00 34.25  ? 453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.329 153.964 113.802 1.00 37.13  ? 453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.314 152.994 114.699 1.00 37.14  ? 453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.489 154.343 113.271 1.00 38.84  ? 453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.674 151.036 111.023 1.00 39.49  ? 454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.377 150.330 109.959 1.00 29.54  ? 454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.573 150.309 108.667 1.00 35.88  ? 454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.157 150.334 107.582 1.00 44.90  ? 454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.713 148.909 110.401 1.00 35.12  ? 454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.243 150.256 108.755 1.00 36.21  ? 455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.428 150.349 107.551 1.00 37.84  ? 455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.594 151.710 106.889 1.00 42.06  ? 455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.680 151.806 105.659 1.00 44.54  ? 455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 135.959 150.088 107.888 1.00 39.91  ? 455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.086 149.993 106.654 1.00 47.02  ? 455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.221 149.067 105.855 1.00 48.21  ? 455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.182 150.951 106.492 1.00 43.06  ? 455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.639 152.776 107.690 1.00 37.39  ? 456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 137.838 154.108 107.130 1.00 34.27  ? 456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.246 154.287 106.573 1.00 37.34  ? 456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.423 154.948 105.544 1.00 44.87  ? 456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.550 155.173 108.187 1.00 38.49  ? 456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.078 155.326 108.528 1.00 47.46  ? 456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 135.866 156.407 109.575 1.00 46.95  ? 456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.420 156.452 110.038 1.00 44.27  ? 456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 134.204 157.499 111.073 1.00 43.38  ? 456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.254 153.713 107.231 1.00 38.11  ? 457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.646 153.958 106.867 1.00 32.41  ? 457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.131 153.030 105.756 1.00 39.59  ? 457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.531 153.490 104.683 1.00 44.38  ? 457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.534 153.813 108.107 1.00 30.49  ? 457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.099 151.720 106.003 1.00 43.18  ? 458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.668 150.765 105.060 1.00 36.05  ? 458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.811 150.611 103.812 1.00 37.04  ? 458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.347 150.343 102.731 1.00 46.79  ? 458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.855 149.411 105.743 1.00 33.84  ? 458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.350 149.506 107.175 1.00 40.38  ? 458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.148 149.489 107.283 1.00 52.20  ? 458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.533 148.058 106.282 1.00 38.12  ? 458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.492 150.766 103.938 1.00 31.24  ? 459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.571 150.645 102.806 1.00 32.01  ? 459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.752 149.310 102.088 1.00 32.41  ? 459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.724 149.230 100.859 1.00 37.41  ? 459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.739 151.812 101.831 1.00 34.12  ? 459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.576 153.182 102.463 1.00 37.18  ? 459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.448 154.212 101.768 1.00 36.20  ? 459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.296 155.581 102.404 1.00 38.30  ? 459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.230 156.573 101.808 1.00 39.74  ? 459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.945 148.251 102.867 1.00 33.97  ? 460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.232 146.940 102.306 1.00 26.33  ? 460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.953 146.243 101.868 1.00 27.73  ? 460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.924 146.312 102.546 1.00 41.83  ? 460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.968 146.076 103.326 1.00 31.40  ? 460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 140.149 145.826 104.453 1.00 40.23  ? 460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.026 145.566 100.722 1.00 25.14  ? 461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.905 144.820 100.171 1.00 21.75  ? 461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.380 143.418 99.820  1.00 29.75  ? 461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.577 143.155 99.691  1.00 45.04  ? 461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.298 145.506 98.930  1.00 24.63  ? 461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.329 145.572 97.804  1.00 15.30  ? 461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.794 146.897 99.280  1.00 35.19  ? 461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.771 146.071 96.497  1.00 24.15  ? 461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.421 142.509 99.680  1.00 25.78  ? 462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.738 141.155 99.275  1.00 18.30  ? 462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.008 140.735 98.019  1.00 16.49  ? 462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.785 140.579 98.031  1.00 35.45  ? 462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.742 140.544 96.931  1.00 17.96  ? 463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.168 140.143 95.651  1.00 20.77  ? 463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.620 138.719 95.354  1.00 28.28  ? 463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.739 138.497 94.885  1.00 38.73  ? 463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.575 141.105 94.542  1.00 29.69  ? 463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.055 140.737 93.154  1.00 21.32  ? 463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.551 140.572 93.203  1.00 15.67  ? 463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.451 141.787 92.133  1.00 23.96  ? 463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.744 137.753 95.631  1.00 22.47  ? 464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.027 136.360 95.382  1.00 24.02  ? 464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.512 135.890 94.031  1.00 23.51  ? 464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.932 136.638 93.248  1.00 29.86  ? 464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.745 134.609 93.768  1.00 20.51  ? 465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.273 133.968 92.553  1.00 22.14  ? 465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.690 132.609 92.905  1.00 32.55  ? 465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.126 131.956 93.855  1.00 43.40  ? 465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.395 133.812 91.521  1.00 32.27  ? 465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.696 132.192 92.126  1.00 39.06  ? 466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.057 130.899 92.304  1.00 38.61  ? 466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.817 130.281 90.935  1.00 38.24  ? 466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.054 130.906 89.898  1.00 45.56  ? 466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.744 131.018 93.087  1.00 40.51  ? 466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.569 131.487 92.254  1.00 36.72  ? 466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.373 132.429 93.211  1.00 50.25  ? 466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.734 133.514 91.943  1.00 46.05  ? 466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.352 129.030 90.945  1.00 31.41  ? 467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.073 128.263 89.733  1.00 28.27  ? 467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.336 127.988 88.924  1.00 32.66  ? 467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.288 127.908 87.695  1.00 43.89  ? 467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.025 128.955 88.854  1.00 31.59  ? 467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.091 127.974 88.178  1.00 39.58  ? 467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 131.242 126.761 88.315  1.00 48.39  ? 467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.113 128.495 87.450  1.00 38.10  ? 467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.478 127.852 89.600  1.00 25.90  ? 468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.700 127.467 88.903  1.00 26.55  ? 468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.603 126.040 88.384  1.00 40.68  ? 468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.844 125.780 87.199  1.00 45.53  ? 468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.907 127.620 89.828  1.00 34.66  ? 468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.256 127.241 89.218  1.00 31.70  ? 468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.723 128.293 88.228  1.00 34.33  ? 468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.294 127.020 90.301  1.00 31.22  ? 468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.234 125.100 89.257  1.00 43.69  ? 469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.105 123.711 88.832  1.00 32.19  ? 469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.974 123.548 87.829  1.00 41.52  ? 469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.083 122.755 86.889  1.00 58.40  ? 469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.884 122.802 90.039  1.00 36.67  ? 469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.090 121.350 89.743  1.00 38.98  ? 469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.790 120.355 90.647  1.00 44.05  ? 469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.567 120.724 88.641  1.00 38.82  ? 469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.074 119.179 90.115  1.00 41.26  ? 469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.547 119.375 88.898  1.00 38.81  ? 469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.877 124.284 88.014  1.00 33.25  ? 470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.794 124.225 87.047  1.00 30.54  ? 470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.228 124.684 85.669  1.00 31.88  ? 470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.921 124.043 84.661  1.00 49.61  ? 470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.959 125.801 85.609  1.00 28.74  ? 471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.448 126.287 84.324  1.00 37.22  ? 471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.430 125.304 83.701  1.00 42.53  ? 471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.378 125.045 82.493  1.00 40.90  ? 471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.108 127.657 84.484  1.00 34.57  ? 471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.618 128.217 83.177  1.00 35.57  ? 471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.749 128.810 82.274  1.00 39.30  ? 471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.958 128.128 82.831  1.00 31.12  ? 471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.198 129.315 81.076  1.00 40.05  ? 471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.418 128.629 81.629  1.00 29.13  ? 471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.530 129.223 80.757  1.00 38.15  ? 471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 136.967 129.726 79.556  1.00 42.84  ? 471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.339 124.750 84.508  1.00 44.47  ? 472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.333 123.826 83.973  1.00 46.01  ? 472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.687 122.551 83.450  1.00 44.17  ? 472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 137.057 122.055 82.380  1.00 47.01  ? 472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.377 123.500 85.041  1.00 42.96  ? 472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.257 124.660 85.507  1.00 37.18  ? 472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.988 124.292 86.788  1.00 41.91  ? 472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.236 125.059 84.418  1.00 35.45  ? 472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.720 122.003 84.188  1.00 40.95  ? 473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 135.085 120.759 83.773  1.00 42.20  ? 473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.158 120.979 82.585  1.00 45.63  ? 473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 134.072 120.127 81.694  1.00 54.21  ? 473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.325 120.145 84.946  1.00 45.11  ? 473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.457 122.113 82.551  1.00 41.24  ? 474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.590 122.419 81.421  1.00 45.25  ? 474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.369 122.822 80.178  1.00 45.91  ? 474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.768 122.943 79.104  1.00 46.99  ? 474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.604 123.524 81.804  1.00 42.98  ? 474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.469 123.043 82.691  1.00 44.30  ? 474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.544 124.162 83.121  1.00 44.88  ? 474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.878 124.785 82.295  1.00 45.65  ? 474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.494 124.419 84.423  1.00 43.89  ? 474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.680 123.033 80.295  1.00 53.18  ? 475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.540 123.325 79.157  1.00 53.23  ? 475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.503 122.180 78.863  1.00 51.29  ? 475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.473 122.362 78.120  1.00 50.33  ? 475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.310 124.624 79.393  1.00 49.03  ? 475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.505 125.851 79.016  1.00 51.33  ? 475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.578 126.333 77.887  1.00 54.36  ? 475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.722 126.357 79.960  1.00 47.59  ? 475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.252 121.005 79.431  1.00 45.91  ? 476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.091 119.844 79.190  1.00 47.47  ? 476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.497 119.952 79.737  1.00 51.91  ? 476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.449 119.529 79.071  1.00 52.77  ? 476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.653 120.508 80.936  1.00 45.46  ? 477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.951 120.637 81.586  1.00 42.38  ? 477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.857 119.995 82.961  1.00 43.75  ? 477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.983 120.353 83.761  1.00 45.07  ? 477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.395 122.105 81.702  1.00 38.76  ? 477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.291 122.806 80.348  1.00 39.69  ? 477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.814 122.189 82.229  1.00 41.95  ? 477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.243 124.307 80.454  1.00 47.02  ? 477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.749 119.049 83.235  1.00 47.32  ? 478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.811 118.446 84.558  1.00 47.10  ? 478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.376 119.443 85.561  1.00 47.11  ? 478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.273 120.226 85.241  1.00 44.58  ? 478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.668 117.182 84.530  1.00 46.22  ? 478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.842 119.408 86.784  1.00 44.93  ? 479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.262 120.360 87.808  1.00 40.76  ? 479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.742 120.206 88.138  1.00 47.51  ? 479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.446 121.202 88.346  1.00 53.19  ? 479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.409 120.181 89.062  1.00 38.47  ? 479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.572 121.269 90.099  1.00 37.75  ? 479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.526 121.163 91.101  1.00 41.48  ? 479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.765 122.398 90.082  1.00 41.12  ? 479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.676 122.152 92.052  1.00 43.84  ? 479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.907 123.392 91.028  1.00 41.69  ? 479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.864 123.263 92.011  1.00 46.46  ? 479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.011 124.251 92.957  1.00 48.56  ? 479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.232 118.969 88.195  1.00 44.22  ? 480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.632 118.720 88.501  1.00 43.41  ? 480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.544 118.888 87.294  1.00 45.14  ? 480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.769 118.869 87.458  1.00 51.87  ? 480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.807 117.310 89.059  1.00 47.30  ? 480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.150 117.074 90.400  1.00 48.46  ? 480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.365 115.784 90.424  1.00 54.88  ? 480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.366 115.684 89.679  1.00 52.49  ? 480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 143.757 114.862 91.167  1.00 54.39  ? 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.984 119.042 86.099  1.00 42.48  ? 481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.799 119.134 84.902  1.00 45.77  ? 481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.597 120.437 84.894  1.00 46.16  ? 481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.139 121.458 85.414  1.00 49.64  ? 481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.922 119.055 83.656  1.00 45.72  ? 481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.552 120.348 83.211  1.00 44.75  ? 481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.803 120.422 84.322  1.00 46.92  ? 482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.585 121.667 84.237  1.00 43.27  ? 482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.898 122.754 83.432  1.00 45.23  ? 482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.168 123.941 83.656  1.00 47.23  ? 482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.894 121.213 83.575  1.00 47.55  ? 482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.961 119.743 83.820  1.00 49.30  ? 482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.544 119.266 83.794  1.00 46.47  ? 482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.024 122.387 82.492  1.00 48.90  ? 483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.270 123.393 81.751  1.00 44.63  ? 483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.330 124.162 82.671  1.00 44.41  ? 483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.134 125.369 82.498  1.00 49.96  ? 483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.494 122.738 80.610  1.00 51.82  ? 483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.363 121.986 79.615  1.00 54.67  ? 483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.601 120.544 80.017  1.00 54.39  ? 483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 145.712 119.954 80.666  1.00 50.24  ? 483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.675 120.001 79.687  1.00 50.45  ? 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.734 123.479 83.650  1.00 39.88  ? 484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.893 124.167 84.623  1.00 39.42  ? 484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.700 125.169 85.436  1.00 44.50  ? 484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.237 126.286 85.694  1.00 46.93  ? 484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.219 123.155 85.546  1.00 35.91  ? 484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.907 124.786 85.855  1.00 41.07  ? 485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.755 125.709 86.601  1.00 34.61  ? 485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.188 126.883 85.733  1.00 38.28  ? 485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.270 128.017 86.214  1.00 49.80  ? 485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.970 124.973 87.160  1.00 39.55  ? 485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.640 124.026 88.296  1.00 40.24  ? 485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.897 123.571 89.009  1.00 42.52  ? 485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.761 122.776 88.145  1.00 44.19  ? 485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.657 121.464 87.986  1.00 43.96  ? 485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.730 120.763 88.618  1.00 42.20  ? 485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.504 120.841 87.172  1.00 37.46  ? 485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.472 126.633 84.454  1.00 41.59  ? 486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.805 127.721 83.540  1.00 40.85  ? 486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.636 128.686 83.382  1.00 40.16  ? 486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.820 129.913 83.398  1.00 42.76  ? 486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.219 127.144 82.187  1.00 47.08  ? 486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.737 128.197 81.236  1.00 51.07  ? 486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.647 128.959 81.623  1.00 53.58  ? 486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.238 128.253 80.094  1.00 50.08  ? 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.423 128.149 83.231  1.00 39.75  ? 487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.247 129.004 83.134  1.00 39.96  ? 487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.043 129.806 84.407  1.00 39.37  ? 487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.704 130.991 84.350  1.00 46.90  ? 487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.996 128.179 82.843  1.00 42.22  ? 487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.728 128.874 83.237  1.00 40.97  ? 487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.213 129.892 82.456  1.00 39.10  ? 487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.065 128.534 84.404  1.00 44.31  ? 487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.059 130.545 82.822  1.00 42.89  ? 487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.908 129.188 84.774  1.00 39.30  ? 487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.407 130.194 83.980  1.00 39.49  ? 487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.210 129.170 85.568  1.00 34.67  ? 488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.058 129.889 86.827  1.00 32.30  ? 488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.100 130.990 86.953  1.00 35.91  ? 488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.787 132.104 87.385  1.00 44.08  ? 488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.155 128.920 88.001  1.00 29.98  ? 488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.342 130.700 86.562  1.00 38.20  ? 489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.389 131.710 86.575  1.00 31.18  ? 489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.992 132.913 85.734  1.00 33.48  ? 489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.014 134.053 86.209  1.00 38.09  ? 489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.696 131.106 86.064  1.00 34.37  ? 489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.915 131.863 86.539  1.00 41.00  ? 489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.016 132.230 87.708  1.00 46.44  ? 489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.855 132.095 85.631  1.00 39.66  ? 489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.596 132.673 84.481  1.00 40.60  ? 490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.249 133.782 83.597  1.00 37.19  ? 490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.028 134.540 84.109  1.00 40.24  ? 490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.023 135.776 84.154  1.00 47.35  ? 490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.006 133.270 82.179  1.00 43.22  ? 490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.140 132.511 81.744  1.00 49.81  ? 490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.788 134.434 81.228  1.00 43.82  ? 490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 143.986 133.810 84.516  1.00 33.67  ? 491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.744 134.445 84.940  1.00 28.70  ? 491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.950 135.293 86.184  1.00 35.66  ? 491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.481 136.434 86.251  1.00 41.55  ? 491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.674 133.381 85.191  1.00 32.40  ? 491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.368 133.936 85.685  1.00 32.59  ? 491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.418 134.399 84.794  1.00 33.63  ? 491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.088 133.990 87.040  1.00 33.23  ? 491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.217 134.909 85.243  1.00 34.23  ? 491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.892 134.502 87.494  1.00 28.90  ? 491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 137.954 134.960 86.595  1.00 34.17  ? 491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.654 134.762 87.183  1.00 38.04  ? 492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.845 135.510 88.412  1.00 22.37  ? 492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.906 136.591 88.281  1.00 25.49  ? 492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.832 137.591 88.997  1.00 39.44  ? 492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.163 134.550 89.557  1.00 29.26  ? 492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.966 133.775 90.030  1.00 34.32  ? 492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.040 134.359 90.875  1.00 32.63  ? 492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.745 132.478 89.598  1.00 32.30  ? 492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.931 133.657 91.302  1.00 27.82  ? 492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.637 131.772 90.021  1.00 24.82  ? 492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.730 132.362 90.875  1.00 30.41  ? 492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.863 136.449 87.358  1.00 32.96  ? 493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.725 137.580 87.045  1.00 30.84  ? 493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.921 138.704 86.408  1.00 31.80  ? 493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.134 139.878 86.721  1.00 41.18  ? 493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.876 137.132 86.139  1.00 28.02  ? 493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.696 138.251 85.481  1.00 37.22  ? 493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 147.965 139.064 84.043  1.00 45.43  ? 493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.962 137.717 82.867  1.00 41.00  ? 493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 144.987 138.360 85.517  1.00 36.18  ? 494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.100 139.365 84.937  1.00 29.38  ? 494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.251 140.029 86.014  1.00 40.65  ? 494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.080 141.256 86.020  1.00 47.49  ? 494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.206 138.706 83.885  1.00 32.42  ? 494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 143.911 138.351 82.587  1.00 35.04  ? 494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 142.795 138.194 81.181  1.00 54.75  ? 494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.326 139.896 80.908  1.00 44.20  ? 494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.717 139.227 86.936  1.00 36.51  ? 495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.887 139.756 88.015  1.00 28.03  ? 495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.695 140.697 88.898  1.00 36.57  ? 495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.230 141.784 89.254  1.00 41.48  ? 495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.274 138.601 88.829  1.00 30.25  ? 495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.729 139.110 90.153  1.00 24.51  ? 495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.182 137.913 88.030  1.00 35.60  ? 495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.916 140.297 89.263  1.00 35.78  ? 496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.773 141.159 90.068  1.00 23.07  ? 496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.128 142.436 89.321  1.00 29.65  ? 496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.118 143.526 89.903  1.00 41.13  ? 496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.038 140.405 90.474  1.00 23.86  ? 496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.763 141.064 91.628  1.00 31.99  ? 496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.150 141.719 92.468  1.00 39.81  ? 496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.078 140.889 91.677  1.00 35.66  ? 496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.440 142.321 88.028  1.00 31.36  ? 497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.774 143.492 87.227  1.00 26.50  ? 497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.634 144.496 87.235  1.00 34.39  ? 497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.838 145.685 87.500  1.00 45.65  ? 497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.099 143.063 85.795  1.00 33.30  ? 497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.456 144.202 84.882  1.00 36.09  ? 497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 147.761 144.649 84.792  1.00 37.62  ? 497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 145.488 144.822 84.111  1.00 37.03  ? 497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 148.093 145.693 83.954  1.00 39.56  ? 497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 145.814 145.866 83.272  1.00 34.31  ? 497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.118 146.302 83.193  1.00 33.97  ? 497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.416 144.030 86.971  1.00 36.42  ? 498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.301 144.963 86.874  1.00 33.61  ? 498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.820 145.434 88.240  1.00 36.80  ? 498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.308 146.550 88.350  1.00 43.00  ? 498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.167 144.336 86.065  1.00 36.82  ? 498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.532 144.204 84.606  1.00 36.96  ? 498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.852 145.324 83.851  1.00 38.67  ? 498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.581 142.965 83.989  1.00 35.05  ? 498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.199 145.214 82.521  1.00 34.11  ? 498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.924 142.845 82.659  1.00 42.08  ? 498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.232 143.973 81.929  1.00 43.21  ? 498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.575 143.856 80.602  1.00 48.61  ? 498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.009 144.637 89.294  1.00 29.22  ? 499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.699 145.121 90.635  1.00 24.41  ? 499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.666 146.219 91.059  1.00 30.70  ? 499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.246 147.237 91.619  1.00 39.99  ? 499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.724 143.962 91.632  1.00 22.93  ? 499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.046 143.506 91.851  1.00 32.17  ? 499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 143.961 146.037 90.788  1.00 29.15  ? 500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 144.937 147.086 91.068  1.00 29.16  ? 500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.641 148.321 90.227  1.00 31.08  ? 500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.740 149.456 90.707  1.00 42.24  ? 500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.366 146.566 90.826  1.00 29.60  ? 500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.708 145.452 91.811  1.00 25.23  ? 500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.375 147.690 90.956  1.00 30.25  ? 500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.934 144.667 91.424  1.00 29.58  ? 500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.273 148.119 88.959  1.00 33.40  ? 501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 143.958 149.244 88.089  1.00 30.99  ? 501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 142.748 150.016 88.595  1.00 39.26  ? 501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 142.753 151.250 88.608  1.00 47.09  ? 501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.727 148.749 86.662  1.00 37.80  ? 501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.031 149.778 85.591  1.00 38.16  ? 501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.879 149.220 84.192  1.00 42.40  ? 501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.873 148.590 83.869  1.00 44.27  ? 501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 144.882 149.446 83.353  1.00 38.81  ? 501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.702 149.308 89.025  1.00 43.97  ? 502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.519 149.984 89.545  1.00 34.66  ? 502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.812 150.676 90.870  1.00 37.95  ? 502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.296 151.767 91.128  1.00 46.93  ? 502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.366 148.996 89.701  1.00 37.74  ? 502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.039 149.669 89.990  1.00 39.19  ? 502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 137.697 150.675 88.907  1.00 41.75  ? 502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.699 151.638 89.352  1.00 38.41  ? 502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.618 152.888 88.916  1.00 39.77  ? 502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 137.459 153.361 88.011  1.00 41.70  ? 502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.669 153.684 89.401  1.00 40.17  ? 502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.633 150.060 91.723  1.00 34.19  ? 503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.011 150.710 92.974  1.00 30.26  ? 503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 142.784 151.995 92.710  1.00 34.23  ? 503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.531 153.026 93.346  1.00 40.88  ? 503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.832 149.750 93.832  1.00 29.74  ? 503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.945 150.222 95.161  1.00 41.60  ? 503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 143.721 151.958 91.761  1.00 37.79  ? 504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.471 153.158 91.409  1.00 30.30  ? 504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 143.569 154.210 90.776  1.00 41.23  ? 504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 143.738 155.409 91.021  1.00 49.78  ? 504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 145.623 152.798 90.473  1.00 32.04  ? 504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 142.603 153.783 89.959  1.00 44.43  ? 505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 141.668 154.728 89.357  1.00 40.36  ? 505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 140.792 155.389 90.412  1.00 41.87  ? 505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.512 156.590 90.330  1.00 49.05  ? 505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 140.809 154.019 88.312  1.00 39.73  ? 505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 141.520 153.759 86.995  1.00 42.63  ? 505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 140.749 152.813 86.097  1.00 53.05  ? 505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 139.648 152.381 86.494  1.00 50.45  ? 505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 141.246 152.503 84.993  1.00 54.05  ? 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.345 154.622 91.407  1.00 36.89  ? 506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.559 155.194 92.495  1.00 34.58  ? 506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.407 156.158 93.315  1.00 44.50  ? 506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 139.934 157.221 93.732  1.00 52.27  ? 506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 138.960 154.079 93.370  1.00 36.51  ? 506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 137.951 153.253 92.572  1.00 41.25  ? 506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.285 154.665 94.596  1.00 44.66  ? 506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.570 151.952 93.240  1.00 35.38  ? 506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 141.673 155.807 93.556  1.00 41.07  ? 507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.565 156.713 94.272  1.00 37.30  ? 507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 142.768 158.010 93.498  1.00 42.03  ? 507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 142.820 159.096 94.088  1.00 53.07  ? 507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 143.905 156.031 94.539  1.00 39.31  ? 507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 142.894 157.916 92.173  1.00 43.35  ? 508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.035 159.109 91.346  1.00 43.01  ? 508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 141.765 159.953 91.360  1.00 47.81  ? 508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 141.830 161.184 91.463  1.00 56.17  ? 508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.397 158.707 89.916  1.00 49.40  ? 508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 143.040 159.741 88.865  1.00 51.98  ? 508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.853 159.544 87.597  1.00 50.92  ? 508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 143.446 160.536 86.523  1.00 49.19  ? 508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 142.967 161.819 87.106  1.00 52.99  ? 508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 140.599 159.310 91.261  1.00 52.58  ? 509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.342 160.041 91.159  1.00 55.38  ? 509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 138.914 160.646 92.490  1.00 57.04  ? 509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 138.228 161.674 92.504  1.00 58.35  ? 509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.250 159.120 90.605  1.00 48.00  ? 509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 137.263 158.597 91.636  1.00 53.22  ? 509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 136.166 157.755 91.016  1.00 62.97  ? 509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 135.755 156.758 91.644  1.00 63.03  ? 509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 135.717 158.090 89.899  1.00 60.36  ? 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.299 160.034 93.609  1.00 49.16  ? 510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 138.992 160.567 94.928  1.00 47.86  ? 510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.127 161.390 95.514  1.00 50.65  ? 510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 139.906 162.117 96.488  1.00 53.51  ? 510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.639 159.427 95.893  1.00 47.33  ? 510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.530 158.515 95.394  1.00 51.82  ? 510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 136.922 157.707 96.526  1.00 52.51  ? 510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 135.707 156.927 96.053  1.00 49.10  ? 510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 134.653 156.844 97.099  1.00 46.41  ? 510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.330 161.297 94.950  1.00 52.94  ? 511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.460 162.044 95.458  1.00 51.49  ? 511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.066 161.501 96.728  1.00 52.03  ? 511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 143.930 162.159 97.315  1.00 55.58  ? 511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.644 160.320 97.174  1.00 51.54  ? 512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.148 159.739 98.408  1.00 52.25  ? 512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.431 158.259 98.202  1.00 50.90  ? 512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 142.732 157.572 97.454  1.00 53.91  ? 512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.156 159.920 99.565  1.00 51.31  ? 512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 140.747 159.451 99.249  1.00 51.69  ? 512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 139.863 159.397 100.478 1.00 57.66  ? 512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 140.398 159.178 101.585 1.00 57.43  ? 512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 138.634 159.571 100.339 1.00 53.76  ? 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.472 157.781 98.873  1.00 46.10  ? 513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 144.817 156.371 98.935  1.00 42.35  ? 513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.391 155.813 100.288 1.00 43.68  ? 513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 143.741 156.491 101.089 1.00 52.96  ? 513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.317 156.174 98.705  1.00 41.88  ? 513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.043 156.703 99.819  1.00 44.21  ? 513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 146.754 156.896 97.445  1.00 41.29  ? 513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.757 154.562 100.546 1.00 37.81  ? 514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.525 154.033 101.879 1.00 37.19  ? 514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.607 154.536 102.828 1.00 40.34  ? 514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.685 154.963 102.410 1.00 48.27  ? 514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.466 152.501 101.863 1.00 36.42  ? 514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.769 151.827 101.530 1.00 31.13  ? 514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.107 151.558 100.216 1.00 33.25  ? 514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.633 151.421 102.532 1.00 33.20  ? 514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.292 150.923 99.905  1.00 34.66  ? 514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 147.820 150.786 102.228 1.00 36.17  ? 514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.149 150.536 100.913 1.00 38.55  ? 514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.296 154.505 104.122 1.00 46.70  ? 515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.209 155.065 105.108 1.00 46.80  ? 515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.509 154.273 105.148 1.00 46.65  ? 515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.508 153.041 105.097 1.00 53.85  ? 515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.555 155.086 106.489 1.00 48.57  ? 515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.529 156.193 106.629 1.00 53.25  ? 515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 143.972 156.623 105.597 1.00 54.04  ? 515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.281 156.634 107.770 1.00 52.90  ? 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.624 155.002 105.235 1.00 39.79  ? 516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 149.965 154.420 105.197 1.00 43.55  ? 516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.204 153.659 103.896 1.00 43.68  ? 516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 150.822 152.593 103.883 1.00 51.50  ? 516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.217 153.519 106.408 1.00 44.70  ? 516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.107 154.222 107.747 1.00 45.29  ? 516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.211 153.260 108.911 1.00 47.16  ? 516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.299 152.792 109.249 1.00 46.78  ? 516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.077 152.956 109.529 1.00 38.15  ? 516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.703 154.205 102.786 1.00 38.39  ? 517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 149.964 153.591 101.489 1.00 37.92  ? 517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.417 153.761 101.069 1.00 41.00  ? 517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 151.977 152.877 100.409 1.00 48.57  ? 517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.039 154.181 100.425 1.00 35.30  ? 517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 149.619 154.146 99.029  1.00 41.25  ? 517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.637 152.969 98.293  1.00 37.59  ? 517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.157 155.288 98.449  1.00 42.32  ? 517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.170 152.931 97.021  1.00 39.25  ? 517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 150.694 155.259 97.179  1.00 39.25  ? 517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 150.698 154.077 96.470  1.00 41.93  ? 517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.229 154.047 95.202  1.00 44.35  ? 517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.042 154.882 101.439 1.00 42.49  ? 518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.375 155.200 100.938 1.00 46.15  ? 518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.407 154.165 101.365 1.00 48.99  ? 518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.401 153.955 100.660 1.00 47.24  ? 518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.793 156.592 101.411 1.00 46.06  ? 518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.103 157.739 100.684 1.00 48.75  ? 518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 151.653 157.907 101.096 1.00 56.17  ? 518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 151.308 157.518 102.232 1.00 57.21  ? 518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 150.859 158.430 100.286 1.00 54.46  ? 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.198 153.514 102.507 1.00 38.63  ? 519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.100 152.463 102.936 1.00 33.32  ? 519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 154.837 151.104 102.329 1.00 41.92  ? 519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.663 150.201 102.483 1.00 46.65  ? 519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.710 150.939 101.643 1.00 38.81  ? 520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.361 149.655 101.057 1.00 31.29  ? 520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.218 149.369 99.828  1.00 36.17  ? 520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 154.800 150.268 99.216  1.00 38.19  ? 520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 151.881 149.624 100.679 1.00 30.29  ? 520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.605 150.542 99.637  1.00 40.95  ? 520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.293 148.084 99.472  1.00 36.75  ? 521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.066 147.679 98.305  1.00 37.83  ? 521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.457 148.178 97.002  1.00 38.87  ? 521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.145 148.185 95.977  1.00 43.15  ? 521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.205 146.158 98.266  1.00 36.70  ? 521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.913 145.562 98.110  1.00 33.09  ? 521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.837 145.650 99.549  1.00 35.99  ? 521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.184 148.586 97.013  1.00 38.84  ? 522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.607 149.212 95.830  1.00 35.18  ? 522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.300 150.531 95.515  1.00 39.87  ? 522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.603 150.822 94.352  1.00 43.12  ? 522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.108 149.440 96.026  1.00 29.19  ? 522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.314 148.191 96.325  1.00 33.80  ? 522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.122 147.218 95.354  1.00 31.87  ? 522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.740 147.993 97.572  1.00 39.23  ? 522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.390 146.079 95.623  1.00 33.37  ? 522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.005 146.860 97.847  1.00 39.71  ? 522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.836 145.905 96.870  1.00 39.52  ? 522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.105 144.771 97.143  1.00 46.77  ? 522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.559 151.343 96.543  1.00 44.47  ? 523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.214 152.628 96.326  1.00 42.45  ? 523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 155.676 152.447 95.940  1.00 49.75  ? 523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.180 153.144 95.051  1.00 54.92  ? 523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.093 153.496 97.577  1.00 41.07  ? 523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.373 151.520 96.595  1.00 47.54  ? 524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 157.778 151.275 96.300  1.00 46.34  ? 524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 157.988 150.488 95.014  1.00 47.22  ? 524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.121 150.423 94.526  1.00 53.29  ? 524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.442 150.531 97.462  1.00 47.83  ? 524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.147 149.133 97.369  1.00 48.95  ? 524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 157.936 151.064 98.793  1.00 43.16  ? 524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 156.935 149.893 94.457  1.00 42.22  ? 525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.054 149.095 93.256  1.00 44.22  ? 525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.531 147.678 93.472  1.00 43.67  ? 525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.679 146.937 92.492  1.00 46.67  ? 525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 157.781 147.275 94.719  1.00 45.28  ? 526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.228 145.915 94.997  1.00 47.81  ? 526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.138 144.886 94.731  1.00 46.09  ? 526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.453 143.729 94.430  1.00 47.25  ? 526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.710 145.816 96.447  1.00 44.96  ? 526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.304 144.470 96.831  1.00 48.42  ? 526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 158.939 144.055 98.243  1.00 57.36  ? 526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.216 144.830 99.182  1.00 51.74  ? 526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 158.375 142.954 98.413  1.00 51.04  ? 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 155.867 145.282 94.826  1.00 41.50  ? 527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 154.775 144.349 94.572  1.00 41.05  ? 527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.757 143.897 93.117  1.00 44.39  ? 527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.477 142.727 92.828  1.00 48.98  ? 527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.442 144.996 94.950  1.00 35.33  ? 527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.245 144.088 94.783  1.00 42.05  ? 527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.870 143.215 95.794  1.00 44.17  ? 527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.491 144.107 93.618  1.00 37.98  ? 527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.778 142.382 95.649  1.00 42.81  ? 527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.399 143.278 93.464  1.00 41.24  ? 527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.046 142.418 94.481  1.00 44.88  ? 527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 148.957 141.590 94.333  1.00 45.51  ? 527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.054 144.804 92.191  1.00 48.42  ? 528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 154.947 144.541 90.763  1.00 43.23  ? 528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.192 143.884 90.179  1.00 47.04  ? 528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.292 143.771 88.953  1.00 54.50  ? 528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.659 145.842 90.010  1.00 44.57  ? 528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.433 146.566 90.490  1.00 46.64  ? 528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 152.200 146.327 89.909  1.00 41.85  ? 528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 153.514 147.493 91.516  1.00 45.32  ? 528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 151.072 146.993 90.345  1.00 43.05  ? 528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 152.390 148.161 91.955  1.00 42.96  ? 528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.168 147.910 91.368  1.00 42.71  ? 528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.137 143.455 91.018  1.00 51.93  ? 529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.394 142.915 90.507  1.00 50.00  ? 529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.165 141.662 89.671  1.00 49.88  ? 529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.622 141.570 88.525  1.00 53.45  ? 529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.344 142.622 91.668  1.00 49.18  ? 529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 159.946 143.880 92.260  1.00 55.63  ? 529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 159.759 144.965 91.671  1.00 50.84  ? 529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.608 143.783 93.315  1.00 58.28  ? 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.446 140.684 90.227  1.00 53.15  ? 530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.181 139.453 89.494  1.00 53.82  ? 530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.234 139.672 88.323  1.00 56.94  ? 530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.204 138.848 87.404  1.00 57.04  ? 530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.609 138.392 90.435  1.00 51.75  ? 530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.095 138.313 90.432  1.00 51.10  ? 530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.587 137.429 91.550  1.00 51.95  ? 530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.086 137.256 91.461  1.00 52.45  ? 530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.437 137.539 92.768  1.00 53.72  ? 530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.466 140.759 88.334  1.00 55.37  ? 531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.560 141.058 87.235  1.00 45.68  ? 531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.251 141.774 86.087  1.00 48.17  ? 531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.854 141.598 84.929  1.00 53.85  ? 531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.387 141.900 87.740  1.00 46.77  ? 531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.383 141.112 88.547  1.00 51.10  ? 531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.700 140.043 87.983  1.00 49.11  ? 531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.118 141.434 89.870  1.00 50.09  ? 531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 150.782 139.319 88.712  1.00 46.59  ? 531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.200 140.714 90.607  1.00 47.38  ? 531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.536 139.658 90.023  1.00 49.47  ? 531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.621 138.937 90.753  1.00 51.98  ? 531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.276 142.581 86.378  1.00 51.17  ? 532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.069 143.209 85.325  1.00 51.74  ? 532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.259 142.359 84.912  1.00 52.90  ? 532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.949 142.706 83.941  1.00 50.71  ? 532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.567 144.602 85.756  1.00 48.81  ? 532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.401 145.467 86.209  1.00 50.31  ? 532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.611 144.480 86.852  1.00 49.02  ? 532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.531 141.257 85.616  1.00 55.71  ? 533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.630 140.371 85.261  1.00 55.89  ? 533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.187 139.047 84.655  1.00 57.42  ? 533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.986 138.412 83.962  1.00 56.53  ? 533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.499 140.082 86.494  1.00 54.83  ? 533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.076 138.899 87.149  1.00 54.84  ? 533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.950 138.619 84.894  1.00 53.95  ? 534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.446 137.348 84.394  1.00 54.46  ? 534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.179 137.575 83.582  1.00 55.43  ? 534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.331 138.393 83.951  1.00 56.33  ? 534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.158 136.375 85.545  1.00 53.89  ? 534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.284 136.332 86.431  1.00 54.16  ? 534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.892 134.975 85.011  1.00 56.03  ? 534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.056 136.847 82.475  1.00 59.14  ? 535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.863 136.895 81.642  1.00 58.47  ? 535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.899 135.800 82.075  1.00 61.54  ? 535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.271 134.624 82.135  1.00 58.33  ? 535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.224 136.732 80.165  1.00 58.62  ? 535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.028 136.911 79.250  1.00 63.60  ? 535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.050 137.564 79.668  1.00 62.50  ? 535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.067 136.395 78.113  1.00 64.67  ? 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.661 136.190 82.377  1.00 52.27  ? 536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.644 135.264 82.854  1.00 49.10  ? 536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.623 134.915 81.777  1.00 51.89  ? 536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.530 134.438 82.099  1.00 56.40  ? 536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.948 135.839 84.087  1.00 45.15  ? 536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.859 136.008 85.268  1.00 43.93  ? 536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.110 134.949 86.122  1.00 44.50  ? 536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 152.473 137.222 85.520  1.00 50.26  ? 536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 152.951 135.099 87.207  1.00 46.60  ? 536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.314 137.377 86.603  1.00 54.02  ? 536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.552 136.314 87.447  1.00 50.30  ? 536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.955 135.149 80.511  1.00 53.66  ? 537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.102 134.707 79.424  1.00 54.33  ? 537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.066 133.179 79.383  1.00 58.32  ? 537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.016 132.519 79.812  1.00 56.93  ? 537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.607 135.255 78.091  1.00 49.65  ? 537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.940 136.459 77.751  1.00 55.49  ? 537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.972 132.594 78.894  1.00 56.21  ? 538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.858 131.132 78.900  1.00 48.90  ? 538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.962 130.470 78.090  1.00 56.49  ? 538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.352 130.948 77.023  1.00 57.91  ? 538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.480 130.883 78.276  1.00 51.92  ? 538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.730 132.148 78.497  1.00 53.20  ? 538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.752 133.235 78.377  1.00 54.54  ? 538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.467 129.356 78.615  1.00 60.01  ? 539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.474 128.556 77.934  1.00 57.30  ? 539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.870 127.432 77.104  1.00 60.31  ? 539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.612 126.708 76.433  1.00 61.85  ? 539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.461 127.970 78.948  1.00 57.22  ? 539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 152.776 128.887 80.118  1.00 57.55  ? 539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.934 129.817 79.797  1.00 60.37  ? 539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 153.855 131.098 80.613  1.00 62.09  ? 539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 154.165 132.302 79.794  1.00 59.31  ? 539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.551 127.269 77.136  1.00 58.68  ? 540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 148.861 126.225 76.393  1.00 59.13  ? 540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.953 126.857 75.349  1.00 60.72  ? 540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.263 127.843 75.628  1.00 59.19  ? 540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.043 125.329 77.328  1.00 57.11  ? 540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 148.887 124.469 78.240  1.00 59.38  ? 540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.400 123.256 77.803  1.00 60.25  ? 540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.174 124.872 79.536  1.00 60.84  ? 540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.173 122.467 78.633  1.00 58.93  ? 540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.946 124.091 80.373  1.00 60.71  ? 540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.442 122.890 79.916  1.00 59.29  ? 540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.212 122.108 80.745  1.00 60.27  ? 540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.965 126.288 74.141  1.00 61.29  ? 541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.115 126.800 73.072  1.00 60.55  ? 541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.640 126.655 73.426  1.00 61.43  ? 541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.833 127.545 73.133  1.00 61.02  ? 541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.436 126.078 71.761  1.00 61.14  ? 541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 146.437 126.316 70.638  1.00 62.34  ? 541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 145.370 125.240 70.561  1.00 65.81  ? 541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 145.731 124.045 70.524  1.00 59.78  ? 541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 144.171 125.590 70.537  1.00 67.72  ? 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.270 125.537 74.054  1.00 58.89  ? 542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 143.887 125.347 74.478  1.00 57.44  ? 542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.474 126.402 75.496  1.00 57.53  ? 542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.366 126.949 75.423  1.00 55.85  ? 542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.707 123.942 75.054  1.00 58.70  ? 542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.477 123.779 75.933  1.00 60.09  ? 542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.513 122.464 76.693  1.00 59.58  ? 542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 141.124 121.864 76.822  1.00 59.04  ? 542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 140.063 122.908 76.775  1.00 58.01  ? 542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.354 126.705 76.451  1.00 57.68  ? 543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.047 127.720 77.453  1.00 52.13  ? 543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.034 129.109 76.826  1.00 51.95  ? 543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.182 129.943 77.151  1.00 52.34  ? 543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.045 127.630 78.621  1.00 51.29  ? 543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.922 126.275 79.318  1.00 54.97  ? 543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.816 128.761 79.605  1.00 51.95  ? 543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.507 125.917 79.708  1.00 52.11  ? 543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.980 129.381 75.922  1.00 54.03  ? 544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.029 130.687 75.273  1.00 53.88  ? 544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.774 130.956 74.453  1.00 54.40  ? 544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.373 132.115 74.298  1.00 55.25  ? 544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.271 130.789 74.390  1.00 53.89  ? 544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.144 129.906 73.921  1.00 58.79  ? 545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.902 130.090 73.179  1.00 60.82  ? 545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.750 130.471 74.099  1.00 61.25  ? 545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.791 131.113 73.657  1.00 63.10  ? 545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.562 128.820 72.401  1.00 62.29  ? 545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.491 128.591 71.226  1.00 64.75  ? 545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.173 129.510 70.772  1.00 62.73  ? 545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.523 127.361 70.727  1.00 62.58  ? 545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.821 130.078 75.374  1.00 54.32  ? 546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.779 130.451 76.324  1.00 53.50  ? 546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.752 131.954 76.561  1.00 57.42  ? 546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.684 132.524 76.814  1.00 59.72  ? 546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.985 129.710 77.646  1.00 50.10  ? 546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.310 128.351 77.850  1.00 54.20  ? 546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 139.331 127.503 76.588  1.00 56.16  ? 546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 139.968 127.615 79.002  1.00 52.60  ? 546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.908 132.610 76.481  1.00 53.07  ? 547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.022 134.045 76.688  1.00 49.44  ? 547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.935 134.834 75.389  1.00 56.60  ? 547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.162 136.049 75.399  1.00 60.21  ? 547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.334 134.369 77.406  1.00 49.03  ? 547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.365 133.933 78.842  1.00 50.53  ? 547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.926 134.778 79.846  1.00 53.90  ? 547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.830 132.677 79.187  1.00 50.79  ? 547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.956 134.380 81.167  1.00 46.68  ? 547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.858 132.273 80.507  1.00 49.50  ? 547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.420 133.126 81.497  1.00 46.81  ? 547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.627 134.173 74.275  1.00 65.66  ? 548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.515 134.865 72.998  1.00 64.60  ? 548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.416 135.918 73.054  1.00 66.86  ? 548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 138.349 135.697 73.634  1.00 67.31  ? 548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.228 133.865 71.877  1.00 65.90  ? 548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 140.612 134.357 70.493  1.00 69.13  ? 548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 139.423 134.452 69.558  1.00 72.30  ? 548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 139.634 134.476 68.327  1.00 69.79  ? 548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 138.278 134.503 70.054  1.00 69.47  ? 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.683 137.070 72.445  1.00 64.44  ? 549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.775 138.194 72.528  1.00 66.47  ? 549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.945 139.052 73.759  1.00 66.97  ? 549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.165 139.991 73.953  1.00 65.27  ? 549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.936 138.758 74.596  1.00 66.50  ? 550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.216 139.526 75.800  1.00 60.87  ? 550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.699 139.855 75.835  1.00 66.04  ? 550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.538 138.972 75.627  1.00 63.29  ? 550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.813 138.751 77.057  1.00 57.89  ? 550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 138.550 139.262 77.720  1.00 63.37  ? 550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.275 138.493 79.323  1.00 76.27  ? 550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.516 136.769 78.906  1.00 60.98  ? 550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.020 141.118 76.098  1.00 68.85  ? 551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.409 141.569 76.127  1.00 62.32  ? 551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.056 141.082 77.417  1.00 59.40  ? 551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.780 141.600 78.501  1.00 58.20  ? 551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.490 143.086 76.011  1.00 60.07  ? 551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.840 143.642 76.337  1.00 65.07  ? 551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.973 143.312 75.626  1.00 64.51  ? 551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.241 144.502 77.304  1.00 64.23  ? 551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.012 143.945 76.136  1.00 64.12  ? 551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.596 144.674 77.157  1.00 65.38  ? 551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 144.920 140.080 77.302  1.00 54.39  ? 552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.671 139.568 78.443  1.00 55.27  ? 552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.782 140.559 78.766  1.00 54.53  ? 552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.593 140.883 77.885  1.00 55.67  ? 552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.236 138.169 78.158  1.00 56.60  ? 552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.118 137.228 77.708  1.00 57.66  ? 552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 146.929 137.614 79.388  1.00 51.37  ? 552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.612 135.882 77.243  1.00 55.53  ? 552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.850 141.078 79.992  1.00 57.23  ? 553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 147.916 142.028 80.333  1.00 54.42  ? 553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.293 141.408 80.151  1.00 54.93  ? 553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.525 140.246 80.491  1.00 55.93  ? 553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.637 142.361 81.802  1.00 50.56  ? 553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.191 142.048 81.994  1.00 44.71  ? 553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 145.907 140.881 81.104  1.00 51.74  ? 553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.209 142.199 79.608  1.00 60.02  ? 554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.564 141.760 79.334  1.00 59.22  ? 554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.523 142.377 80.348  1.00 60.63  ? 554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.115 143.064 81.290  1.00 63.51  ? 554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 151.952 142.119 77.899  1.00 57.21  ? 554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 151.850 143.536 77.715  1.00 55.90  ? 554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.036 141.417 76.909  1.00 56.45  ? 554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.819 142.120 80.163  1.00 57.27  ? 555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.826 142.725 81.027  1.00 55.13  ? 555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.828 144.243 80.890  1.00 60.53  ? 555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 154.921 144.966 81.889  1.00 58.04  ? 555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.203 142.142 80.701  1.00 59.69  ? 555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.358 140.881 81.365  1.00 58.05  ? 555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 157.313 143.079 81.143  1.00 60.76  ? 555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.710 144.745 79.659  1.00 63.49  ? 556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.655 146.189 79.450  1.00 61.43  ? 556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.389 146.786 80.052  1.00 63.95  ? 556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.425 147.883 80.622  1.00 64.21  ? 556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.769 146.505 77.955  1.00 59.92  ? 556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 153.702 145.870 77.068  1.00 63.59  ? 556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 152.520 146.786 76.796  1.00 67.77  ? 556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 152.353 147.791 77.518  1.00 70.57  ? 556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 151.754 146.497 75.853  1.00 61.66  ? 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.260 146.082 79.939  1.00 57.54  ? 557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.028 146.557 80.563  1.00 55.26  ? 557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.176 146.620 82.078  1.00 56.74  ? 557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.694 147.560 82.720  1.00 58.32  ? 557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.858 145.655 80.174  1.00 56.84  ? 557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.454 145.820 78.724  1.00 60.91  ? 557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.874 146.814 78.098  1.00 61.34  ? 557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 148.716 144.954 78.210  1.00 61.82  ? 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.847 145.628 82.665  1.00 48.37  ? 558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.100 145.663 84.099  1.00 41.99  ? 558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.046 146.795 84.477  1.00 47.18  ? 558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 152.901 147.381 85.553  1.00 52.59  ? 558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.654 144.320 84.567  1.00 49.69  ? 558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.592 143.377 85.027  1.00 48.43  ? 558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.145 142.265 84.378  1.00 46.92  ? 558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.835 143.466 86.239  1.00 47.90  ? 558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.160 141.652 85.114  1.00 46.11  ? 558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.952 142.370 86.262  1.00 43.52  ? 558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.824 144.362 87.312  1.00 51.92  ? 558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.066 142.148 87.313  1.00 43.47  ? 558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.944 144.140 88.353  1.00 47.46  ? 558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.078 143.043 88.345  1.00 46.53  ? 558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.016 147.117 83.617  1.00 55.71  ? 559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 154.877 148.268 83.880  1.00 56.17  ? 559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.082 149.568 83.860  1.00 53.40  ? 559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.284 150.444 84.712  1.00 56.58  ? 559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.015 148.321 82.861  1.00 55.16  ? 559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.184 147.408 83.183  1.00 54.26  ? 559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.221 147.431 82.074  1.00 56.16  ? 559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.014 146.137 82.030  1.00 58.45  ? 559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.481 146.380 82.068  1.00 58.09  ? 559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.177 149.714 82.889  1.00 48.41  ? 560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.321 150.898 82.857  1.00 49.44  ? 560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.435 150.967 84.094  1.00 52.94  ? 560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.228 152.048 84.655  1.00 53.45  ? 560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.468 150.921 81.587  1.00 53.36  ? 560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.230 150.651 80.304  1.00 58.47  ? 560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 153.099 151.834 79.918  1.00 60.20  ? 560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 154.288 151.393 79.080  1.00 57.76  ? 560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 155.561 151.451 79.851  1.00 54.33  ? 560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 150.898 149.827 84.531  1.00 49.46  ? 561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.085 149.815 85.743  1.00 43.34  ? 561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 150.911 150.185 86.969  1.00 45.96  ? 561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.428 150.895 87.857  1.00 50.11  ? 561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.433 148.447 85.936  1.00 47.24  ? 561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.553 148.365 87.185  1.00 45.62  ? 561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.431 149.381 87.094  1.00 45.22  ? 561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.002 146.969 87.385  1.00 45.34  ? 561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.152 149.702 87.042  1.00 42.08  ? 562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.027 150.056 88.155  1.00 42.97  ? 562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.311 151.551 88.175  1.00 45.45  ? 562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.287 152.181 89.238  1.00 48.50  ? 562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.329 149.260 88.061  1.00 45.41  ? 562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.404 149.692 89.039  1.00 45.24  ? 562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.714 148.980 88.748  1.00 45.46  ? 562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 157.815 149.436 89.686  1.00 47.21  ? 562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 158.921 148.443 89.759  1.00 50.20  ? 562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.578 152.137 87.005  1.00 50.23  ? 563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 153.786 153.582 86.935  1.00 47.37  ? 563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.527 154.342 87.337  1.00 51.47  ? 563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 152.598 155.351 88.048  1.00 54.21  ? 563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.228 153.979 85.528  1.00 42.90  ? 563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.362 153.867 86.888  1.00 47.79  ? 564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.102 154.511 87.238  1.00 42.92  ? 564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 149.859 154.461 88.741  1.00 48.08  ? 564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.395 155.439 89.337  1.00 51.87  ? 564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 148.956 153.838 86.480  1.00 47.27  ? 564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 147.653 154.579 86.550  1.00 47.04  ? 564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.386 155.621 85.680  1.00 51.09  ? 564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 146.689 154.223 87.476  1.00 47.04  ? 564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.185 156.298 85.738  1.00 53.73  ? 564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.488 154.898 87.540  1.00 49.38  ? 564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.235 155.937 86.670  1.00 54.59  ? 564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.168 153.327 89.370  1.00 46.65  ? 565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.007 153.197 90.814  1.00 43.04  ? 565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 150.992 154.098 91.547  1.00 47.66  ? 565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 150.644 154.732 92.550  1.00 53.70  ? 565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.162 151.723 91.231  1.00 42.58  ? 565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.353 151.604 92.734  1.00 42.44  ? 565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 148.953 150.925 90.785  1.00 48.48  ? 565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.232 154.173 91.061  1.00 55.07  ? 566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.221 155.035 91.701  1.00 52.82  ? 566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 152.801 156.498 91.635  1.00 52.58  ? 566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 152.957 157.241 92.610  1.00 55.31  ? 566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 154.589 154.837 91.050  1.00 48.81  ? 566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.264 156.929 90.492  1.00 55.47  ? 567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 151.856 158.324 90.351  1.00 56.91  ? 567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.576 158.634 91.120  1.00 55.82  ? 567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.483 159.683 91.767  1.00 58.14  ? 567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 151.687 158.675 88.871  1.00 54.08  ? 567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.915 159.313 88.237  1.00 59.80  ? 567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 154.203 158.586 88.568  1.00 62.56  ? 567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 154.380 157.439 88.107  1.00 55.90  ? 567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 155.041 159.161 89.294  1.00 58.65  ? 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 149.583 157.745 91.069  1.00 54.74  ? 568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.256 158.044 91.589  1.00 53.36  ? 568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 147.916 157.325 92.886  1.00 49.35  ? 568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 146.943 157.706 93.544  1.00 56.22  ? 568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.192 157.709 90.534  1.00 49.11  ? 568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.176 158.656 89.377  1.00 51.81  ? 568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 147.194 160.025 89.537  1.00 54.58  ? 568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.162 158.433 88.043  1.00 52.80  ? 568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 147.179 160.604 88.350  1.00 56.11  ? 568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.160 159.661 87.426  1.00 53.81  ? 568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 148.674 156.308 93.272  1.00 41.72  ? 569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.386 155.598 94.498  1.00 40.60  ? 569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.396 154.466 94.301  1.00 39.88  ? 569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 146.993 154.123 93.188  1.00 50.17  ? 569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.005 153.871 95.426  1.00 31.84  ? 570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.077 152.748 95.434  1.00 34.56  ? 570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.068 152.954 96.552  1.00 36.52  ? 570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.452 153.201 97.698  1.00 48.33  ? 570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 146.828 151.424 95.612  1.00 37.10  ? 570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.172 150.745 94.297  1.00 37.42  ? 570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.266 148.954 94.422  1.00 53.38  ? 570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 145.872 148.625 95.484  1.00 34.63  ? 570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 143.781 152.856 96.216  1.00 26.83  ? 571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.731 153.188 97.174  1.00 28.12  ? 571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.515 152.098 98.215  1.00 34.41  ? 571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.169 152.406 99.361  1.00 40.42  ? 571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.420 153.463 96.439  1.00 33.35  ? 571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.351 154.081 97.311  1.00 33.63  ? 571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.422 155.414 97.687  1.00 38.21  ? 571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.274 153.331 97.760  1.00 30.90  ? 571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.449 155.984 98.482  1.00 39.06  ? 571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.297 153.892 98.557  1.00 33.12  ? 571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.389 155.219 98.914  1.00 42.68  ? 571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.417 155.782 99.708  1.00 44.61  ? 571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.702 150.834 97.848  1.00 37.45  ? 572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.433 149.710 98.735  1.00 25.80  ? 572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.744 149.094 99.195  1.00 32.07  ? 572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.617 148.797 98.374  1.00 40.61  ? 572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.579 148.648 98.039  1.00 24.66  ? 572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.356 149.193 97.370  1.00 29.05  ? 572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.330 149.536 96.037  1.00 32.72  ? 572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.117 149.450 97.850  1.00 27.16  ? 572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.128 149.984 95.723  1.00 31.01  ? 572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.373 149.941 96.805  1.00 34.42  ? 572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 143.880 148.905 100.508 1.00 26.98  ? 573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.033 148.178 101.025 1.00 24.76  ? 573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.018 146.732 100.550 1.00 33.92  ? 573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.060 146.178 100.182 1.00 36.98  ? 573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.054 148.245 102.550 1.00 27.18  ? 573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 143.782 147.930 103.084 1.00 36.29  ? 573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.843 146.109 100.549 1.00 30.04  ? 574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.666 144.743 100.085 1.00 20.58  ? 574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.460 144.687 99.161  1.00 15.45  ? 574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.476 145.405 99.357  1.00 21.57  ? 574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.489 143.776 101.260 1.00 21.19  ? 574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.573 143.905 102.303 1.00 18.85  ? 574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.458 144.815 103.344 1.00 18.38  ? 574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.715 143.122 102.243 1.00 20.76  ? 574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.448 144.943 104.293 1.00 19.42  ? 574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.709 143.240 103.191 1.00 19.71  ? 574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.571 144.152 104.212 1.00 23.50  ? 574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.559 144.272 105.158 1.00 33.02  ? 574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.547 143.837 98.149  1.00 14.94  ? 575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.498 143.792 97.137  1.00 18.90  ? 575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 140.933 142.401 96.908  1.00 29.71  ? 575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.726 142.265 96.694  1.00 42.75  ? 575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.031 144.338 95.808  1.00 26.88  ? 575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.542 145.759 95.866  1.00 21.58  ? 575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.625 145.966 94.830  1.00 27.32  ? 575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 144.851 145.262 95.185  1.00 24.51  ? 575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.266 144.141 94.610  1.00 22.68  ? 575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.573 143.562 93.645  1.00 26.27  ? 575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.405 143.588 95.016  1.00 25.20  ? 575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.767 141.366 96.942  1.00 20.15  ? 576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.374 140.029 96.519  1.00 14.35  ? 576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.489 139.058 97.682  1.00 11.89  ? 576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.534 138.985 98.333  1.00 37.09  ? 576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.244 139.546 95.358  1.00 17.08  ? 576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.397 140.473 94.154  1.00 17.62  ? 576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.336 139.850 93.142  1.00 22.33  ? 576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.052 140.767 93.521  1.00 20.29  ? 576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.418 138.312 97.932  1.00 12.50  ? 577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.448 137.202 98.874  1.00 10.50  ? 577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.339 136.240 98.487  1.00 31.78  ? 577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.204 136.662 98.252  1.00 35.63  ? 577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.293 137.682 100.323 1.00 19.65  ? 577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.618 138.065 100.862 1.00 34.40  ? 577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.671 134.958 98.401  1.00 31.41  ? 578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.760 133.944 97.888  1.00 20.64  ? 578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.079 133.288 99.083  1.00 24.84  ? 578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.662 132.445 99.769  1.00 27.87  ? 578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.487 132.930 97.003  1.00 17.25  ? 578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.050 133.630 95.767  1.00 15.06  ? 578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.548 131.825 96.580  1.00 21.69  ? 578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.797 132.717 94.843  1.00 25.43  ? 578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.835 133.688 99.330  1.00 32.25  ? 579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.005 133.128 100.380 1.00 20.17  ? 579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.513 131.738 99.983  1.00 38.31  ? 579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.605 131.349 98.818  1.00 50.08  ? 579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 134.825 134.056 100.653 1.00 25.24  ? 579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.016 130.950 100.943 1.00 38.23  ? 580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.470 129.629 100.591 1.00 33.73  ? 580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.262 129.674 99.662  1.00 37.60  ? 580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 133.003 128.666 98.992  1.00 46.73  ? 580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.103 129.021 101.953 1.00 33.95  ? 580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.058 130.167 102.899 1.00 35.84  ? 580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.069 131.143 102.401 1.00 37.39  ? 580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.525 130.790 99.600  1.00 31.62  ? 581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.395 130.934 98.680  1.00 41.97  ? 581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.406 129.785 98.817  1.00 42.93  ? 581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.292 128.951 97.913  1.00 45.35  ? 581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.856 131.042 97.223  1.00 42.01  ? 581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 132.145 129.736 96.711  1.00 42.32  ? 581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 133.081 131.935 97.098  1.00 40.23  ? 581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.690 129.727 99.935  1.00 40.88  ? 582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.904 128.556 100.263 1.00 45.20  ? 582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.501 128.602 99.696  1.00 50.02  ? 582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.321 128.412 98.490  1.00 55.45  ? 582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.498 128.832 100.544 1.00 48.83  ? 583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.105 128.733 100.127 1.00 52.47  ? 583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.757 129.631 98.945  1.00 48.35  ? 583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 123.816 129.315 98.210  1.00 46.73  ? 583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.183 129.061 101.304 1.00 57.24  ? 583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 124.716 128.568 102.520 1.00 53.92  ? 583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.483 130.733 98.739  1.00 44.89  ? 584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.237 131.583 97.579  1.00 44.18  ? 584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.768 130.983 96.286  1.00 43.81  ? 584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.408 131.457 95.202  1.00 48.54  ? 584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 125.845 132.985 97.794  1.00 47.53  ? 584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 125.121 134.022 96.934  1.00 41.65  ? 584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 127.335 132.979 97.487  1.00 46.46  ? 584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 123.819 134.511 97.511  1.00 46.39  ? 584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.609 129.949 96.365  1.00 41.33  ? 585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.087 129.299 95.149  1.00 37.26  ? 585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.964 128.558 94.440  1.00 42.76  ? 585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.993 128.416 93.213  1.00 46.87  ? 585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.234 128.344 95.471  1.00 37.31  ? 585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.819 127.343 96.385  1.00 35.85  ? 585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.977 128.069 95.193  1.00 50.08  ? 586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.811 127.447 94.575  1.00 39.24  ? 586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.058 128.449 93.712  1.00 37.77  ? 586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.691 128.151 92.570  1.00 48.40  ? 586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.886 126.882 95.652  1.00 44.17  ? 586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.497 125.783 96.485  1.00 44.42  ? 586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.661 124.508 95.971  1.00 47.47  ? 586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.904 126.022 97.790  1.00 48.37  ? 586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.216 123.501 96.730  1.00 51.97  ? 586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.462 125.020 98.557  1.00 49.90  ? 586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.616 123.761 98.022  1.00 52.52  ? 586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.171 122.757 98.781  1.00 50.06  ? 586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.839 129.656 94.240  1.00 39.05  ? 587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.043 130.659 93.539  1.00 37.69  ? 587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.711 131.058 92.231  1.00 43.46  ? 587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.039 131.293 91.219  1.00 44.39  ? 587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.806 131.878 94.449  1.00 36.23  ? 587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 120.768 132.795 93.840  1.00 41.13  ? 587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.381 131.425 95.835  1.00 41.19  ? 587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.038 131.136 92.226  1.00 48.46  ? 588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.780 131.466 91.017  1.00 44.67  ? 588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.990 130.266 90.108  1.00 43.97  ? 588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.585 130.425 89.036  1.00 49.71  ? 588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.137 132.073 91.377  1.00 33.93  ? 588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.057 133.486 91.910  1.00 36.67  ? 588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.272 134.523 90.828  1.00 44.23  ? 588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.142 134.373 89.972  1.00 38.48  ? 588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.475 135.584 90.859  1.00 53.53  ? 588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.511 129.087 90.501  1.00 43.26  ? 589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.756 127.845 89.773  1.00 45.49  ? 589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.250 127.675 89.513  1.00 46.13  ? 589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.722 127.666 88.375  1.00 49.16  ? 