data_9BXS
# 
_entry.id   9BXS 
# 
_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   9BXS         pdb_00009bxs 10.2210/pdb9bxs/pdb 
WWPDB D_1000284350 ?            ?                   
EMDB  EMD-45010    ?            ?                   
# 
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                        9BXS 
_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 'Refinement from a similar stack of particles in cryoSPARC'                                                     EMD-45004 
'other EM volume'      
PDB  'Refinement from a similar stack of particles in cryoSPARC'                                                     9BXC      
unspecified            
EMDB 'Consensus full-complex model for re-reduction condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45010 
'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 ?        ? ? ? 
8 non-polymer syn 'MANGANESE (II) ION'                                 54.938    4 ?        ? ? ? 
# 
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 
8 'MANGANESE (II) ION'        MN  
# 
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  
MN  non-polymer         . 'MANGANESE (II) ION'        ? 'Mn 2'              54.938  
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  16  ASP ASP C . n 
C 2 38  PHE 38  17  17  PHE PHE C . n 
C 2 39  THR 39  18  18  THR THR C . n 
C 2 40  GLN 40  19  19  GLN GLN C . n 
C 2 41  MET 41  20  20  MET MET C . n 
C 2 42  PHE 42  21  21  PHE PHE C . n 
C 2 43  TYR 43  22  22  TYR TYR C . n 
C 2 44  ASN 44  23  23  ASN ASN C . n 
C 2 45  GLN 45  24  24  GLN GLN C . n 
C 2 46  ASN 46  25  25  ASN ASN C . n 
C 2 47  VAL 47  26  26  VAL VAL C . n 
C 2 48  LYS 48  27  27  LYS LYS C . n 
C 2 49  GLN 49  28  28  GLN GLN C . n 
C 2 50  PHE 50  29  29  PHE PHE C . n 
C 2 51  TRP 51  30  30  TRP TRP C . n 
C 2 52  LEU 52  31  31  LEU LEU C . n 
C 2 53  PRO 53  32  32  PRO PRO C . n 
C 2 54  GLU 54  33  33  GLU GLU C . n 
C 2 55  GLU 55  34  34  GLU GLU C . n 
C 2 56  ILE 56  35  35  ILE ILE C . n 
C 2 57  ALA 57  36  36  ALA ALA C . n 
C 2 58  LEU 58  37  37  LEU LEU C . n 
C 2 59  ASN 59  38  38  ASN ASN C . n 
C 2 60  GLY 60  39  39  GLY GLY C . n 
C 2 61  ASP 61  40  40  ASP ASP C . n 
C 2 62  LEU 62  41  41  LEU LEU C . n 
C 2 63  LEU 63  42  42  LEU LEU C . n 
C 2 64  THR 64  43  43  THR THR C . n 
C 2 65  TRP 65  44  44  TRP TRP C . n 
C 2 66  LYS 66  45  45  LYS LYS C . n 
C 2 67  TYR 67  46  46  TYR TYR C . n 
C 2 68  LEU 68  47  47  LEU LEU C . n 
C 2 69  GLY 69  48  48  GLY GLY C . n 
C 2 70  LYS 70  49  49  LYS LYS C . n 
C 2 71  ASN 71  50  50  ASN ASN C . n 
C 2 72  GLU 72  51  51  GLU GLU C . n 
C 2 73  GLN 73  52  52  GLN GLN C . n 
C 2 74  ASP 74  53  53  ASP ASP C . n 
C 2 75  THR 75  54  54  THR THR C . n 
C 2 76  TYR 76  55  55  TYR TYR C . n 
C 2 77  MET 77  56  56  MET MET C . n 
C 2 78  LYS 78  57  57  LYS LYS C . n 
C 2 79  VAL 79  58  58  VAL VAL C . n 
C 2 80  LEU 80  59  59  LEU LEU C . n 
C 2 81  ALA 81  60  60  ALA ALA C . n 
C 2 82  GLY 82  61  61  GLY GLY C . n 
C 2 83  LEU 83  62  62  LEU LEU C . n 
C 2 84  THR 84  63  63  THR THR C . n 
C 2 85  LEU 85  64  64  LEU LEU C . n 
C 2 86  LEU 86  65  65  LEU LEU C . n 
C 2 87  ASP 87  66  66  ASP ASP C . n 
C 2 88  THR 88  67  67  THR THR C . n 
C 2 89  GLU 89  68  68  GLU GLU C . n 
C 2 90  GLN 90  69  69  GLN GLN C . n 
C 2 91  GLY 91  70  70  GLY GLY C . n 
C 2 92  ASN 92  71  71  ASN ASN C . n 
C 2 93  THR 93  72  72  THR THR C . n 
C 2 94  GLY 94  73  73  GLY GLY C . n 
C 2 95  MET 95  74  74  MET MET C . n 
C 2 96  PRO 96  75  75  PRO PRO C . n 
C 2 97  ILE 97  76  76  ILE ILE C . n 
C 2 98  VAL 98  77  77  VAL VAL C . n 
C 2 99  ALA 99  78  78  ALA ALA C . n 
C 2 100 GLU 100 79  79  GLU GLU C . n 
C 2 101 HIS 101 80  80  HIS HIS C . n 
C 2 102 VAL 102 81  81  VAL VAL C . n 
C 2 103 ASP 103 82  82  ASP ASP C . n 
C 2 104 GLY 104 83  83  GLY GLY C . n 
C 2 105 HIS 105 84  84  HIS HIS C . n 
C 2 106 GLN 106 85  85  GLN GLN C . n 
C 2 107 ARG 107 86  86  ARG ARG C . n 
C 2 108 LYS 108 87  87  LYS LYS C . n 
C 2 109 ALA 109 88  88  ALA ALA C . n 
C 2 110 VAL 110 89  89  VAL VAL C . n 
C 2 111 LEU 111 90  90  LEU LEU C . n 
C 2 112 ASN 112 91  91  ASN ASN C . n 
C 2 113 PHE 113 92  92  PHE PHE C . n 
C 2 114 MET 114 93  93  MET MET C . n 
C 2 115 ALA 115 94  94  ALA ALA C . n 
C 2 116 MET 116 95  95  MET MET C . n 
C 2 117 MET 117 96  96  MET MET C . n 
C 2 118 GLU 118 97  97  GLU GLU C . n 
C 2 119 ASN 119 98  98  ASN ASN C . n 
C 2 120 ALA 120 99  99  ALA ALA C . n 
C 2 121 VAL 121 100 100 VAL VAL C . n 
C 2 122 HIS 122 101 101 HIS HIS C . n 
C 2 123 ALA 123 102 102 ALA ALA C . n 
C 2 124 LYS 124 103 103 LYS LYS C . n 
C 2 125 SER 125 104 104 SER SER C . n 
C 2 126 TYR 126 105 105 TYR TYR C . n 
C 2 127 SER 127 106 106 SER SER C . n 
C 2 128 ASN 128 107 107 ASN ASN C . n 
C 2 129 ILE 129 108 108 ILE ILE C . n 
C 2 130 PHE 130 109 109 PHE PHE C . n 
C 2 131 MET 131 110 110 MET MET C . n 
C 2 132 THR 132 111 111 THR THR C . n 
C 2 133 LEU 133 112 112 LEU LEU C . n 
C 2 134 ALA 134 113 113 ALA ALA C . n 
C 2 135 PRO 135 114 114 PRO PRO C . n 
C 2 136 THR 136 115 115 THR THR C . n 
C 2 137 GLU 137 116 116 GLU GLU C . n 
C 2 138 THR 138 117 117 THR THR C . n 
C 2 139 ILE 139 118 118 ILE ILE C . n 
C 2 140 ASN 140 119 119 ASN ASN C . n 
C 2 141 GLU 141 120 120 GLU GLU C . n 
C 2 142 VAL 142 121 121 VAL VAL C . n 
C 2 143 PHE 143 122 122 PHE PHE C . n 
C 2 144 GLU 144 123 123 GLU GLU C . n 
C 2 145 TRP 145 124 124 TRP TRP C . n 
C 2 146 VAL 146 125 125 VAL VAL C . n 
C 2 147 LYS 147 126 126 LYS LYS C . n 
C 2 148 GLN 148 127 127 GLN GLN C . n 
C 2 149 ASN 149 128 128 ASN ASN C . n 
C 2 150 LYS 150 129 129 LYS LYS C . n 
C 2 151 TYR 151 130 130 TYR TYR C . n 
C 2 152 LEU 152 131 131 LEU LEU C . n 
C 2 153 GLN 153 132 132 GLN GLN C . n 
C 2 154 LYS 154 133 133 LYS LYS C . n 
C 2 155 LYS 155 134 134 LYS LYS C . n 
C 2 156 ALA 156 135 135 ALA ALA C . n 
C 2 157 GLN 157 136 136 GLN GLN C . n 
C 2 158 MET 158 137 137 MET MET C . n 
C 2 159 ILE 159 138 138 ILE ILE C . n 
C 2 160 VAL 160 139 139 VAL VAL C . n 
C 2 161 GLY 161 140 140 GLY GLY C . n 
C 2 162 LEU 162 141 141 LEU LEU C . n 
C 2 163 TYR 163 142 142 TYR TYR C . n 
C 2 164 LYS 164 143 143 LYS LYS C . n 
C 2 165 ALA 165 144 144 ALA ALA C . n 
C 2 166 ILE 166 145 145 ILE ILE C . n 
C 2 167 GLN 167 146 146 GLN GLN C . n 
C 2 168 LYS 168 147 147 LYS LYS C . n 
C 2 169 ASP 169 148 148 ASP ASP C . n 
C 2 170 ASP 170 149 149 ASP ASP C . n 
C 2 171 GLU 171 150 150 GLU GLU C . n 
C 2 172 ILE 172 151 151 ILE ILE C . n 
C 2 173 SER 173 152 152 SER SER C . n 
C 2 174 LEU 174 153 153 LEU LEU C . n 
C 2 175 PHE 175 154 154 PHE PHE C . n 
C 2 176 LYS 176 155 155 LYS LYS C . n 
C 2 177 ALA 177 156 156 ALA ALA C . n 
C 2 178 MET 178 157 157 MET MET C . n 
C 2 179 VAL 179 158 158 VAL VAL C . n 
C 2 180 ALA 180 159 159 ALA ALA C . n 
C 2 181 SER 181 160 160 SER SER C . n 
C 2 182 VAL 182 161 161 VAL VAL C . n 
C 2 183 TYR 183 162 162 TYR TYR C . n 
C 2 184 LEU 184 163 163 LEU LEU C . n 
C 2 185 GLU 185 164 164 GLU GLU C . n 
C 2 186 SER 186 165 165 SER SER C . n 
C 2 187 PHE 187 166 166 PHE PHE C . n 
C 2 188 LEU 188 167 167 LEU LEU C . n 
C 2 189 PHE 189 168 168 PHE PHE C . n 
C 2 190 TYR 190 169 169 TYR TYR C . n 
C 2 191 SER 191 170 170 SER SER C . n 
C 2 192 GLY 192 171 171 GLY GLY C . n 
C 2 193 PHE 193 172 172 PHE PHE C . n 
C 2 194 TYR 194 173 173 TYR TYR C . n 
C 2 195 TYR 195 174 174 TYR TYR C . n 
C 2 196 PRO 196 175 175 PRO PRO C . n 
C 2 197 LEU 197 176 176 LEU LEU C . n 
C 2 198 TYR 198 177 177 TYR TYR C . n 
C 2 199 PHE 199 178 178 PHE PHE C . n 
C 2 200 TYR 200 179 179 TYR TYR C . n 
C 2 201 GLY 201 180 180 GLY GLY C . n 
C 2 202 GLN 202 181 181 GLN GLN C . n 
C 2 203 GLY 203 182 182 GLY GLY C . n 
C 2 204 LYS 204 183 183 LYS LYS C . n 
C 2 205 LEU 205 184 184 LEU LEU C . n 
C 2 206 MET 206 185 185 MET MET C . n 
C 2 207 GLN 207 186 186 GLN GLN C . n 
C 2 208 SER 208 187 187 SER SER C . n 
C 2 209 GLY 209 188 188 GLY GLY C . n 
C 2 210 GLU 210 189 189 GLU GLU C . n 
C 2 211 ILE 211 190 190 ILE ILE C . n 
C 2 212 ILE 212 191 191 ILE ILE C . n 
C 2 213 ASN 213 192 192 ASN ASN C . n 
C 2 214 LEU 214 193 193 LEU LEU C . n 
C 2 215 ILE 215 194 194 ILE ILE C . n 
C 2 216 LEU 216 195 195 LEU LEU C . n 
C 2 217 ARG 217 196 196 ARG ARG C . n 
C 2 218 ASP 218 197 197 ASP ASP C . n 
C 2 219 GLU 219 198 198 GLU GLU C . n 
C 2 220 ALA 220 199 199 ALA ALA C . n 
C 2 221 ILE 221 200 200 ILE ILE C . n 
C 2 222 HIS 222 201 201 HIS HIS C . n 
C 2 223 GLY 223 202 202 GLY GLY C . n 
C 2 224 VAL 224 203 203 VAL VAL C . n 
C 2 225 TYR 225 204 204 TYR TYR C . n 
C 2 226 VAL 226 205 205 VAL VAL C . n 
C 2 227 GLY 227 206 206 GLY GLY C . n 
C 2 228 LEU 228 207 207 LEU LEU C . n 
C 2 229 LEU 229 208 208 LEU LEU C . n 
C 2 230 ALA 230 209 209 ALA ALA C . n 
C 2 231 GLN 231 210 210 GLN GLN C . n 
C 2 232 GLU 232 211 211 GLU GLU C . n 
C 2 233 ILE 233 212 212 ILE ILE C . n 
C 2 234 TYR 234 213 213 TYR TYR C . n 
C 2 235 ASN 235 214 214 ASN ASN C . n 
C 2 236 LYS 236 215 215 LYS LYS C . n 
C 2 237 GLN 237 216 216 GLN GLN C . n 
C 2 238 THR 238 217 217 THR THR C . n 
C 2 239 GLU 239 218 218 GLU GLU C . n 
C 2 240 GLU 240 219 219 GLU GLU C . n 
C 2 241 LYS 241 220 220 LYS LYS C . n 
C 2 242 LYS 242 221 221 LYS LYS C . n 
C 2 243 ALA 243 222 222 ALA ALA C . n 
C 2 244 GLU 244 223 223 GLU GLU C . n 
C 2 245 LEU 245 224 224 LEU LEU C . n 
C 2 246 ARG 246 225 225 ARG ARG C . n 
C 2 247 GLU 247 226 226 GLU GLU C . n 
C 2 248 PHE 248 227 227 PHE PHE C . n 
C 2 249 ALA 249 228 228 ALA ALA C . n 
C 2 250 ILE 250 229 229 ILE ILE C . n 
C 2 251 ASP 251 230 230 ASP ASP C . n 
C 2 252 LEU 252 231 231 LEU LEU C . n 
C 2 253 LEU 253 232 232 LEU LEU C . n 
C 2 254 ASN 254 233 233 ASN ASN C . n 
C 2 255 GLN 255 234 234 GLN GLN C . n 
C 2 256 LEU 256 235 235 LEU LEU C . n 
C 2 257 TYR 257 236 236 TYR TYR C . n 
C 2 258 GLU 258 237 237 GLU GLU C . n 
C 2 259 ASN 259 238 238 ASN ASN C . n 
C 2 260 GLU 260 239 239 GLU GLU C . n 
C 2 261 LEU 261 240 240 LEU LEU C . n 
C 2 262 GLU 262 241 241 GLU GLU C . n 
C 2 263 TYR 263 242 242 TYR TYR C . n 
C 2 264 THR 264 243 243 THR THR C . n 
C 2 265 GLU 265 244 244 GLU GLU C . n 
C 2 266 ASP 266 245 245 ASP ASP C . n 
C 2 267 LEU 267 246 246 LEU LEU C . n 
C 2 268 TYR 268 247 247 TYR TYR C . n 
C 2 269 ASP 269 248 248 ASP ASP C . n 
C 2 270 GLN 270 249 249 GLN GLN C . n 
C 2 271 VAL 271 250 250 VAL VAL C . n 
C 2 272 GLY 272 251 251 GLY GLY C . n 
C 2 273 LEU 273 252 252 LEU LEU C . n 
C 2 274 SER 274 253 253 SER SER C . n 
C 2 275 HIS 275 254 254 HIS HIS C . n 
C 2 276 ASP 276 255 255 ASP ASP C . n 
C 2 277 VAL 277 256 256 VAL VAL C . n 
C 2 278 LYS 278 257 257 LYS LYS C . n 
C 2 279 LYS 279 258 258 LYS LYS C . n 
C 2 280 PHE 280 259 259 PHE PHE C . n 
C 2 281 ILE 281 260 260 ILE ILE C . n 
C 2 282 ARG 282 261 261 ARG ARG C . n 
C 2 283 TYR 283 262 262 TYR TYR C . n 
C 2 284 ASN 284 263 263 ASN ASN C . n 
C 2 285 ALA 285 264 264 ALA ALA C . n 
C 2 286 ASN 286 265 265 ASN ASN C . n 
C 2 287 LYS 287 266 266 LYS LYS C . n 
C 2 288 ALA 288 267 267 ALA ALA C . n 
C 2 289 LEU 289 268 268 LEU LEU C . n 
C 2 290 MET 290 269 269 MET MET C . n 
C 2 291 ASN 291 270 270 ASN ASN C . n 
C 2 292 LEU 292 271 271 LEU LEU C . n 
C 2 293 GLY 293 272 272 GLY GLY C . n 
C 2 294 PHE 294 273 273 PHE PHE C . n 
C 2 295 ASP 295 274 274 ASP ASP C . n 
C 2 296 PRO 296 275 275 PRO PRO C . n 
C 2 297 TYR 297 276 276 TYR TYR C . n 
C 2 298 PHE 298 277 277 PHE PHE C . n 
C 2 299 GLU 299 278 278 GLU GLU C . n 
C 2 300 GLU 300 279 279 GLU GLU C . n 
C 2 301 GLU 301 280 280 GLU GLU C . n 
C 2 302 ASP 302 281 281 ASP ASP C . n 
C 2 303 ILE 303 282 282 ILE ILE C . n 
C 2 304 ASN 304 283 283 ASN ASN C . n 
C 2 305 PRO 305 284 284 PRO PRO C . n 
C 2 306 ILE 306 285 285 ILE ILE C . n 
C 2 307 VAL 307 286 286 VAL VAL C . n 
C 2 308 LEU 308 287 287 LEU LEU C . n 
C 2 309 ASN 309 288 288 ASN ASN C . n 
C 2 310 GLY 310 289 289 GLY GLY C . n 
C 2 311 LEU 311 290 290 LEU LEU 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  16  ASP ASP D . n 
D 2 38  PHE 38  17  17  PHE PHE D . n 
D 2 39  THR 39  18  18  THR THR D . n 
D 2 40  GLN 40  19  19  GLN GLN D . n 
D 2 41  MET 41  20  20  MET MET D . n 
D 2 42  PHE 42  21  21  PHE PHE D . n 
D 2 43  TYR 43  22  22  TYR TYR D . n 
D 2 44  ASN 44  23  23  ASN ASN D . n 
D 2 45  GLN 45  24  24  GLN GLN D . n 
D 2 46  ASN 46  25  25  ASN ASN D . n 
D 2 47  VAL 47  26  26  VAL VAL D . n 
D 2 48  LYS 48  27  27  LYS LYS D . n 
D 2 49  GLN 49  28  28  GLN GLN D . n 
D 2 50  PHE 50  29  29  PHE PHE D . n 
D 2 51  TRP 51  30  30  TRP TRP D . n 
D 2 52  LEU 52  31  31  LEU LEU D . n 
D 2 53  PRO 53  32  32  PRO PRO D . n 
D 2 54  GLU 54  33  33  GLU GLU D . n 
D 2 55  GLU 55  34  34  GLU GLU D . n 
D 2 56  ILE 56  35  35  ILE ILE D . n 
D 2 57  ALA 57  36  36  ALA ALA D . n 
D 2 58  LEU 58  37  37  LEU LEU D . n 
D 2 59  ASN 59  38  38  ASN ASN D . n 
D 2 60  GLY 60  39  39  GLY GLY D . n 
D 2 61  ASP 61  40  40  ASP ASP D . n 
D 2 62  LEU 62  41  41  LEU LEU D . n 
D 2 63  LEU 63  42  42  LEU LEU D . n 
D 2 64  THR 64  43  43  THR THR D . n 
D 2 65  TRP 65  44  44  TRP TRP D . n 
D 2 66  LYS 66  45  45  LYS LYS D . n 
D 2 67  TYR 67  46  46  TYR TYR D . n 
D 2 68  LEU 68  47  47  LEU LEU D . n 
D 2 69  GLY 69  48  48  GLY GLY D . n 
D 2 70  LYS 70  49  49  LYS LYS D . n 
D 2 71  ASN 71  50  50  ASN ASN D . n 
D 2 72  GLU 72  51  51  GLU GLU D . n 
D 2 73  GLN 73  52  52  GLN GLN D . n 
D 2 74  ASP 74  53  53  ASP ASP D . n 
D 2 75  THR 75  54  54  THR THR D . n 
D 2 76  TYR 76  55  55  TYR TYR D . n 
D 2 77  MET 77  56  56  MET MET D . n 
D 2 78  LYS 78  57  57  LYS LYS D . n 
D 2 79  VAL 79  58  58  VAL VAL D . n 
D 2 80  LEU 80  59  59  LEU LEU D . n 
D 2 81  ALA 81  60  60  ALA ALA D . n 
D 2 82  GLY 82  61  61  GLY GLY D . n 
D 2 83  LEU 83  62  62  LEU LEU D . n 
D 2 84  THR 84  63  63  THR THR D . n 
D 2 85  LEU 85  64  64  LEU LEU D . n 
D 2 86  LEU 86  65  65  LEU LEU D . n 
D 2 87  ASP 87  66  66  ASP ASP D . n 
D 2 88  THR 88  67  67  THR THR D . n 
D 2 89  GLU 89  68  68  GLU GLU D . n 
D 2 90  GLN 90  69  69  GLN GLN D . n 
D 2 91  GLY 91  70  70  GLY GLY D . n 
D 2 92  ASN 92  71  71  ASN ASN D . n 
D 2 93  THR 93  72  72  THR THR D . n 
D 2 94  GLY 94  73  73  GLY GLY D . n 
D 2 95  MET 95  74  74  MET MET D . n 
D 2 96  PRO 96  75  75  PRO PRO D . n 
D 2 97  ILE 97  76  76  ILE ILE D . n 
D 2 98  VAL 98  77  77  VAL VAL D . n 
D 2 99  ALA 99  78  78  ALA ALA D . n 
D 2 100 GLU 100 79  79  GLU GLU D . n 
D 2 101 HIS 101 80  80  HIS HIS D . n 
D 2 102 VAL 102 81  81  VAL VAL D . n 
D 2 103 ASP 103 82  82  ASP ASP D . n 
D 2 104 GLY 104 83  83  GLY GLY D . n 
D 2 105 HIS 105 84  84  HIS HIS D . n 
D 2 106 GLN 106 85  85  GLN GLN D . n 
D 2 107 ARG 107 86  86  ARG ARG D . n 
D 2 108 LYS 108 87  87  LYS LYS D . n 
D 2 109 ALA 109 88  88  ALA ALA D . n 
D 2 110 VAL 110 89  89  VAL VAL D . n 
D 2 111 LEU 111 90  90  LEU LEU D . n 
D 2 112 ASN 112 91  91  ASN ASN D . n 
D 2 113 PHE 113 92  92  PHE PHE D . n 
D 2 114 MET 114 93  93  MET MET D . n 
D 2 115 ALA 115 94  94  ALA ALA D . n 
D 2 116 MET 116 95  95  MET MET D . n 
D 2 117 MET 117 96  96  MET MET D . n 
D 2 118 GLU 118 97  97  GLU GLU D . n 
D 2 119 ASN 119 98  98  ASN ASN D . n 
D 2 120 ALA 120 99  99  ALA ALA D . n 
D 2 121 VAL 121 100 100 VAL VAL D . n 
D 2 122 HIS 122 101 101 HIS HIS D . n 
D 2 123 ALA 123 102 102 ALA ALA D . n 
D 2 124 LYS 124 103 103 LYS LYS D . n 
D 2 125 SER 125 104 104 SER SER D . n 
D 2 126 TYR 126 105 105 TYR TYR D . n 
D 2 127 SER 127 106 106 SER SER D . n 
D 2 128 ASN 128 107 107 ASN ASN D . n 
D 2 129 ILE 129 108 108 ILE ILE D . n 
D 2 130 PHE 130 109 109 PHE PHE D . n 
D 2 131 MET 131 110 110 MET MET D . n 
D 2 132 THR 132 111 111 THR THR D . n 
D 2 133 LEU 133 112 112 LEU LEU D . n 
D 2 134 ALA 134 113 113 ALA ALA D . n 
D 2 135 PRO 135 114 114 PRO PRO D . n 
D 2 136 THR 136 115 115 THR THR D . n 
D 2 137 GLU 137 116 116 GLU GLU D . n 
D 2 138 THR 138 117 117 THR THR D . n 
D 2 139 ILE 139 118 118 ILE ILE D . n 
D 2 140 ASN 140 119 119 ASN ASN D . n 
D 2 141 GLU 141 120 120 GLU GLU D . n 
D 2 142 VAL 142 121 121 VAL VAL D . n 
D 2 143 PHE 143 122 122 PHE PHE D . n 
D 2 144 GLU 144 123 123 GLU GLU D . n 
D 2 145 TRP 145 124 124 TRP TRP D . n 
D 2 146 VAL 146 125 125 VAL VAL D . n 
D 2 147 LYS 147 126 126 LYS LYS D . n 
D 2 148 GLN 148 127 127 GLN GLN D . n 
D 2 149 ASN 149 128 128 ASN ASN D . n 
D 2 150 LYS 150 129 129 LYS LYS D . n 
D 2 151 TYR 151 130 130 TYR TYR D . n 
D 2 152 LEU 152 131 131 LEU LEU D . n 
D 2 153 GLN 153 132 132 GLN GLN D . n 
D 2 154 LYS 154 133 133 LYS LYS D . n 
D 2 155 LYS 155 134 134 LYS LYS D . n 
D 2 156 ALA 156 135 135 ALA ALA D . n 
D 2 157 GLN 157 136 136 GLN GLN D . n 
D 2 158 MET 158 137 137 MET MET D . n 
D 2 159 ILE 159 138 138 ILE ILE D . n 
D 2 160 VAL 160 139 139 VAL VAL D . n 
D 2 161 GLY 161 140 140 GLY GLY D . n 
D 2 162 LEU 162 141 141 LEU LEU D . n 
D 2 163 TYR 163 142 142 TYR TYR D . n 
D 2 164 LYS 164 143 143 LYS LYS D . n 
D 2 165 ALA 165 144 144 ALA ALA D . n 
D 2 166 ILE 166 145 145 ILE ILE D . n 
D 2 167 GLN 167 146 146 GLN GLN D . n 
D 2 168 LYS 168 147 147 LYS LYS D . n 
D 2 169 ASP 169 148 148 ASP ASP D . n 
D 2 170 ASP 170 149 149 ASP ASP D . n 
D 2 171 GLU 171 150 150 GLU GLU D . n 
D 2 172 ILE 172 151 151 ILE ILE D . n 
D 2 173 SER 173 152 152 SER SER D . n 
D 2 174 LEU 174 153 153 LEU LEU D . n 
D 2 175 PHE 175 154 154 PHE PHE D . n 
D 2 176 LYS 176 155 155 LYS LYS D . n 
D 2 177 ALA 177 156 156 ALA ALA D . n 
D 2 178 MET 178 157 157 MET MET D . n 
D 2 179 VAL 179 158 158 VAL VAL D . n 
D 2 180 ALA 180 159 159 ALA ALA D . n 
D 2 181 SER 181 160 160 SER SER D . n 
D 2 182 VAL 182 161 161 VAL VAL D . n 
D 2 183 TYR 183 162 162 TYR TYR D . n 
D 2 184 LEU 184 163 163 LEU LEU D . n 
D 2 185 GLU 185 164 164 GLU GLU D . n 
D 2 186 SER 186 165 165 SER SER D . n 
D 2 187 PHE 187 166 166 PHE PHE D . n 
D 2 188 LEU 188 167 167 LEU LEU D . n 
D 2 189 PHE 189 168 168 PHE PHE D . n 
D 2 190 TYR 190 169 169 TYR TYR D . n 
D 2 191 SER 191 170 170 SER SER D . n 
D 2 192 GLY 192 171 171 GLY GLY D . n 
D 2 193 PHE 193 172 172 PHE PHE D . n 
D 2 194 TYR 194 173 173 TYR TYR D . n 
D 2 195 TYR 195 174 174 TYR TYR D . n 
D 2 196 PRO 196 175 175 PRO PRO D . n 
D 2 197 LEU 197 176 176 LEU LEU D . n 
D 2 198 TYR 198 177 177 TYR TYR D . n 
D 2 199 PHE 199 178 178 PHE PHE D . n 
D 2 200 TYR 200 179 179 TYR TYR D . n 
D 2 201 GLY 201 180 180 GLY GLY D . n 
D 2 202 GLN 202 181 181 GLN GLN D . n 
D 2 203 GLY 203 182 182 GLY GLY D . n 
D 2 204 LYS 204 183 183 LYS LYS D . n 
D 2 205 LEU 205 184 184 LEU LEU D . n 
D 2 206 MET 206 185 185 MET MET D . n 
D 2 207 GLN 207 186 186 GLN GLN D . n 
D 2 208 SER 208 187 187 SER SER D . n 
D 2 209 GLY 209 188 188 GLY GLY D . n 
D 2 210 GLU 210 189 189 GLU GLU D . n 
D 2 211 ILE 211 190 190 ILE ILE D . n 
D 2 212 ILE 212 191 191 ILE ILE D . n 
D 2 213 ASN 213 192 192 ASN ASN D . n 
D 2 214 LEU 214 193 193 LEU LEU D . n 
D 2 215 ILE 215 194 194 ILE ILE D . n 
D 2 216 LEU 216 195 195 LEU LEU D . n 
D 2 217 ARG 217 196 196 ARG ARG D . n 
D 2 218 ASP 218 197 197 ASP ASP D . n 
D 2 219 GLU 219 198 198 GLU GLU D . n 
D 2 220 ALA 220 199 199 ALA ALA D . n 
D 2 221 ILE 221 200 200 ILE ILE D . n 
D 2 222 HIS 222 201 201 HIS HIS D . n 
D 2 223 GLY 223 202 202 GLY GLY D . n 
D 2 224 VAL 224 203 203 VAL VAL D . n 
D 2 225 TYR 225 204 204 TYR TYR D . n 
D 2 226 VAL 226 205 205 VAL VAL D . n 
D 2 227 GLY 227 206 206 GLY GLY D . n 
D 2 228 LEU 228 207 207 LEU LEU D . n 
D 2 229 LEU 229 208 208 LEU LEU D . n 
D 2 230 ALA 230 209 209 ALA ALA D . n 
D 2 231 GLN 231 210 210 GLN GLN D . n 
D 2 232 GLU 232 211 211 GLU GLU D . n 
D 2 233 ILE 233 212 212 ILE ILE D . n 
D 2 234 TYR 234 213 213 TYR TYR D . n 
D 2 235 ASN 235 214 214 ASN ASN D . n 
D 2 236 LYS 236 215 215 LYS LYS D . n 
D 2 237 GLN 237 216 216 GLN GLN D . n 
D 2 238 THR 238 217 217 THR THR D . n 
D 2 239 GLU 239 218 218 GLU GLU D . n 
D 2 240 GLU 240 219 219 GLU GLU D . n 
D 2 241 LYS 241 220 220 LYS LYS D . n 
D 2 242 LYS 242 221 221 LYS LYS D . n 
D 2 243 ALA 243 222 222 ALA ALA D . n 
D 2 244 GLU 244 223 223 GLU GLU D . n 
D 2 245 LEU 245 224 224 LEU LEU D . n 
D 2 246 ARG 246 225 225 ARG ARG D . n 
D 2 247 GLU 247 226 226 GLU GLU D . n 
D 2 248 PHE 248 227 227 PHE PHE D . n 
D 2 249 ALA 249 228 228 ALA ALA D . n 
D 2 250 ILE 250 229 229 ILE ILE D . n 
D 2 251 ASP 251 230 230 ASP ASP D . n 
D 2 252 LEU 252 231 231 LEU LEU D . n 
D 2 253 LEU 253 232 232 LEU LEU D . n 
D 2 254 ASN 254 233 233 ASN ASN D . n 
D 2 255 GLN 255 234 234 GLN GLN D . n 
D 2 256 LEU 256 235 235 LEU LEU D . n 
D 2 257 TYR 257 236 236 TYR TYR D . n 
D 2 258 GLU 258 237 237 GLU GLU D . n 
D 2 259 ASN 259 238 238 ASN ASN D . n 
D 2 260 GLU 260 239 239 GLU GLU D . n 
D 2 261 LEU 261 240 240 LEU LEU D . n 
D 2 262 GLU 262 241 241 GLU GLU D . n 
D 2 263 TYR 263 242 242 TYR TYR D . n 
D 2 264 THR 264 243 243 THR THR D . n 
D 2 265 GLU 265 244 244 GLU GLU D . n 
D 2 266 ASP 266 245 245 ASP ASP D . n 
D 2 267 LEU 267 246 246 LEU LEU D . n 
D 2 268 TYR 268 247 247 TYR TYR D . n 
D 2 269 ASP 269 248 248 ASP ASP D . n 
D 2 270 GLN 270 249 249 GLN GLN D . n 
D 2 271 VAL 271 250 250 VAL VAL D . n 
D 2 272 GLY 272 251 251 GLY GLY D . n 
D 2 273 LEU 273 252 252 LEU LEU D . n 
D 2 274 SER 274 253 253 SER SER D . n 
D 2 275 HIS 275 254 254 HIS HIS D . n 
D 2 276 ASP 276 255 255 ASP ASP D . n 
D 2 277 VAL 277 256 256 VAL VAL D . n 
D 2 278 LYS 278 257 257 LYS LYS D . n 
D 2 279 LYS 279 258 258 LYS LYS D . n 
D 2 280 PHE 280 259 259 PHE PHE D . n 
D 2 281 ILE 281 260 260 ILE ILE D . n 
D 2 282 ARG 282 261 261 ARG ARG D . n 
D 2 283 TYR 283 262 262 TYR TYR D . n 
D 2 284 ASN 284 263 263 ASN ASN D . n 
D 2 285 ALA 285 264 264 ALA ALA D . n 
D 2 286 ASN 286 265 265 ASN ASN D . n 
D 2 287 LYS 287 266 266 LYS LYS D . n 
D 2 288 ALA 288 267 267 ALA ALA D . n 
D 2 289 LEU 289 268 268 LEU LEU D . n 
D 2 290 MET 290 269 269 MET MET D . n 
D 2 291 ASN 291 270 270 ASN ASN D . n 
D 2 292 LEU 292 271 271 LEU LEU D . n 
D 2 293 GLY 293 272 272 GLY GLY D . n 
D 2 294 PHE 294 273 273 PHE PHE D . n 
D 2 295 ASP 295 274 274 ASP ASP D . n 
D 2 296 PRO 296 275 275 PRO PRO D . n 
D 2 297 TYR 297 276 276 TYR TYR D . n 
D 2 298 PHE 298 277 277 PHE PHE D . n 
D 2 299 GLU 299 278 278 GLU GLU D . n 
D 2 300 GLU 300 279 279 GLU GLU D . n 
D 2 301 GLU 301 280 280 GLU GLU D . n 
D 2 302 ASP 302 281 281 ASP ASP D . n 
D 2 303 ILE 303 282 282 ILE ILE D . n 
D 2 304 ASN 304 283 283 ASN ASN D . n 
D 2 305 PRO 305 284 284 PRO PRO D . n 
D 2 306 ILE 306 285 285 ILE ILE D . n 
D 2 307 VAL 307 286 286 VAL VAL D . n 
D 2 308 LEU 308 287 287 LEU LEU D . n 
D 2 309 ASN 309 288 288 ASN ASN D . n 
D 2 310 GLY 310 289 289 GLY GLY D . n 
D 2 311 LEU 311 290 290 LEU LEU 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 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 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 . 
N 8 MN  1 401 401 MN  MN  C . 
O 8 MN  1 402 402 MN  MN  C . 
P 8 MN  1 401 401 MN  MN  D . 
Q 8 MN  1 402 402 MN  MN  D . 
# 
_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                   9BXS 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BXS 
_struct.title                        
'Consensus full-complex 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        9BXS 
_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 ? 
N N N 8 ? 
O N N 8 ? 
P N N 8 ? 
Q N N 8 ? 
# 
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 9BXS A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BXS B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BXS C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BXS D 22 ? 350 ? P50621 1 ? 329 ? 1 329 
5 3 9BXS 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 9BXS MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BXS GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BXS SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BXS SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BXS HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BXS HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BXS HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BXS HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BXS HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BXS HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BXS SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BXS SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BXS GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BXS LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BXS VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BXS PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BXS ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BXS GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BXS SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BXS HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BXS MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BXS MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BXS GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BXS SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BXS SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BXS HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BXS HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BXS HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BXS HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BXS HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BXS HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BXS SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BXS SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BXS GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BXS LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BXS VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BXS PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BXS ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BXS GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BXS SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BXS HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BXS 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,N,O,P,Q 
# 
_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 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P67  AH4 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P68  AH5 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P69  AH6 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P70  AH7 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P71  AH8 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P72  AH9 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P73  AI1 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P74  AI2 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P75  AI3 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P76  AI4 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P77  AI5 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P78  AI6 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P79  AI7 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P80  AI8 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P81  AI9 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P82  AJ1 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P83  AJ2 LYS C 337 ? PHE C 341 ? LYS C 316 PHE C 320 5 ? 5  
HELX_P HELX_P84  AJ3 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P85  AJ4 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P86  AJ5 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P87  AJ6 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P88  AJ7 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P89  AJ8 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P90  AJ9 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P91  AK1 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P92  AK2 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P93  AK3 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P94  AK4 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P95  AK5 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P96  AK6 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P97  AK7 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P98  AK8 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P99  AK9 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P100 AL1 ASN D 304 ? LEU D 311 ? ASN D 283 LEU D 290 1 ? 8  
HELX_P HELX_P101 AL2 CYS E 29  ? GLY E 47  ? CYS E 29  GLY E 47  1 ? 19 
HELX_P HELX_P102 AL3 ASN E 60  ? TYR E 67  ? ASN E 60  TYR E 67  1 ? 8  
HELX_P HELX_P103 AL4 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 ? ? ? ? ? ? ? 2.025 ? ? 
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 ? ? ? ? ? ? ? 2.660 ? ? 
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 .   O2A ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.211 ? ? 
metalc4  metalc ? ? J MG  .   MG  ? ? ? 1_555 K TTP .   O1B ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.881 ? ? 
metalc5  metalc ? ? J MG  .   MG  ? ? ? 1_555 K TTP .   O3G ? ? B MG  801 B TTP 802 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc6  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 O MN  .   MN  ? ? C ASP 66  C MN  402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc7  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 N MN  .   MN  ? ? C GLU 97  C MN  401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 O MN  .   MN  ? ? C GLU 97  C MN  402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc9  metalc ? ? C HIS 122 ND1 ? ? ? 1_555 O MN  .   MN  ? ? C HIS 101 C MN  402 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc10 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 N MN  .   MN  ? ? C GLU 164 C MN  401 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc11 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 N MN  .   MN  ? ? C GLU 164 C MN  401 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN  .   MN  ? ? C GLU 198 C MN  401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 O MN  .   MN  ? ? C GLU 198 C MN  402 1_555 ? ? ? ? ? ? ? 2.710 ? ? 
metalc14 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 O MN  .   MN  ? ? C GLU 198 C MN  402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc15 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 N MN  .   MN  ? ? C HIS 201 C MN  401 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 Q MN  .   MN  ? ? D ASP 66  D MN  402 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 Q MN  .   MN  ? ? D ASP 66  D MN  402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 P MN  .   MN  ? ? D GLU 97  D MN  401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc19 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 Q MN  .   MN  ? ? D GLU 97  D MN  402 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc20 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 Q MN  .   MN  ? ? D HIS 101 D MN  402 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 P MN  .   MN  ? ? D GLU 164 D MN  401 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 P MN  .   MN  ? ? D GLU 164 D MN  401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 P MN  .   MN  ? ? D GLU 198 D MN  401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc24 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 Q MN  .   MN  ? ? D GLU 198 D MN  402 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc25 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 P MN  .   MN  ? ? D HIS 201 D MN  401 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
# 
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  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  ? 
3  O2A ? K TTP .   ? B TTP 802 ? 1_555 MG ? J MG . ? B MG 801 ? 1_555 O3G ? K TTP .   ? B TTP 802 ? 1_555 92.1  ? 
4  O1B ? K TTP .   ? B TTP 802 ? 1_555 MG ? J MG . ? B MG 801 ? 1_555 O3G ? K TTP .   ? B TTP 802 ? 1_555 61.1  ? 
5  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
7  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
10 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
11 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
12 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
13 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
14 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? O MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
15 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
16 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
17 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 120.1 ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 78.3  ? 
20 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 142.1 ? 
21 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
22 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 114.2 ? 
23 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 103.9 ? 
24 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? N MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 98.4  ? 
25 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 58.6  ? 
26 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.4  ? 
27 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
29 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.1 ? 
30 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
31 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
32 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
33 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
34 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? Q MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
35 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.3 ? 
36 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.6  ? 
37 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.7 ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
40 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.7 ? 
41 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
42 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
43 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.5 ? 
44 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? P MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
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 1.74  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 2.45  
3 ILE 72  E . ? ILE 72  E PRO 73  E ? PRO 73  E 1 -9.71 
# 
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                   9BXS 
_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 
4 1 NH1 D ARG 86  ? ? OE2 D GLU 211 ? ? 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 ? ? 73.34   -7.48   
2  1 SER A 593 ? ? 61.31   -155.40 
3  1 ASN B 131 ? ? 60.21   61.11   
4  1 ASP B 215 ? ? 71.82   -3.80   
5  1 ASP B 238 ? ? -97.29  30.73   
6  1 MET B 240 ? ? 59.36   2.83    
7  1 SER B 593 ? ? 57.37   -159.10 
8  1 TYR B 626 ? ? -80.97  49.95   
9  1 THR C 72  ? ? -128.03 -59.07  
10 1 ASP C 148 ? ? 58.04   15.67   
11 1 PHE C 166 ? ? -125.60 -60.85  
12 1 THR D 72  ? ? -128.21 -58.37  
13 1 PHE D 166 ? ? -144.14 -61.18  
14 1 ASP D 317 ? ? 62.32   172.23  
15 1 ASP D 318 ? ? 68.57   -4.96   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BXS 
_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 4DR0 ? 16-290 'Rigid-body docking of residues 16-290 from beta dimer model 4DR0'                               ? 16-290 PDB 
'experimental model' 4DR0 2 
3 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                    9BXS 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.37 
_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               367506 
_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                        9BXS 
_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              9BXS 
_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                9BXS 
_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              9BXS 
_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 ASN 291 ? C ASN 312 
72  1 Y 1 C THR 292 ? C THR 313 
73  1 Y 1 C LYS 293 ? C LYS 314 
74  1 Y 1 C THR 294 ? C THR 315 
75  1 Y 1 C LYS 295 ? C LYS 316 
76  1 Y 1 C SER 296 ? C SER 317 
77  1 Y 1 C HIS 297 ? C HIS 318 
78  1 Y 1 C ASP 298 ? C ASP 319 
79  1 Y 1 C PHE 299 ? C PHE 320 
80  1 Y 1 C PHE 300 ? C PHE 321 
81  1 Y 1 C SER 301 ? C SER 322 
82  1 Y 1 C MET 302 ? C MET 323 
83  1 Y 1 C LYS 303 ? C LYS 324 
84  1 Y 1 C GLY 304 ? C GLY 325 
85  1 Y 1 C ASN 305 ? C ASN 326 
86  1 Y 1 C GLY 306 ? C GLY 327 
87  1 Y 1 C TYR 307 ? C TYR 328 
88  1 Y 1 C LYS 308 ? C LYS 329 
89  1 Y 1 C LYS 309 ? C LYS 330 
90  1 Y 1 C ALA 310 ? C ALA 331 
91  1 Y 1 C GLU 323 ? C GLU 344 
92  1 Y 1 C ASP 324 ? C ASP 345 
93  1 Y 1 C GLU 325 ? C GLU 346 
94  1 Y 1 C LYS 326 ? C LYS 347 
95  1 Y 1 C GLU 327 ? C GLU 348 
96  1 Y 1 C GLN 328 ? C GLN 349 
97  1 Y 1 C ILE 329 ? C ILE 350 
98  1 Y 1 D MET -20 ? D MET 1   
99  1 Y 1 D GLY -19 ? D GLY 2   
100 1 Y 1 D SER -18 ? D SER 3   
101 1 Y 1 D SER -17 ? D SER 4   
102 1 Y 1 D HIS -16 ? D HIS 5   
103 1 Y 1 D HIS -15 ? D HIS 6   
104 1 Y 1 D HIS -14 ? D HIS 7   
105 1 Y 1 D HIS -13 ? D HIS 8   
106 1 Y 1 D HIS -12 ? D HIS 9   
107 1 Y 1 D HIS -11 ? D HIS 10  
108 1 Y 1 D SER -10 ? D SER 11  
109 1 Y 1 D SER -9  ? D SER 12  
110 1 Y 1 D GLY -8  ? D GLY 13  
111 1 Y 1 D LEU -7  ? D LEU 14  
112 1 Y 1 D VAL -6  ? D VAL 15  
113 1 Y 1 D PRO -5  ? D PRO 16  
114 1 Y 1 D ARG -4  ? D ARG 17  
115 1 Y 1 D GLY -3  ? D GLY 18  
116 1 Y 1 D SER -2  ? D SER 19  
117 1 Y 1 D HIS -1  ? D HIS 20  
118 1 Y 1 D MET 0   ? D MET 21  
119 1 Y 1 D MET 1   ? D MET 22  
120 1 Y 1 D THR 2   ? D THR 23  
121 1 Y 1 D LYS 3   ? D LYS 24  
122 1 Y 1 D ILE 4   ? D ILE 25  
123 1 Y 1 D TYR 5   ? D TYR 26  
124 1 Y 1 D ASP 6   ? D ASP 27  
125 1 Y 1 D ALA 7   ? D ALA 28  
126 1 Y 1 D ALA 8   ? D ALA 29  
127 1 Y 1 D ASN 9   ? D ASN 30  
128 1 Y 1 D TRP 10  ? D TRP 31  
129 1 Y 1 D SER 11  ? D SER 32  
130 1 Y 1 D LYS 12  ? D LYS 33  
131 1 Y 1 D HIS 13  ? D HIS 34  
132 1 Y 1 D GLU 14  ? D GLU 35  
133 1 Y 1 D ASP 15  ? D ASP 36  
134 1 Y 1 D ASN 291 ? D ASN 312 
135 1 Y 1 D THR 292 ? D THR 313 
136 1 Y 1 D LYS 293 ? D LYS 314 
137 1 Y 1 D THR 294 ? D THR 315 
138 1 Y 1 D LYS 295 ? D LYS 316 
139 1 Y 1 D SER 296 ? D SER 317 
140 1 Y 1 D HIS 297 ? D HIS 318 
141 1 Y 1 D ASP 298 ? D ASP 319 
142 1 Y 1 D PHE 299 ? D PHE 320 
143 1 Y 1 D PHE 300 ? D PHE 321 
144 1 Y 1 D SER 301 ? D SER 322 
145 1 Y 1 D MET 302 ? D MET 323 
146 1 Y 1 D LYS 303 ? D LYS 324 
147 1 Y 1 D GLY 304 ? D GLY 325 
148 1 Y 1 D ASN 305 ? D ASN 326 
149 1 Y 1 D GLY 306 ? D GLY 327 
150 1 Y 1 D TYR 307 ? D TYR 328 
151 1 Y 1 D LYS 308 ? D LYS 329 
152 1 Y 1 D LYS 309 ? D LYS 330 
153 1 Y 1 D ALA 310 ? D ALA 331 
154 1 Y 1 D GLU 323 ? D GLU 344 
155 1 Y 1 D ASP 324 ? D ASP 345 
156 1 Y 1 D GLU 325 ? D GLU 346 
157 1 Y 1 D LYS 326 ? D LYS 347 
158 1 Y 1 D GLU 327 ? D GLU 348 
159 1 Y 1 D GLN 328 ? D GLN 349 
160 1 Y 1 D ILE 329 ? D ILE 350 
161 1 Y 1 E MET 1   ? E MET 1   
162 1 Y 1 E ALA 2   ? E ALA 2   
163 1 Y 1 E ILE 3   ? E ILE 3   
164 1 Y 1 E VAL 4   ? E VAL 4   
165 1 Y 1 E LYS 5   ? E LYS 5   
166 1 Y 1 E ALA 6   ? E ALA 6   
167 1 Y 1 E THR 7   ? E THR 7   
168 1 Y 1 E ASP 8   ? E ASP 8   
169 1 Y 1 E GLN 9   ? E GLN 9   
170 1 Y 1 E SER 10  ? E SER 10  
171 1 Y 1 E PHE 11  ? E PHE 11  
172 1 Y 1 E SER 12  ? E SER 12  
173 1 Y 1 E ALA 13  ? E ALA 13  
174 1 Y 1 E GLU 14  ? E GLU 14  
175 1 Y 1 E THR 15  ? E THR 15  
176 1 Y 1 E SER 16  ? E SER 16  
177 1 Y 1 E GLU 17  ? E GLU 17  
178 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 
MN  MN     MN N N 338 
PHE N      N  N N 339 
PHE CA     C  N S 340 
PHE C      C  N N 341 
PHE O      O  N N 342 
PHE CB     C  N N 343 
PHE CG     C  Y N 344 
PHE CD1    C  Y N 345 
PHE CD2    C  Y N 346 
PHE CE1    C  Y N 347 
PHE CE2    C  Y N 348 
PHE CZ     C  Y N 349 
PHE OXT    O  N N 350 
PHE H      H  N N 351 
PHE H2     H  N N 352 
PHE HA     H  N N 353 
PHE HB2    H  N N 354 
PHE HB3    H  N N 355 
PHE HD1    H  N N 356 
PHE HD2    H  N N 357 
PHE HE1    H  N N 358 
PHE HE2    H  N N 359 
PHE HZ     H  N N 360 
PHE HXT    H  N N 361 
PRO N      N  N N 362 
PRO CA     C  N S 363 
PRO C      C  N N 364 
PRO O      O  N N 365 
PRO CB     C  N N 366 
PRO CG     C  N N 367 
PRO CD     C  N N 368 
PRO OXT    O  N N 369 
PRO H      H  N N 370 
PRO HA     H  N N 371 
PRO HB2    H  N N 372 
PRO HB3    H  N N 373 
PRO HG2    H  N N 374 
PRO HG3    H  N N 375 
PRO HD2    H  N N 376 
PRO HD3    H  N N 377 
PRO HXT    H  N N 378 
SER N      N  N N 379 
SER CA     C  N S 380 
SER C      C  N N 381 
SER O      O  N N 382 
SER CB     C  N N 383 
SER OG     O  N N 384 
SER OXT    O  N N 385 
SER H      H  N N 386 
SER H2     H  N N 387 
SER HA     H  N N 388 
SER HB2    H  N N 389 
SER HB3    H  N N 390 
SER HG     H  N N 391 
SER HXT    H  N N 392 
THR N      N  N N 393 
THR CA     C  N S 394 
THR C      C  N N 395 
THR O      O  N N 396 
THR CB     C  N R 397 
THR OG1    O  N N 398 
THR CG2    C  N N 399 
THR OXT    O  N N 400 
THR H      H  N N 401 
THR H2     H  N N 402 
THR HA     H  N N 403 
THR HB     H  N N 404 
THR HG1    H  N N 405 
THR HG21   H  N N 406 
THR HG22   H  N N 407 
THR HG23   H  N N 408 
THR HXT    H  N N 409 
TRP N      N  N N 410 
TRP CA     C  N S 411 
TRP C      C  N N 412 
TRP O      O  N N 413 
TRP CB     C  N N 414 
TRP CG     C  Y N 415 
TRP CD1    C  Y N 416 
TRP CD2    C  Y N 417 
TRP NE1    N  Y N 418 
TRP CE2    C  Y N 419 
TRP CE3    C  Y N 420 
TRP CZ2    C  Y N 421 
TRP CZ3    C  Y N 422 
TRP CH2    C  Y N 423 
TRP OXT    O  N N 424 
TRP H      H  N N 425 
TRP H2     H  N N 426 
TRP HA     H  N N 427 
TRP HB2    H  N N 428 
TRP HB3    H  N N 429 
TRP HD1    H  N N 430 
TRP HE1    H  N N 431 
TRP HE3    H  N N 432 
TRP HZ2    H  N N 433 
TRP HZ3    H  N N 434 
TRP HH2    H  N N 435 
TRP HXT    H  N N 436 
TTP PA     P  N S 437 
TTP O1A    O  N N 438 
TTP O2A    O  N N 439 
TTP O3A    O  N N 440 
TTP PB     P  N S 441 
TTP O1B    O  N N 442 
TTP O2B    O  N N 443 
TTP O3B    O  N N 444 
TTP PG     P  N N 445 
TTP O1G    O  N N 446 
TTP O2G    O  N N 447 
TTP O3G    O  N N 448 
TTP "O5'"  O  N N 449 
TTP "C5'"  C  N N 450 
TTP "C4'"  C  N R 451 
TTP "O4'"  O  N N 452 
TTP "C3'"  C  N S 453 
TTP "O3'"  O  N N 454 
TTP "C2'"  C  N N 455 
TTP "C1'"  C  N R 456 
TTP N1     N  N N 457 
TTP C2     C  N N 458 
TTP O2     O  N N 459 
TTP N3     N  N N 460 
TTP C4     C  N N 461 
TTP O4     O  N N 462 
TTP C5     C  N N 463 
TTP C5M    C  N N 464 
TTP C6     C  N N 465 
TTP HOA2   H  N N 466 
TTP HOB2   H  N N 467 
TTP HOG2   H  N N 468 
TTP HOG3   H  N N 469 
TTP "H5'1" H  N N 470 
TTP "H5'2" H  N N 471 
TTP "H4'"  H  N N 472 
TTP "H3'"  H  N N 473 
TTP "HO3'" H  N N 474 
TTP "H2'1" H  N N 475 
TTP "H2'2" H  N N 476 
TTP "H1'"  H  N N 477 
TTP HN3    H  N N 478 
TTP HM51   H  N N 479 
TTP HM52   H  N N 480 
TTP HM53   H  N N 481 
TTP H6     H  N N 482 
TYR N      N  N N 483 
TYR CA     C  N S 484 
TYR C      C  N N 485 
TYR O      O  N N 486 
TYR CB     C  N N 487 
TYR CG     C  Y N 488 
TYR CD1    C  Y N 489 
TYR CD2    C  Y N 490 
TYR CE1    C  Y N 491 
TYR CE2    C  Y N 492 
TYR CZ     C  Y N 493 
TYR OH     O  N N 494 
TYR OXT    O  N N 495 
TYR H      H  N N 496 
TYR H2     H  N N 497 
TYR HA     H  N N 498 
TYR HB2    H  N N 499 
TYR HB3    H  N N 500 
TYR HD1    H  N N 501 
TYR HD2    H  N N 502 
TYR HE1    H  N N 503 
TYR HE2    H  N N 504 
TYR HH     H  N N 505 
TYR HXT    H  N N 506 
VAL N      N  N N 507 
VAL CA     C  N S 508 
VAL C      C  N N 509 
VAL O      O  N N 510 
VAL CB     C  N N 511 
VAL CG1    C  N N 512 
VAL CG2    C  N N 513 
VAL OXT    O  N N 514 
VAL H      H  N N 515 
VAL H2     H  N N 516 
VAL HA     H  N N 517 
VAL HB     H  N N 518 
VAL HG11   H  N N 519 
VAL HG12   H  N N 520 
VAL HG13   H  N N 521 
VAL HG21   H  N N 522 
VAL HG22   H  N N 523 
VAL HG23   H  N N 524 
VAL HXT    H  N N 525 
# 
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           9BXS 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              
'Consensus full-complex 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 ? ? RELION          ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION          ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? RELION          ? 
'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 'experimental model' PDB       4DR0 
3 'in silico model'    AlphaFold ?    
# 
_atom_sites.entry_id                    9BXS 
_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 
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 103.925 116.602 98.880  1.00 66.72  ? 6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.060 117.427 98.493  1.00 69.66  ? 6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 104.633 118.460 97.453  1.00 71.51  ? 6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 103.707 118.220 96.677  1.00 68.97  ? 6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.227 116.559 97.971  1.00 70.94  ? 6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.538 115.444 98.957  1.00 69.01  ? 6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 105.901 115.984 96.602  1.00 68.04  ? 6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.290 119.619 97.451  1.00 67.79  ? 7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 104.969 120.642 96.452  1.00 62.41  ? 7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 105.381 120.208 95.057  1.00 61.32  ? 7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.265 119.365 94.877  1.00 65.31  ? 7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 105.774 121.861 96.918  1.00 60.86  ? 7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.131 121.570 98.348  1.00 60.79  ? 7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.306 120.091 98.405  1.00 63.21  ? 7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 104.719 120.795 94.057  1.00 62.02  ? 8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 104.987 120.425 92.672  1.00 62.33  ? 8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 106.421 120.731 92.265  1.00 63.56  ? 8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.066 119.913 91.600  1.00 63.71  ? 8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.016 121.145 91.734  1.00 60.47  ? 8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.004 120.588 90.321  1.00 62.20  ? 8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 103.173 121.452 89.389  1.00 65.94  ? 8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 103.618 121.289 87.945  1.00 63.30  ? 8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 102.463 121.228 87.007  1.00 59.19  ? 8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 106.938 121.900 92.648  1.00 64.75  ? 9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.304 122.254 92.284  1.00 61.30  ? 9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 109.322 121.356 92.973  1.00 61.23  ? 9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 110.311 120.947 92.355  1.00 64.30  ? 9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 108.581 123.718 92.618  1.00 61.40  ? 9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.279 124.104 94.035  1.00 57.27  ? 9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.137 124.060 95.092  1.00 54.61  ? 9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.041 124.610 94.546  1.00 60.05  ? 9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 108.510 124.499 96.232  1.00 54.53  ? 9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.221 124.843 95.922  1.00 58.13  ? 9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 105.795 124.884 93.974  1.00 59.35  ? 9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.205 125.336 96.735  1.00 58.79  ? 9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 104.788 125.372 94.783  1.00 62.76  ? 9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 104.999 125.594 96.148  1.00 64.17  ? 9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.100 121.043 94.251  1.00 65.25  ? 10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.003 120.142 94.961  1.00 63.67  ? 10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 109.944 118.749 94.352  1.00 64.56  ? 10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 110.974 118.088 94.174  1.00 68.99  ? 10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 109.668 120.126 96.463  1.00 63.24  ? 10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.009 121.480 97.088  1.00 67.19  ? 10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.414 119.005 97.164  1.00 64.71  ? 10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.004 121.485 98.597  1.00 66.28  ? 10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 108.739 118.287 94.007  1.00 69.43  ? 11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 108.595 116.983 93.369  1.00 66.39  ? 11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.322 116.940 92.031  1.00 67.07  ? 11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 109.977 115.944 91.704  1.00 69.00  ? 11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 107.112 116.651 93.193  1.00 68.48  ? 11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 106.789 115.820 91.965  1.00 72.19  ? 11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 105.336 115.942 91.550  1.00 71.26  ? 11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 104.438 115.956 92.391  1.00 67.89  ? 11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 105.099 116.032 90.246  1.00 67.31  ? 11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.222 118.015 91.246  1.00 67.51  ? 12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 109.948 118.078 89.981  1.00 67.61  ? 12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 111.453 118.113 90.213  1.00 68.28  ? 12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.224 117.557 89.421  1.00 70.50  ? 12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 109.500 119.299 89.179  1.00 65.54  ? 12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 108.347 119.087 88.198  1.00 66.51  ? 12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 107.808 120.421 87.708  1.00 68.14  ? 12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 108.790 118.224 87.031  1.00 68.34  ? 12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 111.889 118.770 91.289  1.00 69.12  ? 13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.312 118.807 91.608  1.00 67.70  ? 13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 113.834 117.422 91.968  1.00 71.07  ? 13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 114.983 117.085 91.663  1.00 74.62  ? 13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 113.569 119.792 92.748  1.00 67.02  ? 13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 114.998 119.742 93.251  1.00 68.16  ? 13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 115.313 119.012 94.189  1.00 67.67  ? 13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 115.873 120.520 92.625  1.00 72.73  ? 13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.005 116.604 92.622  1.00 72.31  ? 14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 113.418 115.249 92.967  1.00 71.85  ? 14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 113.557 114.343 91.750  1.00 72.74  ? 14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.125 113.254 91.875  1.00 77.20  ? 14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 112.435 114.627 93.960  1.00 72.41  ? 14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 112.230 115.485 95.190  1.00 73.92  ? 14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 111.099 115.735 95.606  1.00 76.55  ? 14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.326 115.946 95.778  1.00 73.37  ? 14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.059 114.760 90.586  1.00 75.68  ? 15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.240 113.991 89.363  1.00 78.54  ? 15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 114.623 114.173 88.753  1.00 78.61  ? 15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 114.920 113.539 87.736  1.00 78.66  ? 15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.167 114.363 88.336  1.00 77.92  ? 15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 110.797 114.609 88.937  1.00 79.59  ? 15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 109.691 113.902 88.180  1.00 81.39  ? 15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.000 113.192 87.200  1.00 78.74  ? 15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 108.513 114.055 88.566  1.00 80.39  ? 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 115.462 115.029 89.340  1.00 78.78  ? 16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 116.844 115.148 88.885  1.00 79.04  ? 16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 117.574 113.825 89.080  1.00 77.00  ? 16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.282 113.346 88.187  1.00 78.29  ? 16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 117.555 116.298 89.623  1.00 80.76  ? 16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 116.945 117.650 89.240  1.00 74.37  ? 16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.049 116.275 89.338  1.00 79.12  ? 16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 117.477 118.229 87.953  1.00 74.11  ? 16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 117.399 113.209 90.250  1.00 78.29  ? 17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.074 111.958 90.569  1.00 80.32  ? 17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 117.369 110.733 90.004  1.00 80.53  ? 17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 117.967 109.651 89.988  1.00 79.82  ? 17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.218 111.811 92.085  1.00 79.64  ? 17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 118.667 113.080 92.782  1.00 80.88  ? 17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.409 113.443 92.498  1.00 92.51  ? 17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 121.184 112.368 93.702  1.00 81.01  ? 17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.125 110.863 89.547  1.00 80.80  ? 18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 115.450 109.757 88.880  1.00 81.52  ? 18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 116.069 109.617 87.497  1.00 82.75  ? 18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 115.855 110.458 86.615  1.00 83.07  ? 18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 113.926 109.969 88.812  1.00 81.00  ? 18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.292 109.669 90.172  1.00 79.90  ? 18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 113.303 109.072 87.753  1.00 79.43  ? 18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 112.304 110.712 90.636  1.00 80.83  ? 18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 116.862 108.568 87.309  1.00 85.59  ? 19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 117.675 108.430 86.110  1.00 84.68  ? 19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 116.910 107.684 85.026  1.00 86.89  ? 19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 116.419 106.572 85.252  1.00 87.36  ? 19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 118.976 107.700 86.439  1.00 84.19  ? 19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.036 108.585 87.074  1.00 83.60  ? 19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 121.440 108.218 86.639  1.00 86.31  ? 19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 121.834 108.465 85.501  1.00 87.08  ? 19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 122.205 107.626 87.550  1.00 84.26  ? 19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 116.809 108.298 83.852  1.00 91.62  ? 20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 116.216 107.675 82.677  1.00 92.85  ? 20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 117.269 107.590 81.583  1.00 93.61  ? 20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 117.991 108.563 81.335  1.00 90.03  ? 20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 114.983 108.450 82.196  1.00 91.33  ? 20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.243 109.904 81.843  1.00 92.56  ? 20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 114.382 110.352 80.675  1.00 93.30  ? 20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 114.760 109.614 79.403  1.00 92.94  ? 20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 116.228 109.655 79.168  1.00 92.57  ? 20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 117.371 106.418 80.953  1.00 94.77  ? 21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 118.378 106.145 79.926  1.00 95.05  ? 21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 119.794 106.341 80.466  1.00 94.89  ? 21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 120.712 106.702 79.725  1.00 92.13  ? 21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 118.147 107.005 78.677  1.00 95.60  ? 21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 118.849 106.457 77.449  1.00 95.15  ? 21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 118.377 105.441 76.896  1.00 93.81  ? 21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 119.871 107.042 77.034  1.00 94.95  ? 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 119.981 106.108 81.764  1.00 90.47  ? 22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 121.293 106.213 82.365  1.00 88.25  ? 22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 121.798 107.619 82.588  1.00 88.35  ? 22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 122.966 107.790 82.948  1.00 86.80  ? 22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 120.960 108.634 82.389  1.00 88.20  ? 23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 121.361 110.026 82.528  1.00 85.56  ? 23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 120.432 110.740 83.500  1.00 85.99  ? 23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 119.226 110.475 83.529  1.00 86.88  ? 23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 121.345 110.749 81.175  1.00 85.01  ? 23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 121.648 109.858 79.980  1.00 89.09  ? 23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.104 109.424 79.958  1.00 88.31  ? 23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.010 110.552 79.505  1.00 86.05  ? 23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 123.360 111.403 78.470  1.00 84.85  ? 23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 121.000 111.643 84.295  1.00 77.81  ? 24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 120.197 112.461 85.192  1.00 75.23  ? 24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 119.298 113.394 84.391  1.00 77.80  ? 24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 119.688 113.906 83.337  1.00 76.42  ? 24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 121.095 113.275 86.123  1.00 71.96  ? 24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 121.770 112.457 87.187  1.00 73.01  ? 24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 121.149 112.227 88.401  1.00 74.68  ? 24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.027 111.920 86.972  1.00 73.70  ? 24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 121.768 111.477 89.382  1.00 75.09  ? 24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 123.650 111.167 87.948  1.00 76.12  ? 24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.019 110.948 89.155  1.00 76.08  ? 24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 118.085 113.616 84.896  1.00 79.47  ? 25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 117.119 114.495 84.235  1.00 76.36  ? 25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 117.391 115.942 84.645  1.00 78.93  ? 25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 116.645 116.568 85.401  1.00 81.94  ? 25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 115.695 114.078 84.573  1.00 79.51  ? 25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 115.328 112.680 84.116  1.00 78.54  ? 25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 113.907 112.308 84.480  1.00 79.43  ? 25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 112.966 112.611 83.746  1.00 78.44  ? 25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 113.742 111.650 85.620  1.00 80.41  ? 25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 118.495 116.476 84.117  1.00 75.07  ? 26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 118.896 117.836 84.462  1.00 70.70  ? 26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 117.916 118.869 83.923  1.00 69.40  ? 26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 117.770 119.948 84.509  1.00 67.68  ? 26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 120.306 118.113 83.940  1.00 68.80  ? 26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 121.382 117.387 84.695  1.00 67.51  ? 26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 121.427 117.435 86.077  1.00 66.67  ? 26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 122.344 116.653 84.023  1.00 66.25  ? 26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 122.414 116.768 86.775  1.00 68.39  ? 26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 123.334 115.984 84.715  1.00 66.67  ? 26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 123.368 116.042 86.093  1.00 70.25  ? 26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 117.238 118.563 82.815  1.00 78.17  ? 27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 116.256 119.489 82.263  1.00 78.01  ? 27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.042 119.654 83.167  1.00 79.28  ? 27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 114.296 120.626 83.010  1.00 78.41  ? 27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 115.812 119.023 80.877  1.00 78.82  ? 27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 115.904 120.122 79.836  1.00 82.43  ? 27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.218 121.271 80.210  1.00 80.15  ? 27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 115.659 119.837 78.645  1.00 80.62  ? 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 114.825 118.728 84.103  1.00 75.78  ? 28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 113.726 118.865 85.052  1.00 76.00  ? 28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 113.914 120.051 85.987  1.00 76.71  ? 28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 112.932 120.529 86.565  1.00 78.00  ? 28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 113.573 117.583 85.873  1.00 74.64  ? 28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 112.964 116.419 85.110  1.00 77.78  ? 28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 111.452 116.391 85.256  1.00 78.18  ? 28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 110.783 115.912 83.981  1.00 76.83  ? 28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 111.142 116.760 82.811  1.00 75.56  ? 28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.149 120.530 86.154  1.00 72.97  ? 29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 115.394 121.633 87.076  1.00 71.75  ? 29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 114.744 122.923 86.592  1.00 69.87  ? 29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.172 123.667 87.392  1.00 70.97  ? 29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 116.894 121.828 87.279  1.00 71.70  ? 29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.251 122.127 88.722  1.00 71.39  ? 29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.497 121.702 89.622  1.00 69.88  ? 29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.289 122.780 88.957  1.00 70.82  ? 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 114.813 123.203 85.287  1.00 73.26  ? 30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.155 124.393 84.755  1.00 73.11  ? 30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 112.646 124.316 84.953  1.00 76.35  ? 30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.003 125.312 85.311  1.00 77.75  ? 30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 114.494 124.563 83.274  1.00 72.92  ? 30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 115.977 124.723 82.993  1.00 76.28  ? 30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 116.257 124.717 81.499  1.00 77.87  ? 30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 117.733 124.487 81.215  1.00 78.01  ? 30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 117.950 123.817 79.903  1.00 76.63  ? 30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.064 123.136 84.723  1.00 73.60  ? 31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 110.660 122.927 85.053  1.00 71.97  ? 31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 110.405 123.160 86.533  1.00 71.56  ? 31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.341 123.665 86.907  1.00 71.79  ? 31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 110.232 121.514 84.659  1.00 72.37  ? 31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 109.847 121.363 83.199  1.00 75.11  ? 31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.362 120.071 82.596  1.00 77.98  ? 31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 110.010 118.991 83.115  1.00 78.82  ? 31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.119 120.136 81.606  1.00 73.53  ? 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.370 122.808 87.387  1.00 62.95  ? 32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.223 123.073 88.813  1.00 61.92  ? 32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.178 124.570 89.096  1.00 64.23  ? 32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.376 125.018 89.920  1.00 65.53  ? 32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.352 122.406 89.596  1.00 63.51  ? 32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.020 125.362 88.424  1.00 64.37  ? 33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 111.975 126.813 88.612  1.00 60.08  ? 33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 110.634 127.364 88.149  1.00 60.57  ? 33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.025 128.208 88.817  1.00 64.66  ? 33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.135 127.505 87.873  1.00 61.97  ? 33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 112.995 129.016 87.981  1.00 61.90  ? 33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.465 127.063 88.411  1.00 63.28  ? 33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.168 126.912 86.982  1.00 64.58  ? 34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 108.898 127.407 86.458  1.00 65.81  ? 34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 107.750 127.079 87.404  1.00 68.41  ? 34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 106.914 127.939 87.709  1.00 70.74  ? 34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 108.641 126.818 85.071  1.00 69.17  ? 34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 107.828 127.703 84.180  1.00 69.74  ? 34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 106.603 128.212 84.556  1.00 71.06  ? 34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.062 128.170 82.931  1.00 69.83  ? 34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.118 128.954 83.577  1.00 71.98  ? 34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 106.984 128.945 82.579  1.00 71.75  ? 34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 107.702 125.836 87.889  1.00 66.93  ? 35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 106.654 125.437 88.821  1.00 62.76  ? 35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 106.749 126.225 90.120  1.00 63.12  ? 35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 105.739 126.720 90.632  1.00 67.50  ? 35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 106.739 123.936 89.092  1.00 63.01  ? 35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 105.960 123.574 90.217  1.00 67.11  ? 35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 107.962 126.357 90.665  1.00 60.24  ? 36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.158 127.114 91.895  1.00 59.27  ? 36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.621 128.525 91.753  1.00 56.73  ? 36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 106.795 128.971 92.557  1.00 58.27  ? 36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 109.644 127.138 92.255  1.00 56.27  ? 36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 109.965 127.870 93.537  1.00 53.87  ? 36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.397 127.486 94.742  1.00 58.68  ? 36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 110.844 128.945 93.541  1.00 55.82  ? 36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 109.694 128.150 95.914  1.00 57.16  ? 36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.144 129.616 94.707  1.00 59.96  ? 36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.566 129.215 95.892  1.00 59.40  ? 36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 110.863 129.882 97.058  1.00 60.34  ? 36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.045 129.230 90.704  1.00 60.59  ? 37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 107.582 130.596 90.507  1.00 61.03  ? 37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.068 130.640 90.365  1.00 67.33  ? 37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.383 131.233 91.204  1.00 69.93  ? 37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.277 131.219 89.298  1.00 60.48  ? 37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 109.519 131.977 89.655  1.00 65.70  ? 37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.741 131.333 89.724  1.00 65.49  ? 37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 109.459 133.327 89.950  1.00 64.10  ? 37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.881 132.026 90.065  1.00 62.74  ? 37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 110.598 134.024 90.290  1.00 65.75  ? 37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 111.811 133.373 90.348  1.00 64.68  ? 37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 105.527 129.921 89.376  1.00 70.51  ? 38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.109 130.036 89.044  1.00 69.40  ? 38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.231 129.682 90.240  1.00 68.49  ? 38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.221 130.347 90.500  1.00 70.02  ? 38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 103.783 129.160 87.820  1.00 68.13  ? 38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 102.281 128.968 87.676  1.00 71.66  ? 38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.368 129.776 86.561  1.00 64.15  ? 38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 103.601 128.649 90.998  1.00 65.82  ? 39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 102.723 128.153 92.049  1.00 70.26  ? 39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 102.950 128.803 93.407  1.00 72.31  ? 39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.028 128.803 94.230  1.00 74.80  ? 39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 102.875 126.635 92.183  1.00 69.32  ? 39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 102.785 125.920 90.849  1.00 72.92  ? 39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.106 126.439 89.939  1.00 72.15  ? 39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 103.391 124.837 90.711  1.00 74.82  ? 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.135 129.354 93.677  1.00 67.09  ? 40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.422 129.936 94.980  1.00 67.39  ? 40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 104.743 131.419 94.899  1.00 72.44  ? 40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.126 132.224 95.606  1.00 73.70  ? 40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.588 129.171 95.628  1.00 61.70  ? 40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 105.818 129.454 97.098  1.00 63.55  ? 40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 104.838 130.045 97.881  1.00 66.16  ? 40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.021 129.120 97.702  1.00 67.06  ? 40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.054 130.298 99.223  1.00 70.26  ? 40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.247 129.369 99.039  1.00 68.13  ? 40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.261 129.958 99.796  1.00 72.19  ? 40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.481 130.208 101.131 1.00 70.60  ? 40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.678 131.808 94.031  1.00 64.93  ? 41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.214 133.161 94.070  1.00 59.65  ? 41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.210 134.151 93.501  1.00 62.39  ? 41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 104.781 135.083 94.190  1.00 68.97  ? 41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 107.555 133.218 93.315  1.00 62.86  ? 41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.583 132.299 93.978  1.00 63.14  ? 41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.079 134.639 93.258  1.00 61.63  ? 41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 108.733 132.517 95.462  1.00 58.66  ? 41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 104.794 133.945 92.249  1.00 61.71  ? 42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 103.855 134.866 91.618  1.00 67.21  ? 42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 102.564 134.987 92.415  1.00 70.80  ? 42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 101.904 136.032 92.374  1.00 70.10  ? 42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 103.559 134.413 90.189  1.00 66.63  ? 42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 104.806 134.324 89.336  1.00 68.49  ? 42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 105.855 134.859 89.696  1.00 71.56  ? 42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 104.700 133.648 88.198  1.00 70.03  ? 42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.186 133.934 93.141  1.00 72.76  ? 43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.012 134.006 93.999  1.00 70.78  ? 43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.283 134.767 95.291  1.00 71.92  ? 43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.411 135.509 95.758  1.00 72.54  ? 43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 100.507 132.598 94.317  1.00 69.36  ? 43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 100.614 131.624 93.156  1.00 71.62  ? 43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 99.906  132.121 91.912  1.00 75.15  ? 43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 98.771  132.594 91.976  1.00 72.70  ? 43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 100.576 132.022 90.770  1.00 76.02  ? 43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 102.471 134.607 95.883  1.00 67.05  ? 44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 102.771 135.196 97.183  1.00 68.17  ? 44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 103.758 136.358 97.108  1.00 66.87  ? 44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.507 136.587 98.063  1.00 69.42  ? 44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 103.290 134.131 98.152  1.00 65.30  ? 44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.398 132.905 98.210  1.00 70.11  ? 44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 101.591 132.665 97.317  1.00 71.14  ? 44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 102.527 132.135 99.284  1.00 70.45  ? 44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 103.781 137.094 96.001  1.00 62.86  ? 45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.474 138.376 95.939  1.00 66.54  ? 45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.454 139.502 95.892  1.00 67.01  ? 45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.524 139.473 95.079  1.00 66.99  ? 45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.410 138.471 94.731  1.00 65.65  ? 45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 104.667 138.294 93.517  1.00 65.48  ? 45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.543 137.465 94.830  1.00 68.25  ? 45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.632 140.491 96.767  1.00 64.32  ? 46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 102.733 141.638 96.800  1.00 63.06  ? 46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 102.944 142.457 95.534  1.00 64.94  ? 46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.056 142.920 95.255  1.00 65.60  ? 46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 102.970 142.485 98.056  1.00 61.48  ? 46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 101.903 143.559 98.178  1.00 66.10  ? 46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 102.995 141.608 99.292  1.00 62.35  ? 46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 101.877 142.636 94.764  1.00 69.39  ? 47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 101.928 143.397 93.526  1.00 71.29  ? 47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.171 144.704 93.705  1.00 74.11  ? 47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.058 144.721 94.240  1.00 73.57  ? 47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.337 142.604 92.356  1.00 72.33  ? 47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 101.505 143.278 91.024  1.00 76.19  ? 47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 102.767 143.471 90.486  1.00 73.04  ? 47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.403 143.719 90.310  1.00 73.31  ? 47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 102.926 144.091 89.261  1.00 71.76  ? 47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 100.556 144.339 89.085  1.00 71.80  ? 47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 101.819 144.525 88.560  1.00 70.80  ? 47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 101.783 145.794 93.255  1.00 70.03  ? 48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.219 147.127 93.378  1.00 67.26  ? 48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 100.872 147.663 91.997  1.00 69.74  ? 48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.415 147.213 90.984  1.00 70.05  ? 48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.190 148.079 94.087  1.00 66.66  ? 48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.637 147.597 95.441  1.00 70.56  ? 48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 103.671 146.683 95.565  1.00 68.43  ? 48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 102.029 148.070 96.591  1.00 71.78  ? 48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 104.084 146.247 96.810  1.00 64.36  ? 48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 102.437 147.638 97.838  1.00 69.40  ? 48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.466 146.725 97.947  1.00 65.20  ? 48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 99.949  148.628 91.969  1.00 75.54  ? 49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.477  149.171 90.699  1.00 78.28  ? 49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.604 149.824 89.910  1.00 78.31  ? 49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.567 149.843 88.673  1.00 79.18  ? 49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.351  150.175 90.947  1.00 77.63  ? 49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.078  149.550 91.428  1.00 80.66  ? 49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.025  148.273 91.945  1.00 79.67  ? 49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 95.812  150.028 91.475  1.00 79.58  ? 49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 95.780  147.991 92.288  1.00 76.12  ? 49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.025  149.039 92.013  1.00 77.40  ? 49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.607 150.361 90.599  1.00 70.90  ? 50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 102.759 150.961 89.945  1.00 71.44  ? 50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 103.935 150.954 90.912  1.00 71.71  ? 50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.787 150.659 92.100  1.00 72.46  ? 50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.442 152.377 89.438  1.00 70.91  ? 50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.158 153.364 90.561  1.00 72.53  ? 50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.148 153.009 91.739  1.00 70.49  ? 50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.926 154.618 90.193  1.00 73.66  ? 50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.117 151.271 90.380  1.00 62.49  ? 51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.314 151.304 91.213  1.00 64.61  ? 51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.231 152.395 92.272  1.00 67.05  ? 51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 106.818 152.258 93.350  1.00 67.75  ? 51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.554 151.501 90.342  1.00 64.87  ? 51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 108.906 151.532 91.057  1.00 63.01  ? 51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.121 150.261 91.861  1.00 61.20  ? 51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.030 151.739 90.062  1.00 65.27  ? 51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.511 153.483 91.985  1.00 67.15  ? 52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.369 154.556 92.963  1.00 65.44  ? 52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.670 154.066 94.222  1.00 67.82  ? 52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.112 154.353 95.342  1.00 67.18  ? 52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 104.604 155.727 92.346  1.00 67.04  ? 52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.502 156.948 93.240  1.00 68.15  ? 52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.874 157.406 93.700  1.00 71.57  ? 52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.791 158.729 94.441  1.00 68.13  ? 52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 105.853 159.884 93.506  1.00 65.10  ? 52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.578 153.314 94.058  1.00 75.56  ? 53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 102.863 152.786 95.215  1.00 74.41  ? 53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.729 151.810 95.996  1.00 72.61  ? 53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.717 151.813 97.232  1.00 72.21  ? 53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.564 152.116 94.769  1.00 73.63  ? 53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.612 151.787 95.906  1.00 73.46  ? 53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.433  150.949 95.455  1.00 77.58  ? 53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.393  150.568 94.266  1.00 78.00  ? 53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 98.546  150.671 96.288  1.00 75.50  ? 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.490 150.968 95.294  1.00 66.68  ? 54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.366 150.018 95.973  1.00 68.35  ? 54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.437 150.738 96.781  1.00 62.93  ? 54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.703 150.385 97.937  1.00 65.14  ? 54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.009 149.078 94.954  1.00 67.52  ? 54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.103 148.208 95.538  1.00 64.73  ? 54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.604 147.199 94.528  1.00 64.15  ? 54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.456 146.136 95.194  1.00 64.59  ? 54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.527 144.896 94.376  1.00 68.72  ? 54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.068 151.751 96.185  1.00 62.77  ? 55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.103 152.495 96.892  1.00 63.12  ? 55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.528 153.229 98.095  1.00 67.05  ? 55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.138 153.242 99.172  1.00 69.94  ? 55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.787 153.476 95.940  1.00 65.17  ? 55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.668 152.858 94.852  1.00 66.38  ? 55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.211 153.942 93.939  1.00 63.80  ? 55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.799 152.047 95.463  1.00 62.41  ? 55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.354 153.844 97.936  1.00 71.43  ? 56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.723 154.522 99.065  1.00 68.85  ? 56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.384 153.539 100.177 1.00 68.23  ? 56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.611 153.825 101.357 1.00 67.72  ? 56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.473 155.265 98.598  1.00 69.78  ? 56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 104.791 156.397 97.642  1.00 74.08  ? 56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 105.922 156.429 97.112  1.00 73.49  ? 56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 103.913 157.258 97.425  1.00 72.11  ? 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.856 152.367 99.818  1.00 67.84  ? 57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.531 151.358 100.820 1.00 67.33  ? 57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.779 150.886 101.552 1.00 69.48  ? 57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.756 150.690 102.772 1.00 74.85  ? 57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.814 150.180 100.154 1.00 65.24  ? 57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.557 148.996 101.062 1.00 65.88  ? 57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 104.499 147.986 101.207 1.00 67.72  ? 57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 102.367 148.886 101.767 1.00 69.82  ? 57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 104.268 146.906 102.033 1.00 72.32  ? 57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 102.125 147.807 102.594 1.00 69.94  ? 57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.079 146.820 102.724 1.00 70.05  ? 57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.844 145.744 103.548 1.00 66.45  ? 57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.880 150.695 100.824 1.00 63.51  ? 58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.084 150.153 101.444 1.00 59.58  ? 58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.789 151.180 102.323 1.00 60.28  ? 58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.272 150.836 103.408 1.00 60.12  ? 58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.025 149.617 100.365 1.00 56.97  ? 58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.506 148.349 99.682  1.00 56.82  ? 58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.299 148.027 98.431  1.00 60.15  ? 58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.528 147.176 100.644 1.00 59.63  ? 58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.863 152.440 101.887 1.00 65.42  ? 59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.480 153.463 102.727 1.00 65.61  ? 59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.598 153.787 103.928 1.00 69.37  ? 59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.089 153.924 105.054 1.00 68.17  ? 59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.805 154.725 101.907 1.00 61.68  ? 59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.649 155.674 102.731 1.00 64.31  ? 59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.561 154.352 100.651 1.00 63.97  ? 59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.287 153.923 103.710 1.00 72.71  ? 60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.387 154.300 104.797 1.00 71.85  ? 60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.324 153.225 105.873 1.00 71.74  ? 60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.299 153.538 107.069 1.00 72.42  ? 60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.993 154.590 104.241 1.00 73.40  ? 60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.857 155.965 103.605 1.00 73.82  ? 60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.573 156.117 102.814 1.00 77.52  ? 60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.756 155.172 102.818 1.00 75.44  ? 60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.384 157.178 102.184 1.00 74.47  ? 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.295 151.953 105.475 1.00 67.28  ? 61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.230 150.846 106.423 1.00 67.10  ? 61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.590 150.477 107.001 1.00 69.26  ? 61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.738 149.375 107.544 1.00 68.85  ? 61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.591 149.622 105.764 1.00 68.44  ? 61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.140 149.853 105.397 1.00 73.92  ? 61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.722 150.983 105.144 1.00 70.54  ? 61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.358 148.781 105.373 1.00 73.50  ? 61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.574 151.371 106.887 1.00 67.15  ? 62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.905 151.180 107.467 1.00 66.85  ? 62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.577 149.920 106.928 1.00 66.69  ? 62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.298 149.223 107.645 1.00 67.55  ? 62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.843 151.154 108.997 1.00 68.40  ? 62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 108.992 152.259 109.614 1.00 69.84  ? 62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.273 153.627 109.022 1.00 70.57  ? 62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.425 154.037 108.891 1.00 69.93  ? 62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 108.214 154.343 108.661 1.00 68.76  ? 62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.338 149.621 105.652 1.00 67.83  ? 63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.071 148.560 104.974 1.00 64.88  ? 63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.309 149.084 104.266 1.00 66.27  ? 63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.329 148.387 104.218 1.00 68.94  ? 63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.173 147.846 103.959 1.00 61.75  ? 63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.126 146.945 104.574 1.00 66.95  ? 63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.486 145.896 105.409 1.00 63.36  ? 63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.778 147.136 104.307 1.00 66.47  ? 63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.531 145.069 105.968 1.00 63.44  ? 63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.817 146.315 104.860 1.00 66.11  ? 63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.198 145.283 105.690 1.00 68.41  ? 63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.240 144.464 106.241 1.00 70.80  ? 63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.244 150.295 103.722 1.00 59.32  ? 64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.366 150.927 103.048 1.00 53.96  ? 64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.766 152.200 103.777 1.00 58.38  ? 64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 112.947 152.839 104.443 1.00 60.18  ? 64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.029 151.276 101.595 1.00 54.71  ? 64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.018 150.101 100.651 1.00 55.06  ? 64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.486 148.857 101.048 1.00 55.75  ? 64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.547 150.242 99.355  1.00 56.55  ? 64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.479 147.784 100.181 1.00 54.81  ? 64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.538 149.180 98.483  1.00 55.68  ? 64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.003 147.953 98.900  1.00 56.18  ? 64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 112.989 146.896 98.023  1.00 57.03  ? 64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.039 152.557 103.649 1.00 65.93  ? 65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.497 153.869 104.079 1.00 66.73  ? 65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.070 154.916 103.060 1.00 66.51  ? 65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.028 154.651 101.856 1.00 64.79  ? 65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.015 153.883 104.249 1.00 64.59  ? 65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.536 152.854 105.236 1.00 63.23  ? 65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.049 152.836 105.308 1.00 69.66  ? 65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.696 152.918 104.243 1.00 71.91  ? 65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.593 152.734 106.428 1.00 67.13  ? 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.744 156.109 103.550 1.00 69.54  ? 66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.310 157.197 102.687 1.00 70.69  ? 66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.485 158.010 102.154 1.00 71.36  ? 66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.391 158.567 101.055 1.00 71.35  ? 66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.337 158.108 103.462 1.00 70.89  ? 66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.845 159.444 102.829 1.00 72.52  ? 66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 112.732 159.485 101.299 1.00 76.33  ? 66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 112.655 158.430 100.634 1.00 73.46  ? 66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.712 160.608 100.752 1.00 75.88  ? 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.605 158.045 102.881 1.00 70.95  ? 67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.717 158.912 102.504 1.00 71.50  ? 67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.308 158.524 101.152 1.00 73.01  ? 67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.631 159.400 100.340 1.00 72.60  ? 67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.792 158.883 103.591 1.00 71.43  ? 67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 119.152 157.490 104.093 1.00 74.75  ? 67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 120.344 156.896 103.365 1.00 76.28  ? 67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 121.191 157.674 102.878 1.00 72.00  ? 67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 120.431 155.653 103.277 1.00 73.97  ? 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.460 157.225 100.885 1.00 65.57  ? 68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.095 156.815 99.638  1.00 63.02  ? 68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.158 156.950 98.444  1.00 66.29  ? 68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.622 157.212 97.329  1.00 68.48  ? 68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.621 155.380 99.752  1.00 64.99  ? 68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.630 154.323 99.356  1.00 63.63  ? 68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.633 153.921 100.227 1.00 62.08  ? 68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.713 153.711 98.116  1.00 61.70  ? 68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 116.728 152.941 99.862  1.00 61.38  ? 68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 117.813 152.733 97.746  1.00 62.94  ? 68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 116.821 152.345 98.621  1.00 62.55  ? 68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 116.850 156.778 98.646  1.00 66.22  ? 69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 115.897 156.985 97.563  1.00 65.11  ? 69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.627 158.457 97.293  1.00 66.42  ? 69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.187 158.799 96.189  1.00 66.49  ? 69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.577 156.274 97.870  1.00 64.57  ? 69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.546 154.765 97.621  1.00 64.20  ? 69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.263 154.153 98.155  1.00 61.55  ? 69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.716 154.457 96.143  1.00 62.20  ? 69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 115.878 159.333 98.269  1.00 68.32  ? 70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.659 160.760 98.069  1.00 68.97  ? 70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.691 161.378 97.134  1.00 69.44  ? 70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.454 162.468 96.605  1.00 68.63  ? 70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.675 161.488 99.413  1.00 68.47  ? 70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.814 161.123 100.174 1.00 68.83  ? 70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.826 160.709 96.923  1.00 62.51  ? 71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.846 161.217 96.015  1.00 61.51  ? 71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.445 161.096 94.552  1.00 63.84  ? 71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.125 161.670 93.695  1.00 64.57  ? 71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.167 160.484 96.251  1.00 62.15  ? 71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.509 160.153 97.704  1.00 66.89  ? 71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.640 159.141 97.771  1.00 63.36  ? 71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 120.870 161.415 98.470  1.00 64.54  ? 71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.371 160.372 94.248  1.00 59.40  ? 72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 116.901 160.181 92.884  1.00 59.47  ? 72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.478 160.695 92.749  1.00 59.98  ? 72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.661 160.536 93.660  1.00 63.12  ? 72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 116.929 158.702 92.477  1.00 60.16  ? 72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.215 157.973 92.779  1.00 55.39  ? 72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.423 157.377 94.016  1.00 56.43  ? 72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.210 157.856 91.820  1.00 54.30  ? 72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.591 156.706 94.293  1.00 55.37  ? 72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.381 157.182 92.088  1.00 57.19  ? 72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.566 156.610 93.326  1.00 55.91  ? 72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 121.730 155.939 93.605  1.00 56.83  ? 72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.185 161.312 91.609  1.00 65.85  ? 73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 113.801 161.555 91.244  1.00 67.16  ? 73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.125 160.229 90.908  1.00 69.51  ? 73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 113.780 159.230 90.603  1.00 69.02  ? 73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 113.714 162.514 90.057  1.00 65.32  ? 73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.109 161.876 88.855  1.00 68.74  ? 73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 111.792 160.221 90.979  1.00 69.15  ? 74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.069 158.978 90.729  1.00 68.43  ? 74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.266 158.493 89.299  1.00 70.99  ? 74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.203 157.287 89.034  1.00 75.00  ? 74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 109.580 159.140 91.026  1.00 68.78  ? 74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 108.786 157.898 90.755  1.00 71.46  ? 74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.037 156.738 91.469  1.00 67.44  ? 74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 107.815 157.876 89.769  1.00 72.35  ? 74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.324 155.585 91.218  1.00 70.91  ? 74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.096 156.724 89.514  1.00 70.73  ? 74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.353 155.577 90.238  1.00 71.83  ? 74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.495 159.413 88.360  1.00 75.02  ? 75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 111.773 159.004 86.987  1.00 76.15  ? 75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.048 158.176 86.915  1.00 77.43  ? 75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.102 157.157 86.215  1.00 78.61  ? 75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 111.876 160.234 86.081  1.00 76.17  ? 75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.667 161.213 86.020  1.00 77.98  ? 75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.252 160.624 86.198  1.00 82.17  ? 75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.040 159.392 86.207  1.00 78.77  ? 75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.318 161.441 86.340  1.00 80.90  ? 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.083 158.595 87.643  1.00 69.46  ? 76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.342 157.859 87.652  1.00 65.84  ? 76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.172 156.472 88.263  1.00 67.97  ? 76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 115.694 155.484 87.732  1.00 75.21  ? 76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.394 158.665 88.410  1.00 69.32  ? 76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.573 160.058 87.839  1.00 73.27  ? 76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.727 160.174 86.605  1.00 71.86  ? 76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 116.556 161.035 88.617  1.00 71.55  ? 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.433 156.379 89.371  1.00 57.07  ? 77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.199 155.085 90.008  1.00 59.61  ? 77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.401 154.171 89.087  1.00 62.08  ? 77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.690 152.974 88.970  1.00 60.45  ? 77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.495 155.279 91.362  1.00 61.31  ? 77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.323 156.190 92.268  1.00 61.86  ? 77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.260 153.941 92.033  1.00 60.49  ? 77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 113.572 156.683 93.483  1.00 62.42  ? 77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.375 154.717 88.431  1.00 68.30  ? 78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.579 153.918 87.507  1.00 65.07  ? 78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.418 153.433 86.333  1.00 68.29  ? 78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.284 152.284 85.901  1.00 72.63  ? 78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.377 154.727 87.020  1.00 68.08  ? 78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.414 153.952 86.140  1.00 70.61  ? 78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.236 154.822 85.743  1.00 70.68  ? 78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.437 154.199 84.615  1.00 72.74  ? 78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.573 155.207 83.942  1.00 70.87  ? 78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.295 154.292 85.805  1.00 67.80  ? 79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.177 153.868 84.722  1.00 68.18  ? 79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.132 152.775 85.185  1.00 66.03  ? 79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.412 151.829 84.441  1.00 69.83  ? 79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 114.954 155.064 84.174  1.00 67.31  ? 79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.135 155.969 83.270  1.00 70.11  ? 79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 113.504 155.217 82.115  1.00 74.60  ? 79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 114.241 154.534 81.373  1.00 74.15  ? 79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 112.270 155.310 81.947  1.00 70.66  ? 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.643 152.889 86.413  1.00 54.52  ? 80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.528 151.858 86.951  1.00 52.38  ? 80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 115.794 150.526 87.066  1.00 61.58  ? 80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.318 149.472 86.678  1.00 63.64  ? 80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.101 152.317 88.305  1.00 53.36  ? 80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.647 151.139 89.086  1.00 53.54  ? 80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.179 153.363 88.090  1.00 57.32  ? 80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.568 150.553 87.593  1.00 61.63  ? 81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 113.795 149.322 87.728  1.00 55.69  ? 81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.447 148.733 86.365  1.00 54.34  ? 81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.448 147.509 86.195  1.00 61.52  ? 81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.532 149.577 88.548  1.00 53.50  ? 81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.746 149.489 90.033  1.00 52.19  ? 81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.514 150.433 90.692  1.00 54.25  ? 81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.180 148.463 90.770  1.00 55.99  ? 81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.712 150.358 92.057  1.00 56.05  ? 81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.376 148.383 92.137  1.00 53.30  ? 81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.144 149.331 92.780  1.00 51.27  ? 81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.141 149.586 85.384  1.00 54.52  ? 82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 112.915 149.106 84.025  1.00 56.86  ? 82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.166 148.439 83.469  1.00 57.81  ? 82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.080 147.405 82.797  1.00 61.20  ? 82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.482 150.261 83.122  1.00 61.40  ? 82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.079 150.780 83.382  1.00 62.19  ? 82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.033 149.861 82.780  1.00 62.40  ? 82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.056 150.634 81.911  1.00 63.22  ? 82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.483 150.657 80.485  1.00 60.09  ? 82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.335 149.024 83.735  1.00 54.02  ? 83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.587 148.418 83.298  1.00 56.19  ? 83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 116.783 147.048 83.933  1.00 57.46  ? 83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.252 146.112 83.278  1.00 58.02  ? 83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 117.761 149.339 83.632  1.00 54.57  ? 83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.511 150.645 83.100  1.00 58.50  ? 83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.052 148.799 83.037  1.00 54.62  ? 83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.433 146.915 85.216  1.00 48.39  ? 84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.537 145.613 85.867  1.00 48.21  ? 84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 115.595 144.596 85.235  1.00 56.29  ? 84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 115.985 143.449 84.987  1.00 61.75  ? 84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.252 145.746 87.361  1.00 48.63  ? 84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.357 144.998 84.957  1.00 57.71  ? 85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.372 144.098 84.374  1.00 50.10  ? 85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.495 143.969 82.862  1.00 52.76  ? 85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 112.891 143.057 82.286  1.00 58.41  ? 85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 111.956 144.559 84.736  1.00 52.12  ? 85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.554 144.233 86.157  1.00 54.06  ? 85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.855 145.096 87.202  1.00 53.50  ? 85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 110.878 143.059 86.453  1.00 56.13  ? 85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.489 144.800 88.500  1.00 53.57  ? 85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.509 142.753 87.749  1.00 58.55  ? 85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 110.817 143.627 88.767  1.00 57.75  ? 85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.450 143.325 90.058  1.00 54.84  ? 85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.253 144.850 82.204  1.00 54.10  ? 86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.456 144.713 80.766  1.00 56.05  ? 86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.271 143.471 80.431  1.00 58.53  ? 86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.106 142.895 79.350  1.00 58.96  ? 86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.140 145.958 80.203  1.00 51.34  ? 86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.153 143.049 81.339  1.00 55.82  ? 87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 116.947 141.849 81.102  1.00 53.23  ? 87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.078 140.599 81.062  1.00 54.26  ? 87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 116.407 139.641 80.353  1.00 52.58  ? 87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.028 141.721 82.178  1.00 53.65  ? 87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 118.682 140.351 82.262  1.00 55.54  ? 87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.122 140.390 81.786  1.00 52.08  ? 87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 120.708 138.990 81.694  1.00 48.22  ? 87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 120.972 138.409 83.038  1.00 46.21  ? 87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 114.960 140.602 81.792  1.00 63.24  ? 88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.085 139.439 81.922  1.00 62.95  ? 88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 114.860 138.252 82.496  1.00 57.74  ? 88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 114.869 137.148 81.947  1.00 57.73  ? 88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 113.430 139.085 80.582  1.00 60.55  ? 88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 112.620 140.220 79.970  1.00 59.50  ? 88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 111.306 140.436 80.706  1.00 59.22  ? 88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 110.384 139.225 80.618  1.00 62.60  ? 88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 110.596 138.407 79.388  1.00 64.15  ? 88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 115.527 138.512 83.617  1.00 52.49  ? 89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.346 137.498 84.262  1.00 53.02  ? 89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 115.492 136.326 84.719  1.00 54.18  ? 89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 114.435 136.504 85.330  1.00 56.99  ? 89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.091 138.098 85.455  1.00 51.82  ? 89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 117.882 137.094 86.244  1.00 51.52  ? 89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.149 136.717 85.835  1.00 49.34  ? 89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.359 136.527 87.393  1.00 48.04  ? 89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 119.878 135.795 86.557  1.00 48.49  ? 89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.084 135.603 88.117  1.00 49.20  ? 89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.344 135.237 87.700  1.00 50.65  ? 89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 115.958 135.117 84.419  1.00 54.83  ? 90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.297 133.893 84.844  1.00 54.63  ? 90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.297 133.030 85.595  1.00 54.63  ? 90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 117.413 132.809 85.114  1.00 54.14  ? 90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 114.722 133.122 83.651  1.00 54.30  ? 90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 113.788 133.938 82.774  1.00 53.78  ? 90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 112.342 133.784 83.213  1.00 54.92  ? 90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 111.830 135.002 83.829  1.00 54.32  ? 90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.399 136.058 83.155  1.00 57.36  ? 90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 110.964 137.122 83.824  1.00 57.57  ? 90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.391 136.078 81.833  1.00 60.49  ? 90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 115.901 132.556 86.765  1.00 51.80  ? 91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 116.745 131.653 87.533  1.00 50.49  ? 91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 116.872 130.330 86.791  1.00 56.03  ? 91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 115.850 129.746 86.409  1.00 57.82  ? 91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.158 131.433 88.923  1.00 50.53  ? 91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.336 132.603 89.848  1.00 53.25  ? 91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 117.547 132.825 90.481  1.00 57.90  ? 91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.292 133.479 90.086  1.00 53.38  ? 91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 117.712 133.897 91.335  1.00 49.31  ? 91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.452 134.554 90.938  1.00 52.40  ? 91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 116.664 134.762 91.563  1.00 48.81  ? 91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.086 129.820 86.562  1.00 56.19  ? 92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.240 128.570 85.814  1.00 55.30  ? 92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.127 127.310 86.656  1.00 58.02  ? 92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.041 126.213 86.086  1.00 58.52  ? 92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 119.650 128.709 85.221  1.00 57.88  ? 92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.380 129.666 86.155  1.00 56.29  ? 92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.374 130.293 87.092  1.00 54.70  ? 92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.128 127.432 87.980  1.00 54.09  ? 93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 117.952 126.299 88.873  1.00 53.39  ? 93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 116.955 126.680 89.954  1.00 56.13  ? 93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.868 127.844 90.356  1.00 56.67  ? 93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.280 125.860 89.503  1.00 54.88  ? 93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.085 124.784 90.404  1.00 58.12  ? 93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.191 125.687 90.415  1.00 60.21  ? 94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.195 125.945 91.448  1.00 54.98  ? 94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 115.848 126.388 92.749  1.00 59.01  ? 94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.291 127.213 93.482  1.00 62.20  ? 94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.337 124.700 91.678  1.00 57.51  ? 94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 113.699 124.653 93.034  1.00 58.85  ? 94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 112.660 125.507 93.356  1.00 58.08  ? 94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.145 123.762 93.993  1.00 58.43  ? 94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.081 125.471 94.605  1.00 58.52  ? 94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 113.564 123.722 95.243  1.00 57.22  ? 94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 112.531 124.577 95.548  1.00 54.79  ? 94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.029 125.846 93.056  1.00 52.98  ? 95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 117.691 126.178 94.312  1.00 50.33  ? 95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.088 127.647 94.370  1.00 51.68  ? 95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.069 128.246 95.448  1.00 57.51  ? 95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 118.915 125.282 94.505  1.00 54.45  ? 95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 119.713 125.534 95.778  1.00 59.50  ? 95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.796 125.379 97.325  1.00 72.89  ? 95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.738 123.973 96.995  1.00 55.77  ? 95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.435 128.245 93.228  1.00 47.09  ? 96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 118.767 129.667 93.200  1.00 42.04  ? 96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.580 130.518 93.635  1.00 48.39  ? 96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 117.699 131.374 94.524  1.00 52.17  ? 96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.218 130.060 91.795  1.00 44.10  ? 96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.132 129.114 91.271  1.00 49.91  ? 96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.424 130.296 93.008  1.00 53.90  ? 97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.224 131.040 93.368  1.00 47.90  ? 97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 114.807 130.750 94.801  1.00 48.46  ? 97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.366 131.653 95.520  1.00 55.47  ? 97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.091 130.705 92.400  1.00 47.02  ? 97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 114.928 129.492 95.231  1.00 47.28  ? 98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.576 129.142 96.603  1.00 48.28  ? 98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.444 129.903 97.598  1.00 53.99  ? 98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 114.936 130.496 98.556  1.00 63.78  ? 98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.709 127.633 96.805  1.00 55.95  ? 98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.458 127.183 98.215  1.00 57.35  ? 98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.165 127.003 98.677  1.00 58.48  ? 98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.513 126.933 99.077  1.00 57.23  ? 98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 112.929 126.588 99.972  1.00 58.44  ? 98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.282 126.519 100.373 1.00 59.95  ? 98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 113.989 126.346 100.822 1.00 60.44  ? 98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 116.759 129.923 97.366  1.00 54.49  ? 99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.660 130.667 98.239  1.00 51.60  ? 99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.317 132.148 98.260  1.00 54.79  ? 99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.222 132.753 99.333  1.00 57.82  ? 99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.112 130.463 97.806  1.00 49.54  ? 99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.914 129.574 98.734  1.00 54.36  ? 99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.156 128.330 99.127  1.00 53.57  ? 99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 119.870 127.608 100.253 1.00 56.13  ? 99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 119.953 128.445 101.481 1.00 53.98  ? 99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.122 132.756 97.087  1.00 48.14  ? 100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 116.855 134.189 97.081  1.00 42.45  ? 100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 115.547 134.507 97.793  1.00 49.82  ? 100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 115.508 135.352 98.693  1.00 56.82  ? 100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 116.824 134.752 95.663  1.00 42.04  ? 100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.479 136.212 95.627  1.00 43.18  ? 100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.427 137.165 95.957  1.00 48.81  ? 100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.198 136.630 95.315  1.00 50.36  ? 100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.113 138.507 95.949  1.00 50.77  ? 100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 114.878 137.972 95.308  1.00 48.24  ? 100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 115.837 138.911 95.625  1.00 48.20  ? 