589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.952 127.799 88.471  1.00 46.89  ? 589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 122.579 127.563 88.732  1.00 52.63  ? 589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.994 127.549 90.608  1.00 42.71  ? 590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.445 127.516 90.555  1.00 41.02  ? 590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.978 126.538 91.587  1.00 45.19  ? 590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.318 126.226 92.581  1.00 46.06  ? 590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.043 128.904 90.805  1.00 39.33  ? 590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.353 129.083 92.175  1.00 42.53  ? 590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.189 126.052 91.334  1.00 37.84  ? 591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.910 125.293 92.340  1.00 41.74  ? 591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.450 126.238 93.410  1.00 36.31  ? 591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.750 127.404 93.145  1.00 34.44  ? 591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.050 124.502 91.702  1.00 45.25  ? 591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.123 125.390 91.367  1.00 48.33  ? 591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.564 123.810 90.441  1.00 32.44  ? 591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.566 125.724 94.629  1.00 36.87  ? 592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.928 126.569 95.758  1.00 40.13  ? 592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.397 126.964 95.685  1.00 44.57  ? 592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.284 126.105 95.697  1.00 50.09  ? 592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.639 125.848 97.072  1.00 42.62  ? 592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.646 128.268 95.608  1.00 41.45  ? 593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.992 128.851 95.673  1.00 29.47  ? 593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.820 128.319 94.503  1.00 28.69  ? 593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.274 127.926 93.463  1.00 40.64  ? 593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.588 128.581 97.044  1.00 39.81  ? 593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.768 129.331 97.254  1.00 37.31  ? 593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.144 128.314 94.658  1.00 33.33  ? 594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.039 127.668 93.711  1.00 28.44  ? 594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.318 126.223 94.105  1.00 35.43  ? 594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.138 125.554 93.470  1.00 37.18  ? 594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.348 128.459 93.563  1.00 31.02  ? 594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.076 129.823 92.950  1.00 26.52  ? 594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.033 128.608 94.912  1.00 35.26  ? 594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.651 125.730 95.145  1.00 37.79  ? 595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.828 124.357 95.581  1.00 35.79  ? 595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.238 123.392 94.555  1.00 46.88  ? 595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.284 123.729 93.848  1.00 51.45  ? 595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.151 124.136 96.931  1.00 38.47  ? 595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 137.970 124.470 98.184  1.00 44.15  ? 595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.750 124.171 98.129  1.00 53.95  ? 595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 140.360 125.726 97.481  1.00 39.89  ? 595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.787 122.185 94.452  1.00 46.81  ? 596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.136 121.148 93.648  1.00 39.88  ? 596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.858 120.663 94.315  1.00 48.37  ? 596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.666 120.788 95.527  1.00 55.08  ? 596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.189 120.040 93.576  1.00 43.59  ? 596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.033 120.245 94.786  1.00 43.86  ? 596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.057 121.724 95.037  1.00 45.75  ? 596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.970 120.102 93.495  1.00 50.12  ? 597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.665 119.676 93.985  1.00 49.73  ? 597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.819 118.456 94.884  1.00 51.21  ? 597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.579 117.526 94.583  1.00 53.76  ? 597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.714 119.391 92.810  1.00 48.71  ? 597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.259 118.269 91.925  1.00 46.58  ? 597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.506 120.649 91.987  1.00 49.80  ? 597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.223 117.652 91.023  1.00 46.60  ? 597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.103 118.465 96.010  1.00 59.60  ? 598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.173 117.341 96.940  1.00 60.53  ? 598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.501 116.104 96.358  1.00 62.81  ? 598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.056 115.001 96.407  1.00 66.58  ? 598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.532 117.726 98.273  1.00 58.98  ? 598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.443 118.514 99.196  1.00 60.68  ? 598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.581 119.159 100.642 1.00 77.83  ? 598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 132.450 120.892 100.214 1.00 61.42  ? 598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.304 116.270 95.802  1.00 56.29  ? 599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.555 115.172 95.210  1.00 60.39  ? 599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.964 115.640 93.890  1.00 61.57  ? 599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.635 116.816 93.726  1.00 63.50  ? 599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.449 114.680 96.153  1.00 58.55  ? 599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 128.630 115.797 96.780  1.00 60.57  ? 599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.180 115.473 98.192  1.00 64.46  ? 599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.576 114.400 98.396  1.00 62.73  ? 599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 128.430 116.295 99.098  1.00 62.77  ? 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.851 114.711 92.939  1.00 59.23  ? 600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.300 115.069 91.635  1.00 52.25  ? 600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.830 115.457 91.740  1.00 52.48  ? 600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.390 116.416 91.096  1.00 59.57  ? 600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.491 113.916 90.654  1.00 53.88  ? 600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.895 113.834 90.098  1.00 51.09  ? 600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.988 112.831 88.974  1.00 53.47  ? 600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.330 112.764 88.411  1.00 52.64  ? 600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.304 112.003 88.890  1.00 54.21  ? 600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.130 111.255 89.967  1.00 57.09  ? 600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.483 111.996 88.275  1.00 49.61  ? 600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.059 114.725 92.537  1.00 59.33  ? 601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.652 115.026 92.778  1.00 62.32  ? 601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.452 115.139 94.282  1.00 60.88  ? 601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.678 114.168 95.015  1.00 61.71  ? 601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.720 113.958 92.184  1.00 63.86  ? 601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.976 113.803 90.684  1.00 63.13  ? 601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.268 114.319 92.444  1.00 61.32  ? 601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.198 112.681 90.043  1.00 61.06  ? 601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.032 116.315 94.739  1.00 68.13  ? 602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.864 116.559 96.164  1.00 71.54  ? 602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.541 115.987 96.653  1.00 74.44  ? 602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.484 116.258 96.076  1.00 76.68  ? 602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 124.933 118.055 96.463  1.00 71.79  ? 602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 126.204 118.488 97.169  1.00 73.99  ? 602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 126.387 119.990 97.167  1.00 75.94  ? 602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 125.368 120.706 97.104  1.00 72.95  ? 602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 127.544 120.454 97.240  1.00 73.90  ? 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.604 115.198 97.720  1.00 79.01  ? 603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.426 114.603 98.342  1.00 78.69  ? 603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.077 115.426 99.579  1.00 80.15  ? 603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.778 115.360 100.593 1.00 81.15  ? 603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.693 113.139 98.688  1.00 81.24  ? 603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 121.487 112.226 98.566  1.00 83.00  ? 603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.676 110.919 99.309  1.00 82.32  ? 603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 122.347 110.018 98.762  1.00 80.14  ? 603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.163 110.790 100.439 1.00 80.76  ? 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.001 116.204 99.488  1.00 81.18  ? 604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.601 117.137 100.533 1.00 82.20  ? 604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.221 116.777 101.063 1.00 84.32  ? 604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.343 116.363 100.297 1.00 84.12  ? 604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.608 118.578 100.013 1.00 82.86  ? 604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.935 119.008 99.418  1.00 85.85  ? 604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.771 119.735 100.461 1.00 82.59  ? 604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.323 118.828 101.461 1.00 84.86  ? 604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 124.502 118.229 101.367 1.00 85.24  ? 604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.292 118.417 100.324 1.00 81.97  ? 604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 124.900 117.423 102.348 1.00 84.05  ? 604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.037 116.936 102.372 1.00 91.38  ? 605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.776 116.651 103.044 1.00 91.43  ? 605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.104 117.966 103.414 1.00 89.97  ? 605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.714 118.813 104.076 1.00 88.10  ? 605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 118.001 115.801 104.296 1.00 92.04  ? 605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.613 114.560 103.929 1.00 91.60  ? 605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.680 115.525 104.997 1.00 91.54  ? 605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.855 118.136 102.988 1.00 89.19  ? 606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.072 119.328 103.299 1.00 90.58  ? 606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.699 118.878 103.777 1.00 90.91  ? 606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.893 118.384 102.982 1.00 88.26  ? 606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 114.960 120.244 102.081 1.00 89.41  ? 606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.288 120.824 101.662 1.00 89.16  ? 606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 116.973 121.710 102.482 1.00 88.24  ? 606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.864 120.476 100.449 1.00 87.28  ? 606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.192 122.235 102.103 1.00 86.43  ? 606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.080 120.996 100.061 1.00 89.75  ? 606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.739 121.874 100.892 1.00 89.38  ? 606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.953 122.391 100.506 1.00 86.40  ? 606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.431 119.055 105.065 1.00 97.44  ? 607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.177 118.581 105.628 1.00 97.29  ? 607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.095 117.073 105.552 1.00 99.50  ? 607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 112.990 116.367 106.022 1.00 98.51  ? 607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.014 116.572 104.958 1.00 100.95 ? 608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 110.809 115.141 104.767 1.00 101.78 ? 608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.188 114.683 103.365 1.00 100.87 ? 608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.845 113.561 102.974 1.00 99.81  ? 608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.355 114.770 105.066 1.00 101.07 ? 608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.204 113.340 105.549 1.00 101.78 ? 608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 108.841 112.448 104.782 1.00 100.05 ? 608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 109.481 113.114 106.828 1.00 100.07 ? 608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.885 115.518 102.603 1.00 95.48  ? 609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.217 115.235 101.216 1.00 93.84  ? 609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.724 115.104 101.040 1.00 96.54  ? 609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.509 115.709 101.775 1.00 95.04  ? 609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.688 116.334 100.294 1.00 93.56  ? 609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.465 117.513 100.421 1.00 94.60  ? 609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 114.117 114.306 100.054 1.00 88.28  ? 610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.519 114.106 99.700  1.00 86.64  ? 610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.748 114.794 98.358  1.00 86.59  ? 610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 115.180 114.389 97.340  1.00 84.88  ? 610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.860 112.621 99.640  1.00 86.38  ? 610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 117.288 112.311 100.029 1.00 87.85  ? 610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 117.479 112.532 101.519 1.00 89.72  ? 610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 118.454 111.533 102.112 1.00 86.90  ? 610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 119.863 111.961 101.910 1.00 84.73  ? 610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.573 115.835 98.362  1.00 84.47  ? 611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.807 116.637 97.169  1.00 80.09  ? 611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.202 116.380 96.614  1.00 79.08  ? 611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.164 116.213 97.367  1.00 81.85  ? 611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.637 118.124 97.477  1.00 80.68  ? 611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 115.585 118.294 98.435  1.00 82.63  ? 611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.282 118.881 96.215  1.00 80.23  ? 611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.303 116.355 95.288  1.00 74.05  ? 612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.558 116.091 94.600  1.00 74.41  ? 612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.979 117.307 93.786  1.00 76.29  ? 612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.177 117.878 93.042  1.00 77.50  ? 612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.427 114.874 93.685  1.00 74.93  ? 612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.904 113.644 94.385  1.00 77.59  ? 612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 117.614 113.190 94.155  1.00 76.32  ? 612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 119.696 112.942 95.284  1.00 75.95  ? 612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 117.127 112.068 94.793  1.00 77.99  ? 612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 119.217 111.819 95.927  1.00 77.71  ? 612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 117.933 111.386 95.679  1.00 80.47  ? 612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.450 110.268 96.317  1.00 80.83  ? 612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.242 117.698 93.932  1.00 66.19  ? 613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.809 118.826 93.192  1.00 62.21  ? 613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.060 118.402 92.438  1.00 62.75  ? 613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.158 118.367 93.021  1.00 64.41  ? 613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.132 119.987 94.130  1.00 64.73  ? 613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.807 121.146 93.431  1.00 61.66  ? 613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.225 121.755 92.328  1.00 58.66  ? 613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.032 121.625 93.870  1.00 61.69  ? 613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.838 122.813 91.690  1.00 58.78  ? 613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.654 122.680 93.238  1.00 64.71  ? 613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.053 123.271 92.149  1.00 64.89  ? 613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.672 124.323 91.516  1.00 64.53  ? 613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.952 118.060 91.157  1.00 59.04  ? 614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.160 117.895 90.345  1.00 58.87  ? 614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.886 119.222 90.196  1.00 61.32  ? 614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.262 120.283 90.118  1.00 62.79  ? 614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.625 117.393 88.998  1.00 57.32  ? 614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.214 116.962 89.262  1.00 60.66  ? 614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.726 117.811 90.386  1.00 59.33  ? 614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.213 119.157 90.164  1.00 57.39  ? 615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.997 120.360 89.943  1.00 58.91  ? 615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.709 120.930 88.555  1.00 58.68  ? 615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.420 120.183 87.617  1.00 55.77  ? 615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.485 120.067 90.123  1.00 53.90  ? 615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.802 119.449 91.472  1.00 50.30  ? 615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.372 120.623 92.776  1.00 59.61  ? 615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.368 119.584 94.231  1.00 58.29  ? 615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.749 122.254 88.409  1.00 54.84  ? 616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.303 122.875 87.155  1.00 54.67  ? 616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.100 122.385 85.957  1.00 52.68  ? 616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.320 122.222 86.023  1.00 53.70  ? 616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.528 124.370 87.402  1.00 52.76  ? 616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.555 124.503 88.883  1.00 54.02  ? 616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.173 123.256 89.399  1.00 47.00  ? 616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.393 122.152 84.856  1.00 50.57  ? 617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 127.026 121.673 83.646  1.00 51.63  ? 617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.404 120.213 83.660  1.00 55.18  ? 617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 128.042 119.747 82.711  1.00 56.87  ? 617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 127.037 119.475 84.703  1.00 52.60  ? 618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.353 118.056 84.762  1.00 50.78  ? 618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.517 117.286 83.748  1.00 51.46  ? 618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.308 117.501 83.623  1.00 51.34  ? 618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.112 117.509 86.167  1.00 49.39  ? 618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.451 116.037 86.397  1.00 51.49  ? 618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.916 115.775 86.102  1.00 52.17  ? 618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.108 115.628 87.818  1.00 50.75  ? 618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.170 116.385 83.027  1.00 60.75  ? 619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.516 115.577 82.007  1.00 61.30  ? 619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.397 114.364 81.734  1.00 63.26  ? 619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.366 114.104 82.455  1.00 67.79  ? 619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.250 116.400 80.743  1.00 58.00  ? 619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.056 113.615 80.686  1.00 68.55  ? 620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.813 112.409 80.364  1.00 68.89  ? 620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.190 112.746 79.808  1.00 68.70  ? 620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.173 112.060 80.114  1.00 66.50  ? 620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.025 111.553 79.375  1.00 70.19  ? 620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 125.673 111.433 79.778  1.00 69.21  ? 620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.283 113.796 78.987  1.00 66.43  ? 621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.553 114.123 78.347  1.00 65.27  ? 621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.585 114.631 79.347  1.00 68.18  ? 621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.776 114.329 79.210  1.00 69.83  ? 621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.335 115.158 77.243  1.00 65.95  ? 621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.329 116.221 77.631  1.00 68.86  ? 621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.542 116.034 78.557  1.00 67.96  ? 621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 129.350 117.343 76.923  1.00 66.80  ? 621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.159 115.398 80.350  1.00 59.35  ? 622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.067 115.971 81.336  1.00 57.19  ? 622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.902 115.336 82.713  1.00 59.55  ? 622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.177 115.972 83.734  1.00 66.37  ? 622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.885 117.489 81.409  1.00 57.14  ? 622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.476 117.905 81.810  1.00 60.24  ? 622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.849 117.296 82.676  1.00 64.84  ? 622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.975 118.956 81.175  1.00 59.73  ? 622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.449 114.080 82.758  1.00 53.45  ? 623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.295 113.398 84.038  1.00 55.40  ? 623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.634 113.179 84.728  1.00 57.31  ? 623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.738 113.365 85.947  1.00 55.94  ? 623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.577 112.063 83.843  1.00 58.49  ? 623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.372 111.301 85.118  1.00 57.75  ? 623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.221 110.391 85.676  1.00 54.52  ? 623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.246 111.391 85.999  1.00 57.01  ? 623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.694 109.906 86.847  1.00 54.79  ? 623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.481 110.503 87.067  1.00 55.19  ? 623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.061 112.133 85.987  1.00 55.42  ? 623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.577 110.340 88.114  1.00 54.50  ? 623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.166 111.969 87.027  1.00 55.40  ? 623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.429 111.080 88.075  1.00 56.93  ? 623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.663 112.783 83.981  1.00 58.70  ? 624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 134.968 112.526 84.576  1.00 59.93  ? 624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.804 113.787 84.736  1.00 59.62  ? 624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.774 113.774 85.503  1.00 59.99  ? 624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.727 111.479 83.748  1.00 58.61  ? 624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 136.764 112.052 82.824  1.00 60.89  ? 624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 138.097 112.112 83.203  1.00 59.48  ? 624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 136.411 112.513 81.567  1.00 57.60  ? 624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 139.052 112.631 82.353  1.00 56.19  ? 624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 137.363 113.031 80.711  1.00 61.05  ? 624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 138.685 113.090 81.106  1.00 60.01  ? 624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.452 114.872 84.042  1.00 55.73  ? 625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.082 116.157 84.326  1.00 49.14  ? 625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.634 116.707 85.673  1.00 51.14  ? 625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.396 117.418 86.336  1.00 56.88  ? 625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.775 117.162 83.218  1.00 46.32  ? 625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.401 116.822 81.897  1.00 49.61  ? 625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.777 116.740 81.771  1.00 47.63  ? 625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.615 116.593 80.781  1.00 53.07  ? 625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.357 116.433 80.558  1.00 52.61  ? 625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.191 116.283 79.564  1.00 53.02  ? 625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 137.564 116.203 79.453  1.00 54.96  ? 625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.410 116.389 86.092  1.00 45.83  ? 626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.925 116.789 87.405  1.00 45.87  ? 626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.392 115.798 88.461  1.00 46.22  ? 626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.577 115.246 89.207  1.00 54.25  ? 626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.400 116.890 87.412  1.00 44.03  ? 626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.879 118.236 86.976  1.00 46.11  ? 626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.911 119.325 87.837  1.00 47.67  ? 626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.346 118.418 85.709  1.00 46.43  ? 626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.437 120.557 87.444  1.00 46.28  ? 626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.867 119.648 85.308  1.00 45.06  ? 626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.916 120.711 86.180  1.00 48.63  ? 626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.441 121.940 85.785  1.00 55.11  ? 626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.699 115.563 88.525  1.00 44.39  ? 627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.247 114.626 89.495  1.00 51.01  ? 627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.984 115.117 90.913  1.00 46.73  ? 627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.112 116.308 91.209  1.00 51.96  ? 627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.747 114.450 89.257  1.00 52.06  ? 627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.413 113.388 90.108  1.00 47.38  ? 627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.856 113.196 89.675  1.00 47.18  ? 627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.585 112.220 90.579  1.00 55.59  ? 627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.025 112.116 90.223  1.00 52.33  ? 627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.598 114.195 91.789  1.00 53.02  ? 628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.320 114.554 93.171  1.00 53.83  ? 628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.597 114.994 93.876  1.00 56.58  ? 628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.690 114.494 93.602  1.00 60.27  ? 628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.685 113.381 93.916  1.00 57.58  ? 628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.221 113.159 93.581  1.00 57.35  ? 628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.630 111.975 94.318  1.00 62.36  ? 628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 133.242 111.526 95.310  1.00 58.23  ? 628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.551 111.497 93.909  1.00 61.57  ? 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.442 115.943 94.803  1.00 53.73  ? 629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.597 116.525 95.479  1.00 50.50  ? 629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.373 115.478 96.266  1.00 56.15  ? 629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.610 115.500 96.290  1.00 54.80  ? 629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.146 117.657 96.399  1.00 49.42  ? 629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.666 114.559 96.925  1.00 64.51  ? 630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.340 113.532 97.711  1.00 61.71  ? 630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.143 112.584 96.829  1.00 63.54  ? 630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.152 112.030 97.278  1.00 65.86  ? 630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.319 112.758 98.541  1.00 57.23  ? 630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.481 113.641 99.432  1.00 58.88  ? 630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.951 114.055 100.669 1.00 57.77  ? 630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.221 114.068 99.034  1.00 59.27  ? 630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.190 114.866 101.487 1.00 60.43  ? 630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.453 114.878 99.846  1.00 62.04  ? 630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.942 115.273 101.072 1.00 62.58  ? 630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.182 116.080 101.885 1.00 61.11  ? 630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.718 112.389 95.580  1.00 60.66  ? 631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.465 111.548 94.655  1.00 59.95  ? 631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.707 112.238 94.107  1.00 59.90  ? 631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.596 111.557 93.587  1.00 58.64  ? 631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.566 111.115 93.494  1.00 61.96  ? 631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.419 110.234 93.943  1.00 66.68  ? 631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.635 109.371 94.819  1.00 64.91  ? 631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.298 110.405 93.418  1.00 68.70  ? 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.788 113.561 94.216  1.00 54.90  ? 632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 141.921 114.292 93.671  1.00 53.36  ? 632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.172 114.088 94.518  1.00 58.18  ? 632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.112 113.755 95.705  1.00 58.99  ? 632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.618 115.787 93.585  1.00 51.03  ? 632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.288 116.140 92.965  1.00 52.51  ? 632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.392 117.657 92.003  1.00 57.47  ? 632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.086 117.386 90.816  1.00 49.12  ? 632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.321 114.297 93.882  1.00 52.34  ? 633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.589 114.374 94.590  1.00 51.70  ? 633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.666 115.729 95.283  1.00 51.60  ? 633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.590 116.772 94.626  1.00 54.67  ? 633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.754 114.188 93.619  1.00 48.37  ? 633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.095 114.058 94.321  1.00 56.91  ? 633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.166 114.283 95.547  1.00 55.98  ? 633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.088 113.729 93.640  1.00 54.86  ? 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.807 115.714 96.611  1.00 46.34  ? 634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.843 116.967 97.356  1.00 44.16  ? 634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.065 117.802 96.995  1.00 46.29  ? 634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.031 119.029 97.117  1.00 48.41  ? 634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.816 116.691 98.858  1.00 44.59  ? 634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.435 116.707 99.531  1.00 54.61  ? 634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.264 118.002 99.047  1.00 64.07  ? 634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.442 117.278 97.624  1.00 46.20  ? 634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.147 117.161 96.550  1.00 45.87  ? 635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.328 117.913 96.136  1.00 43.99  ? 635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.040 118.758 94.901  1.00 43.21  ? 635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.476 119.912 94.815  1.00 42.72  ? 635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.496 116.961 95.879  1.00 43.08  ? 635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.265 116.593 97.117  1.00 48.24  ? 635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.603 116.251 98.285  1.00 46.29  ? 635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.649 116.588 97.112  1.00 43.40  ? 635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.308 115.911 99.422  1.00 42.30  ? 635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.358 116.250 98.247  1.00 44.42  ? 635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.686 115.912 99.403  1.00 45.27  ? 635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.297 118.210 93.940  1.00 46.89  ? 636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.964 118.983 92.748  1.00 47.05  ? 636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.943 120.073 93.052  1.00 49.26  ? 636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.964 121.133 92.418  1.00 52.40  ? 636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.463 118.050 91.647  1.00 43.24  ? 636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.512 117.048 91.191  1.00 45.54  ? 636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 147.996 116.158 90.078  1.00 53.89  ? 636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.940 114.999 89.813  1.00 51.60  ? 636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.348 114.005 88.877  1.00 48.73  ? 636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.062 119.847 94.029  1.00 39.93  ? 637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.166 120.913 94.468  1.00 35.05  ? 637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.959 122.022 95.152  1.00 44.90  ? 637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.657 123.211 94.991  1.00 44.78  ? 637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.070 120.342 95.385  1.00 38.64  ? 637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.127 121.442 95.836  1.00 38.67  ? 637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.306 119.243 94.668  1.00 46.33  ? 637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.987 121.651 95.919  1.00 44.27  ? 638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.884 122.643 96.505  1.00 36.78  ? 638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.591 123.428 95.411  1.00 39.22  ? 638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.754 124.649 95.509  1.00 45.87  ? 638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.891 121.963 97.452  1.00 35.56  ? 638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.034 122.905 97.779  1.00 36.39  ? 638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.204 121.504 98.724  1.00 38.05  ? 638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.030 122.739 94.356  1.00 36.55  ? 639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.644 123.423 93.222  1.00 37.91  ? 639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.676 124.413 92.587  1.00 40.32  ? 639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.052 125.550 92.278  1.00 45.55  ? 639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.115 122.406 92.183  1.00 41.16  ? 639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.186 121.483 92.713  1.00 46.99  ? 639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.759 121.795 93.775  1.00 51.58  ? 639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.455 120.448 92.069  1.00 44.86  ? 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.425 123.997 92.393  1.00 36.02  ? 640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.419 124.882 91.813  1.00 37.87  ? 640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.206 126.118 92.679  1.00 39.90  ? 640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.189 127.249 92.178  1.00 44.13  ? 640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.105 124.122 91.632  1.00 43.86  ? 640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.896 125.011 91.421  1.00 41.72  ? 640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 144.022 126.002 89.927  1.00 43.50  ? 640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.216 124.929 88.745  1.00 39.04  ? 640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.055 125.920 93.989  1.00 38.78  ? 641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.783 127.045 94.878  1.00 31.81  ? 641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.985 127.978 94.949  1.00 32.15  ? 641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.835 129.205 94.931  1.00 40.91  ? 641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.361 126.541 96.269  1.00 34.92  ? 641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.078 125.715 96.164  1.00 38.40  ? 641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.137 127.708 97.213  1.00 35.98  ? 641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.044 126.306 95.229  1.00 39.64  ? 641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.197 127.417 95.019  1.00 32.17  ? 642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.402 128.239 95.033  1.00 30.25  ? 642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.557 129.021 93.738  1.00 33.24  ? 642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.050 130.156 93.754  1.00 35.93  ? 642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.631 127.366 95.279  1.00 31.14  ? 642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.161 128.432 92.610  1.00 34.65  ? 643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.117 129.184 91.363  1.00 33.05  ? 643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.123 130.333 91.458  1.00 33.16  ? 643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.402 131.448 91.003  1.00 34.52  ? 643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.758 128.252 90.205  1.00 29.55  ? 643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.812 127.300 90.013  1.00 35.81  ? 643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.565 129.040 88.933  1.00 29.77  ? 643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.956 130.079 92.051  1.00 31.77  ? 644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.003 131.157 92.301  1.00 28.75  ? 644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.524 132.096 93.381  1.00 30.21  ? 644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.347 133.318 93.298  1.00 33.90  ? 644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.628 130.579 92.676  1.00 28.55  ? 644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.130 129.624 91.594  1.00 30.63  ? 644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.630 131.694 92.902  1.00 26.52  ? 644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.921 128.829 92.012  1.00 32.25  ? 644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.172 131.545 94.412  1.00 30.65  ? 645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.557 132.345 95.571  1.00 23.48  ? 645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.552 133.439 95.209  1.00 32.82  ? 645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.546 134.509 95.827  1.00 40.53  ? 645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.137 131.441 96.660  1.00 22.44  ? 645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.530 132.165 97.931  1.00 24.23  ? 645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.337 132.485 98.803  1.00 31.10  ? 645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.880 133.625 98.852  1.00 35.64  ? 645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.826 131.477 99.501  1.00 25.84  ? 645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.405 133.200 94.212  1.00 38.20  ? 646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.405 134.193 93.843  1.00 36.67  ? 646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.798 135.448 93.229  1.00 29.77  ? 646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.494 136.461 93.126  1.00 35.43  ? 646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.420 133.580 92.878  1.00 32.34  ? 646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.933 133.474 91.449  1.00 40.84  ? 646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.884 132.688 90.570  1.00 43.33  ? 646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.534 131.628 90.052  1.00 40.76  ? 646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 153.095 133.204 90.399  1.00 41.77  ? 646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.528 135.413 92.835  1.00 32.25  ? 647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.850 136.578 92.288  1.00 29.71  ? 647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.813 137.154 93.238  1.00 27.07  ? 647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.142 138.129 92.886  1.00 38.85  ? 647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.189 136.226 90.952  1.00 30.79  ? 647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.136 135.651 89.947  1.00 30.57  ? 647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.182 136.371 89.415  1.00 27.11  ? 647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.199 134.422 89.383  1.00 27.93  ? 647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.847 135.612 88.563  1.00 37.94  ? 647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.271 134.425 88.525  1.00 35.73  ? 647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.664 136.580 94.428  1.00 29.77  ? 648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.722 137.053 95.434  1.00 33.46  ? 648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.538 137.646 96.573  1.00 32.63  ? 648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.378 136.957 97.166  1.00 31.78  ? 648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.811 135.919 95.928  1.00 16.29  ? 648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.060 135.287 94.754  1.00 27.35  ? 648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.827 136.431 96.954  1.00 17.68  ? 648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.083 136.216 94.074  1.00 21.35  ? 648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.302 138.925 96.877  1.00 24.43  ? 649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.097 139.587 97.907  1.00 29.86  ? 649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.736 139.080 99.300  1.00 30.04  ? 649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.607 138.973 100.171 1.00 37.39  ? 649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.937 141.105 97.811  1.00 35.60  ? 649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.509 141.562 98.011  1.00 34.54  ? 649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.611 140.705 98.099  1.00 34.96  ? 649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 145.284 142.786 98.079  1.00 35.30  ? 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.466 138.771 99.529  1.00 15.39  ? 650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.049 138.099 100.749 1.00 16.88  ? 650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.112 136.590 100.527 1.00 13.99  ? 650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.696 136.107 99.555  1.00 24.00  ? 650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.659 138.561 101.174 1.00 13.85  ? 650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.535 140.054 101.391 1.00 12.25  ? 650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.189 140.443 101.960 1.00 20.96  ? 650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.868 140.116 103.099 1.00 23.91  ? 650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.394 141.151 101.167 1.00 21.80  ? 650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.519 135.821 101.439 1.00 9.60   ? 651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.562 134.378 101.357 1.00 19.13  ? 651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.399 133.786 100.586 1.00 22.19  ? 651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.541 134.481 100.044 1.00 26.76  ? 651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.388 132.457 100.541 1.00 31.01  ? 652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.350 131.677 99.880  1.00 21.14  ? 652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.829 130.654 100.876 1.00 29.25  ? 652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.616 130.009 101.577 1.00 34.40  ? 652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.883 130.981 98.613  1.00 17.73  ? 652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.433 132.009 97.627  1.00 16.83  ? 652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.796 130.144 97.961  1.00 24.97  ? 652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.104 131.389 96.438  1.00 22.55  ? 652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.508 130.507 100.940 1.00 27.63  ? 653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.917 129.524 101.838 1.00 22.33  ? 653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.160 128.128 101.282 1.00 29.32  ? 653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.351 127.605 100.510 1.00 41.18  ? 653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.423 129.790 102.020 1.00 29.71  ? 653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.205 131.027 102.673 1.00 29.56  ? 653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.278 127.523 101.673 1.00 32.18  ? 654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.743 126.263 101.106 1.00 28.14  ? 654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.324 125.125 102.028 1.00 30.45  ? 654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.884 124.957 103.115 1.00 38.13  ? 654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.258 126.292 100.916 1.00 31.92  ? 654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.820 125.055 100.280 1.00 30.85  ? 654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.038 124.252 99.469  1.00 32.99  ? 654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.138 124.695 100.496 1.00 34.03  ? 654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.559 123.116 98.889  1.00 36.23  ? 654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.663 123.561 99.918  1.00 33.19  ? 654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.873 122.771 99.113  1.00 31.87  ? 654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.352 124.337 101.582 1.00 44.02  ? 655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.857 123.189 102.327 1.00 40.05  ? 655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.542 121.928 101.818 1.00 39.12  ? 655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.592 121.689 100.608 1.00 42.27  ? 655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.339 123.060 102.184 1.00 43.48  ? 655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.700 124.169 102.827 1.00 47.48  ? 655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.847 121.767 102.810 1.00 39.59  ? 655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.075 121.131 102.740 1.00 46.33  ? 656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.689 119.858 102.394 1.00 48.96  ? 656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.628 118.767 102.388 1.00 44.62  ? 656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.878 118.616 103.357 1.00 50.25  ? 656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.803 119.498 103.376 1.00 49.71  ? 656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.038 120.397 103.370 1.00 48.43  ? 656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.130 119.810 104.250 1.00 45.90  ? 656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.536 120.609 101.954 1.00 47.50  ? 656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.572 118.011 101.299 1.00 42.57  ? 657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.611 116.928 101.128 1.00 48.56  ? 657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.373 115.616 101.252 1.00 53.23  ? 657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.139 115.248 100.355 1.00 49.32  ? 657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.903 117.041 99.782  1.00 52.56  ? 657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.346 118.409 99.501  1.00 51.03  ? 657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.102 118.781 99.977  1.00 49.70  ? 657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.073 119.321 98.753  1.00 53.25  ? 657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.593 120.040 99.714  1.00 55.13  ? 657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.568 120.578 98.485  1.00 49.61  ? 657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.327 120.939 98.966  1.00 54.42  ? 657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.159 114.912 102.359 1.00 62.39  ? 658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.957 113.753 102.727 1.00 61.77  ? 658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.117 112.486 102.659 1.00 64.49  ? 658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.930 112.497 102.997 1.00 66.11  ? 658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.526 113.926 104.138 1.00 63.35  ? 658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.630 114.970 104.303 1.00 64.26  ? 658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.193 116.019 105.298 1.00 59.09  ? 658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.916 114.315 104.770 1.00 66.14  ? 658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.734 111.400 102.201 1.00 71.01  ? 659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.102 110.093 102.262 1.00 73.25  ? 659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.215 109.520 103.672 1.00 74.82  ? 659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.025 109.964 104.489 1.00 73.90  ? 659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.732 109.135 101.249 1.00 72.75  ? 659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.644 109.603 99.803  1.00 72.19  ? 659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.940 108.465 98.836  1.00 75.24  ? 659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.850 108.918 97.387  1.00 75.14  ? 659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.680 107.767 96.458  1.00 74.67  ? 659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.375 108.523 103.956 1.00 80.49  ? 660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.421 107.879 105.264 1.00 81.16  ? 660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.709 107.089 105.456 1.00 80.84  ? 660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 141.207 106.980 106.583 1.00 78.67  ? 660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 138.207 106.969 105.444 1.00 79.61  ? 660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.226 107.500 106.472 1.00 81.72  ? 660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 137.586 108.443 107.208 1.00 79.42  ? 660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 136.097 106.974 106.543 1.00 80.71  ? 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 141.262 106.536 104.375 1.00 81.32  ? 661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.449 105.697 104.474 1.00 81.44  ? 661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.731 106.491 104.682 1.00 77.18  ? 661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.739 105.908 105.097 1.00 75.44  ? 661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.593 104.836 103.218 1.00 81.98  ? 661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 143.851 104.151 103.249 1.00 81.62  ? 661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 142.526 105.704 101.970 1.00 77.36  ? 661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.727 107.792 104.408 1.00 76.31  ? 662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 144.947 108.581 104.508 1.00 78.98  ? 662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.183 109.008 105.952 1.00 78.43  ? 662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.299 109.581 106.595 1.00 78.27  ? 662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 144.872 109.795 103.583 1.00 75.92  ? 662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.764 109.412 102.111 1.00 79.09  ? 662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.827 110.795 100.953 1.00 83.58  ? 662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 144.847 112.187 102.075 1.00 74.38  ? 662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.384 108.731 106.453 1.00 68.66  ? 663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.703 108.864 107.865 1.00 67.75  ? 663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.041 110.313 108.212 1.00 67.12  ? 663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.862 111.230 107.406 1.00 67.37  ? 663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 147.856 107.932 108.231 1.00 68.29  ? 663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.102 108.608 108.019 1.00 62.85  ? 663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.819 106.679 107.369 1.00 67.87  ? 663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.534 110.530 109.434 1.00 63.09  ? 664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.955 111.868 109.836 1.00 62.88  ? 664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.266 112.265 109.173 1.00 59.25  ? 664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.523 113.458 108.982 1.00 61.96  ? 664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.097 111.954 111.355 1.00 60.74  ? 664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 148.991 110.932 111.812 1.00 59.38  ? 664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.747 111.787 112.027 1.00 61.16  ? 664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.108 111.290 108.827 1.00 61.82  ? 665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.328 111.611 108.095 1.00 61.51  ? 665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.004 112.179 106.721 1.00 65.17  ? 665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.679 113.098 106.252 1.00 65.87  ? 665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.218 110.376 107.965 1.00 63.88  ? 665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.463 110.618 107.124 1.00 60.96  ? 665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.415 109.435 107.166 1.00 65.11  ? 665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.377 109.464 106.069 1.00 67.64  ? 665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.075 109.250 104.795 1.00 65.78  ? 665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 153.841 108.963 104.414 1.00 60.88  ? 665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.037 109.320 103.881 1.00 63.05  ? 665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.973 111.646 106.060 1.00 60.48  ? 666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.562 112.194 104.771 1.00 57.40  ? 666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.052 113.623 104.916 1.00 60.30  ? 666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.371 114.490 104.092 1.00 66.24  ? 666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.497 111.301 104.139 1.00 63.30  ? 666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.941 109.856 104.029 1.00 67.46  ? 666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.048 109.613 103.505 1.00 65.60  ? 666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.186 108.964 104.468 1.00 66.92  ? 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.260 113.889 105.956 1.00 49.42  ? 667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.780 115.246 106.193 1.00 48.47  ? 667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.937 116.195 106.476 1.00 51.95  ? 667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 148.950 117.335 105.998 1.00 52.80  ? 667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.782 115.254 107.351 1.00 49.55  ? 667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 145.696 116.332 107.353 1.00 48.64  ? 667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 144.478 115.840 108.114 1.00 49.76  ? 667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 146.203 117.633 107.947 1.00 51.00  ? 667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.921 115.740 107.255 1.00 53.22  ? 668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.090 116.566 107.535 1.00 47.99  ? 668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.913 116.804 106.276 1.00 51.87  ? 668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.469 117.891 106.092 1.00 57.93  ? 668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 151.942 115.912 108.620 1.00 48.53  ? 668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.558 116.362 110.010 1.00 53.63  ? 668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.027 117.457 110.195 1.00 55.78  ? 668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.818 115.516 110.998 1.00 57.80  ? 668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.015 115.798 105.406 1.00 48.56  ? 669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.708 115.984 104.137 1.00 47.14  ? 669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 151.997 117.017 103.275 1.00 46.45  ? 669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.642 117.856 102.640 1.00 46.35  ? 669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.819 114.655 103.390 1.00 47.89  ? 669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 153.812 113.677 103.985 1.00 53.48  ? 669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.858 113.272 102.961 1.00 53.94  ? 669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 154.257 112.821 101.713 1.00 51.91  ? 669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 154.671 113.190 100.508 1.00 57.04  ? 669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 155.697 114.010 100.351 1.00 48.20  ? 669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 154.041 112.722 99.434  1.00 58.23  ? 669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.663 116.970 103.244 1.00 46.65  ? 670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.906 117.973 102.496 1.00 46.90  ? 670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.133 119.359 103.085 1.00 49.53  ? 670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.322 120.337 102.351 1.00 51.85  ? 670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.411 117.608 102.464 1.00 46.84  ? 670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.203 116.255 101.783 1.00 46.21  ? 670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.620 118.679 101.740 1.00 47.35  ? 670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.902 115.583 102.155 1.00 45.53  ? 670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.123 119.467 104.416 1.00 48.01  ? 671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.343 120.759 105.061 1.00 41.26  ? 671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.735 121.303 104.757 1.00 43.21  ? 671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.897 122.491 104.457 1.00 49.47  ? 671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.145 120.632 106.572 1.00 47.39  ? 671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.694 120.432 106.958 1.00 57.86  ? 671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.807 120.761 106.143 1.00 56.07  ? 671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.440 119.948 108.082 1.00 55.55  ? 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.754 120.444 104.823 1.00 42.51  ? 672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.121 120.890 104.580 1.00 37.61  ? 672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.359 121.204 103.110 1.00 39.27  ? 672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.167 122.081 102.793 1.00 49.12  ? 672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.113 119.836 105.067 1.00 44.78  ? 672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.154 119.622 106.580 1.00 46.50  ? 672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.734 118.258 106.912 1.00 45.86  ? 672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.944 120.731 107.255 1.00 41.59  ? 672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.679 120.502 102.203 1.00 38.79  ? 673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.772 120.847 100.790 1.00 40.32  ? 673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.068 122.165 100.502 1.00 41.35  ? 673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.530 122.954 99.669  1.00 46.59  ? 673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.187 119.722 99.939  1.00 36.15  ? 673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.391 119.912 98.457  1.00 39.36  ? 673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.664 119.891 97.903  1.00 41.68  ? 673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.311 120.107 97.611  1.00 39.93  ? 673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.853 120.063 96.548  1.00 41.27  ? 673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.491 120.278 96.258  1.00 42.45  ? 673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.762 120.256 95.729  1.00 42.22  ? 673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.942 120.427 94.377  1.00 40.07  ? 673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.943 122.417 101.176 1.00 35.73  ? 674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.285 123.713 101.063 1.00 39.18  ? 674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.191 124.828 101.562 1.00 41.51  ? 674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.307 125.881 100.924 1.00 45.69  ? 674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.969 123.697 101.838 1.00 34.24  ? 674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.854 124.609 102.699 1.00 39.35  ? 675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.804 125.591 103.206 1.00 31.22  ? 675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.963 125.787 102.235 1.00 38.03  ? 675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.416 126.917 102.017 1.00 46.09  ? 675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.316 125.157 104.579 1.00 33.68  ? 675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.416 126.017 105.114 1.00 42.43  ? 675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.749 125.743 104.897 1.00 42.22  ? 675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.381 127.144 105.862 1.00 35.07  ? 675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.487 126.667 105.486 1.00 39.75  ? 675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.681 127.528 106.079 1.00 37.37  ? 675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.453 124.696 101.645 1.00 41.61  ? 676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.569 124.777 100.710 1.00 43.94  ? 676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.171 125.453 99.404  1.00 44.23  ? 676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.999 126.123 98.779  1.00 41.92  ? 676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.118 123.377 100.439 1.00 43.73  ? 676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.184 123.332 99.390  1.00 52.94  ? 676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 157.932 122.962 98.087  1.00 52.78  ? 676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 159.509 123.608 99.453  1.00 49.08  ? 676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.053 123.013 97.391  1.00 49.94  ? 676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 160.025 123.402 98.196  1.00 50.28  ? 676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.920 125.293 98.978  1.00 36.83  ? 677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.456 125.857 97.718  1.00 39.47  ? 677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 153.958 127.288 97.848  1.00 43.57  ? 677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.547 127.878 96.845  1.00 46.71  ? 677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.349 124.982 97.120  1.00 38.27  ? 677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.853 123.725 96.432  1.00 42.09  ? 677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.882 124.053 95.360  1.00 40.60  ? 677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 154.477 125.182 94.530  1.00 48.95  ? 677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.571 125.119 93.563  1.00 50.15  ? 677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 152.964 123.985 93.258  1.00 43.21  ? 677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 153.269 126.222 92.884  1.00 42.94  ? 677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 153.984 127.859 99.047  1.00 33.51  ? 678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.554 129.225 99.241  1.00 29.25  ? 678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.108 129.398 99.640  1.00 30.14  ? 678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.602 130.525 99.588  1.00 31.63  ? 678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.422 128.323 100.026 1.00 35.14  ? 679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.048 128.444 100.495 1.00 31.61  ? 679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.036 129.249 101.785 1.00 33.70  ? 679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.836 129.006 102.697 1.00 45.78  ? 679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.420 127.057 100.697 1.00 34.27  ? 679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.287 126.334 99.357  1.00 31.00  ? 679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.066 127.172 101.374 1.00 37.83  ? 679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.489 127.097 98.345  1.00 30.96  ? 679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.133 130.224 101.863 1.00 27.21  ? 680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.101 131.109 103.017 1.00 20.06  ? 680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.300 130.505 104.164 1.00 18.83  ? 680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.771 130.462 105.305 1.00 32.11  ? 680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.528 132.465 102.611 1.00 17.38  ? 680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.435 133.277 101.706 1.00 16.47  ? 680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.791 134.597 101.330 1.00 16.32  ? 680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.654 135.384 100.366 1.00 27.74  ? 680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.082 136.727 100.094 1.00 28.06  ? 680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.089 130.029 103.881 1.00 30.92  ? 681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.211 129.468 104.896 1.00 22.11  ? 681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.637 128.143 104.418 1.00 34.90  ? 681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.481 127.910 103.217 1.00 43.72  ? 681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.048 130.415 105.239 1.00 29.89  ? 681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.195 130.561 104.098 1.00 40.94  ? 681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.559 131.778 105.655 1.00 22.13  ? 681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.323 127.277 105.377 1.00 30.89  ? 682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.614 126.026 105.128 1.00 28.30  ? 682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.347 126.045 105.970 1.00 29.69  ? 682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.415 126.175 107.198 1.00 42.23  ? 682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.478 124.801 105.455 1.00 22.70  ? 682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.873 124.959 104.849 1.00 37.75  ? 682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.820 123.541 104.940 1.00 34.30  ? 682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.759 123.756 105.040 1.00 39.46  ? 682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.193 125.917 105.313 1.00 24.57  ? 683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.926 126.138 106.001 1.00 21.26  ? 683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.469 124.897 106.761 1.00 36.74  ? 683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.421 124.894 107.994 1.00 51.38  ? 683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.859 126.575 104.991 1.00 33.80  ? 683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.511 126.916 105.589 1.00 23.95  ? 683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.390 127.292 106.919 1.00 22.66  ? 683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.361 126.868 104.817 1.00 19.07  ? 683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.162 127.605 107.463 1.00 29.16  ? 683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.128 127.182 105.353 1.00 27.48  ? 683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.035 127.548 106.676 1.00 31.05  ? 683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.810 127.861 107.215 1.00 30.52  ? 683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.156 123.821 106.048 1.00 41.01  ? 684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.488 122.688 106.670 1.00 33.87  ? 684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.124 121.389 106.211 1.00 46.06  ? 684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.725 121.314 105.137 1.00 51.88  ? 684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.989 122.668 106.342 1.00 40.39  ? 684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.110 123.250 107.424 1.00 31.95  ? 684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.378 123.018 108.764 1.00 39.50  ? 684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.011 124.034 107.102 1.00 41.27  ? 684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.576 123.550 109.756 1.00 46.66  ? 684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.203 124.569 108.085 1.00 43.61  ? 684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.489 124.325 109.409 1.00 47.44  ? 684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.686 124.857 110.391 1.00 45.93  ? 684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 139.979 120.365 107.043 1.00 46.89  ? 685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.399 119.006 106.726 1.00 45.12  ? 685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.132 118.156 106.681 1.00 49.42  ? 685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.700 117.602 107.694 1.00 51.73  ? 685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.399 118.486 107.750 1.00 49.72  ? 685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.533 118.066 105.497 1.00 53.83  ? 686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.291 117.326 105.304 1.00 53.76  ? 686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.632 115.878 104.978 1.00 59.82  ? 686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.202 115.587 103.922 1.00 60.25  ? 686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.456 117.961 104.195 1.00 53.10  ? 686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.760 119.245 104.608 1.00 58.64  ? 686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.536 119.508 103.751 1.00 60.89  ? 686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.680 118.334 103.642 1.00 59.95  ? 686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.446 118.259 104.121 1.00 60.32  ? 686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.888 119.277 104.754 1.00 55.45  ? 686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.754 117.135 103.959 1.00 61.56  ? 686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.283 114.970 105.884 1.00 68.61  ? 687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.568 113.552 105.726 1.00 69.82  ? 687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.313 112.827 105.261 1.00 67.70  ? 687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 135.236 113.005 105.840 1.00 68.72  ? 687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 138.073 112.946 107.035 1.00 70.33  ? 687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.155 113.737 107.543 1.00 67.76  ? 687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.564 111.526 106.807 1.00 67.88  ? 687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.453 112.016 104.218 1.00 73.41  ? 688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.333 111.249 103.687 1.00 76.94  ? 688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 135.408 109.796 104.142 1.00 78.25  ? 688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.299 109.053 103.732 1.00 77.06  ? 688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.307 111.322 102.161 1.00 73.00  ? 688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 134.198 110.509 101.518 1.00 71.08  ? 688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 134.232 110.636 100.005 1.00 72.76  ? 688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.162 109.780 99.354  1.00 74.01  ? 688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.189 109.898 97.870  1.00 73.31  ? 688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 151.729 114.869 163.673 1.00 63.43  ? 6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 150.768 115.907 164.021 1.00 65.94  ? 6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 151.470 117.027 164.789 1.00 67.47  ? 6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 152.350 116.770 165.612 1.00 66.45  ? 6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 149.574 115.313 164.822 1.00 65.98  ? 6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 149.957 115.036 166.270 1.00 63.88  ? 6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 148.360 116.229 164.749 1.00 66.13  ? 6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 151.118 118.276 164.483 1.00 62.94  ? 7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 151.670 119.400 165.247 1.00 57.20  ? 7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 151.211 119.359 166.696 1.00 58.33  ? 7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 150.133 118.852 167.011 1.00 63.66  ? 7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 151.121 120.628 164.513 1.00 56.88  ? 7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 150.862 120.140 163.126 1.00 58.87  ? 7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 150.360 118.740 163.307 1.00 60.91  ? 7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 152.051 119.897 167.584 1.00 57.79  ? 8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 151.727 119.891 169.006 1.00 58.95  ? 8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 150.474 120.703 169.304 1.00 60.87  ? 8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 149.643 120.286 170.119 1.00 63.37  ? 8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 152.905 120.429 169.820 1.00 58.30  ? 8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 152.619 120.549 171.308 1.00 60.12  ? 8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 153.902 120.600 172.119 1.00 61.27  ? 8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 153.738 121.473 173.353 1.00 58.75  ? 8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.046 121.981 173.853 1.00 57.85  ? 8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 150.322 121.863 168.662 1.00 60.89  ? 9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 149.154 122.698 168.925 1.00 56.50  ? 9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 147.873 122.022 168.461 1.00 55.00  ? 9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 146.836 122.127 169.124 1.00 58.69  ? 9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 149.309 124.059 168.250 1.00 56.78  ? 9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 149.729 124.003 166.813 1.00 55.76  ? 9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 148.912 123.901 165.727 1.00 54.97  ? 9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 151.066 124.068 166.305 1.00 54.62  ? 9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 149.656 123.890 164.573 1.00 54.73  ? 9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 150.983 123.993 164.901 1.00 57.56  ? 9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 152.326 124.179 166.899 1.00 54.44  ? 9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 152.109 124.022 164.084 1.00 58.34  ? 9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 153.441 124.209 166.086 1.00 56.18  ? 9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 153.327 124.129 164.694 1.00 56.84  ? 9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 147.921 121.328 167.323 1.00 56.64  ? 10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 146.738 120.631 166.833 1.00 59.60  ? 10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 146.397 119.457 167.743 1.00 61.16  ? 10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 145.222 119.200 168.035 1.00 64.46  ? 10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 146.951 120.188 165.375 1.00 59.12  ? 10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 146.846 121.396 164.442 1.00 60.27  ? 10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 145.941 119.126 164.979 1.00 62.42  ? 10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.254 121.108 163.020 1.00 62.09  ? 10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 147.416 118.735 168.215 1.00 62.14  ? 11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 147.176 117.628 169.137 1.00 61.22  ? 11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 146.578 118.122 170.450 1.00 59.49  ? 11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 145.682 117.482 171.009 1.00 62.54  ? 11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 148.477 116.863 169.381 1.00 63.90  ? 11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 148.645 116.333 170.796 1.00 65.01  ? 11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 150.091 116.044 171.140 1.00 67.38  ? 11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 150.822 115.445 170.352 1.00 67.32  ? 11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 150.514 116.471 172.325 1.00 63.48  ? 11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 147.061 119.260 170.956 1.00 60.95  ? 12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 146.472 119.843 172.157 1.00 63.30  ? 12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 145.049 120.320 171.894 1.00 63.33  ? 12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 144.180 120.218 172.768 1.00 64.36  ? 12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 147.340 120.993 172.663 1.00 62.82  ? 12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 148.404 120.639 173.703 1.00 63.35  ? 12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 149.477 121.713 173.759 1.00 61.97  ? 12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 147.769 120.444 175.068 1.00 62.42  ? 12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 144.795 120.851 170.697 1.00 61.53  ? 13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 143.437 121.220 170.316 1.00 62.41  ? 13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 142.570 119.987 170.098 1.00 63.86  ? 13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 141.355 120.037 170.316 1.00 66.76  ? 13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 143.467 122.091 169.060 1.00 60.15  ? 13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 142.097 122.288 168.450 1.00 61.11  ? 13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 141.732 121.616 167.486 1.00 63.01  ? 13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 141.328 123.215 169.008 1.00 64.21  ? 13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 143.174 118.876 169.670 1.00 64.46  ? 14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 142.451 117.618 169.536 1.00 64.14  ? 14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 142.004 117.055 170.878 1.00 63.39  ? 14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 141.139 116.174 170.903 1.00 68.38  ? 14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 143.322 116.587 168.817 1.00 66.41  ? 14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 143.138 116.618 167.316 1.00 66.22  ? 14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 142.469 117.499 166.783 1.00 64.63  ? 14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 143.733 115.651 166.625 1.00 65.10  ? 14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 142.567 117.540 171.982 1.00 66.02  ? 15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 142.225 117.063 173.313 1.00 67.69  ? 15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 140.933 117.672 173.842 1.00 70.58  ? 15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 140.507 117.318 174.948 1.00 71.34  ? 15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 143.379 117.356 174.279 1.00 69.79  ? 15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 143.464 116.408 175.463 1.00 72.83  ? 15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 144.870 115.896 175.698 1.00 73.23  ? 15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 145.830 116.658 175.455 1.00 73.16  ? 15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 145.016 114.732 176.125 1.00 71.66  ? 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 140.310 118.582 173.089 1.00 73.58  ? 16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 139.050 119.178 173.524 1.00 72.33  ? 16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 137.980 118.106 173.675 1.00 70.24  ? 16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 137.291 118.028 174.701 1.00 71.18  ? 16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 138.608 120.272 172.534 1.00 70.10  ? 16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 139.583 121.453 172.557 1.00 67.35  ? 16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 137.188 120.729 172.842 1.00 71.42  ? 16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 139.318 122.454 173.654 1.00 68.70  ? 16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 137.834 117.250 172.661 1.00 69.85  ? 17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 136.792 116.230 172.673 1.00 75.05  ? 17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 137.176 114.991 173.468 1.00 75.10  ? 17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 136.313 114.139 173.709 1.00 73.32  ? 17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 136.424 115.837 171.243 1.00 72.48  ? 17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 136.906 116.819 170.199 1.00 72.44  ? 17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 135.897 118.311 170.214 1.00 78.66  ? 17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 134.324 117.659 169.660 1.00 74.76  ? 17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 138.436 114.864 173.879 1.00 75.50  ? 18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 138.829 113.764 174.753 1.00 75.01  ? 18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 138.290 114.080 176.140 1.00 74.94  ? 18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 138.899 114.842 176.897 1.00 77.40  ? 18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 140.356 113.551 174.781 1.00 74.93  ? 18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 140.970 113.503 173.373 1.00 74.40  ? 18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 140.701 112.287 175.556 1.00 73.63  ? 18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 140.101 112.876 172.288 1.00 71.88  ? 18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 137.145 113.498 176.480 1.00 78.03  ? 19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 136.444 113.865 177.702 1.00 79.69  ? 19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 137.042 113.148 178.903 1.00 80.63  ? 19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 137.111 111.915 178.931 1.00 79.21  ? 19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 134.957 113.531 177.579 1.00 80.20  ? 19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 134.256 114.225 176.425 1.00 80.15  ? 19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 132.779 113.890 176.358 1.00 80.35  ? 19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 132.256 113.168 177.206 1.00 79.13  ? 19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 132.099 114.410 175.343 1.00 78.87  ? 19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 137.477 113.922 179.893 1.00 86.11  ? 20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 137.890 113.389 181.181 1.00 88.22  ? 20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 136.832 113.739 182.219 1.00 88.53  ? 20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 136.288 114.850 182.215 1.00 87.22  ? 20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 139.267 113.924 181.601 1.00 86.39  ? 20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 139.279 115.334 182.171 1.00 86.78  ? 20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 140.616 116.015 181.935 1.00 86.68  ? 20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 140.527 117.513 182.181 1.00 87.27  ? 20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 141.772 118.217 181.770 1.00 86.86  ? 20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 136.511 112.770 183.077 1.00 90.74  ? 21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 135.460 112.902 184.084 1.00 91.48  ? 21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 134.107 113.228 183.453 1.00 91.51  ? 21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 133.240 113.826 184.099 1.00 90.46  ? 21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 135.838 113.952 185.140 1.00 91.80  ? 21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 135.005 113.840 186.404 1.00 92.18  ? 21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 135.246 112.904 187.196 1.00 90.90  ? 21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 134.116 114.693 186.612 1.00 91.57  ? 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 133.911 112.846 182.193 1.00 87.44  ? 22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 132.670 113.118 181.498 1.00 86.02  ? 22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 132.504 114.537 181.006 1.00 87.29  ? 22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 131.414 114.889 180.541 1.00 85.40  ? 22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 133.544 115.362 181.087 1.00 89.39  ? 23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 133.471 116.766 180.708 1.00 86.41  ? 23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 134.499 117.069 179.627 1.00 85.97  ? 23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 135.583 116.477 179.604 1.00 86.49  ? 23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 133.709 117.674 181.920 1.00 84.21  ? 23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 132.881 117.304 183.139 1.00 87.21  ? 23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 131.395 117.355 182.833 1.00 88.14  ? 23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 130.935 118.782 182.602 1.00 87.00  ? 23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 131.507 119.705 183.622 1.00 85.93  ? 23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 134.149 117.989 178.732 1.00 78.09  ? 24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 135.068 118.406 177.682 1.00 75.81  ? 24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 136.257 119.147 178.277 1.00 76.76  ? 24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 136.122 119.892 179.252 1.00 74.77  ? 24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 134.348 119.300 176.673 1.00 72.54  ? 24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 133.583 118.545 175.625 1.00 74.08  ? 24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 134.214 118.084 174.484 1.00 75.01  ? 24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 132.230 118.301 175.779 1.00 74.62  ? 24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 133.511 117.391 173.517 1.00 73.97  ? 24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 131.523 117.609 174.816 1.00 76.31  ? 24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 132.165 117.155 173.683 1.00 74.51  ? 24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 137.433 118.939 177.685 1.00 76.29  ? 25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 138.650 119.625 178.124 1.00 76.28  ? 25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 138.794 120.945 177.366 1.00 76.65  ? 25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 139.664 121.128 176.514 1.00 77.38  ? 25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 139.869 118.733 177.928 1.00 76.64  ? 25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 139.792 117.397 178.638 1.00 76.05  ? 25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 141.022 116.545 178.400 1.00 77.45  ? 25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 142.035 116.694 179.083 1.00 78.21  ? 25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 140.940 115.646 177.429 1.00 76.84  ? 25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 137.906 121.883 177.704 1.00 67.63  ? 26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 137.938 123.198 177.074 1.00 65.77  ? 26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 139.179 123.994 177.451 1.00 65.50  ? 26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 139.545 124.925 176.726 1.00 65.66  ? 26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 136.680 123.985 177.440 1.00 64.05  ? 26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 135.431 123.452 176.804 1.00 65.03  ? 26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 135.388 123.194 175.444 1.00 62.83  ? 26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 134.300 123.205 177.562 1.00 64.06  ? 26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 134.243 122.702 174.855 1.00 62.63  ? 26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 133.151 122.713 176.977 1.00 61.75  ? 26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 133.124 122.463 175.622 1.00 63.61  ? 26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 139.833 123.653 178.563 1.00 69.38  ? 27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 141.061 124.339 178.946 1.00 67.57  ? 27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 142.228 123.981 178.037 1.00 68.02  ? 27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 143.259 124.661 178.078 1.00 68.62  ? 27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 141.413 124.016 180.398 1.00 69.20  ? 27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 140.426 124.609 181.383 1.00 72.40  ? 27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 139.994 125.762 181.173 1.00 70.57  ? 27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 140.083 123.923 182.368 1.00 70.97  ? 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 142.091 122.935 177.221 1.00 68.80  ? 28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 143.160 122.551 176.308 1.00 69.13  ? 28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 143.280 123.502 175.126 1.00 71.51  ? 28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 144.321 123.517 174.462 1.00 74.35  ? 28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 142.933 121.126 175.804 1.00 68.60  ? 28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 143.215 120.046 176.834 1.00 69.70  ? 28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 144.707 119.845 177.032 1.00 71.36  ? 28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 144.987 118.914 178.198 1.00 69.37  ? 28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 146.433 118.573 178.300 1.00 69.17  ? 28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 142.239 124.291 174.845 1.00 67.38  ? 29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 142.302 125.226 173.727 1.00 65.88  ? 29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 143.274 126.364 174.013 1.00 64.02  ? 29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 143.995 126.811 173.114 1.00 63.26  ? 29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 140.907 125.767 173.421 1.00 66.46  ? 29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 140.687 126.004 171.940 1.00 66.25  ? 29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.317 125.300 171.124 1.00 65.70  ? 29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 139.873 126.883 171.593 1.00 64.30  ? 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 143.303 126.852 175.256 1.00 62.29  ? 30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 144.305 127.841 175.637 1.00 63.48  ? 30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 145.709 127.259 175.542 1.00 64.91  ? 30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 146.636 127.923 175.062 1.00 65.92  ? 30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 144.026 128.351 177.051 1.00 63.14  ? 30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.489 129.774 177.302 1.00 65.47  ? 30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.539 129.824 178.399 1.00 65.48  ? 30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.087 130.703 179.552 1.00 66.08  ? 30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 144.289 131.867 179.079 1.00 64.83  ? 30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 145.880 126.013 175.992 1.00 65.54  ? 31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 147.151 125.326 175.797 1.00 63.89  ? 31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 147.456 125.165 174.315 1.00 64.40  ? 31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 148.612 125.296 173.893 1.00 65.27  ? 31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 147.121 123.965 176.491 1.00 66.19  ? 31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 147.084 124.040 178.007 1.00 68.98  ? 31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 147.208 122.677 178.657 1.00 71.86  ? 31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.006 121.853 178.166 1.00 71.13  ? 31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 146.504 122.430 179.661 1.00 69.26  ? 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 146.429 124.881 173.511 1.00 58.67  ? 32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 146.630 124.736 172.074 1.00 57.22  ? 32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 147.113 126.037 171.445 1.00 57.84  ? 32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 148.028 126.026 170.616 1.00 62.46  ? 32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 145.339 124.265 171.407 1.00 61.39  ? 32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 146.522 127.170 171.832 1.00 56.51  ? 33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 146.932 128.449 171.256 1.00 55.05  ? 33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 148.327 128.834 171.743 1.00 56.56  ? 33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 149.133 129.393 170.988 1.00 59.52  ? 33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 145.885 129.544 171.547 1.00 55.05  ? 33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.098 130.194 172.903 1.00 57.20  ? 33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 145.926 130.603 170.458 1.00 56.79  ? 33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 148.638 128.534 173.008 1.00 62.82  ? 34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 149.979 128.812 173.513 1.00 59.16  ? 34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 151.025 128.001 172.760 1.00 62.05  ? 34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 152.071 128.534 172.365 1.00 64.90  ? 34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 150.050 128.519 175.010 1.00 62.73  ? 34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 151.111 129.296 175.727 1.00 63.98  ? 34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 152.282 128.722 176.170 1.00 64.91  ? 34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 151.173 130.601 176.082 1.00 64.39  ? 34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 153.023 129.642 176.764 1.00 64.58  ? 34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 152.372 130.790 176.724 1.00 65.25  ? 34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 150.758 126.711 172.550 1.00 59.56  ? 35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 151.670 125.875 171.779 1.00 57.86  ? 35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 151.789 126.381 170.348 1.00 60.20  ? 35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 152.893 126.460 169.799 1.00 63.75  ? 35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 151.194 124.424 171.800 1.00 58.67  ? 35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 151.838 123.666 170.791 1.00 62.18  ? 35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 150.658 126.737 169.733 1.00 57.83  ? 36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 150.672 127.268 168.376 1.00 54.84  ? 36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 151.602 128.462 168.272 1.00 53.41  ? 36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 152.519 128.480 167.445 1.00 55.47  ? 36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 149.253 127.653 167.956 1.00 52.30  ? 36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 149.135 128.170 166.540 1.00 51.84  ? 36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 149.562 127.409 165.462 1.00 54.87  ? 36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 148.590 129.421 166.282 1.00 51.29  ? 36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 149.452 127.878 164.168 1.00 51.99  ? 36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 148.476 129.898 164.994 1.00 51.17  ? 36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 148.908 129.123 163.939 1.00 51.69  ? 36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 148.797 129.595 162.653 1.00 55.53  ? 36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 151.413 129.448 169.148 1.00 57.27  ? 37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 152.260 130.632 169.108 1.00 56.10  ? 37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 153.720 130.260 169.324 1.00 58.60  ? 37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 154.545 130.440 168.424 1.00 62.75  ? 37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 151.789 131.655 170.139 1.00 56.88  ? 37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 150.791 132.627 169.594 1.00 55.99  ? 37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.205 133.693 168.814 1.00 57.05  ? 37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 149.440 132.466 169.837 1.00 56.48  ? 37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.292 134.587 168.301 1.00 58.85  ? 37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 148.523 133.357 169.326 1.00 58.04  ? 37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 148.949 134.418 168.557 1.00 60.09  ? 37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 154.023 129.629 170.462 1.00 63.76  ? 38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 155.411 129.412 170.864 1.00 64.59  ? 38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 156.162 128.580 169.830 1.00 63.92  ? 38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 157.340 128.835 169.549 1.00 65.77  ? 38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 155.459 128.762 172.261 1.00 64.22  ? 38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 156.869 128.305 172.596 1.00 63.70  ? 38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 154.950 129.736 173.313 1.00 60.79  ? 38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 155.501 127.588 169.230 1.00 60.31  ? 39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 156.200 126.653 168.362 1.00 63.66  ? 39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 156.131 127.001 166.880 1.00 65.87  ? 39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 156.973 126.514 166.118 1.00 68.18  ? 39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 155.653 125.235 168.568 1.00 62.61  ? 39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 155.512 124.874 170.033 1.00 65.75  ? 39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 156.253 125.444 170.859 1.00 63.18  ? 39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 154.660 124.020 170.357 1.00 66.39  ? 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 155.170 127.814 166.440 1.00 62.03  ? 40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 155.082 128.164 165.029 1.00 61.39  ? 40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 155.167 129.660 164.783 1.00 66.64  ? 40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 155.946 130.098 163.930 1.00 69.24  ? 40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 153.778 127.610 164.435 1.00 58.98  ? 40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 153.645 127.816 162.944 1.00 59.45  ? 40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 154.615 127.345 162.071 1.00 61.31  ? 40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 152.550 128.480 162.411 1.00 61.54  ? 40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 154.497 127.531 160.707 1.00 64.39  ? 40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 152.423 128.670 161.050 1.00 63.32  ? 40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 153.399 128.194 160.202 1.00 65.73  ? 40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 153.278 128.381 158.844 1.00 65.00  ? 40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 154.400 130.464 165.518 1.00 63.61  ? 41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.207 131.856 165.129 1.00 59.75  ? 41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.433 132.686 165.475 1.00 56.55  ? 41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 155.957 133.422 164.632 1.00 60.66  ? 41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 152.935 132.418 165.789 1.00 55.30  ? 41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 151.713 131.596 165.377 1.00 57.20  ? 41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 152.724 133.857 165.386 1.00 57.64  ? 41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 151.479 131.570 163.888 1.00 54.63  ? 41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 155.912 132.580 166.716 1.00 56.48  ? 42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.107 133.317 167.111 1.00 60.90  ? 42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.325 132.857 166.322 1.00 64.89  ? 42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.173 133.673 165.940 1.00 65.04  ? 42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.347 133.161 168.612 1.00 60.93  ? 42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.199 133.696 169.443 1.00 61.99  ? 42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.325 134.399 168.935 1.00 64.09  ? 42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.195 133.368 170.729 1.00 62.40  ? 42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 158.433 131.550 166.072 1.00 66.57  ? 43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 159.566 131.031 165.315 1.00 64.67  ? 43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.527 131.492 163.863 1.00 62.93  ? 43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.575 131.759 163.264 1.00 64.55  ? 43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 159.592 129.505 165.395 1.00 65.00  ? 43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 159.697 128.962 166.809 1.00 65.55  ? 43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 159.870 127.458 166.842 1.00 66.20  ? 43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.240 126.842 165.843 1.00 64.01  ? 43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 159.604 126.857 167.996 1.00 63.74  ? 43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.332 131.592 163.279 1.00 61.49  ? 44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.172 131.937 161.874 1.00 62.60  ? 44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 157.804 133.402 161.666 1.00 63.19  ? 44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.335 133.768 160.583 1.00 64.46  ? 44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 157.123 131.032 161.227 1.00 59.93  ? 44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.553 129.579 161.189 1.00 64.31  ? 44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 157.901 128.996 162.215 1.00 63.64  ? 44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 157.529 128.985 160.002 1.00 64.38  ? 44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 158.004 134.244 162.674 1.00 61.24  ? 45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 157.802 135.681 162.550 1.00 61.46  ? 45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 159.158 136.361 162.447 1.00 61.99  ? 45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 159.997 136.222 163.344 1.00 61.64  ? 45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 157.025 136.244 163.742 1.00 61.12  ? 45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 155.780 135.547 163.878 1.00 63.56  ? 45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 156.749 137.727 163.545 1.00 60.29  ? 45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 159.370 137.093 161.359 1.00 64.29  ? 46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 160.620 137.817 161.161 1.00 65.37  ? 46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 160.596 139.048 162.059 1.00 65.47  ? 46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 159.596 139.772 162.116 1.00 63.07  ? 46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 160.821 138.191 159.684 1.00 63.51  ? 46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 159.590 137.825 158.868 1.00 62.90  ? 46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.182 139.662 159.515 1.00 62.54  ? 46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 161.681 139.263 162.794 1.00 67.79  ? 47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 161.760 140.338 163.770 1.00 67.41  ? 47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 162.803 141.360 163.341 1.00 69.35  ? 47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 163.860 141.002 162.810 1.00 69.16  ? 47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 162.101 139.787 165.157 1.00 67.70  ? 47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 161.750 140.715 166.282 1.00 69.36  ? 47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 160.476 140.716 166.823 1.00 68.25  ? 47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 162.696 141.578 166.808 1.00 67.61  ? 47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 160.148 141.566 167.862 1.00 68.23  ? 47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 162.375 142.431 167.848 1.00 68.17  ? 47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 161.099 142.424 168.375 1.00 70.51  ? 47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 162.498 142.631 163.573 1.00 68.45  ? 48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 163.383 143.735 163.240 1.00 65.06  ? 48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 163.883 144.403 164.513 1.00 66.45  ? 48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 163.212 144.384 165.549 1.00 68.68  ? 48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 162.674 144.766 162.355 1.00 65.47  ? 48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 162.142 144.200 161.068 1.00 67.36  ? 48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 160.908 143.573 161.025 1.00 66.41  ? 48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 162.872 144.305 159.898 1.00 66.35  ? 48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 160.416 143.061 159.841 1.00 66.78  ? 48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 162.386 143.792 158.711 1.00 66.93  ? 48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 161.156 143.170 158.683 1.00 67.35  ? 48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 165.077 144.996 164.424 1.00 72.66  ? 49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 165.689 145.615 165.595 1.00 74.94  ? 49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 164.837 146.755 166.143 1.00 75.13  ? 49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 164.888 147.044 167.344 1.00 76.04  ? 49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 167.090 146.118 165.247 1.00 75.48  ? 49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 167.803 145.267 164.243 1.00 78.05  ? 49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.296 145.769 163.059 1.00 77.54  ? 49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 168.107 143.947 164.248 1.00 76.81  ? 49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 168.873 144.796 162.376 1.00 75.38  ? 49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 168.772 143.680 163.076 1.00 74.79  ? 49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 164.055 147.407 165.288 1.00 72.07  ? 50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 163.173 148.482 165.718 1.00 71.74  ? 50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 162.041 148.608 164.707 1.00 72.88  ? 50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 162.104 148.063 163.604 1.00 71.75  ? 50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 163.931 149.804 165.873 1.00 70.72  ? 50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 164.628 150.229 164.598 1.00 72.34  ? 50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 164.898 149.409 163.721 1.00 71.16  ? 50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 164.926 151.518 164.487 1.00 72.27  ? 50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 160.995 149.335 165.109 1.00 66.17  ? 51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 159.845 149.523 164.231 1.00 65.48  ? 51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 160.222 150.277 162.962 1.00 66.52  ? 51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 159.592 150.082 161.916 1.00 69.80  ? 51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 158.732 150.262 164.974 1.00 63.73  ? 51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 157.400 150.414 164.239 1.00 62.24  ? 51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 156.884 149.066 163.765 1.00 60.79  ? 51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 156.379 151.102 165.124 1.00 63.45  ? 51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 161.236 151.142 163.036 1.00 65.02  ? 52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 161.673 151.869 161.848 1.00 64.20  ? 52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 162.161 150.910 160.770 1.00 67.50  ? 52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 161.808 151.057 159.594 1.00 67.20  ? 52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 162.772 152.865 162.217 1.00 66.55  ? 52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 162.952 154.019 161.234 1.00 67.64  ? 52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 161.690 154.290 160.429 1.00 68.27  ? 52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 161.912 155.402 159.418 1.00 67.36  ? 52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 161.902 156.747 160.059 1.00 67.07  ? 52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 162.963 149.915 161.158 1.00 71.09  ? 53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 163.436 148.929 160.193 1.00 69.85  ? 53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 162.284 148.135 159.598 1.00 69.01  ? 53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 162.266 147.882 158.389 1.00 69.52  ? 53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 164.447 147.990 160.849 1.00 69.09  ? 53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 165.226 147.135 159.864 1.00 70.95  ? 53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 165.876 145.931 160.520 1.00 72.57  ? 53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 165.708 145.754 161.745 1.00 72.58  ? 53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.555 145.161 159.810 1.00 69.72  ? 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 161.311 147.740 160.424 1.00 64.00  ? 54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 160.162 146.992 159.925 1.00 62.67  ? 54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 159.354 147.802 158.921 1.00 59.67  ? 54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 159.013 147.299 157.844 1.00 63.29  ? 54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 159.269 146.562 161.088 1.00 64.37  ? 54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 158.015 145.825 160.652 1.00 64.09  ? 54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 157.638 144.738 161.640 1.00 60.46  ? 54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 156.147 144.467 161.617 1.00 61.51  ? 54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 155.790 143.310 162.481 1.00 63.60  ? 54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 159.040 149.055 159.255 1.00 62.07  ? 55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 158.271 149.893 158.345 1.00 64.91  ? 55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 159.037 150.173 157.060 1.00 66.78  ? 55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 158.452 150.148 155.972 1.00 67.30  ? 55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 157.879 151.199 159.034 1.00 64.70  ? 55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 156.943 151.056 160.234 1.00 63.75  ? 55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 156.821 152.374 160.972 1.00 64.36  ? 55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 155.578 150.553 159.792 1.00 62.53  ? 55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 160.343 150.439 157.161 1.00 68.84  ? 56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 161.143 150.666 155.963 1.00 68.14  ? 56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 161.169 149.428 155.076 1.00 67.79  ? 56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 161.008 149.529 153.855 1.00 69.17  ? 56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 162.562 151.079 156.353 1.00 69.59  ? 56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 162.630 152.494 156.891 1.00 73.19  ? 56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 161.584 153.176 156.907 1.00 75.22  ? 56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 163.729 152.922 157.302 1.00 70.00  ? 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 161.363 148.250 155.674 1.00 61.06  ? 57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 161.397 147.015 154.898 1.00 60.29  ? 57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 160.057 146.749 154.226 1.00 61.51  ? 57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 160.012 146.336 153.062 1.00 66.42  ? 57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 161.799 145.845 155.801 1.00 60.89  ? 57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 161.611 144.471 155.191 1.00 61.71  ? 57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 160.403 143.793 155.306 1.00 63.02  ? 57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 162.645 143.849 154.504 1.00 62.44  ? 57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 160.230 142.541 154.750 1.00 65.37  ? 57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 162.481 142.596 153.946 1.00 61.82  ? 57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 161.271 141.946 154.072 1.00 64.63  ? 57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 161.102 140.698 153.519 1.00 65.19  ? 57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 158.954 146.975 154.941 1.00 58.69  ? 58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 157.641 146.702 154.370 1.00 59.05  ? 58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 157.264 147.707 153.288 1.00 57.42  ? 58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 156.634 147.328 152.295 1.00 57.70  ? 58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 156.586 146.677 155.476 1.00 58.04  ? 58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 156.726 145.499 156.445 1.00 57.88  ? 58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 155.874 145.696 157.683 1.00 56.95  ? 58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 156.372 144.192 155.754 1.00 57.57  ? 58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 157.635 148.978 153.450 1.00 62.58  ? 59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 157.340 149.967 152.419 1.00 63.58  ? 59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 158.202 149.729 151.184 1.00 65.89  ? 59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 157.712 149.782 150.049 1.00 65.27  ? 59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 157.526 151.389 152.977 1.00 61.32  ? 59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.569 152.404 151.848 1.00 60.69  ? 59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 156.410 151.724 153.953 1.00 61.29  ? 59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 159.495 149.453 151.381 1.00 68.27  ? 60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 160.401 149.300 150.247 1.00 67.61  ? 60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 160.123 148.025 149.459 1.00 69.29  ? 60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 160.339 147.996 148.242 1.00 69.09  ? 60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 161.853 149.335 150.728 1.00 65.96  ? 60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 162.338 148.056 151.395 1.00 68.07  ? 60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 163.765 148.161 151.896 1.00 71.03  ? 60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 164.097 149.177 152.543 1.00 71.14  ? 60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 164.554 147.226 151.646 1.00 69.23  ? 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 159.649 146.970 150.121 1.00 63.35  ? 61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 159.392 145.693 149.468 1.00 63.29  ? 61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 157.968 145.576 148.938 1.00 63.09  ? 61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 157.478 144.456 148.752 1.00 62.45  ? 61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 159.693 144.540 150.426 1.00 64.26  ? 61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 161.166 144.190 150.472 1.00 64.62  ? 61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 161.653 143.398 149.664 1.00 64.75  ? 61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 161.884 144.775 151.421 1.00 65.53  ? 61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 157.298 146.705 148.696 1.00 63.03  ? 62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 155.953 146.734 148.120 1.00 61.48  ? 62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 154.944 145.968 148.973 1.00 63.51  ? 62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 154.006 145.363 148.448 1.00 64.10  ? 62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 155.950 146.199 146.684 1.00 63.02  ? 62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 157.007 146.822 145.784 1.00 65.06  ? 62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 156.773 148.299 145.544 1.00 64.52  ? 62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 155.757 148.694 144.972 1.00 62.76  ? 62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.715 149.126 145.981 1.00 62.11  ? 62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 155.126 145.986 150.294 1.00 66.92  ? 63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 154.152 145.389 151.200 1.00 62.27  ? 63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 153.149 146.415 151.710 1.00 58.72  ? 63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 151.962 146.103 151.855 1.00 63.58  ? 63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 154.859 144.731 152.387 1.00 58.52  ? 63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 155.570 143.443 152.049 1.00 61.69  ? 63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 154.877 142.359 151.529 1.00 59.80  ? 63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 156.934 143.307 152.259 1.00 61.32  ? 63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 155.526 141.180 151.221 1.00 62.02  ? 63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 157.591 142.134 151.956 1.00 60.03  ? 63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 156.884 141.073 151.438 1.00 63.11  ? 63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 157.540 139.904 151.134 1.00 64.00  ? 63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 153.606 147.633 151.983 1.00 53.05  ? 64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 152.763 148.711 152.476 1.00 50.05  ? 64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 152.774 149.872 151.495 1.00 56.23  ? 64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 153.766 150.112 150.800 1.00 60.64  ? 64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 153.234 149.222 153.841 1.00 54.44  ? 64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 152.925 148.315 155.006 1.00 56.77  ? 64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 152.124 147.192 154.851 1.00 52.99  ? 64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 153.430 148.593 156.267 1.00 56.43  ? 64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 151.843 146.368 155.921 1.00 48.25  ? 64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 153.152 147.779 157.339 1.00 53.83  ? 64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 152.362 146.668 157.161 1.00 53.94  ? 64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 152.091 145.857 158.237 1.00 59.66  ? 64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 151.660 150.595 151.447 1.00 59.75  ? 65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 151.632 151.864 150.736 1.00 57.65  ? 65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 152.416 152.904 151.525 1.00 60.33  ? 65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 152.254 153.025 152.743 1.00 59.02  ? 65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 150.192 152.329 150.531 1.00 55.75  ? 65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 149.303 151.324 149.823 1.00 55.36  ? 65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 147.853 151.763 149.786 1.00 60.65  ? 65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 147.412 152.442 150.735 1.00 60.95  ? 65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 147.154 151.426 148.806 1.00 59.25  ? 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 153.276 153.651 150.834 1.00 61.05  ? 66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 154.013 154.721 151.493 1.00 60.42  ? 66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 153.160 155.965 151.694 1.00 59.84  ? 66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 153.522 156.827 152.502 1.00 60.69  ? 66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 155.268 155.067 150.688 1.00 60.64  ? 66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 156.313 155.859 151.459 1.00 61.74  ? 66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.668 155.858 150.776 1.00 63.13  ? 66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 157.786 155.257 149.688 1.00 62.00  ? 66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.614 156.455 151.330 1.00 62.09  ? 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.035 156.070 150.985 1.00 60.05  ? 67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 151.199 157.261 151.082 1.00 60.18  ? 67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 150.531 157.365 152.449 1.00 61.48  ? 67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 150.563 158.424 153.085 1.00 61.63  ? 67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 150.150 157.253 149.971 1.00 59.76  ? 67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 150.730 157.099 148.574 1.00 60.11  ? 67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 150.657 155.672 148.068 1.00 62.77  ? 67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 149.532 155.156 147.899 1.00 64.33  ? 67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 151.724 155.066 147.837 1.00 60.93  ? 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 149.927 156.271 152.922 1.00 56.23  ? 68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 149.137 156.347 154.148 1.00 53.99  ? 68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 150.017 156.443 155.390 1.00 53.69  ? 68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 149.559 156.925 156.432 1.00 55.33  ? 68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 148.193 155.145 154.244 1.00 54.75  ? 68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 148.753 153.981 155.011 1.00 51.20  ? 68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 149.641 153.105 154.413 1.00 53.81  ? 68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 148.374 153.750 156.324 1.00 48.11  ? 68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.152 152.031 155.115 1.00 54.59  ? 68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 148.882 152.679 157.028 1.00 51.22  ? 68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 149.771 151.816 156.422 1.00 55.46  ? 68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 151.269 155.994 155.306 1.00 53.34  ? 69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 152.178 156.113 156.438 1.00 52.57  ? 69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 152.883 157.461 156.488 1.00 54.56  ? 69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 153.499 157.785 157.508 1.00 55.29  ? 69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 153.223 154.996 156.399 1.00 54.01  ? 69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 152.771 153.614 156.876 1.00 55.70  ? 69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 153.852 152.576 156.619 1.00 54.24  ? 69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 152.387 153.642 158.345 1.00 52.83  ? 69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 152.807 158.251 155.414 1.00 60.90  ? 70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 153.522 159.519 155.355 1.00 56.67  ? 70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 152.839 160.631 156.140 1.00 59.03  ? 70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 153.507 161.598 156.518 1.00 58.17  ? 70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 153.699 159.955 153.899 1.00 54.66  ? 70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 152.591 159.560 153.112 1.00 56.83  ? 70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 151.531 160.525 156.392 1.00 54.54  ? 71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 150.839 161.574 157.131 1.00 53.90  ? 71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 151.191 161.583 158.611 1.00 56.29  ? 71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 150.845 162.545 159.305 1.00 57.40  ? 71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 149.320 161.447 156.977 1.00 52.37  ? 71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 148.692 161.266 155.593 1.00 56.01  ? 71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 148.651 159.808 155.188 1.00 56.60  ? 71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 147.297 161.872 155.557 1.00 57.35  ? 71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 151.864 160.549 159.107 1.00 52.87  ? 72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 152.269 160.469 160.501 1.00 54.41  ? 72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 153.784 160.549 160.605 1.00 56.57  ? 72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 154.503 159.908 159.832 1.00 54.45  ? 72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 151.795 159.166 161.151 1.00 55.16  ? 72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 150.346 158.814 160.917 1.00 50.93  ? 72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 149.964 158.072 159.809 1.00 52.08  ? 72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 149.363 159.200 161.816 1.00 49.54  ? 72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 148.645 157.740 159.593 1.00 52.08  ? 72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 148.040 158.872 161.609 1.00 51.01  ? 72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 147.687 158.141 160.497 1.00 53.83  ? 72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 146.371 157.812 160.283 1.00 57.99  ? 72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 154.264 161.336 161.561 1.00 64.13  ? 73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 155.665 161.265 161.940 1.00 62.89  ? 73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 155.949 159.908 162.572 1.00 66.19  ? 73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 155.053 159.252 163.110 1.00 66.09  ? 73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 156.019 162.390 162.910 1.00 61.05  ? 73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 155.395 162.190 164.165 1.00 62.55  ? 73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 157.211 159.475 162.489 1.00 65.48  ? 74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 157.545 158.134 162.960 1.00 63.03  ? 74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 157.264 157.956 164.445 1.00 61.13  ? 74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 156.939 156.847 164.879 1.00 61.90  ? 74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.007 157.801 162.676 1.00 63.93  ? 74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 159.414 156.457 163.200 1.00 64.97  ? 74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 158.827 155.304 162.707 1.00 62.48  ? 74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 160.350 156.348 164.213 1.00 65.31  ? 74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 159.183 154.066 163.199 1.00 61.88  ? 74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 160.711 155.111 164.708 1.00 65.09  ? 74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 160.126 153.970 164.202 1.00 64.84  ? 74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 157.386 159.020 165.241 1.00 64.99  ? 75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 157.068 158.898 166.660 1.00 68.15  ? 75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 155.588 158.601 166.865 1.00 67.25  ? 75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 155.220 157.830 167.759 1.00 65.06  ? 75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 157.484 160.166 167.410 1.00 67.30  ? 75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 156.878 161.453 166.879 1.00 67.35  ? 75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 155.648 161.881 167.654 1.00 70.10  ? 75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 155.386 161.297 168.727 1.00 68.22  ? 75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 154.944 162.804 167.193 1.00 68.00  ? 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 154.725 159.189 166.033 1.00 63.74  ? 76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 153.294 158.926 166.134 1.00 61.81  ? 76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 152.976 157.470 165.815 1.00 61.46  ? 76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 152.209 156.818 166.533 1.00 66.02  ? 76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 152.529 159.863 165.200 1.00 64.60  ? 76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 152.599 161.310 165.643 1.00 65.83  ? 76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 152.267 161.593 166.814 1.00 62.35  ? 76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 152.984 162.167 164.820 1.00 68.45  ? 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 153.565 156.939 164.740 1.00 54.30  ? 77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 153.356 155.537 164.384 1.00 55.23  ? 77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 153.906 154.626 165.473 1.00 55.69  ? 77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 153.291 153.612 165.830 1.00 56.62  ? 77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 153.999 155.235 163.018 1.00 55.51  ? 77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 153.308 156.033 161.914 1.00 58.23  ? 77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 153.936 153.749 162.713 1.00 54.46  ? 77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 154.039 156.000 160.594 1.00 55.10  ? 77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 155.077 154.971 166.009 1.00 60.08  ? 78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 155.669 154.185 167.083 1.00 58.26  ? 78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 154.752 154.139 168.297 1.00 57.82  ? 78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 154.534 153.072 168.876 1.00 60.15  ? 78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 157.030 154.770 167.459 1.00 61.02  ? 78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 157.955 153.819 168.194 1.00 59.79  ? 78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 159.207 154.548 168.653 1.00 61.12  ? 78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 159.809 153.910 169.892 1.00 60.93  ? 78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 161.037 153.136 169.564 1.00 59.12  ? 78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 154.187 155.285 168.682 1.00 60.19  ? 79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 153.304 155.318 169.842 1.00 60.16  ? 79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 151.984 154.608 169.563 1.00 57.12  ? 79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 151.401 154.010 170.475 1.00 61.73  ? 79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.084 156.767 170.283 1.00 58.37  ? 79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 151.775 157.400 169.850 1.00 60.95  ? 79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 151.557 158.758 170.493 1.00 64.61  ? 79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 152.342 159.685 170.204 1.00 63.00  ? 79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 150.608 158.898 171.291 1.00 63.21  ? 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 151.514 154.631 168.313 1.00 50.02  ? 80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 150.327 153.859 167.950 1.00 49.76  ? 80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 150.596 152.368 168.120 1.00 54.03  ? 80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 149.775 151.627 168.676 1.00 55.58  ? 80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 149.886 154.195 166.514 1.00 50.31  ? 80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 148.923 153.145 165.989 1.00 49.93  ? 80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 149.243 155.572 166.468 1.00 52.55  ? 80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 151.757 151.906 167.652 1.00 54.67  ? 81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 152.115 150.503 167.842 1.00 49.73  ? 81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 152.266 150.163 169.322 1.00 51.67  ? 81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 151.831 149.095 169.765 1.00 55.57  ? 81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 153.395 150.165 167.079 1.00 49.40  ? 81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 153.173 149.858 165.624 1.00 47.88  ? 81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 152.683 150.821 164.758 1.00 50.28  ? 81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 153.446 148.596 165.123 1.00 49.58  ? 81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 152.481 150.534 163.422 1.00 51.34  ? 81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 153.242 148.304 163.789 1.00 48.29  ? 81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 152.758 149.274 162.939 1.00 47.21  ? 81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 152.883 151.055 170.102 1.00 54.48  ? 82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 153.045 150.803 171.532 1.00 56.09  ? 82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 151.695 150.677 172.227 1.00 57.50  ? 82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 151.496 149.787 173.061 1.00 58.93  ? 82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 153.879 151.908 172.182 1.00 56.07  ? 82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 155.274 152.075 171.615 1.00 55.95  ? 82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 156.306 151.367 172.470 1.00 57.88  ? 82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 156.826 152.285 173.565 1.00 55.70  ? 82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 158.302 152.180 173.725 1.00 57.34  ? 82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 150.752 151.562 171.897 1.00 51.81  ? 83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 149.422 151.455 172.485 1.00 55.03  ? 83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 148.638 150.281 171.910 1.00 53.34  ? 83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 147.625 149.885 172.494 1.00 55.74  ? 83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 148.649 152.764 172.301 1.00 55.62  ? 83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 147.673 152.894 173.343 1.00 57.84  ? 83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 147.950 152.804 170.957 1.00 52.33  ? 83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 149.081 149.720 170.782 1.00 46.83  ? 84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 148.512 148.459 170.315 1.00 45.30  ? 84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 149.040 147.286 171.131 1.00 46.90  ? 84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 148.297 146.352 171.448 1.00 46.95  ? 84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 148.810 148.262 168.830 1.00 45.47  ? 84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 150.328 147.317 171.474 1.00 50.45  ? 85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 150.922 146.283 172.310 1.00 50.01  ? 85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 150.734 146.544 173.797 1.00 51.79  ? 85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 150.995 145.644 174.602 1.00 51.71  ? 85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 152.412 146.144 171.993 1.00 49.71  ? 85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 152.693 145.476 170.668 1.00 52.60  ? 85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 152.959 144.117 170.597 1.00 51.96  ? 85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 152.682 146.203 169.487 1.00 51.32  ? 85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 153.216 143.504 169.389 1.00 50.80  ? 85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 152.935 145.600 168.276 1.00 48.67  ? 85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 153.202 144.251 168.232 1.00 49.41  ? 85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 153.455 143.648 167.025 1.00 50.86  ? 85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 150.297 147.746 174.181 1.00 53.60  ? 86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 149.994 148.012 175.582 1.00 54.42  ? 86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 148.849 147.148 176.084 1.00 57.27  ? 86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 148.808 146.815 177.275 1.00 57.73  ? 86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 149.659 149.491 175.778 1.00 53.09  ? 86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 147.919 146.781 175.205 1.00 56.04  ? 87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 146.842 145.865 175.550 1.00 56.41  ? 87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 147.342 144.471 175.895 1.00 58.09  ? 87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 146.745 143.810 176.755 1.00 55.32  ? 87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 145.841 145.782 174.392 1.00 52.17  ? 87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 144.797 144.682 174.519 1.00 56.37  ? 87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 143.573 145.158 175.280 1.00 56.54  ? 87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 142.779 143.985 175.832 1.00 57.13  ? 87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 143.660 142.850 176.225 1.00 57.16  ? 87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 148.430 144.026 175.269 1.00 58.01  ? 88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 148.949 142.670 175.430 1.00 55.50  ? 88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 147.864 141.646 175.103 1.00 51.33  ? 88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 147.556 140.743 175.882 1.00 53.04  ? 88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 149.512 142.460 176.838 1.00 58.72  ? 88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 150.996 142.766 176.968 1.00 55.01  ? 88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 151.666 141.845 177.975 1.00 58.58  ? 88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 153.178 141.860 177.819 1.00 58.03  ? 88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 153.689 140.600 177.211 1.00 56.01  ? 88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 147.277 141.820 173.921 1.00 50.13  ? 89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 146.160 140.985 173.500 1.00 51.94  ? 89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 146.598 139.534 173.361 1.00 54.59  ? 89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 147.614 139.235 172.726 1.00 53.93  ? 89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 145.589 141.494 172.176 1.00 48.29  ? 89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 144.513 140.615 171.602 1.00 48.18  ? 89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 143.201 140.740 172.023 1.00 48.45  ? 89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 144.814 139.667 170.637 1.00 47.60  ? 89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 142.211 139.935 171.496 1.00 49.08  ? 89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 143.827 138.858 170.110 1.00 47.70  ? 89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.525 138.992 170.539 1.00 48.11  ? 89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 145.824 138.633 173.957 1.00 51.05  ? 90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 146.056 137.200 173.871 1.00 47.24  ? 90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 144.842 136.548 173.226 1.00 51.96  ? 90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 143.712 136.759 173.674 1.00 54.96  ? 90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 146.312 136.599 175.255 1.00 50.87  ? 90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 147.579 137.098 175.934 1.00 52.93  ? 90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 148.827 136.635 175.201 1.00 53.65  ? 90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 149.435 137.699 174.413 1.00 55.54  ? 90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 150.472 138.424 174.808 1.00 55.42  ? 90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.045 138.228 175.984 1.00 53.49  ? 90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 150.947 139.371 174.004 1.00 55.46  ? 90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 145.078 135.769 172.174 1.00 49.38  ? 91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 143.992 135.059 171.526 1.00 46.68  ? 91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 143.408 134.016 172.479 1.00 53.02  ? 91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 144.148 133.285 173.141 1.00 54.60  ? 91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 144.479 134.386 170.246 1.00 46.05  ? 91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.618 135.327 169.081 1.00 49.63  ? 91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.518 135.679 168.320 1.00 51.26  ? 91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 145.852 135.857 168.748 1.00 51.47  ? 91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 143.645 136.542 167.248 1.00 47.23  ? 91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 145.986 136.719 167.678 1.00 46.72  ? 91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 144.880 137.061 166.927 1.00 44.93  ? 91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.080 133.929 172.566 1.00 54.77  ? 92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 141.465 133.036 173.555 1.00 51.50  ? 92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 141.358 131.598 173.077 1.00 50.66  ? 92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 141.203 130.678 173.886 1.00 54.12  ? 92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 140.077 133.661 173.772 1.00 53.59  ? 92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 139.999 134.858 172.804 1.00 53.97  ? 92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 141.057 134.627 171.781 1.00 54.78  ? 92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 141.437 131.392 171.765 1.00 48.68  ? 93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 141.278 130.068 171.187 1.00 51.66  ? 93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 142.350 129.857 170.129 1.00 53.74  ? 93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 142.857 130.808 169.529 1.00 56.28  ? 93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 139.879 129.888 170.588 1.00 53.64  ? 93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 139.697 130.726 169.459 1.00 55.48  ? 93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 142.689 128.586 169.905 1.00 53.44  ? 94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 143.657 128.243 168.870 1.00 51.74  ? 94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 143.150 128.614 167.482 1.00 55.53  ? 94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 143.928 129.072 166.637 1.00 58.24  ? 94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 143.988 126.752 168.928 1.00 54.01  ? 94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 144.550 126.209 167.646 1.00 54.13  ? 94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 145.855 126.477 167.277 1.00 53.68  ? 94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 143.769 125.431 166.808 1.00 58.39  ? 94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 146.369 125.981 166.096 1.00 55.42  ? 94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 144.279 124.932 165.627 1.00 56.73  ? 94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 145.581 125.207 165.271 1.00 53.20  ? 94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 141.855 128.414 167.230 1.00 51.89  ? 95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 141.314 128.683 165.904 1.00 48.59  ? 95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 141.393 130.160 165.553 1.00 52.09  ? 95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 141.575 130.502 164.383 1.00 59.87  ? 95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 139.869 128.199 165.814 1.00 52.98  ? 95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 139.366 127.996 164.394 1.00 54.38  ? 95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 140.196 126.645 163.538 1.00 63.65  ? 95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 140.256 125.413 164.836 1.00 57.17  ? 95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 141.275 131.046 166.543 1.00 41.63  ? 96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 141.387 132.476 166.272 1.00 39.84  ? 96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 142.760 132.821 165.709 1.00 48.48  ? 96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 142.875 133.443 164.644 1.00 48.52  ? 96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.121 133.266 167.553 1.00 44.53  ? 96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 140.028 132.723 168.269 1.00 49.63  ? 96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 143.817 132.405 166.410 1.00 51.32  ? 97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.171 132.683 165.952 1.00 46.57  ? 97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 145.463 131.976 164.637 1.00 46.89  ? 97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.106 132.546 163.748 1.00 56.22  ? 97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.180 132.266 167.020 1.00 46.32  ? 97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.008 130.729 164.499 1.00 44.60  ? 98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 145.256 129.988 163.266 1.00 47.48  ? 98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 144.610 130.697 162.082 1.00 48.74  ? 98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.251 130.907 161.045 1.00 56.78  ? 98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 144.755 128.544 163.431 1.00 52.32  ? 98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 144.705 127.727 162.152 1.00 55.03  ? 98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 143.817 128.018 161.122 1.00 55.11  ? 98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.569 126.658 161.987 1.00 54.28  ? 98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 143.794 127.261 159.969 1.00 54.66  ? 98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.550 125.899 160.835 1.00 56.18  ? 98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 144.661 126.201 159.825 1.00 56.89  ? 98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 143.345 131.097 162.228 1.00 49.07  ? 99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 142.651 131.781 161.147 1.00 48.69  ? 99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.316 133.108 160.818 1.00 51.26  ? 99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.502 133.438 159.641 1.00 55.98  ? 99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.184 131.996 161.516 1.00 47.08  ? 99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 140.283 130.835 161.149 1.00 52.42  ? 99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 140.309 130.572 159.655 1.00 53.92  ? 99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 139.379 129.431 159.285 1.00 52.95  ? 99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.193 128.488 160.423 1.00 51.67  ? 99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.695 133.881 161.841 1.00 47.65  ? 100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.330 135.164 161.566 1.00 44.29  ? 100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.649 134.980 160.829 1.00 46.52  ? 100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 145.865 135.572 159.766 1.00 52.84  ? 100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.559 135.951 162.854 1.00 42.92  ? 100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 145.347 137.205 162.639 1.00 46.24  ? 100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 144.779 138.288 161.991 1.00 48.09  ? 100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 146.668 137.288 163.038 1.00 46.51  ? 100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 145.504 139.439 161.771 1.00 47.47  ? 100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 147.398 138.436 162.818 1.00 47.72  ? 100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 146.815 139.513 162.183 1.00 45.83  ? 100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.535 134.145 161.363 1.00 44.73  ? 101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 147.858 133.988 160.775 1.00 46.17  ? 101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 147.853 133.129 159.518 1.00 46.38  ? 101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 148.903 132.991 158.883 1.00 52.15  ? 101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 148.825 133.412 161.812 1.00 44.33  ? 101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.173 134.400 162.903 1.00 45.11  ? 101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 150.070 135.433 162.670 1.00 47.62  ? 101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.592 134.310 164.160 1.00 45.93  ? 101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.384 136.344 163.661 1.00 43.73  ? 101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 148.900 135.215 165.155 1.00 47.08  ? 101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 149.797 136.230 164.900 1.00 46.16  ? 101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 150.108 137.132 165.890 1.00 47.80  ? 101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 146.711 132.554 159.143 1.00 50.89  ? 102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 146.604 131.854 157.872 1.00 53.25  ? 102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 145.884 132.656 156.796 1.00 54.11  ? 102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.114 132.412 155.608 1.00 55.04  ? 102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 145.881 130.517 158.065 1.00 52.84  ? 102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 146.840 129.355 158.224 1.00 56.03  ? 102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 147.810 129.434 158.978 1.00 57.97  ? 102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 146.572 128.266 157.516 1.00 53.24  ? 102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 145.022 133.604 157.171 1.00 54.16  ? 103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 144.225 134.334 156.195 1.00 55.76  ? 103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 144.554 135.816 156.094 1.00 57.34  ? 103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 144.480 136.370 154.996 1.00 59.16  ? 103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.731 134.193 156.518 1.00 58.87  ? 103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.259 132.750 156.503 1.00 62.54  ? 103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.095 131.844 156.315 1.00 59.20  ? 103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.044 132.522 156.685 1.00 62.35  ? 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 144.915 136.472 157.195 1.00 49.48  ? 104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 145.041 137.922 157.217 1.00 50.36  ? 104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 146.438 138.427 157.533 1.00 54.20  ? 104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 146.802 139.506 157.060 1.00 58.37  ? 104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 144.062 138.527 158.238 1.00 51.68  ? 104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 142.671 137.944 158.161 1.00 52.77  ? 104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 141.742 138.439 157.257 1.00 51.46  ? 104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 142.289 136.897 158.986 1.00 51.54  ? 104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 140.472 137.908 157.180 1.00 52.15  ? 104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.022 136.360 158.915 1.00 53.00  ? 104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 140.117 136.869 158.011 1.00 53.59  ? 104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 138.853 136.337 157.938 1.00 51.67  ? 104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 147.222 137.696 158.322 1.00 53.46  ? 105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 148.558 138.158 158.676 1.00 47.94  ? 105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 149.434 138.259 157.435 1.00 54.61  ? 105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 149.455 137.352 156.598 1.00 54.54  ? 105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 149.192 137.214 159.696 1.00 44.45  ? 105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 150.154 139.373 157.317 1.00 56.73  ? 106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 151.035 139.577 156.176 1.00 50.32  ? 106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 152.192 138.590 156.221 1.00 53.90  ? 106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 152.842 138.423 157.257 1.00 54.27  ? 106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 151.566 141.008 156.160 1.00 51.90  ? 106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 152.354 141.445 154.923 1.00 55.36  ? 106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 151.604 141.097 153.648 1.00 53.78  ? 106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 152.659 142.931 154.980 1.00 54.37  ? 106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 152.448 137.939 155.093 1.00 64.20  ? 107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 153.553 137.009 154.953 1.00 64.29  ? 107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 154.466 137.470 153.826 1.00 62.73  ? 107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 154.086 138.290 152.986 1.00 59.74  ? 107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 153.054 135.584 154.685 1.00 59.97  ? 107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 152.478 134.894 155.910 1.00 59.11  ? 107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 151.909 133.532 155.562 1.00 63.30  ? 107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.362 132.836 156.797 1.00 61.77  ? 107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.521 131.659 156.447 1.00 57.87  ? 107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 155.683 136.935 153.822 1.00 67.14  ? 108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 156.652 137.293 152.801 1.00 68.34  ? 108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 156.198 136.784 151.433 1.00 69.64  ? 108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 155.234 136.023 151.307 1.00 68.15  ? 108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 158.030 136.737 153.154 1.00 68.61  ? 108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 157.923 135.334 153.427 1.00 69.99  ? 108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 158.589 137.443 154.378 1.00 65.33  ? 108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 156.912 137.224 150.393 1.00 71.03  ? 109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 156.526 136.884 149.026 1.00 71.19  ? 109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 156.528 135.378 148.790 1.00 72.23  ? 109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 155.782 134.886 147.936 1.00 73.23  ? 109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 157.454 137.580 148.031 1.00 71.09  ? 109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 157.252 139.082 147.998 1.00 71.09  ? 109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 156.288 139.601 148.560 1.00 72.51  ? 109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 158.163 139.788 147.338 1.00 70.48  ? 109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 157.350 134.635 149.525 1.00 73.95  ? 110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 157.359 133.181 149.433 1.00 75.11  ? 110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.382 132.524 150.398 1.00 75.35  ? 110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.321 131.290 150.447 1.00 73.44  ? 110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.773 132.642 149.682 1.00 76.10  ? 110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 159.368 133.138 150.982 1.00 76.83  ? 110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.844 134.125 151.536 1.00 75.38  ? 110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.360 132.543 151.451 1.00 74.99  ? 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.618 133.316 151.156 1.00 75.74  ? 111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.626 132.807 152.107 1.00 76.33  ? 111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.257 131.839 153.106 1.00 74.86  ? 111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 154.658 130.830 153.484 1.00 75.53  ? 111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.447 132.151 151.383 1.00 74.56  ? 111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 152.992 132.884 150.131 1.00 73.26  ? 111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 152.350 134.218 150.473 1.00 75.30  ? 111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 150.962 134.029 151.060 1.00 76.18  ? 111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 150.343 135.326 151.450 1.00 73.37  ? 111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.477 132.150 153.539 1.00 70.04  ? 112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.215 131.294 154.457 1.00 72.32  ? 112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.379 131.883 155.849 1.00 70.67  ? 112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 157.483 131.125 156.815 1.00 69.60  ? 112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 158.604 130.976 153.888 1.00 71.49  ? 112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 158.575 130.047 152.685 1.00 72.27  ? 112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 159.532 128.881 152.857 1.00 71.85  ? 112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 160.335 128.639 151.590 1.00 70.62  ? 112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.225 127.451 151.712 1.00 68.19  ? 112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.400 133.207 155.976 1.00 65.74  ? 113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.571 133.869 157.260 1.00 66.37  ? 113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 156.453 134.880 157.476 1.00 64.74  ? 113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 155.881 135.413 156.522 1.00 63.98  ? 113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 158.932 134.568 157.348 1.00 64.21  ? 113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 160.079 133.643 157.719 1.00 64.00  ? 113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 160.526 133.869 159.154 1.00 65.45  ? 113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.677 132.951 159.526 1.00 63.84  ? 113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.624 132.551 160.959 1.00 64.09  ? 113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 156.149 135.138 158.744 1.00 59.51  ? 114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 155.062 136.035 159.119 1.00 56.78  ? 114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 155.635 137.426 159.353 1.00 56.80  ? 114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 156.535 137.606 160.180 1.00 57.26  ? 114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 154.327 135.523 160.367 1.00 56.01  ? 114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.430 134.338 160.005 1.00 55.41  ? 114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.509 136.634 160.999 1.00 56.98  ? 114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.003 133.515 161.193 1.00 54.26  ? 114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 155.114 138.410 158.622 1.00 53.92  ? 115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 155.585 139.784 158.740 1.00 53.80  ? 115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 154.746 140.620 159.694 1.00 55.54  ? 115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 155.246 141.613 160.235 1.00 52.52  ? 115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 155.601 140.455 157.365 1.00 55.27  ? 115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 156.632 139.952 156.354 1.00 54.89  ? 115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 156.305 140.466 154.965 1.00 55.11  ? 115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 158.029 140.379 156.767 1.00 54.27  ? 115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 153.488 140.249 159.914 1.00 54.69  ? 116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 152.558 141.044 160.703 1.00 50.61  ? 116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 152.033 140.238 161.880 1.00 49.65  ? 116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 151.555 139.113 161.703 1.00 53.95  ? 116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 151.383 141.524 159.848 1.00 51.62  ? 116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 151.498 142.955 159.370 1.00 51.78  ? 116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 150.374 143.338 158.430 1.00 52.98  ? 116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 149.560 142.456 158.090 1.00 51.97  ? 116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 150.304 144.518 158.030 1.00 56.07  ? 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 152.117 140.819 163.073 1.00 44.56  ? 117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 151.381 140.310 164.215 1.00 45.28  ? 117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 149.933 140.786 164.139 1.00 47.69  ? 117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 149.536 141.510 163.223 1.00 53.16  ? 117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 152.024 140.777 165.521 1.00 47.26  ? 117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 153.537 140.902 165.471 1.00 50.28  ? 117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.238 139.569 165.610 1.00 54.95  ? 117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 153.944 138.937 166.891 1.00 54.58  ? 117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 153.735 137.639 167.053 1.00 50.20  ? 117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 153.785 136.801 166.032 1.00 48.10  ? 117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 153.473 137.171 168.269 1.00 47.06  ? 117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 149.126 140.363 165.115 1.00 47.70  ? 118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 147.777 140.908 165.215 1.00 43.18  ? 118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 147.817 142.391 165.550 1.00 45.72  ? 118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 147.069 143.191 164.975 1.00 48.62  ? 118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 146.971 140.136 166.258 1.00 43.55  ? 118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 145.490 140.442 166.234 1.00 42.94  ? 118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 144.773 140.394 165.047 1.00 40.64  ? 118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 144.810 140.773 167.397 1.00 42.28  ? 118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 143.419 140.668 165.019 1.00 39.38  ? 118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 143.457 141.047 167.378 1.00 40.71  ? 118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 142.767 140.994 166.187 1.00 43.10  ? 118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 141.420 141.269 166.163 1.00 44.67  ? 118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 148.705 142.778 166.464 1.00 44.60  ? 119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 148.854 144.167 166.872 1.00 43.46  ? 119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 149.485 145.039 165.796 1.00 46.23  ? 119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 149.359 146.265 165.869 1.00 49.65  ? 119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 149.685 144.244 168.155 1.00 46.31  ? 119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 149.058 143.530 169.339 1.00 48.03  ? 119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 149.639 142.149 169.560 1.00 52.23  ? 119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 149.782 141.398 168.573 1.00 50.82  ? 119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 149.950 141.812 170.722 1.00 50.86  ? 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 150.158 144.451 164.809 1.00 46.30  ? 120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 150.653 145.196 163.657 1.00 43.31  ? 120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 149.607 145.368 162.572 1.00 45.22  ? 120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 149.498 146.451 161.996 1.00 51.43  ? 120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 151.886 144.515 163.057 1.00 42.91  ? 120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 152.980 144.290 164.073 1.00 52.46  ? 120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 152.940 144.930 165.144 1.00 54.83  ? 120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 153.893 143.489 163.793 1.00 56.53  ? 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 148.829 144.322 162.282 1.00 42.91  ? 121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 147.684 144.481 161.394 1.00 41.08  ? 121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 146.720 145.525 161.937 1.00 43.12  ? 121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 146.260 146.402 161.198 1.00 46.61  ? 121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 146.973 143.141 161.212 1.00 36.65  ? 121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 145.934 143.129 160.105 1.00 36.11  ? 121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 146.583 143.224 158.740 1.00 41.75  ? 121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 145.889 144.164 157.868 1.00 43.85  ? 121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 146.492 145.095 157.143 1.00 41.82  ? 121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 147.808 145.236 157.155 1.00 39.24  ? 121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 145.758 145.905 156.387 1.00 40.97  ? 121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 146.421 145.456 163.236 1.00 43.82  ? 122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 145.508 146.419 163.843 1.00 42.74  ? 122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 146.093 147.824 163.792 1.00 40.76  ? 122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 145.383 148.791 163.496 1.00 42.60  ? 122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 145.164 145.989 165.280 1.00 38.53  ? 122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 144.197 144.804 165.248 1.00 34.56  ? 122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 144.591 147.152 166.074 1.00 37.63  ? 122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 143.639 144.437 166.593 1.00 41.92  ? 122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 147.391 147.964 164.071 1.00 42.66  ? 123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 148.016 149.283 164.026 1.00 40.69  ? 123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 147.991 149.865 162.618 1.00 44.21  ? 123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 147.711 151.054 162.439 1.00 49.44  ? 123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 149.451 149.205 164.541 1.00 43.68  ? 123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 149.521 148.464 165.744 1.00 48.95  ? 123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 148.285 149.044 161.608 1.00 42.97  ? 124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 148.284 149.526 160.229 1.00 40.40  ? 124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 146.878 149.928 159.806 1.00 44.23  ? 124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 146.678 150.972 159.170 1.00 47.81  ? 124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 148.878 148.455 159.294 1.00 43.12  ? 124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 150.399 148.394 159.454 1.00 40.66  ? 124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 148.510 148.738 157.848 1.00 40.99  ? 124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 151.051 149.733 159.727 1.00 42.48  ? 124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 145.878 149.115 160.157 1.00 39.57  ? 125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 144.501 149.442 159.803 1.00 34.81  ? 125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 144.054 150.715 160.513 1.00 33.35  ? 125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 143.354 151.553 159.933 1.00 44.99  ? 125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 143.575 148.250 160.116 1.00 35.26  ? 125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 142.132 148.627 159.900 1.00 36.83  ? 125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 143.930 147.066 159.235 1.00 36.85  ? 125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 144.469 150.895 161.769 1.00 28.84  ? 126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 144.122 152.106 162.504 1.00 31.16  ? 126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 144.773 153.338 161.891 1.00 38.81  ? 126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 144.138 154.393 161.780 1.00 47.13  ? 126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 144.533 151.962 163.967 1.00 38.34  ? 126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 146.046 153.228 161.504 1.00 39.45  ? 127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 146.722 154.348 160.860 1.00 32.49  ? 127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 146.086 154.684 159.521 1.00 34.02  ? 127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 146.009 155.860 159.150 1.00 41.58  ? 127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 148.207 154.036 160.680 1.00 39.95  ? 127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 149.053 153.980 161.954 1.00 41.46  ? 127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 150.438 153.446 161.645 1.00 42.75  ? 127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 149.137 155.346 162.610 1.00 39.75  ? 127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 145.634 153.670 158.780 1.00 37.75  ? 128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 144.893 153.933 157.551 1.00 37.33  ? 128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 143.580 154.648 157.845 1.00 38.09  ? 128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 143.211 155.598 157.147 1.00 48.49  ? 128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 144.635 152.626 156.802 1.00 34.96  ? 128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 143.891 152.806 155.511 1.00 40.61  ? 128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 144.565 153.153 154.353 1.00 41.41  ? 128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 142.518 152.633 155.454 1.00 40.59  ? 128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 143.886 153.322 153.164 1.00 42.12  ? 128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 141.834 152.804 154.269 1.00 39.57  ? 128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 142.518 153.147 153.122 1.00 44.64  ? 128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 142.862 154.200 158.878 1.00 33.09  ? 129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 141.565 154.788 159.199 1.00 28.64  ? 129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 141.696 156.244 159.625 1.00 34.25  ? 129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 140.911 157.097 159.197 1.00 36.73  ? 129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 140.884 153.984 160.306 1.00 30.85  ? 129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 140.287 152.689 159.846 1.00 29.46  ? 129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 140.114 152.425 158.500 1.00 34.31  ? 129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 139.883 151.740 160.768 1.00 28.56  ? 129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 139.559 151.233 158.084 1.00 36.94  ? 129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 139.325 150.550 160.358 1.00 33.29  ? 129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 139.163 150.295 159.014 1.00 36.64  ? 129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 142.678 156.545 160.477 1.00 43.61  ? 130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 142.772 157.881 161.059 1.00 43.54  ? 130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 143.131 158.929 160.013 1.00 52.08  ? 130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 142.611 160.051 160.052 1.00 56.60  ? 130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 143.790 157.885 162.194 1.00 39.12  ? 130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.024 158.587 159.084 1.00 53.02  ? 131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 144.439 159.478 158.001 1.00 51.19  ? 131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 145.072 160.761 158.547 1.00 52.30  ? 131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 144.590 161.872 158.323 1.00 55.24  ? 131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 143.262 159.794 157.071 1.00 49.89  ? 131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 143.708 160.343 155.732 1.00 55.79  ? 131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 144.565 159.765 155.065 1.00 57.32  ? 131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.127 161.469 155.331 1.00 52.23  ? 131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 146.171 160.584 159.276 1.00 49.51  ? 132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 146.968 161.692 159.758 1.00 52.55  ? 132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 146.726 162.095 161.197 1.00 55.13  ? 132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 147.454 162.954 161.709 1.00 57.29  ? 132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 145.735 161.509 161.865 1.00 55.83  ? 133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 145.409 161.849 163.246 1.00 56.63  ? 133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 145.988 160.776 164.163 1.00 55.65  ? 133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 145.612 159.604 164.072 1.00 58.36  ? 133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 143.899 161.976 163.429 1.00 55.75  ? 133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 143.526 162.773 164.664 1.00 60.13  ? 133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 144.433 163.121 165.448 1.00 61.26  ? 133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 142.323 163.052 164.850 1.00 57.82  ? 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 146.906 161.178 165.044 1.00 54.15  ? 134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 147.520 160.217 165.955 1.00 55.81  ? 134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 146.548 159.783 167.044 1.00 57.09  ? 134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 146.463 158.592 167.370 1.00 61.48  ? 134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 148.782 160.812 166.574 1.00 61.50  ? 134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 149.610 161.352 165.539 1.00 61.43  ? 134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 149.555 159.745 167.334 1.00 59.21  ? 134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 145.815 160.734 167.627 1.00 57.79  ? 135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 144.849 160.391 168.666 1.00 57.45  ? 135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 143.739 159.507 168.115 1.00 57.89  ? 135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 143.324 158.541 168.765 1.00 62.94  ? 135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 144.270 161.663 169.285 1.00 58.02  ? 135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 145.267 162.450 170.117 1.00 59.82  ? 135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 145.943 161.597 171.173 1.00 65.31  ? 135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 145.229 161.018 172.018 1.00 62.72  ? 135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 147.188 161.505 171.158 1.00 65.91  ? 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 143.251 159.817 166.913 1.00 43.44  ? 136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 142.236 158.972 166.292 1.00 42.59  ? 136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 142.800 157.598 165.953 1.00 45.89  ? 136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 142.092 156.588 166.051 1.00 48.99  ? 136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 141.679 159.654 165.045 1.00 46.91  ? 136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 140.428 159.004 164.489 1.00 46.89  ? 136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 139.201 159.392 165.294 1.00 46.08  ? 136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 137.941 159.312 164.449 1.00 47.04  ? 136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 138.232 159.505 163.003 1.00 51.41  ? 136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 144.073 157.537 165.552 1.00 46.91  ? 137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 144.700 156.247 165.286 1.00 46.02  ? 137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 144.781 155.403 166.550 1.00 46.98  ? 137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 144.522 154.195 166.517 1.00 49.04  ? 137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 146.090 156.450 164.685 1.00 42.83  ? 137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 145.130 156.024 167.679 1.00 47.90  ? 138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 145.154 155.285 168.937 1.00 47.16  ? 138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 143.753 154.886 169.377 1.00 46.23  ? 138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 143.574 153.818 169.974 1.00 48.39  ? 138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 145.838 156.112 170.024 1.00 49.87  ? 138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 147.339 156.237 169.845 1.00 50.09  ? 138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 147.904 157.334 170.723 1.00 51.49  ? 138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.269 156.798 172.097 1.00 53.36  ? 138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 148.745 157.874 173.008 1.00 49.85  ? 138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 142.751 155.721 169.095 1.00 45.17  ? 139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 141.371 155.344 169.384 1.00 41.91  ? 139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 140.956 154.120 168.578 1.00 43.88  ? 139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 140.324 153.199 169.111 1.00 50.81  ? 139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 140.437 156.518 169.096 1.00 42.49  ? 139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 139.781 157.113 170.329 1.00 48.55  ? 139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 138.540 157.917 169.996 1.00 54.41  ? 139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 138.658 158.913 169.251 1.00 50.54  ? 139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 137.447 157.553 170.478 1.00 52.88  ? 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 141.313 154.086 167.293 1.00 36.91  ? 140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 141.025 152.916 166.467 1.00 35.56  ? 140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 141.782 151.691 166.962 1.00 33.35  ? 140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 141.257 150.571 166.936 1.00 36.14  ? 140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 141.381 153.201 165.011 1.00 37.94  ? 140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 140.375 154.047 164.274 1.00 37.68  ? 140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 139.037 153.690 164.230 1.00 37.28  ? 140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 140.768 155.201 163.616 1.00 38.08  ? 140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 138.118 154.462 163.553 1.00 36.30  ? 140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 139.857 155.979 162.939 1.00 37.36  ? 140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 138.536 155.605 162.910 1.00 35.85  ? 140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 137.632 156.383 162.231 1.00 39.91  ? 140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 143.030 151.883 167.392 1.00 43.27  ? 141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 143.814 150.777 167.933 1.00 41.27  ? 141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 143.147 150.205 169.174 1.00 42.39  ? 141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 143.048 148.985 169.337 1.00 44.04  ? 141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 145.254 151.235 168.226 1.00 38.01  ? 141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 146.024 150.129 168.896 1.00 41.49  ? 141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 145.947 151.642 166.944 1.00 45.49  ? 141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 142.684 151.075 170.073 1.00 44.53  ? 142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 141.983 150.602 171.262 1.00 39.62  ? 142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 140.679 149.914 170.886 1.00 40.77  ? 142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 140.280 148.931 171.520 1.00 52.08  ? 142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 141.723 151.766 172.216 1.00 41.78  ? 142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 142.992 152.279 172.865 1.00 44.67  ? 142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 143.826 151.499 173.326 1.00 41.43  ? 142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 143.146 153.597 172.906 1.00 41.83  ? 142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 139.999 150.424 169.858 1.00 33.29  ? 143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 138.750 149.821 169.410 1.00 32.32  ? 143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 138.965 148.404 168.891 1.00 35.04  ? 143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 138.189 147.495 169.204 1.00 41.42  ? 143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 138.123 150.696 168.327 1.00 32.58  ? 143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 136.648 150.482 168.007 1.00 35.40  ? 143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 135.804 151.095 169.100 1.00 38.06  ? 143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 136.321 151.099 166.662 1.00 31.47  ? 143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 140.015 148.198 168.094 1.00 34.35  ? 144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 140.210 146.902 167.449 1.00 24.65  ? 144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 140.944 145.912 168.348 1.00 31.76  ? 144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 140.672 144.708 168.290 1.00 37.83  ? 144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 140.959 147.079 166.130 1.00 30.07  ? 144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 140.283 148.029 165.159 1.00 35.18  ? 144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.050 148.005 163.530 1.00 43.18  ? 144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 141.437 149.739 163.326 1.00 37.35  ? 144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 141.884 146.387 169.166 1.00 32.80  ? 145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 142.610 145.484 170.056 1.00 31.98  ? 145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 141.705 145.001 171.183 1.00 41.83  ? 145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 141.848 143.869 171.659 1.00 43.06  ? 145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 143.895 146.158 170.580 1.00 35.05  ? 145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 144.961 145.103 170.876 1.00 38.83  ? 145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 143.624 147.009 171.811 1.00 36.62  ? 145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 145.565 144.480 169.643 1.00 35.27  ? 145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 140.764 145.837 171.627 1.00 41.60  ? 146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 139.703 145.364 172.504 1.00 36.49  ? 146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 138.705 144.489 171.764 1.00 38.97  ? 146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 137.840 143.884 172.406 1.00 46.31  ? 146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 138.975 146.545 173.147 1.00 32.00  ? 146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 139.853 147.315 174.109 1.00 41.99  ? 146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 140.850 146.796 174.609 1.00 46.04  ? 146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 139.487 148.563 174.374 1.00 44.36  ? 146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 138.811 144.421 170.436 1.00 34.26  ? 147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 137.940 143.610 169.592 1.00 31.61  ? 147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 136.480 144.020 169.736 1.00 33.24  ? 147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 135.580 143.187 169.646 1.00 43.62  ? 147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 138.118 142.116 169.883 1.00 28.62  ? 147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 139.428 141.552 169.361 1.00 26.18  ? 147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 139.467 140.042 169.397 1.00 37.83  ? 147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 139.978 139.401 168.479 1.00 42.09  ? 147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 138.925 139.461 170.460 1.00 42.66  ? 147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 136.240 145.311 169.970 1.00 33.14  ? 148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 134.879 145.829 169.978 1.00 31.40  ? 148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 134.329 145.993 168.570 1.00 30.93  ? 148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 133.129 145.800 168.349 1.00 40.63  ? 148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 134.831 147.167 170.714 1.00 30.88  ? 148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 135.349 147.111 172.136 1.00 31.42  ? 148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 135.573 148.489 172.722 1.00 39.90  ? 148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 136.629 149.093 172.439 1.00 41.03  ? 148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 134.693 148.971 173.463 1.00 44.86  ? 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 135.183 146.344 167.612 1.00 25.10  ? 149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 134.781 146.538 166.228 1.00 26.32  ? 149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 135.738 145.787 165.319 1.00 24.62  ? 149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 136.959 145.877 165.487 1.00 35.73  ? 149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 134.758 148.024 165.865 1.00 29.27  ? 149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 134.731 148.300 164.380 1.00 29.92  ? 149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 133.619 147.987 163.613 1.00 26.22  ? 149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 135.820 148.885 163.746 1.00 29.15  ? 149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 133.593 148.242 162.256 1.00 27.79  ? 149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 135.802 149.144 162.392 1.00 30.68  ? 149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 134.687 148.821 161.652 1.00 27.20  ? 149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 134.668 149.079 160.302 1.00 31.23  ? 149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 135.186 145.051 164.365 1.00 20.64  ? 150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 135.980 144.288 163.406 1.00 19.56  ? 150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 135.723 144.809 162.001 1.00 27.89  ? 150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 134.607 144.635 161.475 1.00 36.16  ? 150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 135.646 142.799 163.491 1.00 28.25  ? 150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 136.338 141.943 162.444 1.00 27.96  ? 150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 137.845 142.096 162.460 1.00 27.24  ? 150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 138.497 141.835 163.471 1.00 28.32  ? 150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 138.408 142.517 161.336 1.00 32.86  ? 150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 136.693 145.461 161.363 1.00 30.99  ? 151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 136.519 145.832 159.956 1.00 25.45  ? 151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 136.351 144.592 159.093 1.00 28.86  ? 151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 136.852 143.513 159.417 1.00 37.23  ? 151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 137.815 146.579 159.618 1.00 27.49  ? 151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 138.370 147.007 160.935 1.00 29.56  ? 151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 137.962 145.958 161.919 1.00 24.60  ? 151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 135.615 144.752 157.997 1.00 31.11  ? 152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 135.344 143.637 157.101 1.00 25.52  ? 152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 136.644 143.007 156.613 1.00 30.42  ? 152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 137.717 143.615 156.654 1.00 37.67  ? 152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 134.507 144.099 155.909 1.00 25.58  ? 152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 135.278 144.884 155.017 1.00 32.50  ? 152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 136.537 141.760 156.156 1.00 30.76  ? 153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 137.712 141.021 155.695 1.00 32.25  ? 153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 138.503 141.759 154.621 1.00 36.26  ? 153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 139.735 141.832 154.745 1.00 38.54  ? 153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 137.283 139.626 155.216 1.00 35.19  ? 153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 136.938 138.816 156.346 1.00 34.14  ? 153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 138.405 138.954 154.441 1.00 31.90  ? 153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 137.895 142.325 153.568 1.00 32.50  ? 154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 138.700 143.137 152.640 1.00 28.81  ? 154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 139.386 144.311 153.316 1.00 27.13  ? 154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 140.561 144.581 153.041 1.00 38.74  ? 154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 137.671 143.603 151.603 1.00 31.02  ? 154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 136.601 142.590 151.656 1.00 28.48  ? 154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 136.506 142.189 153.091 1.00 26.78  ? 154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 138.687 145.004 154.216 1.00 24.59  ? 155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 139.272 146.161 154.883 1.00 21.43  ? 155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 140.387 145.746 155.834 1.00 22.65  ? 155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 141.480 146.319 155.812 1.00 26.96  ? 155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 138.193 146.937 155.635 1.00 28.85  ? 155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 137.068 147.154 154.774 1.00 29.03  ? 155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 138.734 148.273 156.100 1.00 23.63  ? 155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 140.127 144.746 156.678 1.00 33.43  ? 156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 141.137 144.305 157.635 1.00 32.72  ? 156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 142.360 143.742 156.925 1.00 31.53  ? 156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 143.499 143.988 157.340 1.00 32.28  ? 156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 140.534 143.268 158.582 1.00 31.94  ? 156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 141.343 143.037 159.825 1.00 35.78  ? 156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 141.664 144.089 160.663 1.00 32.19  ? 156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 141.776 141.765 160.157 1.00 32.01  ? 156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 142.407 143.880 161.807 1.00 34.72  ? 156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 142.517 141.549 161.300 1.00 30.98  ? 156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 142.833 142.608 162.126 1.00 39.12  ? 156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 142.144 142.987 155.847 1.00 36.60  ? 157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 143.236 142.332 155.139 1.00 28.10  ? 157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 144.029 143.291 154.258 1.00 32.47  ? 157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 145.242 143.117 154.106 1.00 45.48  ? 157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 142.678 141.182 154.297 1.00 33.93  ? 157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 143.601 140.472 153.307 1.00 38.82  ? 157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 144.672 139.681 154.035 1.00 40.39  ? 157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 142.795 139.567 152.389 1.00 35.77  ? 157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 143.383 144.306 153.681 1.00 32.47  ? 158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 144.008 145.101 152.635 1.00 31.66  ? 158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 144.228 146.564 152.996 1.00 34.58  ? 158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 144.675 147.328 152.134 1.00 43.64  ? 158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 143.171 145.026 151.350 1.00 33.64  ? 158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 143.087 143.620 150.792 1.00 39.47  ? 158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.018 142.828 150.933 1.00 44.04  ? 158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 141.967 143.303 150.157 1.00 40.48  ? 158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 143.927 146.982 154.222 1.00 32.81  ? 159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 144.153 148.372 154.597 1.00 37.14  ? 159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 145.644 148.634 154.763 1.00 43.03  ? 159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 146.323 147.959 155.541 1.00 49.59  ? 