100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 114.469 133.817 97.427  1.00 52.60  ? 101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.155 134.132 97.963  1.00 49.65  ? 101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 112.918 133.546 99.347  1.00 47.88  ? 101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 111.829 133.729 99.897  1.00 59.76  ? 101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.073 133.658 96.992  1.00 48.12  ? 101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.009 134.493 95.734  1.00 44.61  ? 101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.398 135.738 95.736  1.00 50.26  ? 101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.576 134.045 94.551  1.00 47.21  ? 101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.343 136.508 94.593  1.00 45.31  ? 101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.527 134.808 93.403  1.00 51.60  ? 101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 111.908 136.038 93.429  1.00 48.81  ? 101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 111.857 136.801 92.286  1.00 51.72  ? 101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 113.896 132.845 99.918  1.00 50.37  ? 102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 113.825 132.449 101.316 1.00 55.39  ? 102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 114.758 133.236 102.223 1.00 59.23  ? 102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 114.453 133.390 103.407 1.00 59.21  ? 102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.136 130.955 101.463 1.00 57.17  ? 102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 112.916 130.084 101.250 1.00 60.76  ? 102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.125 130.316 100.335 1.00 59.99  ? 102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 112.752 129.077 102.100 1.00 57.12  ? 102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 115.882 133.738 101.710 1.00 62.73  ? 103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 116.864 134.440 102.526 1.00 60.40  ? 103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 116.962 135.924 102.209 1.00 56.92  ? 103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 116.931 136.753 103.123 1.00 62.08  ? 103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.248 133.792 102.356 1.00 63.54  ? 103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.256 132.316 102.706 1.00 67.10  ? 103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.181 131.760 103.009 1.00 62.03  ? 103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 119.346 131.707 102.675 1.00 68.03  ? 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.077 136.289 100.930 1.00 47.63  ? 104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.430 137.650 100.552 1.00 52.91  ? 104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.266 138.478 100.034 1.00 51.23  ? 104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.372 139.708 100.012 1.00 56.16  ? 104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.539 137.631 99.490  1.00 53.43  ? 104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 119.719 136.774 99.883  1.00 54.83  ? 104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 120.712 137.266 100.718 1.00 52.18  ? 104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 119.835 135.468 99.425  1.00 51.37  ? 104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 121.787 136.484 101.084 1.00 52.80  ? 104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 120.908 134.679 99.787  1.00 51.47  ? 104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 121.881 135.191 100.617 1.00 55.27  ? 104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 122.953 134.411 100.979 1.00 57.83  ? 104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.171 137.851 99.617  1.00 56.96  ? 105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.009 138.609 99.173  1.00 54.57  ? 105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.307 139.236 100.370 1.00 59.98  ? 105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.105 138.581 101.397 1.00 62.01  ? 105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.044 137.711 98.404  1.00 48.27  ? 105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 112.942 140.508 100.239 1.00 57.99  ? 106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.243 141.195 101.315 1.00 54.86  ? 106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 110.828 140.652 101.451 1.00 54.18  ? 106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.105 140.513 100.460 1.00 53.89  ? 106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.212 142.700 101.057 1.00 56.44  ? 106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.523 143.565 102.114 1.00 55.52  ? 106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.294 143.528 103.422 1.00 56.47  ? 106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.374 144.992 101.618 1.00 55.26  ? 106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.436 140.343 102.682 1.00 63.76  ? 107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.112 139.827 102.984 1.00 63.89  ? 107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.388 140.781 103.924 1.00 65.62  ? 107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.000 141.634 104.572 1.00 64.53  ? 107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.184 138.431 103.614 1.00 60.02  ? 107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.589 137.332 102.650 1.00 60.07  ? 107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 109.927 136.056 103.396 1.00 65.84  ? 107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.438 134.984 102.452 1.00 61.86  ? 107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.137 133.891 103.182 1.00 62.14  ? 107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.069 140.628 103.985 1.00 71.88  ? 108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.265 141.429 104.890 1.00 73.53  ? 108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.593 141.084 106.341 1.00 74.55  ? 108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.222 140.065 106.640 1.00 76.81  ? 108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 104.776 141.213 104.620 1.00 75.30  ? 108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.492 139.809 104.589 1.00 74.91  ? 108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.382 141.832 103.287 1.00 71.12  ? 108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.162 141.962 107.251 1.00 75.29  ? 109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.481 141.794 108.666 1.00 75.81  ? 109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 105.943 140.488 109.237 1.00 77.24  ? 109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 106.483 139.994 110.233 1.00 74.92  ? 109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 105.939 142.977 109.470 1.00 73.95  ? 109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.759 144.236 109.276 1.00 75.42  ? 109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 107.959 144.173 109.012 1.00 75.86  ? 109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.114 145.390 109.403 1.00 74.94  ? 109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 104.900 139.918 108.638 1.00 79.56  ? 110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 104.379 138.623 109.050 1.00 80.92  ? 110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 104.961 137.470 108.243 1.00 80.94  ? 110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 104.564 136.320 108.458 1.00 80.15  ? 110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 102.851 138.610 108.945 1.00 81.51  ? 110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.350 139.205 107.647 1.00 83.04  ? 110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.082 140.016 107.045 1.00 81.63  ? 110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.224 138.864 107.227 1.00 81.73  ? 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 105.879 137.750 107.317 1.00 74.90  ? 111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 106.579 136.761 106.501 1.00 76.64  ? 111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 105.643 135.933 105.629 1.00 75.93  ? 111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.073 134.929 105.049 1.00 73.11  ? 111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 107.440 135.828 107.365 1.00 75.20  ? 111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 108.934 135.982 107.145 1.00 74.94  ? 111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.536 136.974 108.126 1.00 76.08  ? 111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 111.055 136.938 108.089 1.00 76.57  ? 111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 111.658 137.849 109.100 1.00 75.14  ? 111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 104.372 136.323 105.518 1.00 80.28  ? 112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 103.431 135.547 104.717 1.00 82.11  ? 112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 103.637 135.786 103.227 1.00 79.99  ? 112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 103.486 134.863 102.418 1.00 79.24  ? 112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 101.997 135.883 105.123 1.00 79.85  ? 112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 101.630 135.438 106.530 1.00 80.96  ? 112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 100.188 135.790 106.860 1.00 82.65  ? 112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 99.821  135.353 108.267 1.00 80.89  ? 112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 98.427  135.740 108.620 1.00 78.71  ? 112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 103.980 137.012 102.846 1.00 72.00  ? 113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.102 137.398 101.449 1.00 68.47  ? 113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.531 137.840 101.155 1.00 66.19  ? 113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.373 137.952 102.050 1.00 69.19  ? 113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.115 138.521 101.106 1.00 67.49  ? 113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.010 138.113 100.143 1.00 64.80  ? 113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.283 136.872 100.636 1.00 66.61  ? 113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.309 136.349 99.594  1.00 69.46  ? 113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 99.384  135.329 100.160 1.00 67.71  ? 113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 105.799 138.090 99.875  1.00 58.80  ? 114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.114 138.505 99.397  1.00 61.39  ? 114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 106.992 139.904 98.812  1.00 57.80  ? 114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.117 140.159 97.976  1.00 57.68  ? 114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.673 137.519 98.357  1.00 60.33  ? 114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.028 136.188 99.018  1.00 60.35  ? 114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 108.892 138.103 97.666  1.00 55.94  ? 114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.175 135.050 98.042  1.00 56.70  ? 114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 107.861 140.810 99.253  1.00 54.69  ? 115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 107.833 142.189 98.784  1.00 54.43  ? 115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 108.830 142.474 97.671  1.00 55.91  ? 115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.583 143.364 96.852  1.00 54.84  ? 115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.100 143.150 99.947  1.00 56.27  ? 115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.020 143.219 101.026 1.00 53.72  ? 115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.557 143.890 102.277 1.00 55.33  ? 115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 105.795 143.952 100.505 1.00 54.10  ? 115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 109.941 141.746 97.614  1.00 60.63  ? 116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.013 142.021 96.668  1.00 56.57  ? 116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.209 140.848 95.719  1.00 56.52  ? 116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.310 139.698 96.156  1.00 61.89  ? 116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.326 142.307 97.398  1.00 54.02  ? 116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.660 143.775 97.532  1.00 57.46  ? 116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 113.921 144.003 98.335  1.00 60.30  ? 116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.498 143.012 98.829  1.00 57.63  ? 116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.339 145.170 98.470  1.00 62.88  ? 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.267 141.148 94.424  1.00 49.00  ? 117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 111.756 140.197 93.441  1.00 49.83  ? 117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.280 140.282 93.376  1.00 51.44  ? 117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 113.916 141.049 94.104  1.00 59.75  ? 117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.129 140.472 92.076  1.00 51.94  ? 117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.668 140.076 91.962  1.00 56.69  ? 117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.295 139.799 90.513  1.00 61.79  ? 117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 108.024 139.093 90.389  1.00 62.59  ? 117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 107.847 137.810 90.669  1.00 58.89  ? 117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 106.637 137.276 90.525  1.00 55.34  ? 117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.845 137.047 91.082  1.00 58.32  ? 117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 113.884 139.482 92.498  1.00 46.11  ? 118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.321 139.599 92.280  1.00 43.33  ? 118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 115.657 140.926 91.612  1.00 46.78  ? 118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 116.593 141.625 92.021  1.00 52.79  ? 118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 115.827 138.423 91.446  1.00 46.15  ? 118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.328 138.258 91.473  1.00 44.20  ? 118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.012 138.171 92.675  1.00 40.47  ? 118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.060 138.184 90.298  1.00 44.87  ? 118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.382 138.019 92.707  1.00 41.65  ? 118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.430 138.028 90.319  1.00 42.77  ? 118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.086 137.947 91.527  1.00 45.32  ? 118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.453 137.795 91.556  1.00 47.93  ? 118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 114.888 141.295 90.589  1.00 50.73  ? 119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.056 142.565 89.899  1.00 45.34  ? 119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 114.742 143.762 90.784  1.00 46.09  ? 119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.128 144.881 90.435  1.00 54.22  ? 119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.173 142.592 88.652  1.00 49.76  ? 119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 114.767 141.865 87.459  1.00 50.52  ? 119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.010 140.598 87.110  1.00 56.29  ? 119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 113.740 139.794 88.026  1.00 54.07  ? 119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 113.690 140.406 85.918  1.00 58.32  ? 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.055 143.560 91.905  1.00 50.00  ? 120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.777 144.616 92.871  1.00 49.25  ? 120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 114.888 144.791 93.890  1.00 46.51  ? 120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.317 145.918 94.145  1.00 54.51  ? 120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.464 144.330 93.604  1.00 48.84  ? 120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.250 144.616 92.752  1.00 56.66  ? 120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.355 145.452 91.832  1.00 58.94  ? 120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.191 144.002 92.997  1.00 60.37  ? 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.365 143.690 94.474  1.00 40.92  ? 121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.523 143.759 95.356  1.00 37.23  ? 121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.748 144.282 94.622  1.00 42.90  ? 121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.485 145.113 95.163  1.00 52.27  ? 121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 116.805 142.381 95.954  1.00 36.97  ? 121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.039 142.309 96.835  1.00 38.74  ? 121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.691 142.501 98.299  1.00 37.84  ? 121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.475 143.569 98.907  1.00 41.77  ? 121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.003 144.770 99.210  1.00 42.18  ? 121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 118.815 145.663 99.767  1.00 43.60  ? 121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 116.746 145.099 98.972  1.00 44.13  ? 121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 117.973 143.824 93.389  1.00 43.63  ? 122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.111 144.308 92.616  1.00 39.47  ? 122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 118.970 145.795 92.317  1.00 41.68  ? 122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 119.943 146.550 92.416  1.00 51.28  ? 122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.270 143.473 91.333  1.00 40.29  ? 122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.120 142.237 91.621  1.00 37.20  ? 122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 119.888 144.298 90.215  1.00 38.53  ? 122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.338 141.365 90.421  1.00 44.82  ? 122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 117.764 146.241 91.957  1.00 41.17  ? 123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.554 147.661 91.689  1.00 35.13  ? 123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 117.800 148.501 92.934  1.00 39.44  ? 123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.413 149.571 92.857  1.00 50.84  ? 123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.139 147.900 91.167  1.00 40.35  ? 123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 115.786 146.940 90.193  1.00 44.95  ? 123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.325 148.037 94.090  1.00 42.38  ? 124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.514 148.795 95.324  1.00 40.38  ? 124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 118.991 148.853 95.696  1.00 40.52  ? 124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.502 149.904 96.103  1.00 51.27  ? 124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.658 148.194 96.451  1.00 46.43  ? 124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.188 148.548 96.229  1.00 43.54  ? 124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.123 148.690 97.808  1.00 43.69  ? 124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 114.942 150.028 96.035  1.00 43.41  ? 124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.703 147.733 95.552  1.00 39.41  ? 125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.134 147.718 95.848  1.00 37.08  ? 125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 121.885 148.652 94.906  1.00 38.85  ? 125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 122.793 149.380 95.325  1.00 53.36  ? 125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.675 146.277 95.781  1.00 38.78  ? 125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.181 146.272 95.883  1.00 42.18  ? 125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.077 145.437 96.893  1.00 40.75  ? 125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.519 148.650 93.622  1.00 31.16  ? 126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.163 149.540 92.661  1.00 31.57  ? 126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 121.893 151.003 92.983  1.00 38.46  ? 126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 122.797 151.843 92.890  1.00 48.53  ? 126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.686 149.211 91.250  1.00 39.02  ? 126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.652 151.330 93.348  1.00 42.77  ? 127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.321 152.703 93.709  1.00 39.35  ? 127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.080 153.135 94.954  1.00 42.08  ? 127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.494 154.294 95.068  1.00 52.63  ? 127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 118.815 152.842 93.921  1.00 38.11  ? 127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 117.948 152.767 92.665  1.00 43.92  ? 127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.489 152.603 93.045  1.00 48.60  ? 127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.144 153.999 91.801  1.00 43.29  ? 127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.265 152.218 95.905  1.00 36.55  ? 128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.089 152.529 97.066  1.00 37.87  ? 128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.533 152.790 96.652  1.00 42.87  ? 128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.151 153.764 97.094  1.00 46.01  ? 128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.013 151.390 98.084  1.00 35.50  ? 128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.007 151.514 99.201  1.00 46.67  ? 128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.736 152.318 100.295 1.00 49.88  ? 128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.208 150.828 99.161  1.00 41.51  ? 128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.647 152.438 101.324 1.00 50.12  ? 128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.122 150.946 100.186 1.00 39.63  ? 128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.841 151.752 101.270 1.00 46.89  ? 128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.077 151.934 95.783  1.00 41.64  ? 129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.477 152.059 95.382  1.00 33.06  ? 129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.739 153.365 94.646  1.00 38.74  ? 129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.760 154.023 94.878  1.00 46.72  ? 129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 125.884 150.880 94.500  1.00 32.71  ? 129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.121 149.606 95.249  1.00 35.58  ? 129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.304 149.611 96.619  1.00 37.84  ? 129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.184 148.399 94.575  1.00 35.24  ? 129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.527 148.436 97.304  1.00 41.79  ? 129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.414 147.223 95.253  1.00 37.80  ? 129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.582 147.241 96.620  1.00 42.35  ? 129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 124.836 153.754 93.743  1.00 46.37  ? 130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.115 154.886 92.867  1.00 46.90  ? 130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.150 156.209 93.622  1.00 56.10  ? 130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 125.926 157.102 93.260  1.00 59.83  ? 130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.084 154.947 91.747  1.00 46.79  ? 130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.320 156.358 94.654  1.00 56.27  ? 131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.275 157.567 95.479  1.00 53.83  ? 131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 123.938 158.801 94.638  1.00 54.23  ? 131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.716 159.750 94.530  1.00 58.92  ? 131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 125.592 157.759 96.241  1.00 52.04  ? 131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.376 158.100 97.701  1.00 58.61  ? 131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.553 157.488 98.379  1.00 57.28  ? 131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.120 159.085 98.193  1.00 56.71  ? 131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 122.750 158.769 94.037  1.00 53.63  ? 132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.219 159.896 93.301  1.00 58.34  ? 132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.506 159.899 91.814  1.00 58.50  ? 132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 121.955 160.746 91.100  1.00 59.18  ? 132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.342 158.988 91.325  1.00 58.61  ? 133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 123.700 158.944 89.913  1.00 61.08  ? 133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 122.799 157.946 89.191  1.00 63.70  ? 133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 122.777 156.761 89.537  1.00 62.89  ? 133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.171 158.566 89.745  1.00 61.07  ? 133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 125.735 158.987 88.402  1.00 64.72  ? 133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 124.941 159.252 87.474  1.00 64.85  ? 133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 126.975 159.051 88.273  1.00 60.49  ? 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.058 158.426 88.191  1.00 61.47  ? 134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.165 157.541 87.449  1.00 58.57  ? 134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 121.941 156.613 86.521  1.00 63.71  ? 134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 121.648 155.414 86.450  1.00 67.85  ? 134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.151 158.361 86.653  1.00 64.23  ? 134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.605 159.390 87.487  1.00 64.29  ? 134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.026 157.469 86.150  1.00 64.82  ? 134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 122.928 157.149 85.799  1.00 63.86  ? 135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 123.716 156.318 84.893  1.00 62.88  ? 135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.518 155.275 85.660  1.00 61.66  ? 135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 124.614 154.118 85.233  1.00 66.42  ? 135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 124.639 157.193 84.046  1.00 62.04  ? 135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 123.950 157.885 82.880  1.00 62.70  ? 135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 122.680 157.180 82.443  1.00 70.95  ? 135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 122.780 156.153 81.739  1.00 70.28  ? 135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.581 157.653 82.800  1.00 70.18  ? 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.099 155.664 86.795  1.00 50.56  ? 136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 125.823 154.703 87.619  1.00 51.73  ? 136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 124.883 153.642 88.177  1.00 54.87  ? 136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.251 152.466 88.280  1.00 56.03  ? 136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.554 155.427 88.749  1.00 57.03  ? 136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 127.524 154.559 89.527  1.00 54.87  ? 136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 128.831 154.375 88.775  1.00 54.33  ? 136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 129.904 153.791 89.679  1.00 55.87  ? 136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.258 153.884 89.066  1.00 56.17  ? 136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 123.661 154.039 88.544  1.00 57.39  ? 137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.684 153.070 89.029  1.00 51.84  ? 137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.306 152.076 87.940  1.00 48.70  ? 137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.179 150.876 88.203  1.00 50.64  ? 137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.444 153.789 89.554  1.00 48.76  ? 137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.122 152.556 86.709  1.00 49.38  ? 138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 121.821 151.649 85.606  1.00 51.94  ? 138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.002 150.733 85.307  1.00 54.32  ? 138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 122.812 149.558 84.971  1.00 55.04  ? 138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.425 152.443 84.362  1.00 54.53  ? 138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.121 153.208 84.511  1.00 54.40  ? 138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 119.477 153.466 83.162  1.00 52.91  ? 138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.387 154.954 82.868  1.00 58.21  ? 138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 118.181 155.285 82.060  1.00 55.62  ? 138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.226 151.252 85.420  1.00 54.42  ? 139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.404 150.409 85.236  1.00 48.76  ? 139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.469 149.317 86.296  1.00 47.64  ? 139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 125.787 148.164 85.991  1.00 63.05  ? 139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.670 151.262 85.265  1.00 51.62  ? 139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.018 151.902 83.933  1.00 52.37  ? 139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.037 153.014 84.070  1.00 60.11  ? 139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 129.052 152.809 84.768  1.00 57.05  ? 139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 127.823 154.095 83.482  1.00 58.39  ? 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.169 149.663 87.549  1.00 36.63  ? 140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.144 148.664 88.613  1.00 37.46  ? 140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.038 147.640 88.386  1.00 41.51  ? 140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.217 146.448 88.664  1.00 40.71  ? 140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 124.964 149.347 89.966  1.00 44.82  ? 140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.241 149.875 90.565  1.00 42.42  ? 140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.335 149.046 90.758  1.00 42.52  ? 140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.351 151.205 90.941  1.00 39.98  ? 140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.502 149.527 91.305  1.00 42.23  ? 140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.513 151.693 91.489  1.00 44.68  ? 140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.584 150.852 91.671  1.00 44.87  ? 140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.743 151.343 92.218  1.00 46.73  ? 140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 122.880 148.095 87.903  1.00 49.54  ? 141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 121.786 147.184 87.582  1.00 44.51  ? 141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.203 146.205 86.495  1.00 44.79  ? 141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 121.936 145.004 86.587  1.00 56.08  ? 141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.533 147.980 87.175  1.00 43.77  ? 141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 119.652 147.150 86.276  1.00 45.05  ? 141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 119.759 148.389 88.404  1.00 46.75  ? 141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 122.857 146.703 85.445  1.00 42.78  ? 142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.349 145.816 84.397  1.00 44.29  ? 142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.396 144.855 84.942  1.00 47.12  ? 142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.439 143.683 84.554  1.00 56.27  ? 142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 123.919 146.634 83.240  1.00 47.80  ? 142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 122.839 147.238 82.368  1.00 52.30  ? 142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 121.890 146.560 81.977  1.00 47.77  ? 142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 122.978 148.521 82.056  1.00 46.47  ? 142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.251 145.338 85.844  1.00 42.95  ? 143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.296 144.499 86.417  1.00 39.84  ? 143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 125.712 143.360 87.243  1.00 42.41  ? 143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.196 142.225 87.176  1.00 51.18  ? 143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.225 145.359 87.272  1.00 44.36  ? 143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.525 144.726 87.756  1.00 42.38  ? 143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.506 144.642 86.610  1.00 46.65  ? 143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.099 145.541 88.898  1.00 41.85  ? 143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 124.675 143.642 88.029  1.00 40.58  ? 144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.122 142.636 88.929  1.00 33.99  ? 144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.076 141.743 88.274  1.00 38.82  ? 144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 122.972 140.565 88.634  1.00 44.98  ? 144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.519 143.306 90.167  1.00 39.89  ? 144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.552 143.739 91.193  1.00 37.04  ? 144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 123.817 144.428 92.685  1.00 52.15  ? 144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.294 146.030 92.089  1.00 42.51  ? 144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.296 142.265 87.327  1.00 37.76  ? 145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.295 141.436 86.665  1.00 35.53  ? 145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 121.943 140.531 85.625  1.00 42.76  ? 145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.407 139.463 85.308  1.00 51.15  ? 145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.184 142.309 86.054  1.00 38.26  ? 145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 118.867 141.534 86.010  1.00 42.13  ? 145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 120.566 142.794 84.663  1.00 40.14  ? 145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.343 141.146 87.371  1.00 40.25  ? 145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.094 140.930 85.080  1.00 40.71  ? 146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 123.924 140.000 84.328  1.00 37.61  ? 146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 124.638 139.019 85.242  1.00 39.79  ? 146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.269 138.080 84.747  1.00 46.04  ? 146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 124.951 140.758 83.486  1.00 35.83  ? 146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.313 141.567 82.378  1.00 39.77  ? 146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.196 141.282 81.950  1.00 43.56  ? 146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.020 142.587 81.909  1.00 44.28  ? 146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 124.555 139.231 86.557  1.00 40.38  ? 147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.201 138.388 87.557  1.00 36.46  ? 147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 126.711 138.348 87.363  1.00 42.92  ? 147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.354 137.334 87.636  1.00 52.40  ? 147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 124.615 136.974 87.554  1.00 38.61  ? 147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.194 136.904 88.082  1.00 36.90  ? 147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 122.835 135.535 88.610  1.00 43.29  ? 147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.103 135.409 89.591  1.00 42.88  ? 147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.347 134.497 87.961  1.00 47.46  ? 147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.285 139.450 86.878  1.00 42.09  ? 148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 128.736 139.553 86.782  1.00 42.04  ? 148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.366 139.778 88.150  1.00 39.20  ? 148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.409 139.196 88.462  1.00 44.02  ? 148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.120 140.685 85.831  1.00 36.24  ? 148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 128.719 140.451 84.388  1.00 43.53  ? 148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 128.869 141.695 83.536  1.00 47.67  ? 148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 127.929 142.515 83.509  1.00 52.30  ? 148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 129.928 141.854 82.896  1.00 50.22  ? 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 128.741 140.612 88.975  1.00 31.08  ? 149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.238 140.940 90.302  1.00 32.13  ? 149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.139 140.705 91.324  1.00 35.75  ? 149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 126.973 141.027 91.081  1.00 47.24  ? 149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 129.720 142.390 90.367  1.00 37.22  ? 149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 129.917 142.920 91.767  1.00 32.41  ? 149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 130.939 142.444 92.574  1.00 31.47  ? 149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.082 143.903 92.280  1.00 29.17  ? 149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.123 142.929 93.851  1.00 35.46  ? 149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.258 144.393 93.557  1.00 38.27  ? 149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.280 143.903 94.338  1.00 40.87  ? 149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.457 144.389 95.613  1.00 36.60  ? 149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.517 140.140 92.462  1.00 27.97  ? 150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 127.573 139.848 93.539  1.00 21.36  ? 150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.019 140.530 94.822  1.00 28.52  ? 150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.049 140.136 95.402  1.00 38.66  ? 150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.453 138.342 93.754  1.00 32.95  ? 150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 126.552 137.945 94.909  1.00 34.08  ? 150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.167 138.556 94.813  1.00 34.67  ? 150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.396 138.237 93.908  1.00 28.52  ? 150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 124.844 139.434 95.752  1.00 34.58  ? 150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.305 141.549 95.298  1.00 30.88  ? 151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.615 142.105 96.618  1.00 26.83  ? 151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.457 141.045 97.696  1.00 28.69  ? 151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 126.648 140.123 97.575  1.00 36.64  ? 151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.587 143.230 96.782  1.00 32.10  ? 151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.169 143.572 95.396  1.00 33.54  ? 151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.235 142.295 94.618  1.00 33.58  ? 151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.257 141.178 98.750  1.00 29.24  ? 152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.249 140.198 99.826  1.00 20.67  ? 152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 126.858 140.080 100.443 1.00 33.93  ? 152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 125.987 140.932 100.251 1.00 37.50  ? 152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.266 140.577 100.901 1.00 28.63  ? 152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 128.870 141.753 101.585 1.00 38.91  ? 152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.655 138.993 101.186 1.00 43.31  ? 153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.365 138.748 101.827 1.00 39.14  ? 153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 124.900 139.907 102.700 1.00 41.71  ? 153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 123.736 140.316 102.564 1.00 39.74  ? 153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.430 137.435 102.622 1.00 43.31  ? 153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.450 136.326 101.717 1.00 43.39  ? 153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.233 137.308 103.551 1.00 39.39  ? 153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 125.722 140.488 103.587 1.00 37.15  ? 154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.251 141.682 104.310 1.00 29.79  ? 154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 124.908 142.839 103.391 1.00 29.24  ? 154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 123.868 143.485 103.572 1.00 37.23  ? 154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.433 142.017 105.230 1.00 30.82  ? 154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.153 140.735 105.397 1.00 32.91  ? 154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.053 140.068 104.064 1.00 33.07  ? 154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.748 143.105 102.390 1.00 25.25  ? 155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.509 144.237 101.500 1.00 22.98  ? 155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.290 143.998 100.619 1.00 31.88  ? 155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.436 144.878 100.477 1.00 46.21  ? 155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.744 144.503 100.642 1.00 35.04  ? 155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 127.904 144.588 101.479 1.00 34.88  ? 155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.583 145.800 99.873  1.00 29.35  ? 155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.195 142.813 100.014 1.00 37.16  ? 156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.049 142.512 99.162  1.00 34.28  ? 156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 121.755 142.502 99.967  1.00 38.87  ? 156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.720 142.992 99.501  1.00 43.70  ? 156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.258 141.172 98.458  1.00 36.19  ? 156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.394 140.980 97.245  1.00 37.21  ? 156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.380 141.927 96.234  1.00 40.07  ? 156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 121.603 139.854 97.112  1.00 35.87  ? 156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.589 141.755 95.116  1.00 38.64  ? 156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 120.811 139.675 95.996  1.00 38.12  ? 156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 120.804 140.627 94.997  1.00 42.91  ? 156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 121.797 141.949 101.180 1.00 43.37  ? 157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.597 141.842 102.002 1.00 36.20  ? 157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.132 143.205 102.503 1.00 40.04  ? 157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 118.948 143.542 102.397 1.00 47.20  ? 157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 120.865 140.904 103.179 1.00 42.35  ? 157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 119.672 140.445 104.016 1.00 44.29  ? 157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.986 139.268 103.362 1.00 41.86  ? 157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.118 140.089 105.424 1.00 44.92  ? 157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.047 144.003 103.049 1.00 38.49  ? 158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.675 145.165 103.846 1.00 37.06  ? 158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.814 146.494 103.115 1.00 38.82  ? 158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.590 147.540 103.730 1.00 49.13  ? 158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.511 145.200 105.128 1.00 40.27  ? 158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.431 143.907 105.910 1.00 42.62  ? 158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.356 143.328 106.064 1.00 46.42  ? 158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.571 143.443 106.405 1.00 44.63  ? 158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.174 146.493 101.834 1.00 34.04  ? 159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.341 147.750 101.113 1.00 33.19  ? 159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 119.988 148.416 100.905 1.00 42.88  ? 159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.101 147.850 100.259 1.00 50.84  ? 159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.029 147.515 99.773  1.00 39.48  ? 159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.830 149.619 101.450 1.00 57.76  ? 160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.607 150.372 101.272 1.00 57.58  ? 160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.430 149.904 102.095 1.00 52.96  ? 160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.294 150.277 101.784 1.00 55.86  ? 160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.659 149.101 103.131 1.00 50.51  ? 161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.600 148.609 103.999 1.00 55.44  ? 161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.763 149.211 105.386 1.00 58.77  ? 161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.885 149.364 105.876 1.00 59.41  ? 161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.616 147.080 104.082 1.00 50.22  ? 161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 115.611 146.399 103.169 1.00 54.61  ? 161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.206 145.171 102.507 1.00 54.87  ? 161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.131 143.997 103.368 1.00 55.19  ? 161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.028 142.750 102.930 1.00 57.30  ? 161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 115.967 141.755 103.810 1.00 54.50  ? 161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 115.986 142.473 101.637 1.00 57.17  ? 161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.639 149.563 106.014 1.00 65.77  ? 162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.690 150.141 107.353 1.00 68.05  ? 162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 115.905 149.070 108.415 1.00 68.39  ? 162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 116.729 149.239 109.321 1.00 63.41  ? 162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.412 150.931 107.639 1.00 67.36  ? 162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.608 152.075 108.619 1.00 65.11  ? 162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.476 153.080 108.535 1.00 66.62  ? 162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.693 154.067 107.400 1.00 67.10  ? 162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 112.412 154.459 106.754 1.00 67.07  ? 162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.171 147.960 108.324 1.00 69.23  ? 163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.340 146.839 109.249 1.00 69.64  ? 163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.541 146.012 108.789 1.00 73.04  ? 163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.442 145.085 107.983 1.00 71.12  ? 163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.065 146.010 109.325 1.00 71.46  ? 163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 114.200 144.710 110.102 1.00 71.69  ? 163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 113.497 144.797 111.445 1.00 72.16  ? 163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 112.057 144.969 111.295 1.00 71.90  ? 163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 111.187 143.971 111.220 1.00 70.44  ? 163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 109.893 144.246 111.088 1.00 69.91  ? 163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 111.578 142.708 111.271 1.00 68.37  ? 163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.707 146.387 109.312 1.00 60.54  ? 164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 118.957 145.814 108.831 1.00 59.45  ? 164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 119.977 145.657 109.948 1.00 62.51  ? 164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 119.664 145.842 111.128 1.00 59.85  ? 164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.552 146.695 107.734 1.00 57.71  ? 164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 119.646 148.157 108.137 1.00 56.40  ? 164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 120.914 148.811 107.618 1.00 56.97  ? 164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 120.862 149.068 106.184 1.00 55.69  ? 164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 121.721 149.840 105.533 1.00 59.33  ? 164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 121.579 150.006 104.221 1.00 56.20  ? 164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 122.715 150.448 106.158 1.00 57.50  ? 164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.204 145.316 109.568 1.00 57.81  ? 165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.343 145.358 110.458 1.00 53.45  ? 165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.406 146.267 109.879 1.00 54.62  ? 165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.175 147.466 109.701 1.00 55.63  ? 165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.573 145.709 109.580 1.00 56.59  ? 166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.622 146.416 108.866 1.00 55.14  ? 166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 125.926 145.707 107.552 1.00 53.08  ? 166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.787 144.486 107.438 1.00 49.55  ? 166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 126.895 146.523 109.710 1.00 52.01  ? 166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.543 147.901 109.686 1.00 54.69  ? 166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.632 148.991 110.217 1.00 56.79  ? 166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 125.868 148.722 111.167 1.00 56.78  ? 166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.679 150.119 109.683 1.00 58.58  ? 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.342 146.490 106.557 1.00 36.62  ? 167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.794 145.929 105.292 1.00 32.98  ? 167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.182 145.316 105.392 1.00 40.57  ? 167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.635 144.682 104.434 1.00 40.53  ? 167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 126.792 147.004 104.205 1.00 33.84  ? 167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.519 147.834 104.056 1.00 33.48  ? 167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.678 148.827 102.929 1.00 34.30  ? 167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.326 146.939 103.806 1.00 34.38  ? 167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 128.859 145.496 106.517 1.00 40.79  ? 168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.198 144.961 106.716 1.00 30.27  ? 168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.103 143.507 107.155 1.00 41.90  ? 168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.342 143.162 108.066 1.00 44.04  ? 168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 130.961 145.815 107.741 1.00 38.54  ? 168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.324 145.236 107.995 1.00 45.29  ? 168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.079 147.242 107.243 1.00 45.95  ? 168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.879 142.646 106.498 1.00 46.49  ? 169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.836 141.211 106.749 1.00 52.33  ? 169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.726 140.782 107.910 1.00 52.73  ? 169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.394 139.828 108.621 1.00 51.45  ? 169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 131.241 140.447 105.486 1.00 44.38  ? 169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 130.373 140.745 104.407 1.00 48.27  ? 169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.849 141.465 108.123 1.00 42.47  ? 170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 133.854 140.999 109.065 1.00 39.49  ? 170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.176 142.113 110.039 1.00 43.84  ? 170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 133.971 143.292 109.745 1.00 49.87  ? 170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.166 140.614 108.384 1.00 45.38  ? 170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.068 139.408 107.093 1.00 60.31  ? 170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 134.720 141.728 111.185 1.00 33.56  ? 171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.310 142.672 112.118 1.00 23.03  ? 171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 136.501 142.004 112.780 1.00 26.64  ? 171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.342 141.017 113.502 1.00 42.05  ? 171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.291 143.134 113.159 1.00 30.32  ? 171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.047 143.719 112.560 1.00 28.98  ? 171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.041 145.014 112.073 1.00 25.35  ? 171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 131.888 142.968 112.464 1.00 29.55  ? 171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 131.903 145.550 111.513 1.00 19.46  ? 171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 130.746 143.501 111.905 1.00 31.25  ? 171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 130.754 144.795 111.430 1.00 27.00  ? 171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 137.689 142.537 112.528 1.00 23.07  ? 172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 138.926 141.995 113.070 1.00 23.55  ? 172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.412 142.931 114.165 1.00 19.85  ? 172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.817 144.063 113.884 1.00 24.09  ? 172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 139.982 141.832 111.979 1.00 25.66  ? 172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 139.776 140.725 110.944 1.00 11.99  ? 172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 138.828 141.166 109.841 1.00 26.30  ? 172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.111 140.308 110.362 1.00 16.11  ? 172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.377 142.455 115.406 1.00 26.27  ? 173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 139.653 143.277 116.573 1.00 31.70  ? 173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 140.982 142.883 117.195 1.00 32.42  ? 173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.259 141.697 117.396 1.00 41.36  ? 173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 138.542 143.144 117.617 1.00 29.35  ? 173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.105 143.397 117.166 1.00 29.95  ? 173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.167 143.249 118.347 1.00 33.20  ? 173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 136.967 144.770 116.535 1.00 33.44  ? 173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 141.802 143.884 117.496 1.00 37.02  ? 174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.027 143.682 118.253 1.00 32.19  ? 174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 142.725 143.854 119.735 1.00 33.26  ? 174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.183 144.884 120.147 1.00 43.67  ? 174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.103 144.674 117.811 1.00 39.00  ? 174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 144.634 144.442 116.412 1.00 35.21  ? 174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 145.885 143.594 116.403 1.00 37.13  ? 174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 146.373 143.241 117.496 1.00 41.17  ? 174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 146.384 143.281 115.301 1.00 43.40  ? 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.072 142.847 120.530 1.00 30.39  ? 175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 142.811 142.849 121.964 1.00 32.13  ? 175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.135 143.069 122.682 1.00 33.42  ? 175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.045 142.237 122.590 1.00 34.99  ? 175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.142 141.545 122.423 1.00 28.13  ? 175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 141.595 141.700 123.830 1.00 31.11  ? 175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.040 141.151 121.459 1.00 27.19  ? 175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.242 144.187 123.394 1.00 31.56  ? 176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.451 144.497 124.134 1.00 30.74  ? 176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 145.457 143.767 125.475 1.00 34.50  ? 176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 144.438 143.255 125.944 1.00 33.67  ? 176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 145.581 146.005 124.338 1.00 27.22  ? 176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.021 146.468 124.343 1.00 31.93  ? 176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 147.932 145.692 124.624 1.00 34.32  ? 176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.234 147.740 124.029 1.00 35.81  ? 176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 146.632 143.731 126.099 1.00 40.63  ? 177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 146.838 142.965 127.330 1.00 33.48  ? 177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 146.465 143.817 128.544 1.00 39.42  ? 177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.311 144.320 129.286 1.00 46.07  ? 177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.276 142.473 127.408 1.00 34.82  ? 177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 148.492 141.485 128.531 1.00 44.67  ? 177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 147.582 140.670 128.791 1.00 49.21  ? 177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 149.576 141.516 129.149 1.00 44.18  ? 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.157 143.968 128.738 1.00 32.98  ? 178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 144.634 144.672 129.900 1.00 33.54  ? 178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.188 144.257 130.116 1.00 34.57  ? 178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 142.508 143.827 129.182 1.00 43.93  ? 178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 144.739 146.193 129.738 1.00 36.70  ? 178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 143.544 146.734 129.209 1.00 41.88  ? 178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 142.729 144.382 131.364 1.00 34.87  ? 179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.336 144.068 131.666 1.00 31.19  ? 179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.395 145.068 131.010 1.00 27.59  ? 179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.310 144.697 130.552 1.00 31.60  ? 179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.108 144.035 133.176 1.00 41.10  ? 179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 139.692 143.638 133.601 1.00 35.17  ? 179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 139.379 142.217 133.161 1.00 29.89  ? 179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 139.494 143.803 135.098 1.00 34.08  ? 179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 140.785 146.344 130.971 1.00 36.80  ? 180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 139.978 147.338 130.270 1.00 35.66  ? 180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 139.894 147.022 128.784 1.00 35.23  ? 180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 138.818 147.106 128.182 1.00 40.41  ? 180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 140.560 148.734 130.487 1.00 35.20  ? 180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 141.067 148.940 131.898 1.00 39.59  ? 180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 141.978 148.246 132.350 1.00 46.65  ? 180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 140.483 149.900 132.601 1.00 41.66  ? 180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.020 146.638 128.181 1.00 39.97  ? 181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.025 146.298 126.763 1.00 31.64  ? 181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.220 145.033 126.494 1.00 35.85  ? 181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.544 144.934 125.469 1.00 42.46  ? 181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.460 146.140 126.268 1.00 39.44  ? 181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.200 147.461 126.205 1.00 45.59  ? 181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 142.783 148.337 125.421 1.00 44.72  ? 181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.197 147.625 126.938 1.00 47.23  ? 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.266 144.063 127.408 1.00 30.44  ? 182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.492 142.838 127.225 1.00 25.33  ? 182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 137.999 143.119 127.369 1.00 28.63  ? 182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.176 142.594 126.609 1.00 31.42  ? 182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 139.976 141.761 128.211 1.00 26.21  ? 182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.264 141.124 127.692 1.00 28.92  ? 182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 138.907 140.702 128.432 1.00 28.60  ? 182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.050 140.396 128.744 1.00 27.69  ? 182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 137.628 143.955 128.342 1.00 29.47  ? 183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.231 144.340 128.499 1.00 27.44  ? 183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 135.728 145.088 127.272 1.00 35.68  ? 183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 134.609 144.848 126.801 1.00 37.04  ? 183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.066 145.199 129.751 1.00 30.40  ? 183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 136.712 144.611 130.865 1.00 37.10  ? 183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 136.545 145.999 126.740 1.00 35.02  ? 184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.173 146.686 125.512 1.00 28.91  ? 184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.108 145.728 124.332 1.00 34.24  ? 184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.282 145.916 123.437 1.00 42.06  ? 184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.151 147.823 125.222 1.00 31.00  ? 184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.654 148.800 124.172 1.00 37.37  ? 184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 135.217 149.216 124.428 1.00 34.56  ? 184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 135.129 150.444 125.207 1.00 40.84  ? 184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.007 151.118 125.414 1.00 42.98  ? 184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.046 152.238 126.129 1.00 42.11  ? 184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 132.851 150.704 124.922 1.00 36.07  ? 184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 136.961 144.705 124.308 1.00 35.31  ? 185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 136.874 143.696 123.260 1.00 25.51  ? 185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.548 142.955 123.325 1.00 31.51  ? 185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 134.911 142.723 122.295 1.00 38.23  ? 185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.042 142.717 123.371 1.00 26.34  ? 185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.110 142.589 124.532 1.00 33.32  ? 186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 133.811 141.933 124.688 1.00 34.20  ? 186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 132.690 142.861 124.230 1.00 32.27  ? 186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 131.778 142.456 123.494 1.00 33.66  ? 186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 133.601 141.486 126.146 1.00 30.46  ? 186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 134.782 140.649 126.635 1.00 30.36  ? 186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.303 140.711 126.287 1.00 29.49  ? 186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 134.928 139.336 125.926 1.00 35.86  ? 186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 132.749 144.125 124.658 1.00 35.11  ? 187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 131.714 145.088 124.295 1.00 29.83  ? 187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.638 145.273 122.784 1.00 36.82  ? 187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.553 145.233 122.195 1.00 43.73  ? 187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 131.984 146.426 124.986 1.00 38.17  ? 187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.172 147.563 124.396 1.00 48.03  ? 187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 129.934 147.427 124.297 1.00 42.95  ? 187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 131.771 148.595 124.029 1.00 45.69  ? 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 132.789 145.468 122.141 1.00 35.25  ? 188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 132.822 145.700 120.703 1.00 35.72  ? 188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.414 144.441 119.948 1.00 35.60  ? 188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 131.735 144.515 118.918 1.00 43.20  ? 188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.218 146.200 120.285 1.00 33.86  ? 188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.505 147.559 120.920 1.00 38.62  ? 188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.322 146.323 118.788 1.00 35.75  ? 188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 135.907 148.059 120.672 1.00 36.81  ? 188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 132.801 143.267 120.453 1.00 29.14  ? 189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.392 142.019 119.823 1.00 20.59  ? 189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 130.877 141.879 119.832 1.00 25.47  ? 189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.273 141.510 118.822 1.00 37.10  ? 189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.048 140.835 120.532 1.00 28.37  ? 189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.452 140.999 120.602 1.00 40.45  ? 189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.242 142.188 120.965 1.00 34.99  ? 190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 128.784 142.116 121.020 1.00 28.54  ? 190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.140 143.178 120.134 1.00 29.87  ? 190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.144 142.905 119.450 1.00 38.35  ? 190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.302 142.251 122.463 1.00 35.04  ? 190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.764 141.124 123.366 1.00 34.89  ? 190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 127.816 140.993 124.891 1.00 41.08  ? 190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 127.879 142.683 125.472 1.00 31.97  ? 190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 128.698 144.392 120.125 1.00 34.35  ? 191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.100 145.477 119.352 1.00 39.39  ? 191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.260 145.250 117.854 1.00 36.43  ? 191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.513 145.819 117.050 1.00 37.99  ? 191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 128.713 146.817 119.758 1.00 31.68  ? 191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 128.385 147.247 121.177 1.00 35.13  ? 191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 126.955 147.722 121.336 1.00 38.88  ? 191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 126.196 147.790 120.369 1.00 44.26  ? 191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.576 148.041 122.565 1.00 37.17  ? 191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.246 144.450 117.456 1.00 36.28  ? 192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.402 144.138 116.042 1.00 29.05  ? 192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.695 142.844 115.662 1.00 37.71  ? 192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.351 142.655 114.490 1.00 48.95  ? 192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 130.885 144.074 115.683 1.00 28.85  ? 192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 131.610 145.412 115.858 1.00 35.08  ? 192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.103 145.248 115.681 1.00 33.57  ? 192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.063 146.453 114.895 1.00 28.68  ? 192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.472 141.946 116.625 1.00 36.42  ? 193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 127.655 140.769 116.365 1.00 31.13  ? 193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.180 141.115 116.248 1.00 40.29  ? 193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.479 140.504 115.435 1.00 48.74  ? 193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 127.859 139.730 117.465 1.00 35.11  ? 193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 129.196 139.739 117.926 1.00 37.30  ? 193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 125.692 142.076 117.034 1.00 41.25  ? 194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.328 142.555 116.854 1.00 40.20  ? 194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.120 143.218 115.500 1.00 49.73  ? 194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 122.974 143.328 115.048 1.00 52.14  ? 194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 123.946 143.540 117.965 1.00 31.97  ? 194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 124.742 144.828 117.948 1.00 37.84  ? 194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.853 146.058 118.065 1.00 46.81  ? 194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.846 145.927 119.192 1.00 46.95  ? 194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 121.862 147.042 119.187 1.00 40.76  ? 194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.193 143.660 114.850 1.00 47.47  ? 195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.129 144.201 113.502 1.00 41.52  ? 195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.107 143.113 112.436 1.00 46.41  ? 195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.802 143.407 111.277 1.00 56.60  ? 195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.313 145.141 113.256 1.00 39.44  ? 195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.301 146.439 114.066 1.00 48.38  ? 195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.507 147.300 113.726 1.00 46.77  ? 195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.003 147.202 113.855 1.00 46.71  ? 195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.426 141.873 112.798 1.00 35.74  ? 196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.342 140.765 111.868 1.00 37.02  ? 196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.681 140.212 111.429 1.00 43.36  ? 196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 126.821 139.003 111.227 1.00 44.86  ? 196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.673 141.085 111.274 1.00 41.48  ? 197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 128.961 140.649 110.772 1.00 42.26  ? 197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 129.713 139.788 111.769 1.00 37.65  ? 197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.610 139.957 112.984 1.00 26.92  ? 197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.485 138.844 111.234 1.00 28.17  ? 198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.329 138.023 112.077 1.00 25.37  ? 198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 132.517 138.800 112.611 1.00 28.42  ? 198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.046 139.701 111.962 1.00 38.94  ? 198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 132.943 138.441 113.819 1.00 34.89  ? 199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 133.999 139.157 114.523 1.00 24.40  ? 199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.154 138.203 114.786 1.00 22.12  ? 199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 134.953 137.109 115.322 1.00 34.72  ? 199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 133.493 139.767 115.843 1.00 19.09  ? 199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 134.621 140.484 116.562 1.00 20.06  ? 199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.338 140.715 115.581 1.00 30.25  ? 199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.360 138.619 114.410 1.00 22.12  ? 200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 137.582 137.884 114.698 1.00 3.29   ? 200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.463 138.717 115.616 1.00 19.27  ? 200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 138.588 139.931 115.436 1.00 27.48  ? 200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.338 137.544 113.413 1.00 15.35  ? 200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.413 136.660 113.673 1.00 21.04  ? 200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.066 138.066 116.605 1.00 31.41  ? 201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 139.866 138.750 117.608 1.00 19.40  ? 201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.265 138.160 117.667 1.00 16.30  ? 201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.437 136.938 117.651 1.00 32.37  ? 201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.200 138.669 118.982 1.00 24.50  ? 201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 137.817 139.318 119.038 1.00 24.63  ? 201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 136.727 138.260 119.081 1.00 21.27  ? 201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 137.712 140.261 120.222 1.00 27.31  ? 201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.262 139.038 117.731 1.00 18.44  ? 202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 143.655 138.638 117.885 1.00 22.31  ? 202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 143.973 138.592 119.374 1.00 27.20  ? 202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 143.996 139.630 120.044 1.00 41.49  ? 202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 144.581 139.607 117.154 1.00 25.32  ? 202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.005 139.102 117.074 1.00 19.89  ? 202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.264 137.910 117.234 1.00 27.97  ? 202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 146.940 140.010 116.822 1.00 22.21  ? 202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.216 137.392 119.893 1.00 19.68  ? 203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 144.478 137.194 121.310 1.00 24.76  ? 203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 145.953 136.960 121.609 1.00 22.87  ? 203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.293 136.584 122.735 1.00 26.12  ? 203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 143.643 136.027 121.838 1.00 22.64  ? 203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.139 136.096 121.569 1.00 24.77  ? 203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 141.413 135.028 122.359 1.00 23.19  ? 203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 141.581 137.471 121.895 1.00 27.85  ? 203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 146.835 137.175 120.630 1.00 20.36  ? 204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.255 136.920 120.837 1.00 18.22  ? 204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 148.896 137.926 121.782 1.00 36.67  ? 204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 149.922 137.614 122.396 1.00 34.82  ? 204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 148.991 136.925 119.498 1.00 22.40  ? 204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 148.448 135.961 118.614 1.00 36.41  ? 204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 148.325 139.122 121.911 1.00 43.80  ? 205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 148.841 140.114 122.842 1.00 30.22  ? 205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 148.469 139.822 124.286 1.00 29.78  ? 205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.182 140.264 125.194 1.00 37.63  ? 205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 148.336 141.507 122.464 1.00 27.66  ? 205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 148.900 142.017 121.162 1.00 31.72  ? 205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 148.300 143.352 120.794 1.00 35.84  ? 205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.061 143.978 119.651 1.00 38.55  ? 205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.089 143.090 118.460 1.00 32.09  ? 205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 147.373 139.104 124.518 1.00 30.34  ? 206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 146.998 138.728 125.872 1.00 24.34  ? 206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.067 137.834 126.484 1.00 27.86  ? 206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 148.538 136.882 125.858 1.00 35.48  ? 206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 145.652 138.006 125.868 1.00 25.50  ? 206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 144.514 138.708 125.132 1.00 30.35  ? 206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 143.278 137.836 125.133 1.00 29.33  ? 206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 144.225 140.049 125.771 1.00 31.71  ? 206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 148.449 138.147 127.718 1.00 33.81  ? 207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 149.470 137.362 128.388 1.00 37.09  ? 207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 148.925 135.985 128.758 1.00 42.53  ? 207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 147.722 135.790 128.950 1.00 44.22  ? 207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 149.990 138.102 129.620 1.00 37.63  ? 207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 148.969 138.343 130.708 1.00 37.32  ? 207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 149.558 139.214 131.807 1.00 39.16  ? 207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 149.709 140.603 131.393 1.00 38.29  ? 207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 149.588 141.643 132.206 1.00 34.64  ? 207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 149.708 142.871 131.712 1.00 42.66  ? 207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 149.347 141.485 133.497 1.00 36.38  ? 207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 149.835 135.021 128.850 1.00 42.87  ? 208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 149.477 133.618 128.969 1.00 39.07  ? 208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 148.994 133.285 130.379 1.00 44.15  ? 208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 148.947 134.134 131.272 1.00 50.70  ? 208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.665 132.740 128.582 1.00 41.81  ? 208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.614 132.025 130.571 1.00 46.33  ? 209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 148.204 131.547 131.882 1.00 43.67  ? 209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 149.409 131.444 132.807 1.00 54.35  ? 209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 150.484 130.987 132.408 1.00 54.74  ? 209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 147.512 130.191 131.753 1.00 44.89  ? 209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 146.852 129.692 133.025 1.00 51.27  ? 209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 145.943 128.510 132.734 1.00 51.41  ? 209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 146.709 127.199 132.768 1.00 52.02  ? 209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 147.842 127.237 133.732 1.00 54.79  ? 209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.224 131.870 134.053 1.00 53.77  ? 210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 150.316 131.893 135.001 1.00 53.92  ? 210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 151.172 133.135 134.960 1.00 53.68  ? 210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 152.252 133.142 135.562 1.00 58.85  ? 210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.736 134.180 134.267 1.00 46.79  ? 211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 151.461 135.439 134.231 1.00 46.57  ? 211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.036 136.332 135.391 1.00 53.48  ? 211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.112 136.021 136.145 1.00 55.42  ? 211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 151.236 136.163 132.904 1.00 46.67  ? 211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 151.842 135.465 131.704 1.00 47.72  ? 211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 152.834 136.339 130.968 1.00 54.37  ? 211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 153.647 137.007 131.641 1.00 57.40  ? 211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 152.798 136.366 129.721 1.00 51.62  ? 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 151.729 137.459 135.523 1.00 51.17  ? 212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 151.522 138.351 136.654 1.00 47.30  ? 212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 150.561 139.479 136.305 1.00 49.04  ? 212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 150.604 140.038 135.205 1.00 56.41  ? 212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 152.856 138.931 137.119 1.00 50.07  ? 212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 149.687 139.810 137.253 1.00 47.92  ? 213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 148.821 140.982 137.170 1.00 50.03  ? 213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 149.243 141.925 138.287 1.00 53.85  ? 213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 148.905 141.704 139.456 1.00 60.94  ? 213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 147.336 140.617 137.290 1.00 48.42  ? 213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 146.985 139.460 136.358 1.00 53.39  ? 213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 146.466 141.824 136.977 1.00 46.69  ? 213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 145.685 138.774 136.711 1.00 51.68  ? 213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 149.975 142.982 137.929 1.00 57.42  ? 214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 150.526 143.931 138.899 1.00 59.25  ? 214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 151.403 143.217 139.928 1.00 64.81  ? 214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.069 143.131 141.109 1.00 67.66  ? 214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 149.422 144.741 139.584 1.00 59.52  ? 214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 149.417 146.219 139.217 1.00 56.69  ? 214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 148.189 146.954 139.755 1.00 61.00  ? 214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 147.322 146.071 140.640 1.00 60.36  ? 214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 146.163 145.509 139.894 1.00 59.73  ? 214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 152.510 142.654 139.439 1.00 66.42  ? 215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 153.626 142.126 140.225 1.00 70.80  ? 215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.257 140.980 141.166 1.00 71.24  ? 215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.087 140.565 141.983 1.00 70.31  ? 215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.337 143.282 140.967 1.00 67.86  ? 215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 153.706 143.666 142.322 1.00 69.82  ? 215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 152.908 142.924 142.930 1.00 68.79  ? 215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 154.030 144.777 142.791 1.00 69.31  ? 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.037 140.459 141.072 1.00 66.39  ? 216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.676 139.241 141.793 1.00 67.47  ? 216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 151.674 138.092 140.786 1.00 72.63  ? 216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.064 138.184 139.720 1.00 75.74  ? 216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.333 139.377 142.527 1.00 70.06  ? 216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.137 139.366 141.575 1.00 66.09  ? 216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.199 138.294 143.588 1.00 71.77  ? 216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.398 137.022 141.103 1.00 72.47  ? 217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 152.735 136.025 140.099 1.00 71.25  ? 217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 151.657 134.946 139.999 1.00 71.37  ? 217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 150.843 134.749 140.907 1.00 72.17  ? 217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.099 135.413 140.407 1.00 73.12  ? 217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.151 136.444 140.774 1.00 72.75  ? 217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 155.964 136.895 139.579 1.00 73.66  ? 217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.696 136.063 139.004 1.00 73.87  ? 217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 155.868 138.085 139.212 1.00 70.10  ? 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 151.666 134.237 138.865 1.00 67.93  ? 218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.737 133.149 138.577 1.00 67.59  ? 218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.291 133.585 138.760 1.00 68.59  ? 218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.484 132.857 139.347 1.00 67.81  ? 218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.038 131.933 139.454 1.00 65.64  ? 218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 150.828 130.625 138.722 1.00 68.85  ? 218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 149.740 130.049 138.756 1.00 71.77  ? 218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 151.868 130.150 138.048 1.00 66.64  ? 218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.954 134.771 138.258 1.00 58.44  ? 219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 147.645 135.364 138.483 1.00 57.02  ? 219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 146.705 135.206 137.293 1.00 55.71  ? 219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 145.499 135.020 137.478 1.00 55.67  ? 219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 147.802 136.848 138.836 1.00 58.05  ? 219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.229 135.279 136.075 1.00 55.07  ? 220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 146.381 135.196 134.894 1.00 52.28  ? 220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.866 133.779 134.694 1.00 53.41  ? 220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 146.533 132.801 135.042 1.00 55.39  ? 220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 147.152 135.635 133.653 1.00 48.01  ? 220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.351 134.862 133.542 1.00 59.17  ? 220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.525 137.090 133.763 1.00 46.94  ? 220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 144.669 133.671 134.124 1.00 52.63  ? 221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.132 132.390 133.693 1.00 57.53  ? 221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 144.307 132.166 132.197 1.00 58.30  ? 221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.752 131.205 131.655 1.00 55.74  ? 221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 142.656 132.275 134.078 1.00 57.94  ? 221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.787 133.425 133.612 1.00 56.10  ? 221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 140.337 133.200 134.011 1.00 57.29  ? 221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.219 132.776 135.467 1.00 55.07  ? 221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 140.814 133.783 136.389 1.00 53.90  ? 221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.060 133.030 131.526 1.00 55.41  ? 222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 145.415 132.843 130.134 1.00 50.67  ? 222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 144.387 133.421 129.186 1.00 48.97  ? 222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 143.414 134.074 129.574 1.00 51.89  ? 222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.630 133.165 127.897 1.00 46.37  ? 223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.694 133.583 126.860 1.00 47.85  ? 223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 142.458 132.703 126.805 1.00 45.06  ? 223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 141.489 133.064 126.132 1.00 48.52  ? 223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 144.365 133.597 125.474 1.00 40.60  ? 223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 145.717 134.287 125.545 1.00 38.64  ? 223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.508 132.184 124.933 1.00 39.88  ? 223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.461 131.562 127.498 1.00 43.63  ? 224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.304 130.672 127.474 1.00 40.15  ? 224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.121 131.306 128.198 1.00 46.43  ? 224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 138.967 131.150 127.783 1.00 49.73  ? 224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 141.675 129.302 128.068 1.00 45.55  ? 224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 140.450 128.406 128.157 1.00 44.10  ? 224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 142.758 128.643 127.230 1.00 44.99  ? 224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.381 132.031 129.287 1.00 39.75  ? 225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 139.308 132.767 129.938 1.00 35.60  ? 225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.721 133.844 129.045 1.00 38.03  ? 225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 137.505 134.052 129.016 1.00 46.70  ? 225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 139.581 134.543 128.302 1.00 28.01  ? 226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.099 135.542 127.357 1.00 32.38  ? 226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 138.305 134.882 126.238 1.00 36.65  ? 226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 137.323 135.452 125.750 1.00 38.19  ? 226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.274 136.368 126.807 1.00 34.37  ? 226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 139.757 137.563 126.023 1.00 37.05  ? 226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.171 136.820 127.945 1.00 38.47  ? 226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.705 133.682 125.808 1.00 40.23  ? 227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 137.912 132.955 124.822 1.00 34.85  ? 227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.562 132.543 125.389 1.00 36.64  ? 227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.561 132.552 124.671 1.00 42.87  ? 227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.668 131.732 124.308 1.00 33.28  ? 227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.001 132.045 123.677 1.00 28.10  ? 227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.587 130.699 122.644 1.00 46.81  ? 227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.692 129.385 123.847 1.00 46.72  ? 227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.514 132.165 126.666 1.00 33.96  ? 228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.233 131.877 127.305 1.00 36.30  ? 228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 134.332 133.105 127.284 1.00 38.57  ? 228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.146 133.025 126.931 1.00 47.46  ? 228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.456 131.428 128.745 1.00 39.36  ? 228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 135.616 129.944 128.949 1.00 40.54  ? 228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.793 129.693 129.864 1.00 48.43  ? 228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 136.509 128.560 130.816 1.00 46.86  ? 228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 137.632 128.343 131.768 1.00 49.02  ? 228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 134.889 134.255 127.670 1.00 24.10  ? 229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.119 135.494 127.670 1.00 23.31  ? 229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 133.635 135.845 126.269 1.00 28.44  ? 229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 132.475 136.224 126.084 1.00 35.93  ? 229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 134.957 136.634 128.244 1.00 36.33  ? 229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 135.170 136.680 129.755 1.00 27.49  ? 229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 136.325 137.604 130.081 1.00 28.47  ? 229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 133.904 137.141 130.447 1.00 31.32  ? 229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 134.510 135.717 125.270 1.00 31.61  ? 230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.129 136.023 123.896 1.00 26.33  ? 230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.074 135.052 123.383 1.00 33.87  ? 230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.143 135.455 122.681 1.00 46.53  ? 230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.362 135.999 122.997 1.00 33.72  ? 230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.286 137.208 123.112 1.00 38.56  ? 230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 137.596 136.944 122.391 1.00 37.73  ? 230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 135.602 138.442 122.556 1.00 33.36  ? 230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.205 133.769 123.722 1.00 36.57  ? 231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 132.239 132.774 123.278 1.00 35.10  ? 231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 130.862 133.049 123.861 1.00 40.75  ? 231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 129.853 132.979 123.151 1.00 48.50  ? 231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.726 131.377 123.661 1.00 34.51  ? 231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.616 130.350 123.661 1.00 52.62  ? 231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 131.172 129.955 122.563 1.00 55.46  ? 231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.198 129.926 124.758 1.00 50.80  ? 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 130.800 133.393 125.148 1.00 37.11  ? 232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 129.505 133.705 125.743 1.00 36.47  ? 232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 128.971 135.047 125.261 1.00 36.40  ? 232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 127.752 135.236 125.186 1.00 50.84  ? 232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.614 133.671 127.261 1.00 36.74  ? 232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 129.777 132.267 127.786 1.00 48.94  ? 232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 128.798 131.592 128.104 1.00 49.31  ? 232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 131.018 131.802 127.846 1.00 47.33  ? 232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 129.859 135.983 124.922 1.00 28.70  ? 233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 129.424 137.243 124.332 1.00 25.03  ? 233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 128.804 137.025 122.958 1.00 32.55  ? 233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 127.792 137.649 122.620 1.00 41.84  ? 233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 130.603 138.208 124.244 1.00 27.45  ? 233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 129.401 136.146 122.152 1.00 38.88  ? 234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 128.850 135.859 120.831 1.00 35.22  ? 234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 127.579 135.030 120.938 1.00 40.30  ? 234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 126.666 135.178 120.117 1.00 40.95  ? 234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 129.889 135.147 119.967 1.00 31.07  ? 234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.007 136.037 119.507 1.00 34.73  ? 234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 130.739 137.217 118.841 1.00 40.10  ? 234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.324 135.690 119.733 1.00 30.28  ? 234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 131.766 138.036 118.418 1.00 34.88  ? 234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.353 136.507 119.316 1.00 32.29  ? 234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.073 137.678 118.657 1.00 32.08  ? 234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 127.502 134.150 121.938 1.00 41.56  ? 235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.262 133.424 122.187 1.00 39.21  ? 235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.145 134.373 122.597 1.00 43.24  ? 235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 123.993 134.199 122.184 1.00 46.55  ? 235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.478 132.360 123.261 1.00 37.77  ? 235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.131 130.954 122.811 1.00 49.67  ? 235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 125.880 130.036 123.998 1.00 47.66  ? 235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 126.907 130.156 125.026 1.00 48.57  ? 235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.146 129.696 124.909 1.00 46.85  ? 235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 128.996 129.862 125.919 1.00 45.69  ? 235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 128.554 129.073 123.817 1.00 39.13  ? 235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 125.463 135.380 123.413 1.00 38.68  ? 236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 124.447 136.343 123.822 1.00 43.00  ? 236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 123.981 137.187 122.643 1.00 44.24  ? 236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 122.781 137.436 122.487 1.00 47.40  ? 236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 124.988 137.231 124.940 1.00 36.16  ? 236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 123.944 138.139 125.541 1.00 40.07  ? 236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 122.971 137.634 126.390 1.00 39.19  ? 236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 123.930 139.499 125.262 1.00 32.93  ? 236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.014 138.453 126.943 1.00 41.61  ? 236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 122.974 140.327 125.812 1.00 32.30  ? 236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.019 139.796 126.652 1.00 37.28  ? 236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.062 140.608 127.207 1.00 38.00  ? 236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 124.913 137.639 121.809 1.00 43.85  ? 237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 124.575 138.386 120.598 1.00 46.92  ? 237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.361 137.425 119.428 1.00 56.79  ? 237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.103 137.403 118.447 1.00 59.08  ? 237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 125.658 139.414 120.292 1.00 40.92  ? 237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.314 136.611 119.557 1.00 68.59  ? 238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.010 135.563 118.593 1.00 67.54  ? 238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.101 136.027 117.467 1.00 73.03  ? 238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 121.606 135.179 116.715 1.00 78.27  ? 238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 122.381 134.363 119.302 1.00 72.35  ? 238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 123.335 133.196 119.423 1.00 71.53  ? 238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 124.398 133.229 118.768 1.00 72.34  ? 238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 123.026 132.249 120.176 1.00 67.74  ? 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.866 137.335 117.338 1.00 82.10  ? 239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.113 137.894 116.215 1.00 85.28  ? 239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.738 137.238 116.091 1.00 87.36  ? 239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.367 136.726 115.032 1.00 86.05  ? 239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.907 137.751 114.913 1.00 84.47  ? 239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 123.359 138.178 115.033 1.00 81.42  ? 239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 124.206 137.724 113.859 1.00 83.87  ? 239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 123.736 137.667 112.723 1.00 86.40  ? 239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 125.464 137.396 114.131 1.00 80.93  ? 239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.995 137.228 117.201 1.00 96.05  ? 240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.678 136.609 117.351 1.00 98.05  ? 240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 117.758 135.085 117.407 1.00 100.04 ? 240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 116.760 134.432 117.740 1.00 99.76  ? 240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.716 137.036 116.226 1.00 99.56  ? 240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.316 136.441 116.251 1.00 100.22 ? 240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 113.971 137.609 116.029 1.00 106.16 ? 240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.595 136.468 115.927 1.00 97.95  ? 240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 118.925 134.498 117.169 1.00 101.55 ? 241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.018 133.075 116.942 1.00 100.43 ? 241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 118.763 132.667 115.511 1.00 102.44 ? 241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 118.957 131.492 115.173 1.00 100.72 ? 241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 118.337 133.606 114.659 1.00 110.61 ? 242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.147 133.312 113.243 1.00 111.49 ? 242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 119.457 132.884 112.601 1.00 110.88 ? 242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 119.494 131.925 111.821 1.00 107.14 ? 242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 117.577 134.541 112.537 1.00 109.54 ? 242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.120 134.827 112.856 1.00 108.59 ? 242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.623 136.105 112.208 1.00 109.92 ? 242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.335 136.734 111.425 1.00 111.68 ? 242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.398 136.499 112.538 1.00 107.65 ? 242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 120.541 133.588 112.917 1.00 101.12 ? 243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 121.893 133.152 112.597 1.00 100.78 ? 243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 122.717 133.289 113.864 1.00 99.61  ? 243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 122.852 134.394 114.397 1.00 96.91  ? 243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 122.501 133.977 111.459 1.00 98.02  ? 243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.015 133.889 111.389 1.00 98.29  ? 243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 124.461 132.526 110.887 1.00 100.88 ? 243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.907 132.362 110.960 1.00 100.52 ? 243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.714 132.345 109.907 1.00 99.09  ? 243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 128.021 132.183 110.094 1.00 96.53  ? 243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.248 132.488 108.677 1.00 97.90  ? 243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.258 132.172 114.347 1.00 88.50  ? 244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 123.962 132.175 115.621 1.00 88.29  ? 244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.184 133.080 115.559 1.00 86.89  ? 244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 125.846 133.190 114.524 1.00 83.98  ? 244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.379 130.753 116.000 1.00 85.37  ? 244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.248 129.906 116.560 1.00 86.20  ? 244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 123.730 128.569 117.085 1.00 86.56  ? 244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 124.601 127.934 116.491 1.00 84.86  ? 244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.161 128.132 118.202 1.00 84.76  ? 244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 125.471 133.744 116.678 1.00 70.64  ? 245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 126.621 134.621 116.763 1.00 65.45  ? 245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 127.920 133.881 116.526 1.00 64.11  ? 245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.309 133.018 117.319 1.00 62.19  ? 245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 128.599 134.213 115.434 1.00 57.70  ? 246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 129.823 133.538 115.030 1.00 56.45  ? 246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.007 134.460 115.271 1.00 53.24  ? 246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.001 135.615 114.835 1.00 47.83  ? 246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 129.762 133.126 113.558 1.00 55.55  ? 246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 128.759 132.150 113.342 1.00 62.30  ? 246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.013 133.948 115.963 1.00 32.67  ? 247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 133.201 134.724 116.255 1.00 18.38  ? 247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 134.438 133.859 116.160 1.00 19.45  ? 247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 134.398 132.651 116.403 1.00 36.87  ? 247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 135.545 134.495 115.797 1.00 22.12  ? 248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 136.825 133.821 115.665 1.00 21.89  ? 248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 137.813 134.382 116.675 1.00 18.86  ? 248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 137.719 135.541 117.087 1.00 26.19  ? 248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 137.395 133.968 114.252 1.00 18.58  ? 248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 138.757 133.538 117.079 1.00 20.85  ? 249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 139.860 133.939 117.939 1.00 12.54  ? 249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.151 133.438 117.317 1.00 12.34  ? 249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.258 132.257 116.972 1.00 28.01  ? 249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.697 133.385 119.357 1.00 23.96  ? 249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.122 134.329 117.165 1.00 11.89  ? 250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 143.397 133.996 116.550 1.00 17.51  ? 250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 144.514 134.123 117.573 1.00 13.05  ? 250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 144.531 135.059 118.378 1.00 24.98  ? 250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 143.681 134.897 115.349 1.00 22.60  ? 250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.186 134.337 114.036 1.00 22.65  ? 250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 141.841 134.382 113.703 1.00 14.66  ? 250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.066 133.762 113.131 1.00 20.26  ? 250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.385 133.869 112.507 1.00 7.06   ? 250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.620 133.247 111.933 1.00 24.57  ? 250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.279 133.304 111.626 1.00 21.53  ? 250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 141.830 132.794 110.431 1.00 25.20  ? 250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 145.444 133.174 117.541 1.00 14.43  ? 251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 146.573 133.168 118.458 1.00 20.26  ? 251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 147.830 132.772 117.702 1.00 25.15  ? 251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 147.805 131.830 116.907 1.00 32.19  ? 251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 146.339 132.204 119.625 1.00 32.54  ? 251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.248 132.413 120.834 1.00 17.93  ? 251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 146.789 133.612 121.629 1.00 21.81  ? 251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 147.289 131.179 121.706 1.00 22.04  ? 251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 148.919 133.493 117.953 1.00 34.02  ? 252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.202 133.120 117.377 1.00 30.78  ? 252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 150.647 131.773 117.930 1.00 29.46  ? 252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 150.442 131.468 119.107 1.00 35.94  ? 252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.248 134.191 117.675 1.00 23.99  ? 252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 152.384 134.190 116.675 1.00 34.95  ? 252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 153.223 133.292 116.673 1.00 43.19  ? 252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 152.414 135.197 115.814 1.00 32.75  ? 252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 151.247 130.952 117.065 1.00 27.12  ? 253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 151.672 129.624 117.487 1.00 28.93  ? 253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 152.809 129.687 118.498 1.00 36.88  ? 253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.054 128.708 119.212 1.00 43.44  ? 253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.067 128.773 116.267 1.00 28.66  ? 253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 151.991 127.285 116.613 1.00 27.07  ? 253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.454 129.147 115.777 1.00 32.82  ? 253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 151.684 126.399 115.442 1.00 34.05  ? 253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 153.508 130.815 118.586 1.00 37.46  ? 254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 154.555 130.999 119.580 1.00 31.18  ? 254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.023 131.551 120.895 1.00 35.36  ? 254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 154.797 131.698 121.847 1.00 45.76  ? 254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 155.648 131.914 119.026 1.00 34.54  ? 254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 156.583 131.222 118.081 1.00 40.43  ? 254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 157.466 130.261 118.542 1.00 39.74  ? 254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 156.567 131.513 116.729 1.00 43.79  ? 254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 158.322 129.617 117.679 1.00 41.65  ? 254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 157.423 130.870 115.859 1.00 45.63  ? 254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 158.302 129.921 116.336 1.00 45.65  ? 254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 152.734 131.869 120.964 1.00 34.34  ? 255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.109 132.208 122.233 1.00 24.19  ? 255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 152.125 130.994 123.151 1.00 36.86  ? 255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 151.930 129.859 122.709 1.00 47.67  ? 255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 150.675 132.687 121.997 1.00 31.27  ? 255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.061 133.389 123.168 1.00 34.27  ? 255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 149.744 132.746 124.344 1.00 36.92  ? 255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 149.686 134.679 123.334 1.00 31.12  ? 255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.209 133.610 125.187 1.00 26.15  ? 255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 149.162 134.790 124.598 1.00 21.46  ? 255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 152.368 131.238 124.439 1.00 43.25  ? 256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.482 130.139 125.391 1.00 42.06  ? 256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.185 129.345 125.488 1.00 43.83  ? 256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.209 128.113 125.597 1.00 47.69  ? 256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 152.890 130.681 126.757 1.00 44.24  ? 256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.853 129.796 127.508 1.00 48.63  ? 256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.106 128.714 128.256 1.00 47.04  ? 256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.761 129.131 128.632 1.00 49.92  ? 256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 150.928 128.399 129.359 1.00 51.43  ? 256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 149.722 128.880 129.646 1.00 48.85  ? 256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 151.270 127.201 129.802 1.00 48.57  ? 256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.051 130.024 125.441 1.00 40.46  ? 257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 148.742 129.384 125.541 1.00 33.25  ? 257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.339 128.640 124.290 1.00 39.83  ? 257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.162 128.279 124.220 1.00 44.16  ? 257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.673 130.426 125.872 1.00 38.18  ? 257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.752 130.905 127.300 1.00 47.43  ? 257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 148.484 130.284 128.097 1.00 52.83  ? 257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 147.079 131.902 127.625 1.00 53.19  ? 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.231 128.394 123.327 1.00 45.46  ? 258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 148.812 127.801 122.059 1.00 43.60  ? 258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.270 126.392 122.274 1.00 43.59  ? 258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.328 125.968 121.595 1.00 48.92  ? 258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 149.973 127.825 121.045 1.00 41.06  ? 258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.476 127.412 119.659 1.00 37.84  ? 258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.129 126.944 121.500 1.00 36.04  ? 258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.373 128.299 119.134 1.00 33.24  ? 258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 148.847 125.645 123.218 1.00 46.09  ? 259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 148.353 124.299 123.486 1.00 41.31  ? 259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 146.973 124.336 124.130 1.00 43.67  ? 259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.080 123.576 123.740 1.00 48.03  ? 259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 149.342 123.539 124.368 1.00 48.72  ? 259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 150.500 122.961 123.578 1.00 48.93  ? 259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 150.303 122.176 122.651 1.00 47.41  ? 259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 151.716 123.346 123.944 1.00 44.40  ? 259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 146.777 125.215 125.117 1.00 42.07  ? 260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 145.453 125.381 125.703 1.00 39.92  ? 260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 144.489 126.027 124.718 1.00 36.51  ? 260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 143.280 125.773 124.775 1.00 41.64  ? 260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 145.544 126.211 126.983 1.00 41.86  ? 260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 146.561 125.661 127.961 1.00 48.61  ? 260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.717 125.432 127.550 1.00 51.89  ? 260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 146.203 125.455 129.139 1.00 46.67  ? 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.004 126.867 123.819 1.00 41.35  ? 261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.178 127.452 122.768 1.00 39.29  ? 261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 143.601 126.371 121.865 1.00 28.40  ? 261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.426 126.426 121.487 1.00 31.44  ? 261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.020 128.446 121.968 1.00 40.36  ? 261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.298 129.101 120.831 1.00 36.37  ? 261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.527 130.228 121.045 1.00 30.43  ? 261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.421 128.616 119.542 1.00 37.35  ? 261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 142.871 130.844 120.002 1.00 29.94  ? 261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 143.768 129.229 118.495 1.00 34.49  ? 261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 142.995 130.346 118.728 1.00 33.68  ? 261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 144.418 125.377 121.511 1.00 35.42  ? 262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 143.954 124.260 120.696 1.00 39.31  ? 262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.140 123.257 121.501 1.00 44.86  ? 262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 142.264 122.587 120.942 1.00 42.92  ? 262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.148 123.555 120.053 1.00 38.80  ? 262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.003 124.402 119.117 1.00 33.34  ? 262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.272 123.660 118.747 1.00 32.96  ? 262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 145.208 124.763 117.884 1.00 39.11  ? 262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 143.414 123.132 122.803 1.00 52.97  ? 263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 142.728 122.146 123.627 1.00 44.79  ? 263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.238 122.423 123.756 1.00 48.85  ? 263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 140.485 121.519 124.133 1.00 62.87  ? 263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 143.357 122.091 125.020 1.00 53.07  ? 263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 144.621 121.257 125.061 1.00 58.89  ? 263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 144.776 120.362 124.204 1.00 61.27  ? 263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 145.462 121.495 125.953 1.00 54.12  ? 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 140.795 123.643 123.458 1.00 44.07  ? 264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 139.385 123.983 123.593 1.00 47.06  ? 264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 138.531 123.428 122.462 1.00 52.14  ? 264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 137.307 123.354 122.609 1.00 49.98  ? 264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 139.215 125.500 123.666 1.00 49.16  ? 264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 139.697 126.098 122.457 1.00 50.39  ? 264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 139.997 126.056 124.842 1.00 50.46  ? 264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.140 123.041 121.345 1.00 53.17  ? 265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 138.412 122.450 120.230 1.00 53.48  ? 265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 138.402 120.929 120.262 1.00 52.02  ? 265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 137.796 120.312 119.380 1.00 50.25  ? 265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.000 122.929 118.900 1.00 50.88  ? 265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 138.559 124.322 118.504 1.00 49.84  ? 265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.062 124.488 118.671 1.00 50.50  ? 265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 136.614 125.867 118.243 1.00 48.98  ? 265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.212 126.145 118.651 1.00 50.33  ? 265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.056 120.314 121.241 1.00 57.62  ? 266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 139.016 118.865 121.365 1.00 56.18  ? 266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 137.628 118.410 121.795 1.00 62.31  ? 266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 136.975 119.052 122.623 1.00 64.71  ? 266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 140.062 118.387 122.371 1.00 57.44  ? 266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 141.489 118.453 121.857 1.00 60.55  ? 266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 142.536 118.388 122.972 1.00 60.18  ? 266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 142.321 117.233 123.950 1.00 61.19  ? 266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 141.352 117.523 125.049 1.00 62.68  ? 266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 137.171 117.298 121.217 1.00 67.79  ? 267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 135.881 116.742 121.613 1.00 67.49  ? 267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 135.946 116.224 123.043 1.00 66.44  ? 267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 134.986 116.358 123.812 1.00 66.16  ? 267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 135.444 115.642 120.628 1.00 69.73  ? 267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 135.505 116.155 119.189 1.00 68.62  ? 267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 134.041 115.159 120.955 1.00 68.73  ? 267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 136.686 115.633 118.403 1.00 66.75  ? 267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 137.079 115.632 123.425 1.00 68.91  ? 268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 137.263 115.131 124.782 1.00 72.66  ? 268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 137.429 116.244 125.808 1.00 72.21  ? 268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 137.428 115.955 127.010 1.00 69.20  ? 268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 138.475 114.200 124.834 1.00 70.15  ? 268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 139.653 114.873 124.422 1.00 66.44  ? 268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 137.581 117.493 125.371 1.00 78.13  ? 269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 137.766 118.594 126.306 1.00 76.46  ? 269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 136.534 118.770 127.183 1.00 77.89  ? 269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.396 118.667 126.717 1.00 74.96  ? 269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.061 119.889 125.549 1.00 72.65  ? 269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 136.771 119.037 128.464 1.00 83.25  ? 270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 135.686 119.224 129.412 1.00 82.00  ? 270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 134.965 120.545 129.155 1.00 80.80  ? 270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 135.484 121.455 128.503 1.00 82.61  ? 270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 136.219 119.182 130.844 1.00 82.97  ? 270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 137.406 120.102 131.050 1.00 83.11  ? 270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 137.196 121.322 131.204 1.00 80.82  ? 270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 138.551 119.604 131.059 1.00 82.31  ? 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 133.743 120.640 129.684 1.00 84.26  ? 271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 132.947 121.851 129.529 1.00 85.69  ? 271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 133.564 123.048 130.238 1.00 86.39  ? 271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.170 124.187 129.965 1.00 84.99  ? 271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 131.527 121.619 130.049 1.00 84.29  ? 271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 130.835 120.397 129.460 1.00 85.69  ? 271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 130.985 120.305 127.953 1.00 88.52  ? 271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.744 121.319 127.264 1.00 88.19  ? 271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.344 119.216 127.457 1.00 85.56  ? 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 134.520 122.818 131.139 1.00 81.05  ? 272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.178 123.900 131.855 1.00 80.45  ? 272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.263 124.578 131.023 1.00 82.19  ? 272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 136.788 125.613 131.443 1.00 81.84  ? 272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 135.760 123.359 133.170 1.00 80.26  ? 272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 136.433 124.430 134.008 1.00 82.55  ? 272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 135.738 125.071 134.825 1.00 80.20  ? 272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 137.656 124.632 133.852 1.00 79.50  ? 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 136.603 124.035 129.855 1.00 76.28  ? 273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 137.613 124.647 128.997 1.00 74.78  ? 273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.060 124.824 127.586 1.00 73.21  ? 273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 137.518 125.689 126.832 1.00 73.79  ? 273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 138.906 123.808 128.990 1.00 75.56  ? 273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 138.656 122.435 128.382 1.00 75.96  ? 273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.028 124.537 128.259 1.00 72.68  ? 273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.053 124.030 127.232 1.00 71.10  ? 274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 135.581 123.984 125.853 1.00 72.14  ? 274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 134.809 125.248 125.489 1.00 71.25  ? 274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 133.991 125.740 126.270 1.00 72.11  ? 274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 134.705 122.749 125.640 1.00 73.63  ? 274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 133.755 122.848 124.458 1.00 70.68  ? 274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.458 121.479 123.861 1.00 73.18  ? 274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.294 121.173 122.703 1.00 75.51  ? 274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 134.277 121.839 121.554 1.00 74.45  ? 274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.109 121.476 120.583 1.00 71.99  ? 274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 133.445 122.848 121.347 1.00 72.22  ? 274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.079 125.771 124.294 1.00 61.07  ? 275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 134.315 126.867 123.711 1.00 62.16  ? 275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 133.605 126.341 122.471 1.00 63.91  ? 275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.152 125.533 121.712 1.00 67.35  ? 275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.202 128.083 123.365 1.00 57.23  ? 275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.644 128.795 124.634 1.00 57.07  ? 275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.407 127.653 122.546 1.00 62.68  ? 275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 132.372 126.797 122.271 1.00 59.43  ? 276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 131.523 126.274 121.205 1.00 60.39  ? 276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.317 127.242 120.054 1.00 56.70  ? 276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.521 126.866 118.897 1.00 59.56  ? 276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.155 125.870 121.774 1.00 64.65  ? 276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.217 125.233 123.152 1.00 65.03  ? 276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.346 123.722 123.057 1.00 61.40  ? 276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 129.946 123.054 124.362 1.00 62.71  ? 276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.160 123.949 125.532 1.00 61.82  ? 276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 130.914 128.480 120.333 1.00 50.10  ? 277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.628 129.447 119.281 1.00 49.81  ? 277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 131.853 130.233 118.837 1.00 48.43  ? 277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 131.728 131.101 117.967 1.00 52.46  ? 277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.543 130.427 119.742 1.00 52.58  ? 277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.031 131.197 120.847 1.00 47.84  ? 277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.292 129.676 120.164 1.00 50.86  ? 277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.021 129.960 119.407 1.00 43.76  ? 278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.247 130.678 119.071 1.00 39.42  ? 278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.110 129.797 118.178 1.00 35.22  ? 278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 135.727 128.838 118.644 1.00 41.41  ? 278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.002 131.088 120.331 1.00 36.69  ? 278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 135.879 132.328 120.162 1.00 30.11  ? 278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.039 133.516 119.765 1.00 32.01  ? 278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.646 132.619 121.432 1.00 37.91  ? 278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.151 130.129 116.891 1.00 25.83  ? 279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.121 129.511 116.000 1.00 27.42  ? 279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.524 129.957 116.384 1.00 27.93  ? 279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 137.727 131.048 116.923 1.00 43.23  ? 279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 135.825 129.886 114.550 1.00 29.47  ? 279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 134.630 129.275 114.101 1.00 37.19  ? 279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.505 129.102 116.113 1.00 24.15  ? 280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 139.879 129.381 116.499 1.00 28.57  ? 280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 140.773 129.328 115.271 1.00 33.64  ? 280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 140.567 128.525 114.356 1.00 41.22  ? 280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.388 128.412 117.591 1.00 28.04  ? 280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.494 126.984 117.058 1.00 29.95  ? 280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.493 128.470 118.819 1.00 35.95  ? 280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 141.549 126.161 117.759 1.00 27.69  ? 280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 141.753 130.219 115.244 1.00 21.97  ? 281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 142.769 130.202 114.210 1.00 6.75   ? 281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.142 130.324 114.833 1.00 14.92  ? 281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 144.315 130.935 115.889 1.00 31.34  ? 281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.125 129.726 114.166 1.00 24.37  ? 282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.503 129.713 114.640 1.00 19.64  ? 282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 147.377 130.408 113.609 1.00 19.95  ? 282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 147.362 130.046 112.427 1.00 33.68  ? 282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.000 128.282 114.908 1.00 23.70  ? 282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.507 128.268 115.062 1.00 29.68  ? 282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.347 127.736 116.157 1.00 30.33  ? 282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.133 131.404 114.058 1.00 18.04  ? 283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.038 132.159 113.204 1.00 18.99  ? 283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 150.423 131.543 113.332 1.00 25.11  ? 283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.009 131.534 114.421 1.00 35.65  ? 283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.051 133.647 113.584 1.00 19.35  ? 283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 149.813 134.448 112.553 1.00 21.34  ? 283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 147.630 134.161 113.725 1.00 23.94  ? 283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 150.946 131.028 112.226 1.00 28.11  ? 284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 152.201 130.285 112.211 1.00 32.32  ? 284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 153.231 131.112 111.447 1.00 35.53  ? 284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.161 131.199 110.212 1.00 42.17  ? 284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.028 128.898 111.580 1.00 31.55  ? 284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 150.899 128.133 112.273 1.00 26.11  ? 284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.330 128.117 111.652 1.00 33.27  ? 284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 150.815 126.680 111.873 1.00 30.54  ? 284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 154.196 131.730 112.121 1.00 36.76  ? 285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 155.307 132.359 111.404 1.00 39.57  ? 285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 156.206 131.309 110.768 1.00 42.05  ? 285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 156.149 130.122 111.092 1.00 44.81  ? 285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.049 133.138 112.497 1.00 39.74  ? 285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.096 133.205 113.654 1.00 38.43  ? 285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 154.275 131.963 113.571 1.00 35.90  ? 285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.043 131.769 109.835 1.00 52.04  ? 286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 157.975 130.861 109.175 1.00 48.90  ? 286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 158.945 130.236 110.166 1.00 53.63  ? 286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.485 129.155 109.907 1.00 56.54  ? 286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 158.751 131.596 108.081 1.00 48.92  ? 286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.146 131.404 106.706 1.00 57.36  ? 286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 156.967 131.005 106.624 1.00 58.52  ? 286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 158.850 131.655 105.706 1.00 58.10  ? 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 159.182 130.898 111.303 1.00 54.58  ? 287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.116 130.370 112.291 1.00 50.33  ? 287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 159.636 129.039 112.852 1.00 53.49  ? 287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.439 128.124 113.066 1.00 64.19  ? 287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 160.319 131.384 113.416 1.00 50.46  ? 287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 161.462 131.037 114.351 1.00 46.88  ? 287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 162.725 130.722 113.570 1.00 55.48  ? 287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 163.913 130.525 114.490 1.00 57.12  ? 287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 165.186 130.406 113.730 1.00 53.25  ? 287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 158.332 128.913 113.110 1.00 45.52  ? 288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 157.802 127.649 113.608 1.00 44.13  ? 288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 157.983 126.535 112.585 1.00 46.73  ? 288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.320 125.400 112.944 1.00 52.11  ? 288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.327 127.801 113.977 1.00 43.30  ? 288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 155.730 126.569 114.593 1.00 46.97  ? 288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 155.863 126.325 115.948 1.00 48.86  ? 288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.039 125.653 113.817 1.00 46.04  ? 288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.319 125.192 116.519 1.00 52.23  ? 288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 154.494 124.518 114.382 1.00 43.89  ? 288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 154.633 124.288 115.733 1.00 50.49  ? 288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 157.755 126.838 111.306 1.00 53.15  ? 289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 157.931 125.832 110.265 1.00 52.77  ? 289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.395 125.430 110.157 1.00 52.26  ? 289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 159.716 124.253 109.951 1.00 58.74  ? 289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.380 126.354 108.925 1.00 54.67  ? 289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 157.542 125.304 107.838 1.00 51.62  ? 289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 155.921 126.753 109.076 1.00 49.39  ? 289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.308 126.394 110.295 1.00 54.63  ? 290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 161.731 126.069 110.297 1.00 52.89  ? 290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.091 125.176 111.477 1.00 51.88  ? 290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 162.829 124.196 111.319 1.00 62.15  ? 290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 162.565 127.349 110.321 1.00 52.29  ? 290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 162.371 128.243 109.108 1.00 57.89  ? 290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 163.068 129.582 109.253 1.00 61.58  ? 290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 163.960 129.700 110.121 1.00 59.54  ? 290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 162.722 130.517 108.502 1.00 61.50  ? 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 161.577 125.495 112.666 1.00 46.70  ? 291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 161.869 124.683 113.844 1.00 51.40  ? 291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 161.333 123.267 113.685 1.00 56.20  ? 291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 161.997 122.296 114.065 1.00 57.94  ? 291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.283 125.337 115.095 1.00 46.77  ? 291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 161.880 126.678 115.513 1.00 49.36  ? 291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 160.961 127.381 116.494 1.00 49.28  ? 291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.264 126.486 116.111 1.00 51.05  ? 291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.126 123.130 113.130 1.00 54.54  ? 292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 159.574 121.806 112.876 1.00 46.98  ? 292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 160.380 121.051 111.828 1.00 48.76  ? 292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 160.539 119.830 111.931 1.00 55.11  ? 292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.114 121.922 112.440 1.00 49.81  ? 292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 160.891 121.756 110.816 1.00 57.21  ? 293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 161.627 121.100 109.740 1.00 58.11  ? 293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 162.912 120.455 110.247 1.00 64.27  ? 293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 163.236 119.326 109.863 1.00 66.23  ? 293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 161.928 122.107 108.631 1.00 58.59  ? 293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 162.789 121.569 107.504 1.00 60.70  ? 293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.211 122.690 106.573 1.00 63.81  ? 293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.063 123.461 106.109 1.00 67.15  ? 293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 161.996 124.785 106.116 1.00 65.34  ? 293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 160.894 125.381 105.671 1.00 64.51  ? 293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 163.000 125.525 106.558 1.00 58.87  ? 293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 163.653 121.148 111.108 1.00 65.65  ? 294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 164.904 120.624 111.640 1.00 64.92  ? 294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 164.706 119.728 112.855 1.00 67.57  ? 294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 165.693 119.200 113.380 1.00 69.82  ? 294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 165.856 121.772 112.000 1.00 64.13  ? 294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 165.696 123.013 111.141 1.00 67.64  ? 294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.447 122.916 109.828 1.00 70.28  ? 294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 167.243 121.968 109.665 1.00 67.43  ? 294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.239 123.787 108.958 1.00 70.16  ? 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 163.465 119.548 113.309 1.00 67.05  ? 295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 163.148 118.677 114.443 1.00 67.88  ? 295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 163.909 119.097 115.699 1.00 72.61  ? 295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 164.347 118.261 116.491 1.00 73.47  ? 295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 163.419 117.209 114.105 1.00 68.18  ? 295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 162.535 116.254 114.886 1.00 72.36  ? 295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.158 116.584 116.030 1.00 71.15  ? 295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 162.216 115.170 114.354 1.00 70.59  ? 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.074 120.402 115.877 1.00 70.20  ? 296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 164.703 120.955 117.066 1.00 67.87  ? 296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 163.637 121.486 118.014 1.00 65.19  ? 296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 162.570 121.935 117.589 1.00 64.46  ? 296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 165.685 122.071 116.704 1.00 69.98  ? 296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 165.294 122.870 115.473 1.00 69.12  ? 296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 166.206 124.072 115.276 1.00 67.28  ? 296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 167.674 123.695 115.412 1.00 68.52  ? 296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 168.063 122.597 114.484 1.00 67.49  ? 296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 163.936 121.424 119.310 1.00 66.01  ? 297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 162.984 121.857 120.323 1.00 64.34  ? 297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 162.636 123.329 120.144 1.00 65.31  ? 297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 163.519 124.176 119.978 1.00 63.50  ? 297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 163.556 121.615 121.719 1.00 64.59  ? 297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.342 123.631 120.179 1.00 56.29  ? 298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 160.847 124.993 120.070 1.00 56.82  ? 298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.444 125.520 121.440 1.00 60.58  ? 298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 160.367 124.779 122.422 1.00 64.04  ? 298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 159.658 125.067 119.109 1.00 54.96  ? 298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.184 126.823 121.493 1.00 51.24  ? 299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 159.809 127.500 122.726 1.00 47.17  ? 299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.575 128.352 122.480 1.00 44.21  ? 299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.528 129.115 121.510 1.00 53.55  ? 299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 160.955 128.373 123.244 1.00 47.06  ? 299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.089 127.596 123.868 1.00 47.12  ? 299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 161.928 126.957 125.088 1.00 50.86  ? 299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.323 127.512 123.244 1.00 51.33  ? 299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 162.963 126.247 125.664 1.00 50.70  ? 299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.364 126.805 123.811 1.00 55.72  ? 299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.178 126.175 125.021 1.00 54.71  ? 299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.213 125.471 125.591 1.00 53.74  ? 299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.582 128.222 123.355 1.00 42.26  ? 300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.434 129.118 123.381 1.00 46.12  ? 300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.653 130.120 124.504 1.00 47.85  ? 300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 156.963 129.738 125.639 1.00 52.53  ? 300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.113 128.348 123.559 1.00 45.57  ? 300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 154.757 127.614 122.281 1.00 45.31  ? 300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.206 127.371 124.721 1.00 48.11  ? 300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 156.509 131.401 124.189 1.00 41.61  ? 301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 156.915 132.467 125.087 1.00 39.14  ? 301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 155.714 133.083 125.790 1.00 45.44  ? 301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 154.602 133.112 125.256 1.00 49.04  ? 301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 157.673 133.551 124.322 1.00 41.19  ? 301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 158.790 133.021 123.474 1.00 43.92  ? 301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 159.997 132.659 124.044 1.00 43.76  ? 301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 158.629 132.878 122.108 1.00 39.52  ? 301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.025 132.167 123.265 1.00 46.22  ? 301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 159.654 132.387 121.325 1.00 43.71  ? 301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 160.853 132.032 121.905 1.00 50.17  ? 301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 155.952 133.574 126.999 1.00 49.04  ? 302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 154.941 134.341 127.710 1.00 49.11  ? 302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 154.952 135.772 127.186 1.00 47.55  ? 302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 155.974 136.456 127.311 1.00 47.18  ? 302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 155.206 134.318 129.209 1.00 45.31  ? 302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 154.938 132.981 129.866 1.00 41.41  ? 302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 155.838 131.932 129.747 1.00 43.88  ? 302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.787 132.770 130.610 1.00 44.96  ? 302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.600 130.713 130.350 1.00 48.18  ? 302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.539 131.554 131.216 1.00 49.00  ? 302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.448 130.529 131.082 1.00 50.58  ? 302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 154.206 129.315 131.682 1.00 47.96  ? 302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 153.859 136.253 126.586 1.00 41.55  ? 303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 153.910 137.564 125.913 1.00 42.41  ? 303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.248 138.726 126.832 1.00 45.17  ? 303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 154.933 139.664 126.404 1.00 51.05  ? 303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 152.499 137.705 125.326 1.00 40.62  ? 303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 151.982 136.316 125.238 1.00 41.42  ? 303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 152.560 135.587 126.405 1.00 34.19  ? 303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 153.789 138.697 128.084 1.00 45.96  ? 304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 153.992 139.850 128.952 1.00 43.51  ? 304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 155.438 139.982 129.402 1.00 45.91  ? 304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 155.911 141.102 129.608 1.00 52.70  ? 304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.070 139.777 130.169 1.00 47.92  ? 304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.077 141.021 131.000 1.00 51.99  ? 304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.613 141.067 132.268 1.00 50.50  ? 304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 152.627 142.270 130.736 1.00 48.43  ? 304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.482 142.288 132.755 1.00 50.74  ? 304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 152.888 143.038 131.845 1.00 50.72  ? 304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 156.154 138.869 129.557 1.00 45.58  ? 305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 157.580 138.957 129.857 1.00 39.88  ? 305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 158.333 139.632 128.718 1.00 46.02  ? 305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.203 140.479 128.951 1.00 55.74  ? 305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 158.149 137.566 130.128 1.00 43.55  ? 305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.230 136.834 128.900 1.00 51.15  ? 305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 157.259 136.813 131.101 1.00 48.27  ? 305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 157.994 139.281 127.475 1.00 46.36  ? 306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 158.611 139.926 126.320 1.00 45.29  ? 306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.243 141.402 126.272 1.00 46.53  ? 306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.084 142.255 125.964 1.00 53.51  ? 306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.205 139.199 125.025 1.00 45.68  ? 306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 158.804 137.795 125.001 1.00 42.35  ? 306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 158.640 139.990 123.802 1.00 50.26  ? 306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.375 136.983 123.818 1.00 43.21  ? 306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 156.983 141.730 126.566 1.00 43.34  ? 307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 156.573 143.131 126.567 1.00 46.45  ? 307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.326 143.927 127.626 1.00 50.48  ? 307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 157.734 145.067 127.384 1.00 53.16  ? 307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.065 143.241 126.786 1.00 42.25  ? 307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 154.530 144.645 126.624 1.00 45.38  ? 307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.223 145.150 125.370 1.00 45.03  ? 307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.337 145.466 127.726 1.00 48.72  ? 307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 153.737 146.433 125.217 1.00 44.87  ? 307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 153.852 146.750 127.582 1.00 51.57  ? 307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 153.554 147.228 126.325 1.00 52.53  ? 307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.069 148.507 126.176 1.00 53.93  ? 307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 157.510 143.343 128.811 1.00 47.92  ? 308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.259 144.018 129.865 1.00 47.44  ? 308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 159.720 144.199 129.475 1.00 50.73  ? 308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.313 145.253 129.729 1.00 53.96  ? 308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.149 143.228 131.168 1.00 50.07  ? 308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 156.795 143.327 131.847 1.00 48.88  ? 308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 156.876 142.873 133.295 1.00 51.83  ? 308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 157.466 141.476 133.403 1.00 51.61  ? 308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 156.424 140.444 133.653 1.00 51.52  ? 308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.319 143.179 128.856 1.00 47.74  ? 309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 161.746 143.236 128.554 1.00 50.32  ? 309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.043 144.178 127.393 1.00 54.83  ? 309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.004 144.955 127.450 1.00 54.67  ? 309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.268 141.834 128.251 1.00 49.58  ? 309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 163.672 141.813 127.678 1.00 58.34  ? 309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 164.735 142.100 128.717 1.00 59.50  ? 309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 164.418 142.052 129.924 1.00 60.92  ? 309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 165.889 142.376 128.329 1.00 53.24  ? 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.235 144.130 126.334 1.00 53.16  ? 310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 161.523 144.851 125.105 1.00 49.98  ? 310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 160.616 146.047 124.863 1.00 48.54  ? 310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 160.884 146.826 123.941 1.00 46.99  ? 310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.424 143.900 123.903 1.00 48.82  ? 310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.468 142.806 123.896 1.00 50.57  ? 310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 163.745 143.042 123.407 1.00 50.92  ? 310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.175 141.539 124.381 1.00 49.45  ? 310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 164.701 142.045 123.400 1.00 52.11  ? 310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.125 140.537 124.379 1.00 49.01  ? 310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.385 140.795 123.888 1.00 52.88  ? 310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.335 139.800 123.883 1.00 53.92  ? 310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 159.558 146.218 125.652 1.00 46.04  ? 311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 158.648 147.323 125.433 1.00 46.32  ? 311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 157.724 147.162 124.251 1.00 46.96  ? 311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.037 148.121 123.886 1.00 51.54  ? 311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 157.682 145.980 123.640 1.00 51.41  ? 312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 156.846 145.734 122.477 1.00 53.06  ? 312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.166 144.382 122.623 1.00 52.11  ? 312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 156.685 143.476 123.280 1.00 55.14  ? 312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 157.662 145.776 121.179 1.00 49.61  ? 312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 156.931 146.402 120.005 1.00 55.63  ? 312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 157.790 146.477 118.761 1.00 61.63  ? 312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 157.278 146.489 117.641 1.00 60.79  ? 312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 159.103 146.526 118.948 1.00 53.23  ? 312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 154.996 144.257 122.002 1.00 44.86  ? 313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.243 143.015 122.068 1.00 44.51  ? 313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 154.939 141.916 121.275 1.00 49.52  ? 313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 155.723 142.178 120.360 1.00 53.93  ? 313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 152.824 143.223 121.541 1.00 41.57  ? 313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 151.972 144.080 122.425 1.00 47.42  ? 313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 151.458 143.632 123.621 1.00 49.63  ? 313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 151.545 145.357 122.284 1.00 45.05  ? 313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 150.750 144.596 124.182 1.00 46.76  ? 313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 150.787 145.654 123.391 1.00 46.04  ? 313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 154.642 140.667 121.643 1.00 49.35  ? 314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 155.279 139.524 120.996 1.00 48.33  ? 314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 154.947 139.461 119.510 1.00 52.70  ? 314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 155.813 139.138 118.688 1.00 56.37  ? 314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 154.860 138.231 121.695 1.00 53.32  ? 314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 155.750 137.038 121.396 1.00 46.89  ? 314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 154.844 135.480 121.371 1.00 56.39  ? 314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 153.399 135.938 120.419 1.00 50.12  ? 314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 153.705 139.766 119.143 1.00 44.69  ? 315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.264 139.672 117.757 1.00 44.89  ? 315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 153.603 140.905 116.923 1.00 50.95  ? 315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.398 140.879 115.705 1.00 58.40  ? 315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 151.757 139.398 117.701 1.00 44.85  ? 315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 150.956 140.362 118.546 1.00 48.85  ? 315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 151.559 141.045 119.399 1.00 48.42  ? 315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 149.725 140.440 118.354 1.00 48.23  ? 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.110 141.976 117.536 1.00 43.19  ? 316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.645 143.107 116.787 1.00 48.14  ? 316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.113 142.949 116.418 1.00 53.55  ? 316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.659 143.825 115.739 1.00 54.18  ? 316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.470 144.415 117.571 1.00 47.78  ? 316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.190 145.212 117.291 1.00 50.51  ? 316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 151.888 144.471 117.544 1.00 54.35  ? 316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.905 143.286 117.929 1.00 51.25  ? 316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 150.827 145.107 117.382 1.00 58.64  ? 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 156.763 141.872 116.841 1.00 52.50  ? 317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.175 141.658 116.562 1.00 53.88  ? 317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.351 140.472 115.626 1.00 54.46  ? 317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.673 139.449 115.767 1.00 49.58  ? 317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 158.954 141.428 117.857 1.00 54.88  ? 317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 158.552 142.364 118.982 1.00 52.46  ? 317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 159.498 142.123 120.493 1.00 53.64  ? 317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 160.637 143.498 120.389 1.00 54.32  ? 317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.264 140.617 114.667 1.00 58.61  ? 318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 159.557 139.551 113.717 1.00 58.95  ? 318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.150 138.352 114.441 1.00 57.28  ? 318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.287 138.408 114.919 1.00 57.68  ? 318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 160.513 140.043 112.629 1.00 58.63  ? 318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 160.119 139.565 111.246 1.00 63.51  ? 318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 159.946 138.341 111.064 1.00 62.91  ? 318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 159.986 140.412 110.339 1.00 62.11  ? 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 159.384 137.262 114.532 1.00 51.99  ? 319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 159.858 136.095 115.266 1.00 46.47  ? 319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.028 135.422 114.559 1.00 49.41  ? 319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 161.888 134.835 115.221 1.00 53.87  ? 319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 158.716 135.104 115.476 1.00 48.02  ? 319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.085 133.920 116.351 1.00 51.04  ? 319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 158.927 134.263 118.114 1.00 56.09  ? 319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 157.441 135.260 118.135 1.00 52.76  ? 319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.092 135.518 113.229 1.00 59.20  ? 320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.222 134.944 112.505 1.00 59.42  ? 320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 163.536 135.596 112.912 1.00 56.08  ? 320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 164.600 134.982 112.784 1.00 57.03  ? 320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.008 135.081 110.999 1.00 55.59  ? 320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 160.830 134.272 110.503 1.00 57.79  ? 320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 159.785 134.213 111.149 1.00 57.02  ? 320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.995 133.638 109.348 1.00 59.67  ? 320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 163.482 136.834 113.399 1.00 56.09  ? 321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 164.659 137.553 113.866 1.00 55.81  ? 321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 164.807 137.530 115.381 1.00 57.86  ? 321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 165.928 137.430 115.887 1.00 56.98  ? 321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 164.608 139.007 113.383 1.00 55.71  ? 321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 165.750 139.875 113.883 1.00 61.65  ? 321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 165.271 141.207 114.427 1.00 64.39  ? 321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.046 141.447 114.420 1.00 61.03  ? 321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 166.120 142.013 114.864 1.00 60.61  ? 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 163.701 137.607 116.117 1.00 56.90  ? 322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 163.741 137.773 117.563 1.00 53.17  ? 322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 163.516 136.480 118.336 1.00 54.44  ? 322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 163.509 136.514 119.568 1.00 61.15  ? 322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 162.707 138.816 117.998 1.00 52.09  ? 322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.135 140.247 117.726 1.00 59.52  ? 322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 163.492 141.179 119.225 1.00 69.90  ? 322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 163.693 142.826 118.551 1.00 60.30  ? 322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 163.338 135.345 117.657 1.00 47.97  ? 323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.146 134.087 118.372 1.00 44.70  ? 323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 164.387 133.724 119.176 1.00 48.75  ? 323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 164.294 133.341 120.348 1.00 53.08  ? 323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 162.790 132.972 117.389 1.00 51.91  ? 323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 162.709 131.597 118.018 1.00 49.90  ? 323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 161.537 131.153 118.613 1.00 46.38  ? 323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 163.803 130.742 118.009 1.00 50.11  ? 323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 161.459 129.901 119.189 1.00 44.79  ? 323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 163.733 129.488 118.581 1.00 48.82  ? 323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.559 129.073 119.169 1.00 50.01  ? 323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.488 127.825 119.738 1.00 50.76  ? 323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 165.564 133.847 118.560 1.00 55.34  ? 324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 166.805 133.563 119.272 1.00 54.77  ? 324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.013 134.540 120.420 1.00 55.87  ? 324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 167.451 134.148 121.509 1.00 58.95  ? 324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 167.985 133.608 118.304 1.00 56.09  ? 324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 167.861 132.592 117.187 1.00 61.68  ? 324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 167.478 131.438 117.473 1.00 60.57  ? 324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.141 132.947 116.022 1.00 61.87  ? 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 166.698 135.818 120.198 1.00 51.66  ? 325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 166.833 136.810 121.259 1.00 47.22  ? 325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 165.927 136.478 122.438 1.00 51.55  ? 325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 166.330 136.617 123.598 1.00 59.23  ? 325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 166.521 138.203 120.716 1.00 52.89  ? 325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 167.287 138.559 119.455 1.00 52.78  ? 325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 167.303 140.059 119.223 1.00 53.42  ? 325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.621 140.505 118.615 1.00 52.71  ? 325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 169.769 139.729 119.159 1.00 50.36  ? 325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 164.697 136.043 122.159 1.00 50.93  ? 326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 163.800 135.618 123.228 1.00 49.74  ? 326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 164.343 134.390 123.948 1.00 52.17  ? 326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.262 134.295 125.178 1.00 54.54  ? 326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 162.408 135.327 122.668 1.00 51.57  ? 326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 161.730 136.519 122.057 1.00 49.99  ? 326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.096 137.805 122.411 1.00 52.70  ? 326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 160.720 136.349 121.125 1.00 46.76  ? 326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 161.470 138.898 121.846 1.00 56.62  ? 326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.091 137.438 120.557 1.00 48.50  ? 326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 160.466 138.713 120.919 1.00 55.17  ? 326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 164.894 133.434 123.196 1.00 56.07  ? 327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 165.345 132.181 123.796 1.00 55.65  ? 327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 166.541 132.414 124.712 1.00 60.15  ? 327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 166.583 131.906 125.839 1.00 64.49  ? 327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 165.660 131.148 122.700 1.00 53.38  ? 327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 166.440 129.979 123.277 1.00 54.37  ? 327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 164.376 130.660 122.057 1.00 49.32  ? 327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 167.526 133.188 124.257 1.00 57.33  ? 328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 168.695 133.463 125.085 1.00 58.25  ? 328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 168.476 134.605 126.069 1.00 59.22  ? 328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.454 135.126 126.613 1.00 62.41  ? 328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 169.919 133.763 124.212 1.00 60.59  ? 328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 169.940 132.953 122.931 1.00 63.26  ? 328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 169.886 131.708 123.013 1.00 62.56  ? 328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 170.045 133.558 121.844 1.00 62.05  ? 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 167.229 135.005 126.309 1.00 55.78  ? 329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 166.937 136.065 127.262 1.00 57.27  ? 329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 166.431 135.450 128.560 1.00 57.88  ? 329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 165.329 134.886 128.574 1.00 55.17  ? 329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 165.899 137.018 126.694 1.00 53.42  ? 329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 165.930 138.384 127.350 1.00 54.11  ? 329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 165.379 139.344 126.819 1.00 53.64  ? 329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.577 138.479 128.503 1.00 62.61  ? 329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 167.189 135.524 129.658 1.00 62.99  ? 330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 166.705 134.931 130.914 1.00 62.85  ? 330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 165.482 135.627 131.483 1.00 64.78  ? 330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 164.735 135.009 132.251 1.00 68.29  ? 330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 167.916 135.059 131.848 1.00 63.54  ? 330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 168.662 136.236 131.322 1.00 61.98  ? 330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 168.491 136.193 129.827 1.00 61.73  ? 330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 165.250 136.890 131.132 1.00 54.42  ? 331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.087 137.615 131.627 1.00 55.21  ? 331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 162.832 137.347 130.806 1.00 55.88  ? 331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 161.773 137.899 131.125 1.00 55.06  ? 331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 164.380 139.117 131.665 1.00 56.05  ? 331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 165.518 139.489 132.602 1.00 56.81  ? 331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 165.826 140.984 132.560 1.00 56.29  ? 331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 166.449 141.449 131.322 1.00 59.81  ? 331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 167.508 140.911 130.726 1.00 58.33  ? 331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 167.926 141.418 129.569 1.00 59.40  ? 331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 168.175 139.901 131.264 1.00 52.80  ? 331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 162.924 136.526 129.764 1.00 53.36  ? 332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 161.773 136.119 128.966 1.00 50.31  ? 332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 161.393 134.704 129.383 1.00 54.69  ? 332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 162.224 133.789 129.336 1.00 57.71  ? 332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.079 136.193 127.463 1.00 48.36  ? 332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.033 135.431 126.671 1.00 49.40  ? 332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.146 137.641 127.008 1.00 50.09  ? 332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 160.141 134.521 129.795 1.00 54.16  ? 333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.679 133.223 130.269 1.00 47.71  ? 333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 159.139 132.387 129.115 1.00 47.73  ? 333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 158.449 132.896 128.228 1.00 54.63  ? 333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.603 133.396 131.341 1.00 49.14  ? 333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 158.385 132.163 132.201 1.00 51.63  ? 333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.212 132.348 133.150 1.00 52.16  ? 333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 156.934 131.078 133.938 1.00 52.79  ? 333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 155.804 131.253 134.893 1.00 57.06  ? 333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.463 131.095 129.134 1.00 51.59  ? 334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 159.045 130.177 128.085 1.00 53.85  ? 334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 159.115 128.752 128.611 1.00 55.58  ? 334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.692 128.488 129.669 1.00 57.43  ? 334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 159.920 130.321 126.836 1.00 51.31  ? 334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.363 129.903 127.058 1.00 53.31  ? 334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.316 130.655 126.148 1.00 57.26  ? 334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 162.824 131.921 126.809 1.00 53.92  ? 334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 164.105 131.694 127.532 1.00 47.38  ? 334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.509 127.830 127.862 1.00 59.69  ? 335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 158.657 126.402 128.112 1.00 63.64  ? 335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 158.977 125.700 126.801 1.00 59.43  ? 335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.422 126.050 125.755 1.00 58.42  ? 335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.400 125.777 128.727 1.00 61.84  ? 335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.088 126.411 128.315 1.00 63.11  ? 335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 154.930 125.905 129.152 1.00 64.63  ? 335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.123 125.690 130.367 1.00 57.49  ? 335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 153.828 125.714 128.596 1.00 63.13  ? 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 159.868 124.715 126.865 1.00 60.25  ? 336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.203 123.924 125.689 1.00 56.66  ? 336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 158.985 123.159 125.185 1.00 56.95  ? 336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.228 122.577 125.965 1.00 58.89  ? 336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.338 122.954 126.022 1.00 58.75  ? 336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 161.726 122.016 124.892 1.00 61.35  ? 336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 161.262 120.597 125.190 1.00 61.47  ? 336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 161.706 119.619 124.116 1.00 62.02  ? 336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 160.749 118.488 123.973 1.00 60.25  ? 336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 158.795 123.172 123.864 1.00 55.28  ? 337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 157.765 122.382 123.204 1.00 60.60  ? 337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 158.394 121.668 122.014 1.00 62.84  ? 337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 159.538 121.924 121.637 1.00 62.09  ? 337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 156.563 123.231 122.740 1.00 54.90  ? 337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.004 124.257 121.695 1.00 56.07  ? 337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 155.888 123.903 123.924 1.00 57.36  ? 337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 155.957 124.546 120.646 1.00 56.36  ? 337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 157.622 120.762 121.424 1.00 60.63  ? 338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.041 120.059 120.217 1.00 59.39  ? 338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 157.272 120.614 119.028 1.00 58.29  ? 338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.055 120.395 118.931 1.00 61.39  ? 338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 157.802 118.555 120.355 1.00 58.87  ? 338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 158.622 117.740 119.376 1.00 59.93  ? 338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 158.616 118.001 118.174 1.00 62.43  ? 338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 159.331 116.741 119.887 1.00 60.53  ? 338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 157.919 121.342 118.115 1.00 51.83  ? 339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.178 121.918 116.981 1.00 53.63  ? 339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 156.522 120.879 116.090 1.00 54.73  ? 339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 155.430 121.128 115.567 1.00 55.99  ? 339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.254 122.713 116.229 1.00 50.50  ? 339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 159.538 122.073 116.617 1.00 54.07  ? 339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 159.363 121.615 118.032 1.00 50.72  ? 339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 157.152 119.718 115.900 1.00 54.45  ? 340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 156.530 118.672 115.094 1.00 50.36  ? 340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 155.334 118.062 115.812 1.00 53.60  ? 340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 154.323 117.734 115.182 1.00 56.66  ? 340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 157.557 117.599 114.739 1.00 51.42  ? 340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 158.414 117.958 113.544 1.00 50.52  ? 340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 159.302 116.805 113.117 1.00 50.38  ? 340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 160.059 117.136 111.917 1.00 53.48  ? 340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.062 116.413 111.439 1.00 56.22  ? 340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.689 116.822 110.341 1.00 56.95  ? 340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 161.454 115.297 112.031 1.00 54.64  ? 340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 155.428 117.906 117.135 1.00 56.20  ? 341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 154.277 117.444 117.901 1.00 57.12  ? 341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 153.140 118.453 117.836 1.00 56.57  ? 341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 151.967 118.075 117.757 1.00 56.65  ? 341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 154.677 117.175 119.351 1.00 58.56  ? 341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 154.444 115.745 119.802 1.00 59.30  ? 341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 155.414 114.789 119.130 1.00 64.63  ? 341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 155.666 113.562 119.990 1.00 61.80  ? 341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 156.958 112.904 119.653 1.00 57.83  ? 341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 153.466 119.747 117.861 1.00 51.88  ? 342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 152.431 120.769 117.732 1.00 49.92  ? 342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 151.810 120.756 116.340 1.00 50.87  ? 342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 150.602 120.967 116.192 1.00 54.91  ? 342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.008 122.146 118.057 1.00 47.62  ? 342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 151.996 123.268 118.294 1.00 49.82  ? 342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 150.856 122.787 119.174 1.00 47.97  ? 342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 152.675 124.474 118.915 1.00 53.49  ? 342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 152.617 120.506 115.306 1.00 47.74  ? 343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.073 120.384 113.956 1.00 44.81  ? 343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.146 119.179 113.842 1.00 50.71  ? 343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.085 119.258 113.212 1.00 55.42  ? 343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 153.209 120.281 112.940 1.00 49.70  ? 343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 153.642 121.580 112.260 1.00 51.32  ? 343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 154.665 121.293 111.175 1.00 49.07  ? 343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 152.440 122.312 111.689 1.00 48.88  ? 343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 151.536 118.052 114.439 1.00 53.17  ? 344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 150.671 116.876 114.438 1.00 50.18  ? 344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 149.390 117.136 115.221 1.00 52.05  ? 344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 148.313 116.660 114.843 1.00 57.13  ? 344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 151.421 115.675 115.012 1.00 54.48  ? 344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 152.163 114.856 113.968 1.00 54.94  ? 344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 153.554 114.460 114.420 1.00 60.13  ? 344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 153.721 114.124 115.611 1.00 60.52  ? 344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 154.481 114.486 113.584 1.00 57.23  ? 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 149.490 117.884 116.323 1.00 46.26  ? 345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 148.299 118.261 117.075 1.00 49.20  ? 345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 147.376 119.133 116.236 1.00 50.82  ? 345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 146.154 118.953 116.256 1.00 56.04  ? 345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 148.699 118.982 118.362 1.00 45.54  ? 345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 147.529 119.374 119.246 1.00 44.89  ? 345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 147.964 120.322 120.349 1.00 49.33  ? 345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 146.939 120.370 121.469 1.00 52.67  ? 345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 145.549 120.402 120.943 1.00 55.89  ? 345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 147.946 120.076 115.485 1.00 44.59  ? 346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.149 120.888 114.572 1.00 41.14  ? 346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 146.455 120.016 113.536 1.00 46.89  ? 346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 145.263 120.186 113.257 1.00 50.01  ? 346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.036 121.924 113.880 1.00 41.85  ? 346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 148.652 123.054 114.701 1.00 45.02  ? 346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 149.684 123.787 113.869 1.00 46.42  ? 346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 147.581 124.009 115.171 1.00 45.34  ? 346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.195 119.067 112.956 1.00 45.14  ? 347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 146.625 118.213 111.920 1.00 40.46  ? 347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 145.486 117.362 112.466 1.00 50.44  ? 347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 144.435 117.236 111.826 1.00 54.82  ? 347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 147.711 117.328 111.312 1.00 41.93  ? 347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 145.665 116.782 113.654 1.00 51.19  ? 348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 144.604 115.947 114.209 1.00 50.05  ? 348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 143.419 116.785 114.675 1.00 53.93  ? 348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 142.273 116.335 114.572 1.00 54.64  ? 348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 145.142 115.069 115.344 1.00 50.95  ? 348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 144.752 115.495 116.750 1.00 55.08  ? 348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.432 114.396 118.011 1.00 69.17  ? 348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.010 115.171 118.350 1.00 54.37  ? 348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 143.663 118.006 115.157 1.00 46.48  ? 349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 142.558 118.886 115.518 1.00 42.39  ? 349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 141.744 119.274 114.292 1.00 39.92  ? 349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 140.510 119.328 114.351 1.00 37.93  ? 349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.095 120.129 116.228 1.00 42.84  ? 349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.249 120.689 117.372 1.00 43.75  ? 349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.653 120.051 118.689 1.00 45.48  ? 349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 142.378 122.200 117.443 1.00 44.07  ? 349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 142.416 119.545 113.169 1.00 40.65  ? 350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 141.697 119.863 111.940 1.00 41.75  ? 350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 140.975 118.645 111.379 1.00 48.62  ? 350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 139.896 118.782 110.793 1.00 51.02  ? 350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 142.655 120.443 110.899 1.00 40.93  ? 350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 143.380 121.695 111.359 1.00 44.36  ? 350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.091 122.389 110.212 1.00 42.34  ? 350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 143.217 123.341 109.538 1.00 44.36  ? 350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.190 123.535 108.227 1.00 45.43  ? 350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 142.350 124.436 107.723 1.00 46.95  ? 350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.976 122.853 107.411 1.00 44.49  ? 350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 141.554 117.453 111.533 1.00 49.57  ? 351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 140.856 116.243 111.116 1.00 49.85  ? 351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 139.601 116.016 111.950 1.00 50.75  ? 351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 138.548 115.649 111.416 1.00 58.04  ? 351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 141.791 115.039 111.214 1.00 52.52  ? 351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 142.916 115.198 110.368 1.00 54.17  ? 351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 139.693 116.233 113.264 1.00 52.67  ? 352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 138.569 115.956 114.151 1.00 51.84  ? 352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 137.467 117.003 114.035 1.00 52.54  ? 352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 136.281 116.655 114.029 1.00 56.31  ? 352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.060 115.861 115.596 1.00 56.46  ? 352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 139.858 114.605 115.900 1.00 58.96  ? 352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.574 114.679 117.235 1.00 60.31  ? 352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 140.498 115.737 117.894 1.00 56.59  ? 352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 141.213 113.679 117.623 1.00 61.96  ? 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 137.827 118.285 113.946 1.00 53.72  ? 353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 136.838 119.353 113.996 1.00 52.97  ? 353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 136.973 120.407 112.905 1.00 47.41  ? 353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.102 121.279 112.816 1.00 47.75  ? 353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 136.885 120.059 115.360 1.00 51.45  ? 353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 138.119 120.727 115.546 1.00 49.41  ? 353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.016 120.363 112.082 1.00 42.98  ? 354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.222 121.379 111.071 1.00 38.89  ? 354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 138.927 122.626 111.553 1.00 41.57  ? 354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.197 123.518 110.739 1.00 43.87  ? 354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 139.237 122.716 112.841 1.00 43.21  ? 355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 139.925 123.834 113.458 1.00 38.39  ? 355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 141.344 123.428 113.842 1.00 39.09  ? 355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 141.609 122.250 114.089 1.00 45.41  ? 355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.175 124.309 114.708 1.00 40.64  ? 355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 137.839 124.946 114.410 1.00 39.49  ? 355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 137.745 126.040 113.564 1.00 34.95  ? 355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 136.672 124.451 114.973 1.00 48.30  ? 355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 136.527 126.624 113.287 1.00 40.49  ? 355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 135.449 125.029 114.702 1.00 48.97  ? 355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 135.382 126.115 113.859 1.00 44.91  ? 355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.165 126.696 113.586 1.00 44.69  ? 355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.283 124.377 113.919 1.00 33.57  ? 356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.155 125.824 113.715 1.00 34.79  ? 356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.367 126.272 112.277 1.00 34.98  ? 356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 142.835 125.509 111.438 1.00 39.53  ? 356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.260 126.376 114.615 1.00 37.74  ? 356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.348 125.358 114.456 1.00 33.05  ? 356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 143.639 124.026 114.377 1.00 26.62  ? 356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.023 127.519 111.972 1.00 31.93  ? 357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.490 128.133 110.739 1.00 23.70  ? 357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 143.993 128.356 110.830 1.00 32.91  ? 357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.503 128.847 111.842 1.00 41.83  ? 357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 141.778 129.464 110.489 1.00 27.15  ? 357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.286 129.459 110.753 1.00 23.61  ? 357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 139.514 128.342 110.479 1.00 21.07  ? 357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 139.651 130.579 111.270 1.00 30.12  ? 357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.157 128.333 110.711 1.00 27.98  ? 357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.293 130.581 111.510 1.00 33.41  ? 357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 137.551 129.454 111.227 1.00 35.49  ? 357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.195 129.446 111.458 1.00 37.31  ? 357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 144.708 127.994 109.772 1.00 32.30  ? 358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.162 128.093 109.744 1.00 29.30  ? 358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 146.541 129.329 108.942 1.00 36.03  ? 358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.239 129.420 107.747 1.00 42.98  ? 358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 146.800 126.829 109.149 1.00 31.51  ? 358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.329 125.587 109.906 1.00 36.58  ? 358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.311 126.933 109.187 1.00 33.51  ? 358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 146.735 125.568 111.360 1.00 34.02  ? 358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.203 130.280 109.597 1.00 22.88  ? 359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 147.654 131.515 108.965 1.00 12.88  ? 359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.176 131.519 108.952 1.00 20.19  ? 359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 149.810 131.579 110.010 1.00 36.10  ? 359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.111 132.740 109.698 1.00 17.18  ? 359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 146.943 133.959 108.811 1.00 22.89  ? 359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.035 135.521 109.700 1.00 37.14  ? 359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 148.731 135.987 109.381 1.00 21.96  ? 359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 149.758 131.457 107.759 1.00 26.81  ? 360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.209 131.514 107.601 1.00 20.30  ? 360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 151.615 132.980 107.569 1.00 32.47  ? 360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 151.527 133.638 106.530 1.00 45.01  ? 360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 151.638 130.778 106.338 1.00 23.80  ? 360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.227 129.336 106.315 1.00 36.51  ? 360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 151.691 128.454 107.276 1.00 39.62  ? 360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.367 128.863 105.341 1.00 30.92  ? 360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.311 127.127 107.259 1.00 30.23  ? 360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 149.983 127.540 105.319 1.00 28.68  ? 360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 150.455 126.670 106.279 1.00 31.58  ? 360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.070 133.492 108.715 1.00 29.57  ? 361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.275 134.930 108.867 1.00 31.93  ? 361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.308 135.462 107.884 1.00 37.87  ? 361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.117 136.529 107.290 1.00 42.76  ? 361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 152.691 135.252 110.302 1.00 34.21  ? 361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 152.108 136.547 110.834 1.00 26.87  ? 361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 152.818 137.044 112.073 1.00 38.98  ? 361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.277 136.255 112.898 1.00 41.59  ? 361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.904 138.360 112.218 1.00 41.95  ? 361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 154.413 134.738 107.699 1.00 37.21  ? 362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 155.450 135.221 106.797 1.00 34.19  ? 362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.013 135.139 105.342 1.00 35.39  ? 362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 155.446 135.957 104.523 1.00 45.61  ? 362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 156.744 134.441 107.015 1.00 38.85  ? 362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.401 134.768 108.342 1.00 49.29  ? 362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 156.820 134.431 109.394 1.00 43.51  ? 362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 158.499 135.362 108.332 1.00 51.86  ? 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.164 134.169 104.998 1.00 39.73  ? 363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 153.589 134.139 103.656 1.00 29.56  ? 363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 152.704 135.354 103.417 1.00 25.40  ? 363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 152.678 135.906 102.312 1.00 37.36  ? 363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 152.793 132.850 103.452 1.00 23.09  ? 363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 153.676 131.663 103.142 1.00 24.33  ? 363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 154.874 131.811 102.903 1.00 30.46  ? 363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.088 130.475 103.139 1.00 29.72  ? 363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 151.966 135.777 104.443 1.00 18.85  ? 364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.134 136.970 104.326 1.00 28.75  ? 364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 151.999 138.218 104.217 1.00 34.22  ? 364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 151.769 139.082 103.364 1.00 28.52  ? 364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.168 137.066 105.518 1.00 16.93  ? 364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.234 138.234 105.330 1.00 21.27  ? 364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.393 135.775 105.680 1.00 24.12  ? 364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.004 138.332 105.083 1.00 32.74  ? 365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 153.798 139.547 105.192 1.00 20.64  ? 365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 154.933 139.623 104.180 1.00 28.27  ? 365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.549 140.684 104.046 1.00 35.21  ? 365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.366 139.672 106.608 1.00 21.90  ? 365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.281 139.745 107.662 1.00 24.83  ? 365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.471 140.671 107.673 1.00 25.36  ? 365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.258 138.764 108.555 1.00 28.38  ? 365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.226 138.530 103.472 1.00 32.58  ? 366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.242 138.584 102.426 1.00 32.02  ? 366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 155.797 139.475 101.275 1.00 37.67  ? 366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 156.621 140.156 100.653 1.00 36.27  ? 366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 156.554 137.175 101.926 1.00 33.41  ? 366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 157.705 137.094 100.937 1.00 39.73  ? 366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.672 135.800 100.129 1.00 44.54  ? 366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 157.070 134.642 100.917 1.00 39.40  ? 366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 157.906 134.252 102.086 1.00 34.85  ? 366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 154.500 139.486 100.981 1.00 37.37  ? 367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 153.939 140.280 99.899  1.00 30.32  ? 367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 152.895 141.269 100.415 1.00 30.34  ? 367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.073 141.759 99.649  1.00 36.14  ? 367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.353 139.376 98.798  1.00 29.36  ? 367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.470 138.724 98.001  1.00 30.39  ? 367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.454 138.320 99.411  1.00 24.15  ? 367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 152.919 141.565 101.712 1.00 26.05  ? 368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 151.995 142.532 102.290 1.00 15.37  ? 368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.467 143.940 101.954 1.00 21.56  ? 368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 153.609 144.307 102.249 1.00 31.52  ? 368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 151.892 142.341 103.801 1.00 21.23  ? 368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 150.945 143.289 104.465 1.00 17.75  ? 368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.154 143.783 105.733 1.00 21.83  ? 368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 149.783 143.835 104.036 1.00 20.53  ? 368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.163 144.593 106.058 1.00 22.13  ? 368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.317 144.641 105.045 1.00 23.77  ? 368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.587 144.726 101.337 1.00 22.93  ? 369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 151.952 146.059 100.878 1.00 24.95  ? 369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.053 147.075 102.007 1.00 32.14  ? 369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.797 148.052 101.874 1.00 39.74  ? 369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 150.941 146.548 99.842  1.00 28.63  ? 369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.339 146.869 103.108 1.00 30.55  ? 370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.226 147.855 104.176 1.00 26.04  ? 370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 151.921 147.392 105.452 1.00 27.79  ? 370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.402 147.563 106.556 1.00 38.51  ? 370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 149.761 148.179 104.450 1.00 24.77  ? 370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.038 148.685 103.217 1.00 27.53  ? 370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.470 149.646 102.584 1.00 42.47  ? 370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 147.935 148.035 102.868 1.00 26.03  ? 370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.105 146.791 105.312 1.00 24.97  ? 371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 153.881 146.391 106.479 1.00 25.12  ? 371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.326 147.583 107.315 1.00 27.68  ? 371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 154.561 147.428 108.518 1.00 23.32  ? 371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.104 145.580 106.049 1.00 20.88  ? 371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 154.792 144.112 105.861 1.00 27.47  ? 371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 153.840 143.589 106.437 1.00 29.37  ? 371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.598 143.436 105.052 1.00 26.24  ? 371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.455 148.763 106.704 1.00 38.99  ? 372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 154.814 149.955 107.465 1.00 35.06  ? 372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 153.725 150.318 108.467 1.00 35.57  ? 372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.023 150.707 109.602 1.00 35.89  ? 372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.080 151.121 106.513 1.00 30.59  ? 372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 153.861 151.593 105.787 1.00 34.48  ? 372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.175 150.802 104.892 1.00 35.33  ? 372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.198 152.773 105.832 1.00 36.95  ? 372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.143 151.473 104.415 1.00 35.70  ? 372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.136 152.672 104.967 1.00 40.14  ? 372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.458 150.208 108.062 1.00 32.39  ? 373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.355 150.447 108.990 1.00 34.02  ? 373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.377 149.413 110.103 1.00 36.92  ? 373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 151.358 149.748 111.293 1.00 43.02  ? 373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.012 150.432 108.239 1.00 25.32  ? 373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 149.957 151.564 107.214 1.00 29.91  ? 373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 148.853 150.530 109.215 1.00 29.32  ? 373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 148.760 151.496 106.298 1.00 32.87  ? 373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.439 148.136 109.725 1.00 22.05  ? 374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 151.522 147.019 110.654 1.00 21.72  ? 374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 151.683 145.725 109.871 1.00 32.62  ? 374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.253 145.637 108.718 1.00 33.80  ? 374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.279 146.944 111.542 1.00 34.79  ? 374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 150.003 145.607 111.918 1.00 30.91  ? 374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.303 144.722 110.476 1.00 36.02  ? 375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.299 143.397 109.883 1.00 20.46  ? 375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 150.967 142.715 110.164 1.00 25.57  ? 375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.300 142.998 111.162 1.00 32.14  ? 375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.457 142.558 110.423 1.00 21.71  ? 375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 154.688 142.575 109.532 1.00 29.02  ? 375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 155.966 142.574 110.348 1.00 36.07  ? 375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.193 142.561 109.450 1.00 32.70  ? 375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 157.182 141.406 108.511 1.00 32.79  ? 375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.575 141.817 109.266 1.00 29.54  ? 376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.309 141.104 109.407 1.00 24.73  ? 376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.485 140.048 110.491 1.00 24.26  ? 376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.182 139.051 110.295 1.00 33.28  ? 376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 148.864 140.475 108.084 1.00 22.14  ? 376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.509 139.811 108.249 1.00 29.21  ? 376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 148.817 141.524 106.990 1.00 13.12  ? 376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 148.851 140.267 111.641 1.00 23.44  ? 377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.004 139.376 112.780 1.00 18.92  ? 377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 147.922 138.312 112.860 1.00 24.47  ? 377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.130 137.289 113.521 1.00 32.91  ? 377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.007 140.181 114.083 1.00 31.77  ? 377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.080 141.250 114.147 1.00 33.89  ? 377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.546 142.516 114.785 1.00 24.82  ? 377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.425 143.706 114.460 1.00 32.39  ? 377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.769 144.991 114.823 1.00 37.61  ? 377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 146.781 138.522 112.212 1.00 26.90  ? 378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 145.669 137.588 112.310 1.00 9.20   ? 378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 144.722 137.812 111.143 1.00 14.36  ? 378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 144.785 138.832 110.452 1.00 21.46  ? 378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 144.932 137.729 113.648 1.00 12.66  ? 378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.137 138.998 113.784 1.00 16.08  ? 378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 144.731 140.237 113.605 1.00 20.12  ? 378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 142.796 138.951 114.115 1.00 14.45  ? 378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.002 141.395 113.738 1.00 16.21  ? 378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.064 140.109 114.251 1.00 21.65  ? 378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 142.668 141.332 114.063 1.00 17.40  ? 378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 143.844 136.839 110.931 1.00 17.25  ? 379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 142.868 136.857 109.853 1.00 1.83   ? 379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 141.459 136.929 110.434 1.00 11.86  ? 379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.264 137.044 111.645 1.00 28.06  ? 379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.028 135.631 108.951 1.00 12.93  ? 379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 142.439 135.857 107.684 1.00 30.00  ? 379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.469 136.861 109.549 1.00 16.09  ? 380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.076 137.024 109.932 1.00 21.01  ? 380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.447 135.667 110.248 1.00 33.28  ? 380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.127 134.642 110.343 1.00 38.03  ? 380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.309 137.756 108.834 1.00 18.61  ? 380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.281 136.988 107.533 1.00 21.63  ? 380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.289 136.431 107.108 1.00 34.31  ? 380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.120 136.954 106.892 1.00 24.53  ? 380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.123 135.659 110.420 1.00 34.03  ? 381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.405 134.425 110.716 1.00 32.24  ? 381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.424 133.463 109.535 1.00 27.90  ? 381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.406 132.243 109.731 1.00 36.08  ? 381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 134.969 134.751 111.123 1.00 27.81  ? 381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 133.988 133.603 111.361 1.00 33.57  ? 381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.394 132.774 112.566 1.00 32.27  ? 381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 132.582 134.149 111.529 1.00 34.66  ? 381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.464 133.984 108.312 1.00 29.71  ? 382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 136.534 133.161 107.114 1.00 18.44  ? 382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 137.968 132.898 106.677 1.00 22.94  ? 382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.181 132.246 105.651 1.00 31.15  ? 382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 135.749 133.818 105.978 1.00 31.16  ? 382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 133.972 133.951 106.278 1.00 38.20  ? 382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 138.947 133.392 107.436 1.00 25.78  ? 383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.365 133.133 107.184 1.00 17.84  ? 383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 140.778 133.559 105.777 1.00 25.71  ? 383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 141.495 132.842 105.079 1.00 36.10  ? 383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 140.706 131.662 107.429 1.00 31.38  ? 383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.105 131.476 107.545 1.00 40.59  ? 383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.311 134.730 105.348 1.00 24.06  ? 384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 140.671 135.262 104.039 1.00 19.14  ? 384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.020 136.742 104.032 1.00 24.26  ? 384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 141.535 137.223 103.017 1.00 42.46  ? 384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 139.548 134.994 103.021 1.00 23.03  ? 384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 138.120 135.210 103.521 1.00 30.31  ? 384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 137.739 136.667 103.677 1.00 32.79  ? 384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.427 137.530 103.101 1.00 31.29  ? 384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 136.745 136.949 104.378 1.00 31.87  ? 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 140.759 137.479 105.106 1.00 21.27  ? 385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.133 138.887 105.192 1.00 13.80  ? 385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.470 138.995 105.909 1.00 22.49  ? 385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 142.641 138.465 107.011 1.00 36.86  ? 385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.053 139.710 105.905 1.00 11.38  ? 385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.655 140.968 106.488 1.00 10.58  ? 385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 138.978 140.082 104.923 1.00 23.36  ? 385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.421 139.680 105.277 1.00 23.20  ? 386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 144.781 139.830 105.789 1.00 11.99  ? 386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.179 141.294 105.636 1.00 18.10  ? 386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.681 141.707 104.588 1.00 10.34  ? 386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 145.730 138.903 105.055 1.00 7.75   ? 386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.386 137.426 105.223 1.00 7.13   ? 386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.214 136.596 104.289 1.00 11.86  ? 386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.605 136.991 106.660 1.00 23.27  ? 386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 144.955 142.074 106.690 1.00 26.62  ? 387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.172 143.510 106.657 1.00 14.02  ? 387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 145.976 143.947 107.872 1.00 23.71  ? 387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 145.991 143.283 108.911 1.00 35.18  ? 387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 143.842 144.267 106.611 1.00 12.85  ? 387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 142.942 143.851 105.468 1.00 20.73  ? 387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 141.815 144.825 105.244 1.00 20.78  ? 387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 141.808 145.915 105.809 1.00 32.66  ? 387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 140.850 144.439 104.419 1.00 17.54  ? 387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 146.656 145.081 107.721 1.00 19.40  ? 388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.403 145.661 108.826 1.00 21.00  ? 388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.452 146.166 109.903 1.00 28.28  ? 388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.438 146.806 109.609 1.00 34.04  ? 388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.286 146.803 108.330 1.00 27.59  ? 388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 146.788 145.880 111.157 1.00 24.00  ? 389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 145.971 146.296 112.286 1.00 20.71  ? 389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 146.866 146.833 113.388 1.00 25.15  ? 389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 147.949 146.295 113.638 1.00 38.63  ? 389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.122 145.137 112.820 1.00 30.46  ? 389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 145.931 144.014 113.121 1.00 34.17  ? 389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.405 147.890 114.047 1.00 29.44  ? 390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.096 148.481 115.183 1.00 29.77  ? 390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.219 148.319 116.414 1.00 33.00  ? 390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.019 148.607 116.366 1.00 38.15  ? 390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.406 149.959 114.938 1.00 29.07  ? 390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.391 150.206 113.811 1.00 29.82  ? 390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 148.624 151.680 113.557 1.00 35.71  ? 390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 147.973 152.536 114.157 1.00 33.78  ? 390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 149.556 151.986 112.662 1.00 29.56  ? 390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 146.815 147.850 117.510 1.00 38.54  ? 391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.045 147.614 118.722 1.00 37.17  ? 391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.585 148.942 119.310 1.00 46.52  ? 391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.233 149.986 119.149 1.00 36.41  ? 391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 146.859 146.799 119.743 1.00 32.09  ? 391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 147.815 147.695 120.516 1.00 33.76  ? 391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 145.929 146.063 120.691 1.00 32.65  ? 391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.439 148.907 119.982 1.00 48.12  ? 392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 143.879 150.071 120.649 1.00 35.19  ? 392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.087 149.928 122.147 1.00 44.38  ? 392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 143.714 148.908 122.736 1.00 50.91  ? 392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.390 150.225 120.334 1.00 36.41  ? 392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.170 150.288 118.939 1.00 40.25  ? 392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.685 150.946 122.759 1.00 48.57  ? 393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 144.902 150.964 124.201 1.00 46.29  ? 393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.692 151.625 124.845 1.00 48.67  ? 393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.657 152.845 125.024 1.00 51.40  ? 393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.194 151.695 124.545 1.00 54.05  ? 393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.391 151.751 125.947 1.00 55.50  ? 393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.693 150.818 125.190 1.00 45.12  ? 394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.493 151.321 125.850 1.00 42.82  ? 394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 141.810 151.525 127.325 1.00 47.49  ? 394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.042 150.560 128.059 1.00 49.71  ? 394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.329 150.354 125.658 1.00 43.13  ? 394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 139.920 150.158 124.215 1.00 42.85  ? 394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.327 151.187 123.495 1.00 41.88  ? 394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.132 148.948 123.572 1.00 43.06  ? 394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.953 151.012 122.177 1.00 44.00  ? 394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 139.761 148.764 122.256 1.00 43.08  ? 394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.173 149.799 121.562 1.00 48.99  ? 394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.804 149.616 120.249 1.00 53.38  ? 394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.823 152.780 127.755 1.00 51.08  ? 395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.212 153.145 129.107 1.00 52.75  ? 395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 140.998 153.141 130.023 1.00 55.82  ? 395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 139.870 152.901 129.580 1.00 48.44  ? 395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 142.875 154.522 129.127 1.00 50.86  ? 395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 141.888 155.531 128.880 1.00 54.84  ? 395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 143.951 154.604 128.059 1.00 49.58  ? 395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.241 153.391 131.308 1.00 55.34  ? 396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.175 153.495 132.295 1.00 49.97  ? 396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.179 154.585 131.914 1.00 50.39  ? 396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.478 155.437 131.070 1.00 55.74  ? 396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.765 153.771 133.679 1.00 50.16  ? 396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.832 152.763 134.068 1.00 56.17  ? 396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 142.904 152.754 133.426 1.00 58.30  ? 396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 141.601 151.982 135.013 1.00 51.38  ? 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 137.988 154.549 132.512 1.00 48.18  ? 397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.978 155.578 132.294 1.00 46.83  ? 397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.545 156.962 132.586 1.00 48.74  ? 397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 138.597 157.094 133.216 1.00 52.92  ? 397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.750 155.285 133.166 1.00 48.35  ? 397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.487 156.024 132.768 1.00 49.77  ? 397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 134.223 157.303 133.242 1.00 49.14  ? 397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 133.572 155.449 131.895 1.00 46.43  ? 397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 133.079 157.979 132.877 1.00 46.85  ? 397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 132.425 156.121 131.522 1.00 46.39  ? 397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.184 157.385 132.017 1.00 50.26  ? 397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 131.042 158.053 131.645 1.00 51.26  ? 397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 136.870 157.984 132.040 1.00 54.15  ? 398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 137.241 159.403 132.047 1.00 57.38  ? 398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 138.737 159.600 131.807 1.00 56.19  ? 398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.341 160.569 132.281 1.00 52.95  ? 398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 136.741 160.133 133.315 1.00 56.74  ? 398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 137.592 159.897 134.554 1.00 58.91  ? 398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 137.924 158.750 134.876 1.00 56.66  ? 398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 137.857 160.880 135.277 1.00 53.68  ? 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 139.328 158.689 131.036 1.00 59.08  ? 399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 140.675 158.828 130.506 1.00 55.57  ? 399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.619 158.588 129.006 1.00 56.51  ? 399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.909 157.689 128.544 1.00 55.05  ? 399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 141.648 157.842 131.165 1.00 54.99  ? 399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.573 158.459 132.199 1.00 58.24  ? 399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.627 157.480 132.677 1.00 61.15  ? 399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 143.679 156.359 132.131 1.00 61.27  ? 399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.403 157.829 133.592 1.00 60.16  ? 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.355 159.397 128.247 1.00 57.34  ? 400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.321 159.283 126.794 1.00 59.37  ? 400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.948 157.968 126.347 1.00 60.78  ? 400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.029 157.593 126.811 1.00 59.28  ? 400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 142.046 160.463 126.149 1.00 57.31  ? 400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.392 160.963 124.867 1.00 61.05  ? 400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 139.981 161.470 125.090 1.00 63.45  ? 400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 139.761 162.189 126.088 1.00 61.86  ? 400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.092 161.149 124.273 1.00 60.98  ? 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.266 157.269 125.446 1.00 54.45  ? 401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.745 155.997 124.929 1.00 50.67  ? 401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.594 156.207 123.683 1.00 54.99  ? 401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.355 157.118 122.887 1.00 55.91  ? 401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.579 155.064 124.600 1.00 50.86  ? 401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.523 155.042 125.683 1.00 59.36  ? 401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 139.889 154.974 126.874 1.00 62.18  ? 401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.323 155.088 125.341 1.00 55.32  ? 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.594 155.344 123.520 1.00 56.65  ? 402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.436 155.332 122.329 1.00 51.08  ? 402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.805 154.387 121.312 1.00 51.73  ? 402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 143.859 153.165 121.474 1.00 59.53  ? 402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.859 154.904 122.675 1.00 50.35  ? 402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.653 155.954 123.432 1.00 54.11  ? 402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 146.626 155.742 124.933 1.00 58.93  ? 402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 147.158 154.711 125.397 1.00 55.86  ? 402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.070 156.601 125.648 1.00 57.12  ? 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.210 154.951 120.269 1.00 37.92  ? 403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.452 154.181 119.290 1.00 39.80  ? 403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.384 153.719 118.180 1.00 45.52  ? 403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.105 154.526 117.582 1.00 47.64  ? 403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.288 155.010 118.725 1.00 37.70  ? 403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.275 155.323 119.828 1.00 42.64  ? 403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.618 154.278 117.579 1.00 40.57  ? 403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.870 154.117 120.643 1.00 39.91  ? 403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.370 152.422 117.905 1.00 36.90  ? 404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.165 151.812 116.862 1.00 29.50  ? 404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.371 151.566 115.597 1.00 38.36  ? 404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.438 152.308 115.265 1.00 48.44  ? 404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 143.744 150.511 114.877 1.00 36.03  ? 405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.115 150.150 113.610 1.00 19.61  ? 405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.555 148.739 113.723 1.00 31.88  ? 405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.280 147.806 114.082 1.00 39.06  ? 405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.115 150.248 112.458 1.00 28.40  ? 405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.728 151.623 112.190 1.00 31.09  ? 405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 145.801 151.524 111.120 1.00 23.72  ? 405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.662 152.621 111.785 1.00 31.01  ? 405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.270 148.583 113.415 1.00 37.31  ? 406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.616 147.283 113.382 1.00 30.46  ? 406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 139.986 147.056 112.015 1.00 34.52  ? 406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.350 147.954 111.454 1.00 41.36  ? 406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.557 147.166 114.481 1.00 34.59  ? 406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.163 146.941 115.851 1.00 38.76  ? 406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.380 146.675 115.928 1.00 37.99  ? 406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.420 147.022 116.852 1.00 43.01  ? 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.143 145.843 111.500 1.00 29.33  ? 407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 139.836 145.547 110.104 1.00 25.04  ? 407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 138.350 145.247 109.955 1.00 24.36  ? 407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 137.707 144.744 110.883 1.00 40.88  ? 407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 140.697 144.374 109.613 1.00 26.52  ? 407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.178 144.673 109.850 1.00 19.18  ? 407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 140.444 144.090 108.156 1.00 28.22  ? 407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 142.958 143.491 110.364 1.00 26.75  ? 407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 137.800 145.561 108.782 1.00 31.53  ? 408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 136.412 145.285 108.444 1.00 38.59  ? 408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 136.313 144.787 107.006 1.00 44.09  ? 408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.104 145.178 106.142 1.00 46.22  ? 408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 135.546 146.536 108.628 1.00 36.93  ? 408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.321 147.188 107.392 1.00 46.03  ? 408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 135.333 143.919 106.755 1.00 46.28  ? 409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 135.079 143.352 105.434 1.00 47.05  ? 409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 134.089 144.217 104.666 1.00 49.13  ? 409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 132.928 144.341 105.067 1.00 53.04  ? 409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 134.525 141.929 105.525 1.00 51.50  ? 409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 135.695 140.551 105.543 1.00 66.08  ? 409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.540 144.789 103.557 1.00 38.40  ? 410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.647 145.321 102.529 1.00 27.49  ? 410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 133.757 144.365 101.348 1.00 36.56  ? 410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.596 144.549 100.462 1.00 46.78  ? 410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 134.019 146.750 102.154 1.00 33.49  ? 410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 134.299 147.614 103.367 1.00 48.11  ? 410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 133.380 148.047 104.060 1.00 46.72  ? 410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 135.575 147.868 103.632 1.00 46.83  ? 410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 132.913 143.337 101.341 1.00 29.92  ? 411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.084 142.198 100.454 1.00 22.76  ? 411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.184 142.280 99.229  1.00 28.15  ? 411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.069 142.804 99.277  1.00 39.75  ? 411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 132.809 140.885 101.187 1.00 26.22  ? 411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.681 140.582 102.398 1.00 28.26  ? 411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.588 139.115 102.770 1.00 34.13  ? 411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.112 140.971 102.101 1.00 33.91  ? 411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 132.697 141.745 98.129  1.00 23.63  ? 412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 131.922 141.561 96.921  1.00 16.20  ? 412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 132.612 140.544 96.049  1.00 22.73  ? 412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 133.843 140.448 96.041  1.00 43.32  ? 412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 131.821 139.776 95.311  1.00 28.26  ? 413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.336 138.646 94.554  1.00 20.28  ? 413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.059 138.824 93.072  1.00 25.99  ? 413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 130.958 139.222 92.676  1.00 38.51  ? 413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 131.722 137.331 95.041  1.00 26.77  ? 413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.192 137.000 96.334  1.00 31.40  ? 413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.066 138.531 92.257  1.00 30.61  ? 414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 132.901 138.457 90.816  1.00 26.96  ? 414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 132.511 137.042 90.419  1.00 36.71  ? 414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.117 136.068 90.875  1.00 40.98  ? 414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.188 138.856 90.094  1.00 27.33  ? 414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 134.848 140.169 90.500  1.00 37.49  ? 414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.064 140.421 89.633  1.00 36.38  ? 414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 133.857 141.310 90.375  1.00 35.99  ? 414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 131.495 136.933 89.572  1.00 43.78  ? 415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.117 135.650 88.989  1.00 39.54  ? 415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 131.992 135.443 87.763  1.00 38.47  ? 415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 131.756 136.041 86.712  1.00 42.77  ? 415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 129.637 135.628 88.633  1.00 34.86  ? 415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.109 134.227 88.441  1.00 45.77  ? 415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 128.938 133.484 89.401  1.00 47.22  ? 415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.855 133.856 87.194  1.00 44.99  ? 415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.004 134.584 87.898  1.00 30.24  ? 416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.000 134.425 86.842  1.00 31.95  ? 416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 133.339 133.982 85.543  1.00 37.16  ? 416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 133.698 134.452 84.455  1.00 40.33  ? 416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.096 133.443 87.294  1.00 32.51  ? 416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 135.873 134.032 88.470  1.00 26.92  ? 416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.033 133.130 86.150  1.00 31.70  ? 416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 136.842 133.071 89.109  1.00 29.25  ? 416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 132.351 133.089 85.636  1.00 41.47  ? 417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 131.643 132.634 84.444  1.00 40.85  ? 417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 130.970 133.797 83.726  1.00 40.91  ? 417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.205 134.024 82.534  1.00 50.33  ? 417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 130.614 131.571 84.826  1.00 37.93  ? 417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 129.718 130.998 83.726  1.00 38.66  ? 417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.521 130.589 82.504  1.00 37.21  ? 417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 128.917 129.826 84.259  1.00 45.11  ? 417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.156 134.571 84.446  1.00 43.21  ? 418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 129.438 135.668 83.808  1.00 44.74  ? 418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.356 136.844 83.504  1.00 45.14  ? 418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.084 137.616 82.579  1.00 46.73  ? 418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.268 136.111 84.684  1.00 42.48  ? 418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.112 135.133 84.646  1.00 49.79  ? 418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 126.771 134.601 83.591  1.00 52.89  ? 418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 126.502 134.892 85.799  1.00 47.80  ? 418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 131.436 137.003 84.271  1.00 46.25  ? 419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.399 138.058 83.978  1.00 43.18  ? 419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.105 137.788 82.657  1.00 46.71  ? 419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.273 138.693 81.831  1.00 50.52  ? 419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.402 138.207 85.138  1.00 36.84  ? 419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 134.678 138.874 84.661  1.00 43.55  ? 419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 132.785 139.005 86.268  1.00 43.76  ? 419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 133.519 136.540 82.424  1.00 48.13  ? 420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.268 136.239 81.212  1.00 47.35  ? 420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 133.374 135.950 80.014  1.00 47.43  ? 420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 133.836 136.075 78.876  1.00 53.21  ? 420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.218 135.063 81.446  1.00 45.50  ? 420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.463 135.450 82.220  1.00 44.82  ? 420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 137.898 135.733 81.168  1.00 60.55  ? 420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.021 134.179 80.300  1.00 51.75  ? 420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.113 135.565 80.233  1.00 55.78  ? 421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.185 135.452 79.112  1.00 56.07  ? 421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 130.896 136.816 78.503  1.00 55.45  ? 421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 130.772 136.947 77.278  1.00 52.55  ? 421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 129.888 134.776 79.554  1.00 47.71  ? 421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.015 133.284 79.810  1.00 54.02  ? 421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 128.682 132.628 80.112  1.00 61.89  ? 421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 127.987 133.093 81.040  1.00 57.01  ? 421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.330 131.648 79.423  1.00 58.03  ? 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 130.785 137.847 79.340  1.00 50.73  ? 422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 130.532 139.199 78.863  1.00 51.14  ? 422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 131.799 139.924 78.430  1.00 54.53  ? 422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 131.699 141.042 77.911  1.00 52.42  ? 422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 129.823 140.015 79.945  1.00 46.73  ? 422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 128.433 139.547 80.242  1.00 54.30  ? 422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.161 138.564 81.170  1.00 56.69  ? 422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.237 139.925 79.734  1.00 53.20  ? 422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 126.858 138.358 81.220  1.00 53.24  ? 422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.274 139.171 80.359  1.00 52.53  ? 422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 132.972 139.319 78.628  1.00 61.16  ? 423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.253 139.926 78.261  1.00 57.03  ? 423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.408 141.307 78.892  1.00 60.88  ? 423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 134.837 142.267 78.249  1.00 62.14  ? 423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 134.412 140.003 76.741  1.00 54.05  ? 423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 134.112 138.704 76.012  1.00 58.77  ? 423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.290 137.748 76.076  1.00 63.42  ? 423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 134.848 136.310 75.861  1.00 63.27  ? 423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.507 135.377 76.816  1.00 60.10  ? 423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.052 141.408 80.170  1.00 48.30  ? 424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.019 142.678 80.886  1.00 48.06  ? 