159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 143.414 148.713 155.889 1.00 37.05  ? 159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 146.153 149.619 154.025 1.00 44.58  ? 160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 147.550 149.983 154.100 1.00 47.18  ? 160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 148.492 149.106 153.309 1.00 49.08  ? 160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 149.705 149.343 153.344 1.00 50.68  ? 160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 147.983 148.105 152.601 1.00 47.58  ? 161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 148.800 147.198 151.811 1.00 46.54  ? 161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 148.854 147.653 150.356 1.00 49.54  ? 161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 147.929 148.286 149.843 1.00 52.02  ? 161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 148.254 145.771 151.895 1.00 42.99  ? 161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 148.718 145.000 153.118 1.00 45.23  ? 161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 148.505 143.506 152.942 1.00 45.91  ? 161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 147.892 142.906 154.120 1.00 45.69  ? 161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 147.842 141.603 154.360 1.00 48.02  ? 161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.327 140.723 153.499 1.00 51.31  ? 161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 147.288 141.172 155.488 1.00 44.52  ? 161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 149.963 147.322 149.696 1.00 57.66  ? 162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 150.145 147.623 148.280 1.00 60.45  ? 162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 149.612 146.514 147.382 1.00 58.19  ? 162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 148.907 146.791 146.408 1.00 53.28  ? 162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 151.626 147.881 147.977 1.00 62.01  ? 162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 151.870 148.522 146.619 1.00 58.29  ? 162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 152.619 149.839 146.745 1.00 58.69  ? 162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 153.886 149.685 147.567 1.00 62.19  ? 162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.435 151.001 147.999 1.00 60.01  ? 162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 149.934 145.258 147.692 1.00 60.75  ? 163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 149.359 144.129 146.974 1.00 63.43  ? 163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 147.932 143.894 147.452 1.00 65.32  ? 163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 147.643 142.883 148.099 1.00 63.80  ? 163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 150.206 142.871 147.170 1.00 63.14  ? 163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 149.979 141.797 146.117 1.00 61.56  ? 163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 151.263 141.049 145.805 1.00 61.33  ? 163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 152.412 141.944 145.744 1.00 63.88  ? 163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 153.513 141.800 146.468 1.00 64.88  ? 163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 153.653 140.800 147.323 1.00 62.63  ? 163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 154.499 142.682 146.331 1.00 61.64  ? 163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 147.039 144.828 147.139 1.00 53.39  ? 164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 145.676 144.817 147.641 1.00 48.78  ? 164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 144.689 144.948 146.491 1.00 51.20  ? 164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.027 145.434 145.408 1.00 51.80  ? 164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 145.445 145.960 148.637 1.00 49.88  ? 164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 145.432 147.334 147.985 1.00 48.97  ? 164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 144.437 148.271 148.646 1.00 45.59  ? 164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 144.998 148.940 149.812 1.00 48.50  ? 164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.520 150.063 150.330 1.00 51.46  ? 164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.467 150.672 149.807 1.00 48.78  ? 164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 145.112 150.591 151.397 1.00 48.34  ? 164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 143.462 144.501 146.739 1.00 49.48  ? 165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 142.365 144.769 145.833 1.00 49.19  ? 165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 141.655 146.041 146.245 1.00 51.11  ? 165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 142.248 147.123 146.222 1.00 55.94  ? 165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 140.390 145.928 146.623 1.00 43.29  ? 166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 139.642 147.034 147.199 1.00 43.49  ? 166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 139.228 146.691 148.623 1.00 42.74  ? 166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 139.246 145.532 149.043 1.00 42.12  ? 166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 138.413 147.372 146.347 1.00 46.04  ? 166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 138.726 148.167 145.090 1.00 45.12  ? 166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 139.400 149.493 145.382 1.00 46.30  ? 166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 139.116 150.091 146.441 1.00 48.63  ? 166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.217 149.940 144.550 1.00 42.20  ? 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 138.853 147.726 149.369 1.00 37.42  ? 167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 138.369 147.563 150.732 1.00 34.51  ? 167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 136.871 147.308 150.794 1.00 40.03  ? 167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 136.327 147.149 151.891 1.00 40.99  ? 167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 138.715 148.799 151.569 1.00 30.84  ? 167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.189 149.148 151.789 1.00 26.95  ? 167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 140.356 149.878 153.104 1.00 33.84  ? 167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.063 147.910 151.762 1.00 29.55  ? 167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 136.197 147.267 149.652 1.00 31.53  ? 168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 134.757 147.049 149.592 1.00 24.98  ? 168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 134.490 145.557 149.462 1.00 38.80  ? 168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 135.052 144.881 148.593 1.00 37.02  ? 168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 134.137 147.834 148.425 1.00 27.05  ? 168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 132.655 147.564 148.341 1.00 34.37  ? 168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 134.389 149.312 148.597 1.00 34.31  ? 168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 133.626 145.041 150.334 1.00 46.39  ? 169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 133.344 143.615 150.400 1.00 40.89  ? 169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 132.351 143.141 149.349 1.00 40.87  ? 169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 132.329 141.945 149.040 1.00 45.26  ? 169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 132.814 143.250 151.791 1.00 35.89  ? 169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 133.443 144.027 152.794 1.00 40.59  ? 169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 131.536 144.033 148.793 1.00 34.52  ? 170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 130.442 143.603 147.936 1.00 30.84  ? 170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.082 144.721 146.972 1.00 30.94  ? 170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.262 145.898 147.288 1.00 36.64  ? 170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 129.221 143.205 148.779 1.00 35.47  ? 170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 128.923 144.279 150.213 1.00 55.50  ? 170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 129.578 144.347 145.799 1.00 28.52  ? 171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.102 145.302 144.807 1.00 20.96  ? 171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 127.775 144.822 144.246 1.00 20.17  ? 171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 127.567 143.617 144.077 1.00 32.49  ? 171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.110 145.493 143.670 1.00 21.95  ? 171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 131.511 145.765 144.133 1.00 25.85  ? 171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 131.924 147.058 144.406 1.00 19.85  ? 171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 132.420 144.732 144.280 1.00 24.39  ? 171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.212 147.314 144.827 1.00 13.71  ? 171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 133.710 144.983 144.701 1.00 25.75  ? 171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.106 146.275 144.974 1.00 23.20  ? 171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 126.880 145.764 143.963 1.00 17.63  ? 172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 125.570 145.471 143.399 1.00 13.81  ? 172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.423 146.240 142.095 1.00 16.30  ? 172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.468 147.473 142.091 1.00 22.75  ? 172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 124.452 145.846 144.374 1.00 14.93  ? 172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 124.252 144.985 145.622 1.00 12.95  ? 172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 125.282 145.306 146.695 1.00 12.79  ? 172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 122.847 145.165 146.160 1.00 15.92  ? 172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.241 145.515 140.995 1.00 22.30  ? 173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.167 146.103 139.665 1.00 20.90  ? 173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 123.750 145.999 139.123 1.00 26.86  ? 173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.118 144.942 139.222 1.00 32.27  ? 173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.140 145.416 138.705 1.00 21.23  ? 173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 127.607 145.329 139.121 1.00 22.31  ? 173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.408 144.639 138.033 1.00 26.07  ? 173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.166 146.711 139.409 1.00 27.99  ? 173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.258 147.095 138.555 1.00 31.25  ? 174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 121.986 147.101 137.845 1.00 30.49  ? 174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.256 146.898 136.360 1.00 30.52  ? 174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 122.944 147.712 135.732 1.00 37.61  ? 174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.242 148.413 138.084 1.00 33.71  ? 174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 120.607 148.535 139.456 1.00 31.51  ? 174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.112 148.300 139.428 1.00 32.47  ? 174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 118.545 148.217 138.319 1.00 32.43  ? 174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.504 148.200 140.512 1.00 34.27  ? 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 121.721 145.819 135.799 1.00 23.89  ? 175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 121.926 145.474 134.397 1.00 27.27  ? 175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 120.718 145.950 133.604 1.00 29.43  ? 175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 119.588 145.516 133.858 1.00 29.04  ? 175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.145 143.964 134.218 1.00 24.10  ? 175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 122.644 143.664 132.814 1.00 25.58  ? 175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.119 143.447 135.258 1.00 25.56  ? 175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 120.952 146.841 132.646 1.00 28.38  ? 176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 119.880 147.335 131.798 1.00 28.10  ? 176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 119.630 146.372 130.640 1.00 32.61  ? 176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.421 145.466 130.362 1.00 35.35  ? 176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.207 148.733 131.278 1.00 20.67  ? 176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 118.967 149.559 131.015 1.00 26.24  ? 176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 117.869 149.023 130.878 1.00 33.93  ? 176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.137 150.874 130.942 1.00 32.50  ? 176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.508 146.583 129.952 1.00 35.43  ? 177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.046 145.668 128.909 1.00 30.38  ? 177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.617 146.104 127.562 1.00 35.87  ? 177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 117.937 146.685 126.715 1.00 36.76  ? 177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.525 145.620 128.887 1.00 26.63  ? 177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 115.988 144.558 127.954 1.00 35.61  ? 177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.656 143.517 127.792 1.00 44.24  ? 177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 114.898 144.766 127.382 1.00 33.25  ? 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 119.900 145.807 127.366 1.00 27.71  ? 178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.553 146.044 126.086 1.00 26.47  ? 178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 121.820 145.205 126.022 1.00 30.92  ? 178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.339 144.754 127.044 1.00 35.60  ? 178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 120.875 147.528 125.878 1.00 20.23  ? 178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.119 147.870 126.458 1.00 27.75  ? 178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.306 144.993 124.795 1.00 26.24  ? 179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.561 144.268 124.622 1.00 22.04  ? 179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 124.746 145.081 125.119 1.00 25.30  ? 179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 125.682 144.518 125.697 1.00 25.41  ? 179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 123.762 143.888 123.157 1.00 31.26  ? 179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 124.826 142.817 122.907 1.00 23.46  ? 179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 124.521 141.560 123.706 1.00 20.42  ? 179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 124.950 142.504 121.428 1.00 25.21  ? 179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 124.730 146.397 124.896 1.00 30.79  ? 180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 125.775 147.256 125.440 1.00 27.58  ? 180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 125.805 147.169 126.958 1.00 29.09  ? 180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 126.873 147.031 127.567 1.00 31.22  ? 180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.551 148.700 124.993 1.00 25.85  ? 180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 125.966 148.937 123.560 1.00 33.82  ? 180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 126.711 148.151 122.980 1.00 36.69  ? 180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.480 150.025 122.976 1.00 38.03  ? 180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 124.629 147.223 127.584 1.00 32.49  ? 181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 124.559 147.166 129.039 1.00 24.86  ? 181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 124.947 145.791 129.564 1.00 25.39  ? 181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 125.589 145.687 130.611 1.00 34.30  ? 181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.157 147.550 129.505 1.00 29.31  ? 181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 122.833 149.001 129.227 1.00 35.21  ? 181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 123.470 149.880 129.843 1.00 35.37  ? 181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 121.946 149.267 128.390 1.00 39.71  ? 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 124.587 144.724 128.848 1.00 27.57  ? 182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 124.964 143.384 129.288 1.00 25.82  ? 182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.473 143.186 129.182 1.00 27.00  ? 182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.108 142.642 130.093 1.00 25.58  ? 182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.193 142.321 128.484 1.00 24.43  ? 182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 122.760 142.207 129.001 1.00 27.18  ? 182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 124.890 140.972 128.558 1.00 23.24  ? 182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 121.837 141.480 128.063 1.00 28.25  ? 182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.069 143.621 128.070 1.00 28.00  ? 183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.514 143.503 127.912 1.00 19.92  ? 183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.251 144.338 128.949 1.00 27.11  ? 183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.250 143.891 129.525 1.00 31.35  ? 183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 128.921 143.917 126.499 1.00 22.85  ? 183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.957 145.327 126.371 1.00 35.43  ? 183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 128.768 145.555 129.212 1.00 29.03  ? 184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.389 146.378 130.241 1.00 22.84  ? 184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.194 145.780 131.627 1.00 26.69  ? 184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.078 145.901 132.478 1.00 35.05  ? 184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 128.837 147.800 130.179 1.00 28.05  ? 184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.231 148.665 131.356 1.00 31.40  ? 184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 130.684 149.089 131.270 1.00 29.40  ? 184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.000 149.708 129.990 1.00 36.65  ? 184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.225 149.829 129.500 1.00 38.76  ? 184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.278 149.371 130.156 1.00 33.04  ? 184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 132.398 150.424 128.325 1.00 36.66  ? 184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.056 145.128 131.875 1.00 31.48  ? 185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 127.850 144.453 133.150 1.00 18.19  ? 185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 128.829 143.302 133.326 1.00 23.50  ? 185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 129.367 143.103 134.418 1.00 32.72  ? 185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 126.409 143.954 133.254 1.00 24.03  ? 185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.072 142.534 132.261 1.00 32.07  ? 186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.079 141.476 132.321 1.00 31.34  ? 186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 131.456 142.069 132.595 1.00 26.53  ? 186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.220 141.559 133.427 1.00 33.93  ? 186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.071 140.655 131.019 1.00 33.66  ? 186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 128.714 139.980 130.812 1.00 27.70  ? 186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.185 139.621 131.028 1.00 27.43  ? 186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.529 139.417 129.425 1.00 27.18  ? 186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 131.790 143.158 131.898 1.00 26.33  ? 187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.080 143.812 132.099 1.00 27.97  ? 187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.243 144.279 133.539 1.00 29.47  ? 187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.282 144.045 134.165 1.00 38.77  ? 187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.218 144.989 131.133 1.00 30.17  ? 187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.258 145.996 131.586 1.00 41.48  ? 187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 135.420 145.597 131.812 1.00 43.33  ? 187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 133.911 147.188 131.718 1.00 41.41  ? 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.218 144.937 134.084 1.00 24.60  ? 188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.296 145.462 135.442 1.00 26.64  ? 188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 132.333 144.327 136.456 1.00 26.15  ? 188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.026 144.413 137.475 1.00 33.70  ? 188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.127 146.428 135.709 1.00 26.38  ? 188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.223 147.647 134.792 1.00 30.95  ? 188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.124 146.883 137.150 1.00 27.31  ? 188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.035 148.569 134.895 1.00 30.75  ? 188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 131.595 143.246 136.199 1.00 23.38  ? 189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 131.640 142.093 137.091 1.00 15.22  ? 189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.042 141.507 137.147 1.00 26.67  ? 189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 133.554 141.199 138.228 1.00 34.79  ? 189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 130.632 141.039 136.634 1.00 23.54  ? 189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.309 141.539 136.697 1.00 35.04  ? 189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 133.688 141.363 135.988 1.00 28.25  ? 190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.055 140.850 135.975 1.00 23.36  ? 190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.025 141.824 136.636 1.00 27.20  ? 190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 136.944 141.404 137.348 1.00 30.80  ? 190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 135.486 140.533 134.543 1.00 27.64  ? 190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.106 139.128 134.099 1.00 32.79  ? 190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 135.445 138.774 132.365 1.00 33.57  ? 190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 135.076 140.353 131.615 1.00 27.86  ? 190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 135.834 143.129 136.422 1.00 30.44  ? 191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 136.710 144.119 137.043 1.00 29.01  ? 191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 136.597 144.093 138.562 1.00 29.99  ? 191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 137.610 144.157 139.268 1.00 39.51  ? 191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 136.391 145.518 136.513 1.00 26.30  ? 191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 136.725 145.744 135.047 1.00 30.69  ? 191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.192 145.533 134.729 1.00 33.82  ? 191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.058 145.689 135.590 1.00 31.82  ? 191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 138.479 145.184 133.482 1.00 30.62  ? 191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 135.373 144.008 139.083 1.00 31.09  ? 192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.174 144.017 140.527 1.00 26.61  ? 192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 135.535 142.684 141.167 1.00 29.07  ? 192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 135.953 142.656 142.328 1.00 38.70  ? 192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 133.728 144.390 140.855 1.00 27.00  ? 192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.258 145.745 140.322 1.00 25.14  ? 192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 131.773 145.931 140.561 1.00 24.91  ? 192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.048 146.880 140.949 1.00 22.48  ? 192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 135.380 141.573 140.439 1.00 25.20  ? 193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 135.877 140.297 140.937 1.00 26.08  ? 193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 137.397 140.269 140.954 1.00 33.31  ? 193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 137.995 139.618 141.818 1.00 39.13  ? 193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.330 139.155 140.087 1.00 30.71  ? 193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 133.939 139.305 139.882 1.00 33.68  ? 193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.034 140.961 140.008 1.00 31.72  ? 194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 139.479 141.148 140.071 1.00 32.58  ? 194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 139.872 141.894 141.339 1.00 38.79  ? 194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 140.892 141.580 141.964 1.00 43.91  ? 194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 139.957 141.896 138.827 1.00 32.02  ? 194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.399 142.363 138.880 1.00 38.09  ? 194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 141.720 143.267 137.701 1.00 38.13  ? 194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.160 143.744 137.743 1.00 39.26  ? 194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.441 144.743 136.677 1.00 39.31  ? 194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.069 142.882 141.738 1.00 38.99  ? 195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 139.302 143.607 142.980 1.00 39.96  ? 195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 139.043 142.760 144.218 1.00 37.38  ? 195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 139.429 143.169 145.318 1.00 45.90  ? 195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 138.430 144.862 143.019 1.00 38.09  ? 195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 138.671 145.864 141.889 1.00 38.05  ? 195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 137.614 146.956 141.900 1.00 40.10  ? 195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 140.065 146.460 141.988 1.00 37.52  ? 195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 138.402 141.600 144.070 1.00 33.81  ? 196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 138.189 140.682 145.168 1.00 39.31  ? 196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 136.808 140.723 145.788 1.00 43.17  ? 196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 136.479 139.828 146.575 1.00 44.38  ? 196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 135.995 141.721 145.460 1.00 35.68  ? 197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 134.678 141.847 146.051 1.00 32.37  ? 197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 133.619 141.043 145.319 1.00 30.87  ? 197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 133.677 140.858 144.107 1.00 34.28  ? 197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 132.640 140.563 146.081 1.00 26.12  ? 198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 131.527 139.851 145.486 1.00 21.44  ? 198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 130.602 140.784 144.729 1.00 24.87  ? 198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 130.361 141.922 145.128 1.00 33.80  ? 198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.076 140.289 143.613 1.00 22.86  ? 199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 129.257 141.085 142.707 1.00 17.44  ? 199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 127.863 140.479 142.644 1.00 21.58  ? 199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 127.713 139.275 142.407 1.00 34.57  ? 199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 129.880 141.165 141.303 1.00 22.64  ? 199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.000 141.987 140.384 1.00 19.71  ? 199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 131.274 141.757 141.377 1.00 25.60  ? 199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 126.850 141.314 142.858 1.00 22.24  ? 200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 125.453 140.936 142.698 1.00 8.67   ? 200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 124.857 141.738 141.552 1.00 15.93  ? 200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.076 142.950 141.459 1.00 29.87  ? 200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 124.666 141.180 143.985 1.00 16.31  ? 200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 123.383 140.582 143.918 1.00 28.67  ? 200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.110 141.066 140.683 1.00 18.86  ? 201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 123.544 141.692 139.498 1.00 14.53  ? 201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.030 141.549 139.499 1.00 16.15  ? 201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 121.495 140.493 139.847 1.00 20.86  ? 201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.130 141.083 138.222 1.00 18.60  ? 201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 125.649 141.195 138.096 1.00 20.39  ? 201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 126.307 139.834 138.251 1.00 20.31  ? 201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.034 141.838 136.777 1.00 19.80  ? 201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 121.347 142.623 139.111 1.00 17.50  ? 202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 119.894 142.643 139.000 1.00 13.91  ? 202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 119.521 142.332 137.556 1.00 28.82  ? 202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 119.757 143.146 136.657 1.00 36.96  ? 202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.334 143.997 139.432 1.00 20.02  ? 202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 117.840 143.959 139.671 1.00 21.28  ? 202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 117.282 142.923 140.029 1.00 25.89  ? 202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.182 145.095 139.473 1.00 17.70  ? 202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 118.941 141.156 137.336 1.00 20.21  ? 203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 118.542 140.719 136.008 1.00 16.98  ? 203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.058 140.933 135.746 1.00 17.44  ? 203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 116.550 140.484 134.715 1.00 24.36  ? 203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 118.901 139.246 135.810 1.00 17.97  ? 203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 120.341 138.844 136.132 1.00 20.52  ? 203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 120.599 137.412 135.705 1.00 22.19  ? 203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.339 139.788 135.480 1.00 21.72  ? 203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 116.352 141.613 136.653 1.00 17.95  ? 204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 114.919 141.814 136.487 1.00 14.72  ? 204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 114.594 142.794 135.370 1.00 26.73  ? 204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 113.481 142.757 134.836 1.00 31.64  ? 204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.303 142.300 137.798 1.00 17.79  ? 204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 114.615 141.420 138.861 1.00 30.66  ? 204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 115.530 143.670 135.006 1.00 29.14  ? 205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.323 144.572 133.883 1.00 30.75  ? 205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.571 143.906 132.540 1.00 26.68  ? 205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.107 144.419 131.516 1.00 32.02  ? 205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.230 145.799 134.008 1.00 29.53  ? 205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 115.845 146.737 135.132 1.00 28.85  ? 205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 116.603 148.044 135.031 1.00 31.54  ? 205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 115.963 149.109 135.897 1.00 36.43  ? 205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 115.958 148.722 137.332 1.00 32.47  ? 205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.286 142.786 132.522 1.00 24.55  ? 206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.525 142.067 131.280 1.00 22.94  ? 206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.221 141.476 130.764 1.00 26.64  ? 206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.451 140.882 131.524 1.00 30.07  ? 206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 117.557 140.965 131.501 1.00 21.86  ? 206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 118.933 141.457 131.943 1.00 26.36  ? 206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 119.853 140.285 132.179 1.00 28.66  ? 206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.516 142.395 130.905 1.00 28.44  ? 206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 114.976 141.639 129.469 1.00 33.82  ? 207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 113.727 141.173 128.890 1.00 33.66  ? 207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 113.713 139.651 128.794 1.00 36.25  ? 207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 114.756 138.996 128.744 1.00 40.89  ? 207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.504 141.818 127.525 1.00 35.11  ? 207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.280 141.219 126.379 1.00 33.40  ? 207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 113.913 141.930 125.089 1.00 35.13  ? 207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.093 143.372 125.196 1.00 34.74  ? 207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.694 144.122 124.282 1.00 32.52  ? 207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 115.161 143.600 123.160 1.00 35.65  ? 207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 114.821 145.427 124.496 1.00 33.61  ? 207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 112.505 139.095 128.777 1.00 42.86  ? 208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.312 137.666 128.966 1.00 38.55  ? 208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 112.741 136.877 127.729 1.00 40.62  ? 208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.026 137.429 126.664 1.00 43.26  ? 208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.853 137.368 129.300 1.00 37.10  ? 208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 112.795 135.558 127.899 1.00 40.67  ? 209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.117 134.664 126.796 1.00 35.15  ? 209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 111.975 134.627 125.789 1.00 41.43  ? 209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 110.799 134.570 126.159 1.00 43.88  ? 209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.403 133.258 127.323 1.00 36.75  ? 209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.641 132.220 126.242 1.00 43.31  ? 209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 113.906 130.851 126.840 1.00 43.10  ? 209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 115.340 130.414 126.596 1.00 43.55  ? 209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 115.672 130.384 125.145 1.00 41.26  ? 209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.328 134.653 124.507 1.00 44.15  ? 210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.329 134.698 123.463 1.00 45.82  ? 210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 110.777 136.071 123.169 1.00 46.83  ? 210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.709 136.174 122.556 1.00 48.12  ? 210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.460 137.128 123.594 1.00 44.42  ? 211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.023 138.488 123.327 1.00 41.87  ? 211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.645 139.005 122.031 1.00 41.75  ? 211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.442 138.331 121.378 1.00 44.34  ? 211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.376 139.401 124.499 1.00 43.75  ? 211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.512 139.169 125.720 1.00 45.34  ? 211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 109.992 140.454 126.326 1.00 47.37  ? 211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.083 141.068 125.729 1.00 47.30  ? 211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.481 140.842 127.405 1.00 47.80  ? 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.270 140.227 121.668 1.00 44.32  ? 212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.643 140.800 120.383 1.00 43.27  ? 212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.874 141.687 120.524 1.00 45.39  ? 212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 112.981 142.468 121.475 1.00 49.11  ? 212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.482 141.601 119.794 1.00 43.83  ? 212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.801 141.556 119.576 1.00 42.47  ? 213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 114.968 142.429 119.495 1.00 45.84  ? 213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.879 143.253 118.219 1.00 44.04  ? 213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.298 142.800 117.148 1.00 48.95  ? 213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.280 141.625 119.535 1.00 45.28  ? 213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.281 140.658 120.716 1.00 46.26  ? 213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.475 142.558 119.624 1.00 40.81  ? 213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.386 139.635 120.655 1.00 43.23  ? 213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.331 144.465 118.327 1.00 49.00  ? 214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.194 145.376 117.194 1.00 51.94  ? 214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.389 144.742 116.067 1.00 59.34  ? 214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.928 144.486 114.984 1.00 59.74  ? 214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.569 145.812 116.683 1.00 51.78  ? 214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 115.737 147.316 116.561 1.00 51.08  ? 214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.203 147.718 116.477 1.00 54.03  ? 214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 117.964 146.873 115.463 1.00 54.49  ? 214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 118.743 145.771 116.095 1.00 52.07  ? 214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.111 144.455 116.332 1.00 64.58  ? 215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.164 143.910 115.361 1.00 67.96  ? 215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.462 142.452 115.027 1.00 66.82  ? 215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.711 141.820 114.276 1.00 66.74  ? 215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.135 144.750 114.079 1.00 67.95  ? 215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.624 146.157 114.314 1.00 69.50  ? 215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 111.425 147.110 114.201 1.00 66.99  ? 215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 109.421 146.312 114.612 1.00 69.25  ? 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.546 141.907 115.574 1.00 60.30  ? 216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.859 140.493 115.407 1.00 59.21  ? 216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.319 139.759 116.627 1.00 60.04  ? 216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.915 139.806 117.708 1.00 64.59  ? 216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.373 140.267 115.231 1.00 60.47  ? 216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.715 138.796 115.357 1.00 57.53  ? 216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.845 140.813 113.893 1.00 60.36  ? 216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.186 139.079 116.463 1.00 57.73  ? 217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.471 138.494 117.585 1.00 59.81  ? 217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.063 137.138 117.960 1.00 57.90  ? 217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.671 136.448 117.141 1.00 57.71  ? 217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.984 138.361 117.257 1.00 59.65  ? 217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.121 139.478 117.816 1.00 60.36  ? 217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.042 140.674 116.888 1.00 64.15  ? 217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 108.488 140.560 115.727 1.00 64.91  ? 217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.538 141.731 117.324 1.00 63.00  ? 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.872 136.757 119.221 1.00 53.05  ? 218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.300 135.463 119.754 1.00 52.69  ? 218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.781 135.211 119.484 1.00 56.38  ? 218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.193 134.133 119.051 1.00 59.41  ? 218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.440 134.333 119.190 1.00 54.27  ? 218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.464 133.095 120.062 1.00 57.82  ? 218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.741 133.008 121.053 1.00 57.98  ? 218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.305 132.132 119.704 1.00 56.65  ? 218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.592 136.231 119.751 1.00 49.84  ? 219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.029 136.166 119.510 1.00 51.28  ? 219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 115.841 136.152 120.794 1.00 48.85  ? 219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.001 135.723 120.783 1.00 49.45  ? 219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.468 137.341 118.623 1.00 49.57  ? 219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.270 136.614 121.902 1.00 45.55  ? 220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.017 136.700 123.146 1.00 43.81  ? 220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.226 135.319 123.758 1.00 49.02  ? 220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.429 134.394 123.573 1.00 47.91  ? 220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.290 137.588 124.152 1.00 36.95  ? 220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 113.913 137.197 124.226 1.00 47.05  ? 220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 115.365 139.028 123.721 1.00 36.83  ? 220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.322 135.189 124.501 1.00 40.43  ? 221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.592 134.005 125.301 1.00 44.16  ? 221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.159 134.179 126.749 1.00 47.45  ? 221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.404 133.290 127.571 1.00 46.48  ? 221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.077 133.648 125.236 1.00 41.55  ? 221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 119.691 133.847 123.869 1.00 42.54  ? 221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.826 132.871 123.638 1.00 45.15  ? 221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.132 132.742 122.161 1.00 46.17  ? 221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.736 133.964 121.409 1.00 44.47  ? 221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 116.523 135.297 127.076 1.00 45.69  ? 222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.118 135.563 128.434 1.00 42.58  ? 222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.284 135.974 129.307 1.00 43.54  ? 222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 118.364 136.345 128.841 1.00 38.75  ? 222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.043 135.909 130.617 1.00 42.90  ? 223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.091 136.240 131.568 1.00 38.22  ? 223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.064 135.088 131.756 1.00 37.30  ? 223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.155 135.297 132.292 1.00 41.39  ? 223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.484 136.661 132.919 1.00 32.47  ? 223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.403 137.703 132.711 1.00 33.94  ? 223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 116.931 135.453 133.657 1.00 33.43  ? 223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 118.711 133.878 131.314 1.00 38.80  ? 224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 119.544 132.708 131.582 1.00 33.68  ? 224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.826 132.749 130.757 1.00 38.46  ? 224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.887 132.307 131.215 1.00 41.99  ? 224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.745 131.419 131.329 1.00 35.83  ? 224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.557 130.203 131.741 1.00 34.98  ? 224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 117.431 131.465 132.082 1.00 40.36  ? 224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 120.754 133.259 129.528 1.00 34.06  ? 225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.973 133.468 128.765 1.00 27.97  ? 225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 122.905 134.448 129.448 1.00 34.71  ? 225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.126 134.258 129.466 1.00 44.42  ? 225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.339 135.503 130.035 1.00 28.94  ? 226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.141 136.453 130.795 1.00 28.09  ? 226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 123.713 135.792 132.044 1.00 30.91  ? 226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 124.831 136.105 132.464 1.00 35.96  ? 226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.304 137.698 131.135 1.00 28.31  ? 226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.160 138.739 131.837 1.00 35.24  ? 226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 121.694 138.273 129.872 1.00 27.33  ? 226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 122.959 134.879 132.665 1.00 34.48  ? 227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 123.503 134.133 133.796 1.00 31.66  ? 227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 124.685 133.275 133.373 1.00 29.49  ? 227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 125.675 133.179 134.098 1.00 33.45  ? 227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.435 133.259 134.457 1.00 30.86  ? 227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 121.131 133.949 134.778 1.00 27.82  ? 227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.187 133.097 136.055 1.00 43.54  ? 227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.477 132.197 136.910 1.00 39.90  ? 227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 124.596 132.630 132.210 1.00 31.04  ? 228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.727 131.844 131.723 1.00 32.23  ? 228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.937 132.734 131.453 1.00 32.32  ? 228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.071 132.390 131.820 1.00 36.24  ? 228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.335 131.077 130.461 1.00 31.48  ? 228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.979 129.619 130.703 1.00 32.14  ? 228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 123.612 129.291 130.131 1.00 42.14  ? 228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.634 129.335 128.611 1.00 45.15  ? 228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.265 129.331 128.027 1.00 40.52  ? 228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 126.708 133.889 130.823 1.00 30.80  ? 229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 127.797 134.827 130.566 1.00 26.16  ? 229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.446 135.292 131.864 1.00 27.90  ? 229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 129.674 135.297 131.989 1.00 32.90  ? 229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.281 136.029 129.776 1.00 29.60  ? 229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.128 135.887 128.264 1.00 25.71  ? 229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.132 136.907 127.754 1.00 29.18  ? 229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.470 136.060 127.581 1.00 29.21  ? 229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 127.629 135.682 132.843 1.00 33.22  ? 230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.159 136.166 134.113 1.00 25.48  ? 230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.846 135.049 134.886 1.00 28.26  ? 230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 129.850 135.285 135.562 1.00 43.58  ? 230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.036 136.788 134.941 1.00 28.95  ? 230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.485 138.111 134.407 1.00 33.01  ? 230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.156 138.444 135.062 1.00 29.04  ? 230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.488 139.233 134.616 1.00 32.83  ? 230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.321 133.827 134.796 1.00 27.49  ? 231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.941 132.689 135.458 1.00 28.96  ? 231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 130.332 132.427 134.903 1.00 35.27  ? 231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 131.283 132.209 135.662 1.00 40.54  ? 231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.048 131.458 135.296 1.00 32.16  ? 231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 128.635 130.220 135.936 1.00 45.23  ? 231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 128.797 129.203 135.230 1.00 45.54  ? 231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.927 130.261 137.146 1.00 48.98  ? 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 130.477 132.470 133.579 1.00 42.23  ? 232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.797 132.266 132.992 1.00 36.01  ? 232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 132.709 133.461 133.241 1.00 36.29  ? 232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.929 133.304 133.352 1.00 44.97  ? 232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 131.659 131.966 131.505 1.00 35.22  ? 232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 131.480 130.490 131.241 1.00 44.61  ? 232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 132.102 129.654 131.893 1.00 47.30  ? 232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 130.576 130.160 130.340 1.00 44.65  ? 232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.136 134.664 133.341 1.00 29.18  ? 233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 132.928 135.834 133.704 1.00 27.79  ? 233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 133.485 135.711 135.117 1.00 34.66  ? 233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 134.642 136.063 135.369 1.00 37.33  ? 233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.080 137.098 133.569 1.00 25.80  ? 233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 132.673 135.217 136.052 1.00 36.70  ? 234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.132 135.064 137.428 1.00 29.29  ? 234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.099 133.895 137.561 1.00 34.12  ? 234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.029 133.943 138.374 1.00 38.70  ? 234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.940 134.890 138.369 1.00 29.35  ? 234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.147 136.148 138.577 1.00 28.12  ? 234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 131.773 137.319 138.961 1.00 32.74  ? 234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 129.778 136.160 138.393 1.00 27.23  ? 234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.048 138.475 139.155 1.00 29.95  ? 234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.050 137.316 138.580 1.00 27.80  ? 234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 129.684 138.472 138.963 1.00 30.53  ? 234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.894 132.833 136.777 1.00 38.08  ? 235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.877 131.756 136.731 1.00 39.24  ? 235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.209 132.254 136.190 1.00 42.70  ? 235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 137.274 131.876 136.693 1.00 45.98  ? 235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.354 130.598 135.881 1.00 37.92  ? 235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.132 129.314 136.659 1.00 42.95  ? 235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.917 128.125 135.738 1.00 45.63  ? 235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.998 128.426 134.647 1.00 46.55  ? 235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 131.684 128.262 134.714 1.00 47.82  ? 235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 131.100 127.803 135.809 1.00 46.18  ? 235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.937 128.565 133.657 1.00 42.14  ? 235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.170 133.102 135.163 1.00 35.99  ? 236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 137.400 133.616 134.576 1.00 36.79  ? 236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.101 134.576 135.530 1.00 37.90  ? 236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 139.312 134.476 135.751 1.00 41.42  ? 236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.088 134.304 133.248 1.00 35.81  ? 236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 138.279 134.966 132.611 1.00 35.03  ? 236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.221 134.213 131.929 1.00 33.56  ? 236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 138.469 136.338 132.692 1.00 34.32  ? 236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 140.312 134.799 131.343 1.00 32.81  ? 236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 139.563 136.936 132.106 1.00 32.87  ? 236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 140.479 136.159 131.434 1.00 33.71  ? 236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 141.573 136.735 130.845 1.00 42.27  ? 236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 137.351 135.518 136.100 1.00 43.83  ? 237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 137.890 136.465 137.076 1.00 43.03  ? 237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 137.660 135.951 138.498 1.00 46.82  ? 237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 136.976 136.563 139.317 1.00 48.16  ? 237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.272 137.843 136.873 1.00 37.35  ? 237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 138.240 134.783 138.776 1.00 64.85  ? 238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 138.070 134.105 140.055 1.00 66.77  ? 238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 139.216 134.368 141.025 1.00 68.85  ? 238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.534 133.496 141.845 1.00 71.19  ? 238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 137.894 132.602 139.832 1.00 66.90  ? 238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.119 131.952 139.216 1.00 70.29  ? 238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 140.006 132.682 138.725 1.00 72.76  ? 238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 139.190 130.707 139.220 1.00 67.19  ? 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.847 135.540 140.948 1.00 77.68  ? 239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 140.969 135.888 141.819 1.00 82.18  ? 239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 142.043 134.804 141.771 1.00 81.88  ? 239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.526 134.322 142.798 1.00 80.59  ? 239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 140.492 136.143 143.250 1.00 81.47  ? 239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.331 137.117 143.329 1.00 78.74  ? 239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.763 137.253 144.726 1.00 82.23  ? 239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.549 137.349 144.906 1.00 80.07  ? 239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 139.637 137.261 145.725 1.00 81.72  ? 239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 142.338 134.361 140.545 1.00 84.57  ? 240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.443 133.480 140.156 1.00 85.62  ? 240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.403 132.125 140.857 1.00 87.55  ? 240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.293 131.293 140.649 1.00 86.40  ? 240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.820 134.140 140.360 1.00 85.45  ? 240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 145.200 134.656 141.739 1.00 87.03  ? 240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 146.252 133.501 142.634 1.00 92.75  ? 240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 147.841 134.309 142.494 1.00 84.77  ? 240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.378 131.881 141.668 1.00 89.28  ? 241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.266 130.638 142.414 1.00 86.29  ? 241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 142.457 130.773 143.910 1.00 87.24  ? 241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 142.366 129.760 144.619 1.00 86.64  ? 241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.734 131.971 144.428 1.00 94.39  ? 242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.768 132.166 145.873 1.00 95.06  ? 242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 141.407 131.861 146.485 1.00 97.01  ? 242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.310 131.208 147.531 1.00 94.84  ? 242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.194 133.598 146.195 1.00 93.51  ? 242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.612 133.932 145.766 1.00 95.42  ? 242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 144.983 135.373 146.054 1.00 96.86  ? 242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.243 136.096 146.721 1.00 95.72  ? 242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.132 135.802 145.547 1.00 94.00  ? 242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.343 132.325 145.836 1.00 86.00  ? 243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 138.979 131.998 146.221 1.00 82.05  ? 243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.114 132.131 144.978 1.00 81.13  ? 243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.203 133.139 144.271 1.00 78.70  ? 243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 138.478 132.913 147.345 1.00 80.69  ? 243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.831 134.379 147.159 1.00 80.55  ? 243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 137.751 135.279 147.739 1.00 79.02  ? 243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 136.417 134.729 147.536 1.00 82.09  ? 243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 135.688 134.906 146.443 1.00 81.34  ? 243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 136.132 135.620 145.422 1.00 80.49  ? 243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 134.481 134.351 146.371 1.00 77.32  ? 243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 137.297 131.113 144.712 1.00 78.74  ? 244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 136.527 131.076 143.476 1.00 79.57  ? 244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 135.623 132.296 143.362 1.00 78.74  ? 244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 134.990 132.716 144.335 1.00 77.26  ? 244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 135.693 129.796 143.410 1.00 77.78  ? 244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 136.494 128.549 143.071 1.00 77.28  ? 244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 135.616 127.410 142.592 1.00 78.91  ? 244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 134.519 127.197 143.107 1.00 75.98  ? 244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 136.096 126.671 141.597 1.00 76.95  ? 244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.577 132.871 142.161 1.00 64.23  ? 245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.779 134.054 141.909 1.00 61.79  ? 245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 133.309 133.836 142.191 1.00 56.85  ? 245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 132.627 133.107 141.465 1.00 52.10  ? 245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.811 134.468 143.248 1.00 54.33  ? 246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 131.430 134.316 143.680 1.00 54.89  ? 246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 130.625 135.503 143.174 1.00 48.21  ? 246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.941 136.654 143.491 1.00 40.96  ? 246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 131.339 134.213 145.203 1.00 51.70  ? 246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 131.974 133.038 145.675 1.00 53.66  ? 246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 129.591 135.217 142.385 1.00 30.08  ? 247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 128.700 136.244 141.907 1.00 20.42  ? 247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 127.268 135.903 142.270 1.00 18.91  ? 247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.944 134.770 142.620 1.00 35.35  ? 247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 126.413 136.915 142.186 1.00 16.55  ? 248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.008 136.759 142.519 1.00 18.65  ? 248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.150 137.342 141.409 1.00 21.01  ? 248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 124.474 138.390 140.843 1.00 34.28  ? 248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 124.668 137.434 143.851 1.00 21.42  ? 248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.060 136.649 141.098 1.00 20.05  ? 249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.061 137.123 140.154 1.00 12.84  ? 249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 120.723 137.189 140.867 1.00 15.80  ? 249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 120.302 136.212 141.494 1.00 27.20  ? 249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 121.975 136.211 138.929 1.00 24.25  ? 249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.063 138.336 140.782 1.00 16.08  ? 250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 118.778 138.552 141.431 1.00 13.07  ? 250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 117.718 138.813 140.374 1.00 17.20  ? 250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 117.927 139.623 139.466 1.00 31.58  ? 250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 118.848 139.723 142.410 1.00 18.50  ? 250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.215 139.326 143.820 1.00 26.37  ? 250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 120.520 138.990 144.149 1.00 16.68  ? 250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 118.257 139.294 144.822 1.00 20.42  ? 250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.859 138.627 145.435 1.00 10.00  ? 250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 118.587 138.934 146.112 1.00 17.46  ? 250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.889 138.600 146.412 1.00 17.80  ? 250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 120.225 138.242 147.695 1.00 24.29  ? 250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 116.588 138.126 140.493 1.00 11.72  ? 251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 115.485 138.273 139.559 1.00 14.81  ? 251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.180 138.407 140.324 1.00 14.15  ? 251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 113.963 137.717 141.325 1.00 22.69  ? 251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 115.406 137.083 138.601 1.00 25.16  ? 251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 114.533 137.276 137.363 1.00 18.21  ? 251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.327 137.919 136.247 1.00 21.38  ? 251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.954 135.952 136.918 1.00 21.76  ? 251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.317 139.301 139.852 1.00 16.09  ? 252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 111.992 139.437 140.433 1.00 15.41  ? 252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.169 138.185 140.158 1.00 23.74  ? 252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.288 137.564 139.098 1.00 33.85  ? 252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.286 140.668 139.868 1.00 16.90  ? 252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 110.239 141.222 140.810 1.00 23.53  ? 252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.306 140.522 141.199 1.00 37.83  ? 252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 110.387 142.486 141.181 1.00 23.17  ? 252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 110.329 137.809 141.126 1.00 21.02  ? 253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 109.502 136.619 140.978 1.00 23.86  ? 253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 108.408 136.785 139.936 1.00 32.09  ? 253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.804 135.791 139.520 1.00 36.57  ? 253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.884 136.220 142.333 1.00 20.23  ? 253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.615 134.716 142.370 1.00 18.98  ? 253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 107.616 137.013 142.601 1.00 24.90  ? 253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.645 134.124 143.747 1.00 21.60  ? 253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.141 138.013 139.497 1.00 22.28  ? 254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.167 138.263 138.447 1.00 21.25  ? 254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 107.806 138.369 137.071 1.00 27.84  ? 254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.103 138.632 136.092 1.00 39.89  ? 254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.370 139.530 138.763 1.00 26.93  ? 254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.271 139.310 139.762 1.00 31.64  ? 254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.108 138.655 139.398 1.00 30.57  ? 254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.412 139.737 141.070 1.00 33.65  ? 254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.100 138.446 140.316 1.00 29.69  ? 254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 104.406 139.530 141.992 1.00 37.46  ? 254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.250 138.884 141.614 1.00 35.87  ? 254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.117 138.177 136.980 1.00 32.18  ? 255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 109.778 138.038 135.691 1.00 26.44  ? 255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.373 136.717 135.049 1.00 31.33  ? 255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.184 135.710 135.737 1.00 37.02  ? 255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.293 138.101 135.873 1.00 29.84  ? 255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.051 138.397 134.616 1.00 35.29  ? 255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.168 137.491 133.586 1.00 35.98  ? 255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 112.756 139.490 134.238 1.00 23.72  ? 255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 112.898 138.017 132.619 1.00 29.84  ? 255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.268 139.229 132.991 1.00 17.60  ? 255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.229 136.724 133.722 1.00 38.93  ? 256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.797 135.515 133.027 1.00 37.53  ? 256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.815 134.392 133.182 1.00 40.65  ? 256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.443 133.219 133.312 1.00 42.66  ? 256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 108.558 135.810 131.549 1.00 35.47  ? 256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.974 134.637 130.788 1.00 41.53  ? 256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.809 134.304 129.566 1.00 43.81  ? 256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.865 133.345 129.868 1.00 44.28  ? 256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.695 132.032 129.904 1.00 43.79  ? 256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 108.513 131.482 129.676 1.00 39.67  ? 256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 110.735 131.250 130.177 1.00 41.84  ? 256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.101 134.729 133.177 1.00 32.93  ? 257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.169 133.745 133.281 1.00 30.72  ? 257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.363 133.216 134.693 1.00 33.68  ? 257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.392 132.587 134.951 1.00 38.31  ? 257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.487 134.342 132.780 1.00 35.15  ? 257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.657 134.206 131.283 1.00 45.30  ? 257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.117 135.053 130.544 1.00 45.40  ? 257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.337 133.254 130.846 1.00 45.77  ? 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.412 133.445 135.603 1.00 36.15  ? 258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 111.610 133.060 136.999 1.00 33.37  ? 258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.797 131.553 137.123 1.00 34.12  ? 258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 112.634 131.083 137.903 1.00 41.54  ? 258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.445 133.570 137.872 1.00 34.11  ? 258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.697 133.238 139.345 1.00 30.67  ? 258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.108 133.003 137.408 1.00 25.65  ? 258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 111.978 133.823 139.889 1.00 25.80  ? 258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.039 130.770 136.353 1.00 37.61  ? 259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.207 129.322 136.400 1.00 34.87  ? 259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 112.526 128.902 135.764 1.00 35.36  ? 259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.228 128.034 136.294 1.00 35.17  ? 259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.030 128.633 135.715 1.00 38.09  ? 259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 108.823 128.509 136.622 1.00 40.72  ? 259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 108.881 127.857 137.664 1.00 39.42  ? 259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 107.721 129.137 136.231 1.00 38.59  ? 259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 112.880 129.508 134.628 1.00 37.10  ? 260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.185 129.254 134.027 1.00 30.81  ? 260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.307 129.757 134.926 1.00 31.68  ? 260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.369 129.132 135.021 1.00 38.04  ? 260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.262 129.907 132.649 1.00 35.09  ? 260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 112.970 129.772 131.868 1.00 45.27  ? 260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 112.993 129.159 130.780 1.00 44.50  ? 260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 111.932 130.278 132.341 1.00 48.12  ? 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.089 130.900 135.584 1.00 37.88  ? 261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.057 131.420 136.545 1.00 30.49  ? 261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.260 130.447 137.698 1.00 27.10  ? 261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.391 130.222 138.142 1.00 29.99  ? 261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 115.580 132.783 137.050 1.00 27.57  ? 261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.426 133.378 138.139 1.00 32.98  ? 261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 117.530 134.150 137.828 1.00 26.98  ? 261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.089 133.207 139.470 1.00 34.20  ? 261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 118.299 134.711 138.820 1.00 28.57  ? 261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.855 133.766 140.466 1.00 23.97  ? 261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.960 134.522 140.140 1.00 28.52  ? 261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.171 129.858 138.195 1.00 28.77  ? 262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.261 128.904 139.293 1.00 29.86  ? 262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 115.808 127.555 138.848 1.00 39.06  ? 262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 116.470 126.872 139.635 1.00 43.32  ? 262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 113.888 128.717 139.936 1.00 34.70  ? 262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.357 129.902 140.737 1.00 32.16  ? 262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 111.904 129.676 141.111 1.00 30.60  ? 262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.210 130.121 141.968 1.00 30.69  ? 262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 115.545 127.154 137.602 1.00 44.68  ? 263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.000 125.858 137.116 1.00 37.79  ? 263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 117.514 125.773 136.981 1.00 42.39  ? 263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.042 124.665 136.844 1.00 50.47  ? 263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.347 125.540 135.770 1.00 42.01  ? 263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 113.894 125.133 135.910 1.00 47.19  ? 263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 113.494 124.720 137.017 1.00 48.18  ? 263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.151 125.228 134.911 1.00 46.81  ? 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.219 126.906 137.012 1.00 41.78  ? 264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 119.674 126.886 136.928 1.00 40.99  ? 264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.316 126.178 138.114 1.00 44.66  ? 264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 121.429 125.659 137.981 1.00 48.59  ? 264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.215 128.311 136.825 1.00 42.53  ? 264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 119.793 129.068 137.965 1.00 44.73  ? 264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 119.704 128.985 135.564 1.00 39.56  ? 264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 119.645 126.145 139.264 1.00 39.66  ? 265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.170 125.499 140.458 1.00 42.08  ? 265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 119.677 124.070 140.632 1.00 47.73  ? 265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.053 123.414 141.608 1.00 50.88  ? 265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 119.817 126.323 141.700 1.00 43.31  ? 265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 120.703 127.537 141.896 1.00 43.09  ? 265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.171 127.150 141.849 1.00 44.25  ? 265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.069 128.365 141.971 1.00 42.30  ? 265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.500 128.017 141.759 1.00 41.78  ? 265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 118.846 123.573 139.719 1.00 55.96  ? 266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 118.417 122.183 139.780 1.00 52.88  ? 266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 119.587 121.256 139.477 1.00 59.92  ? 266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 120.406 121.530 138.595 1.00 58.67  ? 266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 117.283 121.932 138.789 1.00 53.75  ? 266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 115.901 122.299 139.302 1.00 56.29  ? 266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 114.835 121.950 138.277 1.00 58.27  ? 266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 113.448 121.939 138.894 1.00 56.54  ? 266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 112.380 121.810 137.864 1.00 55.23  ? 266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 119.666 120.150 140.219 1.00 65.40  ? 267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 120.702 119.157 139.955 1.00 66.81  ? 267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 120.445 118.470 138.618 1.00 66.44  ? 267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 121.380 118.187 137.859 1.00 62.34  ? 267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 120.803 118.135 141.107 1.00 65.87  ? 267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.129 118.803 142.453 1.00 66.32  ? 267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 121.843 117.069 140.791 1.00 64.05  ? 267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 119.964 119.463 143.168 1.00 64.95  ? 267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 119.176 118.207 138.303 1.00 66.43  ? 268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 118.818 117.561 137.046 1.00 68.89  ? 268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 118.992 118.470 135.837 1.00 69.65  ? 268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 118.882 117.988 134.704 1.00 66.41  ? 268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 117.373 117.061 137.111 1.00 70.39  ? 268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 116.481 118.120 137.413 1.00 68.19  ? 268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 119.250 119.760 136.044 1.00 77.72  ? 269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 119.390 120.683 134.926 1.00 77.06  ? 269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 120.626 120.353 134.099 1.00 77.51  ? 269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 121.686 120.019 134.638 1.00 77.76  ? 269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 119.467 122.122 135.436 1.00 73.24  ? 269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 120.484 120.449 132.781 1.00 80.09  ? 270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.592 120.181 131.879 1.00 80.86  ? 270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 122.634 121.292 131.960 1.00 80.89  ? 270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 122.354 122.419 132.378 1.00 81.18  ? 270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.090 120.032 130.443 1.00 82.89  ? 270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 120.269 121.221 129.986 1.00 82.32  ? 270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 120.868 122.239 129.579 1.00 80.20  ? 270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 119.024 121.138 130.032 1.00 80.50  ? 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 123.858 120.959 131.541 1.00 81.83  ? 271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 124.967 121.905 131.618 1.00 84.11  ? 271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 124.765 123.122 130.726 1.00 82.00  ? 271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 125.424 124.145 130.940 1.00 80.11  ? 271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.278 121.206 131.252 1.00 82.68  ? 271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 126.788 120.249 132.317 1.00 81.98  ? 271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.243 120.967 133.571 1.00 83.21  ? 271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 127.822 122.068 133.452 1.00 80.90  ? 271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.022 120.432 134.678 1.00 82.72  ? 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 123.878 123.039 129.735 1.00 81.24  ? 272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 123.618 124.172 128.857 1.00 83.57  ? 272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 122.712 125.219 129.489 1.00 82.21  ? 272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.531 126.292 128.903 1.00 79.90  ? 272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 122.999 123.687 127.543 1.00 83.06  ? 272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 124.003 122.979 126.653 1.00 84.00  ? 272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 125.220 123.123 126.895 1.00 83.34  ? 272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 123.575 122.280 125.711 1.00 81.81  ? 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.138 124.938 130.659 1.00 76.38  ? 273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.240 125.874 131.324 1.00 75.71  ? 273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 121.646 126.024 132.786 1.00 73.60  ? 273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 121.088 126.851 133.515 1.00 76.15  ? 273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 119.774 125.417 131.196 1.00 75.71  ? 273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.426 124.415 132.290 1.00 77.06  ? 273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 118.834 126.614 131.232 1.00 72.38  ? 273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 122.628 125.239 133.217 1.00 70.30  ? 274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.052 125.206 134.610 1.00 70.52  ? 274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.223 126.153 134.831 1.00 70.80  ? 274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.210 126.113 134.089 1.00 71.69  ? 274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 123.447 123.788 135.026 1.00 72.28  ? 274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 123.826 123.651 136.491 1.00 71.61  ? 274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 124.450 122.294 136.774 1.00 72.27  ? 274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.354 122.336 137.918 1.00 71.77  ? 274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 126.651 122.604 137.839 1.00 73.07  ? 274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 127.235 122.858 136.680 1.00 72.47  ? 274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 127.378 122.619 138.952 1.00 71.16  ? 274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.108 127.001 135.850 1.00 61.10  ? 275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.201 127.854 136.298 1.00 58.28  ? 275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 125.793 127.241 137.559 1.00 59.01  ? 275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.126 126.488 138.278 1.00 59.13  ? 275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 124.741 129.307 136.550 1.00 53.74  ? 275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 124.063 129.871 135.313 1.00 49.83  ? 275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 123.811 129.372 137.749 1.00 54.23  ? 275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.061 127.563 137.824 1.00 52.49  ? 276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 127.759 126.949 138.946 1.00 55.82  ? 276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.341 127.967 139.920 1.00 51.91  ? 276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.313 127.724 141.133 1.00 58.29  ? 276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 128.870 126.022 138.429 1.00 59.43  ? 276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.853 125.554 139.489 1.00 59.49  ? 276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.224 125.294 138.889 1.00 59.16  ? 276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 131.171 124.165 137.873 1.00 59.95  ? 276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 131.315 122.832 138.519 1.00 56.72  ? 276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 128.850 129.100 139.441 1.00 42.83  ? 277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 129.365 130.141 140.321 1.00 48.07  ? 277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 128.401 131.296 140.539 1.00 46.65  ? 277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 128.757 132.237 141.259 1.00 46.70  ? 277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 130.690 130.703 139.784 1.00 50.25  ? 277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 130.425 131.784 138.882 1.00 47.07  ? 277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 131.471 129.621 139.058 1.00 45.68  ? 277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.209 131.268 139.949 1.00 38.74  ? 278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 126.227 132.336 140.115 1.00 32.36  ? 278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.219 131.934 141.182 1.00 29.29  ? 278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 124.335 131.110 140.939 1.00 38.13  ? 278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.528 132.644 138.797 1.00 33.75  ? 278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 125.366 134.130 138.479 1.00 32.64  ? 278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 126.579 134.909 138.935 1.00 34.69  ? 278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.117 134.344 137.005 1.00 35.69  ? 278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.351 132.520 142.369 1.00 28.68  ? 279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.282 132.447 143.351 1.00 26.09  ? 279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.055 133.172 142.819 1.00 24.96  ? 279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.159 134.217 142.173 1.00 40.98  ? 279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.730 133.067 144.673 1.00 27.45  ? 279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 125.836 132.367 145.215 1.00 31.25  ? 279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.880 132.611 143.080 1.00 24.65  ? 280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.635 133.156 142.557 1.00 25.93  ? 280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 119.801 133.678 143.717 1.00 24.67  ? 280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 119.780 133.085 144.800 1.00 31.54  ? 280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.850 132.118 141.727 1.00 28.61  ? 280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.422 130.926 142.581 1.00 31.07  ? 280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 120.674 131.655 140.537 1.00 31.41  ? 280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.216 130.196 142.033 1.00 22.44  ? 280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 119.150 134.811 143.494 1.00 13.89  ? 281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 118.231 135.364 144.467 1.00 5.64   ? 281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 116.932 135.759 143.800 1.00 15.52  ? 281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.904 136.190 142.650 1.00 30.80  ? 281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.845 135.603 144.547 1.00 20.29  ? 282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 114.501 135.865 144.048 1.00 17.44  ? 282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.894 136.996 144.862 1.00 23.52  ? 282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 113.903 136.953 146.097 1.00 39.01  ? 282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.619 134.606 144.103 1.00 17.27  ? 282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.155 134.979 144.021 1.00 26.02  ? 282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 113.983 133.667 142.970 1.00 28.56  ? 282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 113.374 138.003 144.170 1.00 16.77  ? 283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 112.748 139.160 144.795 1.00 15.92  ? 283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 111.243 138.940 144.784 1.00 19.05  ? 283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 110.632 138.833 143.713 1.00 34.62  ? 283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.129 140.457 144.070 1.00 15.14  ? 283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 112.494 141.649 144.748 1.00 13.13  ? 283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 114.640 140.600 144.020 1.00 14.28  ? 283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 110.643 138.874 145.966 1.00 17.08  ? 284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 109.234 138.532 146.121 1.00 20.64  ? 284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 108.500 139.769 146.630 1.00 27.59  ? 284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 108.622 140.118 147.813 1.00 28.98  ? 284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.042 137.345 147.073 1.00 20.18  ? 284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.828 136.132 146.576 1.00 16.62  ? 284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 107.566 137.007 147.209 1.00 24.46  ? 284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.473 134.843 147.275 1.00 24.35  ? 284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 107.733 140.460 145.791 1.00 34.01  ? 285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 106.858 141.520 146.297 1.00 34.46  ? 285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 105.712 140.936 147.108 1.00 36.43  ? 285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 105.413 139.742 147.048 1.00 33.44  ? 285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 106.345 142.205 145.025 1.00 32.35  ? 285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 107.274 141.766 143.937 1.00 29.79  ? 285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 107.737 140.401 144.321 1.00 30.17  ? 285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.067 141.808 147.889 1.00 42.76  ? 286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 103.913 141.383 148.671 1.00 37.57  ? 286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 102.766 140.909 147.792 1.00 45.91  ? 286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 101.914 140.145 148.260 1.00 51.15  ? 286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 103.433 142.521 149.575 1.00 42.35  ? 286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.125 142.529 150.922 1.00 52.31  ? 286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.121 141.793 151.084 1.00 53.96  ? 286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 103.676 143.274 151.818 1.00 49.35  ? 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 102.723 141.347 146.531 1.00 42.92  ? 287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 101.663 140.910 145.631 1.00 34.06  ? 287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 101.736 139.410 145.377 1.00 40.54  ? 287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 100.704 138.736 145.302 1.00 53.49  ? 287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 101.737 141.683 144.315 1.00 36.89  ? 287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 100.534 141.472 143.413 1.00 36.82  ? 287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 99.241  141.606 144.200 1.00 43.89  ? 287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.025  141.491 143.300 1.00 44.66  ? 287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 96.761  141.703 144.056 1.00 41.69  ? 287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.949 138.869 145.233 1.00 32.03  ? 288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.093 137.432 145.026 1.00 29.77  ? 288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.596 136.648 146.233 1.00 33.94  ? 288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 101.932 135.615 146.082 1.00 40.15  ? 288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 104.551 137.085 144.731 1.00 31.71  ? 288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.762 135.650 144.348 1.00 34.00  ? 288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.501 135.217 143.060 1.00 33.97  ? 288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.213 134.730 145.280 1.00 31.07  ? 288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 104.694 133.897 142.707 1.00 36.62  ? 288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.404 133.410 144.934 1.00 30.75  ? 288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.145 132.992 143.646 1.00 37.98  ? 288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.908 137.121 147.440 1.00 41.51  ? 289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.439 136.448 148.645 1.00 36.29  ? 289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 100.923 136.547 148.753 1.00 40.87  ? 289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.255 135.605 149.194 1.00 44.40  ? 289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.137 137.031 149.886 1.00 37.80  ? 289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 102.775 136.230 151.126 1.00 36.70  ? 289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.643 137.057 149.681 1.00 39.47  ? 289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 100.355 137.688 148.351 1.00 45.21  ? 290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.904  137.832 148.351 1.00 40.25  ? 290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.252  136.860 147.375 1.00 47.27  ? 290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.227  136.245 147.689 1.00 54.04  ? 290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 98.522  139.272 148.009 1.00 41.22  ? 290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.728  140.255 149.148 1.00 48.69  ? 290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 98.675  141.699 148.688 1.00 53.38  ? 290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 97.734  142.054 147.947 1.00 54.86  ? 290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 99.576  142.479 149.065 1.00 48.96  ? 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.831  136.714 146.181 1.00 39.97  ? 291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.279  135.794 145.191 1.00 39.45  ? 291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.397  134.346 145.651 1.00 45.65  ? 291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.470  133.551 145.457 1.00 50.13  ? 291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 98.978  135.984 143.847 1.00 38.37  ? 291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.815  137.345 143.174 1.00 36.20  ? 291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.867  137.528 142.096 1.00 36.48  ? 291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 97.420  137.495 142.597 1.00 44.96  ? 291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.533  133.982 146.249 1.00 42.71  ? 292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 99.700  132.620 146.747 1.00 41.49  ? 292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 98.752  132.332 147.904 1.00 41.93  ? 292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 98.218  131.223 148.015 1.00 42.13  ? 292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.150 132.389 147.168 1.00 35.92  ? 292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 98.540  133.316 148.780 1.00 46.59  ? 293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 97.635  133.130 149.909 1.00 48.30  ? 293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.206  132.889 149.442 1.00 53.14  ? 293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 95.509  132.017 149.974 1.00 54.46  ? 293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 97.701  134.348 150.829 1.00 48.18  ? 293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 96.665  134.363 151.936 1.00 48.19  ? 293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.574  135.744 152.559 1.00 48.39  ? 293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 97.896  136.317 152.780 1.00 57.32  ? 293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.262  137.529 152.385 1.00 55.54  ? 293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.424  138.332 151.752 1.00 52.37  ? 293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 99.502  137.944 152.632 1.00 47.17  ? 293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 95.754  133.646 148.446 1.00 56.44  ? 294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.399  133.524 147.929 1.00 57.47  ? 294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.262  132.436 146.871 1.00 56.51  ? 294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.155  132.217 146.371 1.00 55.27  ? 294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 93.934  134.866 147.355 1.00 54.60  ? 294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 93.601  135.910 148.409 1.00 57.55  ? 294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 92.434  135.500 149.288 1.00 62.28  ? 294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 91.354  135.191 148.741 1.00 61.42  ? 294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 92.598  135.486 150.526 1.00 57.21  ? 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 95.358  131.767 146.516 1.00 56.36  ? 295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 95.391  130.649 145.575 1.00 56.66  ? 295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 94.961  131.038 144.166 1.00 59.23  ? 295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 94.705  130.154 143.338 1.00 57.23  ? 295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 94.538  129.473 146.072 1.00 57.61  ? 295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 95.134  128.128 145.709 1.00 60.01  ? 295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.162  128.102 144.999 1.00 56.82  ? 295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 94.574  127.095 146.132 1.00 58.40  ? 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 94.871  132.330 143.865 1.00 63.38  ? 296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 94.566  132.758 142.508 1.00 61.80  ? 296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 95.741  132.463 141.585 1.00 60.89  ? 296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 96.904  132.514 141.990 1.00 60.97  ? 296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.245  134.251 142.468 1.00 61.70  ? 296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 93.868  134.848 143.808 1.00 62.42  ? 296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.719  136.357 143.711 1.00 62.78  ? 296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.352  136.744 143.176 1.00 61.28  ? 296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.280  136.523 144.184 1.00 59.11  ? 296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 95.428  132.150 140.331 1.00 56.58  ? 297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 96.474  131.936 139.342 1.00 55.39  ? 297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.176  133.253 139.040 1.00 54.15  ? 297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.527  134.260 138.743 1.00 51.92  ? 297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 95.886  131.337 138.066 1.00 52.43  ? 297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 98.500  133.245 139.119 1.00 43.76  ? 298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.300  134.444 138.929 1.00 43.71  ? 298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.895  134.475 137.527 1.00 46.39  ? 298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 99.905  133.480 136.801 1.00 50.67  ? 298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.409 134.525 139.982 1.00 43.38  ? 