424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 134.729 142.560 82.226  1.00 46.97  ? 424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.192 142.924 83.273  1.00 48.86  ? 424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 132.585 143.156 81.087  1.00 52.60  ? 424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 131.957 142.445 82.139  1.00 52.10  ? 424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 135.951 142.025 82.216  1.00 48.43  ? 425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 136.740 141.970 83.444  1.00 40.63  ? 425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.001 143.378 83.963  1.00 44.54  ? 425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 136.809 143.668 85.149  1.00 48.54  ? 425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.055 141.206 83.210  1.00 44.92  ? 425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 137.789 139.710 83.043  1.00 47.31  ? 425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.020 141.440 84.361  1.00 43.91  ? 425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.025 138.912 82.711  1.00 44.56  ? 425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.422 144.279 83.074  1.00 44.98  ? 426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 137.755 145.639 83.487  1.00 39.79  ? 426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.539 146.363 84.052  1.00 40.68  ? 426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.589 146.917 85.157  1.00 49.42  ? 426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.332 146.414 82.303  1.00 44.09  ? 426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.360 147.919 82.497  1.00 48.51  ? 426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 138.972 148.644 81.317  1.00 53.29  ? 426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.202 147.996 80.274  1.00 46.60  ? 426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.224 149.861 81.431  1.00 57.06  ? 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.437 146.370 83.299  1.00 40.37  ? 427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.246 147.095 83.729  1.00 38.78  ? 427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 133.686 146.518 85.021  1.00 38.77  ? 427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.322 147.266 85.937  1.00 45.95  ? 427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.195 147.069 82.619  1.00 47.27  ? 427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 131.868 147.711 82.984  1.00 47.18  ? 427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 130.721 147.042 82.244  1.00 49.35  ? 427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 130.097 145.929 83.069  1.00 51.66  ? 427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 128.925 146.414 83.848  1.00 49.15  ? 427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 133.619 145.188 85.119  1.00 39.88  ? 428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.096 144.564 86.328  1.00 30.36  ? 428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 133.974 144.866 87.532  1.00 39.87  ? 428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.466 145.203 88.607  1.00 45.21  ? 428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 132.966 143.055 86.136  1.00 33.83  ? 428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.197 142.785 84.958  1.00 43.86  ? 428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.279 142.426 87.334  1.00 41.47  ? 428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.296 144.761 87.374  1.00 37.64  ? 429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.196 145.014 88.495  1.00 31.37  ? 429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.094 146.464 88.944  1.00 38.36  ? 429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.043 146.752 90.145  1.00 42.88  ? 429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.641 144.633 88.127  1.00 35.36  ? 429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.608 145.190 89.151  1.00 36.77  ? 429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 137.787 143.127 88.049  1.00 40.32  ? 429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.042 147.400 87.994  1.00 42.83  ? 430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 135.974 148.811 88.365  1.00 37.27  ? 430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.648 149.155 89.033  1.00 37.34  ? 430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.623 149.879 90.036  1.00 46.39  ? 430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.210 149.686 87.134  1.00 38.77  ? 430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.615 149.558 86.567  1.00 38.32  ? 430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 137.955 150.706 85.638  1.00 41.66  ? 430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.421 150.667 85.244  1.00 46.20  ? 430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 139.788 151.801 84.356  1.00 44.83  ? 430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.533 148.643 88.503  1.00 42.49  ? 431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.239 148.916 89.121  1.00 34.34  ? 431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.138 148.277 90.501  1.00 37.12  ? 431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.583 148.876 91.429  1.00 44.19  ? 431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.112 148.428 88.215  1.00 37.45  ? 431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.629 149.413 87.150  1.00 42.90  ? 431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.743 148.711 86.139  1.00 41.46  ? 431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 129.891 150.574 87.794  1.00 41.64  ? 431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.667 147.061 90.655  1.00 30.95  ? 432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.683 146.416 91.962  1.00 29.45  ? 432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.540 147.195 92.949  1.00 38.61  ? 432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.178 147.330 94.123  1.00 43.73  ? 432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.191 144.984 91.825  1.00 36.79  ? 432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.686 147.707 92.494  1.00 41.15  ? 433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.530 148.522 93.356  1.00 34.22  ? 433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 134.807 149.790 93.788  1.00 34.01  ? 433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 134.885 150.191 94.954  1.00 40.59  ? 433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 136.835 148.863 92.634  1.00 38.74  ? 433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.486 147.654 92.229  1.00 36.89  ? 433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.762 149.650 93.544  1.00 36.54  ? 433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.089 150.431 92.862  1.00 30.02  ? 434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.320 151.621 93.217  1.00 36.98  ? 434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.226 151.295 94.229  1.00 41.44  ? 434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.010 152.048 95.187  1.00 42.71  ? 434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.721 152.251 91.962  1.00 40.54  ? 434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.769 152.855 91.055  1.00 49.57  ? 434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 134.774 153.381 91.575  1.00 49.97  ? 434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.590 152.804 89.819  1.00 46.51  ? 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.522 150.177 94.031  1.00 35.77  ? 435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.467 149.789 94.965  1.00 25.23  ? 435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.032 149.488 96.347  1.00 30.34  ? 435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.450 149.885 97.363  1.00 41.76  ? 435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.709 148.580 94.425  1.00 31.48  ? 435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.514 147.416 94.462  1.00 35.44  ? 435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.163 148.784 96.405  1.00 34.65  ? 436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 132.778 148.479 97.691  1.00 23.11  ? 436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.301 149.741 98.363  1.00 24.36  ? 436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.246 149.866 99.591  1.00 34.03  ? 436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 133.898 147.460 97.501  1.00 33.75  ? 436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.428 146.084 97.038  1.00 25.12  ? 436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.603 145.201 96.666  1.00 24.83  ? 436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.578 145.445 98.111  1.00 26.30  ? 436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.810 150.689 97.572  1.00 34.22  ? 437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.217 151.977 98.119  1.00 31.21  ? 437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.029 152.710 98.724  1.00 39.59  ? 437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.137 153.299 99.805  1.00 47.99  ? 437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 134.864 152.824 97.025  1.00 23.89  ? 437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 135.948 152.096 96.437  1.00 37.11  ? 437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.389 154.126 97.597  1.00 32.70  ? 437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 131.886 152.685 98.037  1.00 35.84  ? 438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.684 153.308 98.580  1.00 33.70  ? 438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.245 152.630 99.871  1.00 29.84  ? 438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 129.842 153.302 100.828 1.00 45.02  ? 438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.557 153.267 97.549  1.00 40.01  ? 438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.303 153.941 98.008  1.00 36.47  ? 438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 127.322 153.281 98.716  1.00 40.15  ? 438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.872 155.216 97.867  1.00 34.94  ? 438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.340 154.120 98.989  1.00 42.67  ? 438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.648 155.301 98.484  1.00 46.21  ? 438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.306 151.298 99.913  1.00 25.76  ? 439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 129.927 150.574 101.124 1.00 27.84  ? 439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.847 150.945 102.279 1.00 35.99  ? 439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.394 151.166 103.409 1.00 43.35  ? 439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 129.929 149.055 100.865 1.00 30.94  ? 439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.730 148.292 102.164 1.00 30.37  ? 439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 128.851 148.690 99.870  1.00 30.47  ? 439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.154 151.016 102.016 1.00 40.52  ? 440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.101 151.392 103.061 1.00 36.96  ? 440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.862 152.818 103.541 1.00 36.93  ? 440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.911 153.091 104.746 1.00 41.93  ? 440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.533 151.229 102.550 1.00 34.95  ? 440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.473 151.420 103.592 1.00 41.88  ? 440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.605 153.742 102.612 1.00 36.29  ? 441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.396 155.136 102.989 1.00 37.07  ? 441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.119 155.313 103.801 1.00 44.31  ? 441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.109 156.042 104.799 1.00 51.03  ? 441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.361 156.016 101.740 1.00 37.28  ? 441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.723 156.511 101.295 1.00 44.71  ? 441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.817 156.685 99.794  1.00 50.92  ? 441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 132.764 156.643 99.123  1.00 49.84  ? 441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.942 156.869 99.285  1.00 46.61  ? 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.032 154.656 103.395 1.00 42.55  ? 442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.760 154.815 104.088 1.00 43.36  ? 442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.697 154.057 105.405 1.00 44.13  ? 442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.738 154.246 106.162 1.00 48.14  ? 442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.604 154.370 103.190 1.00 45.07  ? 442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.805 153.011 102.785 1.00 45.37  ? 442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.515 155.260 101.964 1.00 43.50  ? 442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.678 153.210 105.698 1.00 45.44  ? 443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.711 152.501 106.971 1.00 49.28  ? 443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.227 153.438 108.054 1.00 51.24  ? 443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.320 154.000 107.931 1.00 54.11  ? 443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.591 151.257 106.872 1.00 50.95  ? 443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 129.907 150.245 106.124 1.00 53.02  ? 443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.909 150.724 108.260 1.00 48.71  ? 443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.438 153.611 109.112 1.00 60.79  ? 444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 129.816 154.451 110.249 1.00 61.29  ? 444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.366 153.723 111.510 1.00 60.93  ? 444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.192 153.788 111.886 1.00 63.78  ? 444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.193 155.839 110.149 1.00 62.68  ? 444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 129.888 156.855 111.031 1.00 65.64  ? 444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 131.115 157.036 110.882 1.00 60.33  ? 444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 129.209 157.476 111.875 1.00 68.02  ? 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.297 153.030 112.154 1.00 50.34  ? 445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.008 152.234 113.340 1.00 55.39  ? 445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.488 153.023 114.549 1.00 57.74  ? 445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.685 153.284 114.703 1.00 56.60  ? 445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 130.668 150.852 113.264 1.00 53.99  ? 445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 129.870 149.946 112.329 1.00 53.85  ? 445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 130.740 150.222 114.640 1.00 54.33  ? 445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.617 148.721 111.895 1.00 49.61  ? 445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.547 153.412 115.410 1.00 67.70  ? 446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.850 154.316 116.510 1.00 68.46  ? 446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.342 153.598 117.759 1.00 63.19  ? 446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 131.080 154.197 118.547 1.00 60.22  ? 446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.620 155.165 116.858 1.00 65.68  ? 446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.284 154.420 116.875 1.00 65.62  ? 446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.629 154.355 115.496 1.00 65.06  ? 446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.722 155.617 114.770 1.00 70.56  ? 446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 125.997 156.695 115.035 1.00 68.83  ? 446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 126.176 157.793 114.305 1.00 63.58  ? 446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 125.097 156.703 116.005 1.00 66.78  ? 446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 129.960 152.340 117.960 1.00 53.70  ? 447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.336 151.611 119.162 1.00 49.54  ? 447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.666 150.882 119.029 1.00 50.22  ? 447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.150 150.320 120.017 1.00 52.45  ? 447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.237 150.613 119.538 1.00 50.40  ? 447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.324 151.142 120.623 1.00 54.38  ? 447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 128.744 151.333 121.763 1.00 56.80  ? 447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.067 151.382 120.273 1.00 47.99  ? 447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.265 150.878 117.843 1.00 53.71  ? 448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.600 150.318 117.630 1.00 49.18  ? 448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.512 151.434 117.144 1.00 48.65  ? 448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.490 151.781 115.950 1.00 44.00  ? 448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.566 149.169 116.628 1.00 44.53  ? 448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.322 152.027 118.021 1.00 43.57  ? 449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.119 153.194 117.621 1.00 38.96  ? 449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.231 152.842 116.650 1.00 42.31  ? 449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.447 153.545 115.658 1.00 42.81  ? 449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.687 153.708 118.952 1.00 40.91  ? 449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 135.968 152.941 120.029 1.00 46.12  ? 449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.565 151.649 119.419 1.00 37.53  ? 449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 137.948 151.752 116.933 1.00 40.22  ? 450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.043 151.339 116.063 1.00 29.24  ? 450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.532 150.893 114.700 1.00 37.35  ? 450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.157 151.182 113.674 1.00 40.84  ? 450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 139.849 150.226 116.728 1.00 38.46  ? 450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.399 150.188 114.667 1.00 45.06  ? 451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 136.826 149.755 113.395 1.00 35.02  ? 451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.463 150.963 112.542 1.00 35.92  ? 451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.775 151.020 111.349 1.00 42.67  ? 451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.605 148.847 113.635 1.00 33.21  ? 451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.712 148.814 112.407 1.00 39.06  ? 451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.045 147.445 114.008 1.00 33.49  ? 451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 135.804 151.953 113.150 1.00 36.86  ? 452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.418 153.154 112.419 1.00 38.91  ? 452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.640 153.935 111.947 1.00 37.69  ? 452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.683 154.410 110.805 1.00 43.84  ? 452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.526 154.025 113.303 1.00 35.25  ? 452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.218 155.400 112.750 1.00 40.12  ? 452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.800 156.339 113.864 1.00 39.17  ? 452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 132.353 156.516 113.910 1.00 51.24  ? 452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 131.716 157.259 114.805 1.00 52.08  ? 452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 130.390 157.338 114.756 1.00 44.60  ? 452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 132.370 157.921 115.746 1.00 48.87  ? 452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.646 154.070 112.814 1.00 35.47  ? 453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 138.853 154.801 112.443 1.00 32.91  ? 453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.578 154.122 111.288 1.00 38.11  ? 453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.022 154.790 110.348 1.00 46.97  ? 453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.774 154.937 113.655 1.00 33.22  ? 453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.250 154.989 113.311 1.00 33.43  ? 453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.001 155.941 114.221 1.00 33.88  ? 453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.331 156.241 113.704 1.00 34.25  ? 453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.437 155.610 114.073 1.00 37.13  ? 453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 145.599 155.969 113.532 1.00 37.14  ? 453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 144.413 154.636 114.965 1.00 38.84  ? 453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.693 152.793 111.333 1.00 39.49  ? 454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.369 152.079 110.257 1.00 29.54  ? 454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.549 152.081 108.975 1.00 35.88  ? 454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.121 152.101 107.883 1.00 44.90  ? 454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.681 150.649 110.688 1.00 35.12  ? 454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.220 152.054 109.078 1.00 36.21  ? 455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.393 152.171 107.883 1.00 37.84  ? 455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.579 153.532 107.227 1.00 42.06  ? 455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.653 153.633 105.996 1.00 44.54  ? 455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 135.923 151.938 108.236 1.00 39.91  ? 455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.034 151.867 107.012 1.00 47.02  ? 455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.141 150.943 106.206 1.00 48.21  ? 455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.148 152.845 106.866 1.00 43.06  ? 455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.655 154.593 108.033 1.00 37.39  ? 456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 137.875 155.923 107.478 1.00 34.27  ? 456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.279 156.077 106.906 1.00 37.34  ? 456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.458 156.739 105.879 1.00 44.87  ? 456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.620 156.988 108.544 1.00 38.49  ? 456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.156 157.168 108.903 1.00 47.46  ? 456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 135.978 158.248 109.958 1.00 46.95  ? 456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.538 158.319 110.438 1.00 44.27  ? 456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 134.355 159.365 111.482 1.00 43.38  ? 456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.283 155.479 107.549 1.00 38.11  ? 457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.675 155.698 107.170 1.00 32.41  ? 457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.129 154.767 106.049 1.00 39.59  ? 457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.526 155.225 104.973 1.00 44.38  ? 457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.574 155.527 108.399 1.00 30.49  ? 457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.073 153.456 106.289 1.00 43.18  ? 458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.611 152.495 105.335 1.00 36.05  ? 458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.738 152.366 104.095 1.00 37.04  ? 458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.256 152.092 103.007 1.00 46.79  ? 458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.779 151.133 106.008 1.00 33.84  ? 458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.292 151.211 107.434 1.00 40.38  ? 458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.091 151.157 107.521 1.00 52.20  ? 458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.435 149.724 106.509 1.00 38.12  ? 458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.423 152.546 104.237 1.00 31.24  ? 459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.487 152.451 103.115 1.00 32.01  ? 459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.633 151.116 102.388 1.00 32.41  ? 459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.589 151.044 101.160 1.00 37.41  ? 459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.668 153.620 102.145 1.00 34.12  ? 459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.540 154.989 102.787 1.00 37.18  ? 459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.425 156.005 102.087 1.00 36.20  ? 459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.307 157.373 102.732 1.00 38.30  ? 459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.255 158.349 102.131 1.00 39.74  ? 459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.813 150.049 103.159 1.00 33.97  ? 460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.067 148.736 102.588 1.00 26.33  ? 460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.769 148.067 102.161 1.00 27.73  ? 460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.750 148.153 102.851 1.00 41.83  ? 460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.797 147.851 103.594 1.00 31.40  ? 460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 139.987 147.611 104.730 1.00 40.23  ? 460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 138.815 147.395 101.011 1.00 25.14  ? 461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.673 146.676 100.469 1.00 21.75  ? 461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.116 145.266 100.104 1.00 29.75  ? 461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.306 144.980 99.960  1.00 45.04  ? 461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.067 147.381 99.239  1.00 24.63  ? 461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.085 147.432 98.101  1.00 15.30  ? 461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.595 148.779 99.602  1.00 35.19  ? 461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.523 147.949 96.803  1.00 24.15  ? 461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.137 144.378 99.971  1.00 25.78  ? 462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.422 143.020 99.555  1.00 18.30  ? 462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 136.669 142.622 98.305  1.00 16.49  ? 462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.443 142.490 98.330  1.00 35.45  ? 462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.387 142.422 97.208  1.00 17.96  ? 463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 136.789 142.040 95.932  1.00 20.77  ? 463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.209 140.608 95.622  1.00 28.28  ? 463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.319 140.367 95.139  1.00 38.73  ? 463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.204 143.000 94.823  1.00 29.69  ? 463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 136.661 142.650 93.440  1.00 21.32  ? 463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.154 142.515 93.505  1.00 15.67  ? 463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.066 143.698 92.420  1.00 23.96  ? 463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.317 139.659 95.904  1.00 22.47  ? 464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 136.569 138.262 95.644  1.00 24.02  ? 464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.029 137.811 94.297  1.00 23.51  ? 464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.455 138.574 93.524  1.00 29.86  ? 464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.233 136.527 94.024  1.00 20.51  ? 465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 135.734 135.902 92.811  1.00 22.14  ? 465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.128 134.554 93.162  1.00 32.55  ? 465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.561 133.886 94.104  1.00 43.40  ? 465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 136.841 135.730 91.765  1.00 32.27  ? 465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.116 134.161 92.393  1.00 39.06  ? 466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 133.454 132.880 92.571  1.00 38.61  ? 466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.186 132.274 91.202  1.00 38.24  ? 466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 133.423 132.901 90.166  1.00 45.56  ? 466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.153 133.021 93.370  1.00 40.51  ? 466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 130.978 133.518 92.553  1.00 36.72  ? 466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 129.812 134.479 93.529  1.00 50.25  ? 466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.181 135.584 92.274  1.00 46.05  ? 466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 132.695 131.033 91.210  1.00 31.41  ? 467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 132.387 130.279 89.997  1.00 28.27  ? 467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 133.635 129.983 89.173  1.00 32.66  ? 467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 133.571 129.911 87.944  1.00 43.89  ? 467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 131.344 130.997 89.134  1.00 31.59  ? 467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 130.382 130.039 88.464  1.00 39.58  ? 467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.510 128.823 88.592  1.00 48.39  ? 467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 129.406 130.583 87.750  1.00 38.10  ? 467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 134.782 129.821 89.834  1.00 25.90  ? 468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 135.987 129.414 89.121  1.00 26.55  ? 468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 135.856 127.992 88.595  1.00 40.68  ? 468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.078 127.735 87.406  1.00 45.53  ? 468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.208 129.537 90.033  1.00 34.66  ? 468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 138.542 129.135 89.405  1.00 31.70  ? 468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.019 130.183 88.416  1.00 34.33  ? 468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 139.587 128.887 90.474  1.00 31.22  ? 468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.477 127.055 89.468  1.00 43.69  ? 469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.316 125.672 89.037  1.00 32.19  ? 469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.170 125.537 88.046  1.00 41.52  ? 469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.253 124.748 87.100  1.00 58.40  ? 469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.090 124.761 90.241  1.00 36.67  ? 469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.264 123.306 89.935  1.00 38.98  ? 469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 134.953 122.312 90.836  1.00 44.05  ? 469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 135.715 122.677 88.823  1.00 38.82  ? 469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.207 121.134 90.295  1.00 41.26  ? 469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 135.670 121.327 89.074  1.00 38.81  ? 469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.091 126.294 88.248  1.00 33.25  ? 470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 131.996 126.263 87.293  1.00 30.54  ? 470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.423 126.721 85.913  1.00 31.88  ? 470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.091 126.092 84.905  1.00 49.61  ? 470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.175 127.822 85.850  1.00 28.74  ? 471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 133.660 128.306 84.562  1.00 37.22  ? 471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.614 127.307 83.922  1.00 42.53  ? 471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.543 127.056 82.714  1.00 40.90  ? 471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 134.349 129.662 84.722  1.00 34.57  ? 471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 134.855 130.219 83.412  1.00 35.57  ? 471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 133.988 130.834 82.523  1.00 39.30  ? 471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.189 130.105 83.050  1.00 31.12  ? 471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 134.433 131.337 81.322  1.00 40.05  ? 471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 136.645 130.603 81.845  1.00 29.13  ? 471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 135.760 131.219 80.987  1.00 38.15  ? 471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 136.193 131.721 79.784  1.00 42.84  ? 471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.521 126.731 84.716  1.00 44.47  ? 472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.490 125.790 84.164  1.00 46.01  ? 472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 135.812 124.530 83.642  1.00 44.17  ? 472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.160 124.033 82.565  1.00 47.01  ? 472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.539 125.436 85.218  1.00 42.96  ? 472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.448 126.575 85.681  1.00 37.18  ? 472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.186 126.186 86.951  1.00 41.91  ? 472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 139.422 126.961 84.582  1.00 35.45  ? 472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 134.843 123.998 84.388  1.00 40.95  ? 473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.178 122.769 83.974  1.00 42.20  ? 473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.242 123.015 82.798  1.00 45.63  ? 473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.128 122.170 81.903  1.00 54.21  ? 473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 133.419 122.165 85.152  1.00 45.11  ? 473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 132.564 124.163 82.778  1.00 41.24  ? 474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 131.690 124.493 81.660  1.00 45.25  ? 474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.463 124.887 80.410  1.00 45.91  ? 474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 131.853 125.027 79.344  1.00 46.99  ? 474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 130.731 125.616 82.061  1.00 42.98  ? 474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 129.597 125.153 82.957  1.00 44.30  ? 474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 128.700 126.288 83.405  1.00 44.88  ? 474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.038 126.929 82.590  1.00 45.65  ? 474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 128.670 126.539 84.708  1.00 43.89  ? 474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 133.779 125.071 80.513  1.00 53.18  ? 475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 134.632 125.352 79.367  1.00 53.23  ? 475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 135.568 124.190 79.055  1.00 51.29  ? 475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 136.533 124.356 78.302  1.00 50.33  ? 475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.430 126.634 79.600  1.00 49.03  ? 475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 134.647 127.879 79.240  1.00 51.33  ? 475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 134.717 128.366 78.112  1.00 54.36  ? 475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 133.885 128.395 80.196  1.00 47.59  ? 475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.300 123.017 79.619  1.00 45.91  ? 476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.112 121.840 79.363  1.00 47.47  ? 476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 137.526 121.917 79.894  1.00 51.91  ? 476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 138.462 121.478 79.215  1.00 52.77  ? 476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 137.708 122.463 81.094  1.00 45.46  ? 477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.015 122.562 81.730  1.00 42.38  ? 477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 138.923 121.914 83.103  1.00 43.75  ? 477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.066 122.286 83.915  1.00 45.07  ? 477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.490 124.019 81.848  1.00 38.76  ? 477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.385 124.731 80.500  1.00 39.69  ? 477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 140.916 124.073 82.360  1.00 41.95  ? 477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.369 126.232 80.615  1.00 47.02  ? 477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 139.800 120.948 83.361  1.00 47.32  ? 478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 139.865 120.337 84.679  1.00 47.10  ? 478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 140.461 121.317 85.681  1.00 47.11  ? 478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 141.370 122.083 85.355  1.00 44.58  ? 478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 140.695 119.056 84.634  1.00 46.22  ? 478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 139.941 121.285 86.911  1.00 44.93  ? 479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 140.392 122.223 87.935  1.00 40.76  ? 479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 141.872 122.038 88.247  1.00 47.51  ? 479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 142.598 123.018 88.452  1.00 53.19  ? 479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 139.549 122.054 89.198  1.00 38.47  ? 479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 139.746 123.133 90.238  1.00 37.75  ? 479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 140.710 123.002 91.229  1.00 41.48  ? 479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 138.962 124.278 90.236  1.00 41.12  ? 479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 140.890 123.982 92.183  1.00 43.84  ? 479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.136 125.263 91.187  1.00 41.69  ? 479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.101 125.109 92.158  1.00 46.46  ? 479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.278 126.089 93.108  1.00 48.56  ? 479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 142.337 120.791 88.291  1.00 44.22  ? 480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 143.736 120.511 88.579  1.00 43.41  ? 480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 144.637 120.667 87.363  1.00 45.14  ? 480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 145.862 120.623 87.512  1.00 51.87  ? 480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 143.888 119.095 89.128  1.00 47.30  ? 480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.242 118.865 90.475  1.00 48.46  ? 480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 142.431 117.591 90.501  1.00 54.88  ? 480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 141.422 117.515 89.768  1.00 52.49  ? 480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 142.813 116.657 91.235  1.00 54.39  ? 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.066 120.840 86.175  1.00 42.48  ? 481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 144.869 120.922 84.969  1.00 45.77  ? 481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 145.693 122.209 84.959  1.00 46.16  ? 481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.262 123.236 85.490  1.00 49.64  ? 481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 143.977 120.868 83.734  1.00 45.72  ? 481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 143.628 122.170 83.300  1.00 44.75  ? 481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 146.892 122.173 84.373  1.00 46.92  ? 482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 147.698 123.402 84.286  1.00 43.27  ? 482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.024 124.508 83.495  1.00 45.23  ? 482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.321 125.687 83.723  1.00 47.23  ? 482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 148.990 122.926 83.606  1.00 47.55  ? 482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.030 121.453 83.843  1.00 49.30  ? 482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 147.603 121.005 83.831  1.00 46.47  ? 482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.132 124.163 82.563  1.00 48.90  ? 483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.390 125.189 81.837  1.00 44.63  ? 483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.476 125.971 82.771  1.00 44.41  ? 483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.303 127.183 82.607  1.00 49.96  ? 483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 144.588 124.556 80.701  1.00 51.82  ? 483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.430 123.792 79.692  1.00 54.67  ? 483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 145.643 122.343 80.084  1.00 54.39  ? 483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 144.750 121.767 80.739  1.00 50.24  ? 483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.702 121.780 79.738  1.00 50.45  ? 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 143.878 125.295 83.754  1.00 39.88  ? 484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.063 125.994 84.740  1.00 39.42  ? 484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 143.899 126.975 85.549  1.00 44.50  ? 484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 143.462 128.099 85.819  1.00 46.93  ? 484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.379 124.991 85.665  1.00 35.91  ? 484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.103 126.565 85.952  1.00 41.07  ? 485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 145.978 127.467 86.693  1.00 34.61  ? 485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 146.424 128.637 85.827  1.00 38.28  ? 485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 146.534 129.766 86.313  1.00 49.80  ? 485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.183 126.703 87.234  1.00 39.55  ? 485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 146.848 125.756 88.368  1.00 40.24  ? 485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.103 125.272 89.064  1.00 42.52  ? 485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 148.941 124.465 88.186  1.00 44.19  ? 485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 148.809 123.156 88.021  1.00 43.96  ? 485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 149.634 122.521 87.194  1.00 42.20  ? 485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 147.875 122.470 88.660  1.00 37.46  ? 485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 146.688 128.388 84.543  1.00 41.59  ? 486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.033 129.475 83.631  1.00 40.85  ? 486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 145.882 130.464 83.492  1.00 40.16  ? 486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.091 131.686 83.512  1.00 42.76  ? 486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 147.419 128.897 82.271  1.00 47.08  ? 486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 147.948 129.945 81.320  1.00 51.07  ? 486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 148.877 130.686 81.700  1.00 53.58  ? 486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 147.437 130.017 80.183  1.00 50.08  ? 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 144.656 129.952 83.352  1.00 39.75  ? 487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 143.497 130.831 83.273  1.00 39.96  ? 487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 143.324 131.630 84.553  1.00 39.37  ? 487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.009 132.822 84.506  1.00 46.90  ? 487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.226 130.033 82.992  1.00 42.22  ? 487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 140.977 130.752 83.405  1.00 40.97  ? 487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 140.474 131.784 82.635  1.00 39.10  ? 487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 140.321 130.418 84.578  1.00 44.31  ? 487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 139.338 132.459 83.018  1.00 42.89  ? 487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.182 131.093 84.964  1.00 39.30  ? 487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 138.693 132.114 84.182  1.00 39.49  ? 487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 143.492 130.984 85.708  1.00 34.67  ? 488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 143.369 131.699 86.973  1.00 32.30  ? 488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 144.434 132.778 87.093  1.00 35.91  ? 488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.148 133.896 87.535  1.00 44.08  ? 488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 143.459 130.721 88.141  1.00 29.98  ? 488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 145.665 132.465 86.687  1.00 38.20  ? 489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 146.733 133.454 86.692  1.00 31.18  ? 489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.351 134.669 85.862  1.00 33.48  ? 489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 146.402 135.805 86.344  1.00 38.09  ? 489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.022 132.826 86.163  1.00 34.37  ? 489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.261 133.556 86.628  1.00 41.00  ? 489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 149.383 133.914 87.798  1.00 46.44  ? 489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.195 133.774 85.711  1.00 39.66  ? 489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 145.935 134.445 84.613  1.00 40.60  ? 490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 145.601 135.566 83.739  1.00 37.19  ? 490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 144.401 136.345 84.270  1.00 40.24  ? 490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 144.422 137.580 84.321  1.00 47.35  ? 490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 145.331 135.066 82.321  1.00 43.22  ? 490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 146.444 134.287 81.869  1.00 49.81  ? 490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.127 136.240 81.379  1.00 43.82  ? 490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 143.350 135.634 84.684  1.00 33.67  ? 491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.125 136.291 85.126  1.00 28.70  ? 491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.363 137.128 86.373  1.00 35.66  ? 491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 141.918 138.278 86.451  1.00 41.55  ? 491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.038 135.247 85.384  1.00 32.40  ? 491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 139.749 135.826 85.896  1.00 32.59  ? 491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 138.798 136.313 85.019  1.00 33.63  ? 491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 139.485 135.878 87.255  1.00 33.23  ? 491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 137.613 136.845 85.484  1.00 34.23  ? 491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.305 136.412 87.725  1.00 28.90  ? 491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 137.367 136.894 86.839  1.00 34.17  ? 491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.068 136.577 87.360  1.00 38.04  ? 492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.287 137.314 88.591  1.00 22.37  ? 492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.369 138.374 88.454  1.00 25.49  ? 492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.323 139.371 89.176  1.00 39.44  ? 492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 143.600 136.342 89.727  1.00 29.26  ? 492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.393 135.588 90.209  1.00 34.32  ? 492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 141.488 136.186 91.068  1.00 32.63  ? 492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.141 134.299 89.774  1.00 32.30  ? 492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.371 135.504 91.504  1.00 27.82  ? 492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.023 133.613 90.205  1.00 24.82  ? 492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.138 134.216 91.072  1.00 30.41  ? 492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.312 138.218 87.519  1.00 32.96  ? 493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.194 139.334 87.202  1.00 30.84  ? 493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.405 140.477 86.581  1.00 31.80  ? 493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 145.645 141.644 86.897  1.00 41.18  ? 493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.325 138.867 86.280  1.00 28.02  ? 493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.159 139.973 85.619  1.00 37.22  ? 493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 147.429 140.809 84.194  1.00 45.43  ? 493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.385 139.469 83.011  1.00 41.00  ? 493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 144.454 140.157 85.698  1.00 36.18  ? 494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 143.581 141.182 85.134  1.00 29.38  ? 494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 142.759 141.858 86.225  1.00 40.65  ? 494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 142.612 143.088 86.239  1.00 47.49  ? 494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 142.662 140.548 84.089  1.00 32.42  ? 494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 143.345 140.186 82.782  1.00 35.04  ? 494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 142.210 140.059 81.387  1.00 54.75  ? 494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 141.773 141.773 81.130  1.00 44.20  ? 494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.218 141.061 87.148  1.00 36.51  ? 495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.412 141.601 88.239  1.00 28.03  ? 495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.249 142.520 89.118  1.00 36.57  ? 495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 141.810 143.614 89.486  1.00 41.48  ? 495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 140.785 140.454 89.054  1.00 30.25  ? 495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.265 140.966 90.388  1.00 24.51  ? 495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 139.670 139.792 88.265  1.00 35.60  ? 495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.466 142.094 89.468  1.00 35.78  ? 496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.349 142.934 90.267  1.00 23.07  ? 496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 144.722 144.207 89.523  1.00 29.65  ? 496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 144.740 145.294 90.111  1.00 41.13  ? 496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 145.603 142.152 90.655  1.00 23.86  ? 496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.355 142.789 91.803  1.00 31.99  ? 496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 145.765 143.452 92.654  1.00 39.81  ? 496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 147.666 142.588 91.836  1.00 35.66  ? 496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.016 144.093 88.225  1.00 31.36  ? 497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.365 145.262 87.427  1.00 26.50  ? 497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.246 146.289 87.454  1.00 34.39  ? 497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.477 147.472 87.723  1.00 45.65  ? 497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 145.664 144.835 85.990  1.00 33.30  ? 497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.034 145.971 85.079  1.00 36.09  ? 497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 147.346 146.392 84.975  1.00 37.62  ? 497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 145.070 146.615 84.322  1.00 37.03  ? 497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 147.690 147.434 84.140  1.00 39.56  ? 497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 145.407 147.657 83.485  1.00 34.31  ? 497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 146.719 148.067 83.394  1.00 33.97  ? 497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.015 145.849 87.201  1.00 36.42  ? 498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 141.918 146.805 87.122  1.00 33.61  ? 498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.462 147.278 88.497  1.00 36.80  ? 498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 140.975 148.403 88.619  1.00 43.00  ? 498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 140.763 146.206 86.323  1.00 36.82  ? 498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.109 146.075 84.859  1.00 36.96  ? 498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.442 147.192 84.107  1.00 38.67  ? 498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.125 144.838 84.235  1.00 35.05  ? 498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 141.771 147.083 82.772  1.00 34.11  ? 498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.450 144.719 82.900  1.00 42.08  ? 498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 141.773 145.844 82.173  1.00 43.21  ? 498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.097 145.728 80.842  1.00 48.61  ? 498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 141.648 146.471 89.544  1.00 29.22  ? 499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.363 146.953 90.891  1.00 24.41  ? 499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.356 148.029 91.309  1.00 30.70  ? 499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 141.964 149.052 91.880  1.00 39.99  ? 499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.376 145.789 91.881  1.00 22.93  ? 499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 142.691 145.305 92.083  1.00 32.17  ? 499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 143.645 147.823 91.022  1.00 29.15  ? 500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 144.645 148.851 91.297  1.00 29.16  ? 500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.364 150.095 90.466  1.00 31.08  ? 500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.492 151.226 90.951  1.00 42.24  ? 500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.060 148.303 91.036  1.00 29.60  ? 500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.391 147.177 92.011  1.00 25.23  ? 500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.093 149.405 91.160  1.00 30.25  ? 500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.596 146.369 91.605  1.00 29.58  ? 500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 143.978 149.908 89.202  1.00 33.40  ? 501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 143.676 151.045 88.341  1.00 30.99  ? 501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 142.487 151.838 88.865  1.00 39.26  ? 501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 142.518 153.071 88.885  1.00 47.09  ? 501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.418 150.562 86.915  1.00 37.80  ? 501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 143.731 151.591 85.846  1.00 38.16  ? 501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.552 151.045 84.446  1.00 42.40  ? 501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.529 150.437 84.131  1.00 44.27  ? 501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 144.549 151.255 83.597  1.00 38.81  ? 501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.432 151.149 89.304  1.00 43.97  ? 502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.269 151.846 89.841  1.00 34.66  ? 502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.592 152.524 91.166  1.00 37.95  ? 502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.101 153.624 91.436  1.00 46.93  ? 502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.098 150.881 90.005  1.00 37.74  ? 502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 137.789 151.578 90.313  1.00 39.19  ? 502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 137.455 152.597 89.239  1.00 41.75  ? 502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.482 153.578 89.701  1.00 38.41  ? 502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.421 154.832 89.274  1.00 39.77  ? 502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 135.494 155.644 89.773  1.00 41.70  ? 502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 137.261 155.292 88.362  1.00 40.17  ? 502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.410 151.887 92.007  1.00 34.19  ? 503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 141.815 152.522 93.256  1.00 30.26  ? 503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 142.611 153.793 92.991  1.00 34.23  ? 503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.386 154.825 93.635  1.00 40.88  ? 503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.626 151.540 94.100  1.00 29.74  ? 503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.764 152.003 95.430  1.00 41.60  ? 503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 143.536 153.742 92.031  1.00 37.79  ? 504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.306 154.928 91.677  1.00 30.30  ? 504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 143.418 156.002 91.060  1.00 41.23  ? 504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 143.615 157.196 91.310  1.00 49.78  ? 504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 145.440 154.550 90.725  1.00 32.04  ? 504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 142.434 155.599 90.252  1.00 44.43  ? 505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 141.512 156.566 89.666  1.00 40.36  ? 505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 140.662 157.239 90.734  1.00 41.87  ? 505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.405 158.445 90.662  1.00 49.05  ? 505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 140.627 155.881 88.627  1.00 39.73  ? 505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 141.317 155.614 87.300  1.00 42.63  ? 505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 140.518 154.689 86.406  1.00 53.05  ? 505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 139.412 154.277 86.814  1.00 50.45  ? 505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 140.995 154.375 85.295  1.00 54.05  ? 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.211 156.475 91.731  1.00 36.89  ? 506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.449 157.058 92.830  1.00 34.58  ? 506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.326 157.999 93.645  1.00 44.50  ? 506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 139.879 159.069 94.074  1.00 52.27  ? 506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 138.837 155.950 93.706  1.00 36.51  ? 506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 137.803 155.149 92.915  1.00 41.25  ? 506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.188 156.542 94.943  1.00 44.66  ? 506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.403 153.852 93.581  1.00 35.38  ? 506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 141.588 157.621 93.870  1.00 41.07  ? 507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.506 158.505 94.580  1.00 37.30  ? 507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 142.726 159.802 93.811  1.00 42.03  ? 507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 142.807 160.883 94.407  1.00 53.07  ? 507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 143.834 157.794 94.828  1.00 39.31  ? 507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 142.835 159.713 92.485  1.00 43.35  ? 508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 142.990 160.908 91.663  1.00 43.01  ? 508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 141.738 161.777 91.696  1.00 47.81  ? 508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 141.829 163.006 91.805  1.00 56.17  ? 508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.328 160.507 90.227  1.00 49.40  ? 508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 142.980 161.553 89.185  1.00 51.98  ? 508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.774 161.347 87.907  1.00 50.92  ? 508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 143.374 162.354 86.842  1.00 49.19  ? 508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 142.929 163.642 87.438  1.00 52.99  ? 508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 140.558 161.159 91.607  1.00 52.58  ? 509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.315 161.915 91.523  1.00 55.38  ? 509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 138.915 162.522 92.862  1.00 57.04  ? 509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 138.250 163.563 92.890  1.00 58.35  ? 509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.199 161.020 90.978  1.00 48.00  ? 509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 137.213 160.511 92.017  1.00 53.22  ? 509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 136.092 159.695 91.405  1.00 62.97  ? 509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 135.637 160.045 90.295  1.00 63.03  ? 509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 135.668 158.702 92.032  1.00 60.36  ? 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.301 161.895 93.974  1.00 49.16  ? 510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.019 162.426 95.299  1.00 47.86  ? 510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.178 163.224 95.876  1.00 50.65  ? 510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 139.982 163.949 96.857  1.00 53.51  ? 510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.654 161.289 96.262  1.00 47.33  ? 510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.521 160.402 95.770  1.00 51.82  ? 510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 136.910 159.600 96.905  1.00 52.51  ? 510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 135.674 158.847 96.442  1.00 49.10  ? 510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 134.630 158.780 97.500  1.00 46.41  ? 510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.371 163.110 95.298  1.00 52.94  ? 511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.522 163.830 95.797  1.00 51.49  ? 511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.132 163.268 97.057  1.00 52.03  ? 511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.015 163.905 97.637  1.00 55.58  ? 511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.691 162.093 97.502  1.00 51.54  ? 512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.197 161.495 98.726  1.00 52.25  ? 512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.448 160.011 98.509  1.00 50.90  ? 512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 142.726 159.343 97.766  1.00 53.91  ? 512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.222 161.689 99.895  1.00 51.31  ? 512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 140.800 161.251 99.594  1.00 51.69  ? 512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 139.930 161.208 100.833 1.00 57.66  ? 512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 140.473 160.972 101.932 1.00 57.43  ? 512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 138.703 161.408 100.708 1.00 53.76  ? 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.486 159.509 99.165  1.00 46.10  ? 513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 144.803 158.091 99.215  1.00 42.35  ? 513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.382 157.535 100.570 1.00 43.68  ? 513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 143.755 158.221 101.382 1.00 52.96  ? 513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.296 157.865 98.966  1.00 41.88  ? 513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.046 158.373 100.075 1.00 44.21  ? 513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 146.734 158.585 97.706  1.00 41.29  ? 513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.725 156.275 100.817 1.00 37.81  ? 514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.498 155.742 102.149 1.00 37.19  ? 514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.600 156.218 103.089 1.00 40.34  ? 514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.682 156.626 102.661 1.00 48.27  ? 514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.408 154.213 102.127 1.00 36.42  ? 514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.693 153.515 101.774 1.00 31.13  ? 514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.010 153.245 100.455 1.00 33.25  ? 514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.560 153.085 102.764 1.00 33.20  ? 514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.179 152.589 100.127 1.00 34.66  ? 514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 147.731 152.428 102.443 1.00 36.17  ? 514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.039 152.179 101.122 1.00 38.55  ? 514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.304 156.187 104.386 1.00 46.70  ? 515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.240 156.722 105.365 1.00 46.80  ? 515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.524 155.904 105.385 1.00 46.65  ? 515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.497 154.672 105.327 1.00 53.85  ? 515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.602 156.748 106.753 1.00 48.57  ? 515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.600 157.875 106.911 1.00 53.25  ? 515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.040 158.323 105.888 1.00 54.04  ? 515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.374 158.315 108.058 1.00 52.90  ? 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.654 156.610 105.464 1.00 39.79  ? 516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 149.982 156.001 105.407 1.00 43.55  ? 516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.191 155.242 104.098 1.00 43.68  ? 516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 150.787 154.165 104.073 1.00 51.50  ? 516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.230 155.088 106.609 1.00 44.70  ? 516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.150 155.786 107.953 1.00 45.29  ? 516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.247 154.815 109.111 1.00 47.16  ? 516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.329 154.323 109.433 1.00 46.78  ? 516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.114 154.530 109.741 1.00 38.15  ? 516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.688 155.805 102.998 1.00 38.39  ? 517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 149.922 155.193 101.694 1.00 37.92  ? 517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.374 155.336 101.258 1.00 41.00  ? 517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 151.907 154.445 100.587 1.00 48.57  ? 517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 148.997 155.808 100.644 1.00 35.30  ? 517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 149.561 155.769 99.241  1.00 41.25  ? 517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.545 154.596 98.499  1.00 37.59  ? 517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.114 156.903 98.662  1.00 42.32  ? 517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.064 154.554 97.221  1.00 39.25  ? 517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 150.636 156.870 97.386  1.00 39.25  ? 517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 150.608 155.693 96.670  1.00 41.93  ? 517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.124 155.659 95.396  1.00 44.35  ? 517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.025 156.443 101.627 1.00 42.49  ? 518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.359 156.736 101.112 1.00 46.15  ? 518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.374 155.678 101.522 1.00 48.99  ? 518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.355 155.452 100.804 1.00 47.24  ? 518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.810 158.117 101.588 1.00 46.06  ? 518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.135 159.281 100.875 1.00 48.75  ? 518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 151.693 159.476 101.305 1.00 56.17  ? 518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 151.353 159.088 102.443 1.00 57.21  ? 518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 150.901 160.019 100.508 1.00 54.46  ? 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.165 155.025 102.663 1.00 38.63  ? 519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.050 153.954 103.076 1.00 33.32  ? 519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 154.753 152.604 102.464 1.00 41.92  ? 519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.562 151.683 102.604 1.00 46.65  ? 519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.615 152.465 101.790 1.00 38.81  ? 520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.233 151.192 101.201 1.00 31.29  ? 520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.071 150.895 99.962  1.00 36.17  ? 520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 154.663 151.786 99.347  1.00 38.19  ? 520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 151.749 151.193 100.840 1.00 30.29  ? 520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.480 152.122 99.806  1.00 40.95  ? 520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.115 149.612 99.597  1.00 36.75  ? 521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 154.866 149.198 98.420  1.00 37.83  ? 521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.252 149.716 97.126  1.00 38.87  ? 521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 154.929 149.715 96.093  1.00 43.15  ? 521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 154.974 147.674 98.371  1.00 36.70  ? 521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.668 147.105 98.226  1.00 33.09  ? 521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.610 147.146 99.643  1.00 35.99  ? 521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 152.989 150.150 97.155  1.00 38.84  ? 522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.410 150.794 95.981  1.00 35.18  ? 522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.127 152.100 95.666  1.00 39.87  ? 522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.422 152.392 94.501  1.00 43.12  ? 522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 150.919 151.051 96.196  1.00 29.19  ? 522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.103 149.817 96.497  1.00 33.80  ? 522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 149.881 148.853 95.524  1.00 31.87  ? 522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.540 149.624 97.750  1.00 39.23  ? 522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.129 147.727 95.794  1.00 33.37  ? 522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 148.785 148.504 98.028  1.00 39.71  ? 522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.585 147.557 97.047  1.00 39.52  ? 522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 147.835 146.437 97.323  1.00 46.77  ? 522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.414 152.902 96.694  1.00 44.47  ? 523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.093 154.174 96.477  1.00 42.45  ? 523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 155.546 153.966 96.073  1.00 49.75  ? 523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.053 154.657 95.183  1.00 54.92  ? 523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.003 155.037 97.735  1.00 41.07  ? 523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.231 153.021 96.715  1.00 47.54  ? 524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 157.627 152.749 96.402  1.00 46.34  ? 524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 157.807 151.965 95.110  1.00 47.22  ? 524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 158.933 151.880 94.609  1.00 53.29  ? 524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.290 151.986 97.553  1.00 47.83  ? 524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 157.965 150.594 97.455  1.00 48.95  ? 524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 157.809 152.521 98.892  1.00 43.16  ? 524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 156.736 151.395 94.562  1.00 42.22  ? 525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 156.824 150.602 93.356  1.00 44.22  ? 525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.275 149.174 93.558  1.00 43.67  ? 525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.396 148.436 92.572  1.00 46.67  ? 525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 157.531 148.759 94.800  1.00 45.28  ? 526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 157.954 147.389 95.066  1.00 47.81  ? 526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 156.840 146.383 94.806  1.00 46.09  ? 526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.128 145.222 94.496  1.00 47.25  ? 526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.450 147.272 96.509  1.00 44.96  ? 526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.021 145.912 96.879  1.00 48.42  ? 526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 158.664 145.496 98.293  1.00 57.36  ? 526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 158.967 146.260 99.233  1.00 51.74  ? 526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 158.079 144.406 98.464  1.00 51.04  ? 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 155.578 146.805 94.918  1.00 41.50  ? 527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 154.465 145.896 94.672  1.00 41.05  ? 527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.421 145.452 93.215  1.00 44.39  ? 527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.114 144.289 92.923  1.00 48.98  ? 527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.149 146.567 95.069  1.00 35.33  ? 527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 151.933 145.684 94.910  1.00 42.05  ? 527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.552 144.813 95.921  1.00 44.17  ? 527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.166 145.725 93.755  1.00 37.98  ? 527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.441 144.003 95.784  1.00 42.81  ? 527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.055 144.919 93.609  1.00 41.24  ? 527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 149.697 144.060 94.625  1.00 44.88  ? 527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 148.590 143.256 94.485  1.00 45.51  ? 527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 154.726 146.358 92.290  1.00 48.42  ? 528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 154.597 146.105 90.862  1.00 43.23  ? 528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 155.821 145.427 90.260  1.00 47.04  ? 528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 155.905 145.318 89.033  1.00 54.50  ? 528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.326 147.417 90.120  1.00 44.57  ? 528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.121 148.162 90.618  1.00 46.64  ? 528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.233 149.082 91.647  1.00 41.85  ? 528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 151.877 147.951 90.050  1.00 45.32  ? 528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 152.127 149.769 92.103  1.00 43.05  ? 528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 150.768 148.637 90.502  1.00 42.96  ? 528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 150.894 149.546 91.530  1.00 42.71  ? 528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 156.767 144.973 91.086  1.00 51.93  ? 529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.008 144.412 90.558  1.00 50.00  ? 529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 157.743 143.168 89.718  1.00 49.88  ? 529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.185 143.074 88.566  1.00 53.45  ? 529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 158.964 144.093 91.706  1.00 49.18  ? 529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 159.599 145.335 92.298  1.00 55.63  ? 529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 159.427 146.426 91.717  1.00 50.84  ? 529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.271 145.219 93.344  1.00 58.28  ? 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.011 142.202 90.276  1.00 53.15  ? 530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 156.712 140.981 89.540  1.00 53.82  ? 530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 155.757 141.226 88.381  1.00 56.94  ? 530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 155.699 140.407 87.458  1.00 57.04  ? 530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.130 139.926 90.481  1.00 51.75  ? 530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 154.615 139.877 90.495  1.00 51.10  ? 530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.102 138.998 91.615  1.00 51.95  ? 530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 152.597 138.855 91.542  1.00 52.45  ? 530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 151.968 139.145 92.858  1.00 53.72  ? 530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.011 142.328 88.407  1.00 55.37  ? 531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.099 142.651 87.320  1.00 45.68  ? 531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 154.792 143.360 86.168  1.00 48.17  ? 531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.378 143.198 85.013  1.00 53.85  ? 531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 152.949 143.513 87.843  1.00 46.77  ? 531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 151.939 142.741 88.658  1.00 51.10  ? 531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.228 141.690 88.096  1.00 49.11  ? 531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 151.696 143.061 89.985  1.00 50.09  ? 531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 150.303 140.980 88.831  1.00 46.59  ? 531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 150.772 142.356 90.729  1.00 47.38  ? 531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.079 141.316 90.147  1.00 49.47  ? 531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.158 140.610 90.884  1.00 51.98  ? 531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 155.836 144.143 86.451  1.00 51.17  ? 532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 156.629 144.761 85.393  1.00 51.74  ? 532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 157.797 143.890 84.962  1.00 52.90  ? 532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.483 144.229 83.984  1.00 50.71  ? 532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.161 146.142 85.826  1.00 48.81  ? 532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.017 147.027 86.297  1.00 50.31  ? 532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.214 145.993 86.909  1.00 49.02  ? 532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.054 142.778 85.657  1.00 55.71  ? 533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.131 141.873 85.284  1.00 55.89  ? 533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 158.654 140.562 84.676  1.00 57.42  ? 533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.432 139.914 83.970  1.00 56.53  ? 533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.008 141.559 86.505  1.00 54.83  ? 533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 159.568 140.381 87.158  1.00 54.84  ? 533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.412 140.157 84.926  1.00 53.95  ? 534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 156.876 138.900 84.426  1.00 54.46  ? 534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 155.605 139.156 83.630  1.00 55.43  ? 534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 154.778 139.990 84.013  1.00 56.33  ? 534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 156.581 137.926 85.574  1.00 53.89  ? 534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 157.717 137.856 86.447  1.00 54.16  ? 534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.281 136.535 85.036  1.00 56.03  ? 534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 155.454 138.437 82.520  1.00 59.14  ? 535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.254 138.515 81.702  1.00 58.47  ? 535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.273 137.437 82.139  1.00 61.54  ? 535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 153.621 136.253 82.189  1.00 58.33  ? 535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 154.594 138.353 80.219  1.00 58.62  ? 535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 153.391 138.560 79.320  1.00 63.60  ? 535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 152.432 139.231 79.752  1.00 62.50  ? 535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 153.406 138.051 78.179  1.00 64.67  ? 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.046 137.850 82.458  1.00 52.27  ? 536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.016 136.942 82.942  1.00 49.10  ? 536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 149.976 136.620 81.875  1.00 51.89  ? 536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 148.877 136.163 82.207  1.00 56.40  ? 536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.346 137.524 84.186  1.00 45.15  ? 536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.274 137.668 85.357  1.00 43.93  ? 536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 151.513 136.599 86.202  1.00 44.50  ? 536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 151.915 138.868 85.608  1.00 50.26  ? 536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 152.369 136.726 87.278  1.00 46.60  ? 536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 152.771 138.999 86.682  1.00 54.02  ? 536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 152.997 137.927 87.518  1.00 50.30  ? 536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.298 136.855 80.606  1.00 53.66  ? 537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 149.423 136.436 79.526  1.00 54.33  ? 537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 149.356 134.909 79.478  1.00 58.32  ? 537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 150.297 134.228 79.892  1.00 56.93  ? 537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 149.924 136.981 78.191  1.00 49.65  ? 537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.278 138.201 77.866  1.00 55.49  ? 537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.245 134.349 78.999  1.00 56.21  ? 538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.101 132.889 78.998  1.00 48.90  ? 538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.183 132.210 78.171  1.00 56.49  ? 538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 149.570 132.686 77.103  1.00 57.91  ? 538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 146.711 132.672 78.388  1.00 51.92  ? 538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 145.990 133.951 78.625  1.00 53.20  ? 538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.032 135.018 78.499  1.00 54.54  ? 538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 149.671 131.083 78.684  1.00 60.01  ? 539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 150.654 130.266 77.987  1.00 57.30  ? 539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.017 129.160 77.158  1.00 60.31  ? 539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 150.737 128.425 76.475  1.00 61.85  ? 539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 151.640 129.655 78.987  1.00 57.22  ? 539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 151.987 130.559 80.158  1.00 57.55  ? 539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.160 131.467 79.829  1.00 60.37  ? 539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 153.117 132.745 80.652  1.00 62.09  ? 539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.442 133.947 79.836  1.00 59.31  ? 539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 148.696 129.024 77.205  1.00 58.68  ? 540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 147.976 127.998 76.465  1.00 59.13  ? 540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.070 128.654 75.435  1.00 60.72  ? 540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 146.403 129.653 75.727  1.00 59.19  ? 540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 147.151 127.114 77.404  1.00 57.11  ? 540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 147.988 126.231 78.301  1.00 59.38  ? 540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 148.471 125.011 77.852  1.00 60.25  ? 540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 148.298 126.621 79.596  1.00 60.84  ? 540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.237 124.202 78.668  1.00 58.93  ? 540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.064 125.820 80.420  1.00 60.71  ? 540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 149.530 124.612 79.950  1.00 59.29  ? 540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 150.294 123.809 80.766  1.00 60.27  ? 540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.056 128.092 74.223  1.00 61.29  ? 541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 146.205 128.627 73.167  1.00 60.55  ? 541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 144.731 128.510 73.537  1.00 61.43  ? 541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 143.939 129.417 73.259  1.00 61.02  ? 541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 146.495 127.906 71.848  1.00 61.14  ? 541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 145.489 128.171 70.738  1.00 62.34  ? 541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 144.399 127.117 70.668  1.00 65.81  ? 541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 144.735 125.915 70.620  1.00 59.78  ? 541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 143.208 127.491 70.660  1.00 67.72  ? 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 144.345 127.396 74.164  1.00 58.89  ? 542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 142.964 127.232 74.602  1.00 57.44  ? 542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 142.584 128.289 75.630  1.00 57.53  ? 542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 141.487 128.858 75.573  1.00 55.85  ? 542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 142.762 125.828 75.173  1.00 58.70  ? 542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 141.539 125.684 76.065  1.00 60.09  ? 542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 141.558 124.364 76.818  1.00 59.58  ? 542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.158 123.792 76.959  1.00 59.04  ? 542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.118 124.857 76.930  1.00 58.01  ? 542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 143.480 128.569 76.578  1.00 57.68  ? 543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 143.206 129.584 77.588  1.00 52.13  ? 543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 143.214 130.976 76.969  1.00 51.95  ? 543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 142.383 131.826 77.308  1.00 52.34  ? 543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 144.215 129.467 78.744  1.00 51.29  ? 543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.073 128.111 79.435  1.00 54.97  ? 543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.021 130.597 79.737  1.00 51.95  ? 543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 142.655 127.779 79.840  1.00 52.11  ? 543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.155 131.234 76.056  1.00 54.03  ? 544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 144.223 132.543 75.413  1.00 53.88  ? 544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 142.964 132.842 74.609  1.00 54.40  ? 544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 142.585 134.010 74.465  1.00 55.25  ? 544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 145.457 132.624 74.516  1.00 53.89  ? 544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 142.307 131.808 74.079  1.00 58.79  ? 545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.060 132.021 73.352  1.00 60.82  ? 545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 139.927 132.420 74.288  1.00 61.25  ? 545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 138.977 133.084 73.860  1.00 63.10  ? 545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 140.686 130.763 72.571  1.00 62.29  ? 545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 141.596 130.522 71.385  1.00 64.75  ? 545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 142.292 131.429 70.927  1.00 62.73  ? 545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 141.598 129.294 70.879  1.00 62.58  ? 545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.005 132.019 75.559  1.00 54.32  ? 546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 138.982 132.407 76.524  1.00 53.50  ? 546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 138.987 133.908 76.769  1.00 57.42  ? 546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 137.935 134.499 77.038  1.00 59.72  ? 546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.188 131.655 77.839  1.00 50.10  ? 546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 138.488 130.309 78.044  1.00 54.20  ? 546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 138.477 129.467 76.777  1.00 56.16  ? 546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 139.144 129.552 79.184  1.00 52.60  ? 546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.156 134.541 76.679  1.00 53.07  ? 547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 140.301 135.973 76.893  1.00 49.44  ? 547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.216 136.771 75.599  1.00 56.60  ? 547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 140.467 137.981 75.613  1.00 60.21  ? 547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 141.628 136.266 77.598  1.00 49.03  ? 547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 141.666 135.821 79.030  1.00 50.53  ? 547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.257 136.669 80.044  1.00 53.90  ? 547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.109 134.554 79.364  1.00 50.79  ? 547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.293 136.264 81.362  1.00 46.68  ? 547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.145 134.143 80.681  1.00 49.50  ? 547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 141.736 134.999 81.680  1.00 46.81  ? 547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 139.881 136.123 74.485  1.00 65.66  ? 548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 139.769 136.824 73.213  1.00 64.60  ? 548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 138.692 137.899 73.288  1.00 66.86  ? 548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 137.627 137.696 73.879  1.00 67.31  ? 548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 139.449 135.836 72.091  1.00 65.90  ? 548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.827 136.328 70.705  1.00 69.13  ? 548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 138.629 136.453 69.784  1.00 72.30  ? 548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 137.491 136.524 70.293  1.00 69.79  ? 548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 138.826 136.480 68.551  1.00 69.47  ? 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 138.975 139.049 72.682  1.00 64.44  ? 549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.092 140.190 72.782  1.00 66.47  ? 549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.293 141.037 74.015  1.00 66.97  ? 549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 137.534 141.991 74.223  1.00 65.27  ? 549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.287 140.718 74.839  1.00 66.50  ? 550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 139.596 141.474 76.044  1.00 60.87  ? 550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.086 141.773 76.064  1.00 66.04  ? 550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 141.905 140.875 75.841  1.00 63.29  ? 550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.193 140.700 77.302  1.00 57.89  ? 550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 137.947 141.233 77.981  1.00 63.37  ? 550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 137.676 140.461 79.583  1.00 76.27  ? 550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 137.877 138.734 79.155  1.00 60.98  ? 550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 141.436 143.028 76.330  1.00 68.85  ? 551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 142.834 143.450 76.345  1.00 62.32  ? 551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 143.485 142.943 77.625  1.00 59.40  ? 551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.233 143.460 78.715  1.00 58.20  ? 551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 142.944 144.966 76.236  1.00 60.07  ? 551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.309 145.493 76.550  1.00 65.07  ? 551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.426 145.144 75.823  1.00 64.51  ? 551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 144.739 146.339 77.517  1.00 64.23  ? 551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 146.484 145.753 76.326  1.00 64.12  ? 551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.095 146.484 77.355  1.00 65.38  ? 551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 144.328 141.924 77.494  1.00 54.39  ? 552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.081 141.391 78.624  1.00 55.27  ? 552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.216 142.358 78.939  1.00 54.53  ? 552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.023 142.670 78.051  1.00 55.67  ? 552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 145.614 139.982 78.325  1.00 56.60  ? 552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 144.472 139.066 77.883  1.00 57.66  ? 552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 146.310 139.407 79.543  1.00 51.37  ? 552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 144.934 137.714 77.405  1.00 55.53  ? 552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.308 142.868 80.167  1.00 57.23  ? 553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 147.397 143.794 80.500  1.00 54.42  ? 553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 148.759 143.147 80.299  1.00 54.93  ? 553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 148.971 141.979 80.631  1.00 55.93  ? 553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.142 144.124 81.975  1.00 50.56  ? 553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 145.692 143.840 82.182  1.00 44.71  ? 553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 145.374 142.684 81.289  1.00 51.74  ? 553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 149.685 143.923 79.751  1.00 60.02  ? 554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.027 143.458 79.458  1.00 59.22  ? 554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.011 144.050 80.465  1.00 60.63  ? 554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 151.627 144.740 81.414  1.00 63.51  ? 554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 151.406 143.817 78.021  1.00 57.21  ? 554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 151.331 145.237 77.846  1.00 55.90  ? 554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 150.465 143.140 77.038  1.00 56.45  ? 554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.299 143.768 80.263  1.00 57.27  ? 555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.328 144.347 81.119  1.00 55.13  ? 555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.358 145.865 80.990  1.00 60.53  ? 555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 154.477 146.581 81.992  1.00 58.04  ? 555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 155.689 143.738 80.773  1.00 59.69  ? 555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 155.826 142.471 81.428  1.00 58.05  ? 555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.822 144.650 81.208  1.00 60.76  ? 555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.237 146.377 79.763  1.00 63.49  ? 556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.209 147.823 79.563  1.00 61.43  ? 556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 152.962 148.442 80.182  1.00 63.95  ? 556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.027 149.535 80.758  1.00 64.21  ? 556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.312 148.145 78.068  1.00 59.92  ? 556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 153.222 147.537 77.190  1.00 63.59  ? 556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 152.056 148.478 76.937  1.00 67.77  ? 556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 151.918 149.482 77.666  1.00 70.57  ? 556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 151.273 148.210 76.002  1.00 61.66  ? 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 151.817 147.762 80.078  1.00 57.54  ? 557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 150.603 148.258 80.720  1.00 55.26  ? 557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 150.769 148.309 82.233  1.00 56.74  ? 557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.314 149.255 82.886  1.00 58.32  ? 557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.410 147.382 80.339  1.00 56.84  ? 557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 148.993 147.564 78.895  1.00 60.91  ? 557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.426 148.552 78.269  1.00 61.34  ? 557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 148.232 146.716 78.385  1.00 61.82  ? 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.426 147.301 82.807  1.00 48.37  ? 558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 151.697 147.323 84.238  1.00 41.99  ? 558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 152.671 148.433 84.611  1.00 47.18  ? 558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 152.550 149.016 85.691  1.00 52.59  ? 558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.229 145.966 84.692  1.00 49.69  ? 558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.153 145.042 85.160  1.00 48.43  ? 558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 150.677 143.943 84.510  1.00 46.92  ? 558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.412 145.139 86.381  1.00 47.90  ? 558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 149.688 143.346 85.254  1.00 46.11  ? 558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.508 144.061 86.408  1.00 43.52  ? 558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.432 146.029 87.458  1.00 51.92  ? 558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 148.630 143.851 87.468  1.00 43.47  ? 558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.560 145.819 88.508  1.00 47.46  ? 558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 148.671 144.740 88.505  1.00 46.53  ? 558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 153.637 148.740 83.742  1.00 55.71  ? 559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 154.523 149.872 84.001  1.00 56.17  ? 559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 153.755 151.188 83.997  1.00 53.40  ? 559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 153.984 152.055 84.851  1.00 56.58  ? 559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 155.650 149.907 82.969  1.00 55.16  ? 559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 156.805 148.969 83.272  1.00 54.26  ? 559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 157.829 148.978 82.152  1.00 56.16  ? 559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 158.595 147.669 82.092  1.00 58.45  ? 559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.067 147.881 82.114  1.00 58.09  ? 559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 152.842 151.358 83.037  1.00 48.41  ? 560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.010 152.559 83.022  1.00 49.44  ? 560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.140 152.639 84.270  1.00 52.94  ? 560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 150.962 153.720 84.839  1.00 53.45  ? 560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.144 152.607 81.762  1.00 53.36  ? 560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 151.884 152.329 80.469  1.00 58.47  ? 560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 152.773 153.496 80.079  1.00 60.20  ? 560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 153.943 153.035 79.225  1.00 57.76  ? 560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 155.226 153.063 79.981  1.00 54.33  ? 560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 150.584 151.507 84.706  1.00 49.46  ? 561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 149.785 151.504 85.928  1.00 43.34  ? 561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 150.633 151.852 87.146  1.00 45.96  ? 561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.175 152.566 88.044  1.00 50.11  ? 561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.108 150.149 86.121  1.00 47.24  ? 561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.241 150.078 87.380  1.00 45.62  ? 561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.139 151.117 87.307  1.00 45.22  ? 561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 147.664 148.692 87.578  1.00 45.34  ? 561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 151.864 151.342 87.202  1.00 42.08  ? 562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 152.760 151.672 88.306  1.00 42.97  ? 562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.074 153.162 88.331  1.00 45.45  ? 562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.075 153.786 89.399  1.00 48.50  ? 562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.044 150.851 88.193  1.00 45.41  ? 562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.138 151.256 89.161  1.00 45.24  ? 562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.431 150.519 88.851  1.00 45.46  ? 562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 157.551 150.948 89.779  1.00 47.21  ? 562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 158.637 149.932 89.833  1.00 50.20  ? 562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.339 153.749 87.162  1.00 50.23  ? 563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 153.576 155.189 87.097  1.00 47.37  ? 563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.337 155.972 87.518  1.00 51.47  ? 563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 152.436 156.976 88.234  1.00 54.21  ? 563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.010 155.586 85.687  1.00 42.90  ? 563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.158 155.524 87.080  1.00 47.79  ? 564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 149.915 156.191 87.448  1.00 42.92  ? 564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 149.688 156.137 88.953  1.00 48.08  ? 564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.251 157.121 89.560  1.00 51.87  ? 564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 148.747 155.546 86.700  1.00 47.27  ? 564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 147.461 156.312 86.789  1.00 47.04  ? 564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.204 157.364 85.927  1.00 51.09  ? 564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 146.500 155.971 87.724  1.00 47.04  ? 564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.018 158.066 86.003  1.00 53.73  ? 564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.314 156.669 87.805  1.00 49.38  ? 564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.072 157.718 86.944  1.00 54.59  ? 564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 149.982 154.994 89.572  1.00 46.65  ? 565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 149.834 154.859 91.018  1.00 43.04  ? 565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 150.845 155.736 91.744  1.00 47.66  ? 565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 150.523 156.371 92.754  1.00 53.70  ? 565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 149.965 153.380 91.425  1.00 42.58  ? 565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.170 153.249 92.925  1.00 42.44  ? 565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 148.735 152.609 90.988  1.00 48.48  ? 565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.082 155.788 91.244  1.00 55.07  ? 566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.095 156.627 91.877  1.00 52.82  ? 566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 152.704 158.098 91.824  1.00 52.58  ? 566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 152.886 158.833 92.801  1.00 55.31  ? 566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 154.451 156.405 91.210  1.00 48.81  ? 566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.163 158.546 90.690  1.00 55.47  ? 567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 151.782 159.950 90.561  1.00 56.91  ? 567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.517 160.282 91.346  1.00 55.82  ? 567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.453 161.329 92.000  1.00 58.14  ? 567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 151.603 160.313 89.085  1.00 54.08  ? 567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.836 160.930 88.440  1.00 59.80  ? 567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 154.113 160.175 88.752  1.00 62.56  ? 567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 154.262 159.027 88.283  1.00 55.90  ? 567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 154.971 160.729 89.472  1.00 58.65  ? 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 149.506 159.413 91.302  1.00 54.74  ? 568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.191 159.736 91.839  1.00 53.36  ? 568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 147.851 159.016 93.136  1.00 49.35  ? 568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 146.894 159.413 93.807  1.00 56.22  ? 568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.109 159.428 90.795  1.00 49.11  ? 568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.099 160.382 89.643  1.00 51.81  ? 568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 147.146 161.749 89.810  1.00 54.58  ? 568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.064 160.167 88.308  1.00 52.80  ? 568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 147.129 162.336 88.627  1.00 56.11  ? 568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.081 161.398 87.698  1.00 53.81  ? 568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 148.594 157.983 93.508  1.00 41.72  ? 569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.305 157.271 94.733  1.00 40.60  ? 569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.290 156.161 94.542  1.00 39.88  ? 569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 146.868 155.832 93.431  1.00 50.17  ? 569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 146.900 155.567 95.668  1.00 31.84  ? 570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 145.950 154.463 95.681  1.00 34.56  ? 570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 144.958 154.683 96.811  1.00 36.52  ? 570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.360 154.916 97.954  1.00 48.33  ? 570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 146.675 153.123 95.842  1.00 37.10  ? 570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 146.990 152.445 94.520  1.00 37.42  ? 570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.050 150.652 94.634  1.00 53.38  ? 570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 145.662 150.345 95.710  1.00 34.63  ? 570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 143.665 154.614 96.490  1.00 26.83  ? 571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.633 154.961 97.461  1.00 28.12  ? 571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.407 153.870 98.499  1.00 34.41  ? 571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.081 154.178 99.650  1.00 40.42  ? 571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.320 155.267 96.744  1.00 33.35  ? 571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.274 155.901 97.631  1.00 33.63  ? 571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.376 157.231 98.013  1.00 38.21  ? 571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.187 155.171 98.088  1.00 30.90  ? 571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.424 157.816 98.822  1.00 39.06  ? 571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.231 155.747 98.899  1.00 33.12  ? 571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.353 157.069 99.263  1.00 42.68  ? 571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.402 157.648 100.070 1.00 44.61  ? 571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.565 152.605 98.123  1.00 37.45  ? 572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.283 151.481 99.006  1.00 25.80  ? 572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.586 150.836 99.449  1.00 32.07  ? 572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.443 150.526 98.615  1.00 40.61  ? 572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.399 150.440 98.315  1.00 24.66  ? 572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.180 151.014 97.664  1.00 29.05  ? 572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.146 151.365 96.332  1.00 32.72  ? 572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 138.952 151.293 98.158  1.00 27.16  ? 572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 138.950 151.838 96.035  1.00 31.01  ? 572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.206 151.805 97.126  1.00 34.42  ? 572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 143.733 150.637 100.758 1.00 26.98  ? 573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 144.877 149.884 101.258 1.00 24.76  ? 573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 144.828 148.441 100.776 1.00 33.92  ? 573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 145.854 147.868 100.393 1.00 36.98  ? 573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 144.917 149.942 102.783 1.00 27.18  ? 573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 143.646 149.650 103.330 1.00 36.29  ? 573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.640 147.842 100.784 1.00 30.04  ? 574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.430 146.483 100.316 1.00 20.58  ? 574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.213 146.456 99.405  1.00 15.45  ? 574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.246 147.192 99.617  1.00 21.57  ? 574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.247 145.513 101.487 1.00 21.19  ? 574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.346 145.614 102.518 1.00 18.85  ? 574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.260 146.520 103.565 1.00 18.38  ? 574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.470 144.808 102.441 1.00 20.76  ? 574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.264 146.623 104.504 1.00 19.42  ? 574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.478 144.901 103.377 1.00 19.71  ? 574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.369 145.809 104.405 1.00 23.50  ? 574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.371 145.904 105.340 1.00 33.02  ? 574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.271 145.611 98.388  1.00 14.94  ? 575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.210 145.592 97.387  1.00 18.90  ? 575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 140.614 144.214 97.157  1.00 29.71  ? 575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.402 144.104 96.957  1.00 42.75  ? 575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 141.738 146.135 96.056  1.00 26.88  ? 575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.279 147.544 96.115  1.00 21.58  ? 575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.353 147.736 95.068  1.00 27.32  ? 575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 144.569 147.006 95.405  1.00 24.51  ? 575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 144.955 145.880 94.819  1.00 22.68  ? 575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 146.087 145.301 95.209  1.00 26.27  ? 575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 144.239 145.320 93.859  1.00 25.20  ? 575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.427 143.162 97.177  1.00 20.15  ? 576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.002 141.836 96.751  1.00 14.35  ? 576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.111 140.856 97.906  1.00 11.89  ? 576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.161 140.758 98.546  1.00 37.09  ? 576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 141.849 141.342 95.577  1.00 17.08  ? 576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.007 142.272 94.376  1.00 17.62  ? 576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 142.921 141.636 93.351  1.00 22.33  ? 576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 140.661 142.597 93.761  1.00 20.29  ? 576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.028 140.131 98.166  1.00 12.50  ? 577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.047 139.015 99.101  1.00 10.50  ? 577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 138.913 138.078 98.721  1.00 31.78  ? 577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 137.784 138.524 98.502  1.00 35.63  ? 577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 139.918 139.490 100.554 1.00 19.65  ? 577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.257 139.903 101.114 1.00 34.40  ? 577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.219 136.790 98.625  1.00 31.41  ? 578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.282 135.798 98.116  1.00 20.64  ? 578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 137.601 135.149 99.316  1.00 24.84  ? 578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.174 134.290 99.990  1.00 27.87  ? 578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 138.977 134.774 97.218  1.00 17.25  ? 578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 139.540 135.470 95.980  1.00 15.06  ? 578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.011 133.690 96.800  1.00 21.69  ? 578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.258 134.547 95.041  1.00 25.43  ? 578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.368 135.572 99.580  1.00 32.25  ? 579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 135.539 135.023 100.636 1.00 20.17  ? 579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.015 133.646 100.238 1.00 38.31  ? 579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.085 133.262 99.069  1.00 50.08  ? 579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 134.381 135.973 100.927 1.00 25.24  ? 579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 134.513 132.863 101.199 1.00 38.23  ? 580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 133.936 131.555 100.846 1.00 33.73  ? 580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 132.719 131.629 99.931  1.00 37.60  ? 580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.432 130.631 99.258  1.00 46.73  ? 580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 133.573 130.946 102.209 1.00 33.95  ? 580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 133.561 132.088 103.161 1.00 35.84  ? 580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 134.586 133.046 102.657 1.00 37.39  ? 580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.003 132.760 99.884  1.00 31.62  ? 581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 130.867 132.933 98.978  1.00 41.97  ? 581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 129.856 131.803 99.119  1.00 42.93  ? 581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.715 130.977 98.212  1.00 45.35  ? 581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.313 133.039 97.516  1.00 42.01  ? 581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.569 131.731 96.994  1.00 42.32  ? 581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.554 133.908 97.382  1.00 40.23  ? 581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.152 131.753 100.246 1.00 40.88  ? 582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.346 130.596 100.576 1.00 45.20  ? 582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 126.937 130.674 100.026 1.00 50.02  ? 582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 126.740 130.494 98.821  1.00 55.45  ? 582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 125.950 130.919 100.887 1.00 48.83  ? 583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 124.550 130.851 100.485 1.00 52.47  ? 583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.207 131.763 99.312  1.00 48.35  ? 583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 123.251 131.470 98.586  1.00 46.73  ? 583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 123.649 131.191 101.675 1.00 57.24  ? 583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 124.185 130.680 102.882 1.00 53.92  ? 583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 124.953 132.851 99.104  1.00 44.89  ? 584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 124.710 133.712 97.951  1.00 44.18  ? 584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.215 133.109 96.649  1.00 43.81  ? 584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 124.852 133.596 95.572  1.00 48.54  ? 584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 125.349 135.100 98.167  1.00 47.53  ? 584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 124.636 136.157 97.321  1.00 41.65  ? 584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 126.835 135.066 97.843  1.00 46.46  ? 584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 123.352 136.668 97.916  1.00 46.39  ? 584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.035 132.057 96.713  1.00 41.33  ? 585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 126.486 131.405 95.488  1.00 37.26  ? 585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.340 130.691 94.788  1.00 42.76  ? 585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.352 130.555 93.560  1.00 46.87  ? 585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.617 130.425 95.792  1.00 37.31  ? 585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.192 129.428 96.705  1.00 35.85  ? 585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.352 130.217 95.550  1.00 50.08  ? 586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.166 129.623 94.942  1.00 39.24  ? 586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.424 130.645 94.093  1.00 37.77  ? 586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.038 130.361 92.954  1.00 48.40  ? 586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.243 129.070 96.027  1.00 44.17  ? 586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 122.840 127.954 96.847  1.00 44.42  ? 586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 122.973 126.680 96.323  1.00 47.47  ? 586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.268 128.178 98.147  1.00 48.37  ? 586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.516 125.658 97.071  1.00 51.97  ? 586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 123.814 127.161 98.903  1.00 49.90  ? 586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 123.936 125.902 98.359  1.00 52.52  ? 586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 124.480 124.882 99.106  1.00 50.06  ? 586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.236 131.853 94.630  1.00 39.05  ? 587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 121.452 132.876 93.944  1.00 37.69  ? 587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.113 133.268 92.630  1.00 43.46  ? 587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 121.435 133.523 91.628  1.00 44.39  ? 587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.251 134.094 94.863  1.00 36.23  ? 587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 120.224 135.036 94.272  1.00 41.13  ? 587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 120.832 133.642 96.251  1.00 41.19  ? 587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 123.442 133.320 92.611  1.00 48.46  ? 588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.176 133.642 91.395  1.00 44.67  ? 588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.352 132.443 90.477  1.00 43.97  ? 588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 124.937 132.596 89.399  1.00 49.71  ? 588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 125.549 134.219 91.742  1.00 33.93  ? 588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 125.504 135.631 92.284  1.00 36.67  ? 588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 125.727 136.669 91.205  1.00 44.23  ? 588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 126.584 136.506 90.338  1.00 38.48  ? 588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 124.953 137.746 91.251  1.00 53.53  ? 588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 123.853 131.271 90.869  1.00 43.26  ? 589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.064 130.029 90.131  1.00 45.49  ? 589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 125.551 129.830 89.853  1.00 46.13  ? 589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.010 129.818 88.710  1.00 49.16  ? 589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.245 130.007 88.839  1.00 46.89  ? 589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 121.870 129.797 89.114  1.00 52.63  ? 589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.306 129.683 90.939  1.00 42.71  ? 590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 127.754 129.621 90.868  1.00 41.02  ? 590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.280 128.627 91.890  1.00 45.19  ? 590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 127.625 128.322 92.889  1.00 46.06  ? 590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 128.383 130.995 91.120  1.00 39.33  ? 590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 128.712 131.160 92.487  1.00 42.53  ? 590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.477 128.117 91.619  1.00 37.84  ? 591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.195 127.339 92.613  1.00 41.74  ? 591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 130.765 128.266 93.681  1.00 36.31  ? 591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.086 129.428 93.420  1.00 34.44  ? 591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.311 126.529 91.958  1.00 45.25  ? 591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.397 127.397 91.615  1.00 48.33  ? 591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 130.797 125.853 90.699  1.00 32.44  ? 591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 130.885 127.743 94.897  1.00 36.87  ? 592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.277 128.574 96.026  1.00 40.13  ? 592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 132.753 128.940 95.938  1.00 44.57  ? 592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 133.622 128.063 95.935  1.00 50.09  ? 592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 130.989 127.852 97.340  1.00 42.62  ? 592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.027 130.239 95.866  1.00 41.45  ? 593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.386 130.794 95.918  1.00 29.47  ? 593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.189 130.253 94.735  1.00 28.69  ? 593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 134.623 129.876 93.700  1.00 40.64  ? 593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 134.992 130.504 97.281  1.00 39.81  ? 593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.189 131.230 97.481  1.00 37.31  ? 593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 136.514 130.220 94.875  1.00 33.33  ? 594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 137.386 129.561 93.914  1.00 28.44  ? 594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 137.639 128.109 94.297  1.00 35.43  ? 594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 138.438 127.427 93.649  1.00 37.18  ? 594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 138.709 130.326 93.755  1.00 31.02  ? 594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 138.457 131.699 93.153  1.00 26.52  ? 594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 139.411 130.454 95.097  1.00 35.26  ? 594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 136.975 127.623 95.342  1.00 37.79  ? 595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.128 126.245 95.768  1.00 35.79  ? 595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 136.507 125.298 94.744  1.00 46.88  ? 595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 135.552 125.658 94.050  1.00 51.45  ? 595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 136.463 126.029 97.125  1.00 38.47  ? 595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 137.303 126.339 98.370  1.00 44.15  ? 595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.076 126.006 98.293  1.00 53.95  ? 595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.710 127.551 97.647  1.00 39.89  ? 595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.031 124.081 94.628  1.00 46.81  ? 596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 136.350 123.062 93.826  1.00 39.88  ? 596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.070 122.598 94.506  1.00 48.37  ? 596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 134.894 122.721 95.720  1.00 55.08  ? 596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 137.379 121.932 93.736  1.00 43.59  ? 596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.241 122.114 94.937  1.00 43.86  ? 596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.298 123.590 95.196  1.00 45.75  ? 596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.161 122.060 93.692  1.00 50.12  ? 597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 132.853 121.658 94.195  1.00 49.73  ? 597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 132.993 120.430 95.086  1.00 51.21  ? 597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 133.731 119.487 94.771  1.00 53.76  ? 597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 131.884 121.399 93.030  1.00 48.71  ? 597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 132.396 120.271 92.133  1.00 46.58  ? 597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 131.692 122.665 92.217  1.00 49.80  ? 597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 131.337 119.681 91.239  1.00 46.60  ? 597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 132.290 120.447 96.220  1.00 59.60  ? 598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 132.348 119.317 97.143  1.00 60.53  ? 598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 131.644 118.097 96.562  1.00 62.81  ? 598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.178 116.982 96.599  1.00 66.58  ? 598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 131.730 119.706 98.485  1.00 58.98  ? 598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 132.667 120.471 99.402  1.00 60.68  ? 598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 131.836 121.125 100.861 1.00 77.83  ? 598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.735 122.863 100.445 1.00 61.42  ? 598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 130.445 118.290 96.021  1.00 56.29  ? 599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 129.667 117.211 95.432  1.00 60.39  ? 599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.071 117.698 94.122  1.00 61.57  ? 599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 128.764 118.881 93.967  1.00 63.50  ? 599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.562 116.735 96.385  1.00 58.55  ? 599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 127.773 117.866 97.027  1.00 60.57  ? 599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.333 117.543 98.442  1.00 64.46  ? 599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 126.709 116.481 98.648  1.00 62.73  ? 599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.610 118.355 99.351  1.00 62.77  ? 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 128.928 116.777 93.167  1.00 59.23  ? 600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 128.370 117.153 91.871  1.00 52.25  ? 600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 126.909 117.571 91.995  1.00 52.48  ? 600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 126.481 118.542 91.362  1.00 59.57  ? 600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 128.525 116.003 90.882  1.00 53.88  ? 600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 129.921 115.895 90.309  1.00 51.09  ? 600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 129.981 114.897 89.179  1.00 53.47  ? 600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 131.314 114.806 88.600  1.00 52.64  ? 600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.278 114.023 89.063  1.00 54.21  ? 600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.450 113.995 88.434  1.00 57.09  ? 600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 132.102 113.272 90.138  1.00 49.61  ? 600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.132 116.849 92.798  1.00 59.33  ? 601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 124.735 117.178 93.056  1.00 62.32  ? 601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 124.554 117.286 94.563  1.00 60.88  ? 601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 124.769 116.307 95.288  1.00 61.71  ? 601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 123.774 116.132 92.467  1.00 63.86  ? 601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.010 115.980 90.964  1.00 63.13  ? 601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 122.333 116.521 92.746  1.00 61.32  ? 601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.202 114.878 90.325  1.00 61.06  ? 601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.164 118.468 95.031  1.00 68.13  ? 602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.017 118.707 96.459  1.00 71.54  ? 602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 122.688 118.159 96.961  1.00 74.44  ? 602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 121.630 118.455 96.397  1.00 76.68  ? 602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 124.120 120.200 96.766  1.00 71.79  ? 602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 125.407 120.602 97.459  1.00 73.99  ? 602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.620 122.100 97.464  1.00 75.94  ? 602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 124.616 122.838 97.416  1.00 72.95  ? 602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 126.787 122.541 97.525  1.00 73.90  ? 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 122.747 117.363 98.022  1.00 79.01  ? 603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.565 116.788 98.655  1.00 78.69  ? 603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.247 117.611 99.900  1.00 80.15  ? 603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 121.958 117.526 100.906 1.00 81.15  ? 603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.806 115.318 98.990  1.00 81.24  ? 603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.581 114.430 98.877  1.00 83.00  ? 603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.751 113.115 99.611  1.00 82.32  ? 603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 121.397 112.203 99.051  1.00 80.14  ? 603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.248 112.990 100.745 1.00 80.76  ? 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.186 118.411 99.826  1.00 81.18  ? 604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 119.816 119.347 100.881 1.00 82.20  ? 604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.436 119.011 101.425 1.00 84.32  ? 604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 117.541 118.619 100.666 1.00 84.12  ? 604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 119.847 120.790 100.368 1.00 82.86  ? 604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.175 121.196 99.760  1.00 85.85  ? 604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.038 121.900 100.798 1.00 82.59  ? 604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 122.583 120.977 101.786 1.00 84.86  ? 604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 123.748 120.355 101.675 1.00 85.24  ? 604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 124.141 119.535 102.647 1.00 81.97  ? 604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 124.530 120.533 100.624 1.00 84.05  ? 604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.270 119.166 102.736 1.00 91.38  ? 605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.012 118.903 103.422 1.00 91.43  ? 605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.371 120.229 103.807 1.00 89.97  ? 605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.005 121.061 104.466 1.00 88.10  ? 605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.233 118.042 104.666 1.00 92.04  ? 605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 117.816 116.790 104.285 1.00 91.60  ? 605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 115.916 117.788 105.381 1.00 91.54  ? 605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.120 120.427 103.396 1.00 89.19  ? 606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 114.365 121.632 103.722 1.00 90.58  ? 606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 112.989 121.208 104.214 1.00 90.91  ? 606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.164 120.735 103.425 1.00 88.26  ? 606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 114.258 122.558 102.511 1.00 89.41  ? 606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 115.593 123.113 102.080 1.00 89.16  ? 606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 116.304 123.981 102.896 1.00 88.24  ? 606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.148 122.760 100.858 1.00 87.28  ? 606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 117.529 124.483 102.506 1.00 86.43  ? 606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 117.369 123.258 100.459 1.00 89.75  ? 606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.056 124.118 101.287 1.00 89.38  ? 606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.275 124.612 100.890 1.00 86.40  ? 606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 112.740 121.383 105.506 1.00 97.44  ? 607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 111.482 120.931 106.081 1.00 97.29  ? 607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 111.369 119.426 105.998 1.00 99.50  ? 607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 112.256 118.699 106.453 1.00 98.51  ? 607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 110.271 118.950 105.413 1.00 100.95 ? 608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 110.036 117.525 105.217 1.00 101.78 ? 608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 110.389 117.067 103.808 1.00 100.87 ? 608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.019 115.955 103.415 1.00 99.81  ? 608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 108.577 117.182 105.531 1.00 101.07 ? 608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 108.404 115.752 106.008 1.00 101.78 ? 608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 108.014 114.872 105.240 1.00 100.05 ? 608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.691 115.514 107.282 1.00 100.07 ? 608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.094 117.892 103.043 1.00 95.48  ? 609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.404 117.610 101.650 1.00 93.84  ? 609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 112.906 117.450 101.457 1.00 96.54  ? 609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 113.712 118.035 102.185 1.00 95.04  ? 609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 110.888 118.725 100.741 1.00 93.56  ? 609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 111.689 119.887 100.865 1.00 94.60  ? 609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.272 116.649 100.461 1.00 88.28  ? 610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 114.665 116.423 100.090 1.00 86.64  ? 610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 114.892 117.114 98.749  1.00 86.59  ? 610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.305 116.727 97.736  1.00 84.88  ? 610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 114.976 114.932 100.018 1.00 86.38  ? 610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.401 114.591 100.389 1.00 87.85  ? 610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.614 114.800 101.878 1.00 89.72  ? 610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.575 113.778 102.454 1.00 86.90  ? 610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.990 114.178 102.238 1.00 84.73  ? 610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 115.738 118.138 98.749  1.00 84.47  ? 611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 115.975 118.942 97.558  1.00 80.09  ? 611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.359 118.660 96.985  1.00 79.08  ? 611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.325 118.469 97.727  1.00 81.85  ? 611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 115.838 120.430 97.876  1.00 80.68  ? 611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 114.801 120.617 98.847  1.00 82.63  ? 611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 115.484 121.201 96.623  1.00 80.23  ? 611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 117.443 118.641 95.658  1.00 74.05  ? 612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 118.685 118.356 94.954  1.00 74.41  ? 612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.121 119.567 94.142  1.00 76.29  ? 612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 118.322 120.158 93.410  1.00 77.50  ? 612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 118.519 117.147 94.034  1.00 74.93  ? 612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 117.979 115.924 94.734  1.00 77.59  ? 612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 118.766 115.200 95.619  1.00 76.32  ? 612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 116.677 115.497 94.516  1.00 75.95  ? 612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 118.272 114.083 96.262  1.00 77.99  ? 612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 116.175 114.381 95.154  1.00 77.71  ? 612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 116.977 113.678 96.026  1.00 80.47  ? 612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 116.479 112.566 96.664  1.00 80.83  ? 612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 120.393 119.931 94.276  1.00 66.19  ? 613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 120.974 121.052 93.536  1.00 62.21  ? 613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.208 120.607 92.764  1.00 62.75  ? 613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 123.311 120.547 93.335  1.00 64.41  ? 613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 121.332 122.201 94.476  1.00 64.73  ? 613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.022 123.350 93.776  1.00 61.66  ? 613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 121.439 123.977 92.683  1.00 58.66  ? 613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.262 123.802 94.203  1.00 61.69  ? 613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.067 125.026 92.043  1.00 58.78  ? 613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 123.898 124.848 93.569  1.00 64.71  ? 613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.296 125.457 92.490  1.00 64.89  ? 613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 123.929 126.500 91.856  1.00 64.53  ? 613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.078 120.275 91.483  1.00 59.04  ? 614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.274 120.090 90.656  1.00 58.87  ? 614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.024 121.403 90.506  1.00 61.32  ? 614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 123.421 122.477 90.441  1.00 62.79  ? 614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 122.713 119.607 89.313  1.00 57.32  ? 614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.297 119.202 89.590  1.00 60.66  ? 614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 120.838 120.055 90.725  1.00 59.33  ? 614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 125.349 121.311 90.458  1.00 57.39  ? 615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.155 122.499 90.235  1.00 58.91  ? 615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 125.862 123.083 88.853  1.00 58.68  ? 615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.548 122.347 87.915  1.00 55.77  ? 615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 127.639 122.176 90.396  1.00 53.90  ? 615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 127.959 121.543 91.738  1.00 50.30  ? 615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 127.567 122.719 93.053  1.00 59.61  ? 615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.559 121.671 94.502  1.00 58.29  ? 615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 125.927 124.407 88.714  1.00 54.84  ? 616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 125.480 125.044 87.468  1.00 54.67  ? 616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.254 124.545 86.259  1.00 52.68  ? 616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 127.470 124.356 86.310  1.00 53.70  ? 616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 125.738 126.533 87.722  1.00 52.76  ? 616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 125.784 126.656 89.203  1.00 54.02  ? 616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 126.383 125.394 89.705  1.00 47.00  ? 616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.529 124.332 85.165  1.00 50.57  ? 617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.138 123.847 83.945  1.00 51.63  ? 617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.486 122.379 83.946  1.00 55.18  ? 617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.104 121.906 82.988  1.00 56.87  ? 617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.117 121.643 84.990  1.00 52.60  ? 618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 126.405 120.218 85.037  1.00 50.78  ? 618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 125.541 119.471 84.030  1.00 51.46  ? 618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 124.336 119.711 83.919  1.00 51.34  ? 618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.168 119.668 86.442  1.00 49.39  ? 618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 126.480 118.188 86.660  1.00 51.49  ? 618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 127.937 117.898 86.347  1.00 52.17  ? 618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.146 117.778 88.083  1.00 50.75  ? 618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.168 118.561 83.295  1.00 60.75  ? 619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 125.486 117.772 82.279  1.00 61.30  ? 619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 126.339 116.543 81.990  1.00 63.26  ? 619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 127.311 116.260 82.698  1.00 67.79  ? 619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 125.222 118.607 81.023  1.00 58.00  ? 619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 125.971 115.807 80.941  1.00 68.55  ? 620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 126.699 114.588 80.604  1.00 68.89  ? 620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.077 114.900 80.034  1.00 68.70  ? 620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.049 114.193 80.324  1.00 66.50  ? 620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 125.883 113.754 79.619  1.00 70.19  ? 620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 124.534 113.659 80.037  1.00 69.21  ? 620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.182 115.952 79.218  1.00 66.43  ? 621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 129.450 116.258 78.565  1.00 65.27  ? 621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 130.504 116.739 79.555  1.00 68.18  ? 621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 131.686 116.413 79.403  1.00 69.83  ? 621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.241 117.303 77.469  1.00 65.95  ? 621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 128.261 118.384 77.874  1.00 68.86  ? 621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 127.481 118.208 78.809  1.00 67.96  ? 621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 128.296 119.510 77.172  1.00 66.80  ? 621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.104 117.508 80.567  1.00 59.35  ? 622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.035 118.058 81.546  1.00 57.19  ? 622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 130.874 117.418 82.922  1.00 59.55  ? 622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 131.173 118.043 83.942  1.00 66.37  ? 622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 130.885 119.578 81.629  1.00 57.14  ? 622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 129.490 120.020 82.049  1.00 60.24  ? 622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 128.861 119.419 82.919  1.00 64.84  ? 622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.002 121.085 81.425  1.00 59.73  ? 622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 130.396 116.172 82.965  1.00 53.45  ? 623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 130.242 115.486 84.243  1.00 55.40  ? 623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 131.585 115.235 84.916  1.00 57.31  ? 623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 131.706 115.413 86.134  1.00 55.94  ? 623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 129.495 114.166 84.048  1.00 58.49  ? 623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 129.289 113.402 85.322  1.00 57.75  ? 623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 130.126 112.472 85.865  1.00 54.52  ? 623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 128.176 113.509 86.216  1.00 57.01  ? 623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 129.603 111.991 87.039  1.00 54.79  ? 623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 128.405 112.611 87.277  1.00 55.19  ? 623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.007 114.275 86.222  1.00 55.42  ? 623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 127.510 112.460 88.333  1.00 54.50  ? 623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 126.120 114.124 87.271  1.00 55.40  ? 623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 126.377 113.223 88.312  1.00 56.93  ? 623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 132.597 114.823 84.155  1.00 58.70  ? 624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 133.903 114.536 84.733  1.00 59.93  ? 624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 134.766 115.779 84.890  1.00 59.62  ? 624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 135.745 115.743 85.646  1.00 59.99  ? 624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 134.631 113.478 83.891  1.00 58.61  ? 624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 135.669 114.036 82.957  1.00 60.89  ? 624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 135.311 114.511 81.707  1.00 59.48  ? 624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 137.007 114.067 83.322  1.00 57.60  ? 624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 136.263 115.015 80.844  1.00 56.19  ? 624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 137.963 114.571 82.464  1.00 61.05  ? 624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 137.591 115.044 81.223  1.00 60.01  ? 624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 134.429 116.875 84.207  1.00 55.73  ? 625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.087 118.145 84.490  1.00 49.14  ? 625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 134.667 118.696 85.845  1.00 51.14  ? 625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 135.450 119.389 86.503  1.00 56.88  ? 625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 134.788 119.163 83.391  1.00 46.32  ? 625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 135.392 118.818 82.061  1.00 49.61  ? 625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 136.764 118.708 81.919  1.00 47.63  ? 625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 134.589 118.611 80.953  1.00 53.07  ? 625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 137.324 118.396 80.697  1.00 52.61  ? 625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 135.144 118.296 79.728  1.00 53.02  ? 625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 136.514 118.190 79.600  1.00 54.96  ? 625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 133.441 118.401 86.277  1.00 45.83  ? 626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 132.979 118.803 87.597  1.00 45.87  ? 626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 133.439 117.797 88.642  1.00 46.22  ? 626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 132.621 117.258 89.395  1.00 54.25  ? 626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 131.457 118.935 87.623  1.00 44.03  ? 626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 130.958 120.294 87.200  1.00 46.11  ? 626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.023 121.377 88.066  1.00 47.67  ? 626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 130.415 120.494 85.940  1.00 46.43  ? 626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 130.569 122.620 87.686  1.00 46.28  ? 626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 129.956 121.735 85.551  1.00 45.06  ? 626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.037 122.793 86.428  1.00 48.63  ? 626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 129.582 124.033 86.046  1.00 55.11  ? 626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 134.741 117.536 88.690  1.00 44.39  ? 627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 135.281 116.582 89.649  1.00 51.01  ? 627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.045 117.071 91.072  1.00 46.73  ? 627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 135.199 118.257 91.373  1.00 51.96  ? 627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 136.774 116.377 89.392  1.00 52.06  ? 627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 137.428 115.298 90.229  1.00 47.38  ? 627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 138.862 115.078 89.779  1.00 47.18  ? 627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 139.581 114.083 90.669  1.00 55.59  ? 627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.015 113.951 90.296  1.00 52.33  ? 627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 134.650 116.151 91.947  1.00 53.02  ? 628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 134.395 116.508 93.334  1.00 53.83  ? 628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 135.689 116.918 94.027  1.00 56.58  ? 628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 136.768 116.397 93.737  1.00 60.27  ? 628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 133.744 115.344 94.080  1.00 57.58  ? 628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 132.273 115.153 93.761  1.00 57.35  ? 628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 131.666 113.978 94.499  1.00 62.36  ? 628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.280 113.511 95.481  1.00 58.23  ? 628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 130.574 113.523 94.099  1.00 61.57  ? 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 135.563 117.865 94.961  1.00 53.73  ? 629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 136.738 118.419 95.626  1.00 50.50  ? 629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 137.501 117.353 96.399  1.00 56.15  ? 629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 138.738 117.349 96.408  1.00 54.80  ? 629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 136.321 119.555 96.557  1.00 49.42  ? 629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 136.783 116.444 97.061  1.00 64.51  ? 630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 137.445 115.399 97.833  1.00 61.71  ? 630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 138.218 114.441 96.937  1.00 63.54  ? 630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 139.222 113.864 97.371  1.00 65.86  ? 630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 136.418 114.641 98.671  1.00 57.23  ? 630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 135.608 115.537 99.577  1.00 58.88  ? 630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.101 115.934 100.810 1.00 57.77  ? 630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 134.353 115.991 99.195  1.00 59.27  ? 630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 135.366 116.755 101.642 1.00 60.43  ? 630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 133.611 116.812 100.021 1.00 62.04  ? 630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.122 117.190 101.243 1.00 62.58  ? 630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 133.388 118.007 102.069 1.00 61.11  ? 630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 137.775 114.261 95.692  1.00 60.66  ? 631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 138.495 113.410 94.754  1.00 59.95  ? 631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 139.744 114.078 94.196  1.00 59.90  ? 631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 140.614 113.383 93.661  1.00 58.64  ? 631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 137.574 113.002 93.602  1.00 61.96  ? 631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 136.414 112.142 94.058  1.00 66.68  ? 631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 136.623 111.270 94.927  1.00 64.91  ? 631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 135.291 112.339 93.548  1.00 68.70  ? 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 139.853 115.399 94.311  1.00 54.90  ? 632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 140.994 116.110 93.756  1.00 53.36  ? 632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 142.250 115.875 94.588  1.00 58.18  ? 632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 142.198 115.537 95.774  1.00 58.99  ? 632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 140.721 117.611 93.682  1.00 51.03  ? 632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 139.391 117.995 93.080  1.00 52.51  ? 632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 139.515 119.514 92.125  1.00 57.47  ? 632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 138.190 119.277 90.951  1.00 49.12  ? 632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 143.396 116.065 93.939  1.00 52.34  ? 633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 144.674 116.113 94.634  1.00 51.70  ? 633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 144.787 117.461 95.333  1.00 51.60  ? 633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 144.724 118.510 94.683  1.00 54.67  ? 633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 145.823 115.909 93.648  1.00 48.37  ? 633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 147.170 115.747 94.334  1.00 56.91  ? 633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 147.259 115.963 95.560  1.00 55.98  ? 633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 148.148 115.402 93.639  1.00 54.86  ? 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 144.942 117.436 96.659  1.00 46.34  ? 634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.012 118.684 97.410  1.00 44.16  ? 634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 146.246 119.496 97.040  1.00 46.29  ? 634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 146.239 120.723 97.169  1.00 48.41  ? 634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 144.997 118.400 98.911  1.00 44.59  ? 634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 143.624 118.440 99.600  1.00 54.61  ? 634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 142.474 119.761 99.136  1.00 64.07  ? 634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 141.621 119.062 97.720  1.00 46.20  ? 634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 147.310 118.836 96.578  1.00 45.87  ? 635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 148.502 119.567 96.155  1.00 43.99  ? 635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.216 120.424 94.929  1.00 43.21  ? 635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 148.675 121.569 94.843  1.00 42.72  ? 635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 149.647 118.593 95.879  1.00 43.08  ? 635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 150.422 118.202 97.106  1.00 48.24  ? 635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 149.767 117.867 98.280  1.00 46.29  ? 635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 151.805 118.169 97.085  1.00 43.40  ? 635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 150.478 117.506 99.407  1.00 42.30  ? 635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 152.521 117.810 98.210  1.00 44.42  ? 635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 151.855 117.479 99.372  1.00 45.27  ? 635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 147.451 119.896 93.973  1.00 46.89  ? 636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.120 120.683 92.789  1.00 47.05  ? 636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.125 121.791 93.111  1.00 49.26  ? 636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.160 122.854 92.483  1.00 52.40  ? 636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 146.588 119.767 91.689  1.00 43.24  ? 636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 147.611 118.746 91.215  1.00 45.54  ? 636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 147.064 117.873 90.103  1.00 53.89  ? 636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 147.982 116.697 89.822  1.00 51.60  ? 636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 147.358 115.720 88.887  1.00 48.73  ? 636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.252 121.578 94.097  1.00 39.93  ? 637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 144.382 122.659 94.552  1.00 35.05  ? 637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.205 123.748 95.233  1.00 44.90  ? 637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 144.926 124.944 95.082  1.00 44.78  ? 637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.286 122.105 95.479  1.00 38.64  ? 637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.370 123.221 95.946  1.00 38.67  ? 637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 142.491 121.026 94.764  1.00 46.33  ? 637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.235 123.352 95.986  1.00 44.27  ? 638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.158 124.322 96.567  1.00 36.78  ? 638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 147.868 125.100 95.469  1.00 39.22  ? 638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.057 126.316 95.572  1.00 45.87  ? 638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.162 123.616 97.498  1.00 35.56  ? 638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.327 124.534 97.817  1.00 36.39  ? 638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 147.480 123.164 98.775  1.00 38.05  ? 638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.281 124.407 94.405  1.00 36.55  ? 639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 148.896 125.086 93.268  1.00 37.91  ? 639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 147.941 126.098 92.649  1.00 40.32  ? 639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 148.336 127.229 92.342  1.00 45.55  ? 639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.334 124.065 92.218  1.00 41.16  ? 639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 150.392 123.117 92.731  1.00 46.99  ? 639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 150.984 123.412 93.787  1.00 51.58  ? 639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 150.633 122.081 92.077  1.00 44.86  ? 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 146.679 125.709 92.467  1.00 36.02  ? 640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 145.685 126.617 91.904  1.00 37.87  ? 640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.507 127.852 92.779  1.00 39.90  ? 640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 145.507 128.986 92.284  1.00 44.13  ? 640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.354 125.885 91.734  1.00 43.86  ? 640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.160 126.799 91.542  1.00 41.72  ? 640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.289 127.796 90.052  1.00 43.50  ? 640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.448 126.746 88.874  1.00 39.04  ? 640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 145.367 127.650 94.089  1.00 38.78  ? 641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.128 128.775 94.988  1.00 31.81  ? 641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.350 129.683 95.051  1.00 32.15  ? 641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.224 130.913 95.041  1.00 40.91  ? 641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 144.711 128.272 96.381  1.00 34.92  ? 641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 143.411 127.472 96.286  1.00 38.40  ? 641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 144.523 129.438 97.334  1.00 35.98  ? 641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 142.379 128.090 95.366  1.00 39.64  ? 641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 147.551 129.097 95.103  1.00 32.17  ? 642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 148.772 129.895 95.107  1.00 30.25  ? 642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 148.928 130.681 93.815  1.00 33.24  ? 642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 149.444 131.805 93.831  1.00 35.93  ? 642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 149.986 128.996 95.334  1.00 31.14  ? 642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 148.507 130.106 92.689  1.00 34.65  ? 643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 148.464 130.866 91.446  1.00 33.05  ? 643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 147.495 132.034 91.559  1.00 33.16  ? 643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 147.791 133.146 91.107  1.00 34.52  ? 643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.073 129.948 90.288  1.00 29.55  ? 643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.105 128.976 90.078  1.00 35.81  ? 643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 147.881 130.747 89.022  1.00 29.77  ? 643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.330 131.801 92.164  1.00 31.77  ? 644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 145.402 132.896 92.431  1.00 28.75  ? 644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 145.954 133.819 93.510  1.00 30.21  ? 644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 145.801 135.044 93.436  1.00 33.90  ? 644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.019 132.344 92.819  1.00 28.55  ? 644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 143.490 131.406 91.737  1.00 30.63  ? 644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.048 133.478 93.062  1.00 26.52  ? 644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.270 130.633 92.165  1.00 32.25  ? 644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 146.602 133.248 94.530  1.00 30.65  ? 645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.017 134.034 95.690  1.00 23.48  ? 645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.029 135.110 95.321  1.00 32.82  ? 645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.053 136.176 95.946  1.00 40.53  ? 645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 147.591 133.112 96.767  1.00 22.44  ? 645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.013 133.822 98.037  1.00 24.23  ? 645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 146.837 134.160 98.925  1.00 31.10  ? 645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.403 135.309 98.985  1.00 35.64  ? 645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.314 133.159 99.622  1.00 25.84  ? 645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 148.866 134.859 94.313  1.00 38.20  ? 646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 149.882 135.834 93.939  1.00 36.67  ? 646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.294 137.104 93.338  1.00 29.77  ? 646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.009 138.104 93.232  1.00 35.43  ? 646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 150.873 135.206 92.959  1.00 32.34  ? 646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.368 135.118 91.534  1.00 40.84  ? 646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.292 134.318 90.640  1.00 43.33  ? 646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 150.915 133.268 90.120  1.00 40.76  ? 646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 152.511 134.810 90.458  1.00 41.77  ? 646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.019 137.097 92.958  1.00 32.25  ? 647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.358 138.279 92.427  1.00 29.71  ? 647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.344 138.871 93.391  1.00 27.07  ? 647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 145.689 139.860 93.052  1.00 38.85  ? 647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 146.674 137.948 91.096  1.00 30.79  ? 647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 147.598 137.359 90.077  1.00 30.57  ? 647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 148.652 138.062 89.536  1.00 27.11  ? 647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 147.629 136.133 89.506  1.00 27.93  ? 647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.292 137.294 88.673  1.00 37.94  ? 647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 148.691 136.119 88.635  1.00 35.73  ? 647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.197 138.293 94.579  1.00 29.77  ? 648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.276 138.779 95.599  1.00 33.46  ? 648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.117 139.348 96.732  1.00 32.63  ? 648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 146.950 138.639 97.312  1.00 31.78  ? 648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.348 137.661 96.097  1.00 16.29  ? 648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 143.571 137.050 94.929  1.00 27.35  ? 648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.386 138.187 97.138  1.00 17.68  ? 648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 142.605 138.003 94.265  1.00 21.35  ? 648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 145.911 140.631 97.046  1.00 24.43  ? 649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 146.731 141.270 98.070  1.00 29.86  ? 649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.376 140.763 99.464  1.00 30.04  ? 649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.254 140.634 100.324 1.00 37.39  ? 649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.601 142.792 97.984  1.00 35.60  ? 649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.184 143.276 98.202  1.00 34.54  ? 649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.270 142.437 98.297  1.00 34.96  ? 649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.985 144.505 98.280  1.00 35.30  ? 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.102 140.478 99.706  1.00 15.39  ? 650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 144.686 139.808 100.927 1.00 16.88  ? 650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 144.715 138.299 100.696 1.00 13.99  ? 650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.278 137.811 99.715  1.00 24.00  ? 650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.310 140.296 101.371 1.00 13.85  ? 650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.219 141.790 101.597 1.00 12.25  ? 650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 141.888 142.203 102.184 1.00 20.96  ? 650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.573 141.875 103.325 1.00 23.91  ? 650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.098 142.931 101.404 1.00 21.80  ? 650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.117 137.538 101.610 1.00 9.60   ? 651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.131 136.094 101.521 1.00 19.13  ? 651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 142.947 135.530 100.760 1.00 22.19  ? 651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.097 136.245 100.231 1.00 26.76  ? 651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 142.908 134.202 100.708 1.00 31.01  ? 652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 141.847 133.447 100.054 1.00 21.14  ? 652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.317 132.429 101.051 1.00 29.25  ? 652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.099 131.764 101.739 1.00 34.40  ? 652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.351 132.748 98.778  1.00 17.73  ? 652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 142.911 133.770 97.791  1.00 16.83  ? 652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.241 131.937 98.134  1.00 24.97  ? 652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 143.555 133.143 96.591  1.00 22.55  ? 652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 139.994 132.308 101.129 1.00 27.63  ? 653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.393 131.333 102.029 1.00 22.33  ? 653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 139.602 129.935 101.463 1.00 29.32  ? 653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 138.774 129.433 100.697 1.00 41.18  ? 653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 137.908 131.628 102.230 1.00 29.71  ? 653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 137.722 132.866 102.892 1.00 29.56  ? 653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 140.712 129.306 101.837 1.00 32.18  ? 654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.145 128.039 101.258 1.00 28.14  ? 654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 140.713 126.905 102.179 1.00 30.45  ? 654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.282 126.720 103.259 1.00 38.13  ? 654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 142.658 128.039 101.051 1.00 31.92  ? 654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.187 126.795 100.401 1.00 30.85  ? 654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.380 126.012 99.595  1.00 32.99  ? 654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 144.500 126.407 100.600 1.00 34.03  ? 654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 142.871 124.869 99.003  1.00 36.23  ? 654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 144.995 125.266 100.010 1.00 33.19  ? 654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.180 124.496 99.210  1.00 31.87  ? 654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 139.720 126.140 101.740 1.00 44.02  ? 655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.211 124.997 102.484 1.00 40.05  ? 655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 139.864 123.726 101.961 1.00 39.12  ? 655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 139.895 123.493 100.749 1.00 42.27  ? 655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 137.689 124.900 102.358 1.00 43.48  ? 655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.080 126.018 103.014 1.00 47.48  ? 655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.178 123.613 102.983 1.00 39.59  ? 655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 140.391 122.913 102.872 1.00 46.33  ? 656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 140.976 121.630 102.512 1.00 48.96  ? 656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 139.893 120.561 102.513 1.00 44.62  ? 656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.151 120.419 103.489 1.00 50.25  ? 656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.094 121.242 103.479 1.00 49.71  ? 656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 143.346 122.115 103.464 1.00 48.43  ? 656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 144.436 121.502 104.328 1.00 45.90  ? 656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 143.832 122.325 102.042 1.00 47.50  ? 656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 139.809 119.812 101.419 1.00 42.57  ? 657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 138.824 118.750 101.254 1.00 48.56  ? 657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 139.561 117.421 101.362 1.00 53.23  ? 657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 140.309 117.043 100.455 1.00 49.32  ? 657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.103 118.885 99.917  1.00 52.56  ? 657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 137.571 120.265 99.650  1.00 51.03  ? 657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 136.340 120.659 100.142 1.00 49.70  ? 657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 138.307 121.167 98.899  1.00 53.25  ? 657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 135.854 121.930 99.892  1.00 55.13  ? 657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 137.825 122.435 98.643  1.00 49.61  ? 657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 136.597 122.819 99.141  1.00 54.42  ? 657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 139.346 116.716 102.468 1.00 62.39  ? 658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.124 115.539 102.820 1.00 61.77  ? 658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 139.257 114.289 102.754 1.00 64.49  ? 658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.075 114.323 103.106 1.00 66.11  ? 658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 140.713 115.693 104.225 1.00 63.35  ? 658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 141.839 116.713 104.383 1.00 64.26  ? 658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 141.435 117.765 105.389 1.00 59.09  ? 658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.117 116.029 104.831 1.00 66.14  ? 658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 139.847 113.195 102.284 1.00 71.01  ? 659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 139.189 111.900 102.345 1.00 73.25  ? 659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 139.307 111.317 103.750 1.00 74.82  ? 659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 140.136 111.740 104.561 1.00 73.90  ? 659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 139.789 110.935 101.319 1.00 72.75  ? 659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 139.694 111.413 99.877  1.00 72.19  ? 659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 139.955 110.275 98.901  1.00 75.24  ? 659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 139.858 110.738 97.455  1.00 75.14  ? 659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 139.653 109.595 96.522  1.00 74.67  ? 659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 138.450 110.335 104.039 1.00 80.49  ? 660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 138.498 109.683 105.343 1.00 81.16  ? 660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 139.772 108.866 105.515 1.00 80.84  ? 660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 140.280 108.741 106.636 1.00 78.67  ? 660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 137.268 108.797 105.532 1.00 79.61  ? 660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 136.310 109.342 106.574 1.00 81.72  ? 660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.697 110.273 107.311 1.00 79.42  ? 660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 135.171 108.838 106.655 1.00 80.71  ? 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 140.301 108.308 104.425 1.00 81.32  ? 661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 141.472 107.445 104.506 1.00 81.44  ? 661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 142.772 108.211 104.703 1.00 77.18  ? 661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 143.773 107.606 105.103 1.00 75.44  ? 661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 141.584 106.588 103.244 1.00 81.98  ? 661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.828 105.878 103.256 1.00 81.62  ? 661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 141.520 107.464 102.001 1.00 77.36  ? 661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 142.791 109.514 104.437 1.00 76.31  ? 662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 144.028 110.278 104.526 1.00 78.98  ? 662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 144.290 110.691 105.970 1.00 78.43  ? 662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 143.425 111.279 106.627 1.00 78.27  ? 662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 143.967 111.498 103.609 1.00 75.92  ? 662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 143.835 111.126 102.136 1.00 79.09  ? 662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 143.913 112.513 100.985 1.00 83.58  ? 662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 143.973 113.898 102.114 1.00 74.38  ? 662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 145.491 110.387 106.455 1.00 68.66  ? 663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 145.828 110.505 107.865 1.00 67.75  ? 663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 146.199 111.946 108.215 1.00 67.12  ? 663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.030 112.871 107.417 1.00 67.37  ? 663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 146.966 109.548 108.212 1.00 68.29  ? 663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 148.222 110.200 107.989 1.00 62.85  ? 663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 146.893 108.302 107.344 1.00 67.87  ? 663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 146.710 112.146 109.433 1.00 63.09  ? 664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.164 113.472 109.837 1.00 62.88  ? 664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 148.474 113.847 109.161 1.00 59.25  ? 664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 148.753 115.035 108.973 1.00 61.96  ? 664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 147.325 113.547 111.355 1.00 60.74  ? 664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 148.203 112.505 111.795 1.00 59.38  ? 664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 145.979 113.403 112.041 1.00 61.16  ? 664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 149.293 112.857 108.800 1.00 61.82  ? 665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 150.510 113.157 108.055 1.00 61.51  ? 665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 150.182 113.740 106.689 1.00 65.17  ? 665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 150.870 114.648 106.217 1.00 65.87  ? 665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 151.373 111.906 107.908 1.00 63.88  ? 665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 152.613 112.126 107.054 1.00 60.96  ? 665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 153.542 110.925 107.080 1.00 65.11  ? 665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 154.491 110.941 105.972 1.00 67.64  ? 665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 154.171 110.740 104.700 1.00 65.78  ? 665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 155.123 110.796 103.775 1.00 60.88  ? 665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 152.926 110.480 104.331 1.00 63.05  ? 665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.133 113.232 106.037 1.00 60.48  ? 666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 148.719 113.795 104.756 1.00 57.40  ? 666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 148.239 115.233 104.914 1.00 60.30  ? 666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 148.566 116.098 104.091 1.00 66.24  ? 666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 147.628 112.927 104.131 1.00 63.30  ? 666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.042 111.474 104.008 1.00 67.46  ? 666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 149.137 111.212 103.470 1.00 65.60  ? 666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 147.274 110.595 104.451 1.00 66.92  ? 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 147.465 115.509 105.965 1.00 49.42  ? 667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.015 116.874 106.215 1.00 48.47  ? 667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.194 117.798 106.489 1.00 51.95  ? 667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 148.225 118.940 106.017 1.00 52.80  ? 667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.031 116.896 107.385 1.00 49.55  ? 667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 144.967 117.995 107.405 1.00 48.64  ? 667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 143.748 117.524 108.177 1.00 49.76  ? 667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 145.507 119.282 108.000 1.00 51.00  ? 667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.177 117.319 107.255 1.00 53.22  ? 668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 150.366 118.119 107.526 1.00 47.99  ? 668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.179 118.348 106.258 1.00 51.87  ? 668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 151.755 119.424 106.074 1.00 57.93  ? 668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 151.217 117.442 108.597 1.00 48.53  ? 668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 150.859 117.892 109.994 1.00 53.63  ? 668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 150.352 118.996 110.191 1.00 55.78  ? 668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.112 117.035 110.974 1.00 57.80  ? 668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 151.251 117.345 105.382 1.00 48.56  ? 669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 151.933 117.524 104.105 1.00 47.14  ? 669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 151.233 118.576 103.257 1.00 46.45  ? 669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 151.888 119.405 102.620 1.00 46.35  ? 669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.008 116.198 103.351 1.00 47.89  ? 669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 152.989 115.197 103.929 1.00 53.48  ? 669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.014 114.776 102.891 1.00 53.94  ? 669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 153.390 114.344 101.647 1.00 51.91  ? 669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 153.797 114.711 100.439 1.00 57.04  ? 669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 153.145 114.263 99.370  1.00 48.20  ? 669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 154.837 115.511 100.275 1.00 58.23  ? 669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 149.898 118.557 103.242 1.00 46.65  ? 670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.153 119.578 102.508 1.00 46.90  ? 670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 149.415 120.956 103.102 1.00 49.53  ? 670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 149.616 121.934 102.371 1.00 51.85  ? 670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 147.651 119.244 102.492 1.00 46.84  ? 670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 147.408 117.899 101.806 1.00 46.21  ? 670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 146.874 120.335 101.783 1.00 47.35  ? 670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.098 117.251 102.189 1.00 45.53  ? 670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 149.422 121.057 104.433 1.00 48.01  ? 671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 149.676 122.340 105.083 1.00 41.26  ? 671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.075 122.858 104.766 1.00 43.21  ? 671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.258 124.044 104.471 1.00 49.47  ? 671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 149.493 122.209 106.596 1.00 47.39  ? 671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.043 122.036 106.997 1.00 57.86  ? 671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.153 122.388 106.195 1.00 56.07  ? 671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 147.792 121.551 108.121 1.00 55.55  ? 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.077 121.978 104.815 1.00 42.51  ? 672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 153.450 122.398 104.559 1.00 37.61  ? 672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 153.678 122.715 103.089 1.00 39.27  ? 672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 154.500 123.577 102.766 1.00 49.12  ? 672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 154.426 121.322 105.028 1.00 44.78  ? 672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 154.480 121.098 106.540 1.00 46.50  ? 672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.036 119.721 106.858 1.00 45.86  ? 672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.300 122.187 107.212 1.00 41.59  ? 672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 152.973 122.032 102.185 1.00 38.79  ? 673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.057 122.383 100.773 1.00 40.32  ? 673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.376 123.717 100.500 1.00 41.35  ? 673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 152.845 124.501 99.667  1.00 46.59  ? 673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 152.439 121.276 99.923  1.00 36.15  ? 673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 152.631 121.470 98.440  1.00 39.36  ? 673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 153.896 121.426 97.871  1.00 41.68  ? 673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 151.545 121.691 97.607  1.00 39.93  ? 673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.073 121.601 96.515  1.00 41.27  ? 673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 151.713 121.866 96.253  1.00 42.45  ? 673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 152.977 121.821 95.710  1.00 42.22  ? 673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.145 121.997 94.356  1.00 40.07  ? 673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.265 123.988 101.189 1.00 35.73  ? 674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 150.632 125.297 101.090 1.00 39.18  ? 674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 151.566 126.391 101.585 1.00 41.51  ? 674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 151.696 127.445 100.952 1.00 45.69  ? 674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.325 125.304 101.880 1.00 34.24  ? 674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.237 126.152 102.713 1.00 39.35  ? 675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.213 127.112 103.214 1.00 31.22  ? 675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.364 127.290 102.232 1.00 38.03  ? 675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 154.837 128.412 102.014 1.00 46.09  ? 675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 153.732 126.660 104.579 1.00 33.68  ? 675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 154.855 127.495 105.106 1.00 42.43  ? 675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.179 127.195 104.872 1.00 42.22  ? 675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 154.851 128.618 105.860 1.00 35.07  ? 675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 156.943 128.100 105.457 1.00 39.75  ? 675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.162 128.974 106.064 1.00 37.37  ? 675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 154.825 126.192 101.629 1.00 41.61  ? 676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 155.932 126.257 100.682 1.00 43.94  ? 676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 155.533 126.948 99.384  1.00 44.23  ? 676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.367 127.604 98.753  1.00 41.92  ? 676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.449 124.847 100.398 1.00 43.73  ? 676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.502 124.787 99.336  1.00 52.94  ? 676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 157.228 124.430 98.034  1.00 52.78  ? 676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 158.833 125.035 99.385  1.00 49.08  ? 676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 158.341 124.462 97.325  1.00 49.94  ? 676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.331 124.826 98.121  1.00 50.28  ? 676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.274 126.816 98.972  1.00 36.83  ? 677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 153.807 127.395 97.721  1.00 39.47  ? 677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 153.339 128.835 97.865  1.00 43.57  ? 677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 152.929 129.440 96.869  1.00 46.71  ? 677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 152.675 126.547 97.131  1.00 38.27  ? 677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.147 125.284 96.430  1.00 42.09  ? 677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.170 125.597 95.348  1.00 40.60  ? 677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.778 126.739 94.529  1.00 48.95  ? 677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 152.860 126.699 93.572  1.00 50.15  ? 677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 152.572 127.812 92.903  1.00 43.21  ? 677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.227 125.579 93.268  1.00 42.94  ? 677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 153.391 129.399 99.066  1.00 33.51  ? 678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 152.991 130.773 99.273  1.00 29.25  ? 678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 151.554 130.973 99.689  1.00 30.14  ? 678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.070 132.110 99.649  1.00 31.63  ? 678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 150.850 129.910 100.077 1.00 35.14  ? 679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 149.485 130.055 100.563 1.00 31.61  ? 679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 149.504 130.853 101.857 1.00 33.70  ? 679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.309 130.589 102.758 1.00 45.78  ? 679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 148.831 128.680 100.764 1.00 34.27  ? 679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 148.668 127.968 99.422  1.00 31.00  ? 679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 147.487 128.819 101.458 1.00 37.83  ? 679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 147.874 128.752 98.423  1.00 30.96  ? 679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 148.622 131.846 101.950 1.00 27.21  ? 680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 148.621 132.725 103.110 1.00 20.06  ? 680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 147.821 132.131 104.263 1.00 18.83  ? 680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.304 132.072 105.398 1.00 32.11  ? 680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.071 134.095 102.718 1.00 17.38  ? 680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 148.984 134.893 101.807 1.00 16.47  ? 680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.362 136.228 101.446 1.00 16.32  ? 680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.230 137.003 100.476 1.00 27.74  ? 680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 148.682 138.359 100.218 1.00 28.06  ? 680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 146.597 131.681 103.991 1.00 30.92  ? 681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 145.720 131.132 105.013 1.00 22.11  ? 681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.114 129.821 104.535 1.00 34.90  ? 681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 144.940 129.598 103.335 1.00 43.72  ? 681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 144.581 132.100 105.375 1.00 29.89  ? 681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 143.718 132.270 104.244 1.00 40.94  ? 681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.123 133.451 105.792 1.00 22.13  ? 681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 144.794 128.956 105.493 1.00 30.89  ? 682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.056 127.722 105.245 1.00 28.30  ? 682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 142.800 127.762 106.102 1.00 29.69  ? 682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 142.884 127.883 107.330 1.00 42.23  ? 682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 144.899 126.478 105.556 1.00 22.70  ? 682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.290 126.611 104.934 1.00 37.75  ? 682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.210 125.234 105.041 1.00 34.30  ? 682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.153 125.390 105.108 1.00 39.46  ? 682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 141.636 127.661 105.457 1.00 24.57  ? 683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.382 127.904 106.161 1.00 21.26  ? 683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 139.908 126.668 106.920 1.00 36.74  ? 683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 139.874 126.659 108.153 1.00 51.38  ? 683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.313 128.367 105.166 1.00 33.80  ? 683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 137.979 128.733 105.781 1.00 23.95  ? 683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 137.880 129.104 107.116 1.00 22.66  ? 683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 136.819 128.712 105.023 1.00 19.07  ? 683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 136.665 129.438 107.675 1.00 29.16  ? 683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 135.599 129.047 105.574 1.00 27.48  ? 683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 135.528 129.409 106.901 1.00 31.05  ? 683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.316 129.743 107.455 1.00 30.52  ? 683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 139.565 125.602 106.205 1.00 41.01  ? 684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 138.881 124.479 106.828 1.00 33.87  ? 684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 139.486 123.170 106.355 1.00 46.06  ? 684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.073 123.090 105.273 1.00 51.88  ? 684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.378 124.491 106.518 1.00 40.39  ? 684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 136.525 125.085 107.613 1.00 31.95  ? 684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 136.803 124.840 108.948 1.00 39.50  ? 684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 135.437 125.892 107.307 1.00 41.27  ? 684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.023 125.382 109.952 1.00 46.66  ? 684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 134.652 126.439 108.303 1.00 43.61  ? 684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 134.949 126.181 109.622 1.00 47.44  ? 684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.167 126.724 110.616 1.00 45.93  ? 684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 139.330 122.145 107.183 1.00 46.89  ? 685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 139.718 120.779 106.854 1.00 45.12  ? 685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 138.434 119.955 106.819 1.00 49.42  ? 685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.002 119.404 107.833 1.00 51.73  ? 685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 140.719 120.234 107.864 1.00 49.72  ? 685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 137.820 119.884 105.642 1.00 53.83  ? 686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 136.561 119.171 105.458 1.00 53.76  ? 686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 136.868 117.718 105.121 1.00 59.82  ? 686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 137.421 117.422 104.056 1.00 60.25  ? 686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 135.726 119.829 104.363 1.00 53.10  ? 686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.061 121.124 104.791 1.00 58.64  ? 686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 133.833 121.417 103.950 1.00 60.89  ? 686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 132.952 120.261 103.844 1.00 59.95  ? 686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 131.723 120.208 104.337 1.00 60.32  ? 686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.006 119.099 104.177 1.00 55.45  ? 686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.193 121.234 104.982 1.00 61.56  ? 686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 136.511 116.812 106.026 1.00 68.61  ? 687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 136.766 115.390 105.857 1.00 69.82  ? 687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 135.491 114.692 105.403 1.00 67.70  ? 687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.425 114.889 105.995 1.00 68.72  ? 687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.274 114.766 107.157 1.00 70.33  ? 687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 138.377 115.532 107.656 1.00 67.76  ? 687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 137.733 113.338 106.915 1.00 67.88  ? 687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 135.603 113.885 104.354 1.00 73.41  ? 688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 134.461 113.144 103.832 1.00 76.94  ? 688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.512 111.687 104.278 1.00 78.25  ? 688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 135.383 110.929 103.853 1.00 77.06  ? 688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 134.419 113.226 102.306 1.00 73.00  ? 688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 133.287 112.439 101.672 1.00 71.08  ? 688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 133.307 112.574 100.159 1.00 72.76  ? 688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 132.212 111.744 99.516  1.00 74.01  ? 688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 132.224 111.869 98.033  1.00 73.31  ? 688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 151.615 116.091 163.642 1.00 63.43  ? 6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 150.679 117.146 164.007 1.00 65.94  ? 6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 151.413 118.248 164.773 1.00 67.47  ? 6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 152.297 117.969 165.584 1.00 66.45  ? 6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 149.483 116.572 164.818 1.00 65.98  ? 6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 149.876 116.279 166.260 1.00 63.88  ? 6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 148.287 117.513 164.765 1.00 66.13  ? 6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 151.083 119.505 164.477 1.00 62.94  ? 7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 151.667 120.614 165.241 1.00 57.20  ? 7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 151.223 120.574 166.695 1.00 58.33  ? 7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 150.139 120.086 167.020 1.00 63.66  ? 7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 151.134 121.856 164.521 1.00 56.88  ? 7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 150.849 121.382 163.134 1.00 58.87  ? 7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 150.321 119.991 163.313 1.00 60.91  ? 7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 152.084 121.089 167.577 1.00 57.79  ? 8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 151.776 121.082 169.002 1.00 58.95  ? 8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 150.543 121.917 169.319 1.00 60.87  ? 8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 149.713 121.513 170.141 1.00 63.37  ? 8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 152.974 121.592 169.805 1.00 58.30  ? 8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 152.708 121.709 171.298 1.00 60.12  ? 8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 154.000 121.729 172.094 1.00 61.27  ? 8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 153.869 122.598 173.334 1.00 58.75  ? 8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.192 123.076 173.822 1.00 57.85  ? 8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 150.407 123.084 168.685 1.00 60.89  ? 9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 149.260 123.941 168.966 1.00 56.50  ? 9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 147.960 123.294 168.513 1.00 55.00  ? 9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 146.934 123.415 169.189 1.00 58.69  ? 9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 149.435 125.302 168.297 1.00 56.78  ? 9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 149.837 125.246 166.855 1.00 55.76  ? 9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 149.006 125.167 165.778 1.00 54.97  ? 9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 151.169 125.287 166.332 1.00 54.62  ? 9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 149.736 125.147 164.616 1.00 54.73  ? 9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 151.068 125.221 164.928 1.00 57.56  ? 9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 152.438 125.369 166.912 1.00 54.44  ? 9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 152.185 125.232 164.098 1.00 58.34  ? 9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 153.544 125.381 166.086 1.00 56.18  ? 9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 153.412 125.311 164.695 1.00 56.84  ? 9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 147.981 122.606 167.371 1.00 56.64  ? 10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 146.778 121.934 166.891 1.00 59.60  ? 10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 146.424 120.763 167.798 1.00 61.16  ? 10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 145.248 120.528 168.103 1.00 64.46  ? 10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 146.966 121.496 165.429 1.00 59.12  ? 10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 146.875 122.711 164.504 1.00 60.27  ? 10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 145.930 120.457 165.038 1.00 62.42  ? 10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.260 122.423 163.075 1.00 62.09  ? 10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 147.433 120.018 168.255 1.00 62.14  ? 11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 147.182 118.911 169.173 1.00 61.22  ? 11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 146.610 119.409 170.496 1.00 59.49  ? 11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 145.706 118.784 171.062 1.00 62.54  ? 11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 148.470 118.119 169.398 1.00 63.90  ? 11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 148.643 117.577 170.808 1.00 65.01  ? 11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 150.088 117.257 171.134 1.00 67.38  ? 11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 150.797 116.648 170.334 1.00 67.32  ? 11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 150.532 117.669 172.316 1.00 63.48  ? 11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 147.121 120.534 171.003 1.00 60.95  ? 12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 146.557 121.122 172.214 1.00 63.30  ? 12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 145.142 121.629 171.970 1.00 63.33  ? 12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 144.281 121.540 172.853 1.00 64.36  ? 12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 147.455 122.252 172.716 1.00 62.82  ? 12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 148.523 121.870 173.741 1.00 63.35  ? 12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 149.618 122.922 173.791 1.00 61.97  ? 12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 147.900 121.681 175.112 1.00 62.42  ? 12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 144.885 122.173 170.779 1.00 61.53  ? 13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 143.530 122.571 170.416 1.00 62.41  ? 13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 142.637 121.357 170.200 1.00 63.86  ? 13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 141.425 121.430 170.433 1.00 66.76  ? 13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 143.564 123.448 169.164 1.00 60.15  ? 13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 142.191 123.677 168.571 1.00 61.11  ? 13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 141.801 123.017 167.608 1.00 63.01  ? 13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 141.448 124.616 169.143 1.00 64.21  ? 13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 143.213 120.236 169.760 1.00 64.46  ? 14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 142.463 118.994 169.627 1.00 64.14  ? 14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 142.020 118.433 170.971 1.00 63.39  ? 14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 141.138 117.569 171.002 1.00 68.38  ? 14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 143.305 117.950 168.892 1.00 66.41  ? 14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 143.104 117.992 167.394 1.00 66.22  ? 14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 142.446 118.890 166.874 1.00 64.63  ? 14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 143.671 117.019 166.691 1.00 65.10  ? 14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 142.605 118.900 172.071 1.00 66.02  ? 15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 142.269 118.422 173.404 1.00 67.69  ? 15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 140.996 119.054 173.951 1.00 70.58  ? 15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 140.576 118.703 175.059 1.00 71.34  ? 15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 143.439 118.686 174.357 1.00 69.79  ? 15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 143.519 117.730 175.536 1.00 72.83  ? 15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 144.917 117.189 175.751 1.00 73.23  ? 15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 145.889 117.932 175.502 1.00 73.16  ? 15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 145.044 116.019 176.170 1.00 71.66  ? 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 140.383 119.980 173.210 1.00 73.58  ? 16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 139.140 120.600 173.663 1.00 72.33  ? 16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 138.050 119.548 173.821 1.00 70.24  ? 16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 137.372 119.479 174.853 1.00 71.18  ? 16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 138.709 121.708 172.684 1.00 70.10  ? 16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 139.708 122.869 172.702 1.00 67.35  ? 16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 137.302 122.192 173.011 1.00 71.42  ? 16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 139.476 123.868 173.807 1.00 68.70  ? 16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 137.875 118.702 172.804 1.00 69.85  ? 17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 136.813 117.703 172.822 1.00 75.05  ? 17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 137.181 116.452 173.606 1.00 75.10  ? 17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 136.304 115.616 173.853 1.00 73.32  ? 17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 136.420 117.326 171.395 1.00 72.48  ? 17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 136.911 118.303 170.350 1.00 72.44  ? 17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 135.933 119.815 170.385 1.00 78.66  ? 17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 134.340 119.198 169.845 1.00 74.76  ? 17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 138.443 116.297 174.001 1.00 75.50  ? 18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 138.823 115.184 174.865 1.00 75.01  ? 18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 138.307 115.504 176.259 1.00 74.94  ? 18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 138.940 116.249 177.014 1.00 77.40  ? 18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 140.346 114.940 174.874 1.00 74.93  ? 18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 140.943 114.889 173.459 1.00 74.40  ? 18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 140.674 113.666 175.638 1.00 73.63  ? 18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 140.048 114.285 172.380 1.00 71.88  ? 18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 137.154 114.943 176.610 1.00 78.03  ? 19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 136.474 115.317 177.841 1.00 79.69  ? 19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 137.073 114.581 179.031 1.00 80.63  ? 19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 137.117 113.346 179.053 1.00 79.21  ? 19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 134.981 115.014 177.734 1.00 80.20  ? 19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 134.280 115.729 176.593 1.00 80.15  ? 19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 132.796 115.424 176.540 1.00 80.35  ? 19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 132.268 114.708 177.390 1.00 79.13  ? 19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 132.115 115.963 175.536 1.00 78.87  ? 19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 137.534 115.340 180.020 1.00 86.11  ? 20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 137.951 114.792 181.301 1.00 88.22  ? 20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 136.913 115.158 182.353 1.00 88.53  ? 20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 136.391 116.279 182.362 1.00 87.22  ? 20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 139.343 115.297 181.708 1.00 86.39  ? 20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 139.390 116.703 182.286 1.00 86.78  ? 20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 140.738 117.359 182.038 1.00 86.68  ? 20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 140.682 118.856 182.293 1.00 87.27  ? 20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 141.936 119.538 181.871 1.00 86.86  ? 20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 136.582 114.190 183.209 1.00 90.74  ? 21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 135.545 114.338 184.229 1.00 91.48  ? 21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 134.191 114.695 183.616 1.00 91.51  ? 21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 133.344 115.306 184.275 1.00 90.46  ? 21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 135.956 115.373 185.286 1.00 91.80  ? 21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 135.136 115.272 186.560 1.00 92.18  ? 21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 135.367 114.327 187.343 1.00 90.90  ? 21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 134.267 116.142 186.782 1.00 91.57  ? 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 133.973 114.324 182.356 1.00 87.44  ? 22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 132.730 114.625 181.677 1.00 86.02  ? 22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 132.587 116.050 181.194 1.00 87.29  ? 22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 131.500 116.426 180.745 1.00 85.40  ? 22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 133.629 116.889 181.272 1.00 89.39  ? 23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 133.614 118.284 180.793 1.00 86.41  ? 23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 134.566 118.474 179.620 1.00 85.97  ? 23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 135.600 117.815 179.555 1.00 86.49  ? 23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 133.982 119.287 181.899 1.00 84.21  ? 23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.039 119.280 183.109 1.00 87.21  ? 23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 133.082 120.599 183.899 1.00 88.14  ? 23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 134.490 121.028 184.332 1.00 87.00  ? 23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 134.491 122.341 185.026 1.00 85.93  ? 23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 134.240 119.381 178.708 1.00 78.09  ? 24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 135.190 119.849 177.697 1.00 75.81  ? 24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 136.364 120.588 178.357 1.00 76.76  ? 24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 136.188 121.358 179.297 1.00 74.77  ? 24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 134.485 120.758 176.693 1.00 72.54  ? 24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 133.569 120.031 175.736 1.00 74.08  ? 24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 132.242 119.731 176.094 1.00 75.01  ? 24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 134.035 119.670 174.470 1.00 74.62  ? 24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 131.395 119.081 175.189 1.00 73.97  ? 24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 133.193 118.991 173.570 1.00 76.31  ? 24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 131.872 118.706 173.923 1.00 74.51  ? 24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 137.566 120.370 177.841 1.00 76.29  ? 25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 138.802 121.029 178.269 1.00 76.28  ? 25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 138.964 122.350 177.517 1.00 76.65  ? 25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 139.827 122.520 176.656 1.00 77.38  ? 25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 140.000 120.113 178.055 1.00 76.64  ? 25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 139.904 118.775 178.759 1.00 76.05  ? 25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 141.114 117.900 178.501 1.00 77.45  ? 25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 142.138 118.024 179.173 1.00 78.21  ? 25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 141.003 117.008 177.527 1.00 76.84  ? 25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 138.099 123.303 177.870 1.00 67.63  ? 26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 138.151 124.621 177.247 1.00 65.77  ? 26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 139.411 125.390 177.614 1.00 65.50  ? 26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 139.789 126.317 176.890 1.00 65.66  ? 26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 136.913 125.431 177.632 1.00 64.05  ? 26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 135.646 124.927 177.007 1.00 65.03  ? 26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 135.583 124.678 175.647 1.00 62.83  ? 26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 134.519 124.699 177.778 1.00 64.06  ? 26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 134.421 124.213 175.069 1.00 62.63  ? 26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 133.354 124.234 177.204 1.00 61.75  ? 26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 133.306 123.992 175.847 1.00 63.61  ? 26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 140.072 125.029 178.717 1.00 69.38  ? 27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 141.317 125.688 179.089 1.00 67.57  ? 27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 142.466 125.312 178.165 1.00 68.02  ? 27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 143.511 125.971 178.198 1.00 68.62  ? 27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 141.680 125.350 180.536 1.00 69.20  ? 27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 140.716 125.957 181.535 1.00 72.40  ? 27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 140.305 127.120 181.336 1.00 70.57  ? 27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 140.370 125.273 182.520 1.00 70.97  ? 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 142.299 124.273 177.345 1.00 68.80  ? 28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 143.349 123.873 176.418 1.00 69.13  ? 28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 143.475 124.829 175.239 1.00 71.51  ? 28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 144.509 124.826 174.563 1.00 74.35  ? 28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 143.088 122.455 175.908 1.00 68.60  ? 28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 143.360 121.365 176.929 1.00 69.70  ? 28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 144.849 121.133 177.109 1.00 71.36  ? 28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 145.124 120.189 178.267 1.00 69.37  ? 28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 146.564 119.819 178.349 1.00 69.17  ? 28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 142.447 125.639 174.975 1.00 67.38  ? 29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 142.516 126.579 173.861 1.00 65.88  ? 29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 143.515 127.696 174.142 1.00 64.02  ? 29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 144.234 128.134 173.237 1.00 63.26  ? 29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 141.129 127.150 173.574 1.00 66.46  ? 29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 140.897 127.400 172.097 1.00 66.25  ? 29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.503 126.688 171.270 1.00 65.70  ? 29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 140.097 128.297 171.764 1.00 64.30  ? 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 143.567 128.176 175.387 1.00 62.29  ? 30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 144.594 129.143 175.762 1.00 63.48  ? 30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 145.984 128.533 175.647 1.00 64.91  ? 30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 146.919 129.181 175.160 1.00 65.92  ? 30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 144.341 129.650 177.182 1.00 63.14  ? 30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.836 131.062 177.435 1.00 65.47  ? 30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.899 131.085 178.520 1.00 65.48  ? 30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.478 131.966 179.683 1.00 66.08  ? 30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 144.699 133.149 179.226 1.00 64.83  ? 30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 146.135 127.282 176.088 1.00 65.54  ? 31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 147.389 126.570 175.875 1.00 63.89  ? 31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 147.675 126.411 174.389 1.00 64.40  ? 31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 148.827 126.521 173.954 1.00 65.27  ? 31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 147.340 125.206 176.562 1.00 66.19  ? 31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 147.322 125.273 178.079 1.00 68.98  ? 31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 147.425 123.904 178.720 1.00 71.86  ? 31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.201 123.067 178.215 1.00 71.13  ? 31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 146.729 123.666 179.730 1.00 69.26  ? 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 146.633 126.153 173.595 1.00 58.67  ? 32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 146.814 126.011 172.155 1.00 57.22  ? 32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 147.316 127.306 171.528 1.00 57.84  ? 32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 148.221 127.281 170.689 1.00 62.46  ? 32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 145.506 125.571 171.500 1.00 61.39  ? 32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 146.752 128.449 171.928 1.00 56.51  ? 33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 147.182 129.723 171.354 1.00 55.05  ? 33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 148.590 130.076 171.827 1.00 56.56  ? 33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 149.399 130.623 171.066 1.00 59.52  ? 33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 146.161 130.836 171.663 1.00 55.05  ? 33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.403 131.474 173.020 1.00 57.20  ? 33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 146.211 131.900 170.580 1.00 56.79  ? 33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 148.910 129.763 173.087 1.00 62.82  ? 34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 150.261 130.011 173.577 1.00 59.16  ? 34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 151.282 129.183 172.808 1.00 62.05  ? 34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 152.334 129.697 172.404 1.00 64.90  ? 34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 150.344 129.708 175.072 1.00 62.73  ? 34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 151.428 130.459 175.781 1.00 63.98  ? 34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 152.592 129.859 176.207 1.00 64.91  ? 34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 151.520 131.760 176.142 1.00 64.39  ? 34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 153.358 130.760 176.798 1.00 64.58  ? 34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 152.731 131.922 176.771 1.00 65.25  ? 34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 150.986 127.900 172.595 1.00 59.56  ? 35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 151.872 127.051 171.808 1.00 57.86  ? 35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 151.986 127.562 170.379 1.00 60.20  ? 35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 153.084 127.621 169.817 1.00 63.75  ? 35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 151.367 125.609 171.826 1.00 58.67  ? 35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 151.984 124.844 170.806 1.00 62.18  ? 35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 150.855 127.944 169.779 1.00 57.83  ? 36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 150.864 128.482 168.424 1.00 54.84  ? 36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 151.816 129.658 168.317 1.00 53.41  ? 36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 152.724 129.662 167.479 1.00 55.47  ? 36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 149.448 128.898 168.024 1.00 52.30  ? 36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 149.325 129.426 166.611 1.00 51.84  ? 36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 149.723 128.662 165.524 1.00 54.87  ? 36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 148.802 130.688 166.367 1.00 51.29  ? 36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 149.608 129.141 164.234 1.00 51.99  ? 36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 148.683 131.175 165.082 1.00 51.17  ? 36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 149.087 130.398 164.019 1.00 51.69  ? 36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 148.971 130.880 162.736 1.00 55.53  ? 36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 151.657 130.642 169.200 1.00 57.27  ? 37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 152.528 131.809 169.157 1.00 56.10  ? 37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 153.982 131.407 169.354 1.00 58.60  ? 37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 154.801 131.575 168.445 1.00 62.75  ? 37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.089 132.836 170.199 1.00 56.88  ? 37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 151.105 133.831 169.670 1.00 55.99  ? 37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.532 134.893 168.891 1.00 57.05  ? 37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 149.754 133.696 169.928 1.00 56.48  ? 37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.631 135.808 168.393 1.00 58.85  ? 37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 148.850 134.608 169.432 1.00 58.04  ? 37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 149.288 135.665 168.664 1.00 60.09  ? 37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 154.286 130.763 170.485 1.00 63.76  ? 38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 155.674 130.516 170.869 1.00 64.59  ? 38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 156.395 129.675 169.822 1.00 63.92  ? 38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 157.575 129.908 169.529 1.00 65.77  ? 38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 155.725 129.857 172.262 1.00 64.22  ? 38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 157.129 129.369 172.578 1.00 63.70  ? 38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 155.247 130.835 173.325 1.00 60.79  ? 38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 155.708 128.699 169.224 1.00 60.31  ? 39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 156.378 127.755 168.343 1.00 63.66  ? 39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 156.298 128.113 166.864 1.00 65.87  ? 39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 157.121 127.614 166.089 1.00 68.18  ? 39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 155.805 126.348 168.547 1.00 62.61  ? 39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 155.673 125.981 170.012 1.00 65.75  ? 39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 156.435 126.531 170.833 1.00 63.18  ? 39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 154.808 125.143 170.341 1.00 66.39  ? 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 155.350 128.948 166.439 1.00 62.03  ? 40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 155.253 129.308 165.031 1.00 61.39  ? 40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 155.365 130.803 164.792 1.00 66.64  ? 40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 156.143 131.230 163.933 1.00 69.24  ? 40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 153.930 128.784 164.450 1.00 58.98  ? 40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 153.785 129.001 162.962 1.00 59.45  ? 40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 154.735 128.515 162.075 1.00 61.31  ? 40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 152.698 129.690 162.445 1.00 61.54  ? 40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 154.605 128.711 160.713 1.00 64.39  ? 40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 152.559 129.890 161.086 1.00 63.32  ? 40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 153.516 129.399 160.225 1.00 65.73  ? 40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 153.382 129.596 158.869 1.00 65.00  ? 40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 154.623 131.618 165.541 1.00 63.61  ? 41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.453 133.016 165.162 1.00 59.75  ? 41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.700 133.819 165.498 1.00 56.55  ? 41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 156.229 134.549 164.653 1.00 60.66  ? 41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 153.201 133.600 165.839 1.00 55.30  ? 41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 151.958 132.805 165.438 1.00 57.20  ? 41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 153.014 135.046 165.447 1.00 57.64  ? 41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 151.706 132.792 163.951 1.00 54.63  ? 41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 156.191 133.696 166.733 1.00 56.48  ? 42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.405 134.407 167.118 1.00 60.90  ? 42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.604 133.927 166.312 1.00 64.89  ? 42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.464 134.727 165.925 1.00 65.04  ? 42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.659 134.238 168.615 1.00 60.93  ? 42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.532 134.791 169.462 1.00 61.99  ? 42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.667 135.515 168.968 1.00 64.09  ? 42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.536 134.456 170.746 1.00 62.40  ? 42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 158.683 132.619 166.054 1.00 66.57  ? 43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 159.797 132.082 165.282 1.00 64.67  ? 43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.750 132.551 163.832 1.00 62.93  ? 43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.797 132.801 163.223 1.00 64.55  ? 43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 159.793 130.555 165.352 1.00 65.00  ? 43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 159.903 130.002 166.762 1.00 65.55  ? 43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 160.045 128.495 166.785 1.00 66.20  ? 43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.392 127.877 165.779 1.00 64.01  ? 43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 159.780 127.893 167.939 1.00 63.74  ? 43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.551 132.679 163.262 1.00 61.49  ? 44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.382 133.036 161.862 1.00 62.60  ? 44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 158.042 134.509 161.665 1.00 63.19  ? 44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.568 134.890 160.590 1.00 64.46  ? 44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 157.308 132.155 161.222 1.00 59.93  ? 44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.708 130.694 161.171 1.00 64.31  ? 44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.055 130.098 162.190 1.00 63.64  ? 44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 157.658 130.108 159.981 1.00 64.38  ? 44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 158.270 135.341 162.676 1.00 61.24  ? 45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 158.096 136.782 162.562 1.00 61.46  ? 45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 159.464 137.435 162.447 1.00 61.99  ? 45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 160.310 137.274 163.334 1.00 61.64  ? 45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 157.344 137.354 163.766 1.00 61.12  ? 45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.087 136.682 163.913 1.00 63.56  ? 45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 157.096 138.843 163.580 1.00 60.29  ? 45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 159.678 138.169 161.360 1.00 64.29  ? 46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 160.940 138.869 161.152 1.00 65.37  ? 46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 160.952 140.095 162.057 1.00 65.47  ? 46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 159.967 140.838 162.129 1.00 63.07  ? 46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.132 139.247 159.675 1.00 63.51  ? 46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 159.884 138.911 158.871 1.00 62.90  ? 46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.521 140.712 159.510 1.00 62.54  ? 46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.049 140.283 162.781 1.00 67.79  ? 47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 162.161 141.351 163.762 1.00 67.41  ? 47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 163.220 142.355 163.326 1.00 69.35  ? 47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 164.263 141.979 162.781 1.00 69.16  ? 47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 162.507 140.785 165.141 1.00 67.70  ? 47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 162.188 141.714 166.276 1.00 69.36  ? 47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 160.920 141.738 166.831 1.00 68.25  ? 47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 163.157 142.555 166.796 1.00 67.61  ? 47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 160.621 142.588 167.878 1.00 68.23  ? 47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 162.865 143.408 167.844 1.00 68.17  ? 47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 161.595 143.424 168.385 1.00 70.51  ? 47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 162.943 143.630 163.569 1.00 68.45  ? 48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 163.846 144.718 163.231 1.00 65.06  ? 48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 164.375 145.368 164.502 1.00 66.45  ? 48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 163.715 145.357 165.545 1.00 68.68  ? 48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.148 145.768 162.360 1.00 65.47  ? 48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 162.590 145.220 161.076 1.00 67.36  ? 48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 161.343 144.619 161.044 1.00 66.41  ? 48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 163.309 145.317 159.898 1.00 66.35  ? 48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 160.827 144.123 159.863 1.00 66.78  ? 48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 162.799 144.821 158.715 1.00 66.93  ? 48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 161.557 144.223 158.697 1.00 67.35  ? 48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 165.579 145.937 164.403 1.00 72.66  ? 49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 166.217 146.538 165.569 1.00 74.94  ? 49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 165.395 147.691 166.133 1.00 75.13  ? 49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 165.465 147.972 167.335 1.00 76.04  ? 49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 167.623 147.013 165.208 1.00 75.48  ? 49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 168.308 146.155 164.192 1.00 78.05  ? 49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.797 146.653 163.004 1.00 77.54  ? 49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 168.585 144.829 164.185 1.00 76.81  ? 49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 169.347 145.672 162.309 1.00 75.38  ? 49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 169.231 144.555 163.004 1.00 74.79  ? 49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 164.616 148.363 165.291 1.00 72.07  ? 50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 163.761 149.454 165.737 1.00 71.74  ? 50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 162.621 149.609 164.740 1.00 72.88  ? 50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 162.659 149.069 163.633 1.00 71.75  ? 50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 164.548 150.760 165.890 1.00 70.72  ? 50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 165.239 151.177 164.610 1.00 72.34  ? 50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.481 150.357 163.725 1.00 71.16  ? 50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 165.562 152.461 164.503 1.00 72.27  ? 50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 161.594 150.354 165.158 1.00 66.17  ? 51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 160.438 150.570 164.295 1.00 65.48  ? 51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 160.815 151.323 163.026 1.00 66.52  ? 51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.170 151.148 161.986 1.00 69.80  ? 51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 159.349 151.327 165.054 1.00 63.73  ? 51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.012 151.511 164.336 1.00 62.24  ? 51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 157.463 150.176 163.860 1.00 60.79  ? 51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.015 152.214 165.237 1.00 63.45  ? 51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 161.848 152.168 163.092 1.00 65.02  ? 52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.286 152.892 161.903 1.00 64.20  ? 52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 162.741 151.930 160.815 1.00 67.50  ? 52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.379 152.090 159.644 1.00 67.20  ? 52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.409 153.864 162.265 1.00 66.55  ? 52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.601 155.020 161.287 1.00 67.64  ? 52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 162.335 155.321 160.497 1.00 68.27  ? 52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 162.568 156.434 159.490 1.00 67.36  ? 52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 162.593 157.775 160.139 1.00 67.07  ? 52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 163.528 150.917 161.187 1.00 71.09  ? 53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 163.970 149.927 160.212 1.00 69.85  ? 53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 162.795 149.159 159.626 1.00 69.01  ? 53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 162.759 148.914 158.416 1.00 69.52  ? 53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 164.969 148.964 160.852 1.00 69.09  ? 53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 165.719 148.099 159.852 1.00 70.95  ? 53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 166.352 146.879 160.494 1.00 72.57  ? 53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 166.194 146.698 161.721 1.00 72.58  ? 53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.008 146.099 159.772 1.00 69.72  ? 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 161.824 148.780 160.461 1.00 64.00  ? 54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 160.654 148.058 159.972 1.00 62.67  ? 54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 159.851 148.890 158.981 1.00 59.67  ? 54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 159.488 148.400 157.906 1.00 63.29  ? 54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 159.766 147.640 161.142 1.00 64.37  ? 54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 158.493 146.930 160.717 1.00 64.09  ? 54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.105 145.846 161.703 1.00 60.46  ? 54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 156.608 145.605 161.697 1.00 61.51  ? 54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 156.238 144.450 162.558 1.00 63.60  ? 54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 159.567 150.147 159.326 1.00 62.07  ? 55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 158.804 151.006 158.429 1.00 64.91  ? 55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 159.561 151.277 157.137 1.00 66.78  ? 55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 158.963 151.270 156.055 1.00 67.30  ? 55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 158.447 152.315 159.130 1.00 64.70  ? 55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 157.522 152.184 160.340 1.00 63.75  ? 55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.435 153.500 161.087 1.00 64.36  ? 55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.142 151.712 159.911 1.00 62.53  ? 55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 160.874 151.517 157.224 1.00 68.84  ? 56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 161.664 151.734 156.018 1.00 68.14  ? 56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 161.655 150.501 155.124 1.00 67.79  ? 56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 161.482 150.612 153.906 1.00 69.17  ? 56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.096 152.116 156.394 1.00 69.59  ? 56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.198 153.526 156.939 1.00 73.19  ? 56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 162.167 154.229 156.971 1.00 75.22  ? 56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 164.310 153.930 157.340 1.00 70.00  ? 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 161.831 149.315 155.714 1.00 61.06  ? 57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 161.831 148.085 154.931 1.00 60.29  ? 57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 160.479 147.849 154.273 1.00 61.51  ? 57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 160.412 147.444 153.107 1.00 66.42  ? 57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 162.220 146.902 155.823 1.00 60.89  ? 57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 161.997 145.535 155.208 1.00 61.71  ? 57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 160.777 144.881 155.332 1.00 63.02  ? 57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 163.011 144.897 154.505 1.00 62.44  ? 57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 160.572 143.636 154.772 1.00 65.37  ? 57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 162.815 143.650 153.942 1.00 61.82  ? 