298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.397 135.648 137.152 1.00 39.33  ? 299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.007 135.859 135.848 1.00 35.93  ? 299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 102.399 136.439 136.033 1.00 35.97  ? 299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 102.567 137.444 136.729 1.00 46.71  ? 299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.162 136.801 134.985 1.00 37.45  ? 299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.791  136.267 134.644 1.00 40.61  ? 299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.594  135.474 133.523 1.00 41.65  ? 299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 97.695  136.559 135.441 1.00 44.54  ? 299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.342  134.984 133.207 1.00 42.53  ? 299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 96.440  136.075 135.134 1.00 40.88  ? 299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.270  135.288 134.016 1.00 41.86  ? 299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.019  134.804 133.706 1.00 43.21  ? 299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.386 135.809 135.419 1.00 30.31  ? 300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 104.703 136.414 135.274 1.00 27.55  ? 300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 104.740 137.117 133.927 1.00 37.85  ? 300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.177 136.638 132.936 1.00 44.06  ? 300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 105.832 135.373 135.414 1.00 31.24  ? 300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.904 134.865 136.843 1.00 39.90  ? 300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.623 134.223 134.454 1.00 36.99  ? 300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.398 138.269 133.884 1.00 37.67  ? 301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.270 139.184 132.765 1.00 31.73  ? 301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.566 139.260 131.971 1.00 36.96  ? 301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 107.649 138.928 132.462 1.00 40.41  ? 301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 104.874 140.582 133.247 1.00 33.27  ? 301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 103.697 140.585 134.176 1.00 36.83  ? 301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.406 140.573 133.678 1.00 34.52  ? 301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 103.881 140.597 135.546 1.00 33.06  ? 301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.323 140.570 134.529 1.00 36.02  ? 301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 102.801 140.596 136.403 1.00 37.21  ? 301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 101.520 140.584 135.893 1.00 39.28  ? 301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.431 139.700 130.722 1.00 41.69  ? 302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 107.578 139.960 129.869 1.00 41.80  ? 302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.027 141.400 130.078 1.00 41.98  ? 302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.258 142.323 129.780 1.00 45.35  ? 302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.224 139.725 128.410 1.00 40.95  ? 302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 106.999 138.270 128.050 1.00 39.73  ? 302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 105.876 137.587 128.499 1.00 35.09  ? 302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 107.903 137.584 127.255 1.00 41.88  ? 302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 105.667 136.263 128.172 1.00 38.23  ? 302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 107.702 136.261 126.920 1.00 41.93  ? 302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 106.582 135.606 127.381 1.00 43.62  ? 302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.380 134.285 127.052 1.00 47.04  ? 302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.233 141.636 130.600 1.00 35.42  ? 303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.623 143.011 130.956 1.00 36.29  ? 303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.635 143.983 129.789 1.00 39.56  ? 303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.309 145.162 129.982 1.00 43.15  ? 303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.028 142.829 131.546 1.00 37.93  ? 303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.068 141.412 131.991 1.00 37.67  ? 303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.254 140.654 130.992 1.00 32.40  ? 303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.002 143.536 128.586 1.00 38.27  ? 304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.104 144.470 127.469 1.00 38.22  ? 304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.736 144.969 127.027 1.00 44.13  ? 304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.610 146.121 126.601 1.00 48.89  ? 304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 110.835 143.825 126.295 1.00 41.86  ? 304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.099 144.765 125.162 1.00 45.30  ? 304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 111.708 145.988 125.339 1.00 41.84  ? 304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 110.837 144.663 123.838 1.00 43.46  ? 304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 111.809 146.600 124.172 1.00 42.00  ? 304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.289 145.818 123.245 1.00 46.57  ? 304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.705 144.126 127.116 1.00 38.42  ? 305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.355 144.586 126.810 1.00 35.88  ? 305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 105.919 145.678 127.779 1.00 38.02  ? 305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.323 146.682 127.370 1.00 42.75  ? 305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.379 143.412 126.850 1.00 40.62  ? 305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.391 142.825 128.156 1.00 44.94  ? 305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 105.774 142.360 125.826 1.00 41.10  ? 305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.224 145.505 129.066 1.00 43.45  ? 306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 105.902 146.527 130.058 1.00 39.93  ? 306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.680 147.805 129.780 1.00 41.54  ? 306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.148 148.913 129.905 1.00 43.63  ? 306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.173 145.995 131.477 1.00 36.86  ? 306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.295 144.777 131.761 1.00 39.88  ? 306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 105.931 147.081 132.510 1.00 41.25  ? 306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.564 144.135 133.091 1.00 42.15  ? 306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 107.956 147.673 129.408 1.00 43.36  ? 307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.756 148.851 129.089 1.00 41.49  ? 307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.186 149.601 127.891 1.00 41.82  ? 307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.111 150.835 127.899 1.00 47.55  ? 307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.206 148.449 128.825 1.00 39.25  ? 307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.168 149.612 128.856 1.00 46.13  ? 307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.186 150.493 129.928 1.00 46.94  ? 307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 112.050 149.837 127.809 1.00 45.70  ? 307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.060 151.561 129.961 1.00 43.91  ? 307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.927 150.903 127.833 1.00 48.25  ? 307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 112.927 151.762 128.912 1.00 48.03  ? 307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.799 152.826 128.943 1.00 46.83  ? 307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 107.786 148.873 126.847 1.00 41.35  ? 308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.209 149.515 125.672 1.00 40.70  ? 308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 105.878 150.181 125.996 1.00 44.41  ? 308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.592 151.280 125.507 1.00 47.19  ? 308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.036 148.496 124.547 1.00 43.04  ? 308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.340 147.961 123.983 1.00 40.96  ? 308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.096 147.108 122.749 1.00 45.04  ? 308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.140 145.964 123.048 1.00 44.07  ? 308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.786 144.634 122.884 1.00 42.24  ? 308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.049 149.533 126.819 1.00 43.70  ? 309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.723 150.073 127.099 1.00 44.71  ? 309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 103.786 151.279 128.030 1.00 47.81  ? 309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.074 152.267 127.820 1.00 50.08  ? 309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 102.830 148.986 127.695 1.00 45.59  ? 309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.536 148.763 126.933 1.00 48.73  ? 309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.462 149.775 127.287 1.00 50.05  ? 309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 100.722 150.656 128.131 1.00 53.12  ? 309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.352  149.685 126.721 1.00 46.94  ? 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.634 151.222 129.059 1.00 45.93  ? 310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.624 152.224 130.115 1.00 47.15  ? 310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 105.850 153.125 130.134 1.00 45.81  ? 310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 105.792 154.197 130.742 1.00 49.16  ? 310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.491 151.543 131.485 1.00 49.46  ? 310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.244 150.698 131.622 1.00 49.42  ? 310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.050 151.253 132.059 1.00 45.85  ? 310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.261 149.347 131.303 1.00 45.69  ? 310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 100.909 150.485 132.181 1.00 46.96  ? 310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.125 148.573 131.420 1.00 44.92  ? 310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 100.953 149.145 131.861 1.00 48.84  ? 310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 99.819  148.376 131.981 1.00 48.95  ? 310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 106.945 152.727 129.492 1.00 43.47  ? 311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.156 153.517 129.504 1.00 44.78  ? 311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.045 153.312 130.708 1.00 44.80  ? 311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.096 153.959 130.798 1.00 49.63  ? 311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.663 152.440 131.637 1.00 42.65  ? 312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.468 152.131 132.807 1.00 43.41  ? 312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.647 150.624 132.910 1.00 43.41  ? 312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 108.782 149.851 132.493 1.00 45.95  ? 312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.830 152.668 134.098 1.00 44.75  ? 312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.094 153.984 133.931 1.00 47.63  ? 312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 106.925 154.121 134.884 1.00 50.81  ? 312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 107.000 153.708 136.040 1.00 49.67  ? 312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 105.832 154.702 134.400 1.00 47.10  ? 312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 110.783 150.216 133.467 1.00 45.85  ? 313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.057 148.799 133.645 1.00 46.74  ? 313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.104 148.202 134.674 1.00 46.60  ? 313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.571 148.901 135.538 1.00 47.00  ? 313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.506 148.590 134.075 1.00 44.60  ? 313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.506 149.121 133.096 1.00 47.86  ? 313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 113.898 148.419 131.977 1.00 47.64  ? 313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.190 150.289 133.065 1.00 44.69  ? 313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 114.781 149.129 131.301 1.00 43.96  ? 313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 114.976 150.269 131.939 1.00 47.56  ? 313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 109.891 146.888 134.567 1.00 45.45  ? 314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 108.913 146.223 135.424 1.00 44.47  ? 314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.283 146.347 136.897 1.00 44.96  ? 314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.412 146.580 137.744 1.00 44.96  ? 314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.784 144.753 135.025 1.00 42.01  ? 314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 107.829 143.956 135.896 1.00 40.00  ? 314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 107.787 142.213 135.444 1.00 51.27  ? 314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 109.358 141.663 136.102 1.00 40.74  ? 314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.566 146.198 137.225 1.00 40.01  ? 315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 110.995 146.312 138.612 1.00 44.13  ? 315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.034 147.754 139.107 1.00 43.52  ? 315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.160 147.971 140.316 1.00 46.19  ? 315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.369 145.660 138.799 1.00 39.42  ? 315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.448 146.312 137.958 1.00 44.32  ? 315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.113 147.133 137.080 1.00 47.63  ? 315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 114.638 146.000 138.178 1.00 43.65  ? 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 110.931 148.735 138.211 1.00 40.58  ? 316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 110.879 150.135 138.611 1.00 40.88  ? 316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.488 150.583 139.040 1.00 46.74  ? 316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.362 151.653 139.646 1.00 44.51  ? 316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.369 151.029 137.470 1.00 43.33  ? 316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.826 150.826 137.101 1.00 45.09  ? 316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 113.765 151.519 138.065 1.00 51.31  ? 316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 113.326 152.471 138.743 1.00 49.57  ? 316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.944 151.117 138.143 1.00 51.52  ? 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.452 149.808 138.742 1.00 48.31  ? 317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.087 150.148 139.110 1.00 47.37  ? 317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 106.638 149.336 140.318 1.00 50.99  ? 317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.214 148.297 140.651 1.00 45.28  ? 317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.131 149.913 137.936 1.00 45.82  ? 317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 106.806 149.904 136.578 1.00 46.21  ? 317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 105.645 149.776 135.206 1.00 52.26  ? 317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 104.791 151.343 135.334 1.00 49.08  ? 317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 105.593 149.829 140.976 1.00 53.26  ? 318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.042 149.162 142.149 1.00 48.38  ? 318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.224 147.957 141.706 1.00 49.17  ? 318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.205 148.108 141.024 1.00 49.07  ? 318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.183 150.130 142.958 1.00 50.01  ? 318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.089 149.743 144.421 1.00 54.99  ? 318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 104.938 148.954 144.884 1.00 51.52  ? 318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.165 150.227 145.107 1.00 54.87  ? 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 104.670 146.760 142.093 1.00 47.63  ? 319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 103.972 145.546 141.686 1.00 45.46  ? 319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.567 145.486 142.271 1.00 44.16  ? 319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.617 145.109 141.576 1.00 49.34  ? 319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 104.776 144.315 142.100 1.00 45.08  ? 319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.407 143.060 141.338 1.00 47.70  ? 319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 105.213 142.960 139.730 1.00 58.09  ? 319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 103.840 143.340 138.650 1.00 42.97  ? 319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.415 145.867 143.542 1.00 46.91  ? 320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.111 145.793 144.193 1.00 51.19  ? 320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.079 146.663 143.490 1.00 49.68  ? 320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 98.893  146.315 143.456 1.00 46.85  ? 320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.236 146.199 145.661 1.00 50.36  ? 320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.076 145.228 146.463 1.00 50.56  ? 320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 103.287 145.127 146.267 1.00 42.85  ? 320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 101.436 144.508 147.376 1.00 49.91  ? 320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.505 147.792 142.928 1.00 54.32  ? 321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.597  148.682 142.218 1.00 55.20  ? 321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.471  148.328 140.741 1.00 54.32  ? 321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.374  148.405 140.178 1.00 50.45  ? 321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.062 150.135 142.370 1.00 52.76  ? 321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 99.815  151.011 141.150 1.00 55.02  ? 321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 99.842  152.492 141.475 1.00 57.11  ? 321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 99.067  152.923 142.355 1.00 56.83  ? 321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 100.638 153.224 140.851 1.00 57.36  ? 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.567 147.921 140.105 1.00 46.74  ? 322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 100.602 147.753 138.659 1.00 43.75  ? 322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.284 146.334 138.206 1.00 46.06  ? 322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.220 146.092 136.997 1.00 50.56  ? 322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 101.979 148.163 138.123 1.00 44.74  ? 322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.270 149.658 138.202 1.00 49.59  ? 322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.190 150.731 137.233 1.00 51.37  ? 322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 100.980 149.778 135.735 1.00 46.93  ? 322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.075 145.393 139.130 1.00 44.49  ? 323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 99.831  144.008 138.731 1.00 40.53  ? 323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 98.515  143.869 137.976 1.00 45.32  ? 323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.458  143.226 136.921 1.00 50.66  ? 323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 99.842  143.096 139.957 1.00 42.56  ? 323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 99.499  141.656 139.645 1.00 44.37  ? 323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 100.467 140.777 139.183 1.00 44.01  ? 323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.207  141.176 139.813 1.00 45.19  ? 323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.159 139.463 138.897 1.00 38.55  ? 323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 97.890  139.864 139.529 1.00 42.62  ? 323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.870  139.011 139.072 1.00 41.50  ? 323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.559  137.703 138.788 1.00 45.65  ? 323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.440  144.453 138.509 1.00 48.27  ? 324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.146  144.357 137.842 1.00 46.33  ? 324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.163  145.082 136.503 1.00 45.68  ? 324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 95.532  144.633 135.539 1.00 50.31  ? 324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.047  144.914 138.744 1.00 47.43  ? 324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 94.757  144.014 139.929 1.00 50.45  ? 324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 94.715  142.780 139.744 1.00 47.18  ? 324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 94.574  144.541 141.047 1.00 51.86  ? 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 96.879  146.205 136.425 1.00 47.64  ? 325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 96.989  146.924 135.161 1.00 49.34  ? 325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 97.765  146.113 134.129 1.00 51.44  ? 325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.418  146.119 132.943 1.00 60.57  ? 325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 97.642  148.285 135.392 1.00 48.71  ? 325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 96.801  149.219 136.247 1.00 49.47  ? 325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.442  150.588 136.385 1.00 51.08  ? 325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 96.592  151.502 137.252 1.00 49.78  ? 325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.323  152.737 137.646 1.00 52.63  ? 325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 98.818  145.414 134.558 1.00 43.85  ? 326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 99.541  144.528 133.648 1.00 39.09  ? 326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 98.649  143.389 133.173 1.00 41.35  ? 326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 98.639  143.045 131.985 1.00 47.53  ? 326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 100.787 143.963 134.332 1.00 42.47  ? 326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 101.828 144.990 134.667 1.00 41.44  ? 326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 101.814 146.241 134.079 1.00 44.57  ? 326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 102.828 144.695 135.574 1.00 42.09  ? 326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 102.781 147.173 134.393 1.00 42.30  ? 326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 103.793 145.625 135.893 1.00 46.01  ? 326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 103.768 146.865 135.301 1.00 46.00  ? 326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 97.896  142.786 134.095 1.00 45.48  ? 327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.067  141.637 133.745 1.00 47.89  ? 327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 95.946  142.049 132.798 1.00 51.09  ? 327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 95.605  141.318 131.861 1.00 51.12  ? 327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 96.524  140.967 135.021 1.00 41.80  ? 327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 95.425  139.973 134.683 1.00 47.41  ? 327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 97.650  140.276 135.767 1.00 40.31  ? 327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.372  143.230 133.009 1.00 46.68  ? 328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.296  143.718 132.158 1.00 47.20  ? 328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 94.801  144.381 130.884 1.00 51.02  ? 328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 93.985  144.852 130.085 1.00 56.52  ? 328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.416  144.700 132.936 1.00 49.78  ? 328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 92.765  144.064 134.147 1.00 53.81  ? 328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.644  142.821 134.174 1.00 53.24  ? 328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.372  144.805 135.073 1.00 51.34  ? 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.117  144.432 130.675 1.00 47.92  ? 329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 96.684  145.081 129.501 1.00 47.10  ? 329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 96.935  144.037 128.422 1.00 51.37  ? 329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.805  143.172 128.606 1.00 46.74  ? 329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 97.978  145.793 129.861 1.00 42.32  ? 329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.323  146.904 128.893 1.00 45.65  ? 329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.354  147.557 129.027 1.00 48.71  ? 329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 97.457  147.125 127.913 1.00 51.03  ? 329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.212  144.065 127.299 1.00 55.29  ? 330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.505  143.112 126.215 1.00 49.62  ? 330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 97.872  143.308 125.588 1.00 49.38  ? 330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.410  142.356 125.010 1.00 51.61  ? 330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.383  143.376 125.203 1.00 49.25  ? 330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 94.951  144.778 125.477 1.00 48.43  ? 330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.099  144.968 126.957 1.00 49.95  ? 330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.451  144.506 125.681 1.00 45.57  ? 331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.760  144.771 125.101 1.00 47.34  ? 331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 100.908 144.279 125.973 1.00 46.98  ? 331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.046 144.230 125.497 1.00 43.48  ? 331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 99.920  146.270 124.836 1.00 46.45  ? 331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.091  146.780 123.671 1.00 45.67  ? 331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 98.961  148.296 123.700 1.00 48.27  ? 331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.175  148.767 124.834 1.00 48.69  ? 331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 96.860  148.634 124.948 1.00 48.52  ? 331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.140  148.043 124.007 1.00 50.90  ? 331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.251  149.110 126.030 1.00 44.04  ? 331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.641 143.919 127.223 1.00 46.74  ? 332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.659 143.376 128.114 1.00 44.63  ? 332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.574 141.857 128.040 1.00 47.00  ? 332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.625 141.253 128.544 1.00 50.07  ? 332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.476 143.877 129.552 1.00 43.73  ? 332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.363 143.093 130.505 1.00 41.52  ? 332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 101.774 145.365 129.639 1.00 40.70  ? 332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.561 141.239 127.398 1.00 47.68  ? 333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.580 139.788 127.287 1.00 43.17  ? 333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 102.904 139.161 128.636 1.00 40.63  ? 333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 103.711 139.687 129.407 1.00 44.70  ? 333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.599 139.347 126.236 1.00 43.55  ? 333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.457 137.896 125.808 1.00 45.37  ? 333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.593 137.466 124.899 1.00 41.45  ? 333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.514 135.981 124.589 1.00 44.08  ? 333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.608 135.542 123.680 1.00 48.11  ? 333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.266 138.029 128.923 1.00 39.39  ? 334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.457 137.348 130.194 1.00 40.02  ? 334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.087 135.883 130.028 1.00 43.57  ? 334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.418 135.498 129.066 1.00 48.27  ? 334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.618 137.989 131.303 1.00 39.47  ? 334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.141 138.083 130.971 1.00 40.79  ? 334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.496  139.275 131.647 1.00 42.56  ? 334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 98.311  139.779 130.844 1.00 39.04  ? 334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.713  140.804 129.845 1.00 45.64  ? 334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.533 135.071 130.982 1.00 39.59  ? 335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.196 133.656 131.025 1.00 44.95  ? 335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.677 133.312 132.413 1.00 43.07  ? 335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.124 133.883 133.412 1.00 46.10  ? 335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.403 132.778 130.651 1.00 44.68  ? 335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.231 132.282 131.821 1.00 45.44  ? 335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.615 131.828 131.401 1.00 49.58  ? 335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.862 131.713 130.182 1.00 44.32  ? 335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 106.458 131.587 132.290 1.00 49.87  ? 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.714 132.397 132.466 1.00 46.82  ? 336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.050 132.062 133.717 1.00 42.24  ? 336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 100.885 131.071 134.518 1.00 41.80  ? 336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.364 130.068 133.977 1.00 47.51  ? 336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.661  131.486 133.443 1.00 43.72  ? 336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.017  130.814 134.644 1.00 47.66  ? 336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 96.711  130.137 134.264 1.00 47.00  ? 336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.631  131.157 133.948 1.00 45.58  ? 336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.684  132.320 134.876 1.00 44.75  ? 336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.059 131.355 135.808 1.00 37.92  ? 337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 101.768 130.480 136.729 1.00 39.00  ? 337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 100.904 130.284 137.968 1.00 46.16  ? 337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 99.942  131.013 138.208 1.00 46.88  ? 337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.151 131.032 137.127 1.00 35.27  ? 337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 102.994 132.372 137.847 1.00 41.47  ? 337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.047 131.170 135.909 1.00 39.78  ? 337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 103.984 132.585 138.964 1.00 38.33  ? 337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.263 129.274 138.758 1.00 42.27  ? 338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 100.608 129.037 140.035 1.00 40.39  ? 338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 101.510 129.559 141.141 1.00 42.14  ? 338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 102.575 128.970 141.385 1.00 43.64  ? 338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 100.323 127.549 140.230 1.00 40.85  ? 338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 99.331  127.286 141.344 1.00 42.31  ? 338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.582  127.604 142.506 1.00 44.24  ? 338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 98.193  126.700 140.995 1.00 42.46  ? 338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.150 130.651 141.820 1.00 39.38  ? 339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.053 131.209 142.840 1.00 35.81  ? 339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 102.342 130.255 143.983 1.00 38.20  ? 339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 103.456 130.267 144.516 1.00 41.57  ? 339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.308 132.462 143.320 1.00 38.63  ? 339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 99.884  132.216 142.978 1.00 42.19  ? 339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 99.887  131.400 141.724 1.00 38.80  ? 339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 101.374 129.426 144.378 1.00 40.80  ? 340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 101.631 128.442 145.424 1.00 38.94  ? 340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 102.559 127.335 144.945 1.00 39.45  ? 340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 103.441 126.901 145.694 1.00 42.25  ? 340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 100.311 127.855 145.927 1.00 37.27  ? 340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.234 127.726 147.438 1.00 40.82  ? 340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 98.873  127.224 147.883 1.00 39.83  ? 340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 97.979  128.326 148.214 1.00 43.04  ? 340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.008  128.258 149.116 1.00 42.65  ? 340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 96.771  127.148 149.794 1.00 38.57  ? 340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.259  129.333 149.343 1.00 42.72  ? 340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 102.389 126.878 143.703 1.00 40.69  ? 341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 103.325 125.911 143.139 1.00 39.32  ? 341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 104.717 126.513 143.007 1.00 38.27  ? 341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 105.719 125.826 143.229 1.00 39.92  ? 341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 102.821 125.416 141.784 1.00 43.32  ? 341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 101.603 124.505 141.860 1.00 46.89  ? 341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 101.690 123.545 143.035 1.00 46.55  ? 341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.506 122.313 142.680 1.00 43.25  ? 341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.842 121.493 141.629 1.00 44.55  ? 341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 104.801 127.796 142.647 1.00 41.96  ? 342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 106.100 128.456 142.574 1.00 40.26  ? 342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 106.735 128.580 143.954 1.00 39.18  ? 342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 107.953 128.432 144.097 1.00 41.92  ? 342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 105.958 129.830 141.919 1.00 31.99  ? 342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.268 130.556 141.614 1.00 32.11  ? 342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.219 129.642 140.861 1.00 34.25  ? 342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.006 131.819 140.819 1.00 35.70  ? 342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 105.929 128.859 144.981 1.00 38.11  ? 343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 106.453 128.894 146.344 1.00 38.63  ? 343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 106.964 127.525 146.775 1.00 40.50  ? 343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 108.010 127.420 147.428 1.00 41.46  ? 343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 105.376 129.390 147.307 1.00 39.48  ? 343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 105.318 130.899 147.542 1.00 37.50  ? 343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 104.295 131.229 148.612 1.00 34.45  ? 343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 106.687 131.430 147.927 1.00 40.98  ? 343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 106.234 126.464 146.431 1.00 43.06  ? 344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 106.699 125.117 146.746 1.00 39.62  ? 344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 107.985 124.788 145.995 1.00 40.62  ? 344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 108.875 124.123 146.538 1.00 46.88  ? 344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 105.607 124.097 146.427 1.00 41.19  ? 344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 104.364 124.241 147.288 1.00 45.24  ? 344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 103.181 123.470 146.742 1.00 52.68  ? 344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 103.378 122.655 145.815 1.00 52.04  ? 344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 102.053 123.680 147.234 1.00 47.82  ? 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 108.096 125.242 144.745 1.00 36.84  ? 345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 109.335 125.065 143.995 1.00 37.42  ? 345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 110.488 125.806 144.661 1.00 40.01  ? 345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 111.605 125.285 144.740 1.00 38.89  ? 345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 109.150 125.544 142.556 1.00 34.98  ? 345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 110.387 125.397 141.689 1.00 38.59  ? 345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.152 125.947 140.294 1.00 39.20  ? 345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 111.351 125.700 139.395 1.00 41.58  ? 345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.132 126.234 138.023 1.00 41.79  ? 345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 110.233 127.023 145.140 1.00 42.30  ? 346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 111.249 127.762 145.884 1.00 32.55  ? 346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 111.685 126.990 147.120 1.00 35.31  ? 346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 112.882 126.870 147.402 1.00 36.48  ? 346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 110.714 129.137 146.286 1.00 33.03  ? 346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 110.455 130.187 145.210 1.00 36.90  ? 346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 109.735 131.371 145.819 1.00 41.21  ? 346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 111.756 130.630 144.587 1.00 32.06  ? 346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 110.718 126.463 147.872 1.00 39.79  ? 347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 111.038 125.728 149.093 1.00 31.04  ? 347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 111.860 124.483 148.790 1.00 40.26  ? 347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 112.835 124.189 149.491 1.00 48.88  ? 347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 109.756 125.358 149.835 1.00 31.91  ? 347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 111.489 123.742 147.744 1.00 43.35  ? 348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 112.238 122.538 147.402 1.00 40.50  ? 348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 113.630 122.882 146.880 1.00 42.05  ? 348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 114.594 122.156 147.150 1.00 46.42  ? 348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 111.450 121.693 146.397 1.00 44.71  ? 348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 111.531 122.144 144.951 1.00 48.70  ? 348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 112.652 121.141 143.961 1.00 62.99  ? 348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.699 122.094 142.447 1.00 48.30  ? 348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 113.764 123.996 146.154 1.00 37.11  ? 349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 115.083 124.427 145.703 1.00 37.30  ? 349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 115.972 124.809 146.878 1.00 37.06  ? 349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 117.163 124.484 146.890 1.00 41.40  ? 349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 114.953 125.596 144.729 1.00 38.75  ? 349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 114.746 125.244 143.257 1.00 38.80  ? 349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 113.833 126.257 142.597 1.00 38.48  ? 349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 116.080 125.171 142.535 1.00 41.94  ? 349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 115.417 125.513 147.867 1.00 34.88  ? 350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 116.201 125.855 149.050 1.00 34.48  ? 350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 116.566 124.609 149.849 1.00 40.91  ? 350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 117.663 124.524 150.413 1.00 45.94  ? 350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 115.444 126.855 149.925 1.00 34.11  ? 350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 114.962 128.089 149.190 1.00 31.05  ? 350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 114.639 129.218 150.151 1.00 34.81  ? 350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.762 130.132 150.317 1.00 39.44  ? 350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.226 130.543 151.488 1.00 40.74  ? 350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 115.682 130.142 152.626 1.00 36.41  ? 350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 117.261 131.377 151.519 1.00 39.59  ? 350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 115.656 123.636 149.918 1.00 40.64  ? 351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 115.957 122.394 150.622 1.00 42.18  ? 351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 117.066 121.612 149.925 1.00 47.16  ? 351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 117.931 121.030 150.589 1.00 52.89  ? 351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 114.696 121.540 150.744 1.00 42.21  ? 351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 113.562 122.340 151.022 1.00 49.37  ? 351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 117.058 121.587 148.592 1.00 46.26  ? 352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 118.012 120.758 147.864 1.00 45.36  ? 352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 119.354 121.450 147.642 1.00 48.19  ? 352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 120.380 120.769 147.542 1.00 54.55  ? 352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 117.407 120.322 146.526 1.00 48.70  ? 352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.562 121.326 145.396 1.00 50.50  ? 352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.791 120.927 144.154 1.00 55.33  ? 352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 115.692 120.353 144.297 1.00 50.63  ? 352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.275 121.198 143.036 1.00 58.56  ? 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 119.377 122.781 147.562 1.00 42.67  ? 353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 120.614 123.492 147.255 1.00 45.08  ? 353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 120.867 124.731 148.100 1.00 42.13  ? 353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 121.992 125.237 148.076 1.00 40.32  ? 353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 120.639 123.895 145.774 1.00 43.01  ? 353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 119.701 124.923 145.509 1.00 40.34  ? 353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 119.882 125.240 148.839 1.00 33.02  ? 354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 120.042 126.465 149.594 1.00 34.65  ? 354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 119.712 127.730 148.834 1.00 30.39  ? 354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 119.684 128.808 149.439 1.00 36.33  ? 354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 119.456 127.633 147.537 1.00 29.94  ? 355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.079 128.747 146.688 1.00 27.38  ? 355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 117.591 128.687 146.371 1.00 31.66  ? 355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 116.984 127.611 146.408 1.00 37.10  ? 355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 119.893 128.724 145.387 1.00 32.59  ? 355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 121.380 128.870 145.600 1.00 36.19  ? 355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 121.928 130.081 145.997 1.00 28.63  ? 355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 122.237 127.795 145.409 1.00 38.68  ? 355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.285 130.219 146.194 1.00 33.58  ? 355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 123.598 127.924 145.604 1.00 38.18  ? 355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.116 129.138 145.997 1.00 36.80  ? 355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 125.470 129.274 146.193 1.00 38.08  ? 355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 116.962 129.823 146.047 1.00 29.70  ? 356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 117.507 131.176 145.893 1.00 26.30  ? 356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.511 131.999 147.172 1.00 28.48  ? 356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 116.966 131.595 148.195 1.00 31.52  ? 356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.562 131.785 144.860 1.00 27.76  ? 356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.234 131.207 145.252 1.00 23.30  ? 356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 115.526 129.793 145.712 1.00 20.89  ? 356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.134 133.174 147.129 1.00 32.10  ? 357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 117.998 134.140 148.210 1.00 18.46  ? 357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.629 134.798 148.121 1.00 24.89  ? 357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.340 135.515 147.158 1.00 35.06  ? 357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.103 135.191 148.136 1.00 20.60  ? 357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.505 134.639 148.033 1.00 21.65  ? 357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 120.853 133.455 148.663 1.00 24.26  ? 357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 121.487 135.310 147.318 1.00 24.61  ? 357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.131 132.949 148.580 1.00 23.37  ? 357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.771 134.811 147.228 1.00 26.38  ? 357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.087 133.630 147.863 1.00 29.69  ? 357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.362 133.124 147.783 1.00 36.10  ? 357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.786 134.558 149.118 1.00 29.41  ? 358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.431 135.097 149.133 1.00 29.64  ? 358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.489 136.529 149.645 1.00 27.98  ? 358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 114.893 136.773 150.786 1.00 35.84  ? 358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.500 134.237 150.000 1.00 29.87  ? 358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.575 132.770 149.576 1.00 26.12  ? 358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.074 134.749 149.910 1.00 28.15  ? 358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.011 132.502 148.202 1.00 31.80  ? 358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 114.087 137.475 148.802 1.00 16.46  ? 359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 114.050 138.887 149.157 1.00 12.80  ? 359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 112.613 139.375 149.077 1.00 15.24  ? 359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.990 139.307 148.013 1.00 31.31  ? 359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 114.949 139.713 148.236 1.00 15.58  ? 359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.040 141.175 148.630 1.00 18.66  ? 359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 114.989 142.296 147.227 1.00 34.30  ? 359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 114.974 143.870 148.069 1.00 15.99  ? 359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 112.091 139.865 150.197 1.00 18.71  ? 360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 110.735 140.402 150.253 1.00 17.61  ? 360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 110.816 141.895 149.969 1.00 25.64  ? 360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.141 142.690 150.853 1.00 34.54  ? 360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 110.095 140.111 151.605 1.00 19.04  ? 360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.063 138.652 151.953 1.00 21.92  ? 360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 109.282 137.770 151.224 1.00 24.39  ? 360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 110.818 138.160 153.002 1.00 25.51  ? 360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 109.254 136.427 151.539 1.00 23.23  ? 360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 110.793 136.820 153.322 1.00 23.89  ? 360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.009 135.951 152.590 1.00 25.55  ? 360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 110.507 142.277 148.726 1.00 27.85  ? 361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 110.720 143.653 148.288 1.00 22.41  ? 361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 109.895 144.640 149.103 1.00 22.94  ? 361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 110.392 145.705 149.486 1.00 30.97  ? 361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.389 143.785 146.803 1.00 24.42  ? 361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 111.275 144.761 146.056 1.00 26.21  ? 361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 110.752 145.076 144.672 1.00 32.69  ? 361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 109.751 144.514 144.231 1.00 41.56  ? 361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 111.430 145.981 143.975 1.00 32.23  ? 361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 108.632 144.311 149.375 1.00 28.72  ? 362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 107.785 145.241 150.112 1.00 25.84  ? 362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 108.169 145.308 151.584 1.00 27.04  ? 362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 107.941 146.334 152.233 1.00 34.97  ? 362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 106.317 144.851 149.957 1.00 32.03  ? 362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 105.742 145.274 148.619 1.00 40.61  ? 362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 105.229 146.409 148.525 1.00 42.75  ? 362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.805 144.475 147.663 1.00 39.12  ? 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 108.751 144.236 152.125 1.00 31.71  ? 363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 109.283 144.298 153.481 1.00 21.51  ? 363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 110.496 145.213 153.556 1.00 22.43  ? 363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 110.782 145.779 154.618 1.00 28.50  ? 363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 109.647 142.899 153.972 1.00 17.52  ? 363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 108.459 142.151 154.534 1.00 23.79  ? 363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 107.379 142.716 154.703 1.00 28.07  ? 363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 108.652 140.874 154.829 1.00 24.55  ? 363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 111.221 145.363 152.448 1.00 21.73  ? 364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 112.364 146.266 152.414 1.00 20.87  ? 364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 111.909 147.704 152.211 1.00 19.33  ? 364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 112.380 148.619 152.895 1.00 23.82  ? 364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 113.348 145.830 151.316 1.00 14.54  ? 364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 114.578 146.716 151.332 1.00 16.53  ? 364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 113.724 144.374 151.486 1.00 10.29  ? 364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 110.983 147.925 151.278 1.00 24.45  ? 365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 110.602 149.270 150.874 1.00 19.57  ? 365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 109.570 149.911 151.791 1.00 21.67  ? 365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 109.336 151.119 151.677 1.00 28.32  ? 365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.072 149.249 149.439 1.00 21.63  ? 365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 111.112 148.777 148.445 1.00 20.22  ? 365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 112.150 149.412 148.269 1.00 23.69  ? 365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 110.840 147.657 147.789 1.00 22.70  ? 365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 108.947 149.147 152.692 1.00 22.79  ? 366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 107.999 149.753 153.621 1.00 26.69  ? 366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 108.713 150.580 154.680 1.00 29.24  ? 366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 108.137 151.538 155.210 1.00 33.94  ? 366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.135 148.676 154.278 1.00 24.40  ? 366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 107.903 147.689 155.141 1.00 34.60  ? 366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 106.982 146.983 156.121 1.00 32.37  ? 366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 105.966 146.120 155.394 1.00 27.70  ? 366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.172 145.285 156.337 1.00 29.00  ? 366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 109.956 150.231 154.998 1.00 28.89  ? 367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 110.768 150.955 155.965 1.00 24.17  ? 367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.044 151.496 155.323 1.00 23.14  ? 367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 112.966 151.905 156.019 1.00 25.06  ? 367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 111.086 150.076 157.188 1.00 22.47  ? 367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 109.829 149.841 158.007 1.00 24.80  ? 367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 111.681 148.757 156.741 1.00 18.51  ? 367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.104 151.495 153.993 1.00 24.05  ? 368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 113.258 152.020 153.279 1.00 13.93  ? 368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 113.234 153.542 153.314 1.00 22.74  ? 368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.235 154.166 152.946 1.00 28.44  ? 368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 113.260 151.518 151.837 1.00 13.03  ? 368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 114.458 151.941 151.047 1.00 13.05  ? 368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 114.378 152.339 149.731 1.00 25.72  ? 368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 115.766 152.021 151.385 1.00 14.42  ? 368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 115.584 152.648 149.292 1.00 18.84  ? 368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 116.445 152.463 150.275 1.00 18.75  ? 368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 114.339 154.137 153.763 1.00 26.76  ? 369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 114.404 155.582 153.925 1.00 21.48  ? 369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 114.637 156.320 152.615 1.00 30.37  ? 369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 114.316 157.509 152.526 1.00 35.88  ? 369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 115.506 155.947 154.918 1.00 20.94  ? 369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.177 155.650 151.601 1.00 30.55  ? 370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 115.565 156.287 150.348 1.00 20.32  ? 370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 114.724 155.789 149.176 1.00 22.51  ? 370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.237 155.551 148.082 1.00 26.14  ? 370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.048 156.064 150.073 1.00 14.42  ? 370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 117.936 156.711 151.115 1.00 17.54  ? 370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 117.937 157.930 151.275 1.00 33.17  ? 370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 118.696 155.896 151.834 1.00 16.19  ? 370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 113.418 155.620 149.395 1.00 21.31  ? 371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 112.532 155.208 148.313 1.00 19.55  ? 371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 112.399 156.275 147.236 1.00 23.30  ? 371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.074 155.944 146.091 1.00 29.21  ? 371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.150 154.855 148.864 1.00 16.85  ? 371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.091 153.452 149.426 1.00 24.35  ? 371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 111.875 152.586 149.045 1.00 23.31  ? 371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.153 153.219 150.337 1.00 20.11  ? 371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 112.633 157.544 147.576 1.00 26.18  ? 372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 112.593 158.601 146.571 1.00 25.84  ? 372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 113.711 158.431 145.551 1.00 30.18  ? 372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 113.504 158.648 144.351 1.00 35.09  ? 372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 112.679 159.970 147.242 1.00 28.56  ? 372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.003 160.247 147.882 1.00 32.34  ? 372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 114.510 159.477 148.906 1.00 28.14  ? 372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 114.928 161.205 147.638 1.00 34.67  ? 372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 115.690 159.948 149.266 1.00 28.10  ? 372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 115.966 160.998 148.514 1.00 36.31  ? 372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 114.907 158.058 146.011 1.00 25.33  ? 373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.010 157.788 145.094 1.00 26.78  ? 373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 115.677 156.596 144.210 1.00 32.20  ? 373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 115.763 156.667 142.978 1.00 38.72  ? 373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.311 157.556 145.885 1.00 25.35  ? 373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 117.655 158.795 146.707 1.00 26.33  ? 373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 118.451 157.192 144.949 1.00 27.07  ? 373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 118.646 158.539 147.807 1.00 24.28  ? 373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.269 155.491 144.833 1.00 23.79  ? 374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 114.863 154.276 144.140 1.00 15.72  ? 374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.366 153.253 145.150 1.00 23.95  ? 374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 114.777 153.277 146.315 1.00 31.03  ? 374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.020 153.691 143.329 1.00 22.31  ? 374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 115.912 152.283 143.230 1.00 19.44  ? 374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 113.484 152.358 144.724 1.00 31.11  ? 375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.154 151.211 145.552 1.00 18.61  ? 375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.312 150.220 145.542 1.00 23.99  ? 375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.118 150.184 144.610 1.00 36.13  ? 375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 111.877 150.535 145.054 1.00 24.35  ? 375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 110.674 151.458 144.970 1.00 24.56  ? 375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.069 151.685 146.342 1.00 33.75  ? 375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 108.759 152.445 146.250 1.00 29.08  ? 375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 107.630 151.654 146.813 1.00 23.76  ? 375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 114.394 149.415 146.595 1.00 22.61  ? 376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 115.417 148.377 146.674 1.00 21.54  ? 376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 114.928 147.186 145.860 1.00 24.43  ? 376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.035 146.452 146.288 1.00 29.69  ? 376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 115.712 147.980 148.123 1.00 15.52  ? 376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 116.847 146.977 148.165 1.00 19.66  ? 376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.051 149.206 148.949 1.00 12.06  ? 376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 115.510 146.995 144.678 1.00 23.06  ? 377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.047 145.966 143.761 1.00 17.33  ? 377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 115.772 144.639 143.926 1.00 19.00  ? 377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.310 143.632 143.379 1.00 28.91  ? 377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.202 146.445 142.315 1.00 25.97  ? 377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 114.472 147.740 142.018 1.00 24.55  ? 377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.256 148.592 141.042 1.00 23.44  ? 377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 114.872 150.052 141.162 1.00 23.60  ? 377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 115.827 150.930 140.432 1.00 23.05  ? 377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 116.882 144.611 144.656 1.00 15.43  ? 378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 117.657 143.388 144.824 1.00 8.81   ? 378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 118.660 143.598 145.950 1.00 15.26  ? 378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 118.895 144.724 146.398 1.00 26.17  ? 378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 118.361 142.981 143.525 1.00 13.86  ? 378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 119.497 143.882 143.130 1.00 13.29  ? 378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 119.279 145.220 142.848 1.00 19.64  ? 378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 120.782 143.384 143.026 1.00 11.09  ? 378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 120.319 146.042 142.480 1.00 13.19  ? 378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 121.825 144.204 142.658 1.00 14.78  ? 378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 121.592 145.533 142.384 1.00 17.36  ? 378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 119.247 142.495 146.400 1.00 17.11  ? 379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 120.211 142.485 147.487 1.00 8.87   ? 379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 121.589 142.097 146.955 1.00 11.27  ? 379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 121.797 141.955 145.745 1.00 22.35  ? 379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 119.746 141.537 148.594 1.00 16.63  ? 379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 120.243 141.953 149.851 1.00 21.20  ? 379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 122.538 141.932 147.869 1.00 8.91   ? 380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 123.906 141.595 147.510 1.00 12.28  ? 380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 124.080 140.078 147.477 1.00 23.32  ? 380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 123.116 139.313 147.559 1.00 26.39  ? 380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 124.885 142.251 148.480 1.00 11.55  ? 380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 124.819 141.653 149.866 1.00 15.20  ? 380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 123.746 141.535 150.452 1.00 28.43  ? 380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 125.973 141.272 150.401 1.00 20.35  ? 380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 125.330 139.630 147.352 1.00 24.17  ? 381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 125.629 138.204 147.356 1.00 19.11  ? 381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 125.313 137.552 148.696 1.00 19.95  ? 381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 125.047 136.346 148.737 1.00 24.66  ? 381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 127.101 137.994 146.990 1.00 19.49  ? 381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.712 136.594 147.066 1.00 28.11  ? 381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.043 135.656 146.079 1.00 27.11  ? 381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 129.206 136.664 146.815 1.00 23.31  ? 381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 125.323 138.318 149.785 1.00 24.51  ? 382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.996 137.808 151.108 1.00 7.27   ? 382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 123.598 138.211 151.560 1.00 11.70  ? 382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 123.234 137.955 152.711 1.00 25.57  ? 382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 126.034 138.280 152.126 1.00 22.55  ? 382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.712 137.683 151.816 1.00 31.07  ? 382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 122.815 138.834 150.678 1.00 14.95  ? 383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 121.416 139.179 150.941 1.00 12.55  ? 383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 121.263 140.020 152.207 1.00 18.56  ? 383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 120.373 139.791 153.028 1.00 26.95  ? 383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 120.544 137.926 151.018 1.00 21.46  ? 383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 120.920 137.104 152.106 1.00 25.76  ? 383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 122.142 141.010 152.371 1.00 17.35  ? 384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 122.048 141.931 153.495 1.00 8.36   ? 384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 122.215 143.392 153.113 1.00 18.96  ? 384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.003 144.257 153.970 1.00 33.65  ? 384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 123.088 141.580 154.572 1.00 12.97  ? 384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 124.378 140.988 154.037 1.00 19.13  ? 384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 125.419 142.039 153.729 1.00 24.58  ? 384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 125.253 143.188 154.184 1.00 28.16  ? 384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 126.404 141.717 153.032 1.00 27.97  ? 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 122.578 143.700 151.873 1.00 11.04  ? 385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 122.780 145.072 151.425 1.00 8.24   ? 385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 121.546 145.486 150.637 1.00 18.00  ? 385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 121.404 145.147 149.458 1.00 29.39  ? 385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.053 145.210 150.583 1.00 10.77  ? 385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.206 146.635 150.094 1.00 15.41  ? 385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 125.265 144.794 151.393 1.00 17.52  ? 385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 120.650 146.220 151.290 1.00 20.79  ? 386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 119.391 146.664 150.701 1.00 10.70  ? 386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 119.449 148.179 150.548 1.00 13.72  ? 386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.118 148.923 151.474 1.00 14.59  ? 386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 118.218 146.225 151.554 1.00 7.88   ? 386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 118.141 144.710 151.718 1.00 4.89   ? 386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 117.064 144.344 152.694 1.00 12.61  ? 386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 117.876 144.062 150.376 1.00 10.83  ? 386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 119.870 148.630 149.370 1.00 19.96  ? 387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.068 150.043 149.097 1.00 10.07  ? 387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 119.395 150.425 147.788 1.00 15.59  ? 387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.182 149.584 146.911 1.00 23.09  ? 387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 121.557 150.390 149.029 1.00 9.75   ? 387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.336 149.966 150.252 1.00 14.90  ? 387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 123.740 150.513 150.257 1.00 13.28  ? 387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.064 151.420 149.494 1.00 22.51  ? 387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 124.585 149.969 151.122 1.00 17.89  ? 387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.052 151.704 147.674 1.00 16.64  ? 388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 118.501 152.223 146.432 1.00 13.80  ? 388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 119.568 152.230 145.346 1.00 23.87  ? 388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 120.723 152.592 145.589 1.00 33.00  ? 388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 117.954 153.633 146.639 1.00 22.61  ? 388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.177 151.826 144.141 1.00 22.15  ? 389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.090 151.787 143.011 1.00 13.22  ? 389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.366 152.259 141.762 1.00 17.54  ? 389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.161 152.050 141.605 1.00 29.43  ? 389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 120.656 150.380 142.790 1.00 17.01  ? 389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.627 149.406 142.828 1.00 28.28  ? 389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.120 152.893 140.871 1.00 22.13  ? 390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 119.611 153.359 139.591 1.00 20.14  ? 390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.394 152.686 138.476 1.00 24.41  ? 390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 121.620 152.566 138.552 1.00 29.73  ? 390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 119.719 154.881 139.473 1.00 16.79  ? 390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 118.867 155.638 140.477 1.00 22.74  ? 390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.065 157.137 140.396 1.00 32.84  ? 390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 119.940 157.621 139.679 1.00 31.39  ? 390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.250 157.883 141.132 1.00 25.74  ? 390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 119.686 152.243 137.447 1.00 28.37  ? 391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.318 151.513 136.356 1.00 27.75  ? 391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.082 152.489 135.472 1.00 37.62  ? 391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 120.679 153.646 135.292 1.00 29.71  ? 391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.273 150.711 135.560 1.00 24.64  ? 391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.481 151.612 134.623 1.00 28.39  ? 391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 119.945 149.584 134.796 1.00 28.71  ? 391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.211 152.032 134.941 1.00 42.01  ? 392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.054 152.840 134.071 1.00 31.18  ? 392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 122.779 152.474 132.621 1.00 35.09  ? 392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.825 151.296 132.253 1.00 39.32  ? 392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.532 152.633 134.399 1.00 28.37  ? 392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 124.770 152.782 135.786 1.00 33.32  ? 392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 122.494 153.485 131.804 1.00 39.99  ? 393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.226 153.281 130.381 1.00 36.11  ? 393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 123.541 153.440 129.631 1.00 38.04  ? 393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 123.917 154.534 129.211 1.00 40.29  ? 393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.167 154.257 129.886 1.00 40.93  ? 393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.935 154.096 128.499 1.00 46.72  ? 393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.253 152.330 129.464 1.00 38.86  ? 394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 125.514 152.332 128.736 1.00 37.12  ? 394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.227 152.345 127.240 1.00 40.18  ? 394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 124.640 151.398 126.707 1.00 39.95  ? 394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.354 151.118 129.122 1.00 31.73  ? 394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 126.775 151.115 130.573 1.00 36.17  ? 394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 127.778 151.961 131.025 1.00 35.74  ? 394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.161 150.277 131.493 1.00 35.63  ? 394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.165 151.965 132.350 1.00 34.83  ? 394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 126.542 150.274 132.820 1.00 35.21  ? 394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 127.543 151.120 133.244 1.00 41.62  ? 394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 127.926 151.122 134.566 1.00 45.58  ? 394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 125.638 153.415 126.570 1.00 43.53  ? 395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.334 153.609 125.162 1.00 45.62  ? 395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.465 153.045 124.304 1.00 45.55  ? 395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.377 152.377 124.795 1.00 45.14  ? 395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.088 155.089 124.880 1.00 45.71  ? 395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.267 155.838 125.197 1.00 46.21  ? 395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 123.931 155.603 125.719 1.00 44.48  ? 395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.409 153.310 123.002 1.00 45.20  ? 396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.421 152.825 122.080 1.00 44.20  ? 396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 128.759 153.514 122.345 1.00 50.06  ? 396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 128.857 154.476 123.111 1.00 54.86  ? 396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 126.985 153.058 120.635 1.00 46.93  ? 396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 125.732 152.286 120.271 1.00 50.37  ? 396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 125.442 151.272 120.939 1.00 52.67  ? 396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.039 152.692 119.316 1.00 49.56  ? 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 129.803 152.997 121.703 1.00 42.51  ? 397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.114 153.619 121.802 1.00 41.52  ? 397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.081 155.015 121.189 1.00 47.07  ? 397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 130.335 155.284 120.243 1.00 48.39  ? 397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.168 152.755 121.108 1.00 43.37  ? 397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 133.583 153.024 121.564 1.00 45.41  ? 397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.332 154.048 121.001 1.00 44.38  ? 397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.169 152.255 122.559 1.00 44.84  ? 397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.623 154.299 121.414 1.00 45.61  ? 397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 135.462 152.497 122.978 1.00 41.26  ? 397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.184 153.520 122.402 1.00 46.09  ? 397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 137.471 153.766 122.817 1.00 46.38  ? 397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.889 155.911 121.756 1.00 51.64  ? 398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.929 157.332 121.420 1.00 54.24  ? 398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.621 158.044 121.740 1.00 57.14  ? 398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.427 159.193 121.324 1.00 54.79  ? 398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 132.303 157.561 119.947 1.00 54.63  ? 398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 133.801 157.548 119.718 1.00 59.12  ? 398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 134.484 158.479 120.196 1.00 56.88  ? 398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 134.297 156.609 119.060 1.00 57.12  ? 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.719 157.390 122.465 1.00 58.42  ? 399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.476 157.986 122.928 1.00 53.43  ? 399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.491 158.020 124.450 1.00 56.94  ? 399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 128.812 157.013 125.091 1.00 57.10  ? 399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.267 157.198 122.423 1.00 51.62  ? 399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.187 158.050 121.781 1.00 56.66  ? 399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.137 157.218 121.074 1.00 60.01  ? 399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.988 157.367 119.843 1.00 58.79  ? 399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 124.462 156.412 121.748 1.00 59.53  ? 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.158 159.175 125.021 1.00 54.52  ? 400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.199 159.331 126.468 1.00 50.80  ? 400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.178 158.416 127.133 1.00 52.29  ? 400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.015 158.361 126.720 1.00 54.48  ? 400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 127.937 160.787 126.851 1.00 51.68  ? 400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 128.803 161.787 126.106 1.00 54.03  ? 400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.283 161.568 126.345 1.00 57.12  ? 400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 130.682 161.422 127.519 1.00 54.39  ? 400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.048 161.540 125.358 1.00 55.08  ? 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 127.616 157.698 128.162 1.00 42.60  ? 401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 126.749 156.790 128.896 1.00 43.04  ? 401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.023 157.532 130.008 1.00 45.61  ? 401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 126.576 158.441 130.632 1.00 46.48  ? 401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 127.551 155.628 129.484 1.00 43.13  ? 401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.585 155.085 128.519 1.00 49.60  ? 401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.321 155.088 127.300 1.00 54.10  ? 401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 129.660 154.650 128.981 1.00 46.23  ? 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 124.775 157.137 130.250 1.00 40.80  ? 402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 123.986 157.676 131.355 1.00 39.75  ? 402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.297 156.841 132.589 1.00 33.57  ? 402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 123.712 155.776 132.800 1.00 37.94  ? 402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 122.497 157.661 131.022 1.00 43.01  ? 402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.095 158.594 129.887 1.00 41.89  ? 402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.441 158.043 128.516 1.00 45.97  ? 402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.102 156.873 128.240 1.00 46.74  ? 402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.051 158.780 127.714 1.00 42.77  ? 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.225 157.324 133.407 1.00 31.08  ? 403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 125.704 156.567 134.557 1.00 32.08  ? 403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 124.707 156.702 135.700 1.00 34.89  ? 403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.327 157.816 136.082 1.00 31.01  ? 403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.101 157.047 134.979 1.00 26.52  ? 403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.109 156.815 133.851 1.00 30.09  ? 403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 127.547 156.341 136.243 1.00 28.97  ? 403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.047 155.432 133.248 1.00 31.79  ? 403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.280 155.572 136.243 1.00 29.94  ? 404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.384 155.516 137.375 1.00 18.24  ? 404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.116 155.245 138.671 1.00 25.52  ? 404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.305 155.549 138.817 1.00 38.20  ? 404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.400 154.664 139.628 1.00 27.39  ? 405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 123.949 154.339 140.937 1.00 12.68  ? 405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 123.997 152.826 141.097 1.00 19.63  ? 405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 122.958 152.160 141.039 1.00 24.67  ? 405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.114 154.966 142.053 1.00 17.11  ? 405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 122.920 156.481 142.017 1.00 20.49  ? 405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 121.890 156.906 143.047 1.00 23.71  ? 405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.235 157.199 142.250 1.00 20.38  ? 405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.196 152.291 141.304 1.00 32.25  ? 406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.389 150.886 141.626 1.00 21.68  ? 406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 125.954 150.778 143.032 1.00 28.25  ? 406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 126.935 151.446 143.372 1.00 32.96  ? 406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.321 150.199 140.625 1.00 28.32  ? 406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 125.629 149.863 139.318 1.00 37.83  ? 406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 124.425 150.167 139.183 1.00 37.42  ? 406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.291 149.295 138.425 1.00 34.90  ? 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.344 149.923 143.837 1.00 31.37  ? 407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 125.601 149.900 145.271 1.00 24.39  ? 407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 126.995 149.361 145.554 1.00 18.19  ? 407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.384 148.294 145.065 1.00 26.54  ? 407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.528 149.067 145.990 1.00 17.93  ? 407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.141 149.659 145.741 1.00 14.84  ? 407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 124.835 148.978 147.467 1.00 22.19  ? 407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.047 148.631 145.671 1.00 19.30  ? 407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 127.753 150.113 146.347 1.00 32.57  ? 408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.008 149.662 146.925 1.00 34.60  ? 408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 128.867 149.677 148.439 1.00 37.54  ? 408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 128.492 150.698 149.026 1.00 46.71  ? 408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.177 150.550 146.491 1.00 36.97  ? 408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 130.400 150.453 145.097 1.00 39.20  ? 408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.166 148.546 149.068 1.00 37.30  ? 409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 128.921 148.345 150.491 1.00 38.77  ? 409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.235 148.146 151.235 1.00 40.25  ? 409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 130.931 147.148 151.023 1.00 36.56  ? 409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 127.970 147.167 150.702 1.00 37.64  ? 409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.042 145.915 149.398 1.00 49.87  ? 409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 130.556 149.097 152.112 1.00 30.79  ? 410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 131.730 149.034 152.979 1.00 29.29  ? 410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 131.261 148.491 154.324 1.00 31.32  ? 410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 130.497 149.146 155.036 1.00 37.55  ? 410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 132.374 150.409 153.122 1.00 30.14  ? 410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 132.349 151.200 151.830 1.00 37.42  ? 410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 133.227 151.055 150.983 1.00 40.25  ? 410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 131.335 152.042 151.671 1.00 34.74  ? 410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 131.722 147.297 154.672 1.00 23.03  ? 411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 131.170 146.555 155.794 1.00 16.62  ? 411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 132.048 146.682 157.032 1.00 23.64  ? 411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 133.263 146.880 156.944 1.00 32.59  ? 411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 131.000 145.077 155.434 1.00 22.74  ? 411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 130.243 144.756 154.143 1.00 30.68  ? 411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 129.861 143.289 154.108 1.00 26.93  ? 411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 129.010 145.631 153.999 1.00 25.81  ? 411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 131.408 146.575 158.191 1.00 28.46  ? 412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 132.110 146.554 159.459 1.00 19.38  ? 412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 131.217 145.951 160.514 1.00 21.06  ? 412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 129.997 146.139 160.495 1.00 39.64  ? 412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 131.824 145.222 161.445 1.00 19.48  ? 413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 131.079 144.426 162.408 1.00 14.70  ? 413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 131.416 144.839 163.832 1.00 17.65  ? 413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 132.588 145.007 164.183 1.00 28.39  ? 413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 131.369 142.937 162.225 1.00 22.51  ? 413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.015 142.515 160.923 1.00 34.92  ? 413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 130.378 144.998 164.647 1.00 22.04  ? 414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 130.533 145.180 166.082 1.00 17.72  ? 414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 130.508 143.823 166.767 1.00 28.22  ? 414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 129.650 142.985 166.471 1.00 37.72  ? 414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 129.421 146.064 166.644 1.00 26.92  ? 414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 129.182 147.421 165.992 1.00 34.59  ? 414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.097 148.162 166.742 1.00 31.27  ? 414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 130.466 148.227 165.980 1.00 35.66  ? 414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 131.448 143.607 167.681 1.00 34.04  ? 415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 131.442 142.420 168.531 1.00 31.50  ? 415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 130.558 142.739 169.729 1.00 29.72  ? 415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 130.962 143.469 170.635 1.00 30.04  ? 415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 132.858 142.046 168.948 1.00 25.96  ? 415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 132.968 140.616 169.432 1.00 32.15  ? 415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 132.068 140.100 170.090 1.00 36.96  ? 415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 134.079 139.967 169.110 1.00 37.23  ? 415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 129.339 142.193 169.723 1.00 26.49  ? 416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 128.353 142.546 170.741 1.00 28.05  ? 416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 128.867 142.196 172.132 1.00 28.38  ? 416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 128.670 142.954 173.089 1.00 31.45  ? 416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 127.007 141.862 170.436 1.00 26.98  ? 416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 126.397 142.451 169.164 1.00 21.22  ? 416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 126.051 142.015 171.600 1.00 24.41  ? 416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 125.228 141.672 168.623 1.00 24.11  ? 416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 129.545 141.055 172.263 1.00 28.12  ? 417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 130.108 140.671 173.554 1.00 30.47  ? 417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 131.112 141.707 174.049 1.00 33.85  ? 417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 131.029 142.175 175.190 1.00 40.06  ? 417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 130.766 139.297 173.444 1.00 29.18  ? 417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 131.440 138.733 174.695 1.00 32.44  ? 417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 130.518 138.803 175.901 1.00 32.25  ? 417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 131.901 137.309 174.450 1.00 36.21  ? 417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 132.058 142.091 173.192 1.00 41.72  ? 418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 133.094 143.033 173.596 1.00 33.36  ? 418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 132.567 144.457 173.709 1.00 36.16  ? 418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 133.039 145.219 174.559 1.00 42.02  ? 418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 134.261 142.976 172.611 1.00 33.41  ? 418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 135.016 141.666 172.683 1.00 41.63  ? 418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 135.204 141.104 173.760 1.00 44.34  ? 418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 135.447 141.168 171.532 1.00 41.68  ? 418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 131.606 144.833 172.866 1.00 39.61  ? 419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 130.999 146.156 172.973 1.00 34.20  ? 419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 130.231 146.284 174.283 1.00 36.75  ? 419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 130.311 147.307 174.972 1.00 40.19  ? 419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 130.096 146.428 171.755 1.00 28.76  ? 419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 129.170 147.593 172.026 1.00 37.07  ? 419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 130.937 146.697 170.525 1.00 28.26  ? 419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 129.484 145.242 174.653 1.00 38.50  ? 420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 128.670 145.290 175.860 1.00 35.79  ? 420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 129.517 145.164 177.120 1.00 37.17  ? 420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 129.224 145.812 178.131 1.00 37.00  ? 420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 127.613 144.186 175.812 1.00 31.85  ? 420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 126.448 144.479 174.878 1.00 29.38  ? 420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 125.328 145.757 175.476 1.00 41.20  ? 420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 125.335 145.423 177.234 1.00 39.06  ? 420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 130.568 144.338 177.084 1.00 44.87  ? 421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 131.421 144.188 178.259 1.00 45.40  ? 421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 132.199 145.464 178.558 1.00 46.80  ? 421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 132.522 145.731 179.721 1.00 48.26  ? 421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 132.373 143.005 178.075 1.00 42.42  ? 421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 133.550 143.277 177.158 1.00 49.63  ? 421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 134.813 142.561 177.592 1.00 52.02  ? 421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 135.271 142.799 178.729 1.00 50.81  ? 421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.346 141.761 176.796 1.00 49.58  ? 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 132.511 146.257 177.534 1.00 42.07  ? 422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 133.192 147.529 177.727 1.00 46.51  ? 422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 132.236 148.684 177.983 1.00 51.34  ? 422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 132.698 149.791 178.279 1.00 46.61  ? 422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 134.064 147.856 176.510 1.00 41.59  ? 422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 135.277 146.989 176.383 1.00 45.93  ? 422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 135.285 145.822 175.652 1.00 47.18  ? 422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 136.524 147.122 176.894 1.00 45.68  ? 422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 136.485 145.271 175.719 1.00 47.37  ? 422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 137.255 146.040 176.466 1.00 48.55  ? 422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 130.926 148.450 177.885 1.00 53.67  ? 423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 129.914 149.494 178.050 1.00 51.33  ? 423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 130.205 150.677 177.132 1.00 53.43  ? 423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 130.149 151.842 177.532 1.00 55.71  ? 423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 129.817 149.938 179.510 1.00 51.17  ? 423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 128.905 149.071 180.361 1.00 53.77  ? 423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 129.487 148.855 181.747 1.00 53.77  ? 423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 130.911 148.330 181.670 1.00 56.89  ? 423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 130.952 146.846 181.552 1.00 50.35  ? 423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 130.522 150.363 175.879 1.00 42.91  ? 424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 130.998 151.342 174.910 1.00 43.08  ? 424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 130.239 151.219 173.599 1.00 41.69  ? 424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 130.829 151.145 172.521 1.00 40.10  ? 424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 132.495 151.182 174.669 1.00 43.18  ? 424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 132.758 150.053 173.856 1.00 42.59  ? 424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 128.908 151.182 173.670 1.00 42.73  ? 425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 128.111 151.152 172.445 1.00 33.79  ? 425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 128.310 152.438 171.654 1.00 38.49  ? 425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 128.566 152.409 170.444 1.00 45.38  ? 425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 126.625 150.915 172.768 1.00 35.58  ? 425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 126.394 149.471 173.213 1.00 40.41  ? 425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 125.758 151.236 171.561 1.00 32.16  ? 425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 124.953 149.161 173.536 1.00 43.83  ? 425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 128.220 153.585 172.330 1.00 33.86  ? 426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 128.273 154.867 171.630 1.00 26.46  ? 426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 129.622 155.081 170.957 1.00 34.49  ? 426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 129.691 155.370 169.757 1.00 45.72  ? 426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 127.976 156.004 172.607 1.00 32.33  ? 426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 128.211 157.388 172.032 1.00 37.33  ? 426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 127.786 158.490 172.980 1.00 44.49  ? 426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 127.527 158.190 174.164 1.00 40.82  ? 426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 127.709 159.657 172.541 1.00 40.72  ? 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 130.708 154.940 171.719 1.00 38.42  ? 427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 132.035 155.193 171.170 1.00 29.91  ? 427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 132.384 154.193 170.077 1.00 30.01  ? 427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 132.943 154.572 169.042 1.00 36.19  ? 427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 133.085 155.171 172.282 1.00 35.99  ? 427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 132.635 155.800 173.597 1.00 42.79  ? 427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.048 154.774 174.553 1.00 42.21  ? 427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 131.085 155.419 175.534 1.00 42.91  ? 427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 130.150 154.423 176.126 1.00 39.10  ? 427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 132.059 152.914 170.283 1.00 30.89  ? 428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 132.347 151.916 169.258 1.00 25.61  ? 428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 131.570 152.195 167.981 1.00 31.49  ? 428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 132.132 152.134 166.883 1.00 35.05  ? 