57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 161.594 143.024 154.079 1.00 64.63  ? 57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 161.393 141.783 153.521 1.00 65.19  ? 57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 159.389 148.093 155.002 1.00 58.69  ? 58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.065 147.850 154.445 1.00 59.05  ? 58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 157.695 148.869 153.373 1.00 57.42  ? 58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.046 148.508 152.385 1.00 57.70  ? 58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.022 147.841 155.562 1.00 58.04  ? 58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 157.149 146.654 156.523 1.00 57.88  ? 58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 156.315 146.862 157.772 1.00 56.95  ? 58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 156.760 145.358 155.830 1.00 57.57  ? 58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.094 150.132 153.537 1.00 62.58  ? 59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 157.808 151.132 152.515 1.00 63.58  ? 59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 158.650 150.883 151.268 1.00 65.89  ? 59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.148 150.953 150.140 1.00 65.27  ? 59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.028 152.547 153.079 1.00 61.32  ? 59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 158.079 153.567 151.954 1.00 60.69  ? 59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 156.930 152.899 154.069 1.00 61.29  ? 59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 159.939 150.581 151.449 1.00 68.27  ? 60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 160.829 150.416 150.304 1.00 67.61  ? 60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 160.516 149.151 149.513 1.00 69.29  ? 60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 160.717 149.124 148.293 1.00 69.09  ? 60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 162.287 150.419 150.768 1.00 65.96  ? 60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 162.753 149.126 151.423 1.00 68.07  ? 60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 164.188 149.199 151.908 1.00 71.03  ? 60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 164.548 150.204 152.557 1.00 71.14  ? 60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 164.955 148.250 151.643 1.00 69.23  ? 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 160.028 148.102 150.174 1.00 63.35  ? 61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 159.738 146.834 149.517 1.00 63.29  ? 61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 158.306 146.749 149.003 1.00 63.09  ? 61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 157.791 145.641 148.817 1.00 62.45  ? 61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 160.027 145.670 150.465 1.00 64.26  ? 61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 161.492 145.290 150.492 1.00 64.62  ? 61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 161.954 144.493 149.674 1.00 64.75  ? 61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 162.234 145.855 151.436 1.00 65.53  ? 61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 157.656 147.893 148.775 1.00 63.03  ? 62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 156.306 147.952 148.215 1.00 61.48  ? 62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 155.291 147.202 149.076 1.00 63.51  ? 62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 154.335 146.619 148.558 1.00 64.10  ? 62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 156.275 147.425 146.776 1.00 63.02  ? 62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 157.334 148.032 145.867 1.00 65.06  ? 62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 157.127 149.515 145.638 1.00 64.52  ? 62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 156.114 149.933 145.080 1.00 62.76  ? 62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 158.091 150.320 146.069 1.00 62.11  ? 62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 155.489 147.209 150.394 1.00 66.92  ? 63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 154.513 146.626 151.308 1.00 62.27  ? 63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 153.537 147.670 151.835 1.00 58.72  ? 63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 152.346 147.381 151.993 1.00 63.58  ? 63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 155.221 145.947 152.483 1.00 58.52  ? 63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 155.901 144.647 152.130 1.00 61.69  ? 63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 155.180 143.581 151.612 1.00 59.80  ? 63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 157.264 144.483 152.324 1.00 61.32  ? 63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 155.801 142.390 151.290 1.00 62.02  ? 63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 157.894 143.298 152.007 1.00 60.03  ? 63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 157.160 142.255 151.491 1.00 63.11  ? 63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 157.789 141.074 151.173 1.00 64.00  ? 63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.022 148.877 152.110 1.00 53.05  ? 64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 153.207 149.968 152.618 1.00 50.05  ? 64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.230 151.135 151.644 1.00 56.23  ? 64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.219 151.358 150.939 1.00 60.64  ? 64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 153.704 150.462 153.980 1.00 54.44  ? 64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 153.389 149.555 155.144 1.00 56.77  ? 64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 152.565 148.450 154.992 1.00 52.99  ? 64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 153.914 149.815 156.400 1.00 56.43  ? 64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 152.279 147.625 156.060 1.00 48.25  ? 64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 153.633 149.002 157.471 1.00 53.83  ? 64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 152.818 147.907 157.297 1.00 53.94  ? 64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 152.543 147.096 158.371 1.00 59.66  ? 64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 152.130 151.880 151.612 1.00 59.75  ? 65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.120 153.154 150.908 1.00 57.65  ? 65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 152.934 154.173 151.695 1.00 60.33  ? 65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 152.788 154.290 152.914 1.00 59.02  ? 65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 150.687 153.649 150.723 1.00 55.75  ? 65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 149.770 152.666 150.020 1.00 55.36  ? 65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 148.329 153.134 150.002 1.00 60.65  ? 65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 147.912 153.817 150.960 1.00 60.95  ? 65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 147.612 152.818 149.028 1.00 59.25  ? 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 153.801 154.906 150.998 1.00 61.05  ? 66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 154.567 155.957 151.653 1.00 60.42  ? 66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 153.742 157.217 151.871 1.00 59.84  ? 66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.130 158.068 152.679 1.00 60.69  ? 66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 155.820 156.282 150.836 1.00 60.64  ? 66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 156.889 157.049 151.599 1.00 61.74  ? 66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 158.235 157.025 150.900 1.00 63.13  ? 66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 158.329 156.428 149.808 1.00 62.00  ? 66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 159.200 157.599 151.447 1.00 62.09  ? 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.611 157.349 151.176 1.00 60.05  ? 67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 151.800 158.556 151.289 1.00 60.18  ? 67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.151 158.665 152.664 1.00 61.48  ? 67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.211 159.720 153.305 1.00 61.63  ? 67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 150.739 158.576 150.190 1.00 59.76  ? 67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.299 158.418 148.786 1.00 60.11  ? 67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.191 156.996 148.272 1.00 62.77  ? 67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.055 156.504 148.114 1.00 64.33  ? 67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.243 156.370 148.026 1.00 60.93  ? 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 150.530 157.582 153.138 1.00 56.23  ? 68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 149.756 157.666 154.374 1.00 53.99  ? 68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 150.651 157.738 155.606 1.00 53.69  ? 68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 150.215 158.223 156.656 1.00 55.33  ? 68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 148.788 156.483 154.474 1.00 54.75  ? 68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.334 155.304 155.228 1.00 51.20  ? 68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.197 154.413 154.615 1.00 53.81  ? 68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 148.965 155.074 156.544 1.00 48.11  ? 68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.694 153.325 155.305 1.00 54.59  ? 68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 149.459 153.988 157.236 1.00 51.22  ? 68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.324 153.111 156.616 1.00 55.46  ? 68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 151.893 157.264 155.505 1.00 53.34  ? 69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 152.817 157.358 156.627 1.00 52.57  ? 69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 153.550 158.692 156.676 1.00 54.56  ? 69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.185 158.997 157.691 1.00 55.29  ? 69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 153.839 156.220 156.569 1.00 54.01  ? 69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.364 154.845 157.044 1.00 55.70  ? 69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.421 153.787 156.770 1.00 54.24  ? 69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 152.998 154.872 158.518 1.00 52.83  ? 69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 153.478 159.488 155.607 1.00 60.90  ? 70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.218 160.742 155.547 1.00 56.67  ? 70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 153.566 161.864 156.345 1.00 59.03  ? 70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.258 162.815 156.721 1.00 58.17  ? 70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 154.387 161.183 154.092 1.00 54.66  ? 70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 153.262 160.815 153.315 1.00 56.83  ? 70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.260 161.782 156.612 1.00 54.54  ? 71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.597 162.841 157.365 1.00 53.90  ? 71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 151.967 162.834 158.841 1.00 56.29  ? 71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.648 163.799 159.544 1.00 57.40  ? 71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.074 162.745 157.228 1.00 52.37  ? 71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.427 162.586 155.850 1.00 56.01  ? 71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 149.352 161.130 155.438 1.00 56.60  ? 71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 148.045 163.220 155.834 1.00 57.35  ? 71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 152.624 161.785 159.324 1.00 52.87  ? 72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.043 161.688 160.713 1.00 54.41  ? 72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 154.560 161.737 160.799 1.00 56.57  ? 72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.257 161.087 160.014 1.00 54.45  ? 72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 152.551 160.391 161.361 1.00 55.16  ? 72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.092 160.070 161.141 1.00 50.93  ? 72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 150.682 159.343 160.034 1.00 52.08  ? 72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.127 160.471 162.054 1.00 49.54  ? 72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.355 159.038 159.831 1.00 52.08  ? 72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 148.796 160.171 161.860 1.00 51.01  ? 72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 148.416 159.453 160.748 1.00 53.83  ? 72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.090 159.152 160.548 1.00 57.99  ? 72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.067 162.509 161.754 1.00 64.13  ? 73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.471 162.407 162.116 1.00 62.89  ? 73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 156.735 161.041 162.737 1.00 66.19  ? 73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 155.832 160.401 163.282 1.00 66.09  ? 73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 156.859 163.519 163.088 1.00 61.05  ? 73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.245 163.325 164.349 1.00 62.55  ? 73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 157.986 160.583 162.637 1.00 65.48  ? 74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.299 159.234 163.097 1.00 63.03  ? 74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.031 159.053 164.584 1.00 61.13  ? 74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 157.689 157.948 165.016 1.00 61.90  ? 74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.750 158.873 162.795 1.00 63.93  ? 74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.136 157.517 163.307 1.00 64.97  ? 74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.521 156.379 162.814 1.00 62.48  ? 74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.082 157.384 164.308 1.00 65.31  ? 74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 159.857 155.132 163.295 1.00 61.88  ? 74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.423 156.137 164.792 1.00 65.09  ? 74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 160.809 155.011 164.287 1.00 64.84  ? 74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.184 160.110 165.384 1.00 64.99  ? 75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 157.880 159.986 166.807 1.00 68.15  ? 75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.397 159.718 167.027 1.00 67.25  ? 75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.023 158.949 167.921 1.00 65.06  ? 75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.330 161.241 167.558 1.00 67.30  ? 75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 157.744 162.543 167.042 1.00 67.35  ? 75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 156.532 162.991 167.834 1.00 70.10  ? 75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 156.271 162.406 168.905 1.00 68.22  ? 75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 155.841 163.930 167.385 1.00 68.00  ? 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.536 160.327 166.208 1.00 63.74  ? 76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.101 160.093 166.325 1.00 61.81  ? 76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 153.750 158.645 166.001 1.00 61.46  ? 76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 152.978 158.005 166.724 1.00 66.02  ? 76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.344 161.051 165.405 1.00 64.60  ? 76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.449 162.494 165.854 1.00 65.83  ? 76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.137 162.776 167.031 1.00 62.35  ? 76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.842 163.347 165.031 1.00 68.45  ? 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.316 158.109 164.917 1.00 54.30  ? 77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.074 156.713 164.555 1.00 55.23  ? 77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 154.618 155.785 165.633 1.00 55.69  ? 77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 153.987 154.782 165.992 1.00 56.62  ? 77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 154.695 156.406 163.181 1.00 55.51  ? 77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.008 157.224 162.089 1.00 58.23  ? 77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 154.599 154.923 162.868 1.00 54.46  ? 77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 154.723 157.184 160.761 1.00 55.10  ? 77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 155.802 156.103 166.157 1.00 60.08  ? 78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.391 155.300 167.220 1.00 58.26  ? 78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.487 155.266 168.444 1.00 57.82  ? 78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.254 154.199 169.020 1.00 60.15  ? 78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 157.768 155.855 167.583 1.00 61.02  ? 78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.681 154.881 168.303 1.00 59.79  ? 78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 159.953 155.582 168.751 1.00 61.12  ? 78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 160.556 154.925 169.979 1.00 60.93  ? 78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 161.764 154.128 169.633 1.00 59.12  ? 78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 154.950 156.421 168.842 1.00 60.19  ? 79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.081 156.464 170.013 1.00 60.16  ? 79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.743 155.783 169.745 1.00 57.12  ? 79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.159 155.192 170.660 1.00 61.73  ? 79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.895 157.915 170.464 1.00 58.37  ? 79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 152.595 158.577 170.049 1.00 60.95  ? 79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 152.411 159.935 170.702 1.00 64.61  ? 79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 153.212 160.848 170.409 1.00 63.00  ? 79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 151.475 160.090 171.512 1.00 63.21  ? 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.260 155.822 168.501 1.00 50.02  ? 80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.054 155.077 168.147 1.00 49.76  ? 80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.293 153.579 168.306 1.00 54.03  ? 80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 150.464 152.853 168.867 1.00 55.58  ? 80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 150.603 155.430 166.718 1.00 50.31  ? 80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 149.613 154.402 166.199 1.00 49.93  ? 80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 149.988 156.820 166.687 1.00 52.55  ? 80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.440 153.097 167.822 1.00 54.67  ? 81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 152.771 151.686 168.000 1.00 49.73  ? 81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 152.933 151.334 169.476 1.00 51.67  ? 81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 152.481 150.273 169.918 1.00 55.57  ? 81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.035 151.327 167.221 1.00 49.40  ? 81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 153.790 151.032 165.766 1.00 47.88  ? 81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 153.311 152.010 164.912 1.00 50.28  ? 81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.032 149.768 165.256 1.00 49.58  ? 81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 153.087 151.735 163.576 1.00 51.34  ? 81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 153.807 149.487 163.922 1.00 48.29  ? 81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 153.333 150.472 163.083 1.00 47.21  ? 81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 153.577 152.210 170.254 1.00 54.48  ? 82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 153.749 151.947 171.680 1.00 56.09  ? 82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.405 151.844 172.391 1.00 57.50  ? 82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.198 150.953 173.222 1.00 58.93  ? 82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.613 153.031 172.327 1.00 56.07  ? 82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 156.005 153.172 171.745 1.00 55.95  ? 82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.032 152.439 172.584 1.00 57.88  ? 82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 157.583 153.339 173.678 1.00 55.70  ? 82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.058 153.205 173.820 1.00 57.34  ? 82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.477 152.749 172.077 1.00 51.81  ? 83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.152 152.666 172.679 1.00 55.03  ? 83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.338 151.511 172.107 1.00 53.34  ? 83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 148.323 151.132 172.700 1.00 55.74  ? 83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.404 153.992 172.512 1.00 55.62  ? 83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 148.442 154.136 173.565 1.00 57.84  ? 83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 148.690 154.053 171.176 1.00 52.33  ? 83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 149.757 150.947 170.971 1.00 46.83  ? 84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.156 149.702 170.504 1.00 45.30  ? 84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 149.670 148.514 171.307 1.00 46.90  ? 84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 148.912 147.592 171.628 1.00 46.95  ? 84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 149.433 149.507 169.014 1.00 45.47  ? 84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 150.962 148.516 171.635 1.00 50.45  ? 85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 151.544 147.466 172.458 1.00 50.01  ? 85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 151.379 147.722 173.949 1.00 51.79  ? 85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 151.631 146.812 174.746 1.00 51.71  ? 85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 153.027 147.299 172.124 1.00 49.71  ? 85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 153.280 146.632 170.792 1.00 52.60  ? 85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 153.270 147.367 169.615 1.00 51.96  ? 85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 153.518 145.269 170.711 1.00 51.32  ? 85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 153.497 146.765 168.398 1.00 50.80  ? 85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 153.748 144.657 169.496 1.00 48.67  ? 85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 153.736 145.411 168.344 1.00 49.41  ? 85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 153.963 144.810 167.130 1.00 50.86  ? 85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 150.971 148.930 174.345 1.00 53.60  ? 86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 150.690 149.194 175.750 1.00 54.42  ? 86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 149.533 148.351 176.262 1.00 57.27  ? 86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 149.499 148.013 177.450 1.00 57.73  ? 86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 150.387 150.679 175.959 1.00 53.09  ? 86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 148.585 148.008 175.391 1.00 56.04  ? 87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 147.494 147.112 175.744 1.00 56.41  ? 87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 147.970 145.706 176.075 1.00 58.09  ? 87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 147.370 145.052 176.938 1.00 55.32  ? 87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 146.479 147.055 174.597 1.00 52.17  ? 87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 145.414 145.976 174.730 1.00 56.37  ? 87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 144.209 146.473 175.507 1.00 56.54  ? 87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 143.398 145.313 176.062 1.00 57.13  ? 87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 144.259 144.158 176.439 1.00 57.16  ? 87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 149.041 145.242 175.434 1.00 58.01  ? 88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 149.535 143.876 175.582 1.00 55.50  ? 88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 148.425 142.876 175.262 1.00 51.33  ? 88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 148.108 141.975 176.040 1.00 53.04  ? 88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 150.109 143.646 176.982 1.00 58.72  ? 88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 151.600 143.921 177.096 1.00 55.01  ? 88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 152.263 142.981 178.090 1.00 58.58  ? 88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 153.773 142.966 177.917 1.00 58.03  ? 88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 154.252 141.700 177.296 1.00 56.01  ? 88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 147.828 143.068 174.088 1.00 50.13  ? 89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 146.690 142.258 173.674 1.00 51.94  ? 89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 147.097 140.799 173.523 1.00 54.59  ? 89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 148.099 140.484 172.875 1.00 53.93  ? 89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 146.114 142.786 172.360 1.00 48.29  ? 89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 145.014 141.933 171.794 1.00 48.18  ? 89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 143.709 142.082 172.231 1.00 48.45  ? 89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 145.284 140.984 170.821 1.00 47.60  ? 89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 142.697 141.299 171.711 1.00 49.08  ? 89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 144.275 140.198 170.301 1.00 47.70  ? 89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.981 140.356 170.745 1.00 48.11  ? 89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 146.312 139.911 174.123 1.00 51.05  ? 90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 146.513 138.474 174.026 1.00 47.24  ? 90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 145.280 137.850 173.393 1.00 51.96  ? 90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 144.159 138.081 173.855 1.00 54.96  ? 90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 146.774 137.860 175.405 1.00 50.87  ? 90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 148.058 138.330 176.072 1.00 52.93  ? 90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 149.287 137.845 175.321 1.00 53.65  ? 90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 149.908 138.902 174.532 1.00 55.54  ? 90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 150.964 139.604 174.919 1.00 55.42  ? 90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.449 140.545 174.115 1.00 53.49  ? 90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 151.546 139.389 176.087 1.00 55.46  ? 90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 145.487 137.073 172.333 1.00 49.38  ? 91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 144.380 136.389 171.694 1.00 46.68  ? 91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 143.786 135.353 172.648 1.00 53.02  ? 91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 144.518 134.603 173.298 1.00 54.60  ? 91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 144.839 135.714 170.405 1.00 46.05  ? 91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.983 136.658 169.244 1.00 49.63  ? 91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.881 137.036 168.497 1.00 51.26  ? 91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 146.223 137.165 168.899 1.00 51.47  ? 91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 144.013 137.903 167.429 1.00 47.23  ? 91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 146.362 138.030 167.832 1.00 46.72  ? 91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 145.255 138.398 167.096 1.00 44.93  ? 91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.458 135.292 172.750 1.00 54.77  ? 92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 141.836 134.406 173.741 1.00 51.50  ? 92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 141.694 132.973 173.256 1.00 50.66  ? 92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 141.530 132.051 174.062 1.00 54.12  ? 92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 140.464 135.057 173.978 1.00 53.59  ? 92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 140.398 136.261 173.017 1.00 53.97  ? 92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 141.439 136.015 171.980 1.00 54.78  ? 92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 141.754 132.773 171.942 1.00 48.68  ? 93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 141.561 131.455 171.359 1.00 51.66  ? 93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 142.616 131.229 170.288 1.00 53.74  ? 93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 143.136 132.173 169.688 1.00 56.28  ? 93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 140.152 131.307 170.776 1.00 53.64  ? 93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 139.974 132.155 169.654 1.00 55.48  ? 93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 142.927 129.953 170.053 1.00 53.44  ? 94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 143.876 129.596 169.005 1.00 51.74  ? 94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 143.361 129.985 167.626 1.00 55.53  ? 94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 144.138 130.432 166.774 1.00 58.24  ? 94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 144.177 128.099 169.052 1.00 54.01  ? 94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 144.713 127.551 167.760 1.00 54.13  ? 94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 146.019 127.795 167.377 1.00 53.68  ? 94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 143.907 126.794 166.926 1.00 58.39  ? 94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 146.510 127.296 166.187 1.00 55.42  ? 94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 144.393 126.291 165.737 1.00 56.73  ? 94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 145.697 126.542 165.367 1.00 53.20  ? 94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 142.060 129.813 167.387 1.00 51.89  ? 95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 141.509 130.100 166.069 1.00 48.59  ? 95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 141.614 131.577 165.725 1.00 52.09  ? 95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 141.789 131.922 164.555 1.00 59.87  ? 95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 140.053 129.646 165.993 1.00 52.98  ? 95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 139.530 129.461 164.578 1.00 54.38  ? 95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 140.323 128.098 163.705 1.00 63.65  ? 95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 140.373 126.858 164.995 1.00 57.17  ? 95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 141.525 132.460 166.721 1.00 41.63  ? 96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 141.663 133.888 166.457 1.00 39.84  ? 96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.035 134.209 165.880 1.00 48.48  ? 96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 143.151 134.834 164.816 1.00 48.52  ? 96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.428 134.677 167.745 1.00 44.53  ? 96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 140.332 134.151 168.470 1.00 49.63  ? 96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 144.092 133.768 166.566 1.00 51.32  ? 97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.447 134.021 166.094 1.00 46.57  ? 97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 145.709 133.315 164.772 1.00 46.89  ? 97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.353 133.878 163.879 1.00 56.22  ? 97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.458 133.577 167.148 1.00 46.32  ? 97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.227 132.079 164.632 1.00 44.60  ? 98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 145.446 131.340 163.393 1.00 47.48  ? 98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 144.801 132.069 162.219 1.00 48.74  ? 98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.434 132.271 161.176 1.00 56.78  ? 98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 144.918 129.905 163.556 1.00 52.32  ? 98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 144.836 129.097 162.273 1.00 55.03  ? 98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 143.943 129.411 161.255 1.00 55.11  ? 98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.677 128.012 162.092 1.00 54.28  ? 98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 143.891 128.662 160.098 1.00 54.66  ? 98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.628 127.260 160.936 1.00 56.18  ? 98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 144.735 127.585 159.938 1.00 56.89  ? 98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 143.546 132.493 162.383 1.00 49.07  ? 99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 142.853 133.198 161.313 1.00 48.69  ? 99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.542 134.513 160.984 1.00 51.26  ? 99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.721 134.845 159.807 1.00 55.98  ? 99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.396 133.440 161.701 1.00 47.08  ? 99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 140.467 132.299 161.338 1.00 52.42  ? 99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 140.470 132.044 159.842 1.00 53.92  ? 99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 139.513 130.925 159.477 1.00 52.95  ? 99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.322 129.979 160.612 1.00 51.67  ? 99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.948 135.272 162.006 1.00 47.65  ? 100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.605 136.544 161.732 1.00 44.29  ? 100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.912 136.337 160.978 1.00 46.52  ? 100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 146.128 136.930 159.916 1.00 52.84  ? 100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.865 137.318 163.021 1.00 42.92  ? 100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 145.676 138.557 162.804 1.00 46.24  ? 100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 145.123 139.656 162.169 1.00 48.09  ? 100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 147.003 138.611 163.187 1.00 46.51  ? 100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 145.868 140.792 161.947 1.00 47.47  ? 100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 147.754 139.746 162.965 1.00 47.72  ? 100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 147.185 140.837 162.343 1.00 45.83  ? 100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.787 135.481 161.497 1.00 44.73  ? 101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 148.099 135.300 160.894 1.00 46.17  ? 101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 148.063 134.450 159.632 1.00 46.38  ? 101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 149.103 134.293 158.984 1.00 52.15  ? 101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 149.067 134.700 161.916 1.00 44.33  ? 101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.447 135.674 163.008 1.00 45.11  ? 101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 150.362 136.690 162.770 1.00 47.62  ? 101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.879 135.588 164.271 1.00 45.93  ? 101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.705 137.588 163.762 1.00 43.73  ? 101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 149.217 136.482 165.268 1.00 47.08  ? 101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 150.131 137.479 165.008 1.00 46.16  ? 101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 150.471 138.370 165.999 1.00 47.80  ? 101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 146.905 133.900 159.267 1.00 50.89  ? 102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 146.770 133.209 157.993 1.00 53.25  ? 102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.054 134.032 156.931 1.00 54.11  ? 102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.264 133.789 155.738 1.00 55.04  ? 102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.022 131.886 158.188 1.00 52.84  ? 102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 146.959 130.704 158.329 1.00 56.03  ? 102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 147.939 130.759 159.072 1.00 57.97  ? 102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 146.660 129.624 157.618 1.00 53.24  ? 102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 145.216 134.994 157.321 1.00 54.16  ? 103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 144.423 135.746 156.358 1.00 55.76  ? 103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 144.780 137.221 156.261 1.00 57.34  ? 103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 144.704 137.784 155.167 1.00 59.16  ? 103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.930 135.633 156.697 1.00 58.87  ? 103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.428 134.201 156.680 1.00 62.54  ? 103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.243 133.279 156.477 1.00 59.20  ? 103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.211 133.996 156.875 1.00 62.35  ? 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 145.166 137.864 157.361 1.00 49.48  ? 104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 145.322 139.311 157.390 1.00 50.36  ? 104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 146.733 139.786 157.692 1.00 54.20  ? 104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 147.113 140.860 157.221 1.00 58.37  ? 104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 144.368 139.930 158.425 1.00 51.68  ? 104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 142.964 139.376 158.361 1.00 52.77  ? 104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 142.035 139.894 157.470 1.00 51.46  ? 104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 142.570 138.332 159.185 1.00 51.54  ? 104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 140.754 139.389 157.405 1.00 52.15  ? 104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.292 137.821 159.126 1.00 53.00  ? 104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 140.387 138.353 158.235 1.00 53.59  ? 104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 139.112 137.848 158.174 1.00 51.67  ? 104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 147.511 139.035 158.468 1.00 53.46  ? 105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 148.860 139.467 158.809 1.00 47.94  ? 105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 149.723 139.558 157.558 1.00 54.61  ? 105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 149.717 138.656 156.717 1.00 54.54  ? 105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 149.486 138.505 159.816 1.00 44.45  ? 105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 150.464 140.657 157.438 1.00 56.73  ? 106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 151.336 140.851 156.288 1.00 50.32  ? 106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 152.473 139.840 156.314 1.00 53.90  ? 106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 153.131 139.654 157.342 1.00 54.27  ? 106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 151.896 142.271 156.274 1.00 51.90  ? 106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 152.678 142.698 155.030 1.00 55.36  ? 106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 151.907 142.373 153.763 1.00 53.78  ? 106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 153.015 144.178 155.091 1.00 54.37  ? 106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 152.703 139.191 155.180 1.00 64.20  ? 107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 153.787 138.239 155.023 1.00 64.29  ? 107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 154.696 138.687 153.887 1.00 62.73  ? 107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 154.324 139.520 153.056 1.00 59.74  ? 107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 153.257 136.826 154.752 1.00 59.97  ? 107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 152.681 136.141 155.980 1.00 59.11  ? 107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 152.080 134.792 155.631 1.00 63.30  ? 107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.534 134.100 156.868 1.00 61.77  ? 107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.665 132.943 156.522 1.00 57.87  ? 107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 155.902 138.129 153.866 1.00 67.14  ? 108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 156.867 138.473 152.836 1.00 68.34  ? 108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 156.386 137.980 151.471 1.00 69.64  ? 108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 155.406 137.240 151.352 1.00 68.15  ? 108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 158.237 137.886 153.170 1.00 68.61  ? 108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.105 136.485 153.436 1.00 69.99  ? 108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 158.825 138.574 154.391 1.00 65.33  ? 108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 157.098 138.412 150.425 1.00 71.03  ? 109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 156.690 138.087 149.061 1.00 71.19  ? 109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 156.658 136.583 148.816 1.00 72.23  ? 109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 155.892 136.111 147.969 1.00 73.23  ? 109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 157.620 138.770 148.059 1.00 71.09  ? 109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 157.448 140.276 148.037 1.00 71.09  ? 109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 156.501 140.811 148.612 1.00 72.51  ? 109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 158.365 140.967 147.369 1.00 70.48  ? 109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 157.473 135.819 149.538 1.00 73.95  ? 110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 157.452 134.366 149.438 1.00 75.11  ? 110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.472 133.723 150.410 1.00 75.35  ? 110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.387 132.491 150.453 1.00 73.44  ? 110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.857 133.797 149.667 1.00 76.10  ? 110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 159.477 134.274 150.963 1.00 76.83  ? 110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.979 135.268 151.529 1.00 75.38  ? 110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.462 133.656 151.417 1.00 74.99  ? 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.734 134.527 151.181 1.00 75.74  ? 111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.743 134.033 152.141 1.00 76.33  ? 111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.365 133.046 153.127 1.00 74.86  ? 111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 154.750 132.047 153.506 1.00 75.53  ? 111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.542 133.404 151.427 1.00 74.56  ? 111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.088 134.153 150.184 1.00 73.26  ? 111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 152.477 135.498 150.541 1.00 75.30  ? 111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.092 135.334 151.143 1.00 76.18  ? 111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 150.504 136.641 151.548 1.00 73.37  ? 111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.596 133.330 153.548 1.00 70.04  ? 112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.327 132.454 154.453 1.00 72.32  ? 112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.518 133.032 155.846 1.00 70.67  ? 112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 157.619 132.266 156.807 1.00 69.60  ? 112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 158.702 132.112 153.865 1.00 71.49  ? 112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 158.641 131.190 152.658 1.00 72.27  ? 112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 159.576 130.003 152.813 1.00 71.85  ? 112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 160.360 129.753 151.536 1.00 70.62  ? 112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.226 128.546 151.640 1.00 68.19  ? 112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.568 134.354 155.980 1.00 65.74  ? 113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.767 135.006 157.265 1.00 66.37  ? 113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 156.672 136.037 157.500 1.00 64.74  ? 113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 156.100 136.588 156.555 1.00 63.98  ? 113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 159.144 135.676 157.342 1.00 64.21  ? 113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 160.275 134.726 157.694 1.00 64.00  ? 113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 160.743 134.935 159.125 1.00 65.45  ? 113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.879 133.992 159.478 1.00 63.84  ? 113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.835 133.585 160.910 1.00 64.09  ? 113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 156.388 136.294 158.772 1.00 59.51  ? 114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 155.324 137.211 159.165 1.00 56.78  ? 114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 155.928 138.588 159.400 1.00 56.80  ? 114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 156.841 138.746 160.217 1.00 57.26  ? 114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 154.593 136.707 160.418 1.00 56.01  ? 114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.668 135.543 160.061 1.00 55.41  ? 114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.805 137.830 161.067 1.00 56.98  ? 114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.239 134.722 161.249 1.00 54.26  ? 114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 155.419 139.587 158.681 1.00 53.92  ? 115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 155.919 140.950 158.800 1.00 53.80  ? 115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 155.108 141.798 159.769 1.00 55.54  ? 115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 155.634 142.778 160.309 1.00 52.52  ? 115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 155.933 141.629 157.429 1.00 55.27  ? 115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 156.941 141.111 156.404 1.00 54.89  ? 115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 156.609 141.639 155.021 1.00 55.11  ? 115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 158.351 141.508 156.802 1.00 54.27  ? 115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 153.845 141.451 160.001 1.00 54.69  ? 116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 152.941 142.261 160.806 1.00 50.61  ? 116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 152.413 141.459 161.984 1.00 49.65  ? 116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 151.910 140.344 161.807 1.00 53.95  ? 116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 151.766 142.769 159.966 1.00 51.62  ? 116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 151.904 144.200 159.495 1.00 51.78  ? 116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 150.778 144.611 158.570 1.00 52.98  ? 116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 149.942 143.748 158.235 1.00 51.97  ? 116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 150.727 145.795 158.177 1.00 56.07  ? 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 152.522 142.031 163.179 1.00 44.56  ? 117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 151.790 141.530 164.327 1.00 45.28  ? 117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 150.350 142.036 164.270 1.00 47.69  ? 117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 149.958 142.773 163.363 1.00 53.16  ? 117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 152.456 141.977 165.628 1.00 47.26  ? 117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 153.971 142.072 165.560 1.00 50.28  ? 117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.646 140.724 165.685 1.00 54.95  ? 117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.355 140.091 166.966 1.00 54.58  ? 117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 154.121 138.797 167.123 1.00 50.20  ? 117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 153.863 138.327 168.339 1.00 48.10  ? 117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.143 137.963 166.096 1.00 47.06  ? 117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 149.547 141.625 165.253 1.00 47.70  ? 118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 148.210 142.195 165.371 1.00 43.18  ? 118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 148.284 143.676 165.714 1.00 45.72  ? 118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 147.545 144.493 165.152 1.00 48.62  ? 118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 147.401 141.434 166.420 1.00 43.55  ? 118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 145.926 141.770 166.414 1.00 42.94  ? 118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 145.194 141.743 165.236 1.00 40.64  ? 118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 145.266 142.108 167.587 1.00 42.28  ? 118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 143.846 142.045 165.225 1.00 39.38  ? 118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 143.919 142.409 167.585 1.00 40.71  ? 118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 143.214 142.377 166.402 1.00 43.10  ? 118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 141.873 142.680 166.395 1.00 44.67  ? 118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 149.190 144.040 166.620 1.00 44.60  ? 119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 149.372 145.423 167.033 1.00 43.46  ? 119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.008 146.288 165.955 1.00 46.23  ? 119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 149.908 147.516 166.037 1.00 49.65  ? 119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 150.219 145.476 168.307 1.00 46.31  ? 119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 149.591 144.768 169.494 1.00 48.03  ? 119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 150.146 143.374 169.702 1.00 52.23  ? 119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 150.262 142.626 168.708 1.00 50.82  ? 119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 150.464 143.025 170.858 1.00 50.86  ? 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 150.657 145.692 164.957 1.00 46.30  ? 120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 151.154 146.434 163.803 1.00 43.31  ? 120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 150.099 146.633 162.732 1.00 45.22  ? 120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.006 147.721 162.163 1.00 51.43  ? 120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 152.366 145.731 163.185 1.00 42.91  ? 120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 153.467 145.479 164.188 1.00 52.46  ? 120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 153.452 146.113 165.262 1.00 54.83  ? 120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.360 144.660 163.892 1.00 56.53  ? 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 149.297 145.604 162.445 1.00 42.91  ? 121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 148.146 145.792 161.571 1.00 41.08  ? 121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 147.209 146.852 162.131 1.00 43.12  ? 121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 146.758 147.742 161.402 1.00 46.61  ? 121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 147.406 144.467 161.390 1.00 36.65  ? 121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 146.354 144.482 160.295 1.00 36.11  ? 121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 146.989 144.573 158.923 1.00 41.75  ? 121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 146.305 145.530 158.065 1.00 43.85  ? 121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 146.918 146.453 157.337 1.00 41.82  ? 121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.191 147.282 156.595 1.00 39.24  ? 121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 148.236 146.568 157.335 1.00 40.97  ? 121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 146.924 146.782 163.433 1.00 43.82  ? 122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.038 147.759 164.056 1.00 42.74  ? 122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 146.650 149.152 164.005 1.00 40.76  ? 122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 145.957 150.135 163.724 1.00 42.60  ? 122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 145.702 147.328 165.494 1.00 38.53  ? 122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 144.710 146.163 165.468 1.00 34.56  ? 122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 145.162 148.498 166.301 1.00 37.63  ? 122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 144.161 145.800 166.816 1.00 41.92  ? 122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 147.954 149.264 164.270 1.00 42.66  ? 123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 148.605 150.571 164.225 1.00 40.69  ? 123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 148.575 151.161 162.821 1.00 44.21  ? 123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.318 152.357 162.651 1.00 49.44  ? 123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.044 150.460 164.723 1.00 43.68  ? 123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.113 149.712 165.922 1.00 48.95  ? 123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 148.841 150.340 161.803 1.00 42.97  ? 124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 148.834 150.830 160.427 1.00 40.40  ? 124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 147.432 151.263 160.022 1.00 44.23  ? 124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.246 152.314 159.394 1.00 47.81  ? 124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 149.396 149.753 159.480 1.00 43.12  ? 124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 150.917 149.659 159.621 1.00 40.66  ? 124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.017 150.051 158.040 1.00 40.99  ? 124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 151.599 150.984 159.894 1.00 42.48  ? 124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 146.420 150.468 160.381 1.00 39.57  ? 125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.045 150.825 160.044 1.00 34.81  ? 125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 144.633 152.103 160.766 1.00 33.35  ? 125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 143.943 152.958 160.199 1.00 44.99  ? 125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.100 149.650 160.362 1.00 35.26  ? 125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 142.662 150.057 160.165 1.00 36.83  ? 125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 144.421 148.464 159.470 1.00 36.85  ? 125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.066 152.267 162.018 1.00 28.84  ? 126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 144.752 153.480 162.764 1.00 31.16  ? 126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.421 154.702 162.151 1.00 38.81  ? 126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 144.806 155.771 162.052 1.00 47.13  ? 126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.177 153.320 164.221 1.00 38.34  ? 126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 146.687 154.569 161.748 1.00 39.45  ? 127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.378 155.679 161.102 1.00 32.49  ? 127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 146.733 156.035 159.772 1.00 34.02  ? 127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 146.676 157.215 159.408 1.00 41.58  ? 127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 148.854 155.338 160.904 1.00 39.95  ? 127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 149.713 155.257 162.167 1.00 41.46  ? 127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.084 154.697 161.839 1.00 42.75  ? 127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 149.833 156.618 162.829 1.00 39.75  ? 127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.252 155.035 159.032 1.00 37.75  ? 128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 145.503 155.320 157.813 1.00 37.33  ? 128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.208 156.059 158.126 1.00 38.09  ? 128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 143.851 157.020 157.437 1.00 48.49  ? 128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 145.210 154.023 157.060 1.00 34.96  ? 128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 144.455 154.225 155.778 1.00 40.61  ? 128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 145.123 154.565 154.615 1.00 41.41  ? 128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 143.079 154.080 155.736 1.00 40.59  ? 128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 144.434 154.754 153.434 1.00 42.12  ? 128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 142.384 154.272 154.560 1.00 39.57  ? 128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.061 154.606 153.407 1.00 44.64  ? 128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 143.493 155.620 159.165 1.00 33.09  ? 129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.212 156.232 159.504 1.00 28.64  ? 129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.378 157.683 159.936 1.00 34.25  ? 129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 141.605 158.555 159.522 1.00 36.73  ? 129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 141.528 155.436 160.614 1.00 30.85  ? 129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 140.899 154.156 160.154 1.00 29.46  ? 129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 140.705 153.903 158.808 1.00 34.31  ? 129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 140.487 153.210 161.075 1.00 28.56  ? 129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.122 152.725 158.393 1.00 36.94  ? 129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 139.900 152.034 160.666 1.00 33.29  ? 129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 139.718 151.790 159.322 1.00 36.64  ? 129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.375 157.959 160.778 1.00 43.61  ? 130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.502 159.290 161.366 1.00 43.54  ? 130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 143.871 160.336 160.322 1.00 52.08  ? 130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.374 161.468 160.372 1.00 56.60  ? 130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.534 159.267 162.489 1.00 39.12  ? 130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.746 159.982 159.381 1.00 53.02  ? 131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.167 160.870 158.298 1.00 51.19  ? 131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 145.832 162.137 158.843 1.00 52.30  ? 131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.370 163.259 158.631 1.00 55.24  ? 131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 143.986 161.215 157.383 1.00 49.89  ? 131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.427 161.763 156.042 1.00 55.79  ? 131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.264 161.171 155.362 1.00 57.32  ? 131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.864 162.902 155.654 1.00 52.23  ? 131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 146.935 161.934 159.559 1.00 49.51  ? 132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 147.760 163.022 160.038 1.00 52.55  ? 132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.543 163.422 161.482 1.00 55.13  ? 132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.294 164.263 161.990 1.00 57.29  ? 132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.547 162.853 162.157 1.00 55.83  ? 133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.245 163.191 163.544 1.00 56.63  ? 133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 146.812 162.102 164.448 1.00 55.65  ? 133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.412 160.938 164.356 1.00 58.36  ? 133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.740 163.347 163.746 1.00 55.75  ? 133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.397 164.145 164.989 1.00 60.13  ? 133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.320 164.470 165.764 1.00 61.26  ? 133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 143.203 164.448 165.191 1.00 57.82  ? 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.748 162.479 165.321 1.00 54.15  ? 134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.353 161.502 166.219 1.00 55.81  ? 134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.385 161.081 167.317 1.00 57.09  ? 134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.279 159.891 167.638 1.00 61.48  ? 134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.634 162.068 166.828 1.00 61.50  ? 134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.461 162.596 165.786 1.00 61.43  ? 134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.394 160.980 167.572 1.00 59.21  ? 134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.678 162.044 167.914 1.00 57.79  ? 135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.718 161.714 168.962 1.00 57.45  ? 135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.584 160.856 168.419 1.00 57.89  ? 135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.156 159.895 169.069 1.00 62.94  ? 135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 145.172 162.994 169.594 1.00 58.02  ? 135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.194 163.756 170.419 1.00 59.82  ? 135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 146.864 162.884 171.463 1.00 65.31  ? 135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 146.149 162.314 172.313 1.00 62.72  ? 135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.108 162.766 171.433 1.00 65.91  ? 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.088 161.182 167.225 1.00 43.44  ? 136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.050 160.362 166.611 1.00 42.59  ? 136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.581 158.978 166.258 1.00 45.89  ? 136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 142.854 157.983 166.359 1.00 48.99  ? 136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.492 161.062 165.374 1.00 46.91  ? 136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.222 160.440 164.829 1.00 46.89  ? 136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.012 160.849 165.650 1.00 46.08  ? 136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 138.741 160.799 164.820 1.00 47.04  ? 136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 139.020 160.994 163.371 1.00 51.41  ? 136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 144.848 158.894 165.842 1.00 46.91  ? 137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.445 157.593 165.561 1.00 46.02  ? 137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.524 156.741 166.820 1.00 46.98  ? 137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.241 155.539 166.783 1.00 49.04  ? 137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 146.833 157.772 164.946 1.00 42.83  ? 137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 145.899 157.347 167.948 1.00 47.90  ? 138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 145.922 156.602 169.202 1.00 47.16  ? 138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.518 156.228 169.656 1.00 46.23  ? 138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.325 155.161 170.249 1.00 48.39  ? 138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.635 157.408 170.286 1.00 49.87  ? 138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.136 157.504 170.089 1.00 50.09  ? 138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 148.733 158.585 170.967 1.00 51.49  ? 138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 149.103 158.033 172.334 1.00 53.36  ? 138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.612 159.094 173.244 1.00 49.85  ? 138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.530 157.085 169.391 1.00 45.17  ? 139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.146 156.735 169.693 1.00 41.91  ? 139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 141.697 155.523 168.885 1.00 43.88  ? 139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.053 154.613 169.421 1.00 50.81  ? 139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.233 157.929 169.422 1.00 42.49  ? 139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 140.603 158.530 170.666 1.00 48.55  ? 139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 139.376 159.361 170.352 1.00 54.41  ? 139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 139.504 160.358 169.611 1.00 50.54  ? 139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 138.281 159.016 170.844 1.00 52.88  ? 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.039 155.490 167.596 1.00 36.91  ? 140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 141.718 154.331 166.767 1.00 35.56  ? 140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.455 153.088 167.247 1.00 33.35  ? 140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 141.907 151.979 167.220 1.00 36.14  ? 140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.063 154.617 165.309 1.00 37.94  ? 140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.066 155.487 164.588 1.00 37.68  ? 140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 139.720 155.157 164.558 1.00 37.28  ? 140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.474 156.637 163.932 1.00 38.08  ? 140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 138.809 155.952 163.896 1.00 36.30  ? 140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 140.572 157.436 163.270 1.00 37.36  ? 140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.243 157.089 163.253 1.00 35.85  ? 140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.347 157.890 162.589 1.00 39.91  ? 140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 143.712 153.251 167.663 1.00 43.27  ? 141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 144.479 152.127 168.189 1.00 41.27  ? 141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 143.815 151.561 169.435 1.00 42.39  ? 141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 143.693 150.343 169.592 1.00 44.04  ? 141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 145.931 152.554 168.468 1.00 38.01  ? 141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 146.686 151.429 169.122 1.00 41.49  ? 141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 146.618 152.954 167.180 1.00 45.49  ? 141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.381 152.436 170.344 1.00 44.53  ? 142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 142.683 151.970 171.538 1.00 39.62  ? 142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 141.361 151.311 171.173 1.00 40.77  ? 142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 140.950 150.332 171.806 1.00 52.08  ? 142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 142.459 153.134 172.502 1.00 41.78  ? 142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 143.745 153.618 173.139 1.00 44.67  ? 142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 144.568 152.818 173.585 1.00 41.43  ? 142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 143.925 154.932 173.185 1.00 41.83  ? 142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 140.680 151.841 170.156 1.00 33.29  ? 143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 139.414 151.265 169.719 1.00 32.32  ? 143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 139.595 149.847 169.190 1.00 35.04  ? 143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 138.804 148.952 169.507 1.00 41.42  ? 143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 138.792 152.159 168.648 1.00 32.58  ? 143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.311 151.977 168.344 1.00 35.40  ? 143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 136.491 152.600 169.451 1.00 38.06  ? 143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 136.980 152.608 167.006 1.00 31.47  ? 143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 140.631 149.625 168.380 1.00 34.35  ? 144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 140.792 148.329 167.725 1.00 24.65  ? 144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 141.516 147.319 168.610 1.00 31.76  ? 144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 141.220 146.121 168.550 1.00 37.83  ? 144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 141.529 148.498 166.399 1.00 30.07  ? 144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 140.862 149.466 165.441 1.00 35.18  ? 144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.610 149.437 163.803 1.00 43.18  ? 144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 142.029 151.164 163.604 1.00 37.35  ? 144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 142.475 147.770 169.420 1.00 32.80  ? 145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 143.192 146.848 170.297 1.00 31.98  ? 145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 142.292 146.377 171.432 1.00 41.83  ? 145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 142.417 145.239 171.900 1.00 43.06  ? 145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 144.497 147.492 170.809 1.00 35.05  ? 145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 145.545 146.415 171.088 1.00 38.83  ? 145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 144.258 148.341 172.048 1.00 36.62  ? 145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 146.122 145.786 169.844 1.00 35.27  ? 145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 141.372 147.229 171.891 1.00 41.60  ? 146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 140.312 146.773 172.778 1.00 36.49  ? 146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 139.288 145.922 172.044 1.00 38.97  ? 146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 138.418 145.331 172.693 1.00 46.31  ? 146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 139.615 147.965 173.435 1.00 32.00  ? 146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 140.520 148.711 174.391 1.00 41.99  ? 146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 141.512 148.169 174.877 1.00 46.04  ? 146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 140.183 149.965 174.667 1.00 44.36  ? 146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 139.378 145.859 170.715 1.00 34.26  ? 147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 138.480 145.071 169.877 1.00 31.61  ? 147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 137.031 145.509 170.040 1.00 33.24  ? 147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 136.113 144.695 169.956 1.00 43.62  ? 147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 138.631 143.573 170.157 1.00 28.62  ? 147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 139.924 142.985 169.617 1.00 26.18  ? 147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 139.932 141.474 169.645 1.00 37.83  ? 147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.420 140.828 168.717 1.00 42.09  ? 147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 139.391 140.898 170.711 1.00 42.66  ? 147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 136.820 146.804 170.284 1.00 33.14  ? 148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 135.470 147.349 170.310 1.00 31.40  ? 148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 134.907 147.532 168.910 1.00 30.93  ? 148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 133.701 147.365 168.702 1.00 40.63  ? 148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 135.457 148.684 171.054 1.00 30.88  ? 148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 135.991 148.610 172.470 1.00 31.42  ? 148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 136.249 149.979 173.061 1.00 39.90  ? 148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 137.314 150.563 172.769 1.00 41.03  ? 148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 135.388 150.475 173.814 1.00 44.86  ? 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 135.757 147.871 167.944 1.00 25.10  ? 149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 135.343 148.081 166.565 1.00 26.32  ? 149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 136.275 147.316 165.642 1.00 24.62  ? 149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 137.499 147.380 165.796 1.00 35.73  ? 149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 135.346 149.569 166.211 1.00 29.27  ? 149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 135.308 149.855 164.728 1.00 29.92  ? 149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.181 149.568 163.973 1.00 26.22  ? 149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 136.401 150.421 164.085 1.00 29.15  ? 149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.145 149.832 162.617 1.00 27.79  ? 149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.373 150.688 162.733 1.00 30.68  ? 149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.243 150.392 162.004 1.00 27.20  ? 149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.213 150.657 160.655 1.00 31.23  ? 149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 135.696 146.597 164.690 1.00 20.64  ? 150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 136.464 145.824 163.717 1.00 19.56  ? 150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 136.201 146.358 162.319 1.00 27.89  ? 150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 135.076 146.209 161.805 1.00 36.16  ? 150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 136.101 144.342 163.798 1.00 28.25  ? 150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 136.763 143.477 162.739 1.00 27.96  ? 150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 138.273 143.600 162.739 1.00 27.24  ? 150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 138.931 143.320 163.740 1.00 28.32  ? 150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 138.832 144.016 161.610 1.00 32.86  ? 150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 137.177 146.994 161.673 1.00 30.99  ? 151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 136.995 147.376 160.270 1.00 25.45  ? 151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 136.791 146.145 159.403 1.00 28.86  ? 151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 137.274 145.054 159.714 1.00 37.23  ? 151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 138.302 148.099 159.921 1.00 27.49  ? 151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 138.881 148.508 161.235 1.00 29.56  ? 151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 138.462 147.461 162.217 1.00 24.60  ? 151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.047 146.326 158.316 1.00 31.11  ? 152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 135.742 145.222 157.417 1.00 25.52  ? 152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 137.024 144.568 156.910 1.00 30.42  ? 152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 138.109 145.154 156.942 1.00 37.67  ? 152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 134.901 145.707 156.238 1.00 25.58  ? 152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 135.678 146.481 155.341 1.00 32.50  ? 152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 136.886 143.326 156.448 1.00 30.76  ? 153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 138.041 142.567 155.969 1.00 32.25  ? 153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 138.834 143.294 154.891 1.00 36.26  ? 153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 140.069 143.341 155.001 1.00 38.54  ? 153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 137.578 141.182 155.488 1.00 35.19  ? 153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 137.229 140.373 156.617 1.00 34.14  ? 153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 138.678 140.493 154.697 1.00 31.90  ? 153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 138.226 143.878 153.848 1.00 32.50  ? 154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.037 144.679 152.915 1.00 28.81  ? 154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 139.753 145.835 153.589 1.00 27.13  ? 154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 140.930 146.083 153.302 1.00 38.74  ? 154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.005 145.172 151.892 1.00 31.02  ? 154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 136.915 144.181 151.952 1.00 28.48  ? 154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 136.829 143.773 153.386 1.00 26.78  ? 154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.080 146.537 154.501 1.00 24.59  ? 155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 139.696 147.678 155.167 1.00 21.43  ? 155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 140.812 147.235 156.104 1.00 22.65  ? 155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 141.917 147.786 156.072 1.00 26.96  ? 155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 138.641 148.471 155.936 1.00 28.85  ? 155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 137.510 148.716 155.090 1.00 29.03  ? 155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.214 149.794 156.402 1.00 23.63  ? 155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 140.542 146.236 156.944 1.00 33.43  ? 156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 141.553 145.770 157.888 1.00 32.72  ? 156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 142.757 145.186 157.160 1.00 31.53  ? 156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 143.905 145.406 157.563 1.00 32.28  ? 156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 140.940 144.739 158.836 1.00 31.94  ? 156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 141.759 144.485 160.068 1.00 35.78  ? 156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.111 145.526 160.908 1.00 32.19  ? 156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 142.170 143.203 160.388 1.00 32.01  ? 156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 142.863 145.295 162.042 1.00 34.72  ? 156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 142.919 142.965 161.522 1.00 30.98  ? 156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 143.267 144.013 162.349 1.00 39.12  ? 156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 142.513 144.441 156.081 1.00 36.60  ? 157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 143.583 143.769 155.357 1.00 28.10  ? 157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 144.385 144.716 154.472 1.00 32.47  ? 157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 145.593 144.519 154.305 1.00 45.48  ? 157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 142.993 142.635 154.515 1.00 33.93  ? 157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 143.889 141.911 153.511 1.00 38.82  ? 157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 144.953 141.095 154.221 1.00 40.39  ? 157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 143.054 141.029 152.597 1.00 35.77  ? 157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 143.754 145.747 153.908 1.00 32.47  ? 158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 144.382 146.535 152.859 1.00 31.66  ? 158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 144.636 147.991 153.225 1.00 34.58  ? 158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 145.089 148.751 152.363 1.00 43.64  ? 158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 143.529 146.484 151.583 1.00 33.64  ? 158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 143.411 145.084 151.019 1.00 39.47  ? 158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.327 144.273 151.145 1.00 44.04  ? 158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.277 144.793 150.395 1.00 40.48  ? 158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 144.358 148.409 154.457 1.00 32.81  ? 159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 144.617 149.791 154.837 1.00 37.14  ? 159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.114 150.023 154.987 1.00 43.03  ? 159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 146.788 149.330 155.754 1.00 49.59  ? 159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 143.899 150.140 156.139 1.00 37.05  ? 159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 146.634 151.001 154.249 1.00 44.58  ? 160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.039 151.336 154.309 1.00 47.18  ? 160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 148.954 150.444 153.503 1.00 49.08  ? 160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.172 150.657 153.525 1.00 50.68  ? 160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 148.418 149.459 152.795 1.00 47.58  ? 161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 149.207 148.540 151.991 1.00 46.54  ? 161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 149.253 149.001 150.538 1.00 49.54  ? 161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 148.335 149.656 150.039 1.00 52.02  ? 161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 148.632 147.123 152.074 1.00 42.99  ? 161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.095 146.336 153.287 1.00 45.23  ? 161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 148.850 144.848 153.106 1.00 45.91  ? 161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 148.238 144.254 154.287 1.00 45.69  ? 161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 148.165 142.951 154.520 1.00 48.02  ? 161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 147.615 142.524 155.653 1.00 51.31  ? 161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 148.621 142.066 153.649 1.00 44.52  ? 161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 150.347 148.652 149.863 1.00 57.66  ? 162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 150.519 148.957 148.447 1.00 60.45  ? 162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 149.953 147.865 147.549 1.00 58.19  ? 162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 149.243 148.162 146.585 1.00 53.28  ? 162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 152.002 149.187 148.128 1.00 62.01  ? 162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 152.243 149.830 146.771 1.00 58.29  ? 162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.020 151.132 146.895 1.00 58.69  ? 162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.292 150.947 147.702 1.00 62.19  ? 162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.873 152.249 148.135 1.00 60.01  ? 162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 150.254 146.601 147.849 1.00 60.75  ? 163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 149.647 145.487 147.131 1.00 63.43  ? 163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 148.222 145.279 147.624 1.00 65.32  ? 163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 147.920 144.270 148.269 1.00 63.80  ? 163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 150.471 144.211 147.311 1.00 63.14  ? 163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 150.210 143.149 146.254 1.00 61.56  ? 163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 151.475 142.376 145.924 1.00 61.33  ? 163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 152.641 143.248 145.854 1.00 63.88  ? 163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 153.748 143.078 146.564 1.00 64.88  ? 163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 154.750 143.940 146.421 1.00 62.63  ? 163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 153.877 142.071 147.412 1.00 61.64  ? 163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 147.344 146.232 147.326 1.00 53.39  ? 164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 145.987 146.246 147.845 1.00 48.78  ? 164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 144.990 146.403 146.707 1.00 51.20  ? 164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.325 146.889 145.622 1.00 51.80  ? 164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 145.791 147.388 148.849 1.00 49.88  ? 164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 145.798 148.765 148.205 1.00 48.97  ? 164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 144.829 149.718 148.882 1.00 45.59  ? 164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.418 150.370 150.045 1.00 48.50  ? 164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.968 151.499 150.575 1.00 51.46  ? 164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 145.583 152.009 151.638 1.00 48.78  ? 164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 143.922 152.132 150.068 1.00 48.34  ? 164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 143.757 145.980 146.967 1.00 49.48  ? 165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 142.655 146.275 146.075 1.00 49.19  ? 165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 141.976 147.559 146.502 1.00 51.11  ? 165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 142.591 148.629 146.478 1.00 55.94  ? 165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 140.713 147.469 146.894 1.00 43.29  ? 166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 139.995 148.587 147.485 1.00 43.49  ? 166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 139.590 148.245 148.912 1.00 42.74  ? 166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 139.589 147.083 149.325 1.00 42.12  ? 166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 138.763 148.954 146.649 1.00 46.04  ? 166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 139.077 149.750 145.392 1.00 45.12  ? 166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 139.782 151.061 145.684 1.00 46.30  ? 166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 139.522 151.658 146.749 1.00 48.63  ? 166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.598 151.496 144.845 1.00 42.20  ? 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 139.245 149.282 149.667 1.00 37.42  ? 167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 138.774 149.121 151.035 1.00 34.51  ? 167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 137.271 148.896 151.113 1.00 40.03  ? 167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 136.737 148.743 152.215 1.00 40.99  ? 167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.154 150.346 151.874 1.00 30.84  ? 167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.637 150.664 152.079 1.00 26.95  ? 167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 140.834 151.383 153.396 1.00 33.84  ? 167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.486 149.409 152.035 1.00 29.55  ? 167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 136.583 148.876 149.979 1.00 31.53  ? 168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.139 148.687 149.935 1.00 24.98  ? 168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 134.840 147.202 149.799 1.00 38.80  ? 168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 135.378 146.519 148.920 1.00 37.02  ? 168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 134.521 149.491 148.779 1.00 27.05  ? 168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.033 149.251 148.710 1.00 34.37  ? 168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 134.805 150.963 148.956 1.00 34.31  ? 168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 133.976 146.699 150.678 1.00 46.39  ? 169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 133.666 145.278 150.740 1.00 40.89  ? 169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 132.651 144.830 149.698 1.00 40.87  ? 169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 132.601 143.637 149.382 1.00 45.26  ? 169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 133.144 144.915 152.135 1.00 35.89  ? 169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 133.800 145.675 153.135 1.00 40.59  ? 169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 131.849 145.742 149.156 1.00 34.52  ? 170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 130.736 145.338 148.310 1.00 30.84  ? 170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.388 146.469 147.356 1.00 30.94  ? 170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.595 147.640 147.676 1.00 36.64  ? 170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 129.516 144.961 149.164 1.00 35.47  ? 170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 129.257 146.032 150.608 1.00 55.50  ? 170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 129.862 146.112 146.186 1.00 28.52  ? 171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.395 147.082 145.206 1.00 20.96  ? 171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.052 146.633 144.657 1.00 20.17  ? 171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 127.818 145.433 144.485 1.00 32.49  ? 171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.393 147.259 144.058 1.00 21.95  ? 171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 131.805 147.500 144.507 1.00 25.85  ? 171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.247 148.783 144.781 1.00 19.85  ? 171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 132.695 146.448 144.637 1.00 24.39  ? 171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.545 149.010 145.189 1.00 13.71  ? 171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 133.994 146.671 145.045 1.00 25.75  ? 171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.419 147.953 145.320 1.00 23.20  ? 171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.173 147.594 144.390 1.00 17.63  ? 172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 125.851 147.330 143.840 1.00 13.81  ? 172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.704 148.109 142.541 1.00 16.30  ? 172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.775 149.342 142.544 1.00 22.75  ? 172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 124.752 147.723 144.830 1.00 14.93  ? 172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 124.549 146.858 146.075 1.00 12.95  ? 172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 125.597 147.152 147.137 1.00 12.79  ? 172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.155 147.064 146.630 1.00 15.92  ? 172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.495 147.394 141.440 1.00 22.30  ? 173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.419 147.991 140.114 1.00 20.90  ? 173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 123.994 147.919 139.588 1.00 26.86  ? 173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.341 146.875 139.688 1.00 32.27  ? 173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.366 147.290 139.139 1.00 21.23  ? 173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 127.836 147.172 139.537 1.00 22.31  ? 173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.610 146.472 138.437 1.00 26.07  ? 173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.425 148.540 139.826 1.00 27.99  ? 173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.517 149.028 139.031 1.00 31.25  ? 174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.238 149.064 138.337 1.00 30.49  ? 174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.486 148.864 136.847 1.00 30.52  ? 174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.184 149.667 136.216 1.00 37.61  ? 174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.523 150.390 138.591 1.00 33.71  ? 174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 120.907 150.517 139.971 1.00 31.51  ? 174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.407 150.312 139.959 1.00 32.47  ? 174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 118.825 150.247 138.856 1.00 32.43  ? 174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.809 150.218 141.050 1.00 34.27  ? 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 121.923 147.800 136.287 1.00 23.89  ? 175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.105 147.458 134.881 1.00 27.27  ? 175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 120.897 147.963 134.104 1.00 29.43  ? 175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 119.762 147.550 134.369 1.00 29.04  ? 175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.291 145.945 134.690 1.00 24.10  ? 175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 122.768 145.643 133.280 1.00 25.58  ? 175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.266 145.402 135.717 1.00 25.56  ? 175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.139 148.855 133.148 1.00 28.38  ? 176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.068 149.374 132.316 1.00 28.10  ? 176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 119.785 148.423 131.155 1.00 32.61  ? 176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.553 147.504 130.863 1.00 35.35  ? 176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.417 150.768 131.800 1.00 20.67  ? 176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.191 151.621 131.555 1.00 26.24  ? 176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.080 151.108 131.428 1.00 33.93  ? 176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.386 152.932 131.488 1.00 32.50  ? 176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.659 148.662 130.482 1.00 35.43  ? 177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.167 147.761 129.439 1.00 30.38  ? 177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.731 148.193 128.088 1.00 35.87  ? 177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.053 148.793 127.252 1.00 36.76  ? 177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.645 147.744 129.435 1.00 26.63  ? 177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.076 146.699 128.502 1.00 35.61  ? 177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.721 145.645 128.327 1.00 44.24  ? 177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 114.984 146.932 127.943 1.00 33.25  ? 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.006 147.872 127.875 1.00 27.71  ? 178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.648 148.103 126.589 1.00 26.47  ? 178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 121.897 147.239 126.506 1.00 30.92  ? 178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.418 146.771 127.520 1.00 35.60  ? 178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 120.997 149.581 126.386 1.00 20.23  ? 178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.255 149.894 126.953 1.00 27.75  ? 178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.365 147.024 125.272 1.00 26.24  ? 179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.602 146.275 125.081 1.00 22.04  ? 179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 124.810 147.061 125.569 1.00 25.30  ? 179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 125.740 146.476 126.133 1.00 25.41  ? 179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 123.779 145.899 123.611 1.00 31.26  ? 179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 124.819 144.809 123.344 1.00 23.46  ? 179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 124.497 143.554 124.139 1.00 20.42  ? 179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 124.919 144.501 121.862 1.00 25.21  ? 179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 124.817 148.378 125.352 1.00 30.79  ? 180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 125.886 149.213 125.889 1.00 27.58  ? 180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 125.932 149.117 127.406 1.00 29.09  ? 180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.003 148.953 128.002 1.00 31.22  ? 180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.686 150.664 125.453 1.00 25.85  ? 180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.089 150.900 124.016 1.00 33.82  ? 180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 126.811 150.102 123.424 1.00 36.69  ? 180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.619 152.001 123.444 1.00 38.03  ? 180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 124.764 149.190 128.047 1.00 32.49  ? 181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 124.709 149.127 129.501 1.00 24.86  ? 181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.076 147.742 130.014 1.00 25.39  ? 181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 125.728 147.619 131.053 1.00 34.30  ? 181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.321 149.536 129.986 1.00 29.31  ? 181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.024 150.996 129.720 1.00 35.21  ? 181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 123.685 151.858 130.333 1.00 35.37  ? 181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.133 151.283 128.895 1.00 39.71  ? 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 124.686 146.686 129.297 1.00 27.57  ? 182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.041 145.336 129.725 1.00 25.82  ? 182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.544 145.108 129.600 1.00 27.00  ? 182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.179 144.547 130.502 1.00 25.58  ? 182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.239 144.294 128.924 1.00 24.43  ? 182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 122.810 144.206 129.457 1.00 27.18  ? 182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 124.910 142.931 128.983 1.00 23.24  ? 182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 121.862 143.503 128.527 1.00 28.25  ? 182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.136 145.537 128.484 1.00 28.00  ? 183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.577 145.391 128.309 1.00 19.92  ? 183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.342 146.206 129.342 1.00 27.11  ? 183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.339 145.735 129.904 1.00 31.35  ? 183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 128.976 145.805 126.894 1.00 22.85  ? 183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 129.039 147.214 126.773 1.00 35.43  ? 183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 128.887 147.430 129.617 1.00 29.03  ? 184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.537 148.235 130.643 1.00 22.84  ? 184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.345 147.632 132.028 1.00 26.69  ? 184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.241 147.732 132.869 1.00 35.05  ? 184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.013 149.668 130.596 1.00 28.05  ? 184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.438 150.518 131.773 1.00 31.40  ? 184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 130.898 150.913 131.672 1.00 29.40  ? 184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.211 151.533 130.391 1.00 36.65  ? 184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.433 151.631 129.888 1.00 38.76  ? 184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 132.605 152.229 128.714 1.00 33.04  ? 184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.484 151.149 130.529 1.00 36.66  ? 184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.198 147.003 132.286 1.00 31.48  ? 185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 127.993 146.324 133.560 1.00 18.19  ? 185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 128.949 145.153 133.718 1.00 23.50  ? 185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 129.496 144.937 134.802 1.00 32.72  ? 185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 126.543 145.855 133.677 1.00 24.03  ? 185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.165 144.387 132.646 1.00 32.07  ? 186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.151 143.308 132.689 1.00 31.34  ? 186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 131.542 143.872 132.950 1.00 26.53  ? 186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.305 143.341 133.770 1.00 33.93  ? 186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.111 142.495 131.382 1.00 33.66  ? 186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 128.738 141.849 131.188 1.00 27.70  ? 186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.204 141.438 131.373 1.00 27.43  ? 186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.526 141.297 129.799 1.00 27.18  ? 186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 131.891 144.958 132.255 1.00 26.33  ? 187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.195 145.584 132.444 1.00 27.97  ? 187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.385 146.040 133.885 1.00 29.47  ? 187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.426 145.781 134.498 1.00 38.77  ? 187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.346 146.764 131.483 1.00 30.17  ? 187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.411 147.747 131.930 1.00 41.48  ? 187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 135.568 147.323 132.140 1.00 43.33  ? 187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.091 148.945 132.073 1.00 41.41  ? 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.380 146.715 134.445 1.00 24.60  ? 188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.484 147.231 135.805 1.00 26.64  ? 188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 132.510 146.089 136.812 1.00 26.15  ? 188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.216 146.156 137.824 1.00 33.70  ? 188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.338 148.218 136.091 1.00 26.38  ? 188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.447 149.441 135.180 1.00 30.95  ? 188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.360 148.665 137.534 1.00 27.31  ? 188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.280 150.386 135.301 1.00 30.75  ? 188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 131.746 145.025 136.559 1.00 23.38  ? 189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 131.778 143.866 137.443 1.00 15.22  ? 189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.169 143.252 137.480 1.00 26.67  ? 189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 133.687 142.927 138.553 1.00 34.79  ? 189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 130.744 142.835 136.992 1.00 23.54  ? 189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.432 143.361 137.073 1.00 35.04  ? 189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 133.799 143.101 136.312 1.00 28.25  ? 190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.155 142.561 136.281 1.00 23.36  ? 190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.152 143.511 136.936 1.00 27.20  ? 190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.070 143.068 137.635 1.00 30.80  ? 190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 135.562 142.243 134.842 1.00 27.64  ? 190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.149 140.849 134.395 1.00 32.79  ? 190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 135.461 140.498 132.656 1.00 33.57  ? 190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 135.115 142.088 131.918 1.00 27.86  ? 190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 135.984 144.821 136.731 1.00 30.44  ? 191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 136.888 145.789 137.347 1.00 29.01  ? 191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 136.792 145.758 138.867 1.00 29.99  ? 191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 137.814 145.796 139.562 1.00 39.51  ? 191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 136.591 147.198 136.829 1.00 26.30  ? 191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 136.913 147.426 135.360 1.00 30.69  ? 191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.372 147.186 135.024 1.00 33.82  ? 191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.251 147.320 135.876 1.00 31.82  ? 191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 138.637 146.839 133.772 1.00 30.62  ? 191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 135.573 145.694 139.403 1.00 31.09  ? 192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.390 145.699 140.849 1.00 26.61  ? 192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 135.731 144.355 141.477 1.00 29.07  ? 192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.162 144.312 142.633 1.00 38.70  ? 192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 133.955 146.099 141.195 1.00 27.00  ? 192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.507 147.466 140.675 1.00 25.14  ? 192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.029 147.681 140.932 1.00 24.91  ? 192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.327 148.581 141.299 1.00 22.48  ? 192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 135.545 143.252 140.745 1.00 25.20  ? 193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.022 141.963 141.230 1.00 26.08  ? 193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 137.541 141.904 141.229 1.00 33.31  ? 193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.136 141.237 142.082 1.00 39.13  ? 193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.442 140.837 140.380 1.00 30.71  ? 193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 134.052 141.016 140.193 1.00 33.68  ? 193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.182 142.589 140.279 1.00 31.72  ? 194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 139.630 142.746 140.327 1.00 32.58  ? 194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.053 143.477 141.594 1.00 38.79  ? 194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.074 143.138 142.206 1.00 43.91  ? 194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.109 143.492 139.082 1.00 32.02  ? 194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.561 143.929 139.121 1.00 38.09  ? 194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 141.886 144.833 137.942 1.00 38.13  ? 194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.336 145.280 137.971 1.00 39.26  ? 194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.626 146.279 136.907 1.00 39.31  ? 194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.275 144.478 142.009 1.00 38.99  ? 195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 139.537 145.192 143.251 1.00 39.96  ? 195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 139.275 144.343 144.488 1.00 37.38  ? 195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 139.682 144.737 145.585 1.00 45.90  ? 195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 138.691 146.464 143.307 1.00 38.09  ? 195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 138.939 147.467 142.180 1.00 38.05  ? 195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 137.905 148.580 142.209 1.00 40.10  ? 195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 140.346 148.034 142.266 1.00 37.52  ? 195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 138.609 143.197 144.341 1.00 33.81  ? 196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 138.390 142.277 145.436 1.00 39.31  ? 196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.017 142.342 146.072 1.00 43.17  ? 196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 136.679 141.450 146.858 1.00 44.38  ? 196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.221 143.359 145.759 1.00 35.68  ? 197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 134.914 143.508 146.366 1.00 32.37  ? 197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 133.830 142.730 145.641 1.00 30.87  ? 197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 133.871 142.550 144.428 1.00 34.28  ? 197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 132.850 142.265 146.413 1.00 26.12  ? 198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 131.717 141.579 145.826 1.00 21.44  ? 198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 130.802 142.535 145.086 1.00 24.87  ? 198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 130.589 143.676 145.494 1.00 33.80  ? 198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.253 142.057 143.973 1.00 22.86  ? 199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 129.440 142.874 143.081 1.00 17.44  ? 199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.034 142.298 143.031 1.00 21.58  ? 199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 127.856 141.098 142.790 1.00 34.57  ? 199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.048 142.950 141.670 1.00 22.64  ? 199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.175 143.795 140.766 1.00 19.71  ? 199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 131.455 143.514 141.731 1.00 25.60  ? 199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.041 143.151 143.261 1.00 22.24  ? 200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 125.635 142.803 143.115 1.00 8.67   ? 200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.041 143.623 141.980 1.00 15.93  ? 200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.284 144.831 141.892 1.00 29.87  ? 200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 124.867 143.055 144.412 1.00 16.31  ? 200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 123.572 142.484 144.357 1.00 28.67  ? 200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.271 142.972 141.117 1.00 18.86  ? 201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 123.704 143.616 139.942 1.00 14.53  ? 201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.188 143.503 139.960 1.00 16.15  ? 201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 121.635 142.456 140.308 1.00 20.86  ? 201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.263 143.002 138.656 1.00 18.60  ? 201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 125.783 143.084 138.513 1.00 20.39  ? 201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 126.415 141.709 138.653 1.00 20.31  ? 201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.165 143.727 137.193 1.00 19.80  ? 201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 121.522 144.592 139.586 1.00 17.50  ? 202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.069 144.643 139.491 1.00 13.91  ? 202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 119.673 144.348 138.051 1.00 28.82  ? 202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 119.915 145.162 137.153 1.00 36.96  ? 202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.542 146.005 139.937 1.00 20.02  ? 202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.050 145.997 140.193 1.00 21.28  ? 202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 117.475 144.970 140.552 1.00 25.89  ? 202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.413 147.146 140.009 1.00 17.70  ? 202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.067 143.184 137.830 1.00 20.21  ? 203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 118.643 142.764 136.505 1.00 16.98  ? 203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.161 143.009 136.261 1.00 17.44  ? 203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 116.632 142.577 135.234 1.00 24.36  ? 203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 118.970 141.285 136.294 1.00 17.97  ? 203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 120.406 140.851 136.598 1.00 20.52  ? 203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 120.630 139.418 136.160 1.00 22.19  ? 203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.415 141.779 135.940 1.00 21.72  ? 203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 116.480 143.698 137.180 1.00 17.95  ? 204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.049 143.929 137.032 1.00 14.72  ? 204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 114.731 144.921 135.924 1.00 26.73  ? 204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 113.612 144.909 135.403 1.00 31.64  ? 204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.458 144.420 138.352 1.00 17.79  ? 204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 114.765 143.528 139.407 1.00 30.66  ? 204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 115.681 145.780 135.554 1.00 29.14  ? 205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.479 146.693 134.438 1.00 30.75  ? 205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.698 146.030 133.089 1.00 26.68  ? 205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.233 146.557 132.073 1.00 32.02  ? 205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.412 147.900 134.560 1.00 29.53  ? 205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.060 148.840 135.693 1.00 28.85  ? 205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 116.842 150.132 135.590 1.00 31.54  ? 205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.235 151.204 136.469 1.00 36.43  ? 205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.238 150.809 137.902 1.00 32.47  ? 205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.390 144.895 133.056 1.00 24.55  ? 206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.600 144.178 131.808 1.00 22.94  ? 206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.279 143.618 131.304 1.00 26.64  ? 206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.506 143.035 132.070 1.00 30.07  ? 206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 117.612 143.055 132.011 1.00 21.86  ? 206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.003 143.517 132.439 1.00 26.36  ? 206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 119.902 142.324 132.658 1.00 28.66  ? 206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.593 144.448 131.400 1.00 28.44  ? 206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.023 143.793 130.013 1.00 33.82  ? 207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 113.758 143.355 129.446 1.00 33.66  ? 207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 113.711 141.835 129.341 1.00 36.25  ? 207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 114.740 141.158 129.276 1.00 40.89  ? 207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.532 144.012 128.087 1.00 35.11  ? 207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.283 143.404 126.929 1.00 33.40  ? 207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 113.916 144.130 125.647 1.00 35.13  ? 207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.126 145.567 125.759 1.00 34.74  ? 207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.731 146.310 124.843 1.00 32.52  ? 207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.887 147.611 125.062 1.00 35.65  ? 207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.174 145.785 123.713 1.00 33.61  ? 207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 112.492 141.302 129.336 1.00 42.86  ? 208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.273 139.877 129.519 1.00 38.55  ? 208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 112.672 139.086 128.273 1.00 40.62  ? 208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 112.955 139.639 127.207 1.00 43.26  ? 208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.812 139.607 129.868 1.00 37.10  ? 208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 112.700 137.766 128.435 1.00 40.67  ? 209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 112.992 136.871 127.323 1.00 35.15  ? 209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 111.838 136.863 126.330 1.00 41.43  ? 209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 110.665 136.828 126.713 1.00 43.88  ? 209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.255 135.457 127.840 1.00 36.75  ? 209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.460 134.421 126.750 1.00 43.31  ? 209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 113.704 133.043 127.338 1.00 43.10  ? 209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 115.126 132.579 127.075 1.00 43.55  ? 209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 115.440 132.550 125.620 1.00 41.26  ? 209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.177 136.889 125.044 1.00 44.15  ? 210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.167 136.960 124.011 1.00 45.82  ? 210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 110.639 138.346 123.732 1.00 46.83  ? 210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.567 138.474 123.131 1.00 48.12  ? 210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.348 139.387 124.154 1.00 44.42  ? 211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 110.937 140.757 123.900 1.00 41.87  ? 211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.553 141.269 122.600 1.00 41.75  ? 211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.329 140.583 121.933 1.00 44.34  ? 211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.321 141.656 125.073 1.00 43.75  ? 211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.466 141.434 126.302 1.00 45.34  ? 211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 109.979 142.726 126.921 1.00 47.37  ? 211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.077 143.361 126.339 1.00 47.30  ? 211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.489 143.098 127.997 1.00 47.80  ? 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.199 142.500 122.248 1.00 44.32  ? 212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.569 143.072 120.961 1.00 43.27  ? 212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.819 143.933 121.093 1.00 45.39  ? 212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 112.953 144.707 122.047 1.00 49.11  ? 212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.418 143.901 120.390 1.00 43.83  ? 212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.733 143.790 120.134 1.00 42.47  ? 213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 114.916 144.639 120.044 1.00 45.84  ? 213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.829 145.471 118.773 1.00 44.04  ? 213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.227 145.017 117.695 1.00 48.95  ? 213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.212 143.808 120.064 1.00 45.28  ? 213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.207 142.835 121.240 1.00 46.26  ? 213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.426 144.716 120.145 1.00 40.81  ? 213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.290 141.790 121.161 1.00 43.23  ? 213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.307 146.694 118.894 1.00 49.00  ? 214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.176 147.614 117.768 1.00 51.94  ? 214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.345 147.003 116.647 1.00 59.34  ? 214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.866 146.742 115.557 1.00 59.74  ? 214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.553 148.025 117.243 1.00 51.78  ? 214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 115.750 149.526 117.128 1.00 51.08  ? 214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.223 149.899 117.028 1.00 54.03  ? 214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 117.955 149.044 116.002 1.00 54.49  ? 214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 118.719 147.923 116.618 1.00 52.07  ? 214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.065 146.740 116.926 1.00 64.58  ? 215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.095 146.220 115.963 1.00 67.96  ? 215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.360 144.758 115.617 1.00 66.82  ? 215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.588 144.146 114.872 1.00 66.74  ? 215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.069 147.067 114.686 1.00 67.95  ? 215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.589 148.484 114.934 1.00 69.50  ? 215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.393 148.661 115.247 1.00 66.99  ? 215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.408 149.420 114.816 1.00 69.25  ? 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.439 144.188 116.148 1.00 60.30  ? 216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.721 142.769 115.970 1.00 59.21  ? 216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.180 142.039 117.192 1.00 60.04  ? 216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.790 142.068 118.266 1.00 64.59  ? 216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.228 142.514 115.775 1.00 60.47  ? 216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.542 141.035 115.889 1.00 57.53  ? 216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.696 143.057 114.435 1.00 60.36  ? 216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.032 141.384 117.038 1.00 57.73  ? 217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.318 140.806 118.165 1.00 59.81  ? 217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 110.887 139.437 118.525 1.00 57.90  ? 217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.471 138.739 117.695 1.00 57.71  ? 217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.826 140.706 117.853 1.00 59.65  ? 217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 107.992 141.837 118.428 1.00 60.36  ? 217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 107.926 143.039 117.508 1.00 64.15  ? 217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 108.356 142.923 116.341 1.00 64.91  ? 217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.449 144.103 117.955 1.00 63.00  ? 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.702 139.052 119.786 1.00 53.05  ? 218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.111 137.747 120.308 1.00 52.69  ? 218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.583 137.467 120.019 1.00 56.38  ? 218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 112.968 136.384 119.575 1.00 59.41  ? 218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.222 136.638 119.748 1.00 54.27  ? 218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.231 135.395 120.613 1.00 57.82  ? 218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.517 135.316 121.611 1.00 57.98  ? 218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.048 134.417 120.239 1.00 56.65  ? 218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.418 138.469 120.282 1.00 49.84  ? 219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 114.850 138.376 120.024 1.00 51.28  ? 219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 115.676 138.338 121.298 1.00 48.85  ? 219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 116.827 137.886 121.272 1.00 49.45  ? 219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.302 139.547 119.139 1.00 49.57  ? 219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.128 138.805 122.416 1.00 45.55  ? 220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 115.890 138.869 123.652 1.00 43.81  ? 220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.078 137.481 124.253 1.00 49.02  ? 220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.260 136.574 124.073 1.00 47.91  ? 220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.193 139.766 124.670 1.00 36.95  ? 220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 113.810 139.402 124.758 1.00 47.05  ? 220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 115.292 141.207 124.247 1.00 36.83  ? 220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.180 137.324 124.983 1.00 40.43  ? 221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.435 136.131 125.773 1.00 44.16  ? 221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.023 136.305 127.227 1.00 47.45  ? 221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.259 135.407 128.041 1.00 46.48  ? 221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 118.911 135.745 125.689 1.00 41.55  ? 221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 119.514 135.938 124.316 1.00 42.54  ? 221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.626 134.941 124.067 1.00 45.15  ? 221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 120.913 134.814 122.585 1.00 46.17  ? 221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.533 136.048 121.845 1.00 44.47  ? 221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 116.413 137.434 127.567 1.00 45.69  ? 222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.028 137.700 128.931 1.00 42.58  ? 222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.213 138.083 129.793 1.00 43.54  ? 222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 118.295 138.434 129.316 1.00 38.75  ? 222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 116.986 138.015 131.105 1.00 42.90  ? 223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.051 138.320 132.046 1.00 38.22  ? 223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.003 137.148 132.216 1.00 37.30  ? 223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.103 137.331 132.741 1.00 41.39  ? 223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.469 138.745 133.407 1.00 32.47  ? 223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.406 139.810 133.216 1.00 33.94  ? 223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 116.899 137.544 134.144 1.00 33.43  ? 223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 118.620 135.948 131.772 1.00 38.80  ? 224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 119.432 134.759 132.024 1.00 33.68  ? 224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.705 134.778 131.184 1.00 38.46  ? 224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.762 134.313 131.627 1.00 41.99  ? 224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.605 133.488 131.773 1.00 35.83  ? 224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.396 132.254 132.169 1.00 34.98  ? 224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 117.301 133.556 132.542 1.00 40.36  ? 224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 120.629 135.297 129.959 1.00 34.06  ? 225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.843 135.486 129.183 1.00 27.97  ? 225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 122.803 136.442 129.861 1.00 34.71  ? 225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.020 136.228 129.863 1.00 44.42  ? 225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.265 137.506 130.460 1.00 28.94  ? 226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.095 138.435 131.216 1.00 28.09  ? 226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 123.667 137.756 132.454 1.00 30.91  ? 226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 124.797 138.043 132.863 1.00 35.96  ? 226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.287 139.695 131.572 1.00 28.31  ? 226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.172 140.714 132.270 1.00 35.24  ? 226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 121.674 140.289 130.320 1.00 27.33  ? 226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 122.903 136.854 133.079 1.00 34.48  ? 227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 123.445 136.091 134.200 1.00 31.66  ? 227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 124.604 135.212 133.758 1.00 29.49  ? 227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 125.600 135.092 134.471 1.00 33.45  ? 227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.366 135.235 134.868 1.00 30.86  ? 227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 121.081 135.950 135.208 1.00 27.82  ? 227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.134 135.110 136.491 1.00 43.54  ? 227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.416 134.179 137.326 1.00 39.90  ? 227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 124.488 134.575 132.593 1.00 31.04  ? 228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.598 133.769 132.089 1.00 32.23  ? 228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.822 134.636 131.810 1.00 32.32  ? 228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 127.953 134.267 132.162 1.00 36.24  ? 228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.176 133.018 130.827 1.00 31.48  ? 228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.793 131.566 131.065 1.00 32.14  ? 228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 123.413 131.269 130.507 1.00 42.14  ? 228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.418 131.321 128.987 1.00 45.15  ? 228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.043 131.348 128.420 1.00 40.52  ? 228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 126.609 135.799 131.189 1.00 30.80  ? 229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 127.715 136.717 130.924 1.00 26.16  ? 229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.387 137.161 132.216 1.00 27.90  ? 229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 129.617 137.140 132.328 1.00 32.90  ? 229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.214 137.933 130.146 1.00 29.60  ? 229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.040 137.803 128.635 1.00 25.71  ? 229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.060 138.846 128.143 1.00 29.18  ? 229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.378 137.953 127.938 1.00 29.21  ? 229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 127.590 137.562 133.208 1.00 33.22  ? 230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.144 138.028 134.474 1.00 25.48  ? 230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.817 136.893 135.232 1.00 28.26  ? 230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 129.834 137.104 135.898 1.00 43.58  ? 230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.043 138.667 135.318 1.00 28.95  ? 230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.513 140.005 134.798 1.00 33.01  ? 230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.199 140.361 135.469 1.00 29.04  ? 230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.542 141.105 135.001 1.00 32.83  ? 230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.266 135.682 135.142 1.00 27.49  ? 231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.871 134.528 135.791 1.00 28.96  ? 231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 130.249 134.242 135.218 1.00 35.27  ? 231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 131.204 134.000 135.965 1.00 40.54  ? 231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 127.952 133.316 135.633 1.00 32.16  ? 231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 128.520 132.063 136.258 1.00 45.23  ? 231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 128.827 132.091 137.465 1.00 45.54  ? 231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.653 131.047 135.545 1.00 48.98  ? 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 130.380 134.289 133.893 1.00 42.23  ? 232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.689 134.061 133.290 1.00 36.01  ? 232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 132.628 135.237 133.534 1.00 36.29  ? 232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.846 135.054 133.630 1.00 44.97  ? 232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 131.528 133.772 131.803 1.00 35.22  ? 232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 131.316 132.302 131.533 1.00 44.61  ? 232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 131.929 131.450 132.173 1.00 47.30  ? 232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 130.395 131.996 130.640 1.00 44.65  ? 232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.081 136.450 133.648 1.00 29.18  ? 233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 132.900 137.602 134.008 1.00 27.79  ? 233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 133.471 137.459 135.413 1.00 34.66  ? 233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 134.638 137.786 135.654 1.00 37.33  ? 233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.077 138.883 133.889 1.00 25.80  ? 233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 132.660 136.976 136.355 1.00 36.70  ? 234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.131 136.806 137.725 1.00 29.29  ? 234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.076 135.618 137.840 1.00 34.12  ? 234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.016 135.642 138.643 1.00 38.70  ? 234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.947 136.651 138.678 1.00 29.35  ? 234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.182 137.924 138.903 1.00 28.12  ? 234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 131.836 139.080 139.286 1.00 32.74  ? 234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 129.812 137.965 138.735 1.00 27.23  ? 234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.137 140.249 139.494 1.00 29.95  ? 234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.110 139.134 138.936 1.00 27.80  ? 234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 129.771 140.275 139.318 1.00 30.53  ? 234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.840 134.565 137.053 1.00 38.08  ? 235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.801 133.468 136.990 1.00 39.24  ? 235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.137 133.942 136.436 1.00 42.70  ? 235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 137.199 133.540 136.924 1.00 45.98  ? 235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.245 132.326 136.140 1.00 37.92  ? 235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.006 131.042 136.913 1.00 42.95  ? 235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.756 129.863 135.988 1.00 45.63  ? 235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.831 130.188 134.910 1.00 46.55  ? 235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 131.515 130.051 134.991 1.00 47.82  ? 235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 130.762 130.375 133.944 1.00 46.18  ? 235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.934 129.597 136.090 1.00 42.14  ? 235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.103 134.796 135.414 1.00 35.99  ? 236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 137.336 135.289 134.816 1.00 36.79  ? 236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.067 136.229 135.766 1.00 37.90  ? 236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 139.279 136.104 135.973 1.00 41.42  ? 236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.023 135.990 133.495 1.00 35.81  ? 236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 138.220 136.632 132.848 1.00 35.03  ? 236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.138 135.864 132.151 1.00 33.56  ? 236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 138.438 137.999 132.934 1.00 34.32  ? 236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 140.234 136.432 131.555 1.00 32.81  ? 236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 139.537 138.579 132.339 1.00 32.87  ? 236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 140.430 137.787 131.652 1.00 33.71  ? 236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 141.529 138.344 131.053 1.00 42.27  ? 236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 137.343 137.183 136.350 1.00 43.83  ? 237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 137.913 138.113 137.325 1.00 43.03  ? 237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 137.688 137.596 138.747 1.00 46.82  ? 237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.027 138.217 139.578 1.00 48.16  ? 237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.320 139.504 137.137 1.00 37.35  ? 237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 138.248 136.415 139.012 1.00 64.85  ? 238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 138.079 135.733 140.289 1.00 66.77  ? 238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 139.241 135.967 141.247 1.00 68.85  ? 238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.550 135.084 142.058 1.00 71.19  ? 238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 137.870 134.236 140.060 1.00 66.90  ? 238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.074 133.565 139.426 1.00 70.29  ? 238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.970 134.279 138.929 1.00 72.76  ? 238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 139.120 132.318 139.422 1.00 67.19  ? 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.894 137.127 141.170 1.00 77.68  ? 239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.034 137.447 142.029 1.00 82.18  ? 239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 142.085 136.342 141.962 1.00 81.88  ? 239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.569 135.845 142.982 1.00 80.59  ? 239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 140.578 137.704 143.467 1.00 81.47  ? 239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.438 138.700 143.564 1.00 78.74  ? 239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.890 138.840 144.968 1.00 82.23  ? 239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.679 138.959 145.163 1.00 80.07  ? 239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 139.775 138.824 145.958 1.00 81.72  ? 239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 142.356 135.900 140.731 1.00 84.57  ? 240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.438 134.999 140.324 1.00 85.62  ? 240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.379 133.642 141.019 1.00 87.55  ? 240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.250 132.793 140.796 1.00 86.40  ? 240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.831 135.630 140.516 1.00 85.45  ? 240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 145.237 136.130 141.893 1.00 87.03  ? 240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 146.276 134.949 142.770 1.00 92.75  ? 240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 147.880 135.725 142.615 1.00 84.77  ? 240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.359 133.413 141.840 1.00 89.28  ? 241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.230 132.168 142.580 1.00 86.29  ? 241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 142.441 132.291 144.075 1.00 87.24  ? 241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 142.338 131.276 144.779 1.00 86.64  ? 241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.749 133.481 144.596 1.00 94.39  ? 242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.803 133.667 146.042 1.00 95.06  ? 242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 141.444 133.385 146.667 1.00 97.01  ? 242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.345 132.729 147.711 1.00 94.84  ? 242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.262 135.088 146.366 1.00 93.51  ? 242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.681 135.396 145.923 1.00 95.42  ? 242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 145.084 136.827 146.215 1.00 96.86  ? 242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.367 137.561 146.893 1.00 95.72  ? 242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.236 137.235 145.696 1.00 94.00  ? 242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.382 133.875 146.033 1.00 86.00  ? 243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 139.016 133.573 146.433 1.00 82.05  ? 243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.140 133.731 145.201 1.00 81.13  ? 243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.241 134.741 144.498 1.00 78.70  ? 243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 138.547 134.491 147.567 1.00 80.69  ? 243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.927 135.951 147.385 1.00 80.55  ? 243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 137.872 136.869 147.983 1.00 79.02  ? 243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 136.525 136.348 147.792 1.00 82.09  ? 243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 135.787 136.546 146.709 1.00 81.34  ? 243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 134.569 136.016 146.648 1.00 80.49  ? 243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 136.234 137.257 145.687 1.00 77.32  ? 243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 137.299 132.731 144.938 1.00 78.74  ? 244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 136.514 132.717 143.711 1.00 79.57  ? 244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 135.634 133.956 143.614 1.00 78.74  ? 244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 135.021 134.382 144.597 1.00 77.26  ? 244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 135.653 131.454 143.648 1.00 77.78  ? 244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 136.425 130.193 143.293 1.00 77.28  ? 244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 135.519 129.075 142.818 1.00 78.91  ? 244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 134.424 128.882 143.345 1.00 75.98  ? 244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 135.973 128.332 141.814 1.00 76.95  ? 244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.585 134.538 142.418 1.00 64.23  ? 245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.809 135.739 142.181 1.00 61.79  ? 245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 133.338 135.549 142.479 1.00 56.85  ? 245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 132.634 134.838 141.756 1.00 52.10  ? 245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.865 136.184 143.545 1.00 54.33  ? 246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 131.486 136.058 143.992 1.00 54.89  ? 246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 130.700 137.264 143.501 1.00 48.21  ? 246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.043 138.406 143.821 1.00 40.96  ? 246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 131.411 135.948 145.515 1.00 51.70  ? 246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 132.027 134.757 145.974 1.00 53.66  ? 246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 129.652 137.004 142.723 1.00 30.08  ? 247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 128.776 138.051 142.261 1.00 20.42  ? 247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 127.341 137.737 142.638 1.00 18.91  ? 247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.998 136.609 142.987 1.00 35.35  ? 247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 126.506 138.766 142.570 1.00 16.55  ? 248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.102 138.637 142.918 1.00 18.65  ? 248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.244 139.243 141.822 1.00 21.01  ? 248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 124.583 140.287 141.258 1.00 34.28  ? 248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 124.791 139.310 144.258 1.00 21.42  ? 248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.137 138.574 141.520 1.00 20.05  ? 249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.137 139.074 140.590 1.00 12.84  ? 249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 120.809 139.163 141.319 1.00 15.80  ? 249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 120.375 138.190 141.945 1.00 27.20  ? 249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.018 138.170 139.361 1.00 24.25  ? 249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.170 140.324 141.248 1.00 16.08  ? 250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 118.898 140.561 141.913 1.00 13.07  ? 250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 117.832 140.849 140.870 1.00 17.20  ? 250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.047 141.661 139.964 1.00 31.58  ? 250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.003 141.726 142.897 1.00 18.50  ? 250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.378 141.313 144.301 1.00 26.37  ? 250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 120.679 140.949 144.613 1.00 16.68  ? 250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 118.431 141.295 145.314 1.00 20.42  ? 250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.026 140.572 145.892 1.00 10.00  ? 250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 118.768 140.920 146.598 1.00 17.46  ? 250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.067 140.559 146.880 1.00 17.80  ? 250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 120.410 140.186 148.158 1.00 24.29  ? 250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 116.690 140.185 140.998 1.00 11.72  ? 251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 115.579 140.360 140.078 1.00 14.81  ? 251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.286 140.516 140.858 1.00 14.15  ? 251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.067 139.825 141.858 1.00 22.69  ? 251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 115.465 139.176 139.114 1.00 25.16  ? 251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 114.581 139.395 137.887 1.00 18.21  ? 251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.375 140.028 136.765 1.00 21.38  ? 251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.970 138.085 137.442 1.00 21.76  ? 251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.436 141.430 140.402 1.00 16.09  ? 252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.120 141.589 140.999 1.00 15.41  ? 252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.269 140.356 140.726 1.00 23.74  ? 252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.363 139.738 139.662 1.00 33.85  ? 252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.433 142.837 140.448 1.00 16.90  ? 252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 110.409 143.406 141.405 1.00 23.53  ? 252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.466 142.723 141.801 1.00 37.83  ? 252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 110.586 144.666 141.782 1.00 23.17  ? 252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 110.433 139.991 141.702 1.00 21.02  ? 253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 109.580 138.818 141.556 1.00 23.86  ? 253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 108.478 139.013 140.528 1.00 32.09  ? 253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.849 138.034 140.114 1.00 36.57  ? 253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.970 138.425 142.917 1.00 20.23  ? 253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.671 136.926 142.948 1.00 18.98  ? 253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 107.722 139.242 143.204 1.00 24.90  ? 253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.704 136.326 144.322 1.00 21.60  ? 253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.231 140.248 140.099 1.00 22.28  ? 254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.250 140.524 139.062 1.00 21.25  ? 254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 107.876 140.625 137.679 1.00 27.84  ? 254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.166 140.908 136.710 1.00 39.89  ? 254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.482 141.805 139.394 1.00 26.93  ? 254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.391 141.602 140.405 1.00 31.64  ? 254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.211 140.973 140.051 1.00 30.57  ? 254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.555 142.018 141.713 1.00 33.65  ? 254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.210 140.778 140.979 1.00 29.69  ? 254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 104.556 141.826 142.646 1.00 37.46  ? 254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.383 141.206 142.278 1.00 35.87  ? 254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.181 140.407 137.572 1.00 32.18  ? 255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 109.824 140.262 136.275 1.00 26.44  ? 255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.385 138.953 135.630 1.00 31.33  ? 255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.184 137.947 136.315 1.00 37.02  ? 255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.342 140.294 136.439 1.00 29.84  ? 255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.092 140.581 135.176 1.00 35.29  ? 255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.178 139.679 134.139 1.00 35.98  ? 255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 112.814 141.661 134.795 1.00 23.72  ? 255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 112.908 140.196 133.167 1.00 29.84  ? 255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.307 141.398 133.541 1.00 17.60  ? 255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.226 138.971 134.305 1.00 38.93  ? 256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.762 137.774 133.609 1.00 37.53  ? 256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.758 136.630 133.746 1.00 40.65  ? 256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.364 135.464 133.873 1.00 42.66  ? 256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 108.512 138.082 132.135 1.00 35.47  ? 256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.895 136.926 131.374 1.00 41.53  ? 256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.709 136.583 130.142 1.00 43.81  ? 256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.750 135.601 130.426 1.00 44.28  ? 256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.552 134.291 130.457 1.00 43.79  ? 256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 110.580 133.487 130.713 1.00 39.67  ? 256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 108.358 133.767 130.239 1.00 41.84  ? 256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.050 136.941 133.728 1.00 32.93  ? 257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.100 135.935 133.813 1.00 30.72  ? 257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.299 135.394 135.221 1.00 33.68  ? 257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.318 134.743 135.464 1.00 38.31  ? 257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.424 136.508 133.301 1.00 35.15  ? 257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.574 136.378 131.802 1.00 45.30  ? 257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.043 137.239 131.073 1.00 45.40  ? 257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.229 135.415 131.351 1.00 45.77  ? 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.364 135.638 136.143 1.00 36.15  ? 258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 111.569 135.241 137.534 1.00 33.37  ? 258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.728 133.730 137.648 1.00 34.12  ? 258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 112.563 133.238 138.416 1.00 41.54  ? 258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.425 135.769 138.424 1.00 34.11  ? 258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.687 135.423 139.891 1.00 30.67  ? 258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.072 135.231 137.972 1.00 25.65  ? 258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 111.986 135.980 140.424 1.00 25.80  ? 258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 110.945 132.967 136.883 1.00 37.61  ? 259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.085 131.515 136.919 1.00 34.87  ? 259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 112.387 131.072 136.266 1.00 35.36  ? 259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.077 130.187 136.783 1.00 35.17  ? 259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 109.885 130.854 136.244 1.00 38.09  ? 259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 108.687 130.749 137.165 1.00 40.72  ? 259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 108.744 130.090 138.203 1.00 39.42  ? 259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 107.593 131.402 136.790 1.00 38.59  ? 259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 112.740 131.677 135.129 1.00 37.10  ? 260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.033 131.400 134.512 1.00 30.81  ? 260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.175 131.876 135.401 1.00 31.68  ? 260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.225 131.229 135.480 1.00 38.04  ? 260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.107 132.060 133.137 1.00 35.09  ? 260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 112.804 131.955 132.370 1.00 45.27  ? 260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 111.782 132.479 132.858 1.00 44.50  ? 260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.802 131.348 131.279 1.00 48.12  ? 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 114.988 133.018 136.068 1.00 37.88  ? 261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 115.977 133.513 137.020 1.00 30.49  ? 261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.173 132.530 138.165 1.00 27.10  ? 261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.305 132.280 138.595 1.00 29.99  ? 261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 115.534 134.883 137.538 1.00 27.57  ? 261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.403 135.454 138.620 1.00 32.98  ? 261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 117.520 136.206 138.300 1.00 26.98  ? 261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.079 135.283 139.954 1.00 34.20  ? 261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 118.311 136.746 139.287 1.00 28.57  ? 261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.867 135.821 140.944 1.00 23.97  ? 261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.984 136.556 140.609 1.00 28.52  ? 261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.079 131.961 138.672 1.00 28.77  ? 262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.161 130.998 139.763 1.00 29.86  ? 262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 115.676 129.642 139.304 1.00 39.06  ? 262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 116.333 128.941 140.081 1.00 43.32  ? 262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 113.792 130.836 140.421 1.00 34.70  ? 262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.295 132.027 141.235 1.00 32.16  ? 262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 111.842 131.828 141.624 1.00 30.60  ? 262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.167 132.222 142.457 1.00 30.69  ? 262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 115.391 129.253 138.060 1.00 44.68  ? 263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 115.814 127.951 137.561 1.00 37.79  ? 263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 117.324 127.836 137.408 1.00 42.39  ? 263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 117.828 126.718 137.259 1.00 50.47  ? 263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.139 127.653 136.222 1.00 42.01  ? 263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 113.680 127.275 136.376 1.00 47.19  ? 263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 113.284 126.864 137.485 1.00 48.18  ? 263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 112.927 127.391 135.386 1.00 46.81  ? 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.053 128.954 137.437 1.00 41.78  ? 264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 119.505 128.905 137.336 1.00 40.99  ? 264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.146 128.178 138.511 1.00 44.66  ? 264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 121.247 127.637 138.362 1.00 48.59  ? 264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.074 130.320 137.235 1.00 42.53  ? 264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 119.680 131.079 138.384 1.00 44.73  ? 264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 119.563 131.011 135.983 1.00 39.56  ? 264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 119.488 128.152 139.668 1.00 39.66  ? 265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.013 127.489 140.853 1.00 42.08  ? 265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 119.493 126.069 141.025 1.00 47.73  ? 265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 119.868 125.400 141.993 1.00 50.88  ? 265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 119.691 128.312 142.103 1.00 43.31  ? 265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 120.605 129.508 142.295 1.00 43.09  ? 265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.063 129.090 142.229 1.00 44.25  ? 265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 122.987 130.287 142.347 1.00 42.30  ? 265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.409 129.911 142.117 1.00 41.78  ? 265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 118.643 125.594 140.119 1.00 55.96  ? 266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 118.187 124.213 140.177 1.00 52.88  ? 266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 119.334 123.264 139.855 1.00 59.92  ? 266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 120.148 123.526 138.965 1.00 58.67  ? 266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 117.036 123.990 139.198 1.00 53.75  ? 266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 115.668 124.382 139.729 1.00 56.29  ? 266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 114.583 124.061 138.714 1.00 58.27  ? 266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 113.203 124.074 139.348 1.00 56.54  ? 266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 112.121 123.973 138.329 1.00 55.23  ? 266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 119.398 122.153 140.591 1.00 65.40  ? 267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 120.411 121.140 140.309 1.00 66.81  ? 267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 120.125 120.466 138.971 1.00 66.44  ? 267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 121.046 120.168 138.200 1.00 62.34  ? 267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 120.505 120.110 141.454 1.00 65.87  ? 267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 120.860 120.763 142.800 1.00 66.32  ? 267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 121.519 119.025 141.120 1.00 64.05  ? 267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 119.716 121.443 143.532 1.00 64.95  ? 267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 118.847 120.231 138.670 1.00 66.43  ? 268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 118.462 119.599 137.414 1.00 68.89  ? 268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 118.641 120.512 136.208 1.00 69.65  ? 268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 118.508 120.038 135.074 1.00 66.41  ? 268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 117.008 119.128 137.492 1.00 70.39  ? 268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 116.141 120.203 137.810 1.00 68.19  ? 268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 118.927 121.795 136.418 1.00 77.72  ? 269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 119.073 122.721 135.304 1.00 77.06  ? 269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 120.293 122.370 134.461 1.00 77.51  ? 269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 121.352 122.012 134.986 1.00 77.76  ? 269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 119.185 124.155 135.821 1.00 73.24  ? 269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 120.137 122.477 133.145 1.00 80.09  ? 270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.229 122.191 132.229 1.00 80.86  ? 270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 122.294 123.281 132.304 1.00 80.89  ? 270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 122.042 124.411 132.732 1.00 81.18  ? 270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 120.707 122.061 130.798 1.00 82.89  ? 270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 119.906 123.269 130.357 1.00 82.32  ? 270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 120.520 124.277 129.949 1.00 80.20  ? 270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 118.660 123.211 130.417 1.00 80.50  ? 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 123.506 122.926 131.869 1.00 81.83  ? 271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 124.635 123.848 131.938 1.00 84.11  ? 271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 124.448 125.075 131.055 1.00 82.00  ? 271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 125.129 126.083 131.267 1.00 80.11  ? 271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 125.927 123.125 131.553 1.00 82.68  ? 271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 126.430 122.153 132.607 1.00 81.98  ? 271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 126.913 122.854 133.860 1.00 83.21  ? 271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 127.514 123.943 133.740 1.00 80.90  ? 271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 126.695 122.317 134.967 1.00 82.72  ? 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 123.547 125.015 130.074 1.00 81.24  ? 272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 123.301 126.158 129.205 1.00 83.57  ? 272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 122.423 127.219 129.854 1.00 82.21  ? 272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.258 128.299 129.276 1.00 79.90  ? 272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 122.657 125.693 127.896 1.00 83.06  ? 272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 123.636 124.970 126.991 1.00 84.00  ? 272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 124.858 125.088 127.219 1.00 83.34  ? 272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 123.183 124.285 126.050 1.00 81.81  ? 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 121.858 126.944 131.028 1.00 76.38  ? 273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 120.986 127.894 131.709 1.00 75.71  ? 273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 121.412 128.028 133.167 1.00 73.60  ? 273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 120.880 128.861 133.907 1.00 76.15  ? 273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 119.510 127.467 131.596 1.00 75.71  ? 273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.154 126.467 132.688 1.00 77.06  ? 273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 118.595 128.683 131.649 1.00 72.38  ? 273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 122.383 127.220 133.582 1.00 70.30  ? 274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 122.822 127.171 134.970 1.00 70.52  ? 274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.014 128.093 135.183 1.00 70.80  ? 274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 124.992 128.037 134.430 1.00 71.69  ? 274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 123.193 125.742 135.374 1.00 72.28  ? 274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 123.586 125.590 136.834 1.00 71.61  ? 274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 124.185 124.219 137.102 1.00 72.27  ? 274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.103 124.236 138.236 1.00 71.77  ? 274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 126.404 124.478 138.143 1.00 73.07  ? 274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 127.144 124.472 139.248 1.00 72.47  ? 274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 126.980 124.727 136.979 1.00 71.16  ? 274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 123.929 128.936 136.208 1.00 61.10  ? 275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.043 129.765 136.647 1.00 58.28  ? 275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 125.637 129.133 137.898 1.00 59.01  ? 275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 124.963 128.390 138.621 1.00 59.13  ? 275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 124.616 131.225 136.913 1.00 53.74  ? 275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 123.935 131.810 135.686 1.00 49.83  ? 275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 123.701 131.303 138.123 1.00 54.23  ? 275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 126.914 129.428 138.151 1.00 52.49  ? 276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 127.613 128.793 139.261 1.00 55.82  ? 276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.227 129.794 140.233 1.00 51.91  ? 276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.207 129.545 141.446 1.00 58.29  ? 276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 128.699 127.848 138.726 1.00 59.43  ? 276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.684 127.353 139.772 1.00 59.49  ? 276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.043 127.069 139.155 1.00 59.16  ? 276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.955 125.948 138.133 1.00 59.95  ? 276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 131.080 124.608 138.771 1.00 56.72  ? 276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 128.753 130.919 139.755 1.00 42.83  ? 277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 129.299 131.944 140.635 1.00 48.07  ? 277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 128.361 133.117 140.870 1.00 46.65  ? 277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 128.744 134.047 141.591 1.00 46.70  ? 277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 130.629 132.483 140.085 1.00 50.25  ? 277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 130.375 133.574 139.192 1.00 47.07  ? 277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 131.380 131.389 139.344 1.00 45.68  ? 277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.162 133.117 140.294 1.00 38.74  ? 278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 126.204 134.204 140.477 1.00 32.36  ? 278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.200 133.816 141.553 1.00 29.29  ? 278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 124.297 133.012 141.316 1.00 38.13  ? 278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.496 134.533 139.169 1.00 33.75  ? 278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 125.361 136.024 138.860 1.00 32.64  ? 278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 126.594 136.776 139.307 1.00 34.69  ? 278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.099 136.251 137.391 1.00 35.69  ? 278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.358 134.392 142.742 1.00 28.68  ? 279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.299 134.336 143.736 1.00 26.09  ? 279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.080 135.088 143.222 1.00 24.96  ? 279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.199 136.135 142.581 1.00 40.98  ? 279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.775 134.939 145.056 1.00 27.45  ? 279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 125.872 134.214 145.581 1.00 31.25  ? 279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.898 134.550 143.493 1.00 24.65  ? 280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.658 135.123 142.988 1.00 25.93  ? 280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 119.848 135.655 144.160 1.00 24.67  ? 280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 119.828 135.057 145.240 1.00 31.54  ? 280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.842 134.105 142.161 1.00 28.61  ? 280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.401 132.917 143.014 1.00 31.07  ? 280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 120.644 133.633 140.959 1.00 31.41  ? 280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.174 132.216 142.476 1.00 22.44  ? 280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 119.218 136.802 143.951 1.00 13.89  ? 281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 118.322 137.368 144.937 1.00 5.64   ? 281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.023 137.792 144.288 1.00 15.52  ? 281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.991 138.231 143.140 1.00 30.80  ? 281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.941 137.655 145.047 1.00 20.29  ? 282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 114.598 137.947 144.564 1.00 17.44  ? 282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.023 139.085 145.391 1.00 23.52  ? 282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.046 139.035 146.627 1.00 39.01  ? 282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.691 136.705 144.623 1.00 17.27  ? 282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.235 137.109 144.560 1.00 26.02  ? 282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.023 135.766 143.481 1.00 28.56  ? 282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 113.516 140.106 144.711 1.00 16.77  ? 283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 112.921 141.272 145.350 1.00 15.92  ? 283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 111.411 141.083 145.355 1.00 19.05  ? 283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 110.786 140.994 144.290 1.00 34.62  ? 283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.320 142.566 144.628 1.00 15.14  ? 283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 112.716 143.766 145.319 1.00 13.13  ? 283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 114.832 142.678 144.560 1.00 14.28  ? 283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 110.824 141.022 146.544 1.00 17.08  ? 284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 109.410 140.708 146.713 1.00 20.64  ? 284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 108.707 141.957 147.237 1.00 27.59  ? 284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 108.849 142.296 148.421 1.00 28.98  ? 284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.205 139.519 147.661 1.00 20.18  ? 284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.961 138.294 147.148 1.00 16.62  ? 284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 107.724 139.210 147.812 1.00 24.46  ? 284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.588 137.008 147.844 1.00 24.35  ? 284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 107.945 142.668 146.411 1.00 34.01  ? 285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.097 143.742 146.932 1.00 34.46  ? 285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 105.949 143.177 147.754 1.00 36.43  ? 285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 105.626 141.990 147.691 1.00 33.44  ? 285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 106.584 144.444 145.670 1.00 32.35  ? 285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 107.491 143.993 144.569 1.00 29.79  ? 285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 107.931 142.617 144.941 1.00 30.17  ? 285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.331 144.057 148.547 1.00 42.76  ? 286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.178 143.651 149.340 1.00 37.57  ? 286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.011 143.205 148.471 1.00 45.91  ? 286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.149 142.457 148.945 1.00 51.15  ? 286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 103.731 144.793 150.255 1.00 42.35  ? 286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.439 144.779 151.594 1.00 52.31  ? 286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.422 144.023 151.741 1.00 53.96  ? 286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.016 145.528 152.500 1.00 49.35  ? 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 102.963 143.652 147.214 1.00 42.92  ? 287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 101.883 143.241 146.324 1.00 34.06  ? 287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 101.923 141.742 146.060 1.00 40.54  ? 287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 100.877 141.089 145.994 1.00 53.49  ? 287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 101.959 144.020 145.011 1.00 36.89  ? 287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 100.741 143.839 144.122 1.00 36.82  ? 287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 99.460  143.994 144.925 1.00 43.89  ? 287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.232  143.909 144.039 1.00 44.66  ? 287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 96.981  144.141 144.810 1.00 41.69  ? 287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.123 141.177 145.899 1.00 32.03  ? 288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.236 139.738 145.684 1.00 29.77  ? 288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.736 138.958 146.892 1.00 33.94  ? 288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.051 137.939 146.743 1.00 40.15  ? 288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 104.683 139.364 145.369 1.00 31.71  ? 288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.861 137.927 144.976 1.00 34.00  ? 288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.576 137.507 143.689 1.00 33.97  ? 288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.303 136.993 145.898 1.00 31.07  ? 288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 104.738 136.185 143.327 1.00 36.62  ? 288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.464 135.671 145.542 1.00 30.75  ? 288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.181 135.266 144.255 1.00 37.98  ? 288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.073 139.418 148.097 1.00 41.51  ? 289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.603 138.748 149.304 1.00 36.29  ? 289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.091 138.876 149.430 1.00 40.87  ? 289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.410 137.945 149.873 1.00 44.40  ? 289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.327 139.309 150.541 1.00 37.80  ? 289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 102.964 138.509 151.780 1.00 36.70  ? 289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.831 139.305 150.318 1.00 39.47  ? 289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 100.542 140.030 149.041 1.00 45.21  ? 290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.094  140.204 149.058 1.00 40.25  ? 290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.412  139.251 148.085 1.00 47.27  ? 290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.378  138.655 148.408 1.00 54.04  ? 290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 98.738  141.653 148.729 1.00 41.22  ? 290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.977  142.626 149.871 1.00 48.69  ? 290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 98.948  144.073 149.419 1.00 53.38  ? 290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.006  144.451 148.691 1.00 54.86  ? 290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 99.868  144.833 149.790 1.00 48.96  ? 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.974  139.100 146.884 1.00 39.97  ? 291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.392  138.197 145.895 1.00 39.45  ? 291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.485  136.744 146.346 1.00 45.65  ? 291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.540  135.969 146.159 1.00 50.13  ? 291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.079  138.380 144.544 1.00 38.37  ? 291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.936  139.749 143.880 1.00 36.20  ? 291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.979  139.916 142.791 1.00 36.48  ? 291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 97.538  139.929 143.321 1.00 44.96  ? 291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.620  136.354 146.929 1.00 42.71  ? 292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 99.766  134.986 147.417 1.00 41.49  ? 292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 98.826  134.711 148.584 1.00 41.93  ? 292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 98.270  133.613 148.695 1.00 42.13  ? 292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.216 134.724 147.820 1.00 35.92  ? 292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 98.644  135.694 149.467 1.00 46.59  ? 293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 97.748  135.520 150.606 1.00 48.30  ? 293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.309  135.310 150.153 1.00 53.14  ? 293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 95.601  134.450 150.690 1.00 54.46  ? 293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 97.850  136.731 151.532 1.00 48.18  ? 293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 96.827  136.761 152.651 1.00 48.19  ? 293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.771  138.140 153.282 1.00 48.39  ? 293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 98.106  138.685 153.490 1.00 57.32  ? 293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.493  139.891 153.098 1.00 55.54  ? 293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 99.744  140.280 153.333 1.00 52.37  ? 293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 97.664  140.715 152.479 1.00 47.17  ? 293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 95.861  136.082 149.167 1.00 56.44  ? 294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.498  135.991 148.666 1.00 57.47  ? 294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.328  134.912 147.604 1.00 56.51  ? 294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.210  134.717 147.115 1.00 55.27  ? 294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.054  137.345 148.105 1.00 54.60  ? 294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 93.754  138.389 149.167 1.00 57.55  ? 294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 92.590  137.998 150.057 1.00 62.28  ? 294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 91.497  137.714 149.522 1.00 61.42  ? 294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 92.768  137.974 151.294 1.00 57.21  ? 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 95.405  134.222 147.232 1.00 56.36  ? 295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 95.405  133.109 146.285 1.00 56.66  ? 295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 94.967  133.515 144.882 1.00 59.23  ? 295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 94.683  132.641 144.053 1.00 57.23  ? 295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 94.534  131.948 146.785 1.00 57.61  ? 295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 95.098  130.593 146.408 1.00 60.01  ? 295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.117  130.550 145.686 1.00 56.82  ? 295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 94.523  129.570 146.832 1.00 58.40  ? 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 94.899  134.810 144.590 1.00 63.38  ? 296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 94.588  135.252 143.239 1.00 61.80  ? 296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 95.746  134.938 142.301 1.00 60.89  ? 296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 96.914  134.964 142.692 1.00 60.97  ? 296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.296  136.752 143.211 1.00 61.70  ? 296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 93.947  137.349 144.558 1.00 62.42  ? 296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.827  138.860 144.472 1.00 62.78  ? 296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.462  139.279 143.954 1.00 61.28  ? 296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.397  139.073 144.973 1.00 59.11  ? 296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 95.412  134.639 141.049 1.00 56.58  ? 297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 96.442  134.409 140.046 1.00 55.39  ? 297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.167  135.714 139.744 1.00 54.15  ? 297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.535  136.736 139.459 1.00 51.92  ? 297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 95.828  133.830 138.774 1.00 52.43  ? 297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 98.492  135.678 139.807 1.00 43.76  ? 298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.313  136.862 139.614 1.00 43.71  ? 298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.893  136.889 138.206 1.00 46.39  ? 298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 99.874  135.898 137.474 1.00 50.67  ? 298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.435 136.915 140.655 1.00 43.38  ? 298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.414 138.054 137.831 1.00 39.33  ? 299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.013 138.260 136.522 1.00 35.93  ? 299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 102.418 138.811 136.693 1.00 35.97  ? 299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 102.615 139.808 137.393 1.00 46.71  ? 299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.177 139.223 135.674 1.00 37.45  ? 299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.793  138.719 135.345 1.00 40.61  ? 299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.566  137.937 134.222 1.00 41.65  ? 299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 97.711  139.029 136.157 1.00 44.54  ? 299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.301  137.475 133.918 1.00 42.53  ? 299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 96.444  138.572 135.862 1.00 40.88  ? 299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.244  137.796 134.741 1.00 41.86  ? 299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 94.981  137.338 134.443 1.00 43.21  ? 299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.386 138.164 136.065 1.00 30.31  ? 300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 104.713 138.743 135.908 1.00 27.55  ? 300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 104.748 139.453 134.564 1.00 37.85  ? 300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.165 138.991 133.577 1.00 44.06  ? 300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 105.822 137.679 136.029 1.00 31.24  ? 300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.900 137.161 137.455 1.00 39.90  ? 300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.579 136.538 135.065 1.00 36.99  ? 300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.429 140.591 134.520 1.00 37.67  ? 301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.307 141.515 133.407 1.00 31.73  ? 301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.595 141.570 132.599 1.00 36.96  ? 301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 107.676 141.213 133.075 1.00 40.41  ? 301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 104.945 142.919 133.902 1.00 33.27  ? 301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 103.779 142.940 134.844 1.00 36.83  ? 301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.483 142.957 134.361 1.00 34.52  ? 301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 103.979 142.940 136.213 1.00 33.06  ? 301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.410 142.971 135.224 1.00 36.02  ? 301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 102.909 142.957 137.081 1.00 37.21  ? 301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 101.623 142.973 136.587 1.00 39.28  ? 301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.454 142.019 131.354 1.00 41.69  ? 302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 107.596 142.261 130.489 1.00 41.80  ? 302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.077 143.690 130.701 1.00 41.98  ? 302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.324 144.630 130.417 1.00 45.35  ? 302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.222 142.042 129.033 1.00 40.95  ? 302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 106.963 140.594 128.668 1.00 39.73  ? 302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 105.832 139.931 129.126 1.00 35.09  ? 302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 107.844 139.894 127.859 1.00 41.88  ? 302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 105.592 138.613 128.794 1.00 38.23  ? 302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 107.612 138.577 127.519 1.00 41.93  ? 302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 106.484 137.942 127.989 1.00 43.62  ? 302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.252 136.628 127.655 1.00 47.04  ? 302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.294 143.899 131.210 1.00 35.42  ? 303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.716 145.264 131.569 1.00 36.29  ? 303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.734 146.242 130.407 1.00 39.56  ? 303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.434 147.426 130.610 1.00 43.15  ? 303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.124 145.050 132.142 1.00 37.93  ? 303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.139 143.630 132.578 1.00 37.67  ? 303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.300 142.895 131.585 1.00 32.40  ? 303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.078 145.795 129.198 1.00 38.27  ? 304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.186 146.733 128.085 1.00 38.22  ? 304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.824 147.262 127.661 1.00 44.13  ? 304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.716 148.419 127.243 1.00 48.89  ? 304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 110.891 146.079 126.899 1.00 41.86  ? 304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.160 147.021 125.767 1.00 45.30  ? 304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 111.796 148.230 125.945 1.00 41.84  ? 304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 110.881 146.931 124.446 1.00 43.46  ? 304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 111.896 148.847 124.780 1.00 42.00  ? 304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.350 148.080 123.855 1.00 46.57  ? 304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.777 146.439 127.757 1.00 38.42  ? 305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.433 146.928 127.470 1.00 35.88  ? 305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.030 148.024 128.449 1.00 38.02  ? 305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.450 149.042 128.053 1.00 42.75  ? 305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.433 145.774 127.515 1.00 40.62  ? 305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.449 145.179 128.817 1.00 44.94  ? 305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 105.796 144.720 126.481 1.00 41.10  ? 305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.346 147.837 129.732 1.00 43.45  ? 306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.057 148.859 130.733 1.00 39.93  ? 306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.858 150.123 130.454 1.00 41.54  ? 306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.349 151.241 130.590 1.00 43.63  ? 306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.333 148.314 132.146 1.00 36.86  ? 306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.434 147.112 132.433 1.00 39.88  ? 306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.125 149.398 133.187 1.00 41.25  ? 306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.705 146.457 133.757 1.00 42.15  ? 306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.126 149.967 130.065 1.00 43.36  ? 307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.946 151.130 129.744 1.00 41.49  ? 307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.378 151.899 128.557 1.00 41.82  ? 307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.327 153.134 128.573 1.00 47.55  ? 307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.384 150.701 129.461 1.00 39.25  ? 307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.370 151.845 129.487 1.00 46.13  ? 307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.418 152.718 130.564 1.00 46.94  ? 307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 112.244 152.058 128.432 1.00 45.70  ? 307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.314 153.768 130.592 1.00 43.91  ? 307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 113.143 153.105 128.451 1.00 48.25  ? 307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.173 153.958 129.534 1.00 48.03  ? 307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 114.066 155.003 129.561 1.00 46.83  ? 307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 107.951 151.185 127.514 1.00 41.35  ? 308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.374 151.846 126.348 1.00 40.70  ? 308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.060 152.536 126.692 1.00 44.41  ? 308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.791 153.643 126.212 1.00 47.19  ? 308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.167 150.837 125.220 1.00 43.04  ? 308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.454 150.278 124.638 1.00 40.96  ? 308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.178 149.438 123.403 1.00 45.04  ? 308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.203 148.311 123.707 1.00 44.07  ? 308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.820 146.969 123.528 1.00 42.24  ? 308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.228 151.900 127.521 1.00 43.70  ? 309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.916 152.466 127.819 1.00 44.71  ? 309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.015 153.665 128.756 1.00 47.81  ? 309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.320 154.668 128.559 1.00 50.08  ? 309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.008 151.394 128.419 1.00 45.59  ? 309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.701 151.200 127.671 1.00 48.73  ? 309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.653 152.232 128.043 1.00 50.05  ? 309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 100.939 153.103 128.889 1.00 53.12  ? 309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.535  152.168 127.490 1.00 46.94  ? 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.872 153.585 129.775 1.00 45.93  ? 310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.895 154.581 130.836 1.00 47.15  ? 310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.139 155.456 130.846 1.00 45.81  ? 310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.110 156.526 131.460 1.00 49.16  ? 310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.764 153.895 132.204 1.00 49.46  ? 310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.502 153.075 132.350 1.00 49.42  ? 310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.325 153.651 132.804 1.00 45.85  ? 310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.488 151.725 132.024 1.00 45.69  ? 310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.170 152.905 132.935 1.00 46.96  ? 310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.338 150.973 132.150 1.00 44.92  ? 310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.183 151.567 132.608 1.00 48.84  ? 310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.035 150.821 132.737 1.00 48.95  ? 310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.218 155.041 130.189 1.00 43.47  ? 311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.446 155.806 130.191 1.00 44.78  ? 311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.344 155.575 131.384 1.00 44.80  ? 311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.409 156.201 131.465 1.00 49.63  ? 311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.955 154.707 132.313 1.00 42.65  ? 312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.767 154.375 133.472 1.00 43.41  ? 312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.916 152.864 133.564 1.00 43.41  ? 312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.031 152.111 133.153 1.00 45.95  ? 312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 109.155 154.916 134.772 1.00 44.75  ? 312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.444 156.249 134.621 1.00 47.63  ? 312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.288 156.404 135.588 1.00 50.81  ? 312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 107.368 155.983 136.742 1.00 49.67  ? 312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 106.202 157.010 135.120 1.00 47.10  ? 312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 111.050 152.430 134.106 1.00 45.85  ? 313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.298 151.007 134.272 1.00 46.74  ? 313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.344 150.423 135.309 1.00 46.60  ? 313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.836 151.127 136.183 1.00 47.00  ? 313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.747 150.765 134.685 1.00 44.60  ? 313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.746 151.282 133.697 1.00 47.86  ? 313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.111 150.578 132.570 1.00 47.64  ? 313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.453 152.436 133.664 1.00 44.69  ? 313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 115.001 151.275 131.887 1.00 43.96  ? 313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.226 152.406 132.529 1.00 47.56  ? 313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.103 149.115 135.198 1.00 45.45  ? 314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.122 148.464 136.062 1.00 44.47  ? 314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.512 148.573 137.531 1.00 44.96  ? 314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.655 148.818 138.390 1.00 44.96  ? 314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.959 146.999 135.657 1.00 42.01  ? 314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 107.998 146.217 136.534 1.00 40.00  ? 314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 107.915 144.478 136.074 1.00 51.27  ? 314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 109.483 143.893 136.710 1.00 40.74  ? 314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.795 148.396 137.844 1.00 40.01  ? 315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.243 148.493 139.227 1.00 44.13  ? 315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.316 149.931 139.729 1.00 43.52  ? 315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.460 150.139 140.938 1.00 46.19  ? 315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.604 147.813 139.394 1.00 39.42  ? 315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.687 148.447 138.545 1.00 44.32  ? 315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.359 149.279 137.674 1.00 47.63  ? 315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 114.872 148.110 138.749 1.00 43.65  ? 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.223 150.919 138.839 1.00 40.58  ? 316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.203 152.318 139.248 1.00 40.88  ? 316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.827 152.792 139.695 1.00 46.74  ? 316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.729 153.860 140.309 1.00 44.51  ? 316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.699 153.207 138.106 1.00 43.33  ? 316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 113.147 152.978 137.719 1.00 45.09  ? 316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.111 153.646 138.676 1.00 51.31  ? 316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 113.699 154.603 139.364 1.00 49.57  ? 316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 115.282 153.220 138.738 1.00 51.52  ? 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.772 152.039 139.405 1.00 48.31  ? 317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.418 152.404 139.790 1.00 47.37  ? 317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 106.968 151.594 140.999 1.00 50.99  ? 317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.526 150.543 141.320 1.00 45.28  ? 317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.445 152.195 138.627 1.00 45.82  ? 317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.104 152.180 137.261 1.00 46.21  ? 317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 105.925 152.083 135.902 1.00 52.26  ? 317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.104 153.667 136.048 1.00 49.08  ? 317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 105.940 152.105 141.672 1.00 53.26  ? 318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.389 151.443 142.848 1.00 48.38  ? 318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.542 150.257 142.407 1.00 49.17  ? 318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.518 150.433 141.739 1.00 49.07  ? 318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.559 152.423 143.672 1.00 50.01  ? 318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.474 152.030 145.133 1.00 54.99  ? 318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.313 151.221 145.582 1.00 51.52  ? 318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.568 152.528 145.833 1.00 54.87  ? 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 104.968 149.049 142.782 1.00 47.63  ? 319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.241 147.851 142.377 1.00 45.46  ? 319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.842 147.817 142.979 1.00 44.16  ? 319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.876 147.463 142.292 1.00 49.34  ? 319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.025 146.603 142.776 1.00 45.08  ? 319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.622 145.359 142.011 1.00 47.70  ? 319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 105.406 145.252 140.393 1.00 58.09  ? 319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 104.029 145.666 139.331 1.00 42.97  ? 319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.712 148.193 144.253 1.00 46.91  ? 320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.414 148.142 144.918 1.00 51.19  ? 320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.392 149.037 144.233 1.00 49.68  ? 320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.199  148.714 144.210 1.00 46.85  ? 320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.564 148.537 146.387 1.00 50.36  ? 320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.393 147.545 147.174 1.00 50.56  ? 320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 103.600 147.420 146.964 1.00 42.85  ? 320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 101.750 146.832 148.091 1.00 49.91  ? 320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.835 150.160 143.672 1.00 54.32  ? 321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.937  151.072 142.977 1.00 55.20  ? 321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.786  150.729 141.500 1.00 54.32  ? 321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.685  150.832 140.950 1.00 50.45  ? 321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.433 152.515 143.132 1.00 52.76  ? 321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 100.190 153.403 141.920 1.00 55.02  ? 321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 100.250 154.881 142.252 1.00 57.11  ? 321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 99.495  155.322 143.143 1.00 56.83  ? 321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 101.054 155.600 141.623 1.00 57.36  ? 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.866 150.304 140.849 1.00 46.74  ? 322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 100.882 150.143 139.402 1.00 43.75  ? 322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.530 148.733 138.945 1.00 46.06  ? 322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.447 148.500 137.735 1.00 50.56  ? 322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.260 150.528 138.852 1.00 44.74  ? 322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.582 152.017 138.936 1.00 49.59  ? 322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.513 153.117 137.986 1.00 51.37  ? 322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.267 152.177 136.485 1.00 46.93  ? 322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.312 147.792 139.866 1.00 44.49  ? 323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.035 146.415 139.462 1.00 40.53  ? 323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 98.708  146.306 138.722 1.00 45.32  ? 323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.627  145.670 137.664 1.00 50.66  ? 323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.042 145.496 140.683 1.00 42.56  ? 323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 99.667  144.065 140.367 1.00 44.37  ? 323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 100.612 143.169 139.889 1.00 44.01  ? 323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.367  143.610 140.548 1.00 45.19  ? 323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.273 141.863 139.600 1.00 38.55  ? 323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.021  142.306 140.260 1.00 42.62  ? 323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.977  141.437 139.787 1.00 41.50  ? 323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.637  140.136 139.500 1.00 45.65  ? 323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.652  146.909 139.270 1.00 48.27  ? 324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.348  146.843 138.618 1.00 46.33  ? 324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.365  147.575 137.283 1.00 45.68  ? 324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 95.714  147.145 136.324 1.00 50.31  ? 324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.271  147.417 139.536 1.00 47.43  ? 324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 94.977  146.516 140.719 1.00 50.45  ? 324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 94.907  145.285 140.528 1.00 47.18  ? 324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 94.818  147.041 141.842 1.00 51.86  ? 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.103  148.683 137.202 1.00 47.64  ? 325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.213  149.408 135.941 1.00 49.34  ? 325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 97.960  148.587 134.897 1.00 51.44  ? 325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.600  148.607 133.715 1.00 60.57  ? 325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 97.895  150.754 136.172 1.00 48.71  ? 325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.084  151.700 137.042 1.00 49.47  ? 325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.754  153.054 137.180 1.00 51.08  ? 325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 96.933  153.980 138.062 1.00 49.78  ? 325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.693  155.198 138.454 1.00 52.63  ? 325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.004  147.864 135.309 1.00 43.85  ? 326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 99.698  146.969 134.386 1.00 39.09  ? 326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 98.778  145.851 133.915 1.00 41.35  ? 326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 98.747  145.514 132.726 1.00 47.53  ? 326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 100.940 146.376 135.052 1.00 42.47  ? 326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.005 147.379 135.380 1.00 41.44  ? 326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.010 148.633 134.800 1.00 44.57  ? 326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.010 147.059 136.275 1.00 42.09  ? 326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 102.999 149.544 135.108 1.00 42.30  ? 326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 103.997 147.967 136.587 1.00 46.01  ? 326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 103.990 149.211 136.003 1.00 46.00  ? 326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.023  145.258 134.842 1.00 45.48  ? 327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.167  144.128 134.496 1.00 47.89  ? 327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.044  144.568 133.564 1.00 51.09  ? 327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 95.677  143.849 132.627 1.00 51.12  ? 327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 96.625  143.462 135.774 1.00 41.80  ? 327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 95.503  142.492 135.444 1.00 47.41  ? 327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 97.746  142.744 136.504 1.00 40.31  ? 327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.496  145.760 133.788 1.00 46.68  ? 328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.421  146.274 132.952 1.00 47.20  ? 328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 94.925  146.934 131.676 1.00 51.02  ? 328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.109  147.426 130.889 1.00 56.52  ? 328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.570  147.269 133.746 1.00 49.78  ? 328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 92.920  146.639 134.961 1.00 53.81  ? 328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.774  145.399 134.983 1.00 53.24  ? 328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.553  147.383 135.895 1.00 51.34  ? 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.239  146.959 131.453 1.00 47.92  ? 329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 96.805  147.603 130.275 1.00 47.10  ? 329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.023  146.561 129.187 1.00 51.37  ? 329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.877  145.677 129.357 1.00 46.74  ? 329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.118  148.287 130.624 1.00 42.32  ? 329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.474  149.396 129.658 1.00 45.65  ? 329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.520  150.028 129.784 1.00 48.71  ? 329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 97.601  149.640 128.689 1.00 51.03  ? 329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.288  146.610 128.073 1.00 55.29  ? 330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.549  145.657 126.982 1.00 49.62  ? 330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 97.912  145.829 126.340 1.00 49.38  ? 330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.424  144.869 125.750 1.00 51.61  ? 330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.421  145.950 125.983 1.00 49.25  ? 330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.020  147.358 126.270 1.00 48.43  ? 330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.190  147.536 127.750 1.00 49.95  ? 330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.516  147.014 126.432 1.00 45.57  ? 331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.824  147.257 125.838 1.00 47.34  ? 331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 100.971 146.736 126.694 1.00 46.98  ? 331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.103 146.667 126.205 1.00 43.48  ? 331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.011 148.753 125.580 1.00 46.45  ? 331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.179  149.287 124.428 1.00 45.67  ? 331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.080  150.804 124.466 1.00 48.27  ? 331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.317  151.285 125.612 1.00 48.69  ? 331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.001  151.177 125.740 1.00 48.52  ? 331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.414  151.660 126.831 1.00 50.90  ? 331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.259  150.607 124.804 1.00 44.04  ? 331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.712 146.375 127.946 1.00 46.74  ? 332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.728 145.806 128.822 1.00 44.63  ? 332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.612 144.289 128.740 1.00 47.00  ? 332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.656 143.702 129.252 1.00 50.07  ? 332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.572 146.302 130.265 1.00 43.73  ? 332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.454 145.495 131.203 1.00 41.52  ? 332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 101.902 147.783 130.356 1.00 40.70  ? 332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.579 143.655 128.083 1.00 47.68  ? 333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.567 142.205 127.965 1.00 43.17  ? 333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 102.894 141.564 129.306 1.00 40.63  ? 333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 103.720 142.069 130.071 1.00 44.70  ? 333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.565 141.749 126.900 1.00 43.55  ? 333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.388 140.304 126.466 1.00 45.37  ? 333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.505 139.856 125.540 1.00 41.45  ? 333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.392 138.375 125.224 1.00 44.08  ? 333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.467 137.919 124.299 1.00 48.11  ? 333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.236 140.444 129.594 1.00 39.39  ? 334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.428 139.752 130.860 1.00 40.02  ? 334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.027 138.296 130.690 1.00 43.57  ? 334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.338 137.929 129.733 1.00 48.27  ? 334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.615 140.403 131.981 1.00 39.47  ? 334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.137 140.528 131.667 1.00 40.79  ? 334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.524  141.729 132.357 1.00 42.56  ? 334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 98.340  142.262 131.571 1.00 39.04  ? 334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.751  143.285 130.573 1.00 45.64  ? 334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.467 137.468 131.634 1.00 39.59  ? 335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.102 136.061 131.673 1.00 44.95  ? 335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.592 135.720 133.065 1.00 43.07  ? 335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.062 136.276 134.062 1.00 46.10  ? 335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.286 135.160 131.281 1.00 44.68  ? 335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.118 134.641 132.438 1.00 45.44  ? 335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.488 134.161 132.000 1.00 49.58  ? 335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.718 134.049 130.777 1.00 44.32  ? 335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 106.335 133.898 132.878 1.00 49.87  ? 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.611 134.824 133.125 1.00 46.82  ? 336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 99.955  134.495 134.382 1.00 42.24  ? 336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 100.778 133.483 135.167 1.00 41.80  ? 336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.231 132.474 134.616 1.00 47.51  ? 336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.552  133.949 134.120 1.00 43.72  ? 336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 97.908  133.284 135.325 1.00 47.66  ? 336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 96.584  132.635 134.956 1.00 47.00  ? 336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.522  133.678 134.659 1.00 45.58  ? 336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.608  134.835 135.592 1.00 44.75  ? 336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 100.973 133.756 136.457 1.00 37.92  ? 337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 101.675 132.862 137.365 1.00 39.00  ? 337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 100.821 132.676 138.612 1.00 46.16  ? 337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 99.877  133.423 138.868 1.00 46.88  ? 337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.073 133.384 137.750 1.00 35.27  ? 337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 102.952 134.723 138.479 1.00 41.47  ? 337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 103.958 133.510 136.522 1.00 39.78  ? 337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 103.959 134.909 139.585 1.00 38.33  ? 337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.169 131.655 139.393 1.00 42.27  ? 338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 100.524 131.423 140.676 1.00 40.39  ? 338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 101.449 131.921 141.774 1.00 42.14  ? 338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 102.504 131.310 142.003 1.00 43.64  ? 338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 100.211 129.941 140.866 1.00 40.85  ? 338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 99.226  129.692 141.990 1.00 42.31  ? 338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.498  129.998 143.150 1.00 44.24  ? 338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 98.073  129.130 141.651 1.00 42.46  ? 338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.119 133.016 142.463 1.00 39.38  ? 339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.045 133.550 143.476 1.00 35.81  ? 339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 102.327 132.584 144.610 1.00 38.20  ? 339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 103.448 132.570 145.130 1.00 41.57  ? 339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.331 134.815 143.971 1.00 38.63  ? 339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 99.899  134.600 143.644 1.00 42.19  ? 339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 99.871  133.791 142.386 1.00 38.80  ? 339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 101.348 131.772 145.012 1.00 40.80  ? 340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 101.596 130.778 146.050 1.00 38.94  ? 340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 102.496 129.655 145.553 1.00 39.45  ? 340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 103.378 129.199 146.290 1.00 42.25  ? 340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 100.271 130.215 146.565 1.00 37.27  ? 340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.209 130.078 148.076 1.00 40.82  ? 340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 98.843  129.602 148.534 1.00 39.83  ? 340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 97.975  130.720 148.881 1.00 43.04  ? 340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.014  130.667 149.794 1.00 42.65  ? 340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 96.289  131.754 150.035 1.00 38.57  ? 340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.762  129.558 150.469 1.00 42.72  ? 340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 102.303 129.209 144.311 1.00 40.69  ? 341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 103.213 128.226 143.731 1.00 39.32  ? 341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 104.615 128.800 143.586 1.00 38.27  ? 341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 105.605 128.092 143.792 1.00 39.92  ? 341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 102.683 127.748 142.379 1.00 43.32  ? 341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 101.448 126.862 142.464 1.00 46.89  ? 341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 101.529 125.894 143.633 1.00 46.55  ? 341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.315 124.647 143.262 1.00 43.25  ? 341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.623 123.847 142.214 1.00 44.55  ? 341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 104.721 130.083 143.232 1.00 41.96  ? 342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 106.032 130.718 143.148 1.00 40.26  ? 342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 106.685 130.821 144.521 1.00 39.18  ? 342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 107.901 130.647 144.649 1.00 41.92  ? 342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 105.910 132.097 142.502 1.00 31.99  ? 342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.232 132.798 142.185 1.00 32.11  ? 342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.154 131.870 141.417 1.00 34.25  ? 342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 106.986 134.071 141.400 1.00 35.70  ? 342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 105.897 131.110 145.559 1.00 38.11  ? 343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 106.437 131.127 146.916 1.00 38.63  ? 343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 106.925 129.745 147.334 1.00 40.50  ? 343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 107.976 129.616 147.973 1.00 41.46  ? 343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 105.381 131.639 147.894 1.00 39.48  ? 343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 105.357 133.148 148.138 1.00 37.50  ? 343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 104.353 133.492 149.221 1.00 34.45  ? 343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 106.740 133.648 148.510 1.00 40.98  ? 343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 106.170 128.701 146.992 1.00 43.06  ? 344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 106.611 127.343 147.294 1.00 39.62  ? 344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 107.881 126.993 146.527 1.00 40.62  ? 344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 108.764 126.307 147.056 1.00 46.88  ? 344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 105.495 126.347 146.982 1.00 41.19  ? 344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 104.265 126.512 147.859 1.00 45.24  ? 344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 103.060 125.768 147.322 1.00 52.68  ? 344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 103.231 124.954 146.389 1.00 52.04  ? 344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 101.943 125.998 147.828 1.00 47.82  ? 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 107.987 127.451 145.278 1.00 36.84  ? 345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 109.214 127.253 144.513 1.00 37.42  ? 345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 110.389 127.967 145.169 1.00 40.01  ? 345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 111.495 127.424 145.233 1.00 38.89  ? 345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 109.021 127.744 143.078 1.00 34.98  ? 345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 110.245 127.578 142.197 1.00 38.59  ? 345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.006 128.140 140.807 1.00 39.20  ? 345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 111.189 127.874 139.893 1.00 41.58  ? 345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 110.965 128.420 138.526 1.00 41.79  ? 345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 110.164 129.187 145.658 1.00 42.30  ? 346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 111.203 129.901 146.394 1.00 32.55  ? 346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 111.638 129.113 147.621 1.00 35.31  ? 346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 112.835 128.967 147.888 1.00 36.48  ? 346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 110.701 131.284 146.810 1.00 33.03  ? 346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 110.451 132.345 145.742 1.00 36.90  ? 346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 109.762 133.540 146.366 1.00 41.21  ? 346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 111.753 132.765 145.107 1.00 32.06  ? 346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 110.669 128.601 148.381 1.00 39.79  ? 347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 110.988 127.854 149.594 1.00 31.04  ? 347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 111.781 126.593 149.275 1.00 40.26  ? 347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 112.758 126.276 149.963 1.00 48.88  ? 347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 109.708 127.505 150.349 1.00 31.91  ? 347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 111.383 125.867 148.229 1.00 43.35  ? 348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 112.104 124.649 147.872 1.00 40.50  ? 348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 113.496 124.968 147.336 1.00 42.05  ? 348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 114.448 124.221 147.590 1.00 46.42  ? 348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 111.287 123.826 146.871 1.00 44.71  ? 348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 111.361 124.284 145.427 1.00 48.70  ? 348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 112.450 123.264 144.418 1.00 62.99  ? 348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.499 124.224 142.909 1.00 48.30  ? 348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 113.644 126.083 146.615 1.00 37.11  ? 349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 114.967 126.490 146.151 1.00 37.30  ? 349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 115.876 126.848 147.317 1.00 37.06  ? 349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 117.061 126.499 147.314 1.00 41.40  ? 349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 114.850 127.667 145.184 1.00 38.75  ? 349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 114.618 127.327 143.713 1.00 38.80  ? 349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 113.718 128.363 143.070 1.00 38.48  ? 349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 115.942 127.232 142.975 1.00 41.94  ? 349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 115.347 127.557 148.317 1.00 34.88  ? 350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 116.152 127.876 149.492 1.00 34.48  ? 350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 116.500 126.618 150.280 1.00 40.91  ? 350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 117.602 126.508 150.830 1.00 45.94  ? 350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 115.425 128.886 150.381 1.00 34.11  ? 350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 114.960 130.134 149.659 1.00 31.05  ? 350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 114.671 131.263 150.629 1.00 34.81  ? 350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.814 132.153 150.787 1.00 39.44  ? 350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.300 132.549 151.955 1.00 40.74  ? 350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 117.352 133.361 151.979 1.00 36.41  ? 350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 115.761 132.153 153.097 1.00 39.59  ? 350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 115.572 125.664 150.354 1.00 40.64  ? 351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 115.856 124.412 151.048 1.00 42.18  ? 351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 116.940 123.612 150.334 1.00 47.16  ? 351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 117.801 123.008 150.984 1.00 52.89  ? 351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 114.580 123.583 151.179 1.00 42.21  ? 351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 113.465 124.404 151.475 1.00 49.37  ? 351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 116.917 123.594 149.001 1.00 46.26  ? 352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 117.846 122.750 148.257 1.00 45.36  ? 352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 119.198 123.416 148.023 1.00 48.19  ? 352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 120.209 122.716 147.908 1.00 54.55  ? 352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 117.216 122.334 146.924 1.00 48.70  ? 352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.378 123.341 145.798 1.00 50.50  ? 352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.585 122.965 144.563 1.00 55.33  ? 352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 115.477 122.413 144.716 1.00 50.63  ? 352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.062 123.232 143.441 1.00 58.56  ? 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 119.248 124.747 147.950 1.00 42.67  ? 353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 120.495 125.434 147.634 1.00 45.08  ? 353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 120.782 126.663 148.482 1.00 42.13  ? 353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 121.918 127.147 148.448 1.00 40.32  ? 353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 120.511 125.845 146.154 1.00 43.01  ? 353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 119.591 126.893 145.906 1.00 40.34  ? 353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 119.816 127.188 149.235 1.00 33.02  ? 354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 120.010 128.405 149.995 1.00 34.65  ? 354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 119.698 129.681 149.245 1.00 30.39  ? 354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 119.698 130.756 149.856 1.00 36.33  ? 354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 119.425 129.596 147.951 1.00 29.94  ? 355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.060 130.723 147.113 1.00 27.38  ? 355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 117.568 130.694 146.813 1.00 31.66  ? 355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 116.940 129.631 146.850 1.00 37.10  ? 355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 119.858 130.690 145.802 1.00 32.59  ? 355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 121.351 130.805 145.998 1.00 36.19  ? 355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 121.927 132.003 146.395 1.00 28.63  ? 355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 122.184 129.714 145.792 1.00 38.68  ? 355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.290 132.112 146.578 1.00 33.58  ? 355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 123.549 129.815 145.972 1.00 38.18  ? 355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.096 131.016 146.365 1.00 36.80  ? 355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 125.455 131.123 146.547 1.00 38.08  ? 355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 116.958 131.845 146.501 1.00 29.70  ? 356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 117.529 133.187 146.349 1.00 26.30  ? 356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.565 134.003 147.633 1.00 28.48  ? 356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.023 133.605 148.659 1.00 31.52  ? 356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.585 133.821 145.330 1.00 27.76  ? 356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.250 133.268 145.734 1.00 23.30  ? 356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 115.519 131.846 146.184 1.00 20.89  ? 356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.210 135.166 147.589 1.00 32.10  ? 357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.106 136.127 148.677 1.00 18.46  ? 357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.750 136.814 148.607 1.00 24.89  ? 357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.465 137.542 147.651 1.00 35.06  ? 357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.231 137.157 148.596 1.00 20.60  ? 357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.621 136.577 148.473 1.00 21.65  ? 357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 120.952 135.383 149.092 1.00 24.26  ? 357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 121.608 137.232 147.750 1.00 24.61  ? 357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.218 134.851 148.992 1.00 23.37  ? 357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.880 136.708 147.643 1.00 26.38  ? 357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.179 135.517 148.268 1.00 29.69  ? 357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.444 134.985 148.170 1.00 36.10  ? 357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.914 136.585 149.612 1.00 29.41  ? 358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.571 137.151 149.646 1.00 29.64  ? 358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.664 138.578 150.164 1.00 27.98  ? 358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.085 138.808 151.302 1.00 35.84  ? 358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.632 136.306 150.519 1.00 29.87  ? 358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.673 134.840 150.086 1.00 26.12  ? 358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.216 136.846 150.449 1.00 28.15  ? 358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.088 134.591 148.717 1.00 31.80  ? 358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 114.271 139.538 149.331 1.00 16.46  ? 359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 114.267 140.948 149.695 1.00 12.80  ? 359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 112.839 141.465 149.634 1.00 15.24  ? 359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 112.203 141.416 148.577 1.00 31.31  ? 359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 115.172 141.761 148.768 1.00 15.58  ? 359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.297 143.218 149.168 1.00 18.66  ? 359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 115.253 144.348 147.772 1.00 34.30  ? 359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.279 145.917 148.623 1.00 15.99  ? 359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 112.340 141.959 150.763 1.00 18.71  ? 360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 110.996 142.524 150.838 1.00 17.61  ? 360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.104 144.017 150.561 1.00 25.64  ? 360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.456 144.799 151.445 1.00 34.54  ? 360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 110.366 142.238 152.195 1.00 19.04  ? 360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.308 140.778 152.535 1.00 21.92  ? 360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 109.502 139.916 151.811 1.00 24.39  ? 360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.065 140.265 153.573 1.00 25.51  ? 360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 109.449 138.572 152.119 1.00 23.23  ? 360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.017 138.924 153.886 1.00 23.89  ? 360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.207 138.075 153.159 1.00 25.55  ? 360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 110.789 144.411 149.324 1.00 27.85  ? 361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.024 145.786 148.891 1.00 22.41  ? 361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.229 146.784 149.720 1.00 22.94  ? 361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 110.751 147.837 150.103 1.00 30.97  ? 361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.679 145.932 147.410 1.00 24.42  ? 361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 111.576 146.894 146.658 1.00 26.21  ? 361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.044 147.228 145.282 1.00 32.69  ? 361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 110.027 146.688 144.850 1.00 41.56  ? 361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 111.732 148.123 144.583 1.00 32.23  ? 361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 108.963 146.479 150.006 1.00 28.72  ? 362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.143 147.422 150.757 1.00 25.84  ? 362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 108.546 147.473 152.224 1.00 27.04  ? 362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.346 148.499 152.882 1.00 34.97  ? 362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 106.666 147.063 150.617 1.00 32.03  ? 362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.084 147.505 149.288 1.00 40.61  ? 362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 105.593 148.650 149.206 1.00 42.75  ? 362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 106.121 146.710 148.327 1.00 39.12  ? 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.112 146.386 152.753 1.00 31.71  ? 363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 109.660 146.430 154.103 1.00 21.51  ? 363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 110.893 147.319 154.169 1.00 22.43  ? 363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.202 147.874 155.231 1.00 28.50  ? 363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.002 145.021 154.583 1.00 17.52  ? 363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 108.805 144.294 155.154 1.00 23.79  ? 363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 107.739 144.879 155.339 1.00 28.07  ? 363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 108.975 143.011 155.440 1.00 24.55  ? 363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 111.607 147.461 153.054 1.00 21.73  ? 364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 112.768 148.341 153.011 1.00 20.87  ? 364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.340 149.789 152.821 1.00 19.33  ? 364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 112.838 150.690 153.504 1.00 23.82  ? 364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 113.730 147.892 151.899 1.00 14.54  ? 364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 114.979 148.752 151.906 1.00 16.53  ? 364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.079 146.428 152.058 1.00 10.29  ? 364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.409 150.034 151.901 1.00 24.45  ? 365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.050 151.389 151.508 1.00 19.57  ? 365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.041 152.045 152.441 1.00 21.67  ? 365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 109.831 153.258 152.335 1.00 28.32  ? 365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.503 151.387 150.079 1.00 21.63  ? 365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 111.522 150.899 149.071 1.00 20.22  ? 365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 112.571 151.515 148.886 1.00 23.69  ? 365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.220 149.789 148.412 1.00 22.70  ? 365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.414 151.289 153.344 1.00 22.79  ? 366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.489 151.908 154.288 1.00 26.69  ? 366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.231 152.715 155.343 1.00 29.24  ? 366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 108.682 153.682 155.884 1.00 33.94  ? 366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.611 150.846 154.949 1.00 24.40  ? 366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.369 149.838 155.797 1.00 34.60  ? 366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.445 149.145 156.784 1.00 32.37  ? 366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.403 148.307 156.064 1.00 27.70  ? 366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.604 147.483 157.012 1.00 29.00  ? 366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.471 152.339 155.645 1.00 28.89  ? 367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.309 153.041 156.606 1.00 24.17  ? 367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.588 153.560 155.952 1.00 23.14  ? 367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.526 153.947 156.640 1.00 25.06  ? 367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 111.623 152.149 157.820 1.00 22.47  ? 367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 110.371 151.935 158.652 1.00 24.80  ? 367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.186 150.821 157.359 1.00 18.51  ? 367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.632 153.566 154.622 1.00 24.05  ? 368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 113.789 154.071 153.897 1.00 13.93  ? 368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 113.796 155.593 153.941 1.00 22.74  ? 368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.805 156.239 153.587 1.00 28.44  ? 368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 113.764 153.577 152.453 1.00 13.03  ? 368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 114.961 153.980 151.651 1.00 13.05  ? 368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 114.874 154.387 150.338 1.00 25.72  ? 368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.274 154.032 151.974 1.00 14.42  ? 368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.081 154.674 149.887 1.00 18.84  ? 368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 116.949 154.466 150.859 1.00 18.75  ? 368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 114.917 156.163 154.380 1.00 26.76  ? 369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.014 157.605 154.549 1.00 21.48  ? 369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.247 158.346 153.240 1.00 30.37  ? 369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 114.949 159.541 153.161 1.00 35.88  ? 369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.135 157.942 155.531 1.00 20.94  ? 369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.761 157.670 152.217 1.00 30.55  ? 370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.147 158.307 150.962 1.00 20.32  ? 370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.283 157.832 149.798 1.00 22.51  ? 370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.779 157.591 148.697 1.00 26.14  ? 370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.623 158.055 150.669 1.00 14.42  ? 370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.536 158.679 151.704 1.00 17.54  ? 370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.563 159.896 151.871 1.00 33.17  ? 370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.287 157.844 152.410 1.00 16.19  ? 370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 113.977 157.689 150.031 1.00 21.31  ? 371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.070 157.301 148.958 1.00 19.55  ? 371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 112.947 158.377 147.888 1.00 23.30  ? 371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.602 158.059 146.745 1.00 29.21  ? 371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.688 156.973 149.523 1.00 16.85  ? 371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.607 155.568 150.077 1.00 24.35  ? 371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.369 154.688 149.683 1.00 23.31  ? 371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.676 155.349 150.998 1.00 20.11  ? 371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.211 159.639 148.232 1.00 26.18  ? 372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.180 160.702 147.233 1.00 25.84  ? 372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.283 160.515 146.199 1.00 30.18  ? 372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.066 160.743 145.003 1.00 35.09  ? 372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.301 162.065 147.911 1.00 28.56  ? 372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.639 162.311 148.537 1.00 32.34  ? 372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.141 161.525 149.550 1.00 28.14  ? 372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.580 163.252 148.287 1.00 34.67  ? 372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.334 161.971 149.900 1.00 28.10  ? 372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.623 163.020 149.150 1.00 36.31  ? 372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.476 160.115 146.644 1.00 25.33  ? 373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.563 159.829 145.712 1.00 26.78  ? 373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.196 158.649 144.826 1.00 32.20  ? 373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.268 158.724 143.593 1.00 38.72  ? 373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.868 159.565 146.486 1.00 25.35  ? 373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.246 160.793 147.312 1.00 26.33  ? 373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 118.989 159.184 145.536 1.00 27.07  ? 373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.245 160.510 148.399 1.00 24.28  ? 373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.772 157.548 145.447 1.00 23.79  ? 374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.334 156.346 144.752 1.00 15.72  ? 374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.828 155.327 145.763 1.00 23.95  ? 374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.252 155.336 146.923 1.00 31.03  ? 374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.470 155.742 143.925 1.00 22.31  ? 374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 116.332 154.337 143.820 1.00 19.44  ? 374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 113.924 154.452 145.342 1.00 31.11  ? 375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.580 153.308 146.167 1.00 18.61  ? 375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.717 152.294 146.139 1.00 23.99  ? 375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.512 152.247 145.197 1.00 36.13  ? 375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.283 152.661 145.680 1.00 24.35  ? 375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.098 153.608 145.616 1.00 24.56  ? 