428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 132.031 150.512 169.770 1.00 27.52  ? 428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 132.686 150.300 171.025 1.00 32.82  ? 428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 132.503 149.469 168.775 1.00 30.54  ? 428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 130.280 152.512 168.103 1.00 32.55  ? 429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 129.469 152.766 166.915 1.00 28.37  ? 429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 129.977 153.998 166.176 1.00 32.19  ? 429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 130.077 153.999 164.945 1.00 34.11  ? 429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 127.982 152.901 167.295 1.00 28.89  ? 429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 127.192 153.453 166.129 1.00 32.20  ? 429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 127.421 151.555 167.703 1.00 31.31  ? 429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 130.327 155.056 166.912 1.00 34.24  ? 430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 130.791 156.275 166.257 1.00 33.47  ? 430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 132.147 156.075 165.589 1.00 32.31  ? 430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 132.360 156.529 164.457 1.00 39.31  ? 430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 130.840 157.421 167.265 1.00 29.19  ? 430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 129.469 157.832 167.773 1.00 29.77  ? 430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 129.479 159.227 168.364 1.00 32.53  ? 430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.063 159.734 168.575 1.00 36.93  ? 430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.041 161.132 169.084 1.00 37.27  ? 430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 133.077 155.393 166.263 1.00 26.11  ? 431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 134.379 155.132 165.658 1.00 25.16  ? 431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 134.254 154.218 164.447 1.00 31.92  ? 431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 134.947 154.414 163.441 1.00 39.05  ? 431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 135.326 154.528 166.693 1.00 32.59  ? 431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 136.117 155.509 167.559 1.00 36.31  ? 431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 136.825 154.770 168.679 1.00 31.12  ? 431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 137.110 156.285 166.713 1.00 34.49  ? 431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 133.380 153.213 164.521 1.00 29.88  ? 432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 133.153 152.337 163.379 1.00 24.72  ? 432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 132.535 153.097 162.214 1.00 27.79  ? 432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 132.887 152.858 161.055 1.00 33.22  ? 432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 132.264 151.168 163.791 1.00 30.06  ? 432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 131.607 154.011 162.503 1.00 34.44  ? 433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 131.033 154.841 161.450 1.00 31.07  ? 433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 132.098 155.712 160.798 1.00 32.95  ? 433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 132.125 155.858 159.572 1.00 39.25  ? 433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 129.909 155.705 162.023 1.00 30.05  ? 433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.014 154.885 162.783 1.00 36.91  ? 433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 129.139 156.392 160.909 1.00 28.14  ? 433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 132.992 156.291 161.604 1.00 28.62  ? 434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 134.079 157.091 161.047 1.00 26.22  ? 434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.006 156.245 160.182 1.00 28.39  ? 434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 135.431 156.678 159.103 1.00 36.35  ? 434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 134.865 157.764 162.172 1.00 30.60  ? 434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 134.082 158.864 162.852 1.00 37.53  ? 434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 133.155 159.411 162.222 1.00 42.25  ? 434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 134.397 159.186 164.017 1.00 34.17  ? 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 135.335 155.035 160.639 1.00 30.37  ? 435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 136.212 154.160 159.866 1.00 24.42  ? 435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 135.563 153.748 158.550 1.00 30.21  ? 435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 136.225 153.709 157.506 1.00 37.94  ? 435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 136.581 152.928 160.689 1.00 27.08  ? 435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 135.474 152.056 160.825 1.00 32.00  ? 435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 134.267 153.432 158.580 1.00 28.51  ? 436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 133.564 153.069 157.354 1.00 20.60  ? 436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 133.453 154.258 156.408 1.00 27.38  ? 436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 133.535 154.095 155.186 1.00 36.89  ? 436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 132.183 152.514 157.691 1.00 28.23  ? 436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 132.168 151.180 158.436 1.00 28.16  ? 436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 130.783 150.887 158.980 1.00 26.41  ? 436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 132.632 150.067 157.522 1.00 28.32  ? 436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 133.266 155.462 156.954 1.00 25.41  ? 437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 133.271 156.660 156.124 1.00 22.68  ? 437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 134.623 156.854 155.455 1.00 27.02  ? 437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 134.696 157.200 154.270 1.00 39.23  ? 437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 132.912 157.881 156.971 1.00 25.28  ? 437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 131.668 157.650 157.642 1.00 27.48  ? 437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 132.791 159.117 156.101 1.00 29.34  ? 437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 135.707 156.631 156.200 1.00 28.14  ? 438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.040 156.724 155.615 1.00 28.85  ? 438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 137.239 155.685 154.519 1.00 28.23  ? 438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 137.818 155.983 153.468 1.00 40.34  ? 438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.103 156.561 156.700 1.00 34.86  ? 438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 139.505 156.614 156.181 1.00 38.67  ? 438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 140.132 157.794 155.848 1.00 34.14  ? 438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 140.399 155.629 155.929 1.00 38.06  ? 438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 141.354 157.535 155.419 1.00 36.07  ? 438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 141.541 156.228 155.457 1.00 38.92  ? 438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 136.774 154.457 154.751 1.00 30.86  ? 439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 136.907 153.405 153.745 1.00 30.12  ? 439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.135 153.771 152.485 1.00 34.69  ? 439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 136.621 153.584 151.364 1.00 41.79  ? 439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 136.445 152.055 154.321 1.00 28.05  ? 439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 136.314 151.020 153.217 1.00 26.28  ? 439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 137.414 151.578 155.377 1.00 32.21  ? 439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 134.919 154.297 152.649 1.00 29.37  ? 440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.129 154.714 151.497 1.00 30.99  ? 440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 134.804 155.857 150.747 1.00 35.99  ? 440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 134.797 155.887 149.511 1.00 39.53  ? 440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 132.725 155.121 151.945 1.00 33.98  ? 440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 131.888 155.377 150.832 1.00 35.95  ? 440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 135.389 156.809 151.479 1.00 36.70  ? 441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.013 157.960 150.835 1.00 33.11  ? 441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.270 157.564 150.071 1.00 36.60  ? 441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 137.455 157.969 148.918 1.00 41.94  ? 441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 136.338 159.028 151.877 1.00 28.32  ? 441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 135.141 159.840 152.330 1.00 34.31  ? 441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 135.423 160.624 153.595 1.00 41.47  ? 441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 136.589 160.634 154.042 1.00 45.41  ? 441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 134.481 161.234 154.142 1.00 37.55  ? 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.148 156.776 150.694 1.00 38.55  ? 442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 139.397 156.389 150.047 1.00 39.14  ? 442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.198 155.384 148.923 1.00 40.24  ? 442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.139 155.147 148.158 1.00 43.70  ? 442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 140.374 155.814 151.073 1.00 37.69  ? 442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 139.826 154.618 151.641 1.00 36.96  ? 442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 140.644 156.822 152.171 1.00 38.75  ? 442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.016 154.794 148.799 1.00 37.94  ? 443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 137.752 153.804 147.765 1.00 44.91  ? 443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 137.282 154.499 146.495 1.00 40.28  ? 443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 136.246 155.173 146.496 1.00 43.05  ? 443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 136.705 152.792 148.225 1.00 44.50  ? 443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.184 152.094 149.382 1.00 49.29  ? 443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.418 151.800 147.115 1.00 33.93  ? 443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.044 154.336 145.418 1.00 47.29  ? 444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 137.613 154.727 144.083 1.00 50.83  ? 444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 137.779 153.539 143.147 1.00 50.27  ? 444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 138.705 152.739 143.310 1.00 49.72  ? 444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 138.356 155.984 143.590 1.00 52.15  ? 444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 139.823 155.741 143.227 1.00 56.09  ? 444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 140.369 154.642 143.444 1.00 50.17  ? 444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 140.447 156.689 142.704 1.00 56.55  ? 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 136.841 153.380 142.223 1.00 42.60  ? 445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 136.854 152.275 141.274 1.00 45.41  ? 445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 136.666 152.889 139.894 1.00 47.23  ? 445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 135.577 153.361 139.547 1.00 46.66  ? 445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 135.776 151.233 141.594 1.00 40.48  ? 445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.212 150.381 142.786 1.00 37.07  ? 445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 135.544 150.327 140.402 1.00 43.09  ? 445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.154 150.237 143.852 1.00 39.77  ? 445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 137.739 152.900 139.105 1.00 53.09  ? 446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 137.723 153.575 137.815 1.00 56.74  ? 446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 136.981 152.791 136.742 1.00 55.21  ? 446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 136.454 153.401 135.806 1.00 51.84  ? 446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 139.155 153.857 137.351 1.00 52.39  ? 446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 140.123 154.214 138.473 1.00 52.84  ? 446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 139.632 155.412 139.287 1.00 52.70  ? 446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 140.085 156.694 138.756 1.00 53.29  ? 446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 141.352 157.076 138.666 1.00 57.10  ? 446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 142.341 156.313 139.104 1.00 56.30  ? 446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 141.636 158.262 138.134 1.00 55.97  ? 446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 136.921 151.467 136.855 1.00 44.99  ? 447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.315 150.638 135.822 1.00 41.65  ? 447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 134.823 150.411 136.027 1.00 43.70  ? 447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.187 149.787 135.172 1.00 47.65  ? 447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.033 149.289 135.747 1.00 38.92  ? 447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.097 149.258 134.670 1.00 41.12  ? 447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 137.796 149.361 133.482 1.00 47.68  ? 447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.351 149.120 135.082 1.00 37.25  ? 447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.254 150.894 137.128 1.00 40.58  ? 448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 132.815 150.813 137.374 1.00 36.72  ? 448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.282 152.218 137.606 1.00 37.23  ? 448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.302 152.713 138.747 1.00 38.69  ? 448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 132.509 149.916 138.572 1.00 34.31  ? 448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 131.811 152.905 136.562 1.00 37.38  ? 449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 131.373 154.299 136.743 1.00 34.33  ? 449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.219 154.446 137.715 1.00 36.97  ? 449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.177 155.413 138.485 1.00 35.75  ? 449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 130.975 154.731 135.323 1.00 33.75  ? 449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.371 153.601 134.418 1.00 40.06  ? 449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 131.440 152.375 135.243 1.00 36.55  ? 449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.279 153.500 137.706 1.00 39.52  ? 450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.112 153.606 138.573 1.00 28.46  ? 450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 128.461 153.293 140.022 1.00 32.11  ? 450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 127.958 153.953 140.936 1.00 31.65  ? 450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.006 152.682 138.072 1.00 29.50  ? 450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.320 152.298 140.247 1.00 36.08  ? 451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 129.771 151.998 141.605 1.00 31.08  ? 451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 130.511 153.196 142.187 1.00 29.76  ? 451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.286 153.589 143.337 1.00 37.04  ? 451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 130.647 150.732 141.613 1.00 28.82  ? 451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 131.487 150.668 142.878 1.00 29.97  ? 451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 129.784 149.489 141.484 1.00 29.11  ? 451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.397 153.801 141.393 1.00 32.44  ? 452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.137 154.973 141.848 1.00 32.59  ? 452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.208 156.152 142.114 1.00 30.52  ? 452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.347 156.849 143.130 1.00 36.93  ? 452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.196 155.338 140.807 1.00 31.99  ? 452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.105 156.485 141.190 1.00 37.92  ? 452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 134.529 157.266 139.959 1.00 33.31  ? 452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 135.910 157.723 140.048 1.00 40.13  ? 452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 136.285 158.993 139.965 1.00 39.63  ? 452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 135.406 159.962 139.769 1.00 37.38  ? 452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 137.576 159.296 140.076 1.00 40.15  ? 452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.248 156.388 141.215 1.00 33.86  ? 453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.314 157.493 141.395 1.00 27.26  ? 453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 128.471 157.307 142.649 1.00 29.04  ? 453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.269 158.256 143.416 1.00 33.07  ? 453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 128.422 157.625 140.161 1.00 28.31  ? 453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.212 158.514 140.362 1.00 28.97  ? 453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 126.542 158.843 139.041 1.00 27.40  ? 453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.098 158.666 139.107 1.00 26.77  ? 453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.255 159.565 139.595 1.00 31.47  ? 453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 124.681 160.720 140.081 1.00 29.14  ? 453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 122.952 159.299 139.598 1.00 31.59  ? 453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 127.981 156.087 142.883 1.00 29.75  ? 454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.174 155.832 144.069 1.00 25.40  ? 454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.011 155.867 145.339 1.00 29.47  ? 454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 127.507 156.257 146.394 1.00 36.22  ? 454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 126.456 154.492 143.942 1.00 28.10  ? 454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.280 155.466 145.267 1.00 30.65  ? 455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.149 155.596 146.431 1.00 25.66  ? 455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.374 157.059 146.783 1.00 33.19  ? 455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.376 157.426 147.965 1.00 37.27  ? 455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 131.481 154.893 146.174 1.00 28.24  ? 455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.339 154.802 147.418 1.00 36.72  ? 455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 131.991 154.118 148.378 1.00 39.55  ? 455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 133.468 155.499 147.409 1.00 33.88  ? 455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 130.562 157.912 145.774 1.00 40.13  ? 456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 130.789 159.327 146.050 1.00 33.00  ? 456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 129.517 160.020 146.527 1.00 39.21  ? 456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 129.571 160.878 147.416 1.00 43.80  ? 456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.344 160.030 144.812 1.00 30.06  ? 456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.859 160.084 144.763 1.00 39.82  ? 456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 133.356 160.495 143.389 1.00 43.24  ? 456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 134.479 159.589 142.923 1.00 42.02  ? 456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 135.367 159.174 144.042 1.00 37.25  ? 456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.367 159.666 145.957 1.00 32.63  ? 457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.131 160.383 146.250 1.00 28.89  ? 457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 126.402 159.825 147.468 1.00 33.18  ? 457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.042 160.578 148.378 1.00 34.48  ? 457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.210 160.352 145.027 1.00 31.49  ? 457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.172 158.513 147.495 1.00 37.87  ? 458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 125.373 157.915 148.558 1.00 26.88  ? 458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.142 157.860 149.869 1.00 31.54  ? 458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 125.560 158.052 150.942 1.00 39.20  ? 458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 124.930 156.512 148.145 1.00 24.30  ? 458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.143 156.470 146.851 1.00 31.69  ? 458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 122.363 156.487 147.099 1.00 45.24  ? 458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.075 158.252 147.086 1.00 33.96  ? 458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 127.446 157.582 149.804 1.00 29.12  ? 459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 128.290 157.437 150.990 1.00 26.23  ? 459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 127.732 156.391 151.948 1.00 28.94  ? 459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 127.866 156.512 153.168 1.00 34.26  ? 459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 128.478 158.777 151.708 1.00 26.55  ? 459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 128.980 159.892 150.810 1.00 29.74  ? 459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 128.402 161.233 151.226 1.00 33.93  ? 459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 128.829 162.334 150.272 1.00 34.70  ? 459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.242 163.649 150.642 1.00 36.91  ? 459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.100 155.358 151.400 1.00 28.36  ? 460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 126.482 154.323 152.213 1.00 20.90  ? 460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 127.537 153.403 152.807 1.00 19.17  ? 460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 128.479 152.988 152.125 1.00 27.16  ? 460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 125.495 153.509 151.380 1.00 21.87  ? 460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.170 152.816 150.347 1.00 25.42  ? 460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 127.371 153.082 154.088 1.00 17.93  ? 461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 128.274 152.193 154.801 1.00 19.70  ? 461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 127.457 151.074 155.428 1.00 23.81  ? 461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 126.236 151.162 155.563 1.00 33.46  ? 461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.090 152.933 155.881 1.00 18.02  ? 461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 128.161 153.457 156.975 1.00 13.22  ? 461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 129.891 154.066 155.260 1.00 23.32  ? 461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 128.882 154.037 158.158 1.00 17.63  ? 461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.148 150.003 155.799 1.00 17.59  ? 462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 127.494 148.911 156.488 1.00 11.11  ? 462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 128.123 148.604 157.829 1.00 15.33  ? 462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 129.254 148.116 157.892 1.00 37.63  ? 462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 127.401 148.879 158.909 1.00 14.66  ? 463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 127.873 148.600 160.261 1.00 18.14  ? 463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 127.059 147.433 160.809 1.00 27.14  ? 463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 125.940 147.617 161.295 1.00 35.99  ? 463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 127.759 149.833 161.150 1.00 23.35  ? 463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 128.297 149.640 162.568 1.00 20.93  ? 463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 129.694 149.056 162.512 1.00 15.50  ? 463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 128.293 150.952 163.330 1.00 23.79  ? 463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 127.627 146.233 160.727 1.00 26.76  ? 464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 126.974 145.037 161.209 1.00 18.51  ? 464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 127.265 144.767 162.671 1.00 13.10  ? 464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 127.861 145.574 163.386 1.00 20.16  ? 464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 126.826 143.594 163.116 1.00 17.22  ? 465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 127.059 143.152 164.480 1.00 13.84  ? 465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 127.222 141.642 164.477 1.00 20.12  ? 465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 126.744 140.947 163.579 1.00 37.09  ? 465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 125.920 143.572 165.414 1.00 19.79  ? 465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.908 141.142 165.498 1.00 24.22  ? 466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.179 139.718 165.614 1.00 30.55  ? 466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.331 139.365 167.084 1.00 27.50  ? 466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 128.339 140.237 167.957 1.00 36.39  ? 466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.420 139.327 164.809 1.00 33.13  ? 466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 130.677 140.053 165.234 1.00 31.44  ? 466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.080 139.685 164.170 1.00 47.91  ? 466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 133.400 140.415 165.122 1.00 27.13  ? 466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.449 138.063 167.348 1.00 21.80  ? 467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.527 137.524 168.707 1.00 26.61  ? 467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 127.269 137.831 169.513 1.00 29.92  ? 467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 127.329 137.999 170.732 1.00 37.24  ? 467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 129.766 138.033 169.448 1.00 27.98  ? 467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.440 136.952 170.265 1.00 34.20  ? 467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 129.985 135.810 170.300 1.00 39.70  ? 467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.538 137.304 170.919 1.00 36.60  ? 467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 126.121 137.920 168.839 1.00 23.50  ? 468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 124.861 138.050 169.559 1.00 22.33  ? 468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 124.569 136.797 170.373 1.00 30.65  ? 468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.331 136.867 171.585 1.00 37.52  ? 468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 123.721 138.328 168.581 1.00 26.24  ? 468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.322 138.322 169.196 1.00 19.82  ? 468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 122.143 139.499 170.138 1.00 27.19  ? 468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 121.261 138.330 168.115 1.00 21.50  ? 468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 124.608 135.631 169.723 1.00 31.28  ? 469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 124.341 134.384 170.429 1.00 21.41  ? 469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 125.422 134.096 171.460 1.00 31.79  ? 469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 125.129 133.585 172.545 1.00 44.37  ? 469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 124.218 133.227 169.439 1.00 27.68  ? 469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 123.684 131.967 170.049 1.00 29.86  ? 469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 123.657 130.768 169.371 1.00 32.51  ? 469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 123.156 131.722 171.270 1.00 31.01  ? 469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 123.137 129.836 170.151 1.00 29.64  ? 469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 122.825 130.389 171.309 1.00 30.58  ? 469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 126.677 134.413 171.140 1.00 31.57  ? 470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 127.742 134.230 172.114 1.00 25.75  ? 470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 127.551 135.087 173.348 1.00 27.59  ? 470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 127.725 134.617 174.476 1.00 40.97  ? 470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 127.182 136.356 173.155 1.00 24.95  ? 471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 126.928 137.231 174.295 1.00 28.73  ? 471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 125.743 136.737 175.113 1.00 37.08  ? 471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 125.784 136.748 176.349 1.00 42.74  ? 471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 126.680 138.663 173.822 1.00 26.87  ? 471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 126.303 139.607 174.940 1.00 30.29  ? 471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 127.266 140.096 175.811 1.00 35.31  ? 471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 124.986 139.992 175.139 1.00 27.46  ? 471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 126.929 140.953 176.839 1.00 34.23  ? 471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 124.641 140.845 176.167 1.00 27.93  ? 471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 125.616 141.324 177.012 1.00 37.15  ? 471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.275 142.177 178.035 1.00 41.17  ? 471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 124.671 136.310 174.441 1.00 32.78  ? 472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 123.486 135.848 175.156 1.00 28.79  ? 472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 123.777 134.581 175.952 1.00 32.32  ? 472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 123.365 134.457 177.111 1.00 39.79  ? 472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 122.339 135.616 174.172 1.00 34.55  ? 472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 121.818 136.853 173.440 1.00 32.53  ? 472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 120.962 136.440 172.260 1.00 28.24  ? 472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 121.044 137.755 174.385 1.00 29.02  ? 472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 124.485 133.627 175.345 1.00 28.81  ? 473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 124.784 132.377 176.032 1.00 30.72  ? 473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 125.775 132.590 177.167 1.00 41.27  ? 473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 125.658 131.961 178.225 1.00 47.22  ? 473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 125.316 131.349 175.034 1.00 29.63  ? 473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 126.759 133.470 176.971 1.00 36.12  ? 474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 127.700 133.777 178.038 1.00 34.47  ? 474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 127.079 134.620 179.142 1.00 37.19  ? 474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 127.707 134.799 180.190 1.00 40.93  ? 474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 128.928 134.484 177.462 1.00 33.07  ? 474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 129.919 133.535 176.811 1.00 34.42  ? 474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 131.068 134.255 176.141 1.00 41.51  ? 474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 131.855 134.937 176.796 1.00 40.97  ? 474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 131.175 134.102 174.827 1.00 43.79  ? 474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 125.870 135.138 178.931 1.00 40.59  ? 475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 125.119 135.847 179.956 1.00 41.58  ? 475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 123.925 135.044 180.454 1.00 39.74  ? 475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 123.071 135.591 181.160 1.00 40.54  ? 475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 124.660 137.206 179.429 1.00 35.62  ? 475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 125.773 138.228 179.419 1.00 37.13  ? 475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 125.922 139.012 180.356 1.00 44.22  ? 475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 126.576 138.214 178.364 1.00 35.80  ? 475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 123.845 133.765 180.103 1.00 30.70  ? 476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 122.731 132.930 180.514 1.00 35.59  ? 476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 121.403 133.312 179.899 1.00 39.80  ? 476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 120.373 133.271 180.583 1.00 40.38  ? 476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 121.399 133.684 178.621 1.00 34.24  ? 477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 120.185 134.064 177.909 1.00 32.54  ? 477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 120.032 133.143 176.708 1.00 38.23  ? 477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 120.937 133.054 175.869 1.00 37.91  ? 477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 120.216 135.536 177.469 1.00 31.43  ? 477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 120.495 136.446 178.665 1.00 38.15  ? 477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 118.904 135.919 176.816 1.00 33.89  ? 477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 120.947 137.834 178.282 1.00 40.62  ? 477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 118.894 132.459 176.628 1.00 41.20  ? 478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 118.610 131.618 175.474 1.00 36.79  ? 478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 118.273 132.481 174.266 1.00 39.30  ? 478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 117.513 133.445 174.368 1.00 39.59  ? 478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 117.458 130.663 175.781 1.00 30.76  ? 478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 118.843 132.121 173.112 1.00 35.61  ? 479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 118.667 132.925 171.906 1.00 31.95  ? 479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 117.200 133.044 171.513 1.00 38.11  ? 479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 116.784 134.076 170.973 1.00 36.33  ? 479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 119.486 132.324 170.762 1.00 28.15  ? 479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 119.457 133.105 169.467 1.00 29.75  ? 479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 118.472 132.878 168.515 1.00 34.10  ? 479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 120.427 134.058 169.191 1.00 26.99  ? 479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 118.448 133.587 167.331 1.00 32.73  ? 479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 120.410 134.770 168.009 1.00 31.98  ? 479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 119.418 134.530 167.082 1.00 34.63  ? 479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 119.398 135.239 165.903 1.00 34.74  ? 479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 116.401 132.009 171.772 1.00 43.77  ? 480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 114.977 132.046 171.462 1.00 38.30  ? 480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 114.142 132.681 172.565 1.00 41.95  ? 480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 112.943 132.897 172.359 1.00 48.08  ? 480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 114.457 130.634 171.194 1.00 40.73  ? 480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 115.206 129.879 170.116 1.00 41.77  ? 480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 114.852 128.406 170.099 1.00 49.24  ? 480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 115.299 127.675 171.006 1.00 49.86  ? 480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 114.117 127.982 169.184 1.00 47.01  ? 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 114.734 132.978 173.717 1.00 38.16  ? 481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 113.970 133.516 174.828 1.00 38.61  ? 481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 113.528 134.949 174.534 1.00 43.68  ? 481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 114.181 135.666 173.772 1.00 45.22  ? 481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 114.797 133.479 176.109 1.00 39.61  ? 481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 115.462 134.711 176.322 1.00 44.29  ? 481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 112.407 135.385 175.118 1.00 48.05  ? 482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.001 136.790 174.953 1.00 43.31  ? 482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.010 137.777 175.510 1.00 41.02  ? 482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 113.074 138.917 175.038 1.00 41.39  ? 482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 110.665 136.858 175.706 1.00 44.13  ? 482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 110.176 135.448 175.743 1.00 43.23  ? 482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 111.407 134.606 175.865 1.00 42.26  ? 482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 113.796 137.373 176.512 1.00 46.19  ? 483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 114.843 138.249 177.029 1.00 42.74  ? 483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 115.901 138.523 175.968 1.00 41.41  ? 483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 116.421 139.640 175.872 1.00 46.25  ? 483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 115.478 137.629 178.274 1.00 44.27  ? 483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 114.538 137.526 179.462 1.00 46.86  ? 483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 113.880 136.166 179.568 1.00 49.60  ? 483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 113.939 135.398 178.586 1.00 48.15  ? 483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 113.301 135.864 180.633 1.00 50.00  ? 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 116.238 137.510 175.167 1.00 35.84  ? 484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 117.192 137.713 174.084 1.00 38.97  ? 484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 116.662 138.704 173.058 1.00 35.40  ? 484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 117.406 139.565 172.573 1.00 37.11  ? 484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 117.518 136.380 173.418 1.00 38.65  ? 484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 115.379 138.597 172.710 1.00 34.51  ? 485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 114.793 139.549 171.774 1.00 33.05  ? 485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 114.740 140.948 172.371 1.00 35.14  ? 485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 114.945 141.937 171.661 1.00 40.47  ? 485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 113.400 139.087 171.353 1.00 37.42  ? 485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.411 138.006 170.290 1.00 35.06  ? 485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 112.042 137.835 169.663 1.00 36.07  ? 485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 111.039 137.418 170.635 1.00 42.50  ? 485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 110.897 136.177 171.079 1.00 43.63  ? 485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 111.679 135.197 170.657 1.00 40.53  ? 485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 109.943 135.912 171.966 1.00 39.14  ? 485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 114.469 141.054 173.673 1.00 41.14  ? 486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 114.494 142.358 174.328 1.00 36.88  ? 486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 115.887 142.972 174.276 1.00 38.26  ? 486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 116.040 144.169 173.993 1.00 44.90  ? 486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 114.023 142.225 175.775 1.00 41.48  ? 486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 113.641 143.556 176.387 1.00 47.76  ? 486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 113.691 144.578 175.671 1.00 49.43  ? 486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.294 143.580 177.585 1.00 48.66  ? 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 116.917 142.167 174.547 1.00 33.52  ? 487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 118.279 142.679 174.471 1.00 25.76  ? 487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 118.632 143.094 173.053 1.00 31.09  ? 487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 119.289 144.118 172.850 1.00 40.86  ? 487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 119.291 141.649 174.963 1.00 33.57  ? 487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 120.693 141.948 174.515 1.00 36.41  ? 487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 121.415 142.969 175.106 1.00 29.63  ? 487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 121.273 141.238 173.477 1.00 37.11  ? 487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 122.693 143.264 174.687 1.00 30.41  ? 487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 122.554 141.531 173.053 1.00 35.06  ? 487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 123.262 142.546 173.659 1.00 32.72  ? 487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 118.241 142.293 172.061 1.00 37.24  ? 488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 118.518 142.664 170.678 1.00 30.69  ? 488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 117.825 143.969 170.320 1.00 30.41  ? 488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 118.433 144.859 169.715 1.00 36.47  ? 488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 118.082 141.544 169.735 1.00 25.41  ? 488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 116.560 144.113 170.719 1.00 31.59  ? 489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 115.828 145.350 170.483 1.00 31.11  ? 489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 116.567 146.543 171.070 1.00 32.45  ? 489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 116.845 147.522 170.368 1.00 34.36  ? 489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 114.426 145.238 171.082 1.00 34.71  ? 489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 113.439 146.188 170.444 1.00 38.51  ? 489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 113.421 146.359 169.226 1.00 45.63  ? 489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 112.600 146.805 171.265 1.00 36.71  ? 489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 116.928 146.463 172.352 1.00 37.13  ? 490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 117.573 147.598 173.007 1.00 35.99  ? 490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 118.946 147.881 172.404 1.00 32.90  ? 490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 119.262 149.031 172.076 1.00 40.56  ? 490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 117.690 147.345 174.508 1.00 40.08  ? 490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 116.394 147.062 175.048 1.00 43.02  ? 490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 118.267 148.569 175.203 1.00 38.19  ? 490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 119.772 146.844 172.251 1.00 25.34  ? 491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 121.133 147.028 171.763 1.00 27.53  ? 491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 121.139 147.613 170.359 1.00 32.76  ? 491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 121.886 148.553 170.072 1.00 38.10  ? 491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 121.882 145.694 171.794 1.00 31.06  ? 491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 123.268 145.759 171.213 1.00 29.54  ? 491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 124.350 146.089 172.008 1.00 30.73  ? 491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 123.491 145.476 169.875 1.00 28.91  ? 491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 125.625 146.148 171.481 1.00 28.62  ? 491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 124.762 145.536 169.343 1.00 28.49  ? 491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 125.830 145.871 170.147 1.00 31.93  ? 491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 120.306 147.078 169.467 1.00 29.65  ? 492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 120.293 147.584 168.106 1.00 19.43  ? 492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 119.578 148.921 167.986 1.00 19.26  ? 492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 119.906 149.693 167.082 1.00 31.00  ? 492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 119.681 146.543 167.171 1.00 23.46  ? 492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 120.597 145.386 166.895 1.00 23.84  ? 492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 121.647 145.519 166.005 1.00 22.51  ? 492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 120.433 144.178 167.550 1.00 27.73  ? 492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 122.499 144.466 165.755 1.00 21.15  ? 492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 121.285 143.121 167.306 1.00 21.93  ? 492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 122.318 143.264 166.406 1.00 25.59  ? 492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 118.654 149.243 168.896 1.00 24.95  ? 493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 118.129 150.602 168.930 1.00 24.17  ? 493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 119.220 151.592 169.312 1.00 26.14  ? 493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 119.327 152.664 168.710 1.00 35.40  ? 493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 116.944 150.687 169.895 1.00 27.19  ? 493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 116.353 152.086 170.087 1.00 28.05  ? 493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 117.228 153.164 171.241 1.00 44.93  ? 493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 117.183 152.169 172.726 1.00 37.63  ? 493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 120.045 151.248 170.307 1.00 33.98  ? 494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 121.167 152.118 170.657 1.00 30.86  ? 494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 122.165 152.219 169.511 1.00 32.49  ? 494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 122.705 153.299 169.240 1.00 40.87  ? 494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 121.865 151.619 171.923 1.00 29.90  ? 494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 120.941 151.306 173.084 1.00 32.80  ? 494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 121.775 151.288 174.682 1.00 54.75  ? 494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 123.209 152.305 174.339 1.00 41.27  ? 494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 122.431 151.101 168.836 1.00 21.31  ? 495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 123.360 151.108 167.707 1.00 18.88  ? 495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 122.843 152.018 166.601 1.00 26.64  ? 495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 123.592 152.819 166.035 1.00 37.74  ? 495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 123.597 149.674 167.198 1.00 19.96  ? 495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 124.262 149.696 165.833 1.00 18.86  ? 495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 124.446 148.900 168.184 1.00 21.58  ? 495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 121.551 151.912 166.281 1.00 26.20  ? 496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 120.958 152.785 165.274 1.00 20.66  ? 496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 120.999 154.241 165.712 1.00 29.59  ? 496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 121.306 155.130 164.910 1.00 35.54  ? 496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 119.523 152.348 164.986 1.00 18.91  ? 496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 118.952 153.004 163.747 1.00 23.85  ? 496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 119.666 153.258 162.780 1.00 29.88  ? 496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 117.655 153.284 163.771 1.00 29.71  ? 496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 120.697 154.504 166.986 1.00 31.50  ? 497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 120.732 155.867 167.505 1.00 23.00  ? 497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 122.110 156.481 167.328 1.00 26.79  ? 497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 122.248 157.592 166.805 1.00 31.95  ? 497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 120.333 155.866 168.982 1.00 25.67  ? 497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 120.363 157.225 169.624 1.00 25.68  ? 497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 119.260 158.055 169.568 1.00 31.37  ? 497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 121.493 157.666 170.292 1.00 30.06  ? 497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 119.285 159.302 170.159 1.00 33.28  ? 497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 121.522 158.911 170.883 1.00 30.22  ? 497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 120.416 159.729 170.816 1.00 30.76  ? 497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 123.150 155.760 167.742 1.00 33.13  ? 498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 124.495 156.316 167.685 1.00 27.66  ? 498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 125.042 156.349 166.265 1.00 31.38  ? 498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 125.821 157.247 165.935 1.00 41.88  ? 498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 125.421 155.537 168.616 1.00 27.06  ? 498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 125.077 155.747 170.071 1.00 30.63  ? 498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 124.969 157.026 170.597 1.00 29.21  ? 498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 124.847 154.670 170.917 1.00 32.50  ? 498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 124.647 157.229 171.922 1.00 31.62  ? 498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 124.527 154.864 172.245 1.00 32.14  ? 498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 124.429 156.145 172.742 1.00 35.94  ? 498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 124.110 156.342 174.066 1.00 36.34  ? 498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 124.634 155.414 165.405 1.00 23.79  ? 499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.018 155.491 164.000 1.00 20.61  ? 499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 124.402 156.711 163.331 1.00 22.71  ? 499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.082 157.427 162.586 1.00 27.72  ? 499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 124.606 154.211 163.276 1.00 20.70  ? 499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 125.379 154.016 162.106 1.00 29.69  ? 499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 123.121 156.974 163.595 1.00 25.51  ? 500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 122.471 158.163 163.052 1.00 25.44  ? 500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.119 159.423 163.609 1.00 25.28  ? 500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 123.334 160.402 162.885 1.00 31.94  ? 500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 120.961 158.125 163.346 1.00 26.82  ? 500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 120.286 157.008 162.556 1.00 23.16  ? 500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 120.315 159.449 163.004 1.00 23.85  ? 500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 118.871 156.731 162.999 1.00 28.91  ? 500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 123.434 159.420 164.906 1.00 30.52  ? 501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.069 160.580 165.518 1.00 30.21  ? 501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 125.436 160.850 164.907 1.00 33.68  ? 501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 125.774 162.000 164.611 1.00 39.37  ? 501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 124.186 160.374 167.028 1.00 33.38  ? 501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 124.133 161.655 167.836 1.00 34.34  ? 501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 124.266 161.406 169.324 1.00 38.62  ? 501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 125.155 160.678 169.764 1.00 42.78  ? 501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 123.381 162.009 170.106 1.00 37.91  ? 501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 126.233 159.801 164.698 1.00 32.83  ? 502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 127.546 159.981 164.093 1.00 27.62  ? 502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 127.430 160.425 162.642 1.00 28.18  ? 502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 128.221 161.251 162.180 1.00 38.40  ? 502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 128.358 158.692 164.196 1.00 31.02  ? 502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 129.820 158.870 163.834 1.00 35.30  ? 502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 130.451 159.988 164.646 1.00 33.43  ? 502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 131.706 160.443 164.063 1.00 31.50  ? 502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 132.108 161.705 164.040 1.00 33.72  ? 502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 131.383 162.672 164.577 1.00 37.66  ? 502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 133.269 162.007 163.465 1.00 30.76  ? 502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 126.455 159.887 161.904 1.00 27.56  ? 503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 126.251 160.324 160.527 1.00 23.09  ? 503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 125.871 161.798 160.469 1.00 29.10  ? 503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 126.381 162.547 159.628 1.00 38.45  ? 503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 125.178 159.464 159.862 1.00 24.27  ? 503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 125.081 159.747 158.478 1.00 33.88  ? 503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 124.985 162.235 161.366 1.00 28.10  ? 504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 124.606 163.642 161.411 1.00 28.42  ? 504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 125.783 164.520 161.821 1.00 37.14  ? 504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 125.950 165.626 161.300 1.00 40.39  ? 504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 123.428 163.838 162.361 1.00 26.70  ? 504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 126.607 164.044 162.757 1.00 38.86  ? 505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 127.788 164.802 163.161 1.00 34.82  ? 505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 128.784 164.926 162.015 1.00 37.69  ? 505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 129.398 165.983 161.834 1.00 43.53  ? 505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 128.443 164.144 164.373 1.00 36.38  ? 505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 127.685 164.343 165.671 1.00 38.15  ? 505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 128.119 163.371 166.749 1.00 42.89  ? 505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.054 162.583 166.497 1.00 37.69  ? 505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 127.525 163.394 167.846 1.00 45.39  ? 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 128.963 163.859 161.236 1.00 34.22  ? 506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 129.847 163.921 160.076 1.00 26.92  ? 506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 129.286 164.877 159.032 1.00 32.99  ? 506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.029 165.642 158.408 1.00 42.31  ? 506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.073 162.514 159.495 1.00 29.71  ? 506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 130.817 161.633 160.498 1.00 32.03  ? 506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 130.853 162.590 158.197 1.00 31.70  ? 506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 130.708 160.155 160.203 1.00 25.48  ? 506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 127.967 164.852 158.825 1.00 33.16  ? 507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 127.350 165.777 157.879 1.00 33.62  ? 507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 127.513 167.221 158.335 1.00 35.91  ? 507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 127.689 168.125 157.510 1.00 42.20  ? 507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 125.874 165.433 157.696 1.00 32.24  ? 507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 127.444 167.459 159.645 1.00 38.03  ? 508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 127.655 168.803 160.173 1.00 38.30  ? 508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.107 169.236 160.010 1.00 43.97  ? 508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 129.386 170.370 159.603 1.00 48.25  ? 508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 127.240 168.852 161.643 1.00 43.73  ? 508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 127.490 170.188 162.318 1.00 43.95  ? 508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 127.214 170.105 163.810 1.00 45.99  ? 508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 127.314 171.470 164.470 1.00 46.12  ? 508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 126.440 171.570 165.671 1.00 47.37  ? 508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.047 168.344 160.331 1.00 42.26  ? 509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 131.463 168.688 160.260 1.00 42.37  ? 509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 131.904 168.940 158.824 1.00 43.31  ? 509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 132.654 169.885 158.555 1.00 47.01  ? 509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 132.301 167.577 160.891 1.00 42.38  ? 509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 132.517 167.736 162.387 1.00 48.73  ? 509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 132.345 166.431 163.142 1.00 50.30  ? 509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 131.651 166.430 164.181 1.00 44.16  ? 509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.903 165.407 162.696 1.00 49.36  ? 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 131.451 168.107 157.889 1.00 37.23  ? 510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 131.805 168.261 156.486 1.00 35.83  ? 510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 130.858 169.179 155.729 1.00 40.67  ? 510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.144 169.527 154.579 1.00 46.94  ? 510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 131.842 166.890 155.801 1.00 34.07  ? 510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 132.683 165.863 156.537 1.00 38.47  ? 510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.081 164.714 155.631 1.00 40.04  ? 510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.008 163.750 156.353 1.00 37.30  ? 510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.018 163.156 155.437 1.00 40.29  ? 510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 129.744 169.579 156.340 1.00 36.34  ? 511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 128.810 170.473 155.688 1.00 41.82  ? 511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.045 169.874 154.534 1.00 43.33  ? 511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 127.345 170.607 153.830 1.00 47.55  ? 511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.151 168.566 154.312 1.00 40.30  ? 512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 127.508 167.913 153.184 1.00 38.54  ? 512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 126.805 166.645 153.641 1.00 38.20  ? 512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 127.304 165.922 154.508 1.00 35.81  ? 512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 128.521 167.574 152.084 1.00 38.96  ? 512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 129.749 166.828 152.577 1.00 40.27  ? 512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 130.501 166.146 151.454 1.00 45.02  ? 512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 129.850 165.699 150.487 1.00 44.53  ? 512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 131.744 166.056 151.535 1.00 42.09  ? 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 125.642 166.388 153.054 1.00 40.35  ? 513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 124.888 165.161 153.254 1.00 32.74  ? 513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 124.978 164.306 151.998 1.00 33.88  ? 513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 125.510 164.728 150.968 1.00 37.69  ? 513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 123.425 165.472 153.588 1.00 32.10  ? 513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 122.755 165.937 152.411 1.00 39.48  ? 513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 123.346 166.545 154.659 1.00 33.89  ? 513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 124.455 163.086 152.085 1.00 33.19  ? 514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 124.438 162.228 150.911 1.00 30.74  ? 514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 123.459 162.772 149.879 1.00 34.45  ? 514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 122.512 163.491 150.207 1.00 40.85  ? 514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.089 160.784 151.288 1.00 29.66  ? 514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 122.678 160.588 151.773 1.00 31.02  ? 514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 121.665 160.254 150.889 1.00 27.89  ? 514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.375 160.696 153.118 1.00 32.01  ? 514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 120.373 160.059 151.337 1.00 27.88  ? 514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.085 160.502 153.570 1.00 29.59  ? 514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.084 160.183 152.678 1.00 32.58  ? 514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 123.713 162.441 148.614 1.00 37.30  ? 515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 122.911 162.984 147.527 1.00 35.45  ? 515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 121.451 162.573 147.672 1.00 42.00  ? 515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.141 161.431 148.024 1.00 49.58  ? 515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 123.459 162.517 146.179 1.00 38.29  ? 515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 124.553 163.423 145.652 1.00 44.55  ? 515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 125.188 164.126 146.466 1.00 43.38  ? 515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 124.778 163.434 144.423 1.00 44.81  ? 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 120.557 163.523 147.397 1.00 39.27  ? 516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.112 163.327 147.533 1.00 40.10  ? 516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 118.730 162.948 148.962 1.00 38.75  ? 516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 117.856 162.111 149.189 1.00 44.72  ? 516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 118.597 162.283 146.540 1.00 35.99  ? 516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 118.876 162.614 145.087 1.00 39.97  ? 516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 118.347 161.555 144.143 1.00 40.65  ? 516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 117.150 161.495 143.867 1.00 40.49  ? 516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 119.240 160.710 143.641 1.00 39.46  ? 516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 119.395 163.569 149.939 1.00 34.17  ? 517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.016 163.351 151.330 1.00 34.50  ? 517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 117.692 164.026 151.663 1.00 39.38  ? 517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 116.928 163.514 152.488 1.00 47.55  ? 517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.112 163.858 152.269 1.00 32.69  ? 517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 119.602 164.254 153.637 1.00 37.29  ? 517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 119.334 163.293 154.601 1.00 32.92  ? 517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 119.378 165.586 153.959 1.00 36.22  ? 517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 118.864 163.647 155.848 1.00 35.09  ? 517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 118.906 165.948 155.202 1.00 33.90  ? 517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 118.649 164.976 156.142 1.00 38.74  ? 517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 118.181 165.335 157.385 1.00 45.89  ? 517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 117.406 165.167 151.031 1.00 41.90  ? 518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 116.238 165.958 151.404 1.00 43.91  ? 518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 114.939 165.201 151.159 1.00 48.24  ? 518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 113.949 165.429 151.861 1.00 53.28  ? 518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 116.228 167.284 150.640 1.00 42.03  ? 518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 117.357 168.250 150.998 1.00 48.07  ? 518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 118.727 167.759 150.565 1.00 52.96  ? 518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 118.849 167.261 149.426 1.00 51.42  ? 518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 119.681 167.872 151.363 1.00 48.54  ? 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 114.920 164.310 150.174 1.00 34.50  ? 519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 113.748 163.504 149.918 1.00 33.87  ? 519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 113.628 162.253 150.754 1.00 36.90  ? 519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 112.617 161.552 150.659 1.00 37.21  ? 519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 114.630 161.950 151.572 1.00 36.19  ? 520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 114.615 160.748 152.388 1.00 33.00  ? 520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 113.783 160.961 153.649 1.00 32.23  ? 520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 113.479 162.088 154.044 1.00 33.33  ? 520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.038 160.335 152.762 1.00 25.77  ? 520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 116.642 161.301 153.602 1.00 28.49  ? 520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 113.413 159.845 154.281 1.00 30.35  ? 521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 112.637 159.910 155.513 1.00 27.94  ? 521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 113.430 160.508 156.667 1.00 32.20  ? 521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 112.826 160.968 157.642 1.00 33.98  ? 521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.135 158.518 155.895 1.00 28.29  ? 521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.235 157.718 156.346 1.00 32.08  ? 521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 111.479 157.842 154.703 1.00 26.93  ? 521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 114.763 160.503 156.585 1.00 34.12  ? 522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 115.565 161.178 157.601 1.00 30.32  ? 522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 115.292 162.676 157.609 1.00 34.66  ? 522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.169 163.288 158.677 1.00 31.12  ? 522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.052 160.918 157.364 1.00 28.81  ? 522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 117.458 159.465 157.423 1.00 29.11  ? 522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 117.409 158.757 158.616 1.00 26.91  ? 522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 117.913 158.807 156.290 1.00 33.50  ? 522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 117.790 157.433 158.674 1.00 31.07  ? 522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.296 157.483 156.340 1.00 32.53  ? 522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.232 156.800 157.533 1.00 31.43  ? 522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 118.612 155.480 157.585 1.00 35.03  ? 522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.200 163.285 156.424 1.00 40.23  ? 523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 114.949 164.719 156.345 1.00 37.27  ? 523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 113.515 165.054 156.732 1.00 42.03  ? 523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 113.267 166.057 157.411 1.00 44.30  ? 523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.260 165.228 154.939 1.00 33.56  ? 523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 112.556 164.230 156.307 1.00 38.20  ? 524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.155 164.480 156.621 1.00 38.62  ? 524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 110.780 164.051 158.032 1.00 40.50  ? 524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 109.712 164.439 158.517 1.00 45.58  ? 524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.250 163.764 155.615 1.00 39.26  ? 524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.162 162.374 155.953 1.00 40.88  ? 524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 110.804 163.904 154.206 1.00 38.39  ? 524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 111.626 163.267 158.698 1.00 34.71  ? 525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 111.346 162.802 160.038 1.00 35.59  ? 525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 110.511 161.544 160.125 1.00 38.55  ? 525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 110.214 161.096 161.239 1.00 40.35  ? 525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.121 160.961 158.988 1.00 40.84  ? 526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 109.323 159.740 159.014 1.00 40.12  ? 526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.110 158.567 159.588 1.00 40.77  ? 526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 109.517 157.636 160.143 1.00 46.58  ? 526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 108.828 159.416 157.604 1.00 37.88  ? 526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 107.998 158.146 157.496 1.00 39.04  ? 526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 107.737 157.740 156.059 1.00 45.73  ? 526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 107.917 158.587 155.158 1.00 44.81  ? 526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 107.354 156.574 155.830 1.00 42.38  ? 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 111.439 158.601 159.475 1.00 35.19  ? 527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.259 157.515 160.001 1.00 32.25  ? 527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.170 157.435 161.520 1.00 36.84  ? 527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.187 156.340 162.092 1.00 39.87  ? 527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 113.711 157.698 159.558 1.00 28.50  ? 527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 114.606 156.518 159.861 1.00 34.91  ? 527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.288 156.428 161.067 1.00 32.32  ? 527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 114.772 155.497 158.936 1.00 34.71  ? 527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.106 155.352 161.344 1.00 31.99  ? 527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 115.590 154.417 159.206 1.00 34.34  ? 527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 116.254 154.351 160.410 1.00 32.90  ? 527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.070 153.277 160.681 1.00 34.85  ? 527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.073 158.581 162.187 1.00 41.63  ? 528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.115 158.646 163.641 1.00 40.95  ? 528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 110.741 158.546 164.291 1.00 47.36  ? 528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 110.647 158.679 165.514 1.00 54.11  ? 528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 112.792 159.945 164.088 1.00 38.99  ? 528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.148 160.162 163.482 1.00 43.41  ? 528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 115.275 159.609 164.063 1.00 40.84  ? 528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 114.296 160.921 162.336 1.00 39.90  ? 528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 116.523 159.807 163.510 1.00 39.30  ? 528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 115.541 161.122 161.778 1.00 39.17  ? 528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 116.656 160.564 162.366 1.00 41.20  ? 528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 109.681 158.320 163.511 1.00 45.48  ? 529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 108.335 158.281 164.080 1.00 43.67  ? 529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 108.208 157.173 165.119 1.00 48.45  ? 529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 107.763 157.411 166.250 1.00 52.93  ? 529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 107.305 158.095 162.967 1.00 42.34  ? 529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.106 159.348 162.140 1.00 50.30  ? 529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 107.620 160.414 162.539 1.00 52.04  ? 529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 106.435 159.268 161.090 1.00 50.76  ? 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 108.610 155.953 164.759 1.00 45.30  ? 530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 108.531 154.838 165.693 1.00 44.78  ? 530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 109.509 154.982 166.849 1.00 48.57  ? 530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 109.319 154.341 167.887 1.00 49.96  ? 530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 108.779 153.519 164.960 1.00 45.85  ? 530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 110.209 153.022 165.046 1.00 45.41  ? 530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 110.418 151.804 164.170 1.00 45.41  ? 530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 111.788 151.200 164.397 1.00 46.66  ? 530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 112.422 150.821 163.108 1.00 52.05  ? 530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 110.545 155.804 166.696 1.00 45.95  ? 531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 111.501 156.030 167.771 1.00 40.19  ? 531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 111.056 157.123 168.727 1.00 40.07  ? 531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 111.325 157.031 169.931 1.00 45.08  ? 531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 112.871 156.380 167.190 1.00 39.31  ? 531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 113.586 155.201 166.575 1.00 41.19  ? 531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 113.934 154.100 167.344 1.00 40.79  ? 531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 113.916 155.190 165.228 1.00 42.18  ? 531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 114.589 153.020 166.789 1.00 43.43  ? 531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 114.570 154.114 164.663 1.00 41.17  ? 531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 114.904 153.033 165.449 1.00 41.59  ? 531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 115.557 151.959 164.891 1.00 40.59  ? 531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 110.384 158.161 168.221 1.00 44.85  ? 532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 109.807 159.180 169.094 1.00 44.76  ? 532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 108.450 158.773 169.640 1.00 48.02  ? 532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 107.902 159.477 170.498 1.00 51.09  ? 532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 109.676 160.530 168.365 1.00 46.24  ? 532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.003 160.928 167.743 1.00 44.76  ? 532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 108.585 160.458 167.308 1.00 45.58  ? 532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 107.888 157.661 169.167 1.00 49.92  ? 533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 106.620 157.165 169.682 1.00 53.52  ? 533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 106.771 155.968 170.609 1.00 53.83  ? 533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.048 155.879 171.607 1.00 51.33  ? 533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 105.690 156.784 168.525 1.00 50.75  ? 533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.045 155.526 167.980 1.00 48.84  ? 533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 107.686 155.049 170.310 1.00 55.74  ? 534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 107.859 153.823 171.079 1.00 51.81  ? 534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 109.170 153.886 171.849 1.00 49.97  ? 534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 110.199 154.288 171.298 1.00 52.20  ? 534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 107.843 152.593 170.163 1.00 51.59  ? 534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 106.573 152.501 169.506 1.00 50.16  ? 534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.086 151.320 170.961 1.00 51.06  ? 534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 109.128 153.489 173.118 1.00 51.80  ? 535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 110.324 153.397 173.945 1.00 52.89  ? 535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 110.903 151.993 173.835 1.00 54.04  ? 535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 110.190 151.003 174.029 1.00 52.44  ? 535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.002 153.730 175.402 1.00 51.69  ? 535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 111.239 153.768 176.277 1.00 56.76  ? 535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.123 154.612 176.022 1.00 53.64  ? 535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 111.324 152.957 177.221 1.00 59.83  ? 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 112.196 151.911 173.524 1.00 45.35  ? 536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 112.859 150.637 173.278 1.00 42.63  ? 536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 113.770 150.223 174.428 1.00 44.42  ? 536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 114.685 149.416 174.232 1.00 47.78  ? 536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 113.644 150.697 171.968 1.00 41.30  ? 536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 112.776 150.830 170.750 1.00 39.12  ? 536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 112.295 149.709 170.099 1.00 37.38  ? 536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 112.439 152.079 170.257 1.00 43.60  ? 536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 111.493 149.829 168.980 1.00 38.84  ? 536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 111.640 152.205 169.140 1.00 46.34  ? 536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 111.167 151.079 168.500 1.00 45.64  ? 536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 113.543 150.763 175.623 1.00 47.65  ? 537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 114.285 150.322 176.791 1.00 49.93  ? 537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 113.906 148.882 177.134 1.00 51.53  ? 537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 112.802 148.432 176.818 1.00 49.58  ? 537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 114.000 151.237 177.979 1.00 47.00  ? 537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 114.390 152.571 177.700 1.00 50.12  ? 537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 114.812 148.132 177.763 1.00 52.45  ? 538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 114.514 146.727 178.071 1.00 51.93  ? 538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 113.301 146.592 178.979 1.00 53.05  ? 538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 113.108 147.372 179.913 1.00 53.15  ? 538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 115.791 146.236 178.763 1.00 51.99  ? 538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 116.853 147.190 178.332 1.00 51.67  ? 538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 116.169 148.510 178.191 1.00 48.27  ? 538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 112.480 145.582 178.692 1.00 56.30  ? 539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 111.310 145.288 179.509 1.00 55.21  ? 539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 111.599 144.283 180.612 1.00 56.91  ? 539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 110.759 144.099 181.500 1.00 57.62  ? 539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 110.171 144.763 178.631 1.00 55.19  ? 539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 109.883 145.625 177.412 1.00 54.29  ? 539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 108.544 146.331 177.536 1.00 55.36  ? 539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 108.365 147.369 176.440 1.00 58.60  ? 539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 109.323 148.500 176.585 1.00 57.28  ? 539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 112.758 143.634 180.578 1.00 56.47  ? 540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 113.154 142.652 181.579 1.00 57.19  ? 540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 114.285 143.224 182.419 1.00 56.07  ? 540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 115.232 143.805 181.877 1.00 56.82  ? 540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 113.586 141.342 180.919 1.00 55.88  ? 540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 112.473 140.638 180.176 1.00 54.36  ? 540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 111.619 139.764 180.832 1.00 55.00  ? 540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.276 140.851 178.819 1.00 54.38  ? 540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 110.599 139.120 180.157 1.00 54.84  ? 540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.260 140.213 178.136 1.00 58.02  ? 540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 110.425 139.349 178.810 1.00 58.24  ? 540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 109.410 138.710 178.133 1.00 57.26  ? 540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 114.180 143.065 183.741 1.00 62.58  ? 541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 115.200 143.606 184.634 1.00 61.40  ? 541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 116.555 142.951 184.403 1.00 63.08  ? 541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 117.593 143.600 184.575 1.00 64.37  ? 541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 114.768 143.436 186.089 1.00 62.44  ? 541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 114.134 144.679 186.692 1.00 65.56  ? 541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 114.524 144.886 188.142 1.00 68.41  ? 541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 115.403 144.147 188.634 1.00 67.75  ? 541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 113.952 145.788 188.790 1.00 66.43  ? 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 116.568 141.672 184.023 1.00 58.16  ? 542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 117.829 141.009 183.707 1.00 57.42  ? 542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 118.502 141.658 182.504 1.00 57.67  ? 542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 119.721 141.867 182.501 1.00 56.92  ? 542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 117.590 139.521 183.455 1.00 54.18  ? 542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 118.737 138.816 182.750 1.00 55.88  ? 542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 118.601 137.308 182.851 1.00 55.00  ? 542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 119.796 136.606 182.230 1.00 52.90  ? 542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.068 136.963 182.914 1.00 56.73  ? 542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 117.721 141.984 181.473 1.00 51.42  ? 543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 118.280 142.630 180.291 1.00 48.38  ? 543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 118.701 144.059 180.606 1.00 48.11  ? 543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 119.752 144.526 180.150 1.00 50.43  ? 543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 117.269 142.576 179.132 1.00 50.08  ? 543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 116.974 141.125 178.752 1.00 53.34  ? 543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 117.792 143.345 177.936 1.00 48.81  ? 543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 118.214 140.287 178.539 1.00 50.04  ? 543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 117.891 144.778 181.388 1.00 50.04  ? 544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 118.228 146.154 181.735 1.00 50.31  ? 544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 119.516 146.231 182.543 1.00 54.15  ? 544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 120.253 147.217 182.441 1.00 56.68  ? 544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 117.077 146.800 182.505 1.00 51.02  ? 544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 119.804 145.206 183.349 1.00 58.25  ? 545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 121.051 145.176 184.101 1.00 58.23  ? 545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 122.269 145.035 183.197 1.00 55.77  ? 545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 123.368 145.437 183.594 1.00 57.03  ? 545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 121.023 144.036 185.121 1.00 58.96  ? 545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 120.140 144.344 186.313 1.00 60.15  ? 545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 119.284 145.226 186.254 1.00 61.88  ? 545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 120.344 143.616 187.405 1.00 57.47  ? 545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 122.101 144.470 181.999 1.00 49.48  ? 546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 123.214 144.384 181.062 1.00 48.70  ? 546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 123.648 145.763 180.584 1.00 50.38  ? 546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 124.845 146.001 180.388 1.00 53.57  ? 546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 122.836 143.506 179.870 1.00 48.34  ? 546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 122.369 142.082 180.175 1.00 48.93  ? 546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.048 141.344 178.888 1.00 49.37  ? 546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 123.418 141.330 180.976 1.00 43.01  ? 546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 122.699 146.678 180.396 1.00 48.97  ? 547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 122.988 148.030 179.942 1.00 47.24  ? 547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 123.296 148.982 181.091 1.00 48.04  ? 547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 123.165 150.201 180.926 1.00 52.83  ? 547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 121.819 148.566 179.112 1.00 46.58  ? 547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 121.608 147.833 177.821 1.00 46.57  ? 547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 122.303 148.198 176.681 1.00 47.08  ? 547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 120.722 146.772 177.747 1.00 45.51  ? 547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 122.114 147.525 175.492 1.00 43.31  ? 547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 120.531 146.094 176.561 1.00 43.55  ? 547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 121.227 146.470 175.433 1.00 42.91  ? 547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 123.694 148.459 182.247 1.00 54.58  ? 548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 124.062 149.313 183.367 1.00 56.09  ? 548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 125.340 150.077 183.050 1.00 57.88  ? 548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 126.265 149.546 182.429 1.00 59.07  ? 548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 124.244 148.481 184.636 1.00 55.40  ? 548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 122.950 148.188 185.377 1.00 61.23  ? 548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 122.172 149.444 185.719 1.00 60.59  ? 548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 122.803 150.455 186.099 1.00 57.65  ? 548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 120.928 149.424 185.607 1.00 56.65  ? 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 125.388 151.335 183.480 1.00 55.32  ? 549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 126.499 152.198 183.146 1.00 56.51  ? 549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 126.481 152.732 181.735 1.00 58.41  ? 549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 127.467 153.340 181.305 1.00 57.44  ? 549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 125.392 152.522 180.999 1.00 55.62  ? 550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 125.256 152.986 179.627 1.00 54.46  ? 550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 123.950 153.753 179.499 1.00 58.44  ? 550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 122.923 153.326 180.036 1.00 56.79  ? 550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 125.278 151.816 178.642 1.00 53.63  ? 550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 126.572 151.680 177.869 1.00 58.34  ? 550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 126.432 150.465 176.553 1.00 60.49  ? 550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 126.390 148.946 177.498 1.00 56.23  ? 550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 123.989 154.879 178.792 1.00 59.81  ? 551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 122.804 155.711 178.616 1.00 56.32  ? 551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 121.975 155.158 177.465 1.00 54.67  ? 551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 122.348 155.300 176.296 1.00 54.87  ? 551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 123.201 157.161 178.358 1.00 56.82  ? 551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.065 158.023 177.903 1.00 59.52  ? 551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.012 158.359 178.726 1.00 59.31  ? 551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 121.815 158.612 176.710 1.00 58.18  ? 551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.163 159.121 178.061 1.00 58.18  ? 551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 120.626 159.290 176.835 1.00 58.94  ? 551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 120.852 154.525 177.791 1.00 49.03  ? 552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 119.936 154.005 176.781 1.00 49.21  ? 552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 119.158 155.172 176.186 1.00 50.21  ? 552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 118.530 155.938 176.931 1.00 51.28  ? 552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 118.991 152.949 177.375 1.00 48.87  ? 552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 119.791 151.867 178.102 1.00 49.43  ? 552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 118.133 152.331 176.286 1.00 47.46  ? 552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 118.932 150.867 178.837 1.00 50.08  ? 552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 119.181 155.355 174.867 1.00 45.78  ? 553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 118.441 156.471 174.256 1.00 42.29  ? 553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 116.946 156.353 174.515 1.00 48.33  ? 553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 116.310 155.361 174.152 1.00 47.05  ? 553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 118.771 156.337 172.766 1.00 43.31  ? 553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 120.051 155.577 172.726 1.00 43.39  ? 553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 120.000 154.631 173.883 1.00 42.82  ? 553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 116.389 157.381 175.148 1.00 56.17  ? 554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 114.970 157.420 175.453 1.00 52.83  ? 554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 114.206 158.091 174.314 1.00 52.81  ? 554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 114.759 158.414 173.261 1.00 54.04  ? 554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 114.728 158.146 176.776 1.00 52.65  ? 554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 114.565 159.547 176.531 1.00 52.24  ? 554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 115.900 157.933 177.723 1.00 51.58  ? 554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 112.905 158.295 174.529 1.00 49.60  ? 555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 112.085 158.969 173.529 1.00 49.09  ? 555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 112.524 160.417 173.340 1.00 51.44  ? 555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 112.575 160.917 172.209 1.00 49.46  ? 555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 110.611 158.894 173.933 1.00 50.81  ? 555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 110.132 157.557 173.744 1.00 51.64  ? 555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 109.771 159.845 173.100 1.00 51.10  ? 555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 112.853 161.105 174.436 1.00 55.21  ? 556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 113.321 162.484 174.335 1.00 53.93  ? 556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 114.650 162.564 173.593 1.00 55.48  ? 556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 114.869 163.479 172.789 1.00 54.38  ? 556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 113.447 163.096 175.730 1.00 55.05  ? 556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 112.239 163.908 176.163 1.00 54.67  ? 556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 112.336 165.365 175.756 1.00 58.82  ? 556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 112.271 165.652 174.543 1.00 57.16  ? 556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 112.478 166.224 176.651 1.00 58.60  ? 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 115.553 161.617 173.856 1.00 53.39  ? 557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 116.825 161.594 173.142 1.00 49.98  ? 557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 116.614 161.348 171.655 1.00 48.77  ? 557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 117.305 161.934 170.816 1.00 51.14  ? 557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 117.745 160.529 173.737 1.00 48.32  ? 557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 117.995 160.739 175.215 1.00 51.41  ? 557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 118.166 161.904 175.631 1.00 49.85  ? 557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.021 159.739 175.961 1.00 50.24  ? 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 115.658 160.484 171.307 1.00 40.46  ? 558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 115.357 160.257 169.898 1.00 35.36  ? 558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 114.728 161.483 169.250 1.00 41.06  ? 558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 114.995 161.762 168.079 1.00 47.05  ? 558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 114.449 159.041 169.743 1.00 40.24  ? 558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 115.202 157.765 169.531 1.00 36.77  ? 558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 115.382 156.760 170.434 1.00 38.38  ? 558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 115.883 157.361 168.338 1.00 39.08  ? 558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.130 155.752 169.875 1.00 39.77  ? 558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 116.448 156.096 168.589 1.00 36.73  ? 558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 116.064 157.942 167.079 1.00 44.61  ? 558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 117.183 155.404 167.629 1.00 32.96  ? 558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 116.794 157.254 166.130 1.00 40.05  ? 558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 117.345 156.000 166.410 1.00 33.18  ? 558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 113.898 162.228 169.987 1.00 48.30  ? 559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 113.377 163.487 169.461 1.00 48.14  ? 559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 114.500 164.484 169.211 1.00 46.46  ? 559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 114.515 165.177 168.184 1.00 46.34  ? 559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 112.349 164.078 170.427 1.00 47.23  ? 559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.024 163.341 170.471 1.00 49.12  ? 559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 109.976 164.154 171.210 1.00 49.38  ? 559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.094 163.269 172.073 1.00 49.11  ? 559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.318 163.514 173.525 1.00 48.56  ? 559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 115.447 164.575 170.147 1.00 45.33  ? 560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 116.589 165.465 169.964 1.00 43.70  ? 560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 117.423 165.046 168.761 1.00 45.86  ? 560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 117.880 165.895 167.988 1.00 53.28  ? 560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 117.446 165.491 171.229 1.00 45.13  ? 560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 116.773 166.150 172.422 1.00 48.65  ? 560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 117.408 165.714 173.735 1.00 50.95  ? 560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 118.923 165.636 173.624 1.00 49.74  ? 560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 119.511 164.738 174.656 1.00 46.17  ? 560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 117.629 163.739 168.585 1.00 36.43  ? 561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 118.371 163.253 167.426 1.00 32.42  ? 561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 117.629 163.544 166.128 1.00 40.10  ? 561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 118.252 163.873 165.113 1.00 45.79  ? 561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 118.640 161.755 167.561 1.00 35.52  ? 561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 119.370 161.137 166.370 1.00 37.76  ? 561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 120.742 161.761 166.220 1.00 34.56  ? 561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 119.474 159.632 166.511 1.00 37.96  ? 561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 116.301 163.414 166.135 1.00 38.38  ? 562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 115.514 163.738 164.950 1.00 37.03  ? 562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 115.647 165.212 164.590 1.00 40.42  ? 562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 115.823 165.560 163.416 1.00 40.64  ? 562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.050 163.367 165.185 1.00 38.97  ? 562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.094 163.853 164.112 1.00 40.56  ? 562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 111.652 163.578 164.506 1.00 39.72  ? 562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 110.684 164.106 163.463 1.00 43.21  ? 562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 109.336 163.489 163.596 1.00 38.06  ? 562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 115.575 166.092 165.592 1.00 41.37  ? 563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 115.767 167.517 165.339 1.00 41.59  ? 563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 117.174 167.801 164.825 1.00 42.96  ? 563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 117.361 168.614 163.912 1.00 49.20  ? 563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 115.484 168.319 166.608 1.00 40.35  ? 563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 118.178 167.136 165.403 1.00 37.66  ? 564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 119.558 167.321 164.967 1.00 36.35  ? 564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 119.745 166.882 163.522 1.00 39.53  ? 564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 120.445 167.544 162.747 1.00 44.14  ? 564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 120.492 166.545 165.896 1.00 37.67  ? 564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 121.945 166.889 165.735 1.00 38.25  ? 564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 122.487 167.983 166.388 1.00 40.80  ? 564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 122.773 166.107 164.951 1.00 38.32  ? 564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 123.825 168.297 166.249 1.00 42.66  ? 564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 124.111 166.415 164.808 1.00 41.11  ? 564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 124.637 167.511 165.457 1.00 43.49  ? 564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 119.131 165.761 163.142 1.00 37.12  ? 565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 119.222 165.279 161.767 1.00 31.43  ? 565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 118.510 166.233 160.818 1.00 36.98  ? 565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.001 166.522 159.721 1.00 38.81  ? 565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 118.658 163.850 161.669 1.00 32.53  ? 565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 118.341 163.494 160.228 1.00 35.60  ? 565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 119.643 162.864 162.257 1.00 35.24  ? 565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 117.344 166.743 161.223 1.00 44.10  ? 566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 116.638 167.706 160.386 1.00 45.26  ? 566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 117.467 168.967 160.180 1.00 48.16  ? 566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 117.480 169.540 159.085 1.00 48.84  ? 566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 115.283 168.047 161.005 1.00 40.56  ? 566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 118.167 169.413 161.225 1.00 46.94  ? 567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 118.950 170.639 161.125 1.00 42.57  ? 567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 120.231 170.443 160.317 1.00 44.02  ? 567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 120.576 171.293 159.488 1.00 48.85  ? 567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 119.273 171.162 162.526 1.00 41.93  ? 567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 120.573 171.938 162.626 1.00 46.68  ? 567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 120.468 173.130 163.558 1.00 51.00  ? 567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 119.499 173.187 164.344 1.00 47.38  ? 567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 121.352 174.009 163.502 1.00 48.74  ? 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 120.942 169.333 160.529 1.00 43.79  ? 568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 122.267 169.144 159.951 1.00 42.38  ? 568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 122.334 168.085 158.859 1.00 38.82  ? 568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 123.317 168.059 158.112 1.00 42.44  ? 568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 123.276 168.786 161.051 1.00 43.02  ? 568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 123.536 169.901 162.015 1.00 42.76  ? 568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 123.549 169.717 163.380 1.00 46.64  ? 568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 123.802 171.212 161.809 1.00 40.38  ? 568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 123.803 170.869 163.975 1.00 42.31  ? 568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 123.962 171.792 163.044 1.00 45.38  ? 568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 121.336 167.223 158.741 1.00 37.12  ? 569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 121.354 166.208 157.710 1.00 35.73  ? 569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.042 164.929 158.139 1.00 35.52  ? 569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 122.434 164.734 159.294 1.00 40.65  ? 569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.181 164.030 157.167 1.00 31.72  ? 570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 122.789 162.722 157.372 1.00 27.74  ? 570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 123.853 162.501 156.309 1.00 31.95  ? 570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 123.585 162.673 155.117 1.00 36.93  ? 570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 121.739 161.611 157.306 1.00 33.36  ? 570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 120.865 161.504 158.538 1.00 32.70  ? 570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 121.371 160.148 159.604 1.00 40.94  ? 570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 121.344 158.797 158.433 1.00 30.30  ? 570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.056 162.116 156.739 1.00 23.75  ? 571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.142 161.921 155.785 1.00 16.90  ? 571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 125.994 160.618 155.010 1.00 30.52  ? 571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 126.375 160.553 153.835 1.00 34.37  ? 571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 127.490 161.954 156.501 1.00 26.87  ? 571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 128.665 162.074 155.559 1.00 29.46  ? 571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 128.992 163.292 154.978 1.00 32.78  ? 571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 129.440 160.968 155.240 1.00 27.78  ? 571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.061 163.406 154.114 1.00 31.14  ? 571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 130.510 161.073 154.376 1.00 31.33  ? 571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 130.817 162.293 153.817 1.00 38.02  ? 571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 131.884 162.401 152.956 1.00 39.28  ? 571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 125.456 159.577 155.637 1.00 30.83  ? 572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 125.347 158.259 155.028 1.00 14.94  ? 572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 123.894 157.963 154.691 1.00 24.17  ? 572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.011 158.129 155.539 1.00 33.94  ? 572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 125.893 157.173 155.956 1.00 13.60  ? 572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.228 157.497 156.550 1.00 23.33  ? 572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 127.371 158.243 157.699 1.00 24.89  ? 572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 128.481 157.169 156.157 1.00 22.27  ? 572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 128.654 158.364 157.987 1.00 23.54  ? 572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 129.350 157.721 157.066 1.00 28.30  ? 572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 123.650 157.533 153.452 1.00 21.36  ? 573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.316 157.070 153.084 1.00 19.12  ? 573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 121.952 155.800 153.841 1.00 28.55  ? 573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 120.817 155.650 154.308 1.00 33.72  ? 573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.240 156.840 151.576 1.00 17.51  ? 573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 123.337 156.071 151.125 1.00 28.17  ? 573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 122.902 154.878 153.969 1.00 27.69  ? 574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 122.714 153.634 154.699 1.00 17.92  ? 574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 123.888 153.437 155.641 1.00 16.61  ? 574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.032 153.739 155.288 1.00 21.28  ? 574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 122.586 152.445 153.745 1.00 18.12  ? 574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 121.523 152.641 152.692 1.00 16.04  ? 574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 120.217 152.235 152.915 1.00 17.59  ? 574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 121.822 153.251 151.483 1.00 16.23  ? 574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 119.242 152.421 151.960 1.00 20.35  ? 574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 120.854 153.442 150.523 1.00 12.35  ? 574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 119.567 153.024 150.767 1.00 14.81  ? 574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 118.601 153.211 149.809 1.00 29.00  ? 574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 123.605 152.943 156.839 1.00 17.52  ? 575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 124.626 152.807 157.868 1.00 9.31   ? 575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 124.758 151.399 158.418 1.00 18.51  ? 575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 125.878 150.944 158.663 1.00 30.93  ? 575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 124.335 153.770 159.025 1.00 15.39  ? 575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 124.220 155.222 158.613 1.00 17.26  ? 575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 123.266 155.969 159.521 1.00 15.93  ? 575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 121.895 155.500 159.373 1.00 21.51  ? 575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 121.273 154.713 160.241 1.00 18.85  ? 575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 121.877 154.273 161.331 1.00 18.23  ? 575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.013 154.359 160.008 1.00 14.60  ? 575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 123.653 150.691 158.620 1.00 15.63  ? 576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 123.659 149.410 159.312 1.00 13.95  ? 576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 123.277 148.293 158.353 1.00 12.29  ? 576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 122.248 148.376 157.676 1.00 27.17  ? 576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 122.698 149.431 160.500 1.00 12.71  ? 576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 122.939 150.516 161.548 1.00 14.42  ? 576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 121.843 150.486 162.590 1.00 20.67  ? 576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 124.298 150.348 162.197 1.00 15.54  ? 576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 124.106 147.254 158.303 1.00 14.48  ? 577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 123.792 146.042 157.558 1.00 13.99  ? 577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 124.599 144.906 158.166 1.00 28.18  ? 577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 125.813 145.034 158.343 1.00 34.37  ? 577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 124.090 146.203 156.059 1.00 13.90  ? 577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 125.802 145.956 155.533 1.00 29.35  ? 577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 123.925 143.813 158.505 1.00 20.92  ? 578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 124.529 142.723 159.259 1.00 21.31  ? 578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 124.934 141.641 158.265 1.00 16.68  ? 578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 124.093 140.900 157.750 1.00 19.45  ? 578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 123.583 142.190 160.338 1.00 14.09  ? 578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 123.194 143.321 161.290 1.00 2.32   ? 578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 124.238 141.066 161.111 1.00 15.61  ? 578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 122.320 142.885 162.431 1.00 16.00  ? 578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 126.233 141.554 157.996 1.00 22.86  ? 579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 126.792 140.551 157.107 1.00 17.63  ? 579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 127.049 139.252 157.865 1.00 22.37  ? 579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 127.151 139.252 159.093 1.00 38.53  ? 579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 128.086 141.072 156.489 1.00 23.12  ? 579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 127.137 138.120 157.155 1.00 22.55  ? 580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.397 136.851 157.858 1.00 26.58  ? 580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.707 136.839 158.626 1.00 29.93  ? 580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 128.765 136.275 159.726 1.00 37.13  ? 580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.386 135.814 156.725 1.00 28.34  ? 580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.603 136.594 155.476 1.00 32.28  ? 580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 126.961 137.919 155.708 1.00 25.43  ? 580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 129.756 137.458 158.080 1.00 27.21  ? 581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 131.064 137.556 158.734 1.00 38.49  ? 581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.544 136.192 159.225 1.00 38.92  ? 581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 131.923 136.016 160.383 1.00 39.27  ? 581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.028 138.565 159.882 1.00 39.43  ? 581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.334 137.999 161.000 1.00 23.54  ? 581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.322 139.835 159.444 1.00 34.77  ? 581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.524 135.213 158.319 1.00 44.80  ? 582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 131.864 133.852 158.691 1.00 46.63  ? 582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.346 133.605 158.880 1.00 50.23  ? 582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.720 132.617 159.521 1.00 55.49  ? 582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.196 134.475 158.339 1.00 41.11  ? 583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 135.641 134.284 158.396 1.00 42.75  ? 583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.295 135.070 159.526 1.00 42.80  ? 583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.068 134.506 160.306 1.00 38.48  ? 583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 136.271 134.673 157.053 1.00 47.59  ? 583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 135.977 133.712 156.054 1.00 47.10  ? 583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 136.001 136.369 159.631 1.00 46.24  ? 584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.565 137.191 160.696 1.00 42.73  ? 584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 135.990 136.863 162.062 1.00 41.69  ? 584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.512 137.344 163.074 1.00 49.58  ? 584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 136.352 138.688 160.400 1.00 42.62  ? 584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.005 138.907 159.706 1.00 42.10  ? 584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 137.497 139.235 159.563 1.00 37.97  ? 584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 134.579 140.356 159.633 1.00 38.83  ? 584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 134.921 136.065 162.120 1.00 39.71  ? 585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.341 135.696 163.406 1.00 31.85  ? 585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.309 134.851 164.224 1.00 33.32  ? 585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.347 134.956 165.455 1.00 39.79  ? 585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 133.026 134.949 163.194 1.00 37.10  ? 585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.228 133.762 162.448 1.00 39.19  ? 585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.089 133.997 163.557 1.00 43.66  ? 586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.064 133.175 164.266 1.00 40.12  ? 586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.118 134.038 164.947 1.00 40.12  ? 586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.442 133.832 166.121 1.00 41.89  ? 586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 137.723 132.194 163.297 1.00 39.46  ? 586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 136.801 131.119 162.774 1.00 40.42  ? 586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 136.500 130.002 163.539 1.00 44.47  ? 586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 136.235 131.218 161.510 1.00 40.35  ? 586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 135.660 129.016 163.062 1.00 46.79  ? 586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 135.393 130.238 161.026 1.00 42.93  ? 586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 135.109 129.139 161.805 1.00 48.11  ? 586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 134.272 128.157 161.329 1.00 48.68  ? 586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.647 135.028 164.223 1.00 43.30  ? 587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 139.721 135.865 164.755 1.00 38.75  ? 587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 139.242 136.647 165.970 1.00 40.01  ? 587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 139.968 136.797 166.960 1.00 41.26  ? 587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.258 136.800 163.657 1.00 35.05  ? 587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.439 137.606 164.173 1.00 36.90  ? 587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.646 135.999 162.428 1.00 40.71  ? 587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 138.016 137.157 165.916 1.00 40.58  ? 588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 137.460 137.942 167.008 1.00 36.58  ? 588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 136.884 137.082 168.122 1.00 37.89  ? 588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 136.394 137.637 169.112 1.00 39.09  ? 588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 136.381 138.886 166.474 1.00 27.31  ? 588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 136.925 140.031 165.645 1.00 27.58  ? 588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 137.023 141.322 166.429 1.00 37.54  ? 588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 136.146 141.644 167.229 1.00 35.53  ? 588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 138.095 142.070 166.204 1.00 41.82  ? 588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 136.934 135.758 167.987 1.00 37.32  ? 589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.342 134.832 168.948 1.00 33.45  ? 589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 134.872 135.179 169.178 1.00 36.45  ? 589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.427 135.452 170.295 1.00 39.59  ? 589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.127 134.824 170.262 1.00 39.89  ? 589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.091 133.786 170.269 1.00 42.22  ? 589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.125 135.182 168.078 1.00 35.34  ? 590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 132.735 135.601 168.080 1.00 29.24  ? 590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 131.920 134.667 167.200 1.00 33.44  ? 590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 132.439 134.073 166.252 1.00 33.36  ? 590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.589 137.044 167.582 1.00 29.22  ? 590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.327 137.081 166.192 1.00 35.36  ? 590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 130.639 134.535 167.530 1.00 35.34  ? 591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 129.725 133.801 166.671 1.00 35.19  ? 591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.424 134.612 165.414 1.00 32.19  ? 591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.354 135.842 165.443 1.00 30.34  ? 591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 128.429 133.477 167.411 1.00 32.23  ? 591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 127.610 134.650 167.485 1.00 34.81  ? 591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 128.732 132.988 168.816 1.00 28.99  ? 591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.253 133.904 164.301 1.00 31.17  ? 592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.060 134.560 163.014 1.00 34.53  ? 592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 127.725 135.293 162.989 1.00 31.30  ? 592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 126.673 134.685 163.211 1.00 35.21  ? 592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.132 133.537 161.884 1.00 32.76  ? 592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 127.775 136.601 162.720 1.00 27.04  ? 593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.584 137.430 162.559 1.00 21.42  ? 593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 125.690 137.381 163.790 1.00 29.56  ? 593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.145 137.042 164.887 1.00 31.71  ? 593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 125.801 136.996 161.317 1.00 30.60  ? 593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 124.767 137.915 161.015 1.00 29.12  ? 593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.416 137.725 163.618 1.00 35.29  ? 594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.435 137.631 164.692 1.00 24.60  ? 594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 122.749 136.276 164.605 1.00 25.56  ? 594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 121.771 136.012 165.315 1.00 26.96  ? 594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.414 138.781 164.623 1.00 21.21  ? 594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 123.104 140.115 164.850 1.00 20.60  ? 594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 121.696 138.770 163.286 1.00 23.25  ? 594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.258 135.410 163.733 1.00 29.39  ? 595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 122.703 134.077 163.586 1.00 31.23  ? 595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.040 133.219 164.804 1.00 33.84  ? 595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.081 133.405 165.439 1.00 35.30  ? 595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.247 133.407 162.328 1.00 30.27  ? 595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 122.585 133.836 161.028 1.00 29.61  ? 595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 120.808 134.085 161.167 1.00 34.49  ? 595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 120.723 135.871 161.136 1.00 29.54  ? 595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 122.172 132.273 165.153 1.00 33.10  ? 596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 122.526 131.293 166.182 1.00 29.16  ? 596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 123.601 130.339 165.683 1.00 34.17  ? 596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 123.777 130.125 164.481 1.00 39.49  ? 596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 121.207 130.560 166.450 1.00 30.82  ? 596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 120.398 130.771 165.218 1.00 34.33  ? 596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 120.788 132.110 164.678 1.00 32.07  ? 596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 124.330 129.762 166.637 1.00 35.52  ? 597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 125.472 128.920 166.303 1.00 37.60  ? 597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 124.999 127.638 165.630 1.00 44.06  ? 597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 123.992 127.034 166.027 1.00 46.17  ? 597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 126.303 128.619 167.562 1.00 35.64  ? 597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 125.477 127.834 168.582 1.00 37.12  ? 597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 126.805 129.910 168.181 1.00 40.34  ? 597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 126.305 127.002 169.524 1.00 36.45  ? 597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 125.716 127.229 164.582 1.00 45.94  ? 598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 125.389 125.979 163.904 1.00 47.56  ? 598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 125.781 124.776 164.752 1.00 49.33  ? 598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 124.993 123.838 164.920 1.00 49.30  ? 598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 126.084 125.925 162.544 1.00 46.64  ? 598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 125.183 126.248 161.371 1.00 47.41  ? 598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 126.082 126.994 159.999 1.00 59.57  ? 598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 127.423 125.824 159.798 1.00 47.81  ? 598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 126.997 124.786 165.296 1.00 50.00  ? 599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 127.511 123.680 166.090 1.00 46.67  ? 599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 128.179 124.227 167.341 1.00 47.33  ? 599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 128.827 125.275 167.297 1.00 52.41  ? 599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 128.516 122.833 165.298 1.00 47.02  ? 599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 128.055 122.440 163.905 1.00 52.43  ? 599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 129.148 122.588 162.866 1.00 57.57  ? 599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 129.964 121.655 162.724 1.00 58.12  ? 599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 129.191 123.640 162.193 1.00 57.60  ? 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 128.015 123.510 168.455 1.00 48.64  ? 600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 128.675 123.912 169.692 1.00 47.76  ? 600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 130.190 123.820 169.566 1.00 48.72  ? 600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 130.912 124.705 170.035 1.00 52.62  ? 600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 128.180 123.055 170.855 1.00 49.05  ? 600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 126.820 123.465 171.381 1.00 47.86  ? 600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 126.451 122.684 172.624 1.00 49.04  ? 600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 125.099 122.984 173.077 1.00 50.70  ? 600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 124.008 122.383 172.622 1.00 52.76  ? 600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 124.072 121.442 171.695 1.00 50.71  ? 600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 122.822 122.738 173.109 1.00 52.60  ? 600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 130.689 122.755 168.943 1.00 53.41  ? 601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 132.116 122.567 168.704 1.00 51.51  ? 601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 132.271 122.258 167.221 1.00 49.25  ? 601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 131.986 121.139 166.780 1.00 53.68  ? 601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 132.719 121.454 169.566 1.00 51.97  ? 601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 132.413 121.698 171.045 1.00 52.09  ? 601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 134.217 121.371 169.345 1.00 53.09  ? 601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 132.890 120.593 171.954 1.00 50.62  ? 601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 132.719 123.243 166.448 1.00 56.28  ? 602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 132.890 123.052 165.015 1.00 60.22  ? 602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 134.053 122.110 164.733 1.00 63.83  ? 602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 135.125 122.223 165.333 1.00 66.91  ? 602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 133.126 124.395 164.327 1.00 62.34  ? 602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 131.859 125.187 164.057 1.00 64.30  ? 602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 132.137 126.515 163.384 1.00 65.68  ? 602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.321 126.819 163.130 1.00 65.39  ? 602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 131.170 127.258 163.110 1.00 61.58  ? 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 133.834 121.177 163.813 1.00 67.89  ? 603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 134.868 120.253 163.368 1.00 68.82  ? 603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 135.384 120.721 162.014 1.00 70.47  ? 603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 134.623 120.779 161.042 1.00 69.97  ? 603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 134.325 118.827 163.275 1.00 69.34  ? 603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.290 117.760 163.763 1.00 69.86  ? 603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 134.689 116.370 163.719 1.00 72.89  ? 603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.647 116.192 163.053 1.00 70.56  ? 603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 135.256 115.455 164.351 1.00 72.95  ? 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 136.670 121.052 161.952 1.00 68.99  ? 604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 137.286 121.571 160.741 1.00 69.17  ? 604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 138.555 120.792 160.441 1.00 70.13  ? 604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 139.337 120.487 161.346 1.00 70.29  ? 604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 137.609 123.063 160.876 1.00 71.55  ? 604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 136.404 123.978 160.753 1.00 70.71  ? 604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 135.543 123.606 159.558 1.00 70.46  ? 604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 134.253 123.062 159.964 1.00 72.11  ? 604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 133.161 123.790 160.156 1.00 71.70  ? 604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 133.168 125.102 159.989 1.00 70.73  ? 604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 132.035 123.185 160.524 1.00 67.93  ? 604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 138.757 120.474 159.165 1.00 77.06  ? 605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 139.937 119.754 158.700 1.00 78.98  ? 605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 140.768 120.701 157.843 1.00 75.98  ? 605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 140.324 121.129 156.772 1.00 74.22  ? 605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 139.545 118.509 157.908 1.00 77.84  ? 605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 138.838 117.599 158.760 1.00 75.02  ? 605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 140.785 117.818 157.361 1.00 76.57  ? 605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 141.972 121.027 158.314 1.00 76.85  ? 606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 142.914 121.879 157.589 1.00 80.11  ? 606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 144.178 121.054 157.370 1.00 80.17  ? 606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 145.062 121.014 158.229 1.00 77.70  ? 606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 143.195 123.171 158.352 1.00 77.28  ? 606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 141.957 123.998 158.610 1.00 76.73  ? 606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 141.143 124.410 157.564 1.00 75.19  ? 606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 141.596 124.361 159.901 1.00 77.12  ? 606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 140.009 125.163 157.794 1.00 75.92  ? 606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 140.464 125.113 160.142 1.00 78.36  ? 606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 139.674 125.512 159.084 1.00 78.68  ? 606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 138.543 126.260 159.317 1.00 77.44  ? 606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 144.257 120.394 156.218 1.00 83.26  ? 607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 145.342 119.473 155.950 1.00 81.75  ? 607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 144.944 118.042 156.240 1.00 84.76  ? 607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 143.845 117.612 155.878 1.00 85.60  ? 607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 145.831 117.289 156.891 1.00 90.09  ? 608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 145.543 115.923 157.306 1.00 91.63  ? 608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 145.177 115.832 158.781 1.00 89.54  ? 608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 145.155 114.733 159.345 1.00 86.84  ? 608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 146.735 115.015 157.000 1.00 89.81  ? 608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 146.315 113.676 156.432 1.00 90.21  ? 608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 145.167 113.496 156.023 1.00 89.28  ? 608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 147.242 112.727 156.405 1.00 88.80  ? 608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 144.888 116.964 159.415 1.00 86.29  ? 609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 144.558 117.017 160.830 1.00 85.62  ? 609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 143.255 117.777 161.028 1.00 84.78  ? 609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 143.035 118.826 160.410 1.00 83.69  ? 609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 145.677 117.687 161.628 1.00 83.27  ? 609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 146.060 118.910 161.021 1.00 83.54  ? 609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 142.400 117.244 161.896 1.00 76.63  ? 610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 141.150 117.896 162.258 1.00 74.44  ? 610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 141.402 118.884 163.387 1.00 74.96  ? 610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 142.174 118.603 164.307 1.00 74.61  ? 610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 140.105 116.866 162.681 1.00 74.98  ? 610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 139.439 116.153 161.515 1.00 77.55  ? 610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 138.225 115.307 161.918 1.00 75.88  ? 610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 138.322 114.609 163.284 1.00 75.69  ? 610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 139.663 114.066 163.671 1.00 75.25  ? 610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 140.752 120.040 163.312 1.00 73.60  ? 611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 140.940 121.124 164.275 1.00 71.47  ? 611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 139.573 121.524 164.822 1.00 70.58  ? 611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 138.785 122.173 164.129 1.00 71.26  ? 611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 141.645 122.310 163.627 1.00 73.72  ? 611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 140.860 122.785 162.525 1.00 74.14  ? 611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.020 121.901 163.121 1.00 72.37  ? 611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 139.294 121.134 166.064 1.00 66.72  ? 612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 138.011 121.434 166.682 1.00 66.30  ? 612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 137.993 122.869 167.189 1.00 67.20  ? 612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 138.969 123.343 167.776 1.00 67.83  ? 612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 137.727 120.468 167.832 1.00 65.58  ? 612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 138.007 119.024 167.495 1.00 67.24  ? 612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 137.034 118.224 166.913 1.00 66.32  ? 612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 139.240 118.453 167.779 1.00 67.07  ? 612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 137.287 116.901 166.606 1.00 66.81  ? 612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 139.499 117.133 167.480 1.00 68.18  ? 612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 138.521 116.361 166.894 1.00 68.73  ? 612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 138.781 115.043 166.597 1.00 68.11  ? 612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 136.880 123.558 166.958 1.00 58.77  ? 613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 136.690 124.923 167.447 1.00 54.30  ? 613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 135.461 124.996 168.339 1.00 52.53  ? 613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 134.328 125.092 167.832 1.00 54.67  ? 613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 136.565 125.907 166.287 1.00 56.31  ? 613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 136.258 127.312 166.740 1.00 53.29  ? 613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 137.071 127.956 167.661 1.00 51.66  ? 613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 135.153 127.993 166.254 1.00 55.10  ? 613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 136.798 129.237 168.081 1.00 51.60  ? 613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 134.869 129.277 166.669 1.00 56.68  ? 613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 135.696 129.893 167.583 1.00 56.24  ? 613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 135.424 131.172 168.003 1.00 55.04  ? 613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 135.621 124.944 169.659 1.00 50.01  ? 614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 134.482 125.201 170.543 1.00 48.68  ? 614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 133.987 126.630 170.378 1.00 50.30  ? 614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 134.748 127.541 170.049 1.00 52.20  ? 614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 135.054 124.963 171.947 1.00 48.25  ? 614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 136.317 124.190 171.731 1.00 53.38  ? 614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 136.847 124.637 170.411 1.00 52.31  ? 614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 132.689 126.815 170.599 1.00 47.11  ? 615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 132.091 128.128 170.436 1.00 42.47  ? 615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 132.679 129.103 171.455 1.00 46.85  ? 615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 133.090 128.699 172.547 1.00 48.75  ? 615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 130.575 128.050 170.590 1.00 41.81  ? 615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 129.852 127.666 169.312 1.00 44.68  ? 615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 130.211 128.776 167.938 1.00 51.57  ? 615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.176 127.702 166.880 1.00 43.36  ? 615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 132.753 130.391 171.114 1.00 46.18  ? 616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 133.365 131.372 172.025 1.00 43.10  ? 616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 132.669 131.395 173.376 1.00 45.38  ? 616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 131.493 131.744 173.485 1.00 47.09  ? 616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 133.191 132.698 171.278 1.00 41.15  ? 616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 133.061 132.313 169.848 1.00 43.13  ? 616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 132.343 131.003 169.839 1.00 44.68  ? 616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 133.415 131.030 174.416 1.00 45.21  ? 617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 132.874 130.993 175.757 1.00 45.13  ? 617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 132.096 129.745 176.105 1.00 48.58  ? 617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 131.494 129.694 177.183 1.00 51.33  ? 617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 132.079 128.744 175.228 1.00 49.61  ? 618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 131.387 127.498 175.526 1.00 48.47  ? 618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 132.033 126.803 176.716 1.00 50.34  ? 618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 133.257 126.670 176.790 1.00 54.97  ? 618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 131.402 126.576 174.307 1.00 48.01  ? 618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 130.679 125.236 174.448 1.00 47.68  ? 618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 129.176 125.437 174.532 1.00 51.02  ? 618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 131.032 124.315 173.293 1.00 48.86  ? 618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 131.201 126.360 177.651 1.00 52.79  ? 619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 131.669 125.689 178.855 1.00 55.24  ? 619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 130.558 124.769 179.347 1.00 55.14  ? 619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 129.553 124.555 178.659 1.00 57.03  ? 619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 132.095 126.705 179.919 1.00 52.29  ? 619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 130.740 124.217 180.547 1.00 58.84  ? 620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 129.746 123.302 181.097 1.00 59.15  ? 620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 128.526 124.050 181.619 1.00 61.14  ? 620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 127.395 123.563 181.498 1.00 59.34  ? 620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 130.372 122.459 182.206 1.00 63.00  ? 620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 131.635 121.955 181.809 1.00 64.37  ? 620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 128.730 125.233 182.203 1.00 62.64  ? 621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 127.617 125.957 182.808 1.00 61.45  ? 621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 126.703 126.579 181.760 1.00 60.08  ? 621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 125.515 126.794 182.028 1.00 60.33  ? 621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 128.143 127.034 183.757 1.00 60.22  ? 621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 129.307 127.806 183.175 1.00 63.46  ? 621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 130.186 127.234 182.531 1.00 63.68  ? 621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 129.320 129.115 183.399 1.00 60.97  ? 621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 127.226 126.874 180.571 1.00 52.95  ? 622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 126.443 127.478 179.500 1.00 54.87  ? 622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 126.358 126.563 178.282 1.00 55.31  ? 622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 126.309 127.036 177.144 1.00 57.15  ? 622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 127.015 128.842 179.115 1.00 53.37  ? 622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 128.477 128.777 178.716 1.00 56.39  ? 622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 129.053 127.698 178.590 1.00 58.05  ? 622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 129.086 129.940 178.518 1.00 54.98  ? 622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 126.346 125.249 178.508 1.00 51.26  ? 623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 126.280 124.308 177.394 1.00 51.61  ? 623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 124.931 124.370 176.688 1.00 52.90  ? 623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 124.871 124.364 175.453 1.00 51.56  ? 623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 126.559 122.889 177.888 1.00 56.18  ? 623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 126.598 121.875 176.790 1.00 53.87  ? 623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 125.551 121.142 176.315 1.00 52.09  ? 623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 127.741 121.484 176.022 1.00 52.07  ? 623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 125.971 120.318 175.302 1.00 56.74  ? 623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 127.313 120.508 175.103 1.00 55.64  ? 623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 129.087 121.864 176.025 1.00 51.10  ? 623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 128.180 119.908 174.194 1.00 52.95  ? 623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 129.944 121.266 175.122 1.00 55.54  ? 623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 129.489 120.300 174.219 1.00 55.48  ? 623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 123.838 124.425 177.451 1.00 54.88  ? 624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 122.511 124.429 176.850 1.00 54.86  ? 624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 122.059 125.816 176.418 1.00 54.52  ? 624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 121.068 125.930 175.689 1.00 57.66  ? 624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 121.495 123.823 177.819 1.00 53.85  ? 624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 121.695 122.355 178.058 1.00 55.69  ? 624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 121.753 121.470 176.994 1.00 53.58  ? 624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 121.833 121.858 179.343 1.00 56.52  ? 624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 121.939 120.119 177.205 1.00 53.02  ? 624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 122.021 120.506 179.562 1.00 56.82  ? 624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 122.073 119.637 178.491 1.00 56.42  ? 624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 122.757 126.870 176.847 1.00 43.37  ? 625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 122.490 128.191 176.293 1.00 39.55  ? 625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 123.047 128.319 174.884 1.00 38.78  ? 625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 122.513 129.084 174.073 1.00 41.58  ? 625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 123.068 129.275 177.201 1.00 37.01  ? 625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 122.316 129.452 178.487 1.00 35.38  ? 625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 121.005 129.895 178.478 1.00 37.03  ? 625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 122.916 129.175 179.702 1.00 38.28  ? 625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 120.307 130.060 179.657 1.00 38.48  ? 625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 122.222 129.338 180.885 1.00 41.60  ? 625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 120.916 129.781 180.862 1.00 41.38  ? 625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 124.110 127.580 174.574 1.00 37.64  ? 626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 124.650 127.540 173.223 1.00 40.78  ? 626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 123.890 126.518 172.390 1.00 41.51  ? 626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 124.493 125.619 171.796 1.00 45.35  ? 626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 126.142 127.208 173.246 1.00 40.89  ? 626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 127.025 128.411 173.469 1.00 40.60  ? 626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 127.275 129.311 172.443 1.00 40.68  ? 626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 127.608 128.646 174.705 1.00 40.50  ? 626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 128.080 130.413 172.644 1.00 40.27  ? 626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 128.415 129.743 174.915 1.00 41.68  ? 626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 128.646 130.624 173.881 1.00 45.03  ? 626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 129.448 131.719 174.088 1.00 47.24  ? 626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 122.567 126.644 172.351 1.00 43.75  ? 627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 121.739 125.709 171.603 1.00 44.40  ? 627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 122.028 125.829 170.112 1.00 44.84  ? 627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 122.080 126.935 169.567 1.00 46.32  ? 627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 120.264 125.980 171.888 1.00 45.46  ? 627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 119.295 125.014 171.239 1.00 45.05  ? 627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 117.871 125.338 171.655 1.00 44.71  ? 627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 116.864 124.462 170.937 1.00 49.46  ? 627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 115.466 124.871 171.244 1.00 47.30  ? 627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 122.224 124.688 169.457 1.00 48.08  ? 628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 122.528 124.689 168.035 1.00 47.15  ? 628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 121.339 125.200 167.231 1.00 48.52  ? 628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 120.179 124.952 167.568 1.00 51.28  ? 628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 122.916 123.286 167.568 1.00 49.26  ? 628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 124.266 122.818 168.081 1.00 52.38  ? 628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 124.639 121.441 167.568 1.00 55.14  ? 628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 124.050 121.003 166.557 1.00 54.77  ? 628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 125.521 120.798 168.175 1.00 49.65  ? 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 121.646 125.920 166.150 1.00 45.76  ? 629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 120.608 126.578 165.364 1.00 43.07  ? 629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 119.630 125.582 164.754 1.00 50.23  ? 629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 118.457 125.914 164.550 1.00 51.44  ? 629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 121.247 127.426 164.268 1.00 40.61  ? 629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 120.090 124.367 164.453 1.00 56.60  ? 630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 119.207 123.378 163.844 1.00 50.94  ? 630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 118.158 122.875 164.827 1.00 54.08  ? 630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 117.033 122.561 164.422 1.00 56.78  ? 630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 120.027 122.213 163.295 1.00 50.53  ? 630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 121.023 122.624 162.238 1.00 49.71  ? 630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 120.610 122.925 160.948 1.00 51.44  ? 630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 122.377 122.710 162.529 1.00 49.25  ? 630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 121.516 123.301 159.978 1.00 52.10  ? 630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 123.290 123.084 161.565 1.00 50.89  ? 630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 122.854 123.378 160.292 1.00 54.14  ? 630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 123.761 123.753 159.327 1.00 52.44  ? 630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 118.502 122.792 166.111 1.00 51.71  ? 631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 117.555 122.346 167.125 1.00 50.83  ? 631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 116.579 123.436 167.545 1.00 52.94  ? 631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 115.609 123.136 168.250 1.00 53.18  ? 631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 118.307 121.837 168.357 1.00 52.39  ? 631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 119.445 120.901 168.001 1.00 58.82  ? 631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 119.363 120.238 166.946 1.00 59.32  ? 631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 120.421 120.830 168.777 1.00 58.78  ? 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 116.804 124.678 167.132 1.00 50.36  ? 632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 115.973 125.796 167.551 1.00 49.75  ? 632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 114.739 125.926 166.670 1.00 49.79  ? 632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 114.735 125.524 165.503 1.00 51.70  ? 632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 116.765 127.103 167.512 1.00 45.74  ? 632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.008 127.097 168.369 1.00 48.20  ? 632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 118.856 128.683 168.370 1.00 51.12  ? 632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 119.105 128.904 170.126 1.00 46.81  ? 632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 113.687 126.498 167.247 1.00 40.38  ? 633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 112.490 126.825 166.485 1.00 36.97  ? 633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 112.802 127.970 165.532 1.00 42.54  ? 633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 113.204 129.054 165.966 1.00 48.71  ? 633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 111.352 127.203 167.430 1.00 39.03  ? 633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 110.027 127.381 166.713 1.00 47.07  ? 633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 109.958 127.106 165.496 1.00 46.46  ? 633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 109.051 127.803 167.367 1.00 45.76  ? 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 112.624 127.730 164.231 1.00 37.28  ? 634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 112.913 128.767 163.249 1.00 30.81  ? 634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 111.968 129.953 163.364 1.00 27.89  ? 634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 112.334 131.058 162.956 1.00 32.16  ? 634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 112.859 128.189 161.836 1.00 35.50  ? 634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 114.198 127.678 161.349 1.00 38.18  ? 634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 115.417 129.001 161.250 1.00 49.29  ? 634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 116.726 128.321 162.263 1.00 36.76  ? 634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 110.770 129.753 163.914 1.00 35.16  ? 635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 109.879 130.882 164.160 1.00 35.58  ? 635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 110.472 131.828 165.197 1.00 32.86  ? 635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 110.371 133.052 165.065 1.00 35.98  ? 635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 108.504 130.381 164.606 1.00 36.94  ? 635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 107.605 129.981 163.469 1.00 31.40  ? 635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 108.123 129.385 162.331 1.00 27.12  ? 635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 106.241 130.198 163.542 1.00 33.09  ? 635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 107.297 129.018 161.288 1.00 33.76  ? 635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 105.411 129.832 162.501 1.00 37.60  ? 635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 105.941 129.241 161.373 1.00 37.51  ? 635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 111.109 131.276 166.232 1.00 32.97  ? 636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 111.752 132.116 167.236 1.00 34.24  ? 636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 112.945 132.863 166.650 1.00 35.44  ? 636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 113.191 134.024 166.998 1.00 42.34  ? 636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 112.179 131.264 168.430 1.00 36.42  ? 636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.035 130.880 169.354 1.00 35.03  ? 636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 110.123 132.064 169.621 1.00 41.00  ? 636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 108.665 131.642 169.671 1.00 41.47  ? 636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 107.753 132.814 169.783 1.00 41.25  ? 636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 113.695 132.218 165.755 1.00 30.58  ? 637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 114.809 132.894 165.099 1.00 27.54  ? 637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 114.297 134.005 164.189 1.00 33.67  ? 637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 114.903 135.079 164.097 1.00 36.00  ? 637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 115.672 131.878 164.332 1.00 27.62  ? 637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 116.916 132.548 163.782 1.00 31.56  ? 637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 116.042 130.713 165.236 1.00 33.00  ? 637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.176 133.766 163.503 1.00 35.94  ? 638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 112.555 134.815 162.700 1.00 29.99  ? 638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.131 135.978 163.584 1.00 33.52  ? 638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.302 137.147 163.223 1.00 39.72  ? 638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 111.361 134.254 161.906 1.00 28.20  ? 638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 110.549 135.388 161.314 1.00 29.12  ? 638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 111.833 133.316 160.812 1.00 31.15  ? 638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 111.557 135.675 164.750 1.00 31.62  ? 639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.171 136.726 165.685 1.00 29.82  ? 639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.383 137.538 166.124 1.00 32.78  ? 639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.330 138.773 166.176 1.00 39.75  ? 639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 110.470 136.114 166.897 1.00 35.37  ? 639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 108.968 136.289 166.853 1.00 42.83  ? 639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.415 136.400 165.741 1.00 43.14  ? 639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 108.339 136.313 167.932 1.00 41.29  ? 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.490 136.858 166.426 1.00 30.31  ? 640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 114.718 137.550 166.811 1.00 30.36  ? 640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 115.218 138.460 165.697 1.00 32.74  ? 640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.567 139.622 165.937 1.00 35.54  ? 640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 115.795 136.535 167.186 1.00 29.56  ? 640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 117.153 137.161 167.437 1.00 29.09  ? 640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 117.206 138.155 168.932 1.00 29.28  ? 640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.191 137.099 169.982 1.00 34.32  ? 640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.260 137.948 164.467 1.00 28.19  ? 641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 115.809 138.731 163.366 1.00 20.56  ? 641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 114.902 139.913 163.048 1.00 21.88  ? 641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 115.378 141.011 162.737 1.00 30.23  ? 641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 116.046 137.838 162.136 1.00 26.30  ? 641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 117.067 136.748 162.463 1.00 27.27  ? 641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.547 138.660 160.963 1.00 25.90  ? 641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.235 137.230 163.294 1.00 28.59  ? 641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.583 139.717 163.131 1.00 19.27  ? 642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 112.655 140.821 162.920 1.00 24.15  ? 642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 112.769 141.862 164.022 1.00 30.29  ? 642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 112.572 143.055 163.769 1.00 30.39  ? 642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 111.224 140.295 162.828 1.00 25.74  ? 642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 113.070 141.431 165.249 1.00 26.28  ? 643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 113.361 142.384 166.313 1.00 24.32  ? 643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 114.624 143.177 166.003 1.00 34.28  ? 643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 114.680 144.390 166.237 1.00 38.40  ? 643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 113.497 141.650 167.646 1.00 23.86  ? 643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 112.297 140.911 167.907 1.00 37.52  ? 643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 113.722 142.633 168.769 1.00 26.60  ? 643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 115.652 142.506 165.483 1.00 25.87  ? 644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 116.871 143.202 165.085 1.00 15.14  ? 644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 116.628 144.054 163.845 1.00 22.83  ? 644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 117.128 145.181 163.743 1.00 26.98  ? 644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 118.012 142.195 164.856 1.00 19.36  ? 644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 118.268 141.373 166.116 1.00 20.32  ? 644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 119.276 142.910 164.423 1.00 20.03  ? 644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 119.117 140.154 165.869 1.00 27.16  ? 644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 115.860 143.531 162.886 1.00 17.65  ? 645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 115.727 144.190 161.590 1.00 17.56  ? 645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 115.054 145.551 161.703 1.00 25.85  ? 645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 115.328 146.446 160.895 1.00 30.70  ? 645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 114.949 143.293 160.626 1.00 20.10  ? 645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 114.782 143.867 159.232 1.00 19.48  ? 645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 116.005 143.647 158.368 1.00 25.77  ? 645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 116.226 142.551 157.855 1.00 27.67  ? 645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 116.810 144.689 158.207 1.00 18.89  ? 645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 114.180 145.734 162.695 1.00 32.89  ? 646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 113.492 147.012 162.838 1.00 28.86  ? 646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 114.445 148.147 163.186 1.00 24.93  ? 646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.075 149.316 163.038 1.00 29.06  ? 646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 112.395 146.904 163.897 1.00 29.75  ? 646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 112.903 146.859 165.322 1.00 30.35  ? 646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 111.831 146.446 166.307 1.00 34.33  ? 646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 111.930 145.401 166.949 1.00 36.21  ? 646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 110.795 147.266 166.431 1.00 32.19  ? 646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 115.660 147.835 163.632 1.00 27.51  ? 647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 116.669 148.841 163.926 1.00 16.75  ? 647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 117.798 148.858 162.909 1.00 21.75  ? 647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 118.774 149.591 163.100 1.00 33.43  ? 647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 117.239 148.621 165.329 1.00 21.44  ? 647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 116.198 148.582 166.402 1.00 22.98  ? 647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 115.297 149.606 166.600 1.00 20.68  ? 647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 115.910 147.642 167.333 1.00 23.00  ? 647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 114.501 149.299 167.607 1.00 24.22  ? 647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 114.851 148.114 168.070 1.00 23.79  ? 647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 117.696 148.074 161.842 1.00 22.46  ? 648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 118.699 148.025 160.786 1.00 20.93  ? 648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 118.051 148.558 159.516 1.00 22.87  ? 648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 117.025 148.031 159.068 1.00 28.07  ? 648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 119.236 146.600 160.582 1.00 9.95   ? 648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 119.784 146.042 161.898 1.00 19.00  ? 648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 120.314 146.580 159.520 1.00 15.48  ? 648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 120.960 146.812 162.448 1.00 17.86  ? 648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 118.641 149.608 158.939 1.00 16.32  ? 649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 118.057 150.207 157.744 1.00 16.24  ? 649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 118.242 149.319 156.520 1.00 22.51  ? 649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 117.370 149.286 155.645 1.00 38.41  ? 649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 118.659 151.590 157.497 1.00 25.14  ? 649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 120.165 151.600 157.620 1.00 24.97  ? 649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 120.712 150.687 158.269 1.00 28.24  ? 649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 120.801 152.520 157.071 1.00 25.83  ? 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 119.360 148.610 156.436 1.00 12.54  ? 650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 119.570 147.620 155.393 1.00 13.66  ? 650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 119.116 146.253 155.904 1.00 14.04  ? 650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 118.434 146.141 156.925 1.00 23.80  ? 650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 121.028 147.610 154.948 1.00 15.10  ? 650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 121.515 148.925 154.375 1.00 15.23  ? 650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 122.947 148.847 153.897 1.00 21.68  ? 650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 123.227 148.310 152.828 1.00 17.75  ? 650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 123.865 149.383 154.691 1.00 19.69  ? 650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 119.482 145.194 155.185 1.00 10.92  ? 651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 119.044 143.860 155.527 1.00 18.24  ? 651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 119.967 143.150 156.499 1.00 17.58  ? 651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 120.970 143.683 156.969 1.00 20.11  ? 651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 119.596 141.909 156.801 1.00 20.84  ? 652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 120.360 141.023 157.667 1.00 21.10  ? 652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 120.522 139.697 156.943 1.00 24.45  ? 652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 119.558 139.182 156.363 1.00 26.71  ? 652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 119.666 140.811 159.027 1.00 13.08  ? 652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 119.369 142.152 159.697 1.00 4.36   ? 652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.518 139.941 159.935 1.00 13.35  ? 652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 118.645 142.017 161.004 1.00 10.10  ? 652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 121.732 139.144 156.969 1.00 16.85  ? 653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 121.955 137.849 156.341 1.00 13.46  ? 653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.309 136.756 157.178 1.00 29.61  ? 653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 121.962 136.144 158.031 1.00 33.34  ? 653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 123.445 137.575 156.158 1.00 17.87  ? 653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 123.880 137.992 154.877 1.00 16.84  ? 653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 120.025 136.511 156.937 1.00 24.89  ? 654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.244 135.566 157.724 1.00 14.47  ? 654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.337 134.194 157.071 1.00 15.52  ? 654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 118.777 133.970 155.994 1.00 29.76  ? 654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 117.797 136.037 157.831 1.00 20.70  ? 654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 116.935 135.173 158.701 1.00 21.66  ? 654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 117.493 134.349 159.663 1.00 25.86  ? 654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 115.561 135.191 158.561 1.00 23.80  ? 654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 116.699 133.558 160.458 1.00 21.66  ? 654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 114.763 134.403 159.356 1.00 28.97  ? 654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 115.333 133.586 160.307 1.00 20.83  ? 654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.037 133.276 157.728 1.00 27.01  ? 655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 120.174 131.903 157.263 1.00 31.31  ? 655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 119.160 131.029 157.986 1.00 31.94  ? 655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 119.026 131.109 159.211 1.00 34.18  ? 655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 121.591 131.384 157.509 1.00 36.73  ? 655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 122.532 132.199 156.799 1.00 43.58  ? 655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 121.723 129.947 157.043 1.00 28.48  ? 655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 118.440 130.208 157.228 1.00 36.27  ? 656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 117.483 129.274 157.802 1.00 38.18  ? 656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 118.170 127.940 158.058 1.00 39.63  ? 656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 118.734 127.337 157.140 1.00 44.88  ? 656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 116.284 129.085 156.874 1.00 37.27  ? 656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 115.363 130.297 156.728 1.00 39.37  ? 656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 114.133 129.949 155.907 1.00 39.44  ? 656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 114.966 130.837 158.090 1.00 37.76  ? 656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 118.123 127.486 159.304 1.00 36.74  ? 657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 118.747 126.233 159.716 1.00 39.83  ? 657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 117.638 125.208 159.909 1.00 45.33  ? 657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 116.867 125.291 160.871 1.00 48.36  ? 657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 119.565 126.426 160.990 1.00 43.62  ? 657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 120.530 127.575 160.919 1.00 46.68  ? 657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 120.140 128.849 161.303 1.00 46.38  ? 657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.821 127.389 160.459 1.00 44.51  ? 657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 121.022 129.909 161.240 1.00 41.33  ? 657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.706 128.447 160.390 1.00 46.14  ? 657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 122.306 129.707 160.781 1.00 45.84  ? 657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 117.562 124.245 158.997 1.00 51.67  ? 658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 116.457 123.302 158.941 1.00 51.61  ? 658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 116.950 121.887 159.202 1.00 54.68  ? 658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 118.103 121.550 158.920 1.00 58.49  ? 658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 115.761 123.358 157.578 1.00 51.17  ? 658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 115.708 124.730 156.907 1.00 52.00  ? 658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 115.466 124.576 155.418 1.00 49.63  ? 658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 114.639 125.603 157.540 1.00 51.99  ? 658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 116.064 121.065 159.749 1.00 56.66  ? 659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 116.331 119.646 159.919 1.00 58.31  ? 659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 115.835 118.870 158.704 1.00 59.63  ? 659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 114.958 119.320 157.962 1.00 56.94  ? 659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 115.665 119.116 161.189 1.00 55.83  ? 659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 116.243 119.680 162.474 1.00 55.17  ? 659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 115.962 118.759 163.649 1.00 58.38  ? 659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 116.674 119.232 164.906 1.00 57.76  ? 659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 116.883 118.121 165.874 1.00 58.23  ? 659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 116.419 117.688 158.501 1.00 68.04  ? 660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 116.008 116.838 157.391 1.00 68.84  ? 660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 114.588 116.315 157.559 1.00 67.46  ? 660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 113.950 115.956 156.563 1.00 66.52  ? 660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 116.979 115.669 157.236 1.00 67.61  ? 660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 117.842 115.791 155.995 1.00 70.80  ? 660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.813 115.015 155.866 1.00 67.52  ? 660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 117.549 116.662 155.150 1.00 70.58  ? 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 114.081 116.260 158.793 1.00 65.45  ? 661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 112.722 115.781 159.017 1.00 65.46  ? 661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 111.682 116.739 158.452 1.00 64.85  ? 661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 110.635 116.296 157.967 1.00 63.02  ? 661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 112.478 115.564 160.511 1.00 65.56  ? 661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 112.767 116.771 161.225 1.00 63.46  ? 661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 113.364 114.444 161.036 1.00 64.20  ? 661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 111.943 118.042 158.507 1.00 63.92  ? 662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 110.971 119.015 158.031 1.00 63.27  ? 662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 110.870 118.981 156.508 1.00 63.42  ? 662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 111.848 118.725 155.799 1.00 60.98  ? 662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 111.333 120.419 158.520 1.00 60.18  ? 662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 112.014 121.310 157.498 1.00 62.42  ? 662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 112.160 123.011 158.078 1.00 76.44  ? 662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 112.800 122.752 159.730 1.00 58.97  ? 662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 109.658 119.223 156.012 1.00 57.15  ? 663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 109.366 119.132 154.588 1.00 55.16  ? 663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 109.511 120.485 153.903 1.00 53.83  ? 663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 109.999 121.445 154.508 1.00 54.97  ? 663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 107.952 118.589 154.375 1.00 52.97  ? 663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 107.009 119.659 154.504 1.00 54.02  ? 663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 107.637 117.518 155.406 1.00 54.47  ? 663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 109.090 120.572 152.640 1.00 47.97  ? 664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 109.053 121.837 151.919 1.00 48.18  ? 664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 107.935 122.741 152.414 1.00 44.43  ? 664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 108.050 123.967 152.312 1.00 48.70  ? 664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 108.904 121.602 150.415 1.00 47.73  ? 664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 107.622 121.024 150.142 1.00 48.18  ? 664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 109.996 120.674 149.906 1.00 49.99  ? 664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 106.858 122.170 152.950 1.00 45.23  ? 665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 105.816 122.963 153.586 1.00 46.39  ? 665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 106.301 123.672 154.838 1.00 50.39  ? 665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 105.901 124.813 155.079 1.00 52.11  ? 665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 104.611 122.087 153.944 1.00 46.31  ? 665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 103.334 122.875 154.183 1.00 43.86  ? 665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 102.391 122.134 155.111 1.00 46.19  ? 665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 102.852 122.161 156.494 1.00 49.59  ? 665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.086 122.465 157.532 1.00 50.50  ? 665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 100.809 122.776 157.382 1.00 47.06  ? 665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 102.614 122.454 158.754 1.00 49.59  ? 665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 107.152 123.029 155.640 1.00 47.65  ? 666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 107.739 123.710 156.789 1.00 44.11  ? 666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 108.632 124.863 156.346 1.00 47.74  ? 666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 108.616 125.938 156.958 1.00 50.87  ? 666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 108.521 122.714 157.643 1.00 48.36  ? 666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 107.619 121.730 158.361 1.00 52.85  ? 666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 106.516 122.132 158.784 1.00 50.92  ? 666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 108.013 120.553 158.502 1.00 52.21  ? 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 109.413 124.658 155.284 1.00 45.24  ? 667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 110.236 125.738 154.748 1.00 39.48  ? 667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 109.374 126.888 154.246 1.00 36.29  ? 667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 109.693 128.059 154.481 1.00 42.03  ? 667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 111.129 125.204 153.627 1.00 38.79  ? 667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 112.257 126.099 153.108 1.00 41.25  ? 667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 112.801 127.003 154.203 1.00 46.27  ? 667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.367 125.256 152.510 1.00 40.01  ? 667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 108.276 126.575 153.555 1.00 37.09  ? 668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 107.369 127.621 153.092 1.00 32.88  ? 668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 106.717 128.344 154.263 1.00 39.16  ? 668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 106.505 129.559 154.207 1.00 41.99  ? 668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 106.306 127.024 152.172 1.00 36.35  ? 668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 106.751 126.975 150.726 1.00 41.32  ? 668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.556 127.795 150.284 1.00 40.67  ? 668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 106.229 126.010 149.980 1.00 43.83  ? 668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 106.380 127.612 155.325 1.00 46.04  ? 669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 105.805 128.242 156.509 1.00 43.03  ? 669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 106.795 129.196 157.158 1.00 39.65  ? 669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 106.423 130.296 157.578 1.00 44.04  ? 669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 105.356 127.178 157.509 1.00 40.29  ? 669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 104.024 126.540 157.183 1.00 41.59  ? 669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 103.588 125.594 158.288 1.00 45.18  ? 669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 103.655 126.210 159.609 1.00 42.68  ? 669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 102.851 127.176 160.035 1.00 45.42  ? 669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 101.881 127.657 159.274 1.00 44.75  ? 669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.018 127.665 161.259 1.00 46.43  ? 669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 108.064 128.793 157.250 1.00 32.51  ? 670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 109.082 129.685 157.796 1.00 35.10  ? 670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 109.257 130.906 156.902 1.00 37.37  ? 670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 109.395 132.035 157.390 1.00 39.60  ? 670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 110.409 128.933 158.000 1.00 36.53  ? 670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 110.219 127.762 158.963 1.00 41.25  ? 670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 111.473 129.872 158.531 1.00 33.94  ? 670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 111.278 126.690 158.837 1.00 37.95  ? 670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 109.247 130.705 155.581 1.00 36.51  ? 671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 109.374 131.825 154.653 1.00 28.58  ? 671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.225 132.811 154.817 1.00 33.43  ? 671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.436 134.029 154.861 1.00 40.05  ? 671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 109.418 131.304 153.216 1.00 34.18  ? 671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 110.805 130.871 152.789 1.00 44.05  ? 671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 111.778 131.193 153.500 1.00 43.50  ? 671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 110.923 130.205 151.739 1.00 41.76  ? 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 106.996 132.300 154.920 1.00 34.25  ? 672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 105.833 133.168 155.044 1.00 33.15  ? 672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 105.776 133.842 156.407 1.00 33.88  ? 672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.304 134.976 156.513 1.00 40.07  ? 672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 104.555 132.373 154.788 1.00 37.28  ? 672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 104.391 131.825 153.371 1.00 34.22  ? 672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 103.340 130.729 153.341 1.00 35.71  ? 672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.040 132.940 152.401 1.00 30.47  ? 672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.234 133.160 157.460 1.00 32.12  ? 673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.318 133.796 158.769 1.00 29.39  ? 673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.353 134.912 158.763 1.00 31.87  ? 673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.136 135.970 159.363 1.00 35.27  ? 673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 106.644 132.753 159.836 1.00 27.00  ? 673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 106.660 133.296 161.244 1.00 31.23  ? 673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 105.498 133.761 161.841 1.00 28.79  ? 673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 107.834 133.333 161.981 1.00 32.24  ? 673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 105.505 134.256 163.128 1.00 27.23  ? 673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 107.852 133.828 163.268 1.00 36.17  ? 673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 106.686 134.287 163.837 1.00 34.25  ? 673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 106.701 134.779 165.122 1.00 34.87  ? 673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.484 134.691 158.088 1.00 32.98  ? 674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.476 135.747 157.936 1.00 27.01  ? 674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 108.901 136.934 157.178 1.00 27.11  ? 674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 109.105 138.089 157.568 1.00 34.94  ? 674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 110.713 135.200 157.223 1.00 23.05  ? 674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 108.168 136.668 156.095 1.00 31.36  ? 675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.530 137.750 155.352 1.00 31.71  ? 675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.523 138.499 156.219 1.00 34.07  ? 675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 106.442 139.731 156.169 1.00 35.54  ? 675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 106.853 137.195 154.100 1.00 34.33  ? 675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 105.984 138.187 153.394 1.00 37.13  ? 675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.628 138.281 153.617 1.00 34.21  ? 675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 106.279 139.133 152.470 1.00 25.53  ? 675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 104.124 139.240 152.862 1.00 35.18  ? 675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 105.105 139.772 152.156 1.00 32.67  ? 675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 105.748 137.767 157.022 1.00 35.02  ? 676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 104.731 138.392 157.861 1.00 36.48  ? 676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 105.346 139.178 159.012 1.00 36.00  ? 676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 104.799 140.210 159.416 1.00 36.80  ? 676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 103.771 137.324 158.389 1.00 35.82  ? 676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.114 137.683 159.685 1.00 37.20  ? 676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.523 137.167 160.895 1.00 38.76  ? 676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 102.071 138.502 159.959 1.00 35.72  ? 676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.764 137.654 161.860 1.00 39.10  ? 676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 101.875 138.468 161.319 1.00 40.68  ? 676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.478 138.718 159.543 1.00 35.43  ? 677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 107.122 139.380 160.670 1.00 30.74  ? 677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 107.990 140.560 160.255 1.00 36.85  ? 677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 108.560 141.222 161.128 1.00 41.35  ? 677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 107.964 138.376 161.459 1.00 29.95  ? 677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.144 137.375 162.249 1.00 36.62  ? 677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 106.673 137.966 163.564 1.00 34.40  ? 677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 107.787 138.429 164.383 1.00 40.81  ? 677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 107.952 139.682 164.786 1.00 44.10  ? 677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 107.090 140.631 164.460 1.00 42.55  ? 677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 109.008 139.990 165.533 1.00 38.31  ? 677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 108.103 140.839 158.962 1.00 30.66  ? 678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 108.888 141.961 158.496 1.00 21.92  ? 678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 110.311 141.640 158.103 1.00 24.62  ? 678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 111.109 142.568 157.929 1.00 25.15  ? 678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 110.660 140.359 157.965 1.00 24.16  ? 679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.002 140.000 157.528 1.00 17.59  ? 679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 112.207 140.491 156.105 1.00 19.89  ? 679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 111.350 140.301 155.234 1.00 36.54  ? 679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 112.214 138.484 157.637 1.00 19.15  ? 679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 112.068 138.029 159.090 1.00 22.87  ? 679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.575 138.092 157.092 1.00 23.22  ? 679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 113.082 138.626 160.015 1.00 22.20  ? 679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 113.345 141.139 155.866 1.00 21.33  ? 680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 113.598 141.730 154.558 1.00 21.37  ? 680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 114.164 140.707 153.580 1.00 14.81  ? 680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 113.684 140.591 152.448 1.00 25.08  ? 680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 114.547 142.918 154.702 1.00 12.79  ? 680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 113.926 144.133 155.364 1.00 6.90   ? 680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 114.906 145.286 155.425 1.00 13.83  ? 680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 114.378 146.412 156.290 1.00 19.68  ? 680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 115.228 147.626 156.202 1.00 14.68  ? 680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 115.183 139.962 153.997 1.00 20.66  ? 681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 115.838 138.993 153.133 1.00 16.71  ? 681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 116.085 137.706 153.904 1.00 23.14  ? 681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 116.222 137.714 155.129 1.00 29.15  ? 681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 117.174 139.521 152.584 1.00 17.61  ? 681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 117.992 139.981 153.669 1.00 33.22  ? 681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 116.949 140.662 151.612 1.00 16.21  ? 681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.142 136.599 153.168 1.00 19.76  ? 682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.504 135.296 153.712 1.00 18.69  ? 682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.698 134.775 152.930 1.00 23.44  ? 682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.646 134.682 151.698 1.00 28.73  ? 682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.328 134.306 153.653 1.00 17.53  ? 682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.059 134.965 154.195 1.00 27.40  ? 682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 115.657 133.052 154.433 1.00 26.43  ? 682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 112.852 134.071 154.178 1.00 28.49  ? 682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 118.773 134.441 153.642 1.00 22.41  ? 683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.035 134.134 152.978 1.00 18.41  ? 683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.082 132.688 152.496 1.00 31.28  ? 683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.124 132.426 151.291 1.00 39.09  ? 683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.202 134.423 153.928 1.00 23.37  ? 683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.573 134.280 153.307 1.00 15.58  ? 683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.755 134.395 151.936 1.00 20.27  ? 683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.689 134.042 154.096 1.00 14.84  ? 683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.005 134.269 151.369 1.00 26.19  ? 683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 124.943 133.915 153.537 1.00 27.31  ? 683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.095 134.030 152.173 1.00 28.40  ? 683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.344 133.904 151.611 1.00 30.17  ? 683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.051 131.733 153.418 1.00 37.47  ? 684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 120.316 130.349 153.069 1.00 31.19  ? 684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 119.360 129.438 153.822 1.00 45.03  ? 684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 118.801 129.806 154.857 1.00 46.41  ? 684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 121.766 129.959 153.383 1.00 32.08  ? 684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 122.692 130.013 152.191 1.00 33.02  ? 684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 122.329 129.452 150.977 1.00 35.87  ? 684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 123.934 130.625 152.284 1.00 40.39  ? 684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 123.175 129.499 149.886 1.00 40.43  ? 684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 124.787 130.679 151.199 1.00 40.19  ? 684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 124.402 130.114 150.002 1.00 44.40  ? 684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 125.250 130.165 148.920 1.00 42.90  ? 684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 119.178 128.239 153.278 1.00 42.86  ? 685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 118.406 127.178 153.914 1.00 40.23  ? 685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 119.363 126.015 154.145 1.00 44.87  ? 685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 119.535 125.155 153.278 1.00 52.90  ? 685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 117.211 126.772 153.062 1.00 43.16  ? 685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 119.990 125.994 155.317 1.00 44.64  ? 686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 120.949 124.956 155.669 1.00 48.91  ? 686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 120.208 123.765 156.261 1.00 55.19  ? 686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 119.398 123.926 157.181 1.00 53.63  ? 686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 121.986 125.490 156.656 1.00 49.33  ? 686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 122.850 126.606 156.102 1.00 53.05  ? 686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 124.100 126.800 156.941 1.00 51.90  ? 686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 124.727 125.532 157.289 1.00 53.80  ? 686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 125.787 125.028 156.671 1.00 53.73  ? 686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 126.368 125.662 155.666 1.00 51.26  ? 686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 126.276 123.858 157.073 1.00 51.31  ? 686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 120.481 122.576 155.734 1.00 61.39  ? 687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 119.852 121.350 156.197 1.00 63.57  ? 687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 120.878 120.475 156.904 1.00 63.60  ? 687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 122.019 120.346 156.450 1.00 64.08  ? 687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 119.222 120.582 155.033 1.00 64.68  ? 687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.146 120.526 153.940 1.00 65.49  ? 687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 117.943 121.265 154.574 1.00 62.76  ? 687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 120.464 119.876 158.015 1.00 62.91  ? 688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 121.345 119.013 158.792 1.00 66.50  ? 688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 120.972 117.545 158.612 1.00 67.25  ? 688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 119.821 117.158 158.818 1.00 66.50  ? 688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 121.296 119.391 160.274 1.00 60.52  ? 688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 122.249 118.596 161.147 1.00 61.00  ? 688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 122.171 119.040 162.597 1.00 62.97  ? 688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 123.159 118.275 163.460 1.00 64.34  ? 688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 123.104 118.710 164.883 1.00 64.82  ? 688 LYS B NZ    1 
ATOM   11109 N  N     . THR C 2 332 ? 145.461 106.756 110.170 1.00 29.81  ? 311 THR C N     1 
ATOM   11110 C  CA    . THR C 2 332 ? 146.126 106.349 111.401 1.00 29.93  ? 311 THR C CA    1 
ATOM   11111 C  C     . THR C 2 332 ? 146.770 107.541 112.101 1.00 29.61  ? 311 THR C C     1 
ATOM   11112 O  O     . THR C 2 332 ? 146.323 108.675 111.946 1.00 37.54  ? 311 THR C O     1 
ATOM   11113 C  CB    . THR C 2 332 ? 147.201 105.280 111.137 1.00 35.93  ? 311 THR C CB    1 
ATOM   11114 O  OG1   . THR C 2 332 ? 148.436 105.917 110.785 1.00 42.31  ? 311 THR C OG1   1 
ATOM   11115 C  CG2   . THR C 2 332 ? 146.771 104.358 110.008 1.00 32.23  ? 311 THR C CG2   1 
ATOM   11116 N  N     . VAL C 2 333 ? 147.815 107.270 112.880 1.00 26.16  ? 312 VAL C N     1 
ATOM   11117 C  CA    . VAL C 2 333 ? 148.505 108.294 113.657 1.00 21.22  ? 312 VAL C CA    1 
ATOM   11118 C  C     . VAL C 2 333 ? 149.973 108.204 113.222 1.00 25.73  ? 312 VAL C C     1 
ATOM   11119 O  O     . VAL C 2 333 ? 150.909 108.432 113.996 1.00 29.77  ? 312 VAL C O     1 
ATOM   11120 C  CB    . VAL C 2 333 ? 148.207 108.086 115.168 1.00 22.98  ? 312 VAL C CB    1 
ATOM   11121 C  CG1   . VAL C 2 333 ? 149.280 108.584 116.144 1.00 26.04  ? 312 VAL C CG1   1 
ATOM   11122 C  CG2   . VAL C 2 333 ? 146.857 108.704 115.519 1.00 25.62  ? 312 VAL C CG2   1 
ATOM   11123 N  N     . GLU C 2 334 ? 150.175 107.880 111.946 1.00 25.38  ? 313 GLU C N     1 
ATOM   11124 C  CA    . GLU C 2 334 ? 151.518 107.660 111.422 1.00 29.10  ? 313 GLU C CA    1 
ATOM   11125 C  C     . GLU C 2 334 ? 152.407 108.875 111.679 1.00 31.44  ? 313 GLU C C     1 
ATOM   11126 O  O     . GLU C 2 334 ? 152.059 109.997 111.290 1.00 31.58  ? 313 GLU C O     1 
ATOM   11127 C  CB    . GLU C 2 334 ? 151.460 107.370 109.922 1.00 30.13  ? 313 GLU C CB    1 
ATOM   11128 C  CG    . GLU C 2 334 ? 152.768 106.879 109.327 1.00 30.08  ? 313 GLU C CG    1 
ATOM   11129 C  CD    . GLU C 2 334 ? 152.640 106.516 107.861 1.00 34.97  ? 313 GLU C CD    1 
ATOM   11130 O  OE1   . GLU C 2 334 ? 151.507 106.549 107.336 1.00 29.34  ? 313 GLU C OE1   1 
ATOM   11131 O  OE2   . GLU C 2 334 ? 153.672 106.201 107.232 1.00 31.58  ? 313 GLU C OE2   1 
ATOM   11132 N  N     . PRO C 2 335 ? 153.553 108.691 112.332 1.00 24.98  ? 314 PRO C N     1 
ATOM   11133 C  CA    . PRO C 2 335 ? 154.438 109.826 112.622 1.00 29.75  ? 314 PRO C CA    1 
ATOM   11134 C  C     . PRO C 2 335 ? 155.169 110.320 111.385 1.00 28.75  ? 314 PRO C C     1 
ATOM   11135 O  O     . PRO C 2 335 ? 155.307 109.607 110.387 1.00 32.13  ? 314 PRO C O     1 
ATOM   11136 C  CB    . PRO C 2 335 ? 155.424 109.248 113.648 1.00 23.64  ? 314 PRO C CB    1 
ATOM   11137 C  CG    . PRO C 2 335 ? 154.740 108.027 114.194 1.00 23.36  ? 314 PRO C CG    1 
ATOM   11138 C  CD    . PRO C 2 335 ? 153.998 107.471 113.021 1.00 25.64  ? 314 PRO C CD    1 
ATOM   11139 N  N     . LEU C 2 336 ? 155.639 111.562 111.461 1.00 22.20  ? 315 LEU C N     1 
ATOM   11140 C  CA    . LEU C 2 336 ? 156.442 112.138 110.394 1.00 20.58  ? 315 LEU C CA    1 
ATOM   11141 C  C     . LEU C 2 336 ? 157.872 111.612 110.443 1.00 24.93  ? 315 LEU C C     1 
ATOM   11142 O  O     . LEU C 2 336 ? 158.392 111.254 111.503 1.00 24.32  ? 315 LEU C O     1 
ATOM   11143 C  CB    . LEU C 2 336 ? 156.460 113.663 110.500 1.00 19.66  ? 315 LEU C CB    1 
ATOM   11144 C  CG    . LEU C 2 336 ? 155.229 114.439 110.037 1.00 20.82  ? 315 LEU C CG    1 
ATOM   11145 C  CD1   . LEU C 2 336 ? 155.116 115.742 110.808 1.00 21.77  ? 315 LEU C CD1   1 
ATOM   11146 C  CD2   . LEU C 2 336 ? 155.307 114.704 108.548 1.00 18.31  ? 315 LEU C CD2   1 
ATOM   11147 N  N     . LYS C 2 337 ? 158.510 111.574 109.278 1.00 26.00  ? 316 LYS C N     1 
ATOM   11148 C  CA    . LYS C 2 337 ? 159.930 111.276 109.166 1.00 23.07  ? 316 LYS C CA    1 
ATOM   11149 C  C     . LYS C 2 337 ? 160.642 112.456 108.516 1.00 26.80  ? 316 LYS C C     1 
ATOM   11150 O  O     . LYS C 2 337 ? 160.023 113.446 108.120 1.00 26.38  ? 316 LYS C O     1 
ATOM   11151 C  CB    . LYS C 2 337 ? 160.178 109.987 108.369 1.00 23.23  ? 316 LYS C CB    1 
ATOM   11152 C  CG    . LYS C 2 337 ? 159.295 109.812 107.145 1.00 24.82  ? 316 LYS C CG    1 
ATOM   11153 C  CD    . LYS C 2 337 ? 159.399 108.403 106.580 1.00 20.69  ? 316 LYS C CD    1 
ATOM   11154 C  CE    . LYS C 2 337 ? 159.216 107.350 107.661 1.00 24.72  ? 316 LYS C CE    1 
ATOM   11155 N  NZ    . LYS C 2 337 ? 157.931 107.516 108.395 1.00 24.81  ? 316 LYS C NZ    1 
ATOM   11156 N  N     . ASP C 2 338 ? 161.967 112.344 108.419 1.00 23.93  ? 317 ASP C N     1 
ATOM   11157 C  CA    . ASP C 2 338 ? 162.779 113.433 107.891 1.00 19.78  ? 317 ASP C CA    1 
ATOM   11158 C  C     . ASP C 2 338 ? 162.520 113.717 106.417 1.00 21.25  ? 317 ASP C C     1 
ATOM   11159 O  O     . ASP C 2 338 ? 162.869 114.805 105.947 1.00 13.62  ? 317 ASP C O     1 
ATOM   11160 C  CB    . ASP C 2 338 ? 164.263 113.130 108.103 1.00 24.09  ? 317 ASP C CB    1 
ATOM   11161 C  CG    . ASP C 2 338 ? 164.765 113.589 109.458 1.00 26.41  ? 317 ASP C CG    1 
ATOM   11162 O  OD1   . ASP C 2 338 ? 165.100 114.785 109.594 1.00 25.77  ? 317 ASP C OD1   1 
ATOM   11163 O  OD2   . ASP C 2 338 ? 164.822 112.756 110.388 1.00 24.73  ? 317 ASP C OD2   1 
ATOM   11164 N  N     . ASP C 2 339 ? 161.921 112.782 105.680 1.00 26.19  ? 318 ASP C N     1 
ATOM   11165 C  CA    . ASP C 2 339 ? 161.726 112.947 104.247 1.00 17.33  ? 318 ASP C CA    1 
ATOM   11166 C  C     . ASP C 2 339 ? 160.395 113.591 103.881 1.00 19.67  ? 318 ASP C C     1 
ATOM   11167 O  O     . ASP C 2 339 ? 160.156 113.839 102.694 1.00 24.94  ? 318 ASP C O     1 
ATOM   11168 C  CB    . ASP C 2 339 ? 161.844 111.593 103.536 1.00 20.90  ? 318 ASP C CB    1 
ATOM   11169 C  CG    . ASP C 2 339 ? 163.154 111.443 102.787 1.00 25.28  ? 318 ASP C CG    1 
ATOM   11170 O  OD1   . ASP C 2 339 ? 163.169 110.759 101.742 1.00 27.27  ? 318 ASP C OD1   1 
ATOM   11171 O  OD2   . ASP C 2 339 ? 164.169 112.011 103.241 1.00 26.46  ? 318 ASP C OD2   1 
ATOM   11172 N  N     . ASP C 2 340 ? 159.528 113.869 104.854 1.00 15.21  ? 319 ASP C N     1 
ATOM   11173 C  CA    . ASP C 2 340 ? 158.291 114.585 104.563 1.00 12.08  ? 319 ASP C CA    1 
ATOM   11174 C  C     . ASP C 2 340 ? 158.465 116.095 104.592 1.00 12.59  ? 319 ASP C C     1 
ATOM   11175 O  O     . ASP C 2 340 ? 157.509 116.818 104.294 1.00 22.52  ? 319 ASP C O     1 
ATOM   11176 C  CB    . ASP C 2 340 ? 157.190 114.188 105.549 1.00 12.56  ? 319 ASP C CB    1 
ATOM   11177 C  CG    . ASP C 2 340 ? 157.248 112.729 105.941 1.00 22.56  ? 319 ASP C CG    1 
ATOM   11178 O  OD1   . ASP C 2 340 ? 156.879 111.870 105.113 1.00 22.79  ? 319 ASP C OD1   1 
ATOM   11179 O  OD2   . ASP C 2 340 ? 157.640 112.444 107.089 1.00 23.49  ? 319 ASP C OD2   1 
ATOM   11180 N  N     . PHE C 2 341 ? 159.652 116.587 104.946 1.00 9.55   ? 320 PHE C N     1 
ATOM   11181 C  CA    . PHE C 2 341 ? 159.910 118.019 105.026 1.00 13.62  ? 320 PHE C CA    1 
ATOM   11182 C  C     . PHE C 2 341 ? 160.658 118.541 103.807 1.00 16.13  ? 320 PHE C C     1 
ATOM   11183 O  O     . PHE C 2 341 ? 160.967 119.737 103.746 1.00 15.03  ? 320 PHE C O     1 
ATOM   11184 C  CB    . PHE C 2 341 ? 160.687 118.338 106.304 1.00 6.93   ? 320 PHE C CB    1 
ATOM   11185 C  CG    . PHE C 2 341 ? 159.882 118.153 107.558 1.00 0.01   ? 320 PHE C CG    1 
ATOM   11186 C  CD1   . PHE C 2 341 ? 159.103 119.180 108.058 1.00 8.08   ? 320 PHE C CD1   1 
ATOM   11187 C  CD2   . PHE C 2 341 ? 159.894 116.942 108.227 1.00 8.21   ? 320 PHE C CD2   1 
ATOM   11188 C  CE1   . PHE C 2 341 ? 158.360 119.008 109.209 1.00 8.05   ? 320 PHE C CE1   1 
ATOM   11189 C  CE2   . PHE C 2 341 ? 159.150 116.762 109.376 1.00 13.50  ? 320 PHE C CE2   1 
ATOM   11190 C  CZ    . PHE C 2 341 ? 158.383 117.797 109.867 1.00 10.00  ? 320 PHE C CZ    1 
ATOM   11191 N  N     . TYR C 2 342 ? 160.954 117.679 102.837 1.00 14.67  ? 321 TYR C N     1 
ATOM   11192 C  CA    . TYR C 2 342 ? 161.567 118.084 101.582 1.00 16.49  ? 321 TYR C CA    1 
ATOM   11193 C  C     . TYR C 2 342 ? 160.739 117.529 100.435 1.00 17.43  ? 321 TYR C C     1 
ATOM   11194 O  O     . TYR C 2 342 ? 160.303 116.376 100.475 1.00 18.36  ? 321 TYR C O     1 
ATOM   11195 C  CB    . TYR C 2 342 ? 163.017 117.594 101.471 1.00 14.04  ? 321 TYR C CB    1 
ATOM   11196 C  CG    . TYR C 2 342 ? 163.849 117.838 102.710 1.00 13.14  ? 321 TYR C CG    1 
ATOM   11197 C  CD1   . TYR C 2 342 ? 164.462 119.066 102.928 1.00 18.54  ? 321 TYR C CD1   1 
ATOM   11198 C  CD2   . TYR C 2 342 ? 164.024 116.841 103.661 1.00 12.64  ? 321 TYR C CD2   1 
ATOM   11199 C  CE1   . TYR C 2 342 ? 165.224 119.294 104.056 1.00 19.00  ? 321 TYR C CE1   1 
ATOM   11200 C  CE2   . TYR C 2 342 ? 164.785 117.061 104.793 1.00 18.18  ? 321 TYR C CE2   1 
ATOM   11201 C  CZ    . TYR C 2 342 ? 165.382 118.289 104.985 1.00 18.87  ? 321 TYR C CZ    1 
ATOM   11202 O  OH    . TYR C 2 342 ? 166.140 118.510 106.113 1.00 19.85  ? 321 TYR C OH    1 
ATOM   11203 N  N     . PHE C 2 343 ? 160.524 118.356 99.417  1.00 17.75  ? 322 PHE C N     1 
ATOM   11204 C  CA    . PHE C 2 343 ? 159.702 117.963 98.281  1.00 21.55  ? 322 PHE C CA    1 
ATOM   11205 C  C     . PHE C 2 343 ? 160.438 118.191 96.966  1.00 24.96  ? 322 PHE C C     1 
ATOM   11206 O  O     . PHE C 2 343 ? 161.293 119.070 96.863  1.00 18.59  ? 322 PHE C O     1 
ATOM   11207 C  CB    . PHE C 2 343 ? 158.381 118.736 98.289  1.00 23.80  ? 322 PHE C CB    1 
ATOM   11208 C  CG    . PHE C 2 343 ? 157.568 118.534 99.535  1.00 14.87  ? 322 PHE C CG    1 
ATOM   11209 C  CD1   . PHE C 2 343 ? 156.699 117.463 99.645  1.00 19.68  ? 322 PHE C CD1   1 
ATOM   11210 C  CD2   . PHE C 2 343 ? 157.675 119.416 100.599 1.00 11.74  ? 322 PHE C CD2   1 
ATOM   11211 C  CE1   . PHE C 2 343 ? 155.950 117.275 100.791 1.00 17.81  ? 322 PHE C CE1   1 
ATOM   11212 C  CE2   . PHE C 2 343 ? 156.930 119.232 101.746 1.00 12.99  ? 322 PHE C CE2   1 
ATOM   11213 C  CZ    . PHE C 2 343 ? 156.065 118.161 101.843 1.00 15.33  ? 322 PHE C CZ    1 
ATOM   11214 N  N     . THR D 2 332 ? 111.431 116.484 150.688 1.00 32.51  ? 311 THR D N     1 
ATOM   11215 C  CA    . THR D 2 332 ? 110.071 116.022 150.939 1.00 32.98  ? 311 THR D CA    1 
ATOM   11216 C  C     . THR D 2 332 ? 109.055 117.096 150.571 1.00 28.33  ? 311 THR D C     1 
ATOM   11217 O  O     . THR D 2 332 ? 108.778 117.995 151.360 1.00 34.06  ? 311 THR D O     1 
ATOM   11218 C  CB    . THR D 2 332 ? 109.862 115.634 152.416 1.00 32.80  ? 311 THR D CB    1 
ATOM   11219 O  OG1   . THR D 2 332 ? 111.033 114.979 152.914 1.00 35.39  ? 311 THR D OG1   1 
ATOM   11220 C  CG2   . THR D 2 332 ? 108.678 114.687 152.549 1.00 27.32  ? 311 THR D CG2   1 
ATOM   11221 N  N     . VAL D 2 333 ? 108.501 116.993 149.363 1.00 21.04  ? 312 VAL D N     1 
ATOM   11222 C  CA    . VAL D 2 333 ? 107.534 117.981 148.899 1.00 23.06  ? 312 VAL D CA    1 
ATOM   11223 C  C     . VAL D 2 333 ? 106.203 117.771 149.601 1.00 24.35  ? 312 VAL D C     1 
ATOM   11224 O  O     . VAL D 2 333 ? 105.572 116.718 149.471 1.00 27.51  ? 312 VAL D O     1 
ATOM   11225 C  CB    . VAL D 2 333 ? 107.381 117.906 147.368 1.00 21.66  ? 312 VAL D CB    1 
ATOM   11226 C  CG1   . VAL D 2 333 ? 106.387 118.950 146.873 1.00 19.37  ? 312 VAL D CG1   1 
ATOM   11227 C  CG2   . VAL D 2 333 ? 108.741 118.078 146.696 1.00 24.14  ? 312 VAL D CG2   1 
ATOM   11228 N  N     . GLU D 2 334 ? 105.776 118.781 150.356 1.00 22.97  ? 313 GLU D N     1 
ATOM   11229 C  CA    . GLU D 2 334 ? 104.476 118.782 151.017 1.00 25.24  ? 313 GLU D CA    1 
ATOM   11230 C  C     . GLU D 2 334 ? 103.736 120.026 150.542 1.00 26.98  ? 313 GLU D C     1 
ATOM   11231 O  O     . GLU D 2 334 ? 104.249 121.152 150.715 1.00 30.39  ? 313 GLU D O     1 
ATOM   11232 C  CB    . GLU D 2 334 ? 104.636 118.753 152.541 1.00 25.19  ? 313 GLU D CB    1 
ATOM   11233 C  CG    . GLU D 2 334 ? 103.416 118.246 153.285 1.00 25.82  ? 313 GLU D CG    1 
ATOM   11234 C  CD    . GLU D 2 334 ? 103.358 118.743 154.718 1.00 23.31  ? 313 GLU D CD    1 
ATOM   11235 O  OE1   . GLU D 2 334 ? 104.428 118.988 155.306 1.00 22.88  ? 313 GLU D OE1   1 
ATOM   11236 O  OE2   . GLU D 2 334 ? 102.238 118.883 155.257 1.00 23.92  ? 313 GLU D OE2   1 
ATOM   11237 N  N     . PRO D 2 335 ? 102.544 119.893 149.958 1.00 13.93  ? 314 PRO D N     1 
ATOM   11238 C  CA    . PRO D 2 335 ? 101.888 121.054 149.348 1.00 25.32  ? 314 PRO D CA    1 
ATOM   11239 C  C     . PRO D 2 335 ? 101.374 122.030 150.396 1.00 22.50  ? 314 PRO D C     1 
ATOM   11240 O  O     . PRO D 2 335 ? 100.915 121.635 151.470 1.00 23.90  ? 314 PRO D O     1 
ATOM   11241 C  CB    . PRO D 2 335 ? 100.731 120.419 148.546 1.00 20.68  ? 314 PRO D CB    1 
ATOM   11242 C  CG    . PRO D 2 335 ? 101.035 118.875 148.625 1.00 23.47  ? 314 PRO D CG    1 
ATOM   11243 C  CD    . PRO D 2 335 ? 101.553 118.823 150.023 1.00 23.46  ? 314 PRO D CD    1 
ATOM   11244 N  N     . LEU D 2 336 ? 101.467 123.319 150.079 1.00 14.61  ? 315 LEU D N     1 
ATOM   11245 C  CA    . LEU D 2 336 ? 100.870 124.344 150.923 1.00 10.57  ? 315 LEU D CA    1 
ATOM   11246 C  C     . LEU D 2 336 ? 99.357  124.169 150.947 1.00 14.80  ? 315 LEU D C     1 
ATOM   11247 O  O     . LEU D 2 336 ? 98.697  124.170 149.902 1.00 26.75  ? 315 LEU D O     1 
ATOM   11248 C  CB    . LEU D 2 336 ? 101.241 125.738 150.412 1.00 14.40  ? 315 LEU D CB    1 
ATOM   11249 C  CG    . LEU D 2 336 ? 102.536 126.332 150.964 1.00 12.28  ? 315 LEU D CG    1 
ATOM   11250 C  CD1   . LEU D 2 336 ? 102.882 127.635 150.264 1.00 10.98  ? 315 LEU D CD1   1 
ATOM   11251 C  CD2   . LEU D 2 336 ? 102.457 126.529 152.463 1.00 14.92  ? 315 LEU D CD2   1 
ATOM   11252 N  N     . LYS D 2 337 ? 98.807  124.021 152.150 1.00 13.54  ? 316 LYS D N     1 
ATOM   11253 C  CA    . LYS D 2 337 ? 97.416  123.627 152.345 1.00 30.01  ? 316 LYS D CA    1 
ATOM   11254 C  C     . LYS D 2 337 ? 96.565  124.772 152.885 1.00 25.79  ? 316 LYS D C     1 
ATOM   11255 O  O     . LYS D 2 337 ? 95.480  124.544 153.426 1.00 33.47  ? 316 LYS D O     1 
ATOM   11256 C  CB    . LYS D 2 337 ? 97.342  122.413 153.272 1.00 28.27  ? 316 LYS D CB    1 
ATOM   11257 C  CG    . LYS D 2 337 ? 97.553  122.736 154.749 1.00 24.51  ? 316 LYS D CG    1 
ATOM   11258 C  CD    . LYS D 2 337 ? 97.723  121.478 155.592 1.00 27.44  ? 316 LYS D CD    1 
ATOM   11259 C  CE    . LYS D 2 337 ? 97.009  120.278 154.985 1.00 29.88  ? 316 LYS D CE    1 
ATOM   11260 N  NZ    . LYS D 2 337 ? 97.294  119.028 155.744 1.00 29.09  ? 316 LYS D NZ    1 
ATOM   11261 N  N     . ASP D 2 338 ? 97.043  126.010 152.729 1.00 13.62  ? 317 ASP D N     1 
ATOM   11262 C  CA    . ASP D 2 338 ? 96.445  127.190 153.350 1.00 23.84  ? 317 ASP D CA    1 
ATOM   11263 C  C     . ASP D 2 338 ? 96.506  127.068 154.869 1.00 29.46  ? 317 ASP D C     1 
ATOM   11264 O  O     . ASP D 2 338 ? 96.925  126.031 155.395 1.00 33.27  ? 317 ASP D O     1 
ATOM   11265 C  CB    . ASP D 2 338 ? 95.005  127.403 152.869 1.00 26.92  ? 317 ASP D CB    1 
ATOM   11266 C  CG    . ASP D 2 338 ? 94.506  128.809 153.126 1.00 26.65  ? 317 ASP D CG    1 
ATOM   11267 O  OD1   . ASP D 2 338 ? 95.306  129.655 153.577 1.00 23.79  ? 317 ASP D OD1   1 
ATOM   11268 O  OD2   . ASP D 2 338 ? 93.311  129.069 152.871 1.00 27.60  ? 317 ASP D OD2   1 
ATOM   11269 N  N     . ASP D 2 339 ? 96.143  128.143 155.580 1.00 23.80  ? 318 ASP D N     1 
ATOM   11270 C  CA    . ASP D 2 339 ? 96.285  128.257 157.031 1.00 22.70  ? 318 ASP D CA    1 
ATOM   11271 C  C     . ASP D 2 339 ? 97.769  128.335 157.389 1.00 23.02  ? 318 ASP D C     1 
ATOM   11272 O  O     . ASP D 2 339 ? 98.134  128.564 158.547 1.00 26.98  ? 318 ASP D O     1 
ATOM   11273 C  CB    . ASP D 2 339 ? 95.577  127.095 157.748 1.00 24.00  ? 318 ASP D CB    1 
ATOM   11274 C  CG    . ASP D 2 339 ? 95.817  127.087 159.246 1.00 30.89  ? 318 ASP D CG    1 
ATOM   11275 O  OD1   . ASP D 2 339 ? 95.672  128.155 159.876 1.00 33.02  ? 318 ASP D OD1   1 
ATOM   11276 O  OD2   . ASP D 2 339 ? 96.155  126.014 159.789 1.00 30.00  ? 318 ASP D OD2   1 
ATOM   11277 N  N     . ASP D 2 340 ? 98.632  128.186 156.384 1.00 14.41  ? 319 ASP D N     1 
ATOM   11278 C  CA    . ASP D 2 340 ? 100.059 128.425 156.525 1.00 13.17  ? 319 ASP D CA    1 
ATOM   11279 C  C     . ASP D 2 340 ? 100.447 129.846 156.148 1.00 13.84  ? 319 ASP D C     1 
ATOM   11280 O  O     . ASP D 2 340 ? 101.573 130.264 156.433 1.00 19.23  ? 319 ASP D O     1 
ATOM   11281 C  CB    . ASP D 2 340 ? 100.852 127.433 155.665 1.00 10.03  ? 319 ASP D CB    1 
ATOM   11282 C  CG    . ASP D 2 340 ? 100.453 125.995 155.920 1.00 22.05  ? 319 ASP D CG    1 
ATOM   11283 O  OD1   . ASP D 2 340 ? 99.662  125.755 156.857 1.00 26.18  ? 319 ASP D OD1   1 
ATOM   11284 O  OD2   . ASP D 2 340 ? 100.927 125.104 155.184 1.00 26.11  ? 319 ASP D OD2   1 
ATOM   11285 N  N     . PHE D 2 341 ? 99.545  130.585 155.508 1.00 16.86  ? 320 PHE D N     1 
ATOM   11286 C  CA    . PHE D 2 341 ? 99.723  132.002 155.235 1.00 12.88  ? 320 PHE D CA    1 
ATOM   11287 C  C     . PHE D 2 341 ? 99.191  132.873 156.362 1.00 12.06  ? 320 PHE D C     1 
ATOM   11288 O  O     . PHE D 2 341 ? 99.347  134.097 156.310 1.00 15.68  ? 320 PHE D O     1 
ATOM   11289 C  CB    . PHE D 2 341 ? 99.032  132.377 153.920 1.00 14.37  ? 320 PHE D CB    1 
ATOM   11290 C  CG    . PHE D 2 341 ? 99.607  131.692 152.713 1.00 12.00  ? 320 PHE D CG    1 
ATOM   11291 C  CD1   . PHE D 2 341 ? 99.232  130.398 152.388 1.00 7.83   ? 320 PHE D CD1   1 
ATOM   11292 C  CD2   . PHE D 2 341 ? 100.513 132.345 151.896 1.00 12.15  ? 320 PHE D CD2   1 
ATOM   11293 C  CE1   . PHE D 2 341 ? 99.759  129.769 151.278 1.00 9.70   ? 320 PHE D CE1   1 
ATOM   11294 C  CE2   . PHE D 2 341 ? 101.040 131.720 150.783 1.00 8.26   ? 320 PHE D CE2   1 
ATOM   11295 C  CZ    . PHE D 2 341 ? 100.662 130.431 150.475 1.00 8.55   ? 320 PHE D CZ    1 
ATOM   11296 N  N     . TYR D 2 342 ? 98.569  132.270 157.373 1.00 7.62   ? 321 TYR D N     1 
ATOM   11297 C  CA    . TYR D 2 342 ? 98.037  132.984 158.523 1.00 11.59  ? 321 TYR D CA    1 
ATOM   11298 C  C     . TYR D 2 342 ? 98.710  132.446 159.776 1.00 18.48  ? 321 TYR D C     1 
ATOM   11299 O  O     . TYR D 2 342 ? 98.877  131.231 159.919 1.00 23.59  ? 321 TYR D O     1 
ATOM   11300 C  CB    . TYR D 2 342 ? 96.517  132.821 158.625 1.00 9.15   ? 321 TYR D CB    1 
ATOM   11301 C  CG    . TYR D 2 342 ? 95.756  133.412 157.460 1.00 14.71  ? 321 TYR D CG    1 
ATOM   11302 C  CD1   . TYR D 2 342 ? 95.357  132.618 156.393 1.00 13.92  ? 321 TYR D CD1   1 
ATOM   11303 C  CD2   . TYR D 2 342 ? 95.436  134.762 157.427 1.00 21.77  ? 321 TYR D CD2   1 
ATOM   11304 C  CE1   . TYR D 2 342 ? 94.662  133.151 155.326 1.00 13.51  ? 321 TYR D CE1   1 
ATOM   11305 C  CE2   . TYR D 2 342 ? 94.741  135.304 156.363 1.00 15.51  ? 321 TYR D CE2   1 
ATOM   11306 C  CZ    . TYR D 2 342 ? 94.357  134.495 155.316 1.00 17.94  ? 321 TYR D CZ    1 
ATOM   11307 O  OH    . TYR D 2 342 ? 93.665  135.030 154.254 1.00 24.54  ? 321 TYR D OH    1 
ATOM   11308 N  N     . PHE D 2 343 ? 99.095  133.347 160.673 1.00 11.50  ? 322 PHE D N     1 
ATOM   11309 C  CA    . PHE D 2 343 ? 99.804  132.952 161.884 1.00 15.15  ? 322 PHE D CA    1 
ATOM   11310 C  C     . PHE D 2 343 ? 99.142  133.537 163.127 1.00 24.40  ? 322 PHE D C     1 
ATOM   11311 O  O     . PHE D 2 343 ? 98.547  134.613 163.081 1.00 21.09  ? 322 PHE D O     1 
ATOM   11312 C  CB    . PHE D 2 343 ? 101.267 133.389 161.806 1.00 15.27  ? 322 PHE D CB    1 
ATOM   11313 C  CG    . PHE D 2 343 ? 101.966 132.941 160.555 1.00 12.42  ? 322 PHE D CG    1 
ATOM   11314 C  CD1   . PHE D 2 343 ? 102.515 131.673 160.469 1.00 11.68  ? 322 PHE D CD1   1 
ATOM   11315 C  CD2   . PHE D 2 343 ? 102.068 133.785 159.463 1.00 10.73  ? 322 PHE D CD2   1 
ATOM   11316 C  CE1   . PHE D 2 343 ? 103.155 131.258 159.318 1.00 5.83   ? 322 PHE D CE1   1 
ATOM   11317 C  CE2   . PHE D 2 343 ? 102.706 133.374 158.311 1.00 7.52   ? 322 PHE D CE2   1 
ATOM   11318 C  CZ    . PHE D 2 343 ? 103.250 132.110 158.238 1.00 8.62   ? 322 PHE D CZ    1 
ATOM   11319 N  N     . VAL E 3 19  ? 115.630 108.232 196.809 1.00 95.16  ? 19  VAL E N     1 
ATOM   11320 C  CA    . VAL E 3 19  ? 116.209 107.892 195.505 1.00 95.16  ? 19  VAL E CA    1 
ATOM   11321 C  C     . VAL E 3 19  ? 115.382 108.532 194.400 1.00 95.16  ? 19  VAL E C     1 
ATOM   11322 O  O     . VAL E 3 19  ? 114.177 108.288 194.278 1.00 95.16  ? 19  VAL E O     1 
ATOM   11323 C  CB    . VAL E 3 19  ? 116.360 106.375 195.312 1.00 95.16  ? 19  VAL E CB    1 
ATOM   11324 C  CG1   . VAL E 3 19  ? 117.065 106.050 193.987 1.00 95.16  ? 19  VAL E CG1   1 
ATOM   11325 C  CG2   . VAL E 3 19  ? 117.208 105.781 196.443 1.00 95.16  ? 19  VAL E CG2   1 
ATOM   11326 N  N     . VAL E 3 20  ? 116.042 109.348 193.583 1.00 96.12  ? 20  VAL E N     1 
ATOM   11327 C  CA    . VAL E 3 20  ? 115.417 110.117 192.509 1.00 96.12  ? 20  VAL E CA    1 
ATOM   11328 C  C     . VAL E 3 20  ? 116.115 109.835 191.186 1.00 96.12  ? 20  VAL E C     1 
ATOM   11329 O  O     . VAL E 3 20  ? 117.334 109.934 191.091 1.00 96.12  ? 20  VAL E O     1 
ATOM   11330 C  CB    . VAL E 3 20  ? 115.390 111.623 192.835 1.00 96.12  ? 20  VAL E CB    1 
ATOM   11331 C  CG1   . VAL E 3 20  ? 114.546 112.376 191.800 1.00 96.12  ? 20  VAL E CG1   1 
ATOM   11332 C  CG2   . VAL E 3 20  ? 114.802 111.876 194.233 1.00 96.12  ? 20  VAL E CG2   1 
ATOM   11333 N  N     . LEU E 3 21  ? 115.345 109.512 190.149 1.00 96.32  ? 21  LEU E N     1 
ATOM   11334 C  CA    . LEU E 3 21  ? 115.820 109.444 188.770 1.00 96.32  ? 21  LEU E CA    1 
ATOM   11335 C  C     . LEU E 3 21  ? 115.456 110.752 188.064 1.00 96.32  ? 21  LEU E C     1 
ATOM   11336 O  O     . LEU E 3 21  ? 114.289 110.986 187.742 1.00 96.32  ? 21  LEU E O     1 
ATOM   11337 C  CB    . LEU E 3 21  ? 115.224 108.203 188.086 1.00 96.32  ? 21  LEU E CB    1 
ATOM   11338 C  CG    . LEU E 3 21  ? 115.723 107.977 186.648 1.00 96.32  ? 21  LEU E CG    1 
ATOM   11339 C  CD1   . LEU E 3 21  ? 117.209 107.614 186.617 1.00 96.32  ? 21  LEU E CD1   1 
ATOM   11340 C  CD2   . LEU E 3 21  ? 114.949 106.818 186.022 1.00 96.32  ? 21  LEU E CD2   1 
ATOM   11341 N  N     . ALA E 3 22  ? 116.449 111.608 187.847 1.00 97.01  ? 22  ALA E N     1 
ATOM   11342 C  CA    . ALA E 3 22  ? 116.288 112.874 187.147 1.00 97.01  ? 22  ALA E CA    1 
ATOM   11343 C  C     . ALA E 3 22  ? 116.604 112.717 185.653 1.00 97.01  ? 22  ALA E C     1 
ATOM   11344 O  O     . ALA E 3 22  ? 117.720 112.353 185.294 1.00 97.01  ? 22  ALA E O     1 
ATOM   11345 C  CB    . ALA E 3 22  ? 117.153 113.942 187.816 1.00 97.01  ? 22  ALA E CB    1 
ATOM   11346 N  N     . ASP E 3 23  ? 115.639 113.026 184.793 1.00 96.28  ? 23  ASP E N     1 
ATOM   11347 C  CA    . ASP E 3 23  ? 115.749 113.004 183.336 1.00 96.28  ? 23  ASP E CA    1 
ATOM   11348 C  C     . ASP E 3 23  ? 115.890 114.416 182.769 1.00 96.28  ? 23  ASP E C     1 
ATOM   11349 O  O     . ASP E 3 23  ? 114.948 115.216 182.788 1.00 96.28  ? 23  ASP E O     1 
ATOM   11350 C  CB    . ASP E 3 23  ? 114.539 112.264 182.750 1.00 96.28  ? 23  ASP E CB    1 
ATOM   11351 C  CG    . ASP E 3 23  ? 114.454 112.331 181.219 1.00 96.28  ? 23  ASP E CG    1 
ATOM   11352 O  OD1   . ASP E 3 23  ? 115.502 112.284 180.543 1.00 96.28  ? 23  ASP E OD1   1 
ATOM   11353 O  OD2   . ASP E 3 23  ? 113.307 112.401 180.714 1.00 96.28  ? 23  ASP E OD2   1 
ATOM   11354 N  N     . PHE E 3 24  ? 117.082 114.704 182.256 1.00 96.18  ? 24  PHE E N     1 
ATOM   11355 C  CA    . PHE E 3 24  ? 117.394 115.911 181.506 1.00 96.18  ? 24  PHE E CA    1 
ATOM   11356 C  C     . PHE E 3 24  ? 117.058 115.674 180.041 1.00 96.18  ? 24  PHE E C     1 
ATOM   11357 O  O     . PHE E 3 24  ? 117.702 114.866 179.367 1.00 96.18  ? 24  PHE E O     1 
ATOM   11358 C  CB    . PHE E 3 24  ? 118.873 116.269 181.681 1.00 96.18  ? 24  PHE E CB    1 
ATOM   11359 C  CG    . PHE E 3 24  ? 119.225 116.734 183.076 1.00 96.18  ? 24  PHE E CG    1 
ATOM   11360 C  CD1   . PHE E 3 24  ? 119.408 118.104 183.334 1.00 96.18  ? 24  PHE E CD1   1 
ATOM   11361 C  CD2   . PHE E 3 24  ? 119.346 115.805 184.126 1.00 96.18  ? 24  PHE E CD2   1 
ATOM   11362 C  CE1   . PHE E 3 24  ? 119.707 118.544 184.633 1.00 96.18  ? 24  PHE E CE1   1 
ATOM   11363 C  CE2   . PHE E 3 24  ? 119.623 116.249 185.429 1.00 96.18  ? 24  PHE E CE2   1 
ATOM   11364 C  CZ    . PHE E 3 24  ? 119.815 117.617 185.683 1.00 96.18  ? 24  PHE E CZ    1 
ATOM   11365 N  N     . TRP E 3 25  ? 116.062 116.397 179.542 1.00 94.24  ? 25  TRP E N     1 
ATOM   11366 C  CA    . TRP E 3 25  ? 115.469 116.157 178.230 1.00 94.24  ? 25  TRP E CA    1 
ATOM   11367 C  C     . TRP E 3 25  ? 115.180 117.472 177.502 1.00 94.24  ? 25  TRP E C     1 
ATOM   11368 O  O     . TRP E 3 25  ? 115.277 118.540 178.095 1.00 94.24  ? 25  TRP E O     1 
ATOM   11369 C  CB    . TRP E 3 25  ? 114.197 115.316 178.419 1.00 94.24  ? 25  TRP E CB    1 
ATOM   11370 C  CG    . TRP E 3 25  ? 113.012 116.040 178.978 1.00 94.24  ? 25  TRP E CG    1 
ATOM   11371 C  CD1   . TRP E 3 25  ? 112.882 116.464 180.251 1.00 94.24  ? 25  TRP E CD1   1 
ATOM   11372 C  CD2   . TRP E 3 25  ? 111.819 116.502 178.277 1.00 94.24  ? 25  TRP E CD2   1 
ATOM   11373 N  NE1   . TRP E 3 25  ? 111.733 117.218 180.376 1.00 94.24  ? 25  TRP E NE1   1 
ATOM   11374 C  CE2   . TRP E 3 25  ? 111.027 117.256 179.194 1.00 94.24  ? 25  TRP E CE2   1 
ATOM   11375 C  CE3   . TRP E 3 25  ? 111.339 116.380 176.955 1.00 94.24  ? 25  TRP E CE3   1 
ATOM   11376 C  CZ2   . TRP E 3 25  ? 109.830 117.878 178.815 1.00 94.24  ? 25  TRP E CZ2   1 
ATOM   11377 C  CZ3   . TRP E 3 25  ? 110.130 116.989 176.567 1.00 94.24  ? 25  TRP E CZ3   1 
ATOM   11378 C  CH2   . TRP E 3 25  ? 109.384 117.745 177.489 1.00 94.24  ? 25  TRP E CH2   1 
ATOM   11379 N  N     . ALA E 3 26  ? 114.810 117.390 176.223 1.00 92.23  ? 26  ALA E N     1 
ATOM   11380 C  CA    . ALA E 3 26  ? 114.283 118.527 175.470 1.00 92.23  ? 26  ALA E CA    1 
ATOM   11381 C  C     . ALA E 3 26  ? 113.186 118.087 174.480 1.00 92.23  ? 26  ALA E C     1 
ATOM   11382 O  O     . ALA E 3 26  ? 113.212 116.941 174.008 1.00 92.23  ? 26  ALA E O     1 
ATOM   11383 C  CB    . ALA E 3 26  ? 115.416 119.236 174.720 1.00 92.23  ? 26  ALA E CB    1 
ATOM   11384 N  N     . PRO E 3 27  ? 112.259 118.976 174.074 1.00 86.64  ? 27  PRO E N     1 
ATOM   11385 C  CA    . PRO E 3 27  ? 111.149 118.635 173.178 1.00 86.64  ? 27  PRO E CA    1 
ATOM   11386 C  C     . PRO E 3 27  ? 111.577 118.246 171.757 1.00 86.64  ? 27  PRO E C     1 
ATOM   11387 O  O     . PRO E 3 27  ? 110.858 117.528 171.054 1.00 86.64  ? 27  PRO E O     1 
ATOM   11388 C  CB    . PRO E 3 27  ? 110.261 119.886 173.143 1.00 86.64  ? 27  PRO E CB    1 
ATOM   11389 C  CG    . PRO E 3 27  ? 110.613 120.635 174.426 1.00 86.64  ? 27  PRO E CG    1 
ATOM   11390 C  CD    . PRO E 3 27  ? 112.095 120.330 174.586 1.00 86.64  ? 27  PRO E CD    1 
ATOM   11391 N  N     . TRP E 3 28  ? 112.737 118.721 171.307 1.00 80.08  ? 28  TRP E N     1 
ATOM   11392 C  CA    . TRP E 3 28  ? 113.293 118.427 169.984 1.00 80.08  ? 28  TRP E CA    1 
ATOM   11393 C  C     . TRP E 3 28  ? 114.135 117.144 169.951 1.00 80.08  ? 28  TRP E C     1 
ATOM   11394 O  O     . TRP E 3 28  ? 114.394 116.615 168.873 1.00 80.08  ? 28  TRP E O     1 
ATOM   11395 C  CB    . TRP E 3 28  ? 114.090 119.645 169.510 1.00 80.08  ? 28  TRP E CB    1 
ATOM   11396 C  CG    . TRP E 3 28  ? 115.093 120.164 170.489 1.00 80.08  ? 28  TRP E CG    1 
ATOM   11397 C  CD1   . TRP E 3 28  ? 114.901 121.196 171.340 1.00 80.08  ? 28  TRP E CD1   1 
ATOM   11398 C  CD2   . TRP E 3 28  ? 116.446 119.683 170.753 1.00 80.08  ? 28  TRP E CD2   1 
ATOM   11399 N  NE1   . TRP E 3 28  ? 116.027 121.375 172.113 1.00 80.08  ? 28  TRP E NE1   1 
ATOM   11400 C  CE2   . TRP E 3 28  ? 117.008 120.469 171.803 1.00 80.08  ? 28  TRP E CE2   1 
ATOM   11401 C  CE3   . TRP E 3 28  ? 117.257 118.662 170.216 1.00 80.08  ? 28  TRP E CE3   1 
ATOM   11402 C  CZ2   . TRP E 3 28  ? 118.290 120.247 172.317 1.00 80.08  ? 28  TRP E CZ2   1 
ATOM   11403 C  CZ3   . TRP E 3 28  ? 118.560 118.451 170.702 1.00 80.08  ? 28  TRP E CZ3   1 
ATOM   11404 C  CH2   . TRP E 3 28  ? 119.076 119.232 171.751 1.00 80.08  ? 28  TRP E CH2   1 
ATOM   11405 N  N     . CYS E 3 29  ? 114.514 116.605 171.110 1.00 85.92  ? 29  CYS E N     1 
ATOM   11406 C  CA    . CYS E 3 29  ? 115.375 115.434 171.221 1.00 85.92  ? 29  CYS E CA    1 
ATOM   11407 C  C     . CYS E 3 29  ? 114.596 114.135 170.944 1.00 85.92  ? 29  CYS E C     1 
ATOM   11408 O  O     . CYS E 3 29  ? 113.758 113.703 171.739 1.00 85.92  ? 29  CYS E O     1 
ATOM   11409 C  CB    . CYS E 3 29  ? 116.006 115.479 172.613 1.00 85.92  ? 29  CYS E CB    1 
ATOM   11410 S  SG    . CYS E 3 29  ? 117.199 114.185 173.015 1.00 85.92  ? 29  CYS E SG    1 
ATOM   11411 N  N     . GLY E 3 30  ? 114.887 113.485 169.813 1.00 84.06  ? 30  GLY E N     1 
ATOM   11412 C  CA    . GLY E 3 30  ? 114.278 112.206 169.424 1.00 84.06  ? 30  GLY E CA    1 
ATOM   11413 C  C     . GLY E 3 30  ? 114.444 111.104 170.482 1.00 84.06  ? 30  GLY E C     1 
ATOM   11414 O  O     . GLY E 3 30  ? 113.435 110.566 170.943 1.00 84.06  ? 30  GLY E O     1 
ATOM   11415 N  N     . PRO E 3 31  ? 115.673 110.810 170.950 1.00 89.12  ? 31  PRO E N     1 
ATOM   11416 C  CA    . PRO E 3 31  ? 115.901 109.823 172.011 1.00 89.12  ? 31  PRO E CA    1 
ATOM   11417 C  C     . PRO E 3 31  ? 115.171 110.133 173.324 1.00 89.12  ? 31  PRO E C     1 
ATOM   11418 O  O     . PRO E 3 31  ? 114.662 109.229 173.983 1.00 89.12  ? 31  PRO E O     1 
ATOM   11419 C  CB    . PRO E 3 31  ? 117.423 109.763 172.177 1.00 89.12  ? 31  PRO E CB    1 
ATOM   11420 C  CG    . PRO E 3 31  ? 117.951 110.160 170.801 1.00 89.12  ? 31  PRO E CG    1 
ATOM   11421 C  CD    . PRO E 3 31  ? 116.945 111.223 170.366 1.00 89.12  ? 31  PRO E CD    1 
ATOM   11422 N  N     . CYS E 3 32  ? 115.009 111.412 173.660 1.00 91.95  ? 32  CYS E N     1 
ATOM   11423 C  CA    . CYS E 3 32  ? 114.250 111.842 174.830 1.00 91.95  ? 32  CYS E CA    1 
ATOM   11424 C  C     . CYS E 3 32  ? 112.752 111.519 174.710 1.00 91.95  ? 32  CYS E C     1 
ATOM   11425 O  O     . CYS E 3 32  ? 112.095 111.201 175.699 1.00 91.95  ? 32  CYS E O     1 
ATOM   11426 C  CB    . CYS E 3 32  ? 114.441 113.344 175.025 1.00 91.95  ? 32  CYS E CB    1 
ATOM   11427 S  SG    . CYS E 3 32  ? 116.120 113.897 175.430 1.00 91.95  ? 32  CYS E SG    1 
ATOM   11428 N  N     . LYS E 3 33  ? 112.190 111.550 173.495 1.00 89.47  ? 33  LYS E N     1 
ATOM   11429 C  CA    . LYS E 3 33  ? 110.811 111.094 173.253 1.00 89.47  ? 33  LYS E CA    1 
ATOM   11430 C  C     . LYS E 3 33  ? 110.676 109.584 173.412 1.00 89.47  ? 33  LYS E C     1 
ATOM   11431 O  O     . LYS E 3 33  ? 109.641 109.125 173.879 1.00 89.47  ? 33  LYS E O     1 
ATOM   11432 C  CB    . LYS E 3 33  ? 110.326 111.517 171.863 1.00 89.47  ? 33  LYS E CB    1 
ATOM   11433 C  CG    . LYS E 3 33  ? 110.186 113.036 171.757 1.00 89.47  ? 33  LYS E CG    1 
ATOM   11434 C  CD    . LYS E 3 33  ? 109.812 113.446 170.331 1.00 89.47  ? 33  LYS E CD    1 
ATOM   11435 C  CE    . LYS E 3 33  ? 109.724 114.968 170.335 1.00 89.47  ? 33  LYS E CE    1 
ATOM   11436 N  NZ    . LYS E 3 33  ? 109.609 115.554 168.981 1.00 89.47  ? 33  LYS E NZ    1 
ATOM   11437 N  N     . MET E 3 34  ? 111.711 108.822 173.055 1.00 91.65  ? 34  MET E N     1 
ATOM   11438 C  CA    . MET E 3 34  ? 111.714 107.365 173.216 1.00 91.65  ? 34  MET E CA    1 
ATOM   11439 C  C     . MET E 3 34  ? 111.800 106.941 174.685 1.00 91.65  ? 34  MET E C     1 
ATOM   11440 O  O     . MET E 3 34  ? 111.211 105.930 175.054 1.00 91.65  ? 34  MET E O     1 
ATOM   11441 C  CB    . MET E 3 34  ? 112.863 106.725 172.425 1.00 91.65  ? 34  MET E CB    1 
ATOM   11442 C  CG    . MET E 3 34  ? 112.748 106.974 170.920 1.00 91.65  ? 34  MET E CG    1 
ATOM   11443 S  SD    . MET E 3 34  ? 113.849 105.949 169.906 1.00 91.65  ? 34  MET E SD    1 
ATOM   11444 C  CE    . MET E 3 34  ? 115.480 106.609 170.339 1.00 91.65  ? 34  MET E CE    1 
ATOM   11445 N  N     . ILE E 3 35  ? 112.497 107.708 175.530 1.00 92.57  ? 35  ILE E N     1 
ATOM   11446 C  CA    . ILE E 3 35  ? 112.647 107.372 176.953 1.00 92.57  ? 35  ILE E CA    1 
ATOM   11447 C  C     . ILE E 3 35  ? 111.407 107.720 177.785 1.00 92.57  ? 35  ILE E C     1 
ATOM   11448 O  O     . ILE E 3 35  ? 111.173 107.107 178.819 1.00 92.57  ? 35  ILE E O     1 
ATOM   11449 C  CB    . ILE E 3 35  ? 113.950 107.995 177.507 1.00 92.57  ? 35  ILE E CB    1 
ATOM   11450 C  CG1   . ILE E 3 35  ? 114.613 107.018 178.497 1.00 92.57  ? 35  ILE E CG1   1 
ATOM   11451 C  CG2   . ILE E 3 35  ? 113.754 109.380 178.150 1.00 92.57  ? 35  ILE E CG2   1 
ATOM   11452 C  CD1   . ILE E 3 35  ? 116.057 107.412 178.813 1.00 92.57  ? 35  ILE E CD1   1 
ATOM   11453 N  N     . ALA E 3 36  ? 110.583 108.670 177.332 1.00 91.47  ? 36  ALA E N     1 
ATOM   11454 C  CA    . ALA E 3 36  ? 109.376 109.094 178.040 1.00 91.47  ? 36  ALA E CA    1 
ATOM   11455 C  C     . ALA E 3 36  ? 108.431 107.933 178.436 1.00 91.47  ? 36  ALA E C     1 
ATOM   11456 O  O     . ALA E 3 36  ? 108.157 107.817 179.630 1.00 91.47  ? 36  ALA E O     1 
ATOM   11457 C  CB    . ALA E 3 36  ? 108.677 110.193 177.227 1.00 91.47  ? 36  ALA E CB    1 
ATOM   11458 N  N     . PRO E 3 37  ? 107.994 107.033 177.527 1.00 93.27  ? 37  PRO E N     1 
ATOM   11459 C  CA    . PRO E 3 37  ? 107.145 105.897 177.904 1.00 93.27  ? 37  PRO E CA    1 
ATOM   11460 C  C     . PRO E 3 37  ? 107.851 104.904 178.838 1.00 93.27  ? 37  PRO E C     1 
ATOM   11461 O  O     . PRO E 3 37  ? 107.219 104.317 179.710 1.00 93.27  ? 37  PRO E O     1 
ATOM   11462 C  CB    . PRO E 3 37  ? 106.745 105.231 176.582 1.00 93.27  ? 37  PRO E CB    1 
ATOM   11463 C  CG    . PRO E 3 37  ? 107.869 105.620 175.623 1.00 93.27  ? 37  PRO E CG    1 
ATOM   11464 C  CD    . PRO E 3 37  ? 108.215 107.030 176.086 1.00 93.27  ? 37  PRO E CD    1 
ATOM   11465 N  N     . VAL E 3 38  ? 109.173 104.751 178.708 1.00 94.14  ? 38  VAL E N     1 
ATOM   11466 C  CA    . VAL E 3 38  ? 109.966 103.873 179.583 1.00 94.14  ? 38  VAL E CA    1 
ATOM   11467 C  C     . VAL E 3 38  ? 109.934 104.376 181.029 1.00 94.14  ? 38  VAL E C     1 
ATOM   11468 O  O     . VAL E 3 38  ? 109.803 103.583 181.958 1.00 94.14  ? 38  VAL E O     1 
ATOM   11469 C  CB    . VAL E 3 38  ? 111.422 103.767 179.083 1.00 94.14  ? 38  VAL E CB    1 
ATOM   11470 C  CG1   . VAL E 3 38  ? 112.239 102.796 179.932 1.00 94.14  ? 38  VAL E CG1   1 
ATOM   11471 C  CG2   . VAL E 3 38  ? 111.490 103.273 177.630 1.00 94.14  ? 38  VAL E CG2   1 
ATOM   11472 N  N     . LEU E 3 39  ? 110.017 105.695 181.225 1.00 94.75  ? 39  LEU E N     1 
ATOM   11473 C  CA    . LEU E 3 39  ? 109.917 106.311 182.548 1.00 94.75  ? 39  LEU E CA    1 
ATOM   11474 C  C     . LEU E 3 39  ? 108.503 106.206 183.133 1.00 94.75  ? 39  LEU E C     1 
ATOM   11475 O  O     . LEU E 3 39  ? 108.366 106.051 184.342 1.00 94.75  ? 39  LEU E O     1 
ATOM   11476 C  CB    . LEU E 3 39  ? 110.368 107.779 182.467 1.00 94.75  ? 39  LEU E CB    1 
ATOM   11477 C  CG    . LEU E 3 39  ? 111.849 107.988 182.101 1.00 94.75  ? 39  LEU E CG    1 
ATOM   11478 C  CD1   . LEU E 3 39  ? 112.122 109.488 181.978 1.00 94.75  ? 39  LEU E CD1   1 
ATOM   11479 C  CD2   . LEU E 3 39  ? 112.807 107.407 183.139 1.00 94.75  ? 39  LEU E CD2   1 
ATOM   11480 N  N     . GLU E 3 40  ? 107.458 106.260 182.305 1.00 93.96  ? 40  GLU E N     1 
ATOM   11481 C  CA    . GLU E 3 40  ? 106.072 106.062 182.758 1.00 93.96  ? 40  GLU E CA    1 
ATOM   11482 C  C     . GLU E 3 40  ? 105.831 104.630 183.249 1.00 93.96  ? 40  GLU E C     1 
ATOM   11483 O  O     . GLU E 3 40  ? 105.233 104.440 184.307 1.00 93.96  ? 40  GLU E O     1 
ATOM   11484 C  CB    . GLU E 3 40  ? 105.082 106.415 181.639 1.00 93.96  ? 40  GLU E CB    1 
ATOM   11485 C  CG    . GLU E 3 40  ? 105.018 107.925 181.361 1.00 93.96  ? 40  GLU E CG    1 
ATOM   11486 C  CD    . GLU E 3 40  ? 104.089 108.302 180.193 1.00 93.96  ? 40  GLU E CD    1 
ATOM   11487 O  OE1   . GLU E 3 40  ? 104.070 109.508 179.848 1.00 93.96  ? 40  GLU E OE1   1 
ATOM   11488 O  OE2   . GLU E 3 40  ? 103.390 107.413 179.652 1.00 93.96  ? 40  GLU E OE2   1 
ATOM   11489 N  N     . GLU E 3 41  ? 106.333 103.618 182.536 1.00 94.15  ? 41  GLU E N     1 
ATOM   11490 C  CA    . GLU E 3 41  ? 106.285 102.227 183.007 1.00 94.15  ? 41  GLU E CA    1 
ATOM   11491 C  C     . GLU E 3 41  ? 107.099 102.031 184.290 1.00 94.15  ? 41  GLU E C     1 
ATOM   11492 O  O     . GLU E 3 41  ? 106.655 101.357 185.220 1.00 94.15  ? 41  GLU E O     1 
ATOM   11493 C  CB    . GLU E 3 41  ? 106.833 101.274 181.940 1.00 94.15  ? 41  GLU E CB    1 
ATOM   11494 C  CG    . GLU E 3 41  ? 105.911 101.105 180.727 1.00 94.15  ? 41  GLU E CG    1 
ATOM   11495 C  CD    . GLU E 3 41  ? 106.431 100.035 179.749 1.00 94.15  ? 41  GLU E CD    1 
ATOM   11496 O  OE1   . GLU E 3 41  ? 105.966 100.038 178.588 1.00 94.15  ? 41  GLU E OE1   1 
ATOM   11497 O  OE2   . GLU E 3 41  ? 107.255 99.177  180.170 1.00 94.15  ? 41  GLU E OE2   1 
ATOM   11498 N  N     . LEU E 3 42  ? 108.282 102.647 184.365 1.00 93.46  ? 42  LEU E N     1 
ATOM   11499 C  CA    . LEU E 3 42  ? 109.128 102.572 185.551 1.00 93.46  ? 42  LEU E CA    1 
ATOM   11500 C  C     . LEU E 3 42  ? 108.444 103.198 186.774 1.00 93.46  ? 42  LEU E C     1 
ATOM   11501 O  O     . LEU E 3 42  ? 108.532 102.639 187.867 1.00 93.46  ? 42  LEU E O     1 
ATOM   11502 C  CB    . LEU E 3 42  ? 110.473 103.247 185.238 1.00 93.46  ? 42  LEU E CB    1 
ATOM   11503 C  CG    . LEU E 3 42  ? 111.541 103.025 186.321 1.00 93.46  ? 42  LEU E CG    1 
ATOM   11504 C  CD1   . LEU E 3 42  ? 111.992 101.567 186.366 1.00 93.46  ? 42  LEU E CD1   1 
ATOM   11505 C  CD2   . LEU E 3 42  ? 112.769 103.879 186.014 1.00 93.46  ? 42  LEU E CD2   1 
ATOM   11506 N  N     . ASP E 3 43  ? 107.727 104.313 186.602 1.00 93.38  ? 43  ASP E N     1 
ATOM   11507 C  CA    . ASP E 3 43  ? 106.945 104.920 187.683 1.00 93.38  ? 43  ASP E CA    1 
ATOM   11508 C  C     . ASP E 3 43  ? 105.798 104.015 188.154 1.00 93.38  ? 43  ASP E C     1 
ATOM   11509 O  O     . ASP E 3 43  ? 105.510 103.940 189.348 1.00 93.38  ? 43  ASP E O     1 
ATOM   11510 C  CB    . ASP E 3 43  ? 106.369 106.282 187.265 1.00 93.38  ? 43  ASP E CB    1 
ATOM   11511 C  CG    . ASP E 3 43  ? 105.698 106.932 188.478 1.00 93.38  ? 43  ASP E CG    1 
ATOM   11512 O  OD1   . ASP E 3 43  ? 106.366 106.996 189.535 1.00 93.38  ? 43  ASP E OD1   1 
ATOM   11513 O  OD2   . ASP E 3 43  ? 104.497 107.294 188.423 1.00 93.38  ? 43  ASP E OD2   1 
ATOM   11514 N  N     . GLN E 3 44  ? 105.155 103.288 187.240 1.00 92.26  ? 44  GLN E N     1 
ATOM   11515 C  CA    . GLN E 3 44  ? 104.090 102.350 187.606 1.00 92.26  ? 44  GLN E CA    1 
ATOM   11516 C  C     . GLN E 3 44  ? 104.612 101.162 188.418 1.00 92.26  ? 44  GLN E C     1 
ATOM   11517 O  O     . GLN E 3 44  ? 103.929 100.695 189.328 1.00 92.26  ? 44  GLN E O     1 
ATOM   11518 C  CB    . GLN E 3 44  ? 103.374 101.845 186.348 1.00 92.26  ? 44  GLN E CB    1 
ATOM   11519 C  CG    . GLN E 3 44  ? 102.516 102.938 185.704 1.00 92.26  ? 44  GLN E CG    1 
ATOM   11520 C  CD    . GLN E 3 44  ? 101.861 102.479 184.407 1.00 92.26  ? 44  GLN E CD    1 
ATOM   11521 O  OE1   . GLN E 3 44  ? 101.699 101.307 184.112 1.00 92.26  ? 44  GLN E OE1   1 
ATOM   11522 N  NE2   . GLN E 3 44  ? 101.415 103.399 183.585 1.00 92.26  ? 44  GLN E NE2   1 
ATOM   11523 N  N     . GLU E 3 45  ? 105.812 100.671 188.106 1.00 91.79  ? 45  GLU E N     1 
ATOM   11524 C  CA    . GLU E 3 45  ? 106.390 99.495  188.765 1.00 91.79  ? 45  GLU E CA    1 
ATOM   11525 C  C     . GLU E 3 45  ? 107.160 99.835  190.048 1.00 91.79  ? 45  GLU E C     1 
ATOM   11526 O  O     . GLU E 3 45  ? 107.196 99.033  190.983 1.00 91.79  ? 45  GLU E O     1 
ATOM   11527 C  CB    . GLU E 3 45  ? 107.306 98.755  187.778 1.00 91.79  ? 45  GLU E CB    1 
ATOM   11528 C  CG    . GLU E 3 45  ? 106.514 98.070  186.650 1.00 91.79  ? 45  GLU E CG    1 
ATOM   11529 C  CD    . GLU E 3 45  ? 107.406 97.301  185.661 1.00 91.79  ? 45  GLU E CD    1 
ATOM   11530 O  OE1   . GLU E 3 45  ? 106.957 97.046  184.517 1.00 91.79  ? 45  GLU E OE1   1 
ATOM   11531 O  OE2   . GLU E 3 45  ? 108.548 96.935  186.017 1.00 91.79  ? 45  GLU E OE2   1 
ATOM   11532 N  N     . MET E 3 46  ? 107.800 101.005 190.100 1.00 90.55  ? 46  MET E N     1 
ATOM   11533 C  CA    . MET E 3 46  ? 108.755 101.363 191.156 1.00 90.55  ? 46  MET E CA    1 
ATOM   11534 C  C     . MET E 3 46  ? 108.453 102.690 191.852 1.00 90.55  ? 46  MET E C     1 
ATOM   11535 O  O     . MET E 3 46  ? 109.198 103.083 192.751 1.00 90.55  ? 46  MET E O     1 
ATOM   11536 C  CB    . MET E 3 46  ? 110.182 101.364 190.594 1.00 90.55  ? 46  MET E CB    1 
ATOM   11537 C  CG    . MET E 3 46  ? 110.584 99.996  190.034 1.00 90.55  ? 46  MET E CG    1 
ATOM   11538 S  SD    . MET E 3 46  ? 112.332 99.870  189.589 1.00 90.55  ? 46  MET E SD    1 
ATOM   11539 C  CE    . MET E 3 46  ? 113.113 99.905  191.215 1.00 90.55  ? 46  MET E CE    1 
ATOM   11540 N  N     . GLY E 3 47  ? 107.362 103.366 191.494 1.00 85.77  ? 47  GLY E N     1 
ATOM   11541 C  CA    . GLY E 3 47  ? 107.037 104.713 191.962 1.00 85.77  ? 47  GLY E CA    1 
ATOM   11542 C  C     . GLY E 3 47  ? 106.781 104.870 193.464 1.00 85.77  ? 47  GLY E C     1 
ATOM   11543 O  O     . GLY E 3 47  ? 106.589 105.997 193.911 1.00 85.77  ? 47  GLY E O     1 
ATOM   11544 N  N     . ASP E 3 48  ? 106.757 103.776 194.232 1.00 86.79  ? 48  ASP E N     1 
ATOM   11545 C  CA    . ASP E 3 48  ? 106.687 103.785 195.703 1.00 86.79  ? 48  ASP E CA    1 
ATOM   11546 C  C     . ASP E 3 48  ? 108.067 103.932 196.365 1.00 86.79  ? 48  ASP E C     1 
ATOM   11547 O  O     . ASP E 3 48  ? 108.166 104.310 197.532 1.00 86.79  ? 48  ASP E O     1 
ATOM   11548 C  CB    . ASP E 3 48  ? 106.056 102.474 196.197 1.00 86.79  ? 48  ASP E CB    1 
ATOM   11549 C  CG    . ASP E 3 48  ? 104.577 102.301 195.839 1.00 86.79  ? 48  ASP E CG    1 
ATOM   11550 O  OD1   . ASP E 3 48  ? 103.891 103.321 195.603 1.00 86.79  ? 48  ASP E OD1   1 
ATOM   11551 O  OD2   . ASP E 3 48  ? 104.143 101.128 195.855 1.00 86.79  ? 48  ASP E OD2   1 
ATOM   11552 N  N     . LYS E 3 49  ? 109.139 103.590 195.641 1.00 90.32  ? 49  LYS E N     1 
ATOM   11553 C  CA    . LYS E 3 49  ? 110.530 103.613 196.131 1.00 90.32  ? 49  LYS E CA    1 
ATOM   11554 C  C     . LYS E 3 49  ? 111.419 104.574 195.350 1.00 90.32  ? 49  LYS E C     1 
ATOM   11555 O  O     . LYS E 3 49  ? 112.487 104.940 195.828 1.00 90.32  ? 49  LYS E O     1 
ATOM   11556 C  CB    . LYS E 3 49  ? 111.133 102.207 196.060 1.00 90.32  ? 49  LYS E CB    1 
ATOM   11557 C  CG    . LYS E 3 49  ? 110.353 101.163 196.862 1.00 90.32  ? 49  LYS E CG    1 
ATOM   11558 C  CD    . LYS E 3 49  ? 111.119 99.840  196.812 1.00 90.32  ? 49  LYS E CD    1 
ATOM   11559 C  CE    . LYS E 3 49  ? 110.312 98.740  197.495 1.00 90.32  ? 49  LYS E CE    1 
ATOM   11560 N  NZ    . LYS E 3 49  ? 111.047 97.455  197.422 1.00 90.32  ? 49  LYS E NZ    1 
ATOM   11561 N  N     . LEU E 3 50  ? 110.987 104.946 194.150 1.00 93.16  ? 50  LEU E N     1 
ATOM   11562 C  CA    . LEU E 3 50  ? 111.695 105.809 193.226 1.00 93.16  ? 50  LEU E CA    1 
ATOM   11563 C  C     . LEU E 3 50  ? 110.818 107.009 192.895 1.00 93.16  ? 50  LEU E C     1 
ATOM   11564 O  O     . LEU E 3 50  ? 109.676 106.851 192.470 1.00 93.16  ? 50  LEU E O     1 
ATOM   11565 C  CB    . LEU E 3 50  ? 112.012 105.000 191.957 1.00 93.16  ? 50  LEU E CB    1 
ATOM   11566 C  CG    . LEU E 3 50  ? 112.750 105.814 190.880 1.00 93.16  ? 50  LEU E CG    1 
ATOM   11567 C  CD1   . LEU E 3 50  ? 114.135 106.230 191.375 1.00 93.16  ? 50  LEU E CD1   1 
ATOM   11568 C  CD2   . LEU E 3 50  ? 112.828 105.001 189.588 1.00 93.16  ? 50  LEU E CD2   1 
ATOM   11569 N  N     . LYS E 3 51  ? 111.383 108.206 193.005 1.00 94.28  ? 51  LYS E N     1 
ATOM   11570 C  CA    . LYS E 3 51  ? 110.779 109.404 192.428 1.00 94.28  ? 51  LYS E CA    1 
ATOM   11571 C  C     . LYS E 3 51  ? 111.396 109.669 191.064 1.00 94.28  ? 51  LYS E C     1 
ATOM   11572 O  O     . LYS E 3 51  ? 112.616 109.649 190.926 1.00 94.28  ? 51  LYS E O     1 
ATOM   11573 C  CB    . LYS E 3 51  ? 110.976 110.551 193.411 1.00 94.28  ? 51  LYS E CB    1 
ATOM   11574 C  CG    . LYS E 3 51  ? 110.212 111.814 193.011 1.00 94.28  ? 51  LYS E CG    1 
ATOM   11575 C  CD    . LYS E 3 51  ? 110.497 112.864 194.081 1.00 94.28  ? 51  LYS E CD    1 
ATOM   11576 C  CE    . LYS E 3 51  ? 109.755 114.162 193.803 1.00 94.28  ? 51  LYS E CE    1 
ATOM   11577 N  NZ    . LYS E 3 51  ? 110.136 115.157 194.824 1.00 94.28  ? 51  LYS E NZ    1 
ATOM   11578 N  N     . ILE E 3 52  ? 110.578 109.948 190.057 1.00 96.24  ? 52  ILE E N     1 
ATOM   11579 C  CA    . ILE E 3 52  ? 111.070 110.344 188.735 1.00 96.24  ? 52  ILE E CA    1 
ATOM   11580 C  C     . ILE E 3 52  ? 110.821 111.838 188.551 1.00 96.24  ? 52  ILE E C     1 
ATOM   11581 O  O     . ILE E 3 52  ? 109.694 112.317 188.697 1.00 96.24  ? 52  ILE E O     1 
ATOM   11582 C  CB    . ILE E 3 52  ? 110.469 109.470 187.619 1.00 96.24  ? 52  ILE E CB    1 
ATOM   11583 C  CG1   . ILE E 3 52  ? 110.763 107.976 187.900 1.00 96.24  ? 52  ILE E CG1   1 
ATOM   11584 C  CG2   . ILE E 3 52  ? 111.036 109.899 186.250 1.00 96.24  ? 52  ILE E CG2   1 
ATOM   11585 C  CD1   . ILE E 3 52  ? 110.294 107.019 186.800 1.00 96.24  ? 52  ILE E CD1   1 
ATOM   11586 N  N     . VAL E 3 53  ? 111.883 112.572 188.234 1.00 96.81  ? 53  VAL E N     1 
ATOM   11587 C  CA    . VAL E 3 53  ? 111.859 114.017 187.993 1.00 96.81  ? 53  VAL E CA    1 
ATOM   11588 C  C     . VAL E 3 53  ? 112.306 114.270 186.559 1.00 96.81  ? 53  VAL E C     1 
ATOM   11589 O  O     . VAL E 3 53  ? 113.337 113.770 186.138 1.00 96.81  ? 53  VAL E O     1 
ATOM   11590 C  CB    . VAL E 3 53  ? 112.745 114.758 189.014 1.00 96.81  ? 53  VAL E CB    1 
ATOM   11591 C  CG1   . VAL E 3 53  ? 112.817 116.258 188.708 1.00 96.81  ? 53  VAL E CG1   1 
ATOM   11592 C  CG2   . VAL E 3 53  ? 112.197 114.610 190.441 1.00 96.81  ? 53  VAL E CG2   1 
ATOM   11593 N  N     . LYS E 3 54  ? 111.558 115.055 185.788 1.00 96.68  ? 54  LYS E N     1 
ATOM   11594 C  CA    . LYS E 3 54  ? 111.942 115.499 184.442 1.00 96.68  ? 54  LYS E CA    1 
ATOM   11595 C  C     . LYS E 3 54  ? 112.259 116.985 184.469 1.00 96.68  ? 54  LYS E C     1 
ATOM   11596 O  O     . LYS E 3 54  ? 111.480 117.761 185.021 1.00 96.68  ? 54  LYS E O     1 
ATOM   11597 C  CB    . LYS E 3 54  ? 110.828 115.191 183.432 1.00 96.68  ? 54  LYS E CB    1 
ATOM   11598 C  CG    . LYS E 3 54  ? 110.668 113.687 183.165 1.00 96.68  ? 54  LYS E CG    1 
ATOM   11599 C  CD    . LYS E 3 54  ? 109.575 113.401 182.125 1.00 96.68  ? 54  LYS E CD    1 
ATOM   11600 C  CE    . LYS E 3 54  ? 110.004 113.725 180.685 1.00 96.68  ? 54  LYS E CE    1 
ATOM   11601 N  NZ    . LYS E 3 54  ? 110.769 112.612 180.078 1.00 96.68  ? 54  LYS E NZ    1 
ATOM   11602 N  N     . ILE E 3 55  ? 113.343 117.389 183.821 1.00 96.24  ? 55  ILE E N     1 
ATOM   11603 C  CA    . ILE E 3 55  ? 113.734 118.793 183.673 1.00 96.24  ? 55  ILE E CA    1 
ATOM   11604 C  C     . ILE E 3 55  ? 114.060 119.094 182.210 1.00 96.24  ? 55  ILE E C     1 
ATOM   11605 O  O     . ILE E 3 55  ? 114.873 118.413 181.586 1.00 96.24  ? 55  ILE E O     1 
ATOM   11606 C  CB    . ILE E 3 55  ? 114.866 119.148 184.656 1.00 96.24  ? 55  ILE E CB    1 
ATOM   11607 C  CG1   . ILE E 3 55  ? 115.142 120.663 184.584 1.00 96.24  ? 55  ILE E CG1   1 
ATOM   11608 C  CG2   . ILE E 3 55  ? 116.143 118.316 184.433 1.00 96.24  ? 55  ILE E CG2   1 
ATOM   11609 C  CD1   . ILE E 3 55  ? 116.001 121.165 185.743 1.00 96.24  ? 55  ILE E CD1   1 
ATOM   11610 N  N     . ASP E 3 56  ? 113.368 120.085 181.651 1.00 95.13  ? 56  ASP E N     1 
ATOM   11611 C  CA    . ASP E 3 56  ? 113.588 120.522 180.272 1.00 95.13  ? 56  ASP E CA    1 
ATOM   11612 C  C     . ASP E 3 56  ? 114.813 121.439 180.215 1.00 95.13  ? 56  ASP E C     1 
ATOM   11613 O  O     . ASP E 3 56  ? 114.799 122.529 180.794 1.00 95.13  ? 56  ASP E O     1 
ATOM   11614 C  CB    . ASP E 3 56  ? 112.328 121.210 179.724 1.00 95.13  ? 56  ASP E CB    1 
ATOM   11615 C  CG    . ASP E 3 56  ? 112.410 121.464 178.213 1.00 95.13  ? 56  ASP E CG    1 
ATOM   11616 O  OD1   . ASP E 3 56  ? 113.540 121.530 177.675 1.00 95.13  ? 56  ASP E OD1   1 
ATOM   11617 O  OD2   . ASP E 3 56  ? 111.329 121.515 177.587 1.00 95.13  ? 56  ASP E OD2   1 
ATOM   11618 N  N     . VAL E 3 57  ? 115.870 121.007 179.530 1.00 94.14  ? 57  VAL E N     1 
ATOM   11619 C  CA    . VAL E 3 57  ? 117.136 121.751 179.434 1.00 94.14  ? 57  VAL E CA    1 
ATOM   11620 C  C     . VAL E 3 57  ? 117.035 123.007 178.567 1.00 94.14  ? 57  VAL E C     1 
ATOM   11621 O  O     . VAL E 3 57  ? 117.896 123.880 178.675 1.00 94.14  ? 57  VAL E O     1 
ATOM   11622 C  CB    . VAL E 3 57  ? 118.288 120.861 178.935 1.00 94.14  ? 57  VAL E CB    1 
ATOM   11623 C  CG1   . VAL E 3 57  ? 118.460 119.624 179.821 1.00 94.14  ? 57  VAL E CG1   1 
ATOM   11624 C  CG2   . VAL E 3 57  ? 118.113 120.405 177.485 1.00 94.14  ? 57  VAL E CG2   1 
ATOM   11625 N  N     . ASP E 3 58  ? 116.003 123.128 177.727 1.00 91.19  ? 58  ASP E N     1 
ATOM   11626 C  CA    . ASP E 3 58  ? 115.760 124.341 176.937 1.00 91.19  ? 58  ASP E CA    1 
ATOM   11627 C  C     . ASP E 3 58  ? 115.173 125.479 177.781 1.00 91.19  ? 58  ASP E C     1 
ATOM   11628 O  O     . ASP E 3 58  ? 115.308 126.647 177.410 1.00 91.19  ? 58  ASP E O     1 
ATOM   11629 C  CB    . ASP E 3 58  ? 114.773 124.059 175.797 1.00 91.19  ? 58  ASP E CB    1 
ATOM   11630 C  CG    . ASP E 3 58  ? 115.355 123.408 174.550 1.00 91.19  ? 58  ASP E CG    1 
ATOM   11631 O  OD1   . ASP E 3 58  ? 116.589 123.268 174.391 1.00 91.19  ? 58  ASP E OD1   1 
ATOM   11632 O  OD2   . ASP E 3 58  ? 114.555 123.207 173.612 1.00 91.19  ? 58  ASP E OD2   1 
ATOM   11633 N  N     . GLU E 3 59  ? 114.502 125.153 178.884 1.00 92.47  ? 59  GLU E N     1 
ATOM   11634 C  CA    . GLU E 3 59  ? 113.883 126.131 179.788 1.00 92.47  ? 59  GLU E CA    1 
ATOM   11635 C  C     . GLU E 3 59  ? 114.643 126.277 181.113 1.00 92.47  ? 59  GLU E C     1 
ATOM   11636 O  O     . GLU E 3 59  ? 114.401 127.234 181.842 1.00 92.47  ? 59  GLU E O     1 
ATOM   11637 C  CB    . GLU E 3 59  ? 112.406 125.770 180.031 1.00 92.47  ? 59  GLU E CB    1 
ATOM   11638 C  CG    . GLU E 3 59  ? 111.566 125.786 178.742 1.00 92.47  ? 59  GLU E CG    1 
ATOM   11639 C  CD    . GLU E 3 59  ? 110.047 125.728 178.993 1.00 92.47  ? 59  GLU E CD    1 
ATOM   11640 O  OE1   . GLU E 3 59  ? 109.302 126.196 178.095 1.00 92.47  ? 59  GLU E OE1   1 
ATOM   11641 O  OE2   . GLU E 3 59  ? 109.619 125.259 180.074 1.00 92.47  ? 59  GLU E OE2   1 
ATOM   11642 N  N     . ASN E 3 60  ? 115.542 125.335 181.423 1.00 94.69  ? 60  ASN E N     1 
ATOM   11643 C  CA    . ASN E 3 60  ? 116.224 125.228 182.713 1.00 94.69  ? 60  ASN E CA    1 
ATOM   11644 C  C     . ASN E 3 60  ? 117.728 124.970 182.527 1.00 94.69  ? 60  ASN E C     1 
ATOM   11645 O  O     . ASN E 3 60  ? 118.275 123.915 182.879 1.00 94.69  ? 60  ASN E O     1 
ATOM   11646 C  CB    . ASN E 3 60  ? 115.537 124.156 183.566 1.00 94.69  ? 60  ASN E CB    1 
ATOM   11647 C  CG    . ASN E 3 60  ? 114.057 124.409 183.730 1.00 94.69  ? 60  ASN E CG    1 
ATOM   11648 O  OD1   . ASN E 3 60  ? 113.616 125.167 184.578 1.00 94.69  ? 60  ASN E OD1   1 
ATOM   11649 N  ND2   . ASN E 3 60  ? 113.245 123.765 182.925 1.00 94.69  ? 60  ASN E ND2   1 
ATOM   11650 N  N     . GLN E 3 61  ? 118.399 125.917 181.872 1.00 94.07  ? 61  GLN E N     1 
ATOM   11651 C  CA    . GLN E 3 61  ? 119.815 125.807 181.535 1.00 94.07  ? 61  GLN E CA    1 
ATOM   11652 C  C     . GLN E 3 61  ? 120.726 125.835 182.769 1.00 94.07  ? 61  GLN E C     1 
ATOM   11653 O  O     . GLN E 3 61  ? 121.816 125.258 182.712 1.00 94.07  ? 61  GLN E O     1 
ATOM   11654 C  CB    . GLN E 3 61  ? 120.234 126.954 180.607 1.00 94.07  ? 61  GLN E CB    1 
ATOM   11655 C  CG    . GLN E 3 61  ? 119.612 126.951 179.210 1.00 94.07  ? 61  GLN E CG    1 
ATOM   11656 C  CD    . GLN E 3 61  ? 118.238 127.593 179.100 1.00 94.07  ? 61  GLN E CD    1 
ATOM   11657 O  OE1   . GLN E 3 61  ? 117.592 127.982 180.056 1.00 94.07  ? 61  GLN E OE1   1 
ATOM   11658 N  NE2   . GLN E 3 61  ? 117.767 127.743 177.887 1.00 94.07  ? 61  GLN E NE2   1 
ATOM   11659 N  N     . GLU E 3 62  ? 120.325 126.485 183.870 1.00 94.65  ? 62  GLU E N     1 
ATOM   11660 C  CA    . GLU E 3 62  ? 121.189 126.632 185.049 1.00 94.65  ? 62  GLU E CA    1 
ATOM   11661 C  C     . GLU E 3 62  ? 121.417 125.283 185.736 1.00 94.65  ? 62  GLU E C     1 
ATOM   11662 O  O     . GLU E 3 62  ? 122.559 124.924 186.038 1.00 94.65  ? 62  GLU E O     1 
ATOM   11663 C  CB    . GLU E 3 62  ? 120.631 127.656 186.054 1.00 94.65  ? 62  GLU E CB    1 
ATOM   11664 C  CG    . GLU E 3 62  ? 120.547 129.085 185.489 1.00 94.65  ? 62  GLU E CG    1 
ATOM   11665 C  CD    . GLU E 3 62  ? 120.135 130.151 186.526 1.00 94.65  ? 62  GLU E CD    1 
ATOM   11666 O  OE1   . GLU E 3 62  ? 120.199 131.355 186.167 1.00 94.65  ? 62  GLU E OE1   1 
ATOM   11667 O  OE2   . GLU E 3 62  ? 119.820 129.783 187.682 1.00 94.65  ? 62  GLU E OE2   1 
ATOM   11668 N  N     . THR E 3 63  ? 120.365 124.485 185.916 1.00 95.30  ? 63  THR E N     1 
ATOM   11669 C  CA    . THR E 3 63  ? 120.461 123.143 186.505 1.00 95.30  ? 63  THR E CA    1 
ATOM   11670 C  C     . THR E 3 63  ? 121.242 122.212 185.596 1.00 95.30  ? 63  THR E C     1 
ATOM   11671 O  O     . THR E 3 63  ? 122.147 121.519 186.063 1.00 95.30  ? 63  THR E O     1 
ATOM   11672 C  CB    . THR E 3 63  ? 119.079 122.543 186.775 1.00 95.30  ? 63  THR E CB    1 
ATOM   11673 O  OG1   . THR E 3 63  ? 118.388 123.371 187.661 1.00 95.30  ? 63  THR E OG1   1 
ATOM   11674 C  CG2   . THR E 3 63  ? 119.155 121.194 187.477 1.00 95.30  ? 63  THR E CG2   1 
ATOM   11675 N  N     . ALA E 3 64  ? 120.957 122.216 184.291 1.00 93.68  ? 64  ALA E N     1 
ATOM   11676 C  CA    . ALA E 3 64  ? 121.711 121.407 183.337 1.00 93.68  ? 64  ALA E CA    1 
ATOM   11677 C  C     . ALA E 3 64  ? 123.212 121.749 183.381 1.00 93.68  ? 64  ALA E C     1 
ATOM   11678 O  O     . ALA E 3 64  ? 124.054 120.851 183.437 1.00 93.68  ? 64  ALA E O     1 
ATOM   11679 C  CB    . ALA E 3 64  ? 121.092 121.609 181.954 1.00 93.68  ? 64  ALA E CB    1 
ATOM   11680 N  N     . GLY E 3 65  ? 123.544 123.040 183.469 1.00 91.87  ? 65  GLY E N     1 
ATOM   11681 C  CA    . GLY E 3 65  ? 124.911 123.521 183.650 1.00 91.87  ? 65  GLY E CA    1 
ATOM   11682 C  C     . GLY E 3 65  ? 125.541 123.104 184.983 1.00 91.87  ? 65  GLY E C     1 
ATOM   11683 O  O     . GLY E 3 65  ? 126.683 122.640 184.998 1.00 91.87  ? 65  GLY E O     1 
ATOM   11684 N  N     . LYS E 3 66  ? 124.803 123.208 186.097 1.00 93.09  ? 66  LYS E N     1 
ATOM   11685 C  CA    . LYS E 3 66  ? 125.253 122.821 187.449 1.00 93.09  ? 66  LYS E CA    1 
ATOM   11686 C  C     . LYS E 3 66  ? 125.668 121.352 187.517 1.00 93.09  ? 66  LYS E C     1 
ATOM   11687 O  O     . LYS E 3 66  ? 126.687 121.036 188.127 1.00 93.09  ? 66  LYS E O     1 
ATOM   11688 C  CB    . LYS E 3 66  ? 124.125 123.115 188.453 1.00 93.09  ? 66  LYS E CB    1 
ATOM   11689 C  CG    . LYS E 3 66  ? 124.507 122.785 189.907 1.00 93.09  ? 66  LYS E CG    1 
ATOM   11690 C  CD    . LYS E 3 66  ? 123.298 122.966 190.834 1.00 93.09  ? 66  LYS E CD    1 
ATOM   11691 C  CE    . LYS E 3 66  ? 123.655 122.555 192.267 1.00 93.09  ? 66  LYS E CE    1 
ATOM   11692 N  NZ    . LYS E 3 66  ? 122.449 122.526 193.134 1.00 93.09  ? 66  LYS E NZ    1 
ATOM   11693 N  N     . TYR E 3 67  ? 124.900 120.471 186.883 1.00 91.99  ? 67  TYR E N     1 
ATOM   11694 C  CA    . TYR E 3 67  ? 125.198 119.039 186.822 1.00 91.99  ? 67  TYR E CA    1 
ATOM   11695 C  C     . TYR E 3 67  ? 126.097 118.654 185.633 1.00 91.99  ? 67  TYR E C     1 
ATOM   11696 O  O     . TYR E 3 67  ? 126.390 117.477 185.439 1.00 91.99  ? 67  TYR E O     1 
ATOM   11697 C  CB    . TYR E 3 67  ? 123.891 118.240 186.896 1.00 91.99  ? 67  TYR E CB    1 
ATOM   11698 C  CG    . TYR E 3 67  ? 123.217 118.334 188.254 1.00 91.99  ? 67  TYR E CG    1 
ATOM   11699 C  CD1   . TYR E 3 67  ? 123.666 117.531 189.319 1.00 91.99  ? 67  TYR E CD1   1 
ATOM   11700 C  CD2   . TYR E 3 67  ? 122.166 119.242 188.471 1.00 91.99  ? 67  TYR E CD2   1 
ATOM   11701 C  CE1   . TYR E 3 67  ? 123.065 117.630 190.591 1.00 91.99  ? 67  TYR E CE1   1 
ATOM   11702 C  CE2   . TYR E 3 67  ? 121.588 119.374 189.746 1.00 91.99  ? 67  TYR E CE2   1 
ATOM   11703 C  CZ    . TYR E 3 67  ? 122.028 118.561 190.807 1.00 91.99  ? 67  TYR E CZ    1 
ATOM   11704 O  OH    . TYR E 3 67  ? 121.458 118.691 192.035 1.00 91.99  ? 67  TYR E OH    1 
ATOM   11705 N  N     . GLY E 3 68  ? 126.578 119.632 184.854 1.00 87.95  ? 68  GLY E N     1 
ATOM   11706 C  CA    . GLY E 3 68  ? 127.503 119.411 183.741 1.00 87.95  ? 68  GLY E CA    1 
ATOM   11707 C  C     . GLY E 3 68  ? 126.906 118.602 182.589 1.00 87.95  ? 68  GLY E C     1 
ATOM   11708 O  O     . GLY E 3 68  ? 127.643 117.915 181.879 1.00 87.95  ? 68  GLY E O     1 
ATOM   11709 N  N     . VAL E 3 69  ? 125.586 118.658 182.412 1.00 88.85  ? 69  VAL E N     1 
ATOM   11710 C  CA    . VAL E 3 69  ? 124.880 117.966 181.336 1.00 88.85  ? 69  VAL E CA    1 
ATOM   11711 C  C     . VAL E 3 69  ? 125.221 118.651 180.013 1.00 88.85  ? 69  VAL E C     1 
ATOM   11712 O  O     . VAL E 3 69  ? 125.009 119.846 179.840 1.00 88.85  ? 69  VAL E O     1 
ATOM   11713 C  CB    . VAL E 3 69  ? 123.360 117.924 181.603 1.00 88.85  ? 69  VAL E CB    1 
ATOM   11714 C  CG1   . VAL E 3 69  ? 122.636 117.122 180.518 1.00 88.85  ? 69  VAL E CG1   1 
ATOM   11715 C  CG2   . VAL E 3 69  ? 123.061 117.253 182.951 1.00 88.85  ? 69  VAL E CG2   1 
ATOM   11716 N  N     . MET E 3 70  ? 125.766 117.885 179.067 1.00 88.20  ? 70  MET E N     1 
ATOM   11717 C  CA    . MET E 3 70  ? 126.106 118.355 177.712 1.00 88.20  ? 70  MET E CA    1 
ATOM   11718 C  C     . MET E 3 70  ? 125.432 117.523 176.615 1.00 88.20  ? 70  MET E C     1 
ATOM   11719 O  O     . MET E 3 70  ? 125.600 117.769 175.424 1.00 88.20  ? 70  MET E O     1 
ATOM   11720 C  CB    . MET E 3 70  ? 127.626 118.342 177.510 1.00 88.20  ? 70  MET E CB    1 
ATOM   11721 C  CG    . MET E 3 70  ? 128.365 119.363 178.380 1.00 88.20  ? 70  MET E CG    1 
ATOM   11722 S  SD    . MET E 3 70  ? 130.158 119.406 178.076 1.00 88.20  ? 70  MET E SD    1 
ATOM   11723 C  CE    . MET E 3 70  ? 130.646 117.899 178.943 1.00 88.20  ? 70  MET E CE    1 
ATOM   11724 N  N     . SER E 3 71  ? 124.684 116.499 177.008 1.00 88.10  ? 71  SER E N     1 
ATOM   11725 C  CA    . SER E 3 71  ? 123.952 115.632 176.098 1.00 88.10  ? 71  SER E CA    1 
ATOM   11726 C  C     . SER E 3 71  ? 122.640 115.203 176.733 1.00 88.10  ? 71  SER E C     1 
ATOM   11727 O  O     . SER E 3 71  ? 122.495 115.228 177.954 1.00 88.10  ? 71  SER E O     1 
ATOM   11728 C  CB    . SER E 3 71  ? 124.792 114.422 175.691 1.00 88.10  ? 71  SER E CB    1 
ATOM   11729 O  OG    . SER E 3 71  ? 125.268 113.723 176.822 1.00 88.10  ? 71  SER E OG    1 
ATOM   11730 N  N     . ILE E 3 72  ? 121.670 114.850 175.901 1.00 90.57  ? 72  ILE E N     1 
ATOM   11731 C  CA    . ILE E 3 72  ? 120.333 114.442 176.305 1.00 90.57  ? 72  ILE E CA    1 
ATOM   11732 C  C     . ILE E 3 72  ? 119.862 113.225 175.481 1.00 90.57  ? 72  ILE E C     1 
ATOM   11733 O  O     . ILE E 3 72  ? 120.192 113.125 174.295 1.00 90.57  ? 72  ILE E O     1 
ATOM   11734 C  CB    . ILE E 3 72  ? 119.336 115.620 176.249 1.00 90.57  ? 72  ILE E CB    1 
ATOM   11735 C  CG1   . ILE E 3 72  ? 119.338 116.314 174.871 1.00 90.57  ? 72  ILE E CG1   1 
ATOM   11736 C  CG2   . ILE E 3 72  ? 119.621 116.619 177.383 1.00 90.57  ? 72  ILE E CG2   1 
ATOM   11737 C  CD1   . ILE E 3 72  ? 118.233 117.361 174.744 1.00 90.57  ? 72  ILE E CD1   1 
ATOM   11738 N  N     . PRO E 3 73  ? 119.084 112.303 176.074 1.00 93.49  ? 73  PRO E N     1 
ATOM   11739 C  CA    . PRO E 3 73  ? 118.718 112.289 177.484 1.00 93.49  ? 73  PRO E CA    1 
ATOM   11740 C  C     . PRO E 3 73  ? 119.938 111.976 178.361 1.00 93.49  ? 73  PRO E C     1 
ATOM   11741 O  O     . PRO E 3 73  ? 120.770 111.134 178.020 1.00 93.49  ? 73  PRO E O     1 
ATOM   11742 C  CB    . PRO E 3 73  ? 117.614 111.241 177.621 1.00 93.49  ? 73  PRO E CB    1 
ATOM   11743 C  CG    . PRO E 3 73  ? 117.956 110.249 176.513 1.00 93.49  ? 73  PRO E CG    1 
ATOM   11744 C  CD    . PRO E 3 73  ? 118.535 111.136 175.411 1.00 93.49  ? 73  PRO E CD    1 
ATOM   11745 N  N     . THR E 3 74  ? 120.047 112.683 179.480 1.00 93.65  ? 74  THR E N     1 
ATOM   11746 C  CA    . THR E 3 74  ? 120.968 112.332 180.564 1.00 93.65  ? 74  THR E CA    1 
ATOM   11747 C  C     . THR E 3 74  ? 120.125 112.030 181.783 1.00 93.65  ? 74  THR E C     1 
ATOM   11748 O  O     . THR E 3 74  ? 119.326 112.855 182.218 1.00 93.65  ? 74  THR E O     1 
ATOM   11749 C  CB    . THR E 3 74  ? 122.005 113.425 180.858 1.00 93.65  ? 74  THR E CB    1 
ATOM   11750 O  OG1   . THR E 3 74  ? 122.979 113.440 179.841 1.00 93.65  ? 74  THR E OG1   1 
ATOM   11751 C  CG2   . THR E 3 74  ? 122.789 113.169 182.146 1.00 93.65  ? 74  THR E CG2   1 
ATOM   11752 N  N     . LEU E 3 75  ? 120.313 110.837 182.327 1.00 95.19  ? 75  LEU E N     1 
ATOM   11753 C  CA    . LEU E 3 75  ? 119.651 110.361 183.523 1.00 95.19  ? 75  LEU E CA    1 
ATOM   11754 C  C     . LEU E 3 75  ? 120.632 110.398 184.691 1.00 95.19  ? 75  LEU E C     1 
ATOM   11755 O  O     . LEU E 3 75  ? 121.670 109.732 184.653 1.00 95.19  ? 75  LEU E O     1 
ATOM   11756 C  CB    . LEU E 3 75  ? 119.128 108.945 183.284 1.00 95.19  ? 75  LEU E CB    1 
ATOM   11757 C  CG    . LEU E 3 75  ? 118.076 108.812 182.172 1.00 95.19  ? 75  LEU E CG    1 
ATOM   11758 C  CD1   . LEU E 3 75  ? 117.709 107.345 182.087 1.00 95.19  ? 75  LEU E CD1   1 
ATOM   11759 C  CD2   . LEU E 3 75  ? 116.805 109.598 182.448 1.00 95.19  ? 75  LEU E CD2   1 
ATOM   11760 N  N     . LEU E 3 76  ? 120.296 111.151 185.732 1.00 95.47  ? 76  LEU E N     1 
ATOM   11761 C  CA    . LEU E 3 76  ? 121.037 111.165 186.990 1.00 95.47  ? 76  LEU E CA    1 
ATOM   11762 C  C     . LEU E 3 76  ? 120.253 110.381 188.035 1.00 95.47  ? 76  LEU E C     1 
ATOM   11763 O  O     . LEU E 3 76  ? 119.077 110.662 188.261 1.00 95.47  ? 76  LEU E O     1 
ATOM   11764 C  CB    . LEU E 3 76  ? 121.308 112.607 187.453 1.00 95.47  ? 76  LEU E CB    1 
ATOM   11765 C  CG    . LEU E 3 76  ? 122.015 113.509 186.429 1.00 95.47  ? 76  LEU E CG    1 
ATOM   11766 C  CD1   . LEU E 3 76  ? 122.330 114.864 187.062 1.00 95.47  ? 76  LEU E CD1   1 
ATOM   11767 C  CD2   . LEU E 3 76  ? 123.331 112.917 185.940 1.00 95.47  ? 76  LEU E CD2   1 
ATOM   11768 N  N     . VAL E 3 77  ? 120.906 109.428 188.696 1.00 96.40  ? 77  VAL E N     1 
ATOM   11769 C  CA    . VAL E 3 77  ? 120.384 108.854 189.939 1.00 96.40  ? 77  VAL E CA    1 
ATOM   11770 C  C     . VAL E 3 77  ? 120.931 109.698 191.070 1.00 96.40  ? 77  VAL E C     1 
ATOM   11771 O  O     . VAL E 3 77  ? 122.149 109.781 191.251 1.00 96.40  ? 77  VAL E O     1 
ATOM   11772 C  CB    . VAL E 3 77  ? 120.752 107.376 190.131 1.00 96.40  ? 77  VAL E CB    1 
ATOM   11773 C  CG1   . VAL E 3 77  ? 120.068 106.798 191.378 1.00 96.40  ? 77  VAL E CG1   1 
ATOM   11774 C  CG2   . VAL E 3 77  ? 120.288 106.544 188.941 1.00 96.40  ? 77  VAL E CG2   1 
ATOM   11775 N  N     . LEU E 3 78  ? 120.034 110.332 191.812 1.00 96.12  ? 78  LEU E N     1 
ATOM   11776 C  CA    . LEU E 3 78  ? 120.361 111.060 193.024 1.00 96.12  ? 78  LEU E CA    1 
ATOM   11777 C  C     . LEU E 3 78  ? 119.885 110.268 194.237 1.00 96.12  ? 78  LEU E C     1 
ATOM   11778 O  O     . LEU E 3 78  ? 118.804 109.680 194.209 1.00 96.12  ? 78  LEU E O     1 
ATOM   11779 C  CB    . LEU E 3 78  ? 119.803 112.494 193.008 1.00 96.12  ? 78  LEU E CB    1 
ATOM   11780 C  CG    . LEU E 3 78  ? 120.283 113.327 191.802 1.00 96.12  ? 78  LEU E CG    1 
ATOM   11781 C  CD1   . LEU E 3 78  ? 119.234 113.363 190.688 1.00 96.12  ? 78  LEU E CD1   1 
ATOM   11782 C  CD2   . LEU E 3 78  ? 120.574 114.773 192.209 1.00 96.12  ? 78  LEU E CD2   1 
ATOM   11783 N  N     . LYS E 3 79  ? 120.686 110.274 195.298 1.00 95.93  ? 79  LYS E N     1 
ATOM   11784 C  CA    . LYS E 3 79  ? 120.320 109.754 196.611 1.00 95.93  ? 79  LYS E CA    1 
ATOM   11785 C  C     . LYS E 3 79  ? 120.553 110.843 197.644 1.00 95.93  ? 79  LYS E C     1 
ATOM   11786 O  O     . LYS E 3 79  ? 121.678 111.315 197.779 1.00 95.93  ? 79  LYS E O     1 
ATOM   11787 C  CB    . LYS E 3 79  ? 121.107 108.474 196.904 1.00 95.93  ? 79  LYS E CB    1 
ATOM   11788 C  CG    . LYS E 3 79  ? 120.630 107.834 198.215 1.00 95.93  ? 79  LYS E CG    1 
ATOM   11789 C  CD    . LYS E 3 79  ? 121.200 106.421 198.355 1.00 95.93  ? 79  LYS E CD    1 
ATOM   11790 C  CE    . LYS E 3 79  ? 120.592 105.744 199.586 1.00 95.93  ? 79  LYS E CE    1 
ATOM   11791 N  NZ    . LYS E 3 79  ? 120.668 104.266 199.469 1.00 95.93  ? 79  LYS E NZ    1 
ATOM   11792 N  N     . ASP E 3 80  ? 119.488 111.262 198.320 1.00 94.33  ? 80  ASP E N     1 
ATOM   11793 C  CA    . ASP E 3 80  ? 119.532 112.304 199.356 1.00 94.33  ? 80  ASP E CA    1 
ATOM   11794 C  C     . ASP E 3 80  ? 120.262 113.586 198.886 1.00 94.33  ? 80  ASP E C     1 
ATOM   11795 O  O     . ASP E 3 80  ? 121.078 114.175 199.593 1.00 94.33  ? 80  ASP E O     1 
ATOM   11796 C  CB    . ASP E 3 80  ? 120.055 111.709 200.676 1.00 94.33  ? 80  ASP E CB    1 
ATOM   11797 C  CG    . ASP E 3 80  ? 119.242 110.486 201.123 1.00 94.33  ? 80  ASP E CG    1 
ATOM   11798 O  OD1   . ASP E 3 80  ? 117.990 110.575 201.104 1.00 94.33  ? 80  ASP E OD1   1 
ATOM   11799 O  OD2   . ASP E 3 80  ? 119.867 109.448 201.456 1.00 94.33  ? 80  ASP E OD2   1 
ATOM   11800 N  N     . GLY E 3 81  ? 119.998 113.994 197.638 1.00 93.05  ? 81  GLY E N     1 
ATOM   11801 C  CA    . GLY E 3 81  ? 120.581 115.184 197.010 1.00 93.05  ? 81  GLY E CA    1 
ATOM   11802 C  C     . GLY E 3 81  ? 121.919 114.988 196.288 1.00 93.05  ? 81  GLY E C     1 
ATOM   11803 O  O     . GLY E 3 81  ? 122.284 115.850 195.483 1.00 93.05  ? 81  GLY E O     1 
ATOM   11804 N  N     . GLU E 3 82  ? 122.635 113.878 196.495 1.00 95.02  ? 82  GLU E N     1 
ATOM   11805 C  CA    . GLU E 3 82  ? 123.914 113.610 195.821 1.00 95.02  ? 82  GLU E CA    1 
ATOM   11806 C  C     . GLU E 3 82  ? 123.759 112.714 194.592 1.00 95.02  ? 82  GLU E C     1 
ATOM   11807 O  O     . GLU E 3 82  ? 123.025 111.729 194.611 1.00 95.02  ? 82  GLU E O     1 
ATOM   11808 C  CB    . GLU E 3 82  ? 124.960 113.019 196.774 1.00 95.02  ? 82  GLU E CB    1 
ATOM   11809 C  CG    . GLU E 3 82  ? 125.416 114.026 197.845 1.00 95.02  ? 82  GLU E CG    1 
ATOM   11810 C  CD    . GLU E 3 82  ? 126.894 113.876 198.253 1.00 95.02  ? 82  GLU E CD    1 
ATOM   11811 O  OE1   . GLU E 3 82  ? 127.430 114.854 198.826 1.00 95.02  ? 82  GLU E OE1   1 
ATOM   11812 O  OE2   . GLU E 3 82  ? 127.511 112.824 197.966 1.00 95.02  ? 82  GLU E OE2   1 
ATOM   11813 N  N     . VAL E 3 83  ? 124.478 113.030 193.510 1.00 95.68  ? 83  VAL E N     1 
ATOM   11814 C  CA    . VAL E 3 83  ? 124.498 112.202 192.295 1.00 95.68  ? 83  VAL E CA    1 
ATOM   11815 C  C     . VAL E 3 83  ? 125.356 110.964 192.543 1.00 95.68  ? 83  VAL E C     1 
ATOM   11816 O  O     . VAL E 3 83  ? 126.566 111.073 192.725 1.00 95.68  ? 83  VAL E O     1 
ATOM   11817 C  CB    . VAL E 3 83  ? 125.020 112.975 191.070 1.00 95.68  ? 83  VAL E CB    1 
ATOM   11818 C  CG1   . VAL E 3 83  ? 125.004 112.108 189.802 1.00 95.68  ? 83  VAL E CG1   1 
ATOM   11819 C  CG2   . VAL E 3 83  ? 124.165 114.214 190.790 1.00 95.68  ? 83  VAL E CG2   1 
ATOM   11820 N  N     . VAL E 3 84  ? 124.732 109.789 192.501 1.00 95.67  ? 84  VAL E N     1 
ATOM   11821 C  CA    . VAL E 3 84  ? 125.390 108.494 192.743 1.00 95.67  ? 84  VAL E CA    1 
ATOM   11822 C  C     . VAL E 3 84  ? 125.666 107.714 191.461 1.00 95.67  ? 84  VAL E C     1 
ATOM   11823 O  O     . VAL E 3 84  ? 126.607 106.925 191.412 1.00 95.67  ? 84  VAL E O     1 
ATOM   11824 C  CB    . VAL E 3 84  ? 124.592 107.639 193.743 1.00 95.67  ? 84  VAL E CB    1 
ATOM   11825 C  CG1   . VAL E 3 84  ? 124.599 108.279 195.134 1.00 95.67  ? 84  VAL E CG1   1 
ATOM   11826 C  CG2   . VAL E 3 84  ? 123.134 107.403 193.329 1.00 95.67  ? 84  VAL E CG2   1 
ATOM   11827 N  N     . GLU E 3 85  ? 124.887 107.941 190.401 1.00 94.20  ? 85  GLU E N     1 
ATOM   11828 C  CA    . GLU E 3 85  ? 125.108 107.316 189.094 1.00 94.20  ? 85  GLU E CA    1 
ATOM   11829 C  C     . GLU E 3 85  ? 124.632 108.250 187.971 1.00 94.20  ? 85  GLU E C     1 
ATOM   11830 O  O     . GLU E 3 85  ? 123.729 109.070 188.146 1.00 94.20  ? 85  GLU E O     1 
ATOM   11831 C  CB    . GLU E 3 85  ? 124.464 105.906 189.060 1.00 94.20  ? 85  GLU E CB    1 
ATOM   11832 C  CG    . GLU E 3 85  ? 125.101 104.936 188.030 1.00 94.20  ? 85  GLU E CG    1 
ATOM   11833 C  CD    . GLU E 3 85  ? 124.960 103.421 188.365 1.00 94.20  ? 85  GLU E CD    1 
ATOM   11834 O  OE1   . GLU E 3 85  ? 125.302 102.547 187.525 1.00 94.20  ? 85  GLU E OE1   1 
ATOM   11835 O  OE2   . GLU E 3 85  ? 124.546 103.070 189.487 1.00 94.20  ? 85  GLU E OE2   1 
ATOM   11836 N  N     . THR E 3 86  ? 125.268 108.162 186.806 1.00 92.29  ? 86  THR E N     1 
ATOM   11837 C  CA    . THR E 3 86  ? 124.935 108.957 185.616 1.00 92.29  ? 86  THR E CA    1 
ATOM   11838 C  C     . THR E 3 86  ? 124.871 108.031 184.416 1.00 92.29  ? 86  THR E C     1 
ATOM   11839 O  O     . THR E 3 86  ? 125.793 107.252 184.174 1.00 92.29  ? 86  THR E O     1 
ATOM   11840 C  CB    . THR E 3 86  ? 125.970 110.065 185.378 1.00 92.29  ? 86  THR E CB    1 
ATOM   11841 O  OG1   . THR E 3 86  ? 125.948 110.960 186.463 1.00 92.29  ? 86  THR E OG1   1 
ATOM   11842 C  CG2   . THR E 3 86  ? 125.726 110.868 184.098 1.00 92.29  ? 86  THR E CG2   1 
ATOM   11843 N  N     . SER E 3 87  ? 123.791 108.124 183.649 1.00 91.65  ? 87  SER E N     1 
ATOM   11844 C  CA    . SER E 3 87  ? 123.585 107.368 182.421 1.00 91.65  ? 87  SER E CA    1 
ATOM   11845 C  C     . SER E 3 87  ? 123.229 108.319 181.289 1.00 91.65  ? 87  SER E C     1 
ATOM   11846 O  O     . SER E 3 87  ? 122.317 109.127 181.413 1.00 91.65  ? 87  SER E O     1 
ATOM   11847 C  CB    . SER E 3 87  ? 122.502 106.314 182.638 1.00 91.65  ? 87  SER E CB    1 
ATOM   11848 O  OG    . SER E 3 87  ? 122.232 105.648 181.418 1.00 91.65  ? 87  SER E OG    1 
ATOM   11849 N  N     . VAL E 3 88  ? 123.934 108.201 180.170 1.00 89.96  ? 88  VAL E N     1 
ATOM   11850 C  CA    . VAL E 3 88  ? 123.741 109.049 178.990 1.00 89.96  ? 88  VAL E CA    1 
ATOM   11851 C  C     . VAL E 3 88  ? 123.156 108.217 177.854 1.00 89.96  ? 88  VAL E C     1 
ATOM   11852 O  O     . VAL E 3 88  ? 123.548 107.061 177.665 1.00 89.96  ? 88  VAL E O     1 
ATOM   11853 C  CB    . VAL E 3 88  ? 125.066 109.723 178.589 1.00 89.96  ? 88  VAL E CB    1 
ATOM   11854 C  CG1   . VAL E 3 88  ? 124.899 110.608 177.354 1.00 89.96  ? 88  VAL E CG1   1 
ATOM   11855 C  CG2   . VAL E 3 88  ? 125.611 110.596 179.728 1.00 89.96  ? 88  VAL E CG2   1 
ATOM   11856 N  N     . GLY E 3 89  ? 122.241 108.822 177.098 1.00 88.38  ? 89  GLY E N     1 
ATOM   11857 C  CA    . GLY E 3 89  ? 121.568 108.200 175.964 1.00 88.38  ? 89  GLY E CA    1 
ATOM   11858 C  C     . GLY E 3 89  ? 120.352 107.374 176.369 1.00 88.38  ? 89  GLY E C     1 
ATOM   11859 O  O     . GLY E 3 89  ? 119.960 107.310 177.540 1.00 88.38  ? 89  GLY E O     1 
ATOM   11860 N  N     . PHE E 3 90  ? 119.719 106.751 175.378 1.00 89.87  ? 90  PHE E N     1 
ATOM   11861 C  CA    . PHE E 3 90  ? 118.537 105.938 175.617 1.00 89.87  ? 90  PHE E CA    1 
ATOM   11862 C  C     . PHE E 3 90  ? 118.893 104.671 176.409 1.00 89.87  ? 90  PHE E C     1 
ATOM   11863 O  O     . PHE E 3 90  ? 119.927 104.032 176.196 1.00 89.87  ? 90  PHE E O     1 
ATOM   11864 C  CB    . PHE E 3 90  ? 117.850 105.628 174.282 1.00 89.87  ? 90  PHE E CB    1 
ATOM   11865 C  CG    . PHE E 3 90  ? 116.676 104.681 174.411 1.00 89.87  ? 90  PHE E CG    1 
ATOM   11866 C  CD1   . PHE E 3 90  ? 116.859 103.310 174.155 1.00 89.87  ? 90  PHE E CD1   1 
ATOM   11867 C  CD2   . PHE E 3 90  ? 115.420 105.155 174.833 1.00 89.87  ? 90  PHE E CD2   1 
ATOM   11868 C  CE1   . PHE E 3 90  ? 115.790 102.412 174.314 1.00 89.87  ? 90  PHE E CE1   1 
ATOM   11869 C  CE2   . PHE E 3 90  ? 114.351 104.255 174.994 1.00 89.87  ? 90  PHE E CE2   1 
ATOM   11870 C  CZ    . PHE E 3 90  ? 114.534 102.886 174.732 1.00 89.87  ? 90  PHE E CZ    1 
ATOM   11871 N  N     . LYS E 3 91  ? 118.005 104.275 177.324 1.00 90.76  ? 91  LYS E N     1 
ATOM   11872 C  CA    . LYS E 3 91  ? 118.108 103.020 178.072 1.00 90.76  ? 91  LYS E CA    1 
ATOM   11873 C  C     . LYS E 3 91  ? 116.744 102.330 178.120 1.00 90.76  ? 91  LYS E C     1 
ATOM   11874 O  O     . LYS E 3 91  ? 115.745 103.007 178.365 1.00 90.76  ? 91  LYS E O     1 
ATOM   11875 C  CB    . LYS E 3 91  ? 118.611 103.281 179.496 1.00 90.76  ? 91  LYS E CB    1 
ATOM   11876 C  CG    . LYS E 3 91  ? 120.043 103.821 179.609 1.00 90.76  ? 91  LYS E CG    1 
ATOM   11877 C  CD    . LYS E 3 91  ? 121.107 102.829 179.122 1.00 90.76  ? 91  LYS E CD    1 
ATOM   11878 C  CE    . LYS E 3 91  ? 122.481 103.491 179.227 1.00 90.76  ? 91  LYS E CE    1 
ATOM   11879 N  NZ    . LYS E 3 91  ? 123.521 102.697 178.538 1.00 90.76  ? 91  LYS E NZ    1 
ATOM   11880 N  N     . PRO E 3 92  ? 116.692 101.003 177.914 1.00 92.45  ? 92  PRO E N     1 
ATOM   11881 C  CA    . PRO E 3 92  ? 115.473 100.231 178.118 1.00 92.45  ? 92  PRO E CA    1 
ATOM   11882 C  C     . PRO E 3 92  ? 115.124 100.154 179.609 1.00 92.45  ? 92  PRO E C     1 
ATOM   11883 O  O     . PRO E 3 92  ? 115.972 100.406 180.473 1.00 92.45  ? 92  PRO E O     1 
ATOM   11884 C  CB    . PRO E 3 92  ? 115.770 98.855  177.521 1.00 92.45  ? 92  PRO E CB    1 
ATOM   11885 C  CG    . PRO E 3 92  ? 117.268 98.692  177.770 1.00 92.45  ? 92  PRO E CG    1 
ATOM   11886 C  CD    . PRO E 3 92  ? 117.801 100.113 177.593 1.00 92.45  ? 92  PRO E CD    1 
ATOM   11887 N  N     . LYS E 3 93  ? 113.883 99.765  179.908 1.00 93.12  ? 93  LYS E N     1 
ATOM   11888 C  CA    . LYS E 3 93  ? 113.351 99.727  181.275 1.00 93.12  ? 93  LYS E CA    1 
ATOM   11889 C  C     . LYS E 3 93  ? 114.210 98.880  182.204 1.00 93.12  ? 93  LYS E C     1 
ATOM   11890 O  O     . LYS E 3 93  ? 114.577 99.341  183.277 1.00 93.12  ? 93  LYS E O     1 
ATOM   11891 C  CB    . LYS E 3 93  ? 111.913 99.191  181.245 1.00 93.12  ? 93  LYS E CB    1 
ATOM   11892 C  CG    . LYS E 3 93  ? 111.267 99.286  182.637 1.00 93.12  ? 93  LYS E CG    1 
ATOM   11893 C  CD    . LYS E 3 93  ? 109.786 98.914  182.603 1.00 93.12  ? 93  LYS E CD    1 
ATOM   11894 C  CE    . LYS E 3 93  ? 109.553 97.448  182.237 1.00 93.12  ? 93  LYS E CE    1 
ATOM   11895 N  NZ    . LYS E 3 93  ? 108.103 97.222  182.058 1.00 93.12  ? 93  LYS E NZ    1 
ATOM   11896 N  N     . GLU E 3 94  ? 114.588 97.683  181.772 1.00 93.86  ? 94  GLU E N     1 
ATOM   11897 C  CA    . GLU E 3 94  ? 115.337 96.717  182.580 1.00 93.86  ? 94  GLU E CA    1 
ATOM   11898 C  C     . GLU E 3 94  ? 116.700 97.285  182.996 1.00 93.86  ? 94  GLU E C     1 
ATOM   11899 O  O     . GLU E 3 94  ? 117.119 97.133  184.141 1.00 93.86  ? 94  GLU E O     1 
ATOM   11900 C  CB    . GLU E 3 94  ? 115.547 95.410  181.793 1.00 93.86  ? 94  GLU E CB    1 
ATOM   11901 C  CG    . GLU E 3 94  ? 114.257 94.684  181.362 1.00 93.86  ? 94  GLU E CG    1 
ATOM   11902 C  CD    . GLU E 3 94  ? 113.478 95.371  180.223 1.00 93.86  ? 94  GLU E CD    1 
ATOM   11903 O  OE1   . GLU E 3 94  ? 112.263 95.108  180.111 1.00 93.86  ? 94  GLU E OE1   1 
ATOM   11904 O  OE2   . GLU E 3 94  ? 114.084 96.192  179.490 1.00 93.86  ? 94  GLU E OE2   1 
ATOM   11905 N  N     . ALA E 3 95  ? 117.360 98.015  182.091 1.00 94.25  ? 95  ALA E N     1 
ATOM   11906 C  CA    . ALA E 3 95  ? 118.630 98.669  182.385 1.00 94.25  ? 95  ALA E CA    1 
ATOM   11907 C  C     . ALA E 3 95  ? 118.464 99.823  183.386 1.00 94.25  ? 95  ALA E C     1 
ATOM   11908 O  O     . ALA E 3 95  ? 119.328 100.019 184.237 1.00 94.25  ? 95  ALA E O     1 
ATOM   11909 C  CB    . ALA E 3 95  ? 119.254 99.153  181.072 1.00 94.25  ? 95  ALA E CB    1 
ATOM   11910 N  N     . LEU E 3 96  ? 117.359 100.576 183.313 1.00 93.58  ? 96  LEU E N     1 
ATOM   11911 C  CA    . LEU E 3 96  ? 117.051 101.626 184.290 1.00 93.58  ? 96  LEU E CA    1 
ATOM   11912 C  C     . LEU E 3 96  ? 116.698 101.054 185.660 1.00 93.58  ? 96  LEU E C     1 
ATOM   11913 O  O     . LEU E 3 96  ? 117.137 101.592 186.673 1.00 93.58  ? 96  LEU E O     1 
ATOM   11914 C  CB    . LEU E 3 96  ? 115.912 102.521 183.773 1.00 93.58  ? 96  LEU E CB    1 
ATOM   11915 C  CG    . LEU E 3 96  ? 116.268 103.319 182.514 1.00 93.58  ? 96  LEU E CG    1 
ATOM   11916 C  CD1   . LEU E 3 96  ? 115.116 104.250 182.141 1.00 93.58  ? 96  LEU E CD1   1 
ATOM   11917 C  CD2   . LEU E 3 96  ? 117.524 104.154 182.742 1.00 93.58  ? 96  LEU E CD2   1 
ATOM   11918 N  N     . GLN E 3 97  ? 115.969 99.940  185.697 1.00 93.40  ? 97  GLN E N     1 
ATOM   11919 C  CA    . GLN E 3 97  ? 115.678 99.220  186.933 1.00 93.40  ? 97  GLN E CA    1 
ATOM   11920 C  C     . GLN E 3 97  ? 116.961 98.732  187.595 1.00 93.40  ? 97  GLN E C     1 
ATOM   11921 O  O     . GLN E 3 97  ? 117.146 98.954  188.787 1.00 93.40  ? 97  GLN E O     1 
ATOM   11922 C  CB    . GLN E 3 97  ? 114.758 98.028  186.653 1.00 93.40  ? 97  GLN E CB    1 
ATOM   11923 C  CG    . GLN E 3 97  ? 113.350 98.504  186.313 1.00 93.40  ? 97  GLN E CG    1 
ATOM   11924 C  CD    . GLN E 3 97  ? 112.360 97.373  186.109 1.00 93.40  ? 97  GLN E CD    1 
ATOM   11925 O  OE1   . GLN E 3 97  ? 112.683 96.308  185.608 1.00 93.40  ? 97  GLN E OE1   1 
ATOM   11926 N  NE2   . GLN E 3 97  ? 111.125 97.613  186.487 1.00 93.40  ? 97  GLN E NE2   1 
ATOM   11927 N  N     . GLU E 3 98  ? 117.868 98.108  186.843 1.00 93.61  ? 98  GLU E N     1 
ATOM   11928 C  CA    . GLU E 3 98  ? 119.174 97.699  187.370 1.00 93.61  ? 98  GLU E CA    1 
ATOM   11929 C  C     . GLU E 3 98  ? 119.975 98.889  187.901 1.00 93.61  ? 98  GLU E C     1 
ATOM   11930 O  O     . GLU E 3 98  ? 120.583 98.791  188.964 1.00 93.61  ? 98  GLU E O     1 
ATOM   11931 C  CB    . GLU E 3 98  ? 119.994 96.979  186.286 1.00 93.61  ? 98  GLU E CB    1 
ATOM   11932 C  CG    . GLU E 3 98  ? 120.166 95.492  186.617 1.00 93.61  ? 98  GLU E CG    1 
ATOM   11933 C  CD    . GLU E 3 98  ? 121.136 94.776  185.663 1.00 93.61  ? 98  GLU E CD    1 
ATOM   11934 O  OE1   . GLU E 3 98  ? 121.505 93.625  185.991 1.00 93.61  ? 98  GLU E OE1   1 
ATOM   11935 O  OE2   . GLU E 3 98  ? 121.547 95.380  184.645 1.00 93.61  ? 98  GLU E OE2   1 
ATOM   11936 N  N     . LEU E 3 99  ? 119.964 100.011 187.182 1.00 92.43  ? 99  LEU E N     1 
ATOM   11937 C  CA    . LEU E 3 99  ? 120.684 101.223 187.564 1.00 92.43  ? 99  LEU E CA    1 
ATOM   11938 C  C     . LEU E 3 99  ? 120.146 101.809 188.880 1.00 92.43  ? 99  LEU E C     1 
ATOM   11939 O  O     . LEU E 3 99  ? 120.925 102.151 189.761 1.00 92.43  ? 99  LEU E O     1 
ATOM   11940 C  CB    . LEU E 3 99  ? 120.584 102.211 186.391 1.00 92.43  ? 99  LEU E CB    1 
ATOM   11941 C  CG    . LEU E 3 99  ? 121.616 103.353 186.450 1.00 92.43  ? 99  LEU E CG    1 
ATOM   11942 C  CD1   . LEU E 3 99  ? 122.642 103.208 185.322 1.00 92.43  ? 99  LEU E CD1   1 
ATOM   11943 C  CD2   . LEU E 3 99  ? 120.931 104.699 186.251 1.00 92.43  ? 99  LEU E CD2   1 
ATOM   11944 N  N     . VAL E 3 100 ? 118.823 101.866 189.048 1.00 93.10  ? 100 VAL E N     1 
ATOM   11945 C  CA    . VAL E 3 100 ? 118.181 102.398 190.262 1.00 93.10  ? 100 VAL E CA    1 
ATOM   11946 C  C     . VAL E 3 100 ? 118.264 101.417 191.434 1.00 93.10  ? 100 VAL E C     1 
ATOM   11947 O  O     . VAL E 3 100 ? 118.558 101.830 192.553 1.00 93.10  ? 100 VAL E O     1 
ATOM   11948 C  CB    . VAL E 3 100 ? 116.723 102.788 189.964 1.00 93.10  ? 100 VAL E CB    1 
ATOM   11949 C  CG1   . VAL E 3 100 ? 115.966 103.172 191.240 1.00 93.10  ? 100 VAL E CG1   1 
ATOM   11950 C  CG2   . VAL E 3 100 ? 116.666 103.987 189.004 1.00 93.10  ? 100 VAL E CG2   1 
ATOM   11951 N  N     . ASN E 3 101 ? 118.045 100.118 191.201 1.00 93.56  ? 101 ASN E N     1 
ATOM   11952 C  CA    . ASN E 3 101 ? 118.018 99.092  192.254 1.00 93.56  ? 101 ASN E CA    1 
ATOM   11953 C  C     . ASN E 3 101 ? 119.333 98.988  193.034 1.00 93.56  ? 101 ASN E C     1 
ATOM   11954 O  O     . ASN E 3 101 ? 119.320 98.561  194.186 1.00 93.56  ? 101 ASN E O     1 
ATOM   11955 C  CB    . ASN E 3 101 ? 117.682 97.722  191.637 1.00 93.56  ? 101 ASN E CB    1 
ATOM   11956 C  CG    . ASN E 3 101 ? 116.199 97.501  191.407 1.00 93.56  ? 101 ASN E CG    1 
ATOM   11957 O  OD1   . ASN E 3 101 ? 115.350 97.908  192.178 1.00 93.56  ? 101 ASN E OD1   1 
ATOM   11958 N  ND2   . ASN E 3 101 ? 115.830 96.780  190.376 1.00 93.56  ? 101 ASN E ND2   1 
ATOM   11959 N  N     . LYS E 3 102 ? 120.459 99.394  192.438 1.00 92.85  ? 102 LYS E N     1 
ATOM   11960 C  CA    . LYS E 3 102 ? 121.752 99.477  193.131 1.00 92.85  ? 102 LYS E CA    1 
ATOM   11961 C  C     . LYS E 3 102 ? 121.753 100.462 194.305 1.00 92.85  ? 102 LYS E C     1 
ATOM   11962 O  O     . LYS E 3 102 ? 122.617 100.345 195.170 1.00 92.85  ? 102 LYS E O     1 
ATOM   11963 C  CB    . LYS E 3 102 ? 122.823 99.918  192.132 1.00 92.85  ? 102 LYS E CB    1 
ATOM   11964 C  CG    . LYS E 3 102 ? 123.165 98.849  191.086 1.00 92.85  ? 102 LYS E CG    1 
ATOM   11965 C  CD    . LYS E 3 102 ? 124.005 99.533  190.007 1.00 92.85  ? 102 LYS E CD    1 
ATOM   11966 C  CE    . LYS E 3 102 ? 124.174 98.709  188.737 1.00 92.85  ? 102 LYS E CE    1 
ATOM   11967 N  NZ    . LYS E 3 102 ? 124.930 99.531  187.756 1.00 92.85  ? 102 LYS E NZ    1 
ATOM   11968 N  N     . HIS E 3 103 ? 120.822 101.419 194.328 1.00 92.02  ? 103 HIS E N     1 
ATOM   11969 C  CA    . HIS E 3 103 ? 120.821 102.549 195.263 1.00 92.02  ? 103 HIS E CA    1 
ATOM   11970 C  C     . HIS E 3 103 ? 119.592 102.618 196.173 1.00 92.02  ? 103 HIS E C     1 
ATOM   11971 O  O     . HIS E 3 103 ? 119.537 103.515 197.020 1.00 92.02  ? 103 HIS E O     1 
ATOM   11972 C  CB    . HIS E 3 103 ? 120.999 103.848 194.467 1.00 92.02  ? 103 HIS E CB    1 
ATOM   11973 C  CG    . HIS E 3 103 ? 122.263 103.847 193.652 1.00 92.02  ? 103 HIS E CG    1 
ATOM   11974 N  ND1   . HIS E 3 103 ? 123.558 103.893 194.171 1.00 92.02  ? 103 HIS E ND1   1 
ATOM   11975 C  CD2   . HIS E 3 103 ? 122.327 103.715 192.300 1.00 92.02  ? 103 HIS E CD2   1 
ATOM   11976 C  CE1   . HIS E 3 103 ? 124.374 103.799 193.110 1.00 92.02  ? 103 HIS E CE1   1 
ATOM   11977 N  NE2   . HIS E 3 103 ? 123.660 103.683 191.981 1.00 92.02  ? 103 HIS E NE2   1 
ATOM   11978 N  N     . LEU E 3 104 ? 118.638 101.693 196.017 1.00 89.57  ? 104 LEU E N     1 
ATOM   11979 C  CA    . LEU E 3 104 ? 117.439 101.577 196.860 1.00 89.57  ? 104 LEU E CA    1 
ATOM   11980 C  C     . LEU E 3 104 ? 117.724 101.062 198.280 1.00 89.57  ? 104 LEU E C     1 
ATOM   11981 O  O     . LEU E 3 104 ? 118.766 100.401 198.491 1.00 89.57  ? 104 LEU E O     1 
ATOM   11982 C  CB    . LEU E 3 104 ? 116.382 100.717 196.134 1.00 89.57  ? 104 LEU E CB    1 
ATOM   11983 C  CG    . LEU E 3 104 ? 115.741 101.369 194.902 1.00 89.57  ? 104 LEU E CG    1 
ATOM   11984 C  CD1   . LEU E 3 104 ? 114.721 100.402 194.319 1.00 89.57  ? 104 LEU E CD1   1 
ATOM   11985 C  CD2   . LEU E 3 104 ? 114.996 102.660 195.234 1.00 89.57  ? 104 LEU E CD2   1 
ATOM   11986 O  OXT   . LEU E 3 104 ? 116.864 101.353 199.141 1.00 89.57  ? 104 LEU E OXT   1 
HETATM 11987 P  PA    . TTP F 4 .   ? 145.296 143.155 133.346 1.00 38.66  ? 801 TTP A PA    1 
HETATM 11988 O  O1A   . TTP F 4 .   ? 143.910 143.730 133.196 1.00 42.70  ? 801 TTP A O1A   1 
HETATM 11989 O  O2A   . TTP F 4 .   ? 146.282 143.894 132.473 1.00 43.26  ? 801 TTP A O2A   1 
HETATM 11990 O  O3A   . TTP F 4 .   ? 145.744 143.143 134.889 1.00 48.32  ? 801 TTP A O3A   1 
HETATM 11991 P  PB    . TTP F 4 .   ? 146.912 144.107 135.427 1.00 46.19  ? 801 TTP A PB    1 
HETATM 11992 O  O1B   . TTP F 4 .   ? 147.060 145.354 134.590 1.00 46.96  ? 801 TTP A O1B   1 
HETATM 11993 O  O2B   . TTP F 4 .   ? 146.657 144.465 136.870 1.00 44.37  ? 801 TTP A O2B   1 
HETATM 11994 O  O3B   . TTP F 4 .   ? 148.189 143.141 135.278 1.00 42.96  ? 801 TTP A O3B   1 
HETATM 11995 P  PG    . TTP F 4 .   ? 149.619 143.723 134.829 1.00 47.86  ? 801 TTP A PG    1 
HETATM 11996 O  O1G   . TTP F 4 .   ? 149.818 145.112 135.388 1.00 48.77  ? 801 TTP A O1G   1 
HETATM 11997 O  O2G   . TTP F 4 .   ? 149.681 143.755 133.323 1.00 48.58  ? 801 TTP A O2G   1 
HETATM 11998 O  O3G   . TTP F 4 .   ? 150.709 142.810 135.335 1.00 45.20  ? 801 TTP A O3G   1 
HETATM 11999 O  "O5'" . TTP F 4 .   ? 145.311 141.590 132.988 1.00 31.26  ? 801 TTP A "O5'" 1 
HETATM 12000 C  "C5'" . TTP F 4 .   ? 146.270 141.118 132.049 1.00 41.84  ? 801 TTP A "C5'" 1 
HETATM 12001 C  "C4'" . TTP F 4 .   ? 146.097 139.628 131.806 1.00 43.19  ? 801 TTP A "C4'" 1 
HETATM 12002 O  "O4'" . TTP F 4 .   ? 145.755 138.967 133.022 1.00 41.64  ? 801 TTP A "O4'" 1 
HETATM 12003 C  "C3'" . TTP F 4 .   ? 144.972 139.339 130.830 1.00 41.37  ? 801 TTP A "C3'" 1 
HETATM 12004 O  "O3'" . TTP F 4 .   ? 145.486 139.091 129.520 1.00 38.80  ? 801 TTP A "O3'" 1 
HETATM 12005 C  "C2'" . TTP F 4 .   ? 144.296 138.094 131.367 1.00 45.87  ? 801 TTP A "C2'" 1 
HETATM 12006 C  "C1'" . TTP F 4 .   ? 144.898 137.860 132.744 1.00 46.86  ? 801 TTP A "C1'" 1 
HETATM 12007 N  N1    . TTP F 4 .   ? 143.843 137.767 133.754 1.00 38.94  ? 801 TTP A N1    1 
HETATM 12008 C  C2    . TTP F 4 .   ? 143.263 136.511 134.031 1.00 42.98  ? 801 TTP A C2    1 
HETATM 12009 O  O2    . TTP F 4 .   ? 143.665 135.502 133.414 1.00 46.36  ? 801 TTP A O2    1 
HETATM 12010 N  N3    . TTP F 4 .   ? 142.298 136.376 134.948 1.00 45.81  ? 801 TTP A N3    1 
HETATM 12011 C  C4    . TTP F 4 .   ? 141.853 137.437 135.623 1.00 44.47  ? 801 TTP A C4    1 
HETATM 12012 O  O4    . TTP F 4 .   ? 140.951 137.312 136.478 1.00 47.60  ? 801 TTP A O4    1 
HETATM 12013 C  C5    . TTP F 4 .   ? 142.442 138.768 135.349 1.00 45.17  ? 801 TTP A C5    1 
HETATM 12014 C  C5M   . TTP F 4 .   ? 141.966 139.985 136.092 1.00 44.48  ? 801 TTP A C5M   1 
HETATM 12015 C  C6    . TTP F 4 .   ? 143.440 138.869 134.393 1.00 43.33  ? 801 TTP A C6    1 
HETATM 12016 MG MG    . MG  G 5 .   ? 147.344 145.554 131.697 1.00 39.74  ? 802 MG  A MG    1 
HETATM 12017 P  PG    . ATP H 6 .   ? 108.615 133.877 78.871  1.00 89.84  ? 803 ATP A PG    1 
HETATM 12018 O  O1G   . ATP H 6 .   ? 110.092 133.712 78.755  1.00 77.50  ? 803 ATP A O1G   1 
HETATM 12019 O  O2G   . ATP H 6 .   ? 108.194 135.072 79.733  1.00 75.92  ? 803 ATP A O2G   1 
HETATM 12020 O  O3G   . ATP H 6 .   ? 107.896 133.957 77.520  1.00 76.37  ? 803 ATP A O3G   1 
HETATM 12021 P  PB    . ATP H 6 .   ? 106.540 132.067 80.043  1.00 86.04  ? 803 ATP A PB    1 
HETATM 12022 O  O1B   . ATP H 6 .   ? 105.542 133.151 80.134  1.00 78.66  ? 803 ATP A O1B   1 
HETATM 12023 O  O2B   . ATP H 6 .   ? 106.186 130.905 79.115  1.00 74.68  ? 803 ATP A O2B   1 
HETATM 12024 O  O3B   . ATP H 6 .   ? 107.965 132.612 79.599  1.00 80.83  ? 803 ATP A O3B   1 
HETATM 12025 P  PA    . ATP H 6 .   ? 106.737 130.034 82.181  1.00 83.90  ? 803 ATP A PA    1 
HETATM 12026 O  O1A   . ATP H 6 .   ? 107.865 129.146 81.832  1.00 73.36  ? 803 ATP A O1A   1 
HETATM 12027 O  O2A   . ATP H 6 .   ? 105.353 129.484 81.836  1.00 78.01  ? 803 ATP A O2A   1 
HETATM 12028 O  O3A   . ATP H 6 .   ? 106.865 131.449 81.473  1.00 77.55  ? 803 ATP A O3A   1 
HETATM 12029 O  "O5'" . ATP H 6 .   ? 106.750 130.419 83.712  1.00 77.37  ? 803 ATP A "O5'" 1 
HETATM 12030 C  "C5'" . ATP H 6 .   ? 106.148 131.644 84.179  1.00 74.63  ? 803 ATP A "C5'" 1 
HETATM 12031 C  "C4'" . ATP H 6 .   ? 107.151 132.394 85.019  1.00 74.40  ? 803 ATP A "C4'" 1 
HETATM 12032 O  "O4'" . ATP H 6 .   ? 107.751 131.493 85.975  1.00 75.89  ? 803 ATP A "O4'" 1 
HETATM 12033 C  "C3'" . ATP H 6 .   ? 108.320 132.999 84.251  1.00 75.44  ? 803 ATP A "C3'" 1 
HETATM 12034 O  "O3'" . ATP H 6 .   ? 107.996 134.297 83.767  1.00 73.55  ? 803 ATP A "O3'" 1 
HETATM 12035 C  "C2'" . ATP H 6 .   ? 109.417 133.048 85.314  1.00 75.53  ? 803 ATP A "C2'" 1 
HETATM 12036 O  "O2'" . ATP H 6 .   ? 109.289 134.190 86.153  1.00 74.32  ? 803 ATP A "O2'" 1 
HETATM 12037 C  "C1'" . ATP H 6 .   ? 109.136 131.768 86.105  1.00 72.95  ? 803 ATP A "C1'" 1 
HETATM 12038 N  N9    . ATP H 6 .   ? 109.882 130.602 85.642  1.00 71.48  ? 803 ATP A N9    1 
HETATM 12039 C  C8    . ATP H 6 .   ? 109.396 129.536 84.933  1.00 73.72  ? 803 ATP A C8    1 
HETATM 12040 N  N7    . ATP H 6 .   ? 110.295 128.625 84.650  1.00 73.74  ? 803 ATP A N7    1 
HETATM 12041 C  C5    . ATP H 6 .   ? 111.457 129.127 85.216  1.00 77.26  ? 803 ATP A C5    1 
HETATM 12042 C  C6    . ATP H 6 .   ? 112.776 128.637 85.271  1.00 75.28  ? 803 ATP A C6    1 
HETATM 12043 N  N6    . ATP H 6 .   ? 113.164 127.480 84.724  1.00 72.17  ? 803 ATP A N6    1 
HETATM 12044 N  N1    . ATP H 6 .   ? 113.699 129.386 85.913  1.00 70.82  ? 803 ATP A N1    1 
HETATM 12045 C  C2    . ATP H 6 .   ? 113.319 130.544 86.459  1.00 69.72  ? 803 ATP A C2    1 
HETATM 12046 N  N3    . ATP H 6 .   ? 112.110 131.107 86.473  1.00 71.91  ? 803 ATP A N3    1 
HETATM 12047 C  C4    . ATP H 6 .   ? 111.218 130.345 85.831  1.00 73.82  ? 803 ATP A C4    1 
HETATM 12048 P  PB    . GDP I 7 .   ? 104.702 148.993 83.277  1.00 86.77  ? 804 GDP A PB    1 
HETATM 12049 O  O1B   . GDP I 7 .   ? 104.527 147.711 82.500  1.00 69.94  ? 804 GDP A O1B   1 
HETATM 12050 O  O2B   . GDP I 7 .   ? 105.020 150.116 82.319  1.00 71.43  ? 804 GDP A O2B   1 
HETATM 12051 O  O3B   . GDP I 7 .   ? 103.432 149.303 84.031  1.00 72.91  ? 804 GDP A O3B   1 
HETATM 12052 O  O3A   . GDP I 7 .   ? 105.924 148.822 84.307  1.00 73.18  ? 804 GDP A O3A   1 
HETATM 12053 P  PA    . GDP I 7 .   ? 105.731 148.098 85.731  1.00 77.70  ? 804 GDP A PA    1 
HETATM 12054 O  O1A   . GDP I 7 .   ? 105.645 149.103 86.855  1.00 71.30  ? 804 GDP A O1A   1 
HETATM 12055 O  O2A   . GDP I 7 .   ? 104.522 147.195 85.719  1.00 70.91  ? 804 GDP A O2A   1 
HETATM 12056 O  "O5'" . GDP I 7 .   ? 107.082 147.237 85.835  1.00 72.45  ? 804 GDP A "O5'" 1 
HETATM 12057 C  "C5'" . GDP I 7 .   ? 108.299 147.819 86.296  1.00 70.07  ? 804 GDP A "C5'" 1 
HETATM 12058 C  "C4'" . GDP I 7 .   ? 109.354 146.726 86.319  1.00 65.18  ? 804 GDP A "C4'" 1 
HETATM 12059 O  "O4'" . GDP I 7 .   ? 109.469 146.234 87.653  1.00 67.00  ? 804 GDP A "O4'" 1 
HETATM 12060 C  "C3'" . GDP I 7 .   ? 108.920 145.566 85.436  1.00 69.06  ? 804 GDP A "C3'" 1 
HETATM 12061 O  "O3'" . GDP I 7 .   ? 109.941 145.249 84.489  1.00 70.95  ? 804 GDP A "O3'" 1 
HETATM 12062 C  "C2'" . GDP I 7 .   ? 108.710 144.390 86.364  1.00 70.71  ? 804 GDP A "C2'" 1 
HETATM 12063 O  "O2'" . GDP I 7 .   ? 109.340 143.223 85.830  1.00 74.21  ? 804 GDP A "O2'" 1 
HETATM 12064 C  "C1'" . GDP I 7 .   ? 109.363 144.810 87.669  1.00 70.10  ? 804 GDP A "C1'" 1 
HETATM 12065 N  N9    . GDP I 7 .   ? 108.591 144.363 88.858  1.00 66.83  ? 804 GDP A N9    1 
HETATM 12066 C  C8    . GDP I 7 .   ? 109.136 143.823 89.961  1.00 67.54  ? 804 GDP A C8    1 
HETATM 12067 N  N7    . GDP I 7 .   ? 108.188 143.520 90.880  1.00 68.66  ? 804 GDP A N7    1 
HETATM 12068 C  C5    . GDP I 7 .   ? 107.001 143.883 90.369  1.00 70.74  ? 804 GDP A C5    1 
HETATM 12069 C  C6    . GDP I 7 .   ? 105.592 143.845 90.822  1.00 69.86  ? 804 GDP A C6    1 
HETATM 12070 O  O6    . GDP I 7 .   ? 105.292 143.383 91.944  1.00 70.16  ? 804 GDP A O6    1 
HETATM 12071 N  N1    . GDP I 7 .   ? 104.653 144.318 89.996  1.00 69.83  ? 804 GDP A N1    1 
HETATM 12072 C  C2    . GDP I 7 .   ? 104.949 144.821 88.784  1.00 67.15  ? 804 GDP A C2    1 
HETATM 12073 N  N2    . GDP I 7 .   ? 103.940 145.281 88.008  1.00 66.79  ? 804 GDP A N2    1 
HETATM 12074 N  N3    . GDP I 7 .   ? 106.217 144.889 88.306  1.00 66.64  ? 804 GDP A N3    1 
HETATM 12075 C  C4    . GDP I 7 .   ? 107.267 144.443 89.036  1.00 68.58  ? 804 GDP A C4    1 
HETATM 12076 MG MG    . MG  J 5 .   ? 117.887 148.558 123.545 1.00 23.04  ? 801 MG  B MG    1 
HETATM 12077 P  PA    . TTP K 4 .   ? 119.388 145.441 122.443 1.00 38.14  ? 802 TTP B PA    1 
HETATM 12078 O  O1A   . TTP K 4 .   ? 120.892 145.484 122.325 1.00 32.84  ? 802 TTP B O1A   1 
HETATM 12079 O  O2A   . TTP K 4 .   ? 118.876 146.602 123.259 1.00 36.02  ? 802 TTP B O2A   1 
HETATM 12080 O  O3A   . TTP K 4 .   ? 118.697 145.395 120.992 1.00 38.55  ? 802 TTP B O3A   1 
HETATM 12081 P  PB    . TTP K 4 .   ? 118.511 146.726 120.110 1.00 40.67  ? 802 TTP B PB    1 
HETATM 12082 O  O1B   . TTP K 4 .   ? 118.842 147.973 120.890 1.00 39.27  ? 802 TTP B O1B   1 
HETATM 12083 O  O2B   . TTP K 4 .   ? 119.361 146.645 118.865 1.00 39.33  ? 802 TTP B O2B   1 
HETATM 12084 O  O3B   . TTP K 4 .   ? 116.950 146.662 119.722 1.00 37.78  ? 802 TTP B O3B   1 
HETATM 12085 P  PG    . TTP K 4 .   ? 115.805 146.944 120.821 1.00 33.98  ? 802 TTP B PG    1 
HETATM 12086 O  O1G   . TTP K 4 .   ? 115.591 145.697 121.643 1.00 30.17  ? 802 TTP B O1G   1 
HETATM 12087 O  O2G   . TTP K 4 .   ? 114.512 147.295 120.128 1.00 39.80  ? 802 TTP B O2G   1 
HETATM 12088 O  O3G   . TTP K 4 .   ? 116.210 148.079 121.729 1.00 41.40  ? 802 TTP B O3G   1 
HETATM 12089 O  "O5'" . TTP K 4 .   ? 118.910 144.052 123.092 1.00 30.68  ? 802 TTP B "O5'" 1 
HETATM 12090 C  "C5'" . TTP K 4 .   ? 118.191 144.073 124.320 1.00 31.77  ? 802 TTP B "C5'" 1 
HETATM 12091 C  "C4'" . TTP K 4 .   ? 117.972 142.656 124.822 1.00 30.48  ? 802 TTP B "C4'" 1 
HETATM 12092 O  "O4'" . TTP K 4 .   ? 118.095 141.723 123.751 1.00 34.93  ? 802 TTP B "O4'" 1 
HETATM 12093 C  "C3'" . TTP K 4 .   ? 119.013 142.260 125.850 1.00 33.58  ? 802 TTP B "C3'" 1 
HETATM 12094 O  "O3'" . TTP K 4 .   ? 118.497 142.403 127.175 1.00 35.23  ? 802 TTP B "O3'" 1 
HETATM 12095 C  "C2'" . TTP K 4 .   ? 119.317 140.804 125.563 1.00 35.50  ? 802 TTP B "C2'" 1 
HETATM 12096 C  "C1'" . TTP K 4 .   ? 118.614 140.489 124.251 1.00 39.81  ? 802 TTP B "C1'" 1 
HETATM 12097 N  N1    . TTP K 4 .   ? 119.556 139.897 123.301 1.00 37.48  ? 802 TTP B N1    1 
HETATM 12098 C  C2    . TTP K 4 .   ? 119.790 138.504 123.341 1.00 36.50  ? 802 TTP B C2    1 
HETATM 12099 O  O2    . TTP K 4 .   ? 119.184 137.805 124.181 1.00 36.23  ? 802 TTP B O2    1 
HETATM 12100 N  N3    . TTP K 4 .   ? 120.640 137.915 122.493 1.00 35.69  ? 802 TTP B N3    1 
HETATM 12101 C  C4    . TTP K 4 .   ? 121.298 138.637 121.585 1.00 37.87  ? 802 TTP B C4    1 
HETATM 12102 O  O4    . TTP K 4 .   ? 122.092 138.089 120.793 1.00 37.46  ? 802 TTP B O4    1 
HETATM 12103 C  C5    . TTP K 4 .   ? 121.074 140.100 121.525 1.00 35.26  ? 802 TTP B C5    1 
HETATM 12104 C  C5M   . TTP K 4 .   ? 121.800 140.939 120.511 1.00 32.09  ? 802 TTP B C5M   1 
HETATM 12105 C  C6    . TTP K 4 .   ? 120.187 140.677 122.418 1.00 35.20  ? 802 TTP B C6    1 
HETATM 12106 P  PG    . ATP L 6 .   ? 152.999 137.525 179.940 1.00 82.63  ? 803 ATP B PG    1 
HETATM 12107 O  O1G   . ATP L 6 .   ? 152.567 136.569 180.998 1.00 70.62  ? 803 ATP B O1G   1 
HETATM 12108 O  O2G   . ATP L 6 .   ? 153.962 138.607 180.444 1.00 71.91  ? 803 ATP B O2G   1 
HETATM 12109 O  O3G   . ATP L 6 .   ? 151.833 138.196 179.205 1.00 69.78  ? 803 ATP B O3G   1 
HETATM 12110 P  PB    . ATP L 6 .   ? 155.148 136.922 177.941 1.00 78.57  ? 803 ATP B PB    1 
HETATM 12111 O  O1B   . ATP L 6 .   ? 155.226 138.239 177.277 1.00 69.20  ? 803 ATP B O1B   1 
HETATM 12112 O  O2B   . ATP L 6 .   ? 156.318 136.571 178.860 1.00 66.79  ? 803 ATP B O2B   1 
HETATM 12113 O  O3B   . ATP L 6 .   ? 153.813 136.766 178.792 1.00 75.48  ? 803 ATP B O3B   1 
HETATM 12114 P  PA    . ATP L 6 .   ? 154.367 134.279 176.868 1.00 74.49  ? 803 ATP B PA    1 
HETATM 12115 O  O1A   . ATP L 6 .   ? 152.992 134.279 177.404 1.00 68.26  ? 803 ATP B O1A   1 
HETATM 12116 O  O2A   . ATP L 6 .   ? 155.346 133.353 177.591 1.00 70.83  ? 803 ATP B O2A   1 
HETATM 12117 O  O3A   . ATP L 6 .   ? 155.000 135.737 176.890 1.00 74.54  ? 803 ATP B O3A   1 
HETATM 12118 O  "O5'" . ATP L 6 .   ? 154.380 133.915 175.332 1.00 70.55  ? 803 ATP B "O5'" 1 
HETATM 12119 C  "C5'" . ATP L 6 .   ? 155.459 134.337 174.472 1.00 68.64  ? 803 ATP B "C5'" 1 
HETATM 12120 C  "C4'" . ATP L 6 .   ? 154.895 135.172 173.349 1.00 68.94  ? 803 ATP B "C4'" 1 
HETATM 12121 O  "O4'" . ATP L 6 .   ? 154.095 134.339 172.481 1.00 71.15  ? 803 ATP B "O4'" 1 
HETATM 12122 C  "C3'" . ATP L 6 .   ? 153.974 136.308 173.782 1.00 68.08  ? 803 ATP B "C3'" 1 
HETATM 12123 O  "O3'" . ATP L 6 .   ? 154.714 137.494 174.046 1.00 68.97  ? 803 ATP B "O3'" 1 
HETATM 12124 C  "C2'" . ATP L 6 .   ? 153.063 136.469 172.565 1.00 70.53  ? 803 ATP B "C2'" 1 
HETATM 12125 O  "O2'" . ATP L 6 .   ? 153.676 137.247 171.543 1.00 69.49  ? 803 ATP B "O2'" 1 
HETATM 12126 C  "C1'" . ATP L 6 .   ? 152.904 135.016 172.113 1.00 69.43  ? 803 ATP B "C1'" 1 
HETATM 12127 N  N9    . ATP L 6 .   ? 151.775 134.323 172.725 1.00 67.69  ? 803 ATP B N9    1 
HETATM 12128 C  C8    . ATP L 6 .   ? 151.825 133.267 173.597 1.00 69.32  ? 803 ATP B C8    1 
HETATM 12129 N  N7    . ATP L 6 .   ? 150.650 132.843 173.991 1.00 69.89  ? 803 ATP B N7    1 
HETATM 12130 C  C5    . ATP L 6 .   ? 149.762 133.680 173.333 1.00 72.52  ? 803 ATP B C5    1 
HETATM 12131 C  C6    . ATP L 6 .   ? 148.355 133.754 173.322 1.00 70.17  ? 803 ATP B C6    1 
HETATM 12132 N  N6    . ATP L 6 .   ? 147.562 132.941 174.025 1.00 67.68  ? 803 ATP B N6    1 
HETATM 12133 N  N1    . ATP L 6 .   ? 147.783 134.708 172.556 1.00 67.83  ? 803 ATP B N1    1 
HETATM 12134 C  C2    . ATP L 6 .   ? 148.569 135.528 171.854 1.00 66.24  ? 803 ATP B C2    1 
HETATM 12135 N  N3    . ATP L 6 .   ? 149.901 135.551 171.783 1.00 66.05  ? 803 ATP B N3    1 
HETATM 12136 C  C4    . ATP L 6 .   ? 150.442 134.598 172.550 1.00 69.17  ? 803 ATP B C4    1 
HETATM 12137 P  PB    . GDP M 7 .   ? 161.870 150.516 172.131 1.00 79.35  ? 804 GDP B PB    1 
HETATM 12138 O  O1B   . GDP M 7 .   ? 161.479 149.345 172.999 1.00 67.14  ? 804 GDP B O1B   1 
HETATM 12139 O  O2B   . GDP M 7 .   ? 162.202 151.699 173.008 1.00 67.24  ? 804 GDP B O2B   1 
HETATM 12140 O  O3B   . GDP M 7 .   ? 163.072 150.145 171.295 1.00 68.08  ? 804 GDP B O3B   1 
HETATM 12141 O  O3A   . GDP M 7 .   ? 160.637 150.891 171.168 1.00 69.78  ? 804 GDP B O3A   1 
HETATM 12142 P  PA    . GDP M 7 .   ? 160.317 149.996 169.869 1.00 71.02  ? 804 GDP B PA    1 
HETATM 12143 O  O1A   . GDP M 7 .   ? 161.034 150.541 168.657 1.00 68.62  ? 804 GDP B O1A   1 
HETATM 12144 O  O2A   . GDP M 7 .   ? 160.696 148.555 170.108 1.00 67.18  ? 804 GDP B O2A   1 
HETATM 12145 O  "O5'" . GDP M 7 .   ? 158.724 150.147 169.702 1.00 65.98  ? 804 GDP B "O5'" 1 
HETATM 12146 C  "C5'" . GDP M 7 .   ? 158.094 149.770 168.483 1.00 65.54  ? 804 GDP B "C5'" 1 
HETATM 12147 C  "C4'" . GDP M 7 .   ? 156.783 149.063 168.789 1.00 63.92  ? 804 GDP B "C4'" 1 
HETATM 12148 O  "O4'" . GDP M 7 .   ? 156.335 148.407 167.602 1.00 64.17  ? 804 GDP B "O4'" 1 
HETATM 12149 C  "C3'" . GDP M 7 .   ? 156.987 148.007 169.862 1.00 68.21  ? 804 GDP B "C3'" 1 
HETATM 12150 O  "O3'" . GDP M 7 .   ? 156.080 148.225 170.947 1.00 68.16  ? 804 GDP B "O3'" 1 
HETATM 12151 C  "C2'" . GDP M 7 .   ? 156.692 146.675 169.207 1.00 66.45  ? 804 GDP B "C2'" 1 
HETATM 12152 O  "O2'" . GDP M 7 .   ? 155.740 145.943 169.983 1.00 64.69  ? 804 GDP B "O2'" 1 
HETATM 12153 C  "C1'" . GDP M 7 .   ? 156.128 147.013 167.836 1.00 64.51  ? 804 GDP B "C1'" 1 
HETATM 12154 N  N9    . GDP M 7 .   ? 156.774 146.221 166.756 1.00 64.21  ? 804 GDP B N9    1 
HETATM 12155 C  C8    . GDP M 7 .   ? 156.127 145.670 165.712 1.00 64.58  ? 804 GDP B C8    1 
HETATM 12156 N  N7    . GDP M 7 .   ? 156.987 145.016 164.891 1.00 65.95  ? 804 GDP B N7    1 
HETATM 12157 C  C5    . GDP M 7 .   ? 158.222 145.158 165.404 1.00 66.21  ? 804 GDP B C5    1 
HETATM 12158 C  C6    . GDP M 7 .   ? 159.588 144.720 165.034 1.00 65.68  ? 804 GDP B C6    1 
HETATM 12159 O  O6    . GDP M 7 .   ? 159.786 144.039 164.006 1.00 68.03  ? 804 GDP B O6    1 
HETATM 12160 N  N1    . GDP M 7 .   ? 160.603 145.074 165.830 1.00 66.68  ? 804 GDP B N1    1 
HETATM 12161 C  C2    . GDP M 7 .   ? 160.419 145.807 166.941 1.00 65.75  ? 804 GDP B C2    1 
HETATM 12162 N  N2    . GDP M 7 .   ? 161.495 146.127 167.698 1.00 65.25  ? 804 GDP B N2    1 
HETATM 12163 N  N3    . GDP M 7 .   ? 159.197 146.243 167.340 1.00 65.49  ? 804 GDP B N3    1 
HETATM 12164 C  C4    . GDP M 7 .   ? 158.080 145.957 166.630 1.00 65.33  ? 804 GDP B C4    1 
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