375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.514 153.840 146.996 1.00 33.75  ? 375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.219 154.627 146.924 1.00 29.08  ? 375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.081 153.855 147.495 1.00 23.76  ? 375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 114.795 151.481 147.186 1.00 22.61  ? 376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 115.797 150.423 147.248 1.00 21.54  ? 376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.275 149.246 146.433 1.00 24.43  ? 376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.373 148.528 146.867 1.00 29.69  ? 376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.101 150.011 148.691 1.00 15.52  ? 376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.215 148.986 148.715 1.00 19.66  ? 376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.474 151.226 149.519 1.00 12.06  ? 376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 115.840 149.050 145.244 1.00 23.06  ? 377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.346 148.036 144.326 1.00 17.33  ? 377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.045 146.694 144.475 1.00 19.00  ? 377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.557 145.699 143.929 1.00 28.91  ? 377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.493 148.520 142.881 1.00 25.97  ? 377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 114.786 149.831 142.600 1.00 24.55  ? 377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.576 150.673 141.620 1.00 23.44  ? 377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.223 152.139 141.752 1.00 23.60  ? 377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.187 153.002 141.016 1.00 23.05  ? 377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.162 146.639 145.193 1.00 15.43  ? 378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 117.914 145.400 145.345 1.00 8.81   ? 378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 118.934 145.583 146.460 1.00 15.26  ? 378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.197 146.701 146.912 1.00 26.17  ? 378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 118.595 144.986 144.036 1.00 13.86  ? 378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 119.744 145.866 143.632 1.00 13.29  ? 378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 119.550 147.210 143.360 1.00 19.64  ? 378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.018 145.343 143.510 1.00 11.09  ? 378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 120.603 148.013 142.985 1.00 13.19  ? 378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.073 146.143 143.135 1.00 14.78  ? 378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 121.864 147.479 142.871 1.00 17.36  ? 378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 119.504 144.466 146.898 1.00 17.11  ? 379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 120.480 144.430 147.973 1.00 8.87   ? 379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 121.843 144.018 147.423 1.00 11.27  ? 379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.034 143.878 146.210 1.00 22.35  ? 379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.008 143.486 149.080 1.00 16.63  ? 379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 120.529 143.884 150.334 1.00 21.20  ? 379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 122.800 143.828 148.325 1.00 8.91   ? 380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.156 143.466 147.948 1.00 12.28  ? 380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 124.299 141.945 147.905 1.00 23.32  ? 380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 123.320 141.200 147.994 1.00 26.39  ? 380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.159 144.097 148.910 1.00 11.55  ? 380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.097 143.491 150.294 1.00 15.20  ? 380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.029 143.392 150.892 1.00 28.43  ? 380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 126.249 143.085 150.813 1.00 20.35  ? 380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 125.538 141.473 147.764 1.00 24.17  ? 381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 125.808 140.042 147.756 1.00 19.11  ? 381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 125.495 139.388 149.096 1.00 19.95  ? 381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 125.204 138.188 149.133 1.00 24.66  ? 381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 127.271 139.803 147.372 1.00 19.49  ? 381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.854 138.391 147.433 1.00 28.11  ? 381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.156 137.473 146.449 1.00 27.11  ? 381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 129.347 138.433 147.165 1.00 23.31  ? 381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 125.533 140.148 150.189 1.00 24.51  ? 382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 125.210 139.636 151.512 1.00 7.27   ? 382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 123.826 140.065 151.983 1.00 11.70  ? 382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 123.470 139.810 153.137 1.00 25.57  ? 382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 126.269 140.083 152.522 1.00 22.55  ? 382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.932 139.453 152.189 1.00 31.07  ? 382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 123.045 140.709 151.114 1.00 14.95  ? 383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 121.657 141.081 151.395 1.00 12.55  ? 383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 121.536 141.918 152.668 1.00 18.56  ? 383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 120.651 141.702 153.497 1.00 26.95  ? 383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 120.761 139.845 151.475 1.00 21.46  ? 383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.133 139.010 152.554 1.00 25.76  ? 383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 122.436 142.889 152.826 1.00 17.35  ? 384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 122.374 143.805 153.957 1.00 8.36   ? 384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 122.566 145.265 153.581 1.00 18.96  ? 384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.382 146.129 154.445 1.00 33.65  ? 384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 123.419 143.427 155.019 1.00 12.97  ? 384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 124.691 142.812 154.466 1.00 19.13  ? 384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 125.749 143.843 154.152 1.00 24.58  ? 384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 125.611 144.993 154.615 1.00 28.16  ? 384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 126.719 143.506 153.442 1.00 27.97  ? 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 122.921 145.572 152.338 1.00 11.04  ? 385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.146 146.942 151.895 1.00 8.24   ? 385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 121.911 147.385 151.124 1.00 18.00  ? 385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 121.749 147.057 149.945 1.00 29.39  ? 385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.412 147.059 151.040 1.00 10.77  ? 385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.588 148.483 150.556 1.00 15.41  ? 385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 125.624 146.614 151.833 1.00 17.52  ? 385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.038 148.133 151.791 1.00 20.79  ? 386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 119.782 148.607 151.219 1.00 10.70  ? 386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 119.869 150.121 151.074 1.00 13.72  ? 386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.564 150.866 152.007 1.00 14.59  ? 386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 118.610 148.186 152.083 1.00 7.88   ? 386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 118.504 146.672 152.239 1.00 4.89   ? 386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 117.431 146.323 153.226 1.00 12.61  ? 386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.211 146.037 150.898 1.00 10.83  ? 386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.286 150.570 149.893 1.00 19.96  ? 387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.509 151.980 149.625 1.00 10.07  ? 387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 119.828 152.383 148.327 1.00 15.59  ? 387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.589 151.552 147.448 1.00 23.09  ? 387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.003 152.298 149.542 1.00 9.75   ? 387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.788 151.851 150.754 1.00 14.90  ? 387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.203 152.370 150.746 1.00 13.28  ? 387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.536 153.274 149.984 1.00 22.51  ? 387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.046 151.804 151.598 1.00 17.89  ? 387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.511 153.669 148.224 1.00 16.64  ? 388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 118.955 154.206 146.991 1.00 13.80  ? 388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.010 154.198 145.893 1.00 23.87  ? 388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.175 154.535 146.124 1.00 33.00  ? 388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.440 155.626 147.212 1.00 22.61  ? 388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.597 153.809 144.691 1.00 22.15  ? 389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.496 153.758 143.550 1.00 13.22  ? 389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.767 154.252 142.311 1.00 17.54  ? 389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.557 154.068 142.168 1.00 29.43  ? 389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 121.031 152.341 143.314 1.00 17.01  ? 389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.983 151.388 143.359 1.00 28.28  ? 389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.524 154.875 141.415 1.00 22.13  ? 390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.010 155.359 140.144 1.00 20.14  ? 390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.766 154.676 139.016 1.00 24.41  ? 390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 121.991 154.531 139.077 1.00 29.73  ? 390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.147 156.879 140.033 1.00 16.79  ? 390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.322 157.647 141.050 1.00 22.74  ? 390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.550 159.143 140.975 1.00 32.84  ? 390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.426 159.613 140.251 1.00 31.39  ? 390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.759 159.900 141.725 1.00 25.74  ? 390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.038 154.254 137.993 1.00 28.37  ? 391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.643 153.518 136.891 1.00 27.75  ? 391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.416 154.482 136.003 1.00 37.62  ? 391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.034 155.648 135.835 1.00 29.71  ? 391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.572 152.741 136.103 1.00 24.64  ? 391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.787 153.663 135.180 1.00 28.39  ? 391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.212 151.605 135.325 1.00 28.71  ? 391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.528 154.006 135.457 1.00 42.01  ? 392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.378 154.801 134.582 1.00 31.18  ? 392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.079 154.449 133.133 1.00 35.09  ? 392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 123.097 153.272 132.758 1.00 39.32  ? 392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.855 154.563 134.891 1.00 28.37  ? 392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.112 154.699 136.276 1.00 33.32  ? 392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 122.805 155.470 132.324 1.00 39.99  ? 393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.517 155.280 130.904 1.00 36.11  ? 393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 123.826 155.416 130.140 1.00 38.04  ? 393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.220 156.506 129.721 1.00 40.29  ? 393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.473 156.280 130.426 1.00 40.93  ? 393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 121.221 156.132 129.041 1.00 46.72  ? 393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.513 154.293 129.958 1.00 38.86  ? 394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 125.766 154.274 129.216 1.00 37.12  ? 394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.462 154.301 127.724 1.00 40.18  ? 394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 124.850 153.370 127.192 1.00 39.95  ? 394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.586 153.042 129.586 1.00 31.73  ? 394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.023 153.022 131.031 1.00 36.17  ? 394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.048 153.844 131.477 1.00 35.74  ? 394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.403 152.191 131.954 1.00 35.63  ? 394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.451 153.833 132.797 1.00 34.83  ? 394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 126.798 152.172 133.276 1.00 35.21  ? 394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 127.822 152.996 133.693 1.00 41.62  ? 394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.220 152.983 135.010 1.00 45.58  ? 394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 125.887 155.366 127.055 1.00 43.53  ? 395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.571 155.575 125.651 1.00 45.62  ? 395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.680 154.993 124.777 1.00 45.55  ? 395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.584 154.304 125.254 1.00 45.14  ? 395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.352 157.061 125.380 1.00 45.71  ? 395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.550 157.784 125.687 1.00 46.21  ? 395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.215 157.593 126.235 1.00 44.48  ? 395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.614 155.267 123.477 1.00 45.20  ? 396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.606 154.766 122.541 1.00 44.20  ? 396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 128.960 155.426 122.794 1.00 50.06  ? 396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.087 156.382 123.564 1.00 54.86  ? 396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.158 155.016 121.102 1.00 46.93  ? 396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 125.886 154.272 120.749 1.00 50.37  ? 396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 125.583 153.260 121.414 1.00 52.67  ? 396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.190 154.697 119.804 1.00 49.56  ? 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 129.987 154.892 122.137 1.00 42.51  ? 397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.311 155.487 122.224 1.00 41.52  ? 397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.300 156.887 121.619 1.00 47.07  ? 397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 130.548 157.176 120.683 1.00 48.39  ? 397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.339 154.605 121.513 1.00 43.37  ? 397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 133.764 154.844 121.954 1.00 45.41  ? 397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.527 155.856 121.388 1.00 44.38  ? 397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.346 154.058 122.939 1.00 44.84  ? 397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.828 156.077 121.788 1.00 45.61  ? 397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 135.648 154.271 123.344 1.00 41.26  ? 397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.384 155.282 122.765 1.00 46.09  ? 397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 137.681 155.500 123.167 1.00 46.38  ? 397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 132.131 157.763 122.182 1.00 51.64  ? 398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 132.197 159.185 121.853 1.00 54.24  ? 398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.907 159.921 122.192 1.00 57.14  ? 398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.731 161.076 121.785 1.00 54.79  ? 398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 132.559 159.414 120.377 1.00 54.63  ? 398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 134.053 159.372 120.131 1.00 59.12  ? 398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 134.760 160.287 120.606 1.00 56.88  ? 398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 134.522 158.428 119.462 1.00 57.12  ? 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 130.001 159.282 122.924 1.00 58.42  ? 399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.775 159.900 123.405 1.00 53.43  ? 399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.809 159.925 124.926 1.00 56.94  ? 399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.116 158.909 125.558 1.00 57.10  ? 399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.544 159.139 122.909 1.00 51.62  ? 399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.475 160.017 122.285 1.00 56.66  ? 399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.400 159.210 121.585 1.00 60.01  ? 399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.716 158.414 122.263 1.00 58.79  ? 399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.241 159.369 120.357 1.00 59.53  ? 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.505 161.083 125.507 1.00 54.52  ? 400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.566 161.230 126.955 1.00 50.80  ? 400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.534 160.333 127.626 1.00 52.29  ? 400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.366 160.303 127.227 1.00 54.48  ? 400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.338 162.689 127.349 1.00 51.68  ? 400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.216 163.675 126.599 1.00 54.03  ? 400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.693 163.425 126.820 1.00 57.12  ? 400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 131.103 163.265 127.989 1.00 54.39  ? 400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.446 163.387 125.824 1.00 55.08  ? 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 127.970 159.600 128.647 1.00 42.60  ? 401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.093 158.705 129.386 1.00 43.04  ? 401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.394 159.455 130.510 1.00 45.61  ? 401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 126.974 160.350 131.133 1.00 46.48  ? 401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 127.878 157.524 129.958 1.00 43.13  ? 401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.889 156.966 128.979 1.00 49.60  ? 401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.611 156.981 127.762 1.00 54.10  ? 401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 129.961 156.507 129.426 1.00 46.23  ? 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.142 159.085 130.764 1.00 40.80  ? 402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.376 159.633 131.882 1.00 39.75  ? 402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.685 158.785 133.107 1.00 33.57  ? 402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.081 157.731 133.319 1.00 37.94  ? 402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 122.884 159.650 131.565 1.00 43.01  ? 402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.489 160.598 130.440 1.00 41.89  ? 402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.807 160.047 129.062 1.00 45.97  ? 402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.441 158.886 128.784 1.00 46.74  ? 402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.423 160.777 128.257 1.00 42.77  ? 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.632 159.245 133.917 1.00 31.08  ? 403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.109 158.471 135.058 1.00 32.08  ? 403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.128 158.620 136.212 1.00 34.89  ? 403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.775 159.740 136.605 1.00 31.01  ? 403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.520 158.920 135.466 1.00 26.52  ? 403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.510 158.674 134.325 1.00 30.09  ? 403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 127.966 158.198 136.720 1.00 28.97  ? 403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.413 157.296 133.715 1.00 31.79  ? 403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.684 157.495 136.754 1.00 29.94  ? 404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.800 157.452 137.896 1.00 18.24  ? 404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.542 157.158 139.182 1.00 25.52  ? 404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.738 157.437 139.316 1.00 38.20  ? 404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.825 156.587 140.144 1.00 27.39  ? 405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.382 156.243 141.445 1.00 12.68  ? 405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.401 154.729 141.596 1.00 19.63  ? 405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.348 154.084 141.546 1.00 24.67  ? 405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.573 156.880 142.574 1.00 17.11  ? 405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.409 158.400 142.548 1.00 20.49  ? 405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.399 158.839 143.593 1.00 23.71  ? 405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.741 159.089 142.770 1.00 20.38  ? 405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.591 154.168 141.786 1.00 32.25  ? 406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.760 152.758 142.098 1.00 21.68  ? 406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.338 152.630 143.497 1.00 28.25  ? 406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.336 153.277 143.829 1.00 32.96  ? 406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.666 152.058 141.083 1.00 28.32  ? 406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 125.952 151.743 139.782 1.00 37.83  ? 406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 124.753 152.072 139.663 1.00 37.42  ? 406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.592 151.168 138.878 1.00 34.90  ? 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.720 151.783 144.305 1.00 31.37  ? 407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 125.993 151.747 145.735 1.00 24.39  ? 407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.379 151.178 145.999 1.00 18.19  ? 407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.741 150.106 145.500 1.00 26.54  ? 407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.912 150.932 146.462 1.00 17.93  ? 407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.534 151.554 146.232 1.00 14.84  ? 407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.234 150.828 147.935 1.00 22.19  ? 407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.419 150.548 146.169 1.00 19.30  ? 407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.161 151.910 146.787 1.00 32.57  ? 408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.414 151.431 147.348 1.00 34.60  ? 408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.291 151.440 148.864 1.00 37.54  ? 408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 128.943 152.465 149.460 1.00 46.71  ? 408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.595 152.297 146.906 1.00 36.97  ? 408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 130.800 152.204 145.508 1.00 39.20  ? 408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.573 150.300 149.483 1.00 37.30  ? 409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.341 150.096 150.907 1.00 38.77  ? 409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.659 149.866 151.636 1.00 40.25  ? 409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.332 148.855 151.410 1.00 36.56  ? 409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.368 148.936 151.124 1.00 37.64  ? 409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.400 147.690 149.812 1.00 49.87  ? 409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.009 150.805 152.514 1.00 30.79  ? 410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.191 150.714 153.367 1.00 29.29  ? 410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 131.727 150.173 154.714 1.00 31.32  ? 410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 130.985 150.839 155.439 1.00 37.55  ? 410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 132.865 152.075 153.510 1.00 30.14  ? 410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 132.841 152.874 152.222 1.00 37.42  ? 410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 133.707 152.715 151.364 1.00 40.25  ? 410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 131.843 153.737 152.080 1.00 34.74  ? 410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.168 148.967 155.050 1.00 23.03  ? 411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 131.614 148.231 156.175 1.00 16.62  ? 411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 132.508 148.333 157.403 1.00 23.64  ? 411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 133.726 148.507 157.302 1.00 32.59  ? 411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 131.410 146.759 155.809 1.00 22.74  ? 411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 130.632 146.460 154.525 1.00 30.68  ? 411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 130.219 145.001 154.486 1.00 26.93  ? 411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 129.415 147.360 154.400 1.00 25.81  ? 411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 131.880 148.232 158.568 1.00 28.46  ? 412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 132.596 148.190 159.828 1.00 19.38  ? 412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 131.703 147.599 160.890 1.00 21.06  ? 412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 130.487 147.812 160.886 1.00 39.64  ? 412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 132.306 146.853 161.810 1.00 19.48  ? 413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 131.556 146.067 162.777 1.00 14.70  ? 413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 131.918 146.465 164.199 1.00 17.65  ? 413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 133.097 146.607 164.538 1.00 28.39  ? 413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 131.813 144.573 162.583 1.00 22.51  ? 413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.436 144.166 161.283 1.00 34.92  ? 413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 130.892 146.640 165.027 1.00 22.04  ? 414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 131.067 146.811 166.461 1.00 17.72  ? 414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 131.023 145.450 167.140 1.00 28.22  ? 414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 130.144 144.632 166.849 1.00 37.72  ? 414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 129.980 147.714 167.042 1.00 26.92  ? 414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 129.761 149.078 166.399 1.00 34.59  ? 414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.700 149.837 167.166 1.00 31.27  ? 414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.061 149.859 166.377 1.00 35.66  ? 414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 131.968 145.210 168.041 1.00 34.04  ? 415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 131.948 144.019 168.885 1.00 31.50  ? 415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 131.084 144.349 170.094 1.00 29.72  ? 415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 131.514 145.066 171.000 1.00 30.04  ? 415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 133.360 143.614 169.284 1.00 25.96  ? 415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 133.448 142.179 169.759 1.00 32.15  ? 415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 132.544 141.678 170.424 1.00 36.96  ? 415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 134.541 141.510 169.419 1.00 37.23  ? 415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 129.855 143.828 170.100 1.00 26.49  ? 416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 128.888 144.195 171.131 1.00 28.05  ? 416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 129.410 143.827 172.514 1.00 28.38  ? 416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 129.240 144.583 173.478 1.00 31.45  ? 416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 127.525 143.539 170.838 1.00 26.98  ? 416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 126.913 144.149 169.577 1.00 21.22  ? 416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 126.586 143.705 172.014 1.00 24.41  ? 416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 125.721 143.396 169.045 1.00 24.11  ? 416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 130.067 142.672 172.631 1.00 28.12  ? 417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 130.637 142.268 173.913 1.00 30.47  ? 417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 131.667 143.281 174.402 1.00 33.85  ? 417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 131.606 143.744 175.547 1.00 40.06  ? 417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 131.265 140.882 173.788 1.00 29.18  ? 417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 131.942 140.298 175.029 1.00 32.44  ? 417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 131.035 140.379 176.245 1.00 32.25  ? 417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 132.372 138.867 174.771 1.00 36.21  ? 417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 132.611 143.651 173.536 1.00 41.72  ? 418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 133.671 144.570 173.933 1.00 33.36  ? 418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 133.173 146.003 174.060 1.00 36.16  ? 418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 133.670 146.751 174.909 1.00 42.02  ? 418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 134.825 144.495 172.935 1.00 33.41  ? 418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 135.554 143.169 172.991 1.00 41.63  ? 418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 135.742 142.598 174.063 1.00 44.34  ? 418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 135.961 142.669 171.832 1.00 41.68  ? 418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 132.211 146.403 173.230 1.00 39.61  ? 419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 131.632 147.738 173.352 1.00 34.20  ? 419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 130.882 147.874 174.671 1.00 36.75  ? 419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 130.991 148.891 175.365 1.00 40.19  ? 419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 130.720 148.035 172.145 1.00 28.76  ? 419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 129.822 149.217 172.434 1.00 37.07  ? 419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 131.553 148.293 170.908 1.00 28.26  ? 419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 130.119 146.845 175.044 1.00 38.50  ? 420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 129.319 146.903 176.261 1.00 35.79  ? 420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 130.178 146.753 177.510 1.00 37.17  ? 420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 129.910 147.400 178.528 1.00 37.00  ? 420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 128.239 145.821 176.219 1.00 31.85  ? 420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.070 146.143 175.300 1.00 29.38  ? 420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 125.983 147.440 175.918 1.00 41.20  ? 420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.004 147.095 177.674 1.00 39.06  ? 420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 131.211 145.906 177.458 1.00 44.87  ? 421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 132.075 145.732 178.622 1.00 45.40  ? 421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 132.882 146.990 178.918 1.00 46.80  ? 421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 133.224 147.244 180.079 1.00 48.26  ? 421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.000 144.531 178.420 1.00 42.42  ? 421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 134.172 144.784 177.491 1.00 49.63  ? 421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 135.425 144.041 177.907 1.00 52.02  ? 421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 135.901 144.263 179.040 1.00 50.81  ? 421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.933 143.234 177.100 1.00 49.58  ? 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 133.198 147.782 177.896 1.00 42.07  ? 422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 133.907 149.039 178.087 1.00 46.51  ? 422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 132.977 150.212 178.361 1.00 51.34  ? 422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 133.465 151.307 178.657 1.00 46.61  ? 422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 134.771 149.355 176.862 1.00 41.59  ? 422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 135.965 148.464 176.717 1.00 45.93  ? 422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 135.941 147.302 175.979 1.00 47.18  ? 422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 137.220 148.569 177.214 1.00 45.68  ? 422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 137.130 146.727 176.029 1.00 47.37  ? 422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 137.924 147.476 176.771 1.00 48.55  ? 422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 131.662 150.005 178.277 1.00 53.67  ? 423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 130.674 151.068 178.459 1.00 51.33  ? 423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 130.978 152.250 177.544 1.00 53.43  ? 423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 130.950 153.414 177.951 1.00 55.71  ? 423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 130.602 151.505 179.923 1.00 51.17  ? 423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 129.682 150.653 180.779 1.00 53.77  ? 423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 130.276 150.417 182.158 1.00 53.77  ? 423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 131.688 149.864 182.061 1.00 56.89  ? 423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 131.697 148.380 181.934 1.00 50.35  ? 423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.274 151.937 176.286 1.00 42.91  ? 424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 131.759 152.912 175.317 1.00 43.08  ? 424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 130.982 152.811 174.014 1.00 41.69  ? 424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 131.558 152.731 172.929 1.00 40.10  ? 424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.249 152.723 175.058 1.00 43.18  ? 424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 133.479 151.593 174.235 1.00 42.59  ? 424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 129.651 152.801 174.100 1.00 42.73  ? 425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 128.840 152.794 172.885 1.00 33.79  ? 425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.056 154.080 172.098 1.00 38.49  ? 425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.298 154.053 170.886 1.00 45.38  ? 425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.353 152.585 173.224 1.00 35.58  ? 425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.098 151.144 173.663 1.00 40.41  ? 425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.479 152.931 172.028 1.00 32.16  ? 425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 125.655 150.861 174.001 1.00 43.83  ? 425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 128.997 155.225 172.781 1.00 33.86  ? 426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.068 156.509 172.088 1.00 26.46  ? 426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.413 156.700 171.401 1.00 34.49  ? 426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.474 156.995 170.201 1.00 45.72  ? 426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.806 157.646 173.074 1.00 32.33  ? 426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.062 159.029 172.505 1.00 37.33  ? 426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 128.670 160.134 173.463 1.00 44.49  ? 426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.418 159.833 174.648 1.00 40.82  ? 426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 128.612 161.305 173.031 1.00 40.72  ? 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.505 156.533 172.149 1.00 38.42  ? 427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 132.830 156.762 171.586 1.00 29.91  ? 427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.147 155.761 170.484 1.00 30.01  ? 427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.701 156.135 169.444 1.00 36.19  ? 427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 133.893 156.713 172.686 1.00 35.99  ? 427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 133.470 157.343 174.010 1.00 42.79  ? 427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.874 156.323 174.966 1.00 42.21  ? 427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 131.935 156.983 175.962 1.00 42.91  ? 427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 130.987 156.002 176.559 1.00 39.10  ? 427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 132.798 154.488 170.686 1.00 30.89  ? 428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.054 153.490 169.653 1.00 25.61  ? 428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.268 153.792 168.387 1.00 31.49  ? 428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 132.816 153.726 167.282 1.00 35.05  ? 428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 132.715 152.090 170.161 1.00 27.52  ? 428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 133.381 151.858 171.407 1.00 32.82  ? 428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.154 151.043 169.154 1.00 30.54  ? 428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 130.986 154.134 168.525 1.00 32.55  ? 429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.167 154.412 167.348 1.00 28.37  ? 429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 130.691 155.637 166.610 1.00 32.19  ? 429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 130.777 155.643 165.377 1.00 34.11  ? 429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 128.688 154.574 167.746 1.00 28.89  ? 429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 127.895 155.149 166.592 1.00 32.20  ? 429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.104 153.237 168.153 1.00 31.31  ? 429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.071 156.683 167.348 1.00 34.24  ? 430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.552 157.897 166.694 1.00 33.47  ? 430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 132.896 157.673 166.009 1.00 32.31  ? 430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.105 158.129 164.877 1.00 39.31  ? 430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.636 159.036 167.708 1.00 29.19  ? 430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.279 159.471 168.233 1.00 29.77  ? 430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.324 160.863 168.831 1.00 32.53  ? 430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.922 161.397 169.062 1.00 36.93  ? 430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.933 162.792 169.579 1.00 37.27  ? 430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 133.820 156.969 166.669 1.00 26.11  ? 431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.109 156.685 166.048 1.00 25.16  ? 431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 134.952 155.781 164.833 1.00 31.92  ? 431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 135.637 155.968 163.820 1.00 39.05  ? 431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.055 156.056 167.068 1.00 32.59  ? 431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 136.876 157.016 167.929 1.00 36.31  ? 431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 137.581 156.256 169.037 1.00 31.12  ? 431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 137.875 157.777 167.076 1.00 34.49  ? 431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.058 154.793 164.912 1.00 29.88  ? 432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 133.801 153.928 163.767 1.00 24.72  ? 432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.185 154.708 162.614 1.00 27.79  ? 432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.519 154.468 161.449 1.00 33.22  ? 432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 132.893 152.776 164.183 1.00 30.06  ? 432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.279 155.638 162.918 1.00 34.44  ? 433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 131.709 156.486 161.877 1.00 31.07  ? 433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 132.785 157.338 161.217 1.00 32.95  ? 433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 132.800 157.491 159.992 1.00 39.25  ? 433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 130.611 157.369 162.467 1.00 30.05  ? 433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.708 156.563 163.233 1.00 36.91  ? 433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 129.841 158.078 161.366 1.00 28.14  ? 433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 133.699 157.894 162.016 1.00 28.62  ? 434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 134.796 158.676 161.451 1.00 26.22  ? 434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.696 157.816 160.570 1.00 28.39  ? 434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.117 158.246 159.489 1.00 36.35  ? 434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.608 159.326 162.570 1.00 30.60  ? 434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 134.856 160.438 163.265 1.00 37.53  ? 434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 133.933 161.007 162.648 1.00 42.25  ? 434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.190 160.747 164.428 1.00 34.17  ? 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.006 156.597 161.017 1.00 30.37  ? 435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 136.855 155.709 160.229 1.00 24.42  ? 435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.183 155.317 158.919 1.00 30.21  ? 435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 136.832 155.271 157.867 1.00 37.94  ? 435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.208 154.465 161.041 1.00 27.08  ? 435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.086 153.615 161.185 1.00 32.00  ? 435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 134.882 155.027 158.962 1.00 28.51  ? 436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.157 154.686 157.742 1.00 20.60  ? 436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.060 155.882 156.804 1.00 27.38  ? 436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.124 155.724 155.580 1.00 36.89  ? 436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 132.769 154.157 158.092 1.00 28.23  ? 436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 132.736 152.819 158.830 1.00 28.16  ? 436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.351 152.551 159.389 1.00 26.41  ? 436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.167 151.702 157.904 1.00 28.32  ? 436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 133.903 157.086 157.358 1.00 25.41  ? 437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 133.923 158.289 156.535 1.00 22.68  ? 437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.271 158.460 155.851 1.00 27.02  ? 437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.338 158.810 154.667 1.00 39.23  ? 437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.598 159.512 157.392 1.00 25.28  ? 437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.358 159.302 158.077 1.00 27.48  ? 437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.492 160.756 156.531 1.00 29.34  ? 437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.359 158.210 156.583 1.00 28.14  ? 438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.687 158.280 155.982 1.00 28.85  ? 438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 137.852 157.244 154.879 1.00 28.23  ? 438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.424 157.535 153.823 1.00 40.34  ? 438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.758 158.089 157.054 1.00 34.86  ? 438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.155 158.116 156.520 1.00 38.67  ? 438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 140.802 159.285 156.186 1.00 34.14  ? 438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.026 157.115 156.252 1.00 38.06  ? 438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.013 159.004 155.741 1.00 36.07  ? 438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.174 157.694 155.770 1.00 38.92  ? 438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.365 156.024 155.110 1.00 30.86  ? 439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.465 154.975 154.097 1.00 30.12  ? 439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.686 155.364 152.848 1.00 34.69  ? 439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.155 155.173 151.720 1.00 41.79  ? 439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 136.982 153.631 154.670 1.00 28.05  ? 439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 136.818 152.605 153.562 1.00 26.28  ? 439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 137.953 153.129 155.713 1.00 32.21  ? 439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.483 155.913 153.029 1.00 29.37  ? 440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.688 156.353 151.888 1.00 30.99  ? 440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.378 157.486 151.136 1.00 35.99  ? 440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.357 157.523 149.901 1.00 39.53  ? 440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.298 156.785 152.355 1.00 33.98  ? 440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.453 157.064 151.253 1.00 35.95  ? 440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 135.990 158.422 151.867 1.00 36.70  ? 441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.630 159.564 151.221 1.00 33.11  ? 441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.870 159.146 150.441 1.00 36.60  ? 441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.050 159.554 149.288 1.00 41.94  ? 441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 136.989 160.619 152.265 1.00 28.32  ? 441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 135.814 161.452 152.737 1.00 34.31  ? 441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 136.126 162.223 154.002 1.00 41.47  ? 441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 137.297 162.207 154.436 1.00 45.41  ? 441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 135.202 162.848 154.564 1.00 37.55  ? 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.739 158.338 151.050 1.00 38.55  ? 442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 139.972 157.929 150.386 1.00 39.14  ? 442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.740 156.935 149.259 1.00 40.24  ? 442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.667 156.682 148.482 1.00 43.70  ? 442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 140.949 157.328 151.398 1.00 37.69  ? 442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.383 156.141 151.966 1.00 36.96  ? 442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.252 158.325 152.498 1.00 38.75  ? 442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.544 156.369 149.146 1.00 37.94  ? 443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.249 155.391 148.109 1.00 44.91  ? 443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 137.778 156.102 146.849 1.00 40.28  ? 443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 136.757 156.797 146.865 1.00 43.05  ? 443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.187 154.397 148.576 1.00 44.50  ? 443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.665 153.683 149.723 1.00 49.29  ? 443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.868 153.417 147.464 1.00 33.93  ? 443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.524 155.930 145.762 1.00 47.29  ? 444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.086 156.337 144.434 1.00 50.83  ? 444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.218 155.151 143.490 1.00 50.27  ? 444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 139.129 154.332 143.638 1.00 49.72  ? 444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 138.849 157.582 143.939 1.00 52.15  ? 444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 140.307 157.311 143.558 1.00 56.09  ? 444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 140.832 156.200 143.763 1.00 50.17  ? 444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 140.944 158.249 143.033 1.00 56.55  ? 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.266 155.016 142.576 1.00 42.60  ? 445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.245 153.917 141.621 1.00 45.41  ? 445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.054 154.542 140.246 1.00 47.23  ? 445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 135.971 155.038 139.915 1.00 46.66  ? 445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.151 152.895 141.948 1.00 40.48  ? 445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.583 152.028 143.130 1.00 37.07  ? 445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 135.887 152.001 140.754 1.00 43.09  ? 445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.534 151.899 144.208 1.00 39.77  ? 445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.119 154.536 139.445 1.00 53.09  ? 446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.101 155.219 138.159 1.00 56.74  ? 446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 137.331 154.456 137.091 1.00 55.21  ? 446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 136.806 155.082 136.164 1.00 51.84  ? 446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 139.533 155.474 137.680 1.00 52.39  ? 446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 140.520 155.805 138.793 1.00 52.84  ? 446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 140.064 157.008 139.619 1.00 52.70  ? 446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 140.536 158.284 139.090 1.00 53.29  ? 446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 141.810 158.640 138.987 1.00 57.10  ? 446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 142.111 159.824 138.458 1.00 56.30  ? 446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 142.788 157.855 139.410 1.00 55.97  ? 446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.245 153.133 137.197 1.00 44.99  ? 447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.611 152.322 136.166 1.00 41.65  ? 447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.117 152.124 136.387 1.00 43.70  ? 447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.459 151.518 135.536 1.00 47.65  ? 447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.301 150.960 136.076 1.00 38.92  ? 447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.351 150.913 134.987 1.00 41.12  ? 447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.039 151.029 133.803 1.00 47.68  ? 447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.607 150.747 135.383 1.00 37.25  ? 447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.571 152.612 137.498 1.00 40.58  ? 448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.133 152.559 137.761 1.00 36.72  ? 448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.632 153.973 138.006 1.00 37.23  ? 448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.674 154.461 139.149 1.00 38.69  ? 448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 132.823 151.662 138.956 1.00 34.31  ? 448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.163 154.675 136.971 1.00 37.38  ? 449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 131.755 156.076 137.165 1.00 34.33  ? 449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.615 156.242 138.151 1.00 36.97  ? 449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.602 157.204 138.927 1.00 35.75  ? 449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.350 156.525 135.752 1.00 33.75  ? 449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.712 155.392 134.836 1.00 40.06  ? 449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 131.766 154.160 135.654 1.00 36.55  ? 449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.656 155.315 138.148 1.00 39.52  ? 450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.502 155.439 139.028 1.00 28.46  ? 450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 128.861 155.111 140.471 1.00 32.11  ? 450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.382 155.776 141.395 1.00 31.65  ? 450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.372 154.541 138.536 1.00 29.50  ? 450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.703 154.098 140.682 1.00 36.08  ? 451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.163 153.781 142.032 1.00 31.08  ? 451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 130.934 154.960 142.612 1.00 29.76  ? 451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.729 155.352 143.767 1.00 37.04  ? 451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.013 152.498 142.024 1.00 28.82  ? 451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 131.866 152.410 143.278 1.00 29.97  ? 451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.124 151.273 141.898 1.00 29.11  ? 451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.822 155.552 141.811 1.00 32.44  ? 452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.591 156.707 142.264 1.00 32.59  ? 452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.689 157.903 142.547 1.00 30.52  ? 452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.854 158.590 143.565 1.00 36.93  ? 452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.645 157.056 141.213 1.00 31.99  ? 452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.582 158.182 141.591 1.00 37.92  ? 452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.007 158.961 140.360 1.00 33.31  ? 452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 136.398 159.390 140.436 1.00 40.13  ? 452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 136.798 160.652 140.355 1.00 39.63  ? 452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 138.096 160.928 140.453 1.00 37.38  ? 452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 135.937 161.640 140.175 1.00 40.15  ? 452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.724 158.163 141.661 1.00 33.86  ? 453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.815 159.285 141.858 1.00 27.26  ? 453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 128.983 159.109 143.120 1.00 29.04  ? 453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.809 160.058 143.895 1.00 33.07  ? 453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 128.912 159.443 140.635 1.00 28.31  ? 453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.722 160.355 140.855 1.00 28.97  ? 453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.044 160.705 139.543 1.00 27.40  ? 453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.597 160.557 139.625 1.00 26.77  ? 453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.779 161.469 140.128 1.00 31.47  ? 453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 123.471 161.230 140.144 1.00 29.14  ? 453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 125.233 162.613 140.615 1.00 31.59  ? 453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.471 157.898 143.354 1.00 29.75  ? 454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.673 157.653 144.547 1.00 25.40  ? 454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.524 157.664 145.807 1.00 29.47  ? 454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.041 158.058 146.870 1.00 36.22  ? 454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 126.926 156.328 144.421 1.00 28.10  ? 454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.785 157.237 145.719 1.00 30.65  ? 455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.669 157.343 146.873 1.00 25.66  ? 455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.927 158.799 147.231 1.00 33.19  ? 455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.951 159.159 148.415 1.00 37.27  ? 455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 131.983 156.615 146.597 1.00 28.24  ? 455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.854 156.500 147.831 1.00 36.72  ? 455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.502 155.817 148.791 1.00 39.55  ? 455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 133.997 157.174 147.812 1.00 33.88  ? 455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.121 159.654 146.224 1.00 40.13  ? 456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.380 161.063 146.505 1.00 33.00  ? 456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.128 161.778 147.001 1.00 39.21  ? 456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.210 162.630 147.894 1.00 43.80  ? 456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.934 161.761 145.265 1.00 30.06  ? 456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 133.450 161.785 145.198 1.00 39.82  ? 456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 133.940 162.194 143.821 1.00 43.24  ? 456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 135.038 161.268 143.337 1.00 42.02  ? 456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 135.930 160.829 144.444 1.00 37.25  ? 456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.964 161.451 146.442 1.00 32.63  ? 457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.747 162.192 146.753 1.00 28.89  ? 457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.021 161.642 147.977 1.00 33.18  ? 457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.686 162.397 148.894 1.00 34.48  ? 457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.811 162.186 145.541 1.00 31.49  ? 457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.765 160.334 147.999 1.00 37.87  ? 458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 125.966 159.746 149.068 1.00 26.88  ? 458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.748 159.668 150.370 1.00 31.54  ? 458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.183 159.866 151.451 1.00 39.20  ? 458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.490 158.354 148.653 1.00 24.30  ? 458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.687 158.336 147.367 1.00 31.69  ? 458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 122.911 158.387 147.636 1.00 45.24  ? 458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.659 160.158 147.636 1.00 33.96  ? 458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.046 159.364 150.288 1.00 29.12  ? 459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 128.900 159.196 151.463 1.00 26.23  ? 459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.332 158.155 152.422 1.00 28.94  ? 459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.483 158.267 153.641 1.00 34.26  ? 459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.124 160.527 152.186 1.00 26.55  ? 459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.637 161.638 151.289 1.00 29.74  ? 459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.092 162.988 151.718 1.00 33.93  ? 459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.530 164.085 150.766 1.00 34.70  ? 459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.975 165.410 151.150 1.00 36.91  ? 459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.673 157.139 151.876 1.00 28.36  ? 460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.043 156.112 152.691 1.00 20.90  ? 460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.087 155.167 153.267 1.00 19.17  ? 460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.012 154.738 152.572 1.00 27.16  ? 460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.031 155.323 151.864 1.00 21.87  ? 460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.679 154.622 150.820 1.00 25.42  ? 460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 127.929 154.842 154.548 1.00 17.93  ? 461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 128.822 153.932 155.246 1.00 19.70  ? 461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 127.989 152.826 155.877 1.00 23.81  ? 461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 126.772 152.938 156.026 1.00 33.46  ? 461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.665 154.649 156.320 1.00 18.02  ? 461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 128.760 155.185 157.428 1.00 13.22  ? 461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 130.481 155.769 155.696 1.00 23.32  ? 461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.505 155.744 158.606 1.00 17.63  ? 461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.663 151.738 156.233 1.00 17.59  ? 462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 127.994 150.657 156.924 1.00 11.11  ? 462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 128.632 150.329 158.255 1.00 15.33  ? 462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 129.754 149.818 158.303 1.00 37.63  ? 462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 127.929 150.612 159.345 1.00 14.66  ? 463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 128.411 150.316 160.690 1.00 18.14  ? 463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 127.579 149.163 161.242 1.00 27.14  ? 463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 126.470 149.367 161.742 1.00 35.99  ? 463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.332 151.546 161.588 1.00 23.35  ? 463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 128.882 151.334 162.998 1.00 20.93  ? 463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.266 150.723 162.922 1.00 15.50  ? 463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 128.914 152.642 163.767 1.00 23.79  ? 463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.122 147.952 161.147 1.00 26.76  ? 464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 127.450 146.767 161.630 1.00 18.51  ? 464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 127.753 146.483 163.087 1.00 13.10  ? 464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 128.373 147.274 163.799 1.00 20.16  ? 464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 127.295 145.316 163.530 1.00 17.22  ? 465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 127.534 144.863 164.888 1.00 13.84  ? 465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 127.667 143.350 164.875 1.00 20.12  ? 465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 127.164 142.669 163.979 1.00 37.09  ? 465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 126.416 145.300 165.838 1.00 19.79  ? 465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 128.355 142.830 165.886 1.00 24.22  ? 466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.598 141.400 165.991 1.00 30.55  ? 466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.760 141.036 167.458 1.00 27.50  ? 466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 128.795 141.902 168.334 1.00 36.39  ? 466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.821 140.989 165.170 1.00 33.13  ? 466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 131.097 141.686 165.585 1.00 31.44  ? 466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.480 141.296 164.502 1.00 47.91  ? 466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 133.826 141.994 165.443 1.00 27.13  ? 466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.854 139.730 167.713 1.00 21.80  ? 467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.936 139.182 169.068 1.00 26.61  ? 467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 127.694 139.509 169.890 1.00 29.92  ? 467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 127.772 139.670 171.110 1.00 37.24  ? 467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 130.194 139.661 169.797 1.00 27.98  ? 467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.855 138.563 170.600 1.00 34.20  ? 467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 130.377 137.430 170.634 1.00 39.70  ? 467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.968 138.889 171.244 1.00 36.60  ? 467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 126.541 139.625 169.230 1.00 23.50  ? 468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 125.292 139.777 169.966 1.00 22.33  ? 468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 124.984 138.525 170.776 1.00 30.65  ? 468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.762 138.594 171.990 1.00 37.52  ? 468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 124.146 140.084 169.002 1.00 26.24  ? 468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.755 140.103 169.633 1.00 19.82  ? 468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 122.611 141.277 170.584 1.00 27.19  ? 468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 121.682 140.138 168.564 1.00 21.50  ? 468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 124.992 137.362 170.119 1.00 31.28  ? 469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 124.708 136.117 170.821 1.00 21.41  ? 469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 125.795 135.802 171.838 1.00 31.79  ? 469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 125.504 135.291 172.924 1.00 44.37  ? 469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 124.550 134.969 169.826 1.00 27.68  ? 469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 123.998 133.716 170.435 1.00 29.86  ? 469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 123.938 132.522 169.752 1.00 32.51  ? 469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 123.479 133.475 171.662 1.00 31.01  ? 469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 123.408 131.597 170.533 1.00 29.64  ? 469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 123.121 132.149 171.697 1.00 30.58  ? 469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 127.052 136.095 171.505 1.00 31.57  ? 470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 128.124 135.885 172.465 1.00 25.75  ? 470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 127.965 136.739 173.707 1.00 27.59  ? 470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.142 136.258 174.830 1.00 40.97  ? 470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 127.619 138.016 173.525 1.00 24.95  ? 471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 127.396 138.890 174.672 1.00 28.73  ? 471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.211 138.415 175.502 1.00 37.08  ? 471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 126.267 138.418 176.737 1.00 42.74  ? 471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 127.172 140.328 174.210 1.00 26.87  ? 471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 126.827 141.274 175.337 1.00 30.29  ? 471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 127.809 141.739 176.200 1.00 35.31  ? 471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 125.521 141.685 175.554 1.00 27.46  ? 471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.502 142.596 177.236 1.00 34.23  ? 471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 125.205 142.538 176.591 1.00 27.93  ? 471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.199 142.993 177.426 1.00 37.15  ? 471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.887 143.847 178.459 1.00 41.17  ? 471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.123 138.014 174.840 1.00 32.78  ? 472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 123.937 137.572 175.566 1.00 28.79  ? 472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 124.211 136.295 176.351 1.00 32.32  ? 472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 123.810 136.172 177.515 1.00 39.79  ? 472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 122.775 137.369 174.594 1.00 34.55  ? 472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 122.271 138.619 173.874 1.00 32.53  ? 472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 121.392 138.230 172.702 1.00 28.24  ? 472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 121.525 139.532 174.833 1.00 29.02  ? 472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 124.893 135.330 175.731 1.00 28.81  ? 473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 125.174 134.070 176.407 1.00 30.72  ? 473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 126.183 134.257 177.532 1.00 41.27  ? 473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.065 133.624 178.589 1.00 47.22  ? 473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 125.674 133.038 175.398 1.00 29.63  ? 473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.182 135.118 177.329 1.00 36.12  ? 474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.141 135.399 178.387 1.00 34.47  ? 474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 127.549 136.248 179.503 1.00 37.19  ? 474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.193 136.409 180.545 1.00 40.93  ? 474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 129.376 136.085 177.801 1.00 33.07  ? 474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 130.340 135.119 177.133 1.00 34.42  ? 474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 131.496 135.820 176.454 1.00 41.51  ? 474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 132.304 136.482 177.104 1.00 40.97  ? 474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 131.585 135.672 175.139 1.00 43.79  ? 474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 126.349 136.792 179.309 1.00 40.59  ? 475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 125.625 137.510 180.347 1.00 41.58  ? 475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 124.421 136.729 180.854 1.00 39.74  ? 475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 123.586 137.289 181.573 1.00 40.54  ? 475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.187 138.881 179.832 1.00 35.62  ? 475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.321 139.881 179.814 1.00 37.13  ? 475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 126.497 140.656 180.754 1.00 44.22  ? 475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.111 139.857 178.750 1.00 35.80  ? 475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.311 135.454 180.497 1.00 30.70  ? 476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.185 134.639 180.916 1.00 35.59  ? 476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 121.858 135.051 180.318 1.00 39.80  ? 476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 120.835 135.028 181.015 1.00 40.38  ? 476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 121.846 135.431 179.043 1.00 34.24  ? 477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 120.632 135.839 178.347 1.00 32.54  ? 477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 120.447 134.928 177.143 1.00 38.23  ? 477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.340 134.825 176.293 1.00 37.91  ? 477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 120.688 137.313 177.915 1.00 31.43  ? 477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 120.999 138.210 179.113 1.00 38.15  ? 477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.377 137.726 177.279 1.00 33.89  ? 477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.475 139.591 178.732 1.00 40.62  ? 477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 119.295 134.268 177.072 1.00 41.20  ? 478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 118.980 133.439 175.917 1.00 36.79  ? 478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 118.647 134.315 174.718 1.00 39.30  ? 478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 117.907 135.294 174.834 1.00 39.59  ? 478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 117.813 132.506 176.232 1.00 30.76  ? 478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 119.196 133.951 173.556 1.00 35.61  ? 479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.023 134.765 172.356 1.00 31.95  ? 479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 117.554 134.916 171.980 1.00 38.11  ? 479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.153 135.959 171.452 1.00 36.33  ? 479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 119.816 134.154 171.200 1.00 28.15  ? 479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 119.788 134.943 169.909 1.00 29.75  ? 479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 118.788 134.741 168.967 1.00 34.10  ? 479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 120.774 135.877 169.627 1.00 26.99  ? 479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 118.764 135.457 167.787 1.00 32.73  ? 479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 120.758 136.597 168.449 1.00 31.98  ? 479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 119.751 136.382 167.533 1.00 34.63  ? 479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 119.731 137.097 166.358 1.00 34.74  ? 479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 116.737 133.895 172.243 1.00 43.77  ? 480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 115.311 133.963 171.950 1.00 38.30  ? 480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 114.502 134.609 173.066 1.00 41.95  ? 480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 113.305 134.850 172.876 1.00 48.08  ? 480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 114.759 132.564 171.680 1.00 40.73  ? 480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 115.480 131.799 170.590 1.00 41.77  ? 480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 115.096 130.334 170.568 1.00 49.24  ? 480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 115.539 129.590 171.466 1.00 49.86  ? 480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 114.343 129.930 169.660 1.00 47.01  ? 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.113 134.888 174.213 1.00 38.16  ? 481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 114.372 135.434 175.336 1.00 38.61  ? 481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 113.956 136.878 175.054 1.00 43.68  ? 481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 114.615 137.585 174.288 1.00 45.22  ? 481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.214 135.373 176.607 1.00 39.61  ? 481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 115.906 136.590 176.819 1.00 44.29  ? 481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 112.851 137.333 175.653 1.00 48.05  ? 482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.471 138.747 175.501 1.00 43.31  ? 482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.507 139.709 176.052 1.00 41.02  ? 482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 113.589 140.851 175.585 1.00 41.39  ? 482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.146 138.838 176.269 1.00 44.13  ? 482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 110.629 137.437 176.305 1.00 43.23  ? 482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 111.844 136.570 176.408 1.00 42.26  ? 482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.296 139.285 177.042 1.00 46.19  ? 483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.367 140.136 177.552 1.00 42.74  ? 483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.417 140.394 176.481 1.00 41.41  ? 483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 116.959 141.501 176.384 1.00 46.25  ? 483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.003 139.496 178.786 1.00 44.27  ? 483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.074 139.406 179.984 1.00 46.86  ? 483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.390 138.059 180.090 1.00 49.60  ? 483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.423 137.295 179.104 1.00 48.15  ? 483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 113.818 137.763 181.160 1.00 50.00  ? 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 116.725 139.380 175.670 1.00 35.84  ? 484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 117.671 139.569 174.577 1.00 38.97  ? 484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 117.149 140.577 173.563 1.00 35.40  ? 484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 117.904 141.425 173.074 1.00 37.11  ? 484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 117.962 138.233 173.900 1.00 38.65  ? 484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 115.860 140.498 173.229 1.00 34.51  ? 485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 115.282 141.466 172.305 1.00 33.05  ? 485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 115.265 142.863 172.910 1.00 35.14  ? 485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 115.482 143.852 172.203 1.00 40.47  ? 485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 113.876 141.035 171.898 1.00 37.42  ? 485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.853 139.960 170.829 1.00 35.06  ? 485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 112.473 139.821 170.216 1.00 36.07  ? 485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 111.473 139.419 171.198 1.00 42.50  ? 485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 111.311 138.178 171.636 1.00 43.63  ? 485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 110.362 137.927 172.533 1.00 40.53  ? 485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 112.068 137.185 171.201 1.00 39.14  ? 485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 115.011 142.967 174.216 1.00 41.14  ? 486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 115.070 144.266 174.878 1.00 36.88  ? 486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 116.474 144.853 174.812 1.00 38.26  ? 486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 116.649 146.048 174.534 1.00 44.90  ? 486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 114.613 144.135 176.329 1.00 41.48  ? 486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 114.265 145.469 176.952 1.00 47.76  ? 486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.327 146.495 176.242 1.00 49.43  ? 486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.933 145.494 178.155 1.00 48.66  ? 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 117.491 144.026 175.068 1.00 33.52  ? 487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 118.862 144.510 174.978 1.00 25.76  ? 487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 119.207 144.926 173.559 1.00 31.09  ? 487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 119.883 145.937 173.354 1.00 40.86  ? 487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 119.859 143.457 175.453 1.00 33.57  ? 487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 121.261 143.730 174.990 1.00 36.41  ? 487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 122.011 144.733 175.579 1.00 29.63  ? 487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 121.815 143.015 173.942 1.00 37.11  ? 487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 123.289 145.005 175.146 1.00 30.41  ? 487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.097 143.284 173.505 1.00 35.06  ? 487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 123.832 144.281 174.108 1.00 32.72  ? 487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 118.789 144.139 172.567 1.00 37.24  ? 488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 119.057 144.511 171.183 1.00 30.69  ? 488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 118.387 145.833 170.840 1.00 30.41  ? 488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.006 146.714 170.233 1.00 36.47  ? 488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 118.588 143.406 170.239 1.00 25.41  ? 488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 117.129 146.000 171.254 1.00 31.59  ? 489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 116.420 147.253 171.033 1.00 31.11  ? 489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 117.190 148.427 171.618 1.00 32.45  ? 489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 117.480 149.404 170.919 1.00 34.36  ? 489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.023 147.166 171.648 1.00 34.71  ? 489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.048 148.139 171.026 1.00 38.51  ? 489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.020 148.317 169.810 1.00 45.63  ? 489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 113.232 148.768 171.861 1.00 36.71  ? 489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 117.564 148.332 172.896 1.00 37.13  ? 490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 118.240 149.450 173.549 1.00 35.99  ? 490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 119.610 149.709 172.932 1.00 32.90  ? 490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 119.946 150.854 172.606 1.00 40.56  ? 490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 118.369 149.187 175.048 1.00 40.08  ? 490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.074 148.927 175.601 1.00 43.02  ? 490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 118.978 150.394 175.743 1.00 38.19  ? 490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 120.413 148.657 172.764 1.00 25.34  ? 491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 121.772 148.816 172.261 1.00 27.53  ? 491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 121.774 149.408 170.860 1.00 32.76  ? 491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 122.537 150.335 170.570 1.00 38.10  ? 491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 122.494 147.467 172.277 1.00 31.06  ? 491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 123.874 147.507 171.680 1.00 29.54  ? 491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 124.973 147.810 172.464 1.00 30.73  ? 491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.077 147.227 170.338 1.00 28.91  ? 491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.242 147.847 171.922 1.00 28.62  ? 491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 125.343 147.264 169.791 1.00 28.49  ? 491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 126.426 147.573 170.585 1.00 31.93  ? 491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 120.920 148.895 169.975 1.00 29.65  ? 492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 120.902 149.410 168.617 1.00 19.43  ? 492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.213 150.762 168.513 1.00 19.26  ? 492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 120.546 151.532 167.609 1.00 31.00  ? 492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 120.258 148.386 167.684 1.00 23.46  ? 492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 121.148 147.212 167.390 1.00 23.84  ? 492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 122.189 147.329 166.489 1.00 22.51  ? 492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 120.966 146.005 168.041 1.00 27.73  ? 492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 123.017 146.260 166.224 1.00 21.15  ? 492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 121.794 144.932 167.781 1.00 21.93  ? 492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 122.819 145.059 166.871 1.00 25.59  ? 492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.306 151.097 169.435 1.00 24.95  ? 493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 118.809 152.466 169.483 1.00 24.17  ? 493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 119.925 153.431 169.857 1.00 26.14  ? 493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.046 154.504 169.260 1.00 35.40  ? 493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 117.637 152.569 170.462 1.00 27.19  ? 493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.078 153.978 170.668 1.00 28.05  ? 493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 117.987 155.032 171.818 1.00 44.93  ? 493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 117.939 154.030 173.298 1.00 37.63  ? 493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 120.754 153.065 170.841 1.00 33.98  ? 494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 121.897 153.910 171.183 1.00 30.86  ? 494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 122.883 153.998 170.025 1.00 32.49  ? 494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.442 155.068 169.754 1.00 40.87  ? 494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 122.599 153.390 172.438 1.00 29.90  ? 494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 121.683 153.090 173.607 1.00 32.80  ? 494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 122.534 153.045 175.195 1.00 54.75  ? 494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 123.984 154.035 174.841 1.00 41.27  ? 494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.119 152.878 169.341 1.00 21.31  ? 495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.035 152.873 168.202 1.00 18.88  ? 495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.524 153.800 167.107 1.00 26.64  ? 495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.283 154.588 166.536 1.00 37.74  ? 495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.237 151.438 167.682 1.00 19.96  ? 495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 124.886 151.454 166.310 1.00 18.86  ? 495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.082 150.640 168.654 1.00 21.58  ? 495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.226 153.721 166.802 1.00 26.20  ? 496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.640 154.611 165.806 1.00 20.66  ? 496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 121.715 156.064 166.252 1.00 29.59  ? 496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.031 156.952 165.451 1.00 35.54  ? 496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.193 154.206 165.532 1.00 18.91  ? 496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 119.621 154.881 164.303 1.00 23.85  ? 496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.329 155.125 163.329 1.00 29.88  ? 496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.330 155.186 164.344 1.00 29.71  ? 496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.433 156.326 167.530 1.00 31.50  ? 497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.502 157.685 168.056 1.00 23.00  ? 497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 122.890 158.272 167.867 1.00 26.79  ? 497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.044 159.384 167.348 1.00 31.95  ? 497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.120 157.684 169.537 1.00 25.67  ? 497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.185 159.038 170.187 1.00 25.68  ? 497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.099 159.891 170.148 1.00 31.37  ? 497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.331 159.453 170.844 1.00 30.06  ? 497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 120.155 161.133 170.745 1.00 33.28  ? 497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.392 160.693 171.442 1.00 30.22  ? 497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 121.303 161.534 171.392 1.00 30.76  ? 497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 123.920 157.528 168.265 1.00 33.13  ? 498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.275 158.057 168.195 1.00 27.66  ? 498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 125.806 158.087 166.769 1.00 31.38  ? 498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.599 158.971 166.435 1.00 41.88  ? 498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.195 157.254 169.111 1.00 27.06  ? 498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 125.873 157.463 170.571 1.00 30.63  ? 498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 125.797 158.741 171.105 1.00 29.21  ? 498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.631 156.386 171.413 1.00 32.50  ? 498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.494 158.943 172.435 1.00 31.62  ? 498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.330 156.579 172.746 1.00 32.14  ? 498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.263 157.858 173.252 1.00 35.94  ? 498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 124.964 158.055 174.580 1.00 36.34  ? 498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.370 157.165 165.909 1.00 23.79  ? 499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.739 157.242 164.500 1.00 20.61  ? 499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.141 158.479 163.845 1.00 22.71  ? 499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.826 159.184 163.096 1.00 27.72  ? 499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.293 155.975 163.773 1.00 20.70  ? 499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 126.048 155.772 162.594 1.00 29.69  ? 499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 123.867 158.766 164.125 1.00 25.51  ? 500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.236 159.971 163.595 1.00 25.44  ? 500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.916 161.214 164.152 1.00 25.28  ? 500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.142 162.193 163.431 1.00 31.94  ? 500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.728 159.962 163.907 1.00 26.82  ? 500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.022 158.863 163.119 1.00 23.16  ? 500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.106 161.301 163.580 1.00 23.85  ? 500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.608 158.612 163.576 1.00 28.91  ? 500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.245 161.197 165.446 1.00 30.52  ? 501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.910 162.341 166.057 1.00 30.21  ? 501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.276 162.587 165.431 1.00 33.68  ? 501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.633 163.731 165.137 1.00 39.37  ? 501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 125.041 162.124 167.564 1.00 33.38  ? 501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 125.023 163.401 168.380 1.00 34.34  ? 501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 125.169 163.141 169.864 1.00 38.62  ? 501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 126.047 162.393 170.290 1.00 42.78  ? 501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 124.305 163.757 170.660 1.00 37.91  ? 501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 127.049 161.523 165.207 1.00 32.83  ? 502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.358 161.680 164.588 1.00 27.62  ? 502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.235 162.135 163.141 1.00 28.18  ? 502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 129.036 162.947 162.674 1.00 38.40  ? 502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.145 160.374 164.674 1.00 31.02  ? 502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.606 160.525 164.296 1.00 35.30  ? 502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.269 161.625 165.108 1.00 33.43  ? 502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.527 162.058 164.512 1.00 31.50  ? 502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 132.953 163.312 164.491 1.00 33.72  ? 502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 134.113 163.593 163.905 1.00 37.66  ? 502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 132.254 164.290 165.041 1.00 30.76  ? 502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.241 161.620 162.411 1.00 27.56  ? 503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 127.029 162.069 161.039 1.00 23.09  ? 503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.679 163.551 160.994 1.00 29.10  ? 503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.194 164.294 160.151 1.00 38.45  ? 503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 125.932 161.235 160.382 1.00 24.27  ? 503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 125.825 161.528 159.001 1.00 33.88  ? 503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.812 164.000 161.903 1.00 28.10  ? 504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.463 165.415 161.960 1.00 28.42  ? 504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.662 166.266 162.362 1.00 37.14  ? 504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.846 167.372 161.844 1.00 40.39  ? 504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 124.300 165.629 162.925 1.00 26.70  ? 504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 127.487 165.769 163.285 1.00 38.86  ? 505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.687 166.500 163.679 1.00 34.82  ? 505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.672 166.611 162.523 1.00 37.69  ? 505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.306 167.656 162.340 1.00 43.53  ? 505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 129.342 165.822 164.880 1.00 36.38  ? 505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.604 166.029 166.188 1.00 38.15  ? 505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 129.030 165.043 167.255 1.00 42.89  ? 505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.946 164.237 166.988 1.00 37.69  ? 505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.450 165.072 168.360 1.00 45.39  ? 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.821 165.544 161.736 1.00 34.22  ? 506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.692 165.596 160.566 1.00 26.92  ? 506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 130.139 166.569 159.534 1.00 32.99  ? 506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.891 167.322 158.906 1.00 42.31  ? 506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.883 164.187 159.975 1.00 29.71  ? 506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.621 163.286 160.964 1.00 32.03  ? 506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.650 164.254 158.668 1.00 31.70  ? 506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.479 161.812 160.663 1.00 25.48  ? 506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.817 166.571 159.342 1.00 33.16  ? 507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 128.209 167.514 158.408 1.00 33.62  ? 507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 128.406 168.951 158.870 1.00 35.91  ? 507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.591 169.856 158.048 1.00 42.20  ? 507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.724 167.201 158.240 1.00 32.24  ? 507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 128.357 169.183 160.182 1.00 38.03  ? 508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 128.601 170.520 160.715 1.00 38.30  ? 508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 130.060 170.924 160.538 1.00 43.97  ? 508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 130.357 172.054 160.133 1.00 48.25  ? 508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 128.204 170.569 162.189 1.00 43.73  ? 508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 128.489 171.896 162.869 1.00 43.95  ? 508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 128.229 171.810 164.364 1.00 45.99  ? 508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 128.364 173.169 165.030 1.00 46.12  ? 508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 127.506 173.280 166.241 1.00 47.37  ? 508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.985 170.012 160.843 1.00 42.26  ? 509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 132.407 170.327 160.757 1.00 42.37  ? 509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.837 170.578 159.317 1.00 43.31  ? 509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 133.602 171.510 159.045 1.00 47.01  ? 509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 133.229 169.196 161.372 1.00 42.38  ? 509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.465 169.342 162.867 1.00 48.73  ? 509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.276 168.037 163.616 1.00 50.30  ? 509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 133.808 167.004 163.158 1.00 44.16  ? 509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.594 168.044 164.663 1.00 49.36  ? 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 132.356 169.761 158.383 1.00 37.23  ? 510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 132.696 169.915 156.977 1.00 35.83  ? 510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.760 170.857 156.236 1.00 40.67  ? 510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 132.040 171.205 155.085 1.00 46.94  ? 510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.698 168.548 156.284 1.00 34.07  ? 510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 133.527 167.500 157.004 1.00 38.47  ? 510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.891 166.348 156.088 1.00 40.04  ? 510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.806 165.361 156.794 1.00 37.30  ? 510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.793 164.753 155.863 1.00 40.29  ? 510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 130.662 171.275 156.863 1.00 36.34  ? 511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 129.738 172.192 156.226 1.00 41.82  ? 511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.948 171.615 155.077 1.00 43.33  ? 511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 128.255 172.366 154.385 1.00 47.55  ? 511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 129.025 170.307 154.848 1.00 40.30  ? 512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 128.356 169.672 153.724 1.00 38.54  ? 512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.633 168.416 154.182 1.00 38.20  ? 512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 128.127 167.679 155.039 1.00 35.81  ? 512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 129.349 169.319 152.610 1.00 38.96  ? 512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.567 168.546 153.084 1.00 40.27  ? 512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.293 167.855 151.949 1.00 45.02  ? 512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.621 167.427 150.987 1.00 44.53  ? 512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.534 167.740 152.016 1.00 42.09  ? 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 126.458 168.187 153.607 1.00 40.35  ? 513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.681 166.974 153.809 1.00 32.74  ? 513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.740 166.124 152.547 1.00 33.88  ? 513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.269 166.541 151.514 1.00 37.69  ? 513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 124.229 167.313 154.162 1.00 32.10  ? 513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.556 167.798 152.995 1.00 39.48  ? 513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 124.185 168.380 155.239 1.00 33.89  ? 513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.193 164.915 152.633 1.00 33.19  ? 514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.145 164.064 151.455 1.00 30.74  ? 514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.166 164.634 150.437 1.00 34.45  ? 514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.238 165.370 150.780 1.00 40.85  ? 514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.772 162.625 151.828 1.00 29.66  ? 514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.363 162.455 152.329 1.00 31.02  ? 514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.077 162.562 153.677 1.00 27.89  ? 514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.333 162.146 151.455 1.00 32.01  ? 514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.789 162.391 154.143 1.00 27.88  ? 514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.042 161.975 151.916 1.00 29.59  ? 514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.771 162.097 153.262 1.00 32.58  ? 514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.398 164.305 149.168 1.00 37.30  ? 515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.595 164.870 148.093 1.00 35.45  ? 515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.129 164.487 148.253 1.00 42.00  ? 515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.800 163.350 148.602 1.00 49.58  ? 515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.118 164.399 146.736 1.00 38.29  ? 515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.224 165.286 146.202 1.00 44.55  ? 515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 125.883 165.971 147.012 1.00 43.38  ? 515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.435 165.299 144.970 1.00 44.81  ? 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.251 165.457 147.994 1.00 39.27  ? 516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.805 165.289 148.145 1.00 40.10  ? 516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.431 164.911 149.576 1.00 38.75  ? 516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.543 164.090 149.809 1.00 44.72  ? 516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.257 164.262 147.153 1.00 35.99  ? 516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.526 164.595 145.698 1.00 39.97  ? 516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 118.965 163.553 144.755 1.00 40.65  ? 516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 117.764 163.518 144.493 1.00 40.49  ? 516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 119.835 162.693 144.238 1.00 39.46  ? 516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.119 165.512 150.549 1.00 34.17  ? 517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.752 165.294 151.943 1.00 34.50  ? 517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.447 165.994 152.295 1.00 39.38  ? 517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.682 165.493 153.126 1.00 47.55  ? 517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.869 165.773 152.872 1.00 32.69  ? 517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.383 166.172 154.248 1.00 37.29  ? 517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.107 165.211 155.210 1.00 32.92  ? 517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.190 167.506 154.580 1.00 36.22  ? 517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.658 165.568 156.464 1.00 35.09  ? 517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.739 167.871 155.830 1.00 33.90  ? 517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.474 166.898 156.768 1.00 38.74  ? 517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 119.027 167.260 158.018 1.00 45.89  ? 517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.176 167.143 151.672 1.00 41.90  ? 518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.029 167.956 152.063 1.00 43.91  ? 518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.713 167.227 151.829 1.00 48.24  ? 518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.735 167.471 152.545 1.00 53.28  ? 518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.037 169.287 151.307 1.00 42.03  ? 518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.190 170.227 151.657 1.00 48.07  ? 518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 119.544 169.711 151.205 1.00 52.96  ? 518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 119.643 169.218 150.063 1.00 51.42  ? 518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.510 169.801 151.992 1.00 48.54  ? 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.664 166.343 150.840 1.00 34.50  ? 519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.473 165.561 150.593 1.00 33.87  ? 519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.337 164.309 151.423 1.00 36.90  ? 519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.311 163.628 151.337 1.00 37.21  ? 519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.342 163.980 152.229 1.00 36.19  ? 520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.312 162.775 153.038 1.00 33.00  ? 520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.499 162.997 154.309 1.00 32.23  ? 520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.222 164.128 154.714 1.00 33.33  ? 520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.730 162.331 153.393 1.00 25.77  ? 520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.364 163.280 154.231 1.00 28.49  ? 520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.114 161.885 154.940 1.00 30.35  ? 521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.353 161.958 156.181 1.00 27.94  ? 521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 114.171 162.535 157.329 1.00 32.20  ? 521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.589 163.000 158.313 1.00 33.98  ? 521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.828 160.575 156.562 1.00 28.29  ? 521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.916 159.750 156.995 1.00 32.08  ? 521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.145 159.920 155.373 1.00 26.93  ? 521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.503 162.503 157.232 1.00 34.12  ? 522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.330 163.156 158.242 1.00 30.32  ? 522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 116.088 164.659 158.261 1.00 34.66  ? 522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.990 165.268 159.333 1.00 31.12  ? 522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.809 162.866 157.986 1.00 28.81  ? 522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 118.187 161.406 158.033 1.00 29.11  ? 522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 118.137 160.693 159.222 1.00 26.91  ? 522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.615 160.745 156.891 1.00 33.50  ? 522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.491 159.360 159.269 1.00 31.07  ? 522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.972 159.413 156.930 1.00 32.53  ? 522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.907 158.725 158.119 1.00 31.43  ? 522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.261 157.398 158.159 1.00 35.03  ? 522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.995 165.276 157.081 1.00 40.23  ? 523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.772 166.716 157.013 1.00 37.27  ? 523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 114.349 167.077 157.417 1.00 42.03  ? 523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 114.130 168.081 158.105 1.00 44.30  ? 523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 116.077 167.225 155.606 1.00 33.56  ? 523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 113.369 166.275 156.999 1.00 38.20  ? 524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.977 166.552 157.331 1.00 38.62  ? 524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.610 166.122 158.744 1.00 40.50  ? 524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 110.556 166.529 159.244 1.00 45.58  ? 524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 111.047 165.860 156.332 1.00 39.26  ? 524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.934 164.470 156.663 1.00 40.88  ? 524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 111.587 165.997 154.917 1.00 38.39  ? 524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 112.447 165.318 159.396 1.00 34.71  ? 525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 112.173 164.851 160.737 1.00 35.59  ? 525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 111.314 163.610 160.826 1.00 38.55  ? 525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 111.021 163.161 161.941 1.00 40.35  ? 525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.900 163.041 159.690 1.00 40.84  ? 526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 110.077 161.836 159.719 1.00 40.12  ? 526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.846 160.645 160.278 1.00 40.77  ? 526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.241 159.723 160.835 1.00 46.58  ? 526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.559 161.530 158.313 1.00 37.88  ? 526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.703 160.278 158.208 1.00 39.04  ? 526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.417 159.886 156.772 1.00 45.73  ? 526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.604 160.733 155.874 1.00 44.81  ? 526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.007 158.729 156.541 1.00 42.38  ? 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 112.175 160.652 160.149 1.00 35.19  ? 527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.979 159.546 160.659 1.00 32.25  ? 527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.906 159.460 162.179 1.00 36.84  ? 527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.907 158.361 162.745 1.00 39.87  ? 527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.428 159.703 160.201 1.00 28.50  ? 527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.303 158.503 160.487 1.00 34.91  ? 527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.997 158.392 161.684 1.00 32.32  ? 527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 115.438 157.484 159.555 1.00 34.71  ? 527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.796 157.299 161.947 1.00 31.99  ? 527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.237 156.387 159.809 1.00 34.34  ? 527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 116.913 156.300 161.005 1.00 32.90  ? 527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.710 155.208 161.261 1.00 34.85  ? 527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.839 160.603 162.853 1.00 41.63  ? 528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.899 160.660 164.307 1.00 40.95  ? 528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.531 160.583 164.973 1.00 47.36  ? 528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.454 160.712 166.197 1.00 54.11  ? 528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.608 161.942 164.754 1.00 38.99  ? 528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.960 162.135 164.134 1.00 43.41  ? 528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 116.083 161.556 164.698 1.00 40.84  ? 528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 115.110 162.897 162.989 1.00 39.90  ? 528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.328 161.732 164.132 1.00 39.30  ? 528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 116.354 163.077 162.419 1.00 39.17  ? 528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.463 162.493 162.991 1.00 41.20  ? 528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.458 160.384 164.204 1.00 45.48  ? 529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.118 160.369 164.788 1.00 43.67  ? 529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 108.981 159.258 165.823 1.00 48.45  ? 529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.553 159.499 166.960 1.00 52.93  ? 529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 108.071 160.209 163.687 1.00 42.34  ? 529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.889 161.471 162.868 1.00 50.30  ? 529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.428 162.524 163.267 1.00 52.04  ? 529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.204 161.411 161.826 1.00 50.76  ? 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.354 158.032 165.452 1.00 45.30  ? 530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.263 156.913 166.380 1.00 44.78  ? 530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.256 157.031 167.526 1.00 48.57  ? 530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.066 156.388 168.562 1.00 49.96  ? 530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.475 155.594 165.637 1.00 45.85  ? 530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 110.896 155.067 165.704 1.00 45.41  ? 530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.071 153.851 164.819 1.00 45.41  ? 530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.430 153.218 165.027 1.00 46.66  ? 530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.042 152.833 163.729 1.00 52.05  ? 530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.307 157.833 167.365 1.00 45.95  ? 531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.280 158.034 168.430 1.00 40.19  ? 531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 111.868 159.130 169.397 1.00 40.07  ? 531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.149 159.025 170.597 1.00 45.08  ? 531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.650 158.358 167.835 1.00 39.31  ? 531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.334 157.169 167.205 1.00 41.19  ? 531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.668 156.057 167.964 1.00 40.79  ? 531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.648 157.159 165.854 1.00 42.18  ? 531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.295 154.967 167.396 1.00 43.43  ? 531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.273 156.073 165.277 1.00 41.17  ? 531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.594 154.981 166.053 1.00 41.59  ? 531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.219 153.897 165.481 1.00 40.59  ? 531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.212 160.184 168.905 1.00 44.85  ? 532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.666 161.209 169.790 1.00 44.76  ? 532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.307 160.827 170.349 1.00 48.02  ? 532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.783 161.536 171.217 1.00 51.09  ? 532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.553 162.566 169.070 1.00 46.24  ? 532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.881 162.940 168.434 1.00 44.76  ? 532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.449 162.522 168.025 1.00 45.58  ? 532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.717 159.729 169.876 1.00 49.92  ? 533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.445 159.256 170.404 1.00 53.52  ? 533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.582 158.050 171.323 1.00 53.83  ? 533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.869 157.971 172.328 1.00 51.33  ? 533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.495 158.900 169.255 1.00 50.75  ? 533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.818 157.639 168.700 1.00 48.84  ? 533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.475 157.115 171.008 1.00 55.74  ? 534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.632 155.882 171.768 1.00 51.81  ? 534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 109.953 155.914 172.523 1.00 49.97  ? 534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 110.984 156.298 171.962 1.00 52.20  ? 534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.581 154.657 170.845 1.00 51.59  ? 534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.302 154.595 170.202 1.00 50.16  ? 534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.807 153.376 171.633 1.00 51.06  ? 534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 109.917 155.510 173.791 1.00 51.80  ? 535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.120 155.390 174.603 1.00 52.89  ? 535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 111.669 153.975 174.478 1.00 54.04  ? 535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 110.939 152.998 174.675 1.00 52.44  ? 535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.822 155.720 176.065 1.00 51.69  ? 535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.069 155.729 176.926 1.00 56.76  ? 535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.968 156.556 176.666 1.00 53.64  ? 535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.149 154.910 177.865 1.00 59.83  ? 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 112.957 153.868 174.153 1.00 45.35  ? 536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 113.592 152.583 173.891 1.00 42.63  ? 536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 114.507 152.144 175.029 1.00 44.42  ? 536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 115.403 151.320 174.818 1.00 47.78  ? 536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.362 152.634 172.573 1.00 41.30  ? 536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.483 152.792 171.366 1.00 39.12  ? 536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 112.972 151.685 170.714 1.00 37.38  ? 536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.166 154.050 170.884 1.00 43.60  ? 536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.160 151.827 169.606 1.00 38.84  ? 536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.357 154.198 169.776 1.00 46.34  ? 536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 111.854 153.086 169.136 1.00 45.64  ? 536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.304 152.681 176.229 1.00 47.65  ? 537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.051 152.219 177.386 1.00 49.93  ? 537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 114.647 150.785 177.726 1.00 51.53  ? 537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 113.530 150.359 177.420 1.00 49.58  ? 537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 114.798 153.133 178.582 1.00 47.00  ? 537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 115.212 154.460 178.306 1.00 50.12  ? 537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 115.544 150.013 178.340 1.00 52.45  ? 538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 115.222 148.613 178.644 1.00 51.93  ? 538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.017 148.497 179.565 1.00 53.05  ? 538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 113.850 149.275 180.506 1.00 53.15  ? 538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 116.497 148.093 179.318 1.00 51.99  ? 538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 117.572 149.027 178.881 1.00 51.67  ? 538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 116.913 150.362 178.755 1.00 48.27  ? 538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 113.172 147.506 179.282 1.00 56.30  ? 539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.006 147.231 180.111 1.00 55.21  ? 539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 112.287 146.214 181.205 1.00 56.91  ? 539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 111.454 146.042 182.102 1.00 57.62  ? 539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 110.846 146.734 179.243 1.00 55.19  ? 539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 110.562 147.609 178.032 1.00 54.29  ? 539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 109.239 148.341 178.176 1.00 55.36  ? 539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 109.069 149.388 177.087 1.00 58.60  ? 539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 110.051 150.499 177.227 1.00 57.28  ? 539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 113.432 145.542 181.154 1.00 56.47  ? 540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 113.819 144.547 182.145 1.00 57.19  ? 540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 114.972 145.091 182.975 1.00 56.07  ? 540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 115.923 145.656 182.426 1.00 56.82  ? 540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 114.217 143.231 181.473 1.00 55.88  ? 540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 113.082 142.554 180.739 1.00 54.36  ? 540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 112.218 141.694 181.400 1.00 55.00  ? 540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.874 142.780 179.386 1.00 54.38  ? 540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 111.178 141.075 180.734 1.00 54.84  ? 540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.837 142.166 178.711 1.00 58.02  ? 540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 110.992 141.315 179.390 1.00 58.24  ? 540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 109.958 140.701 178.722 1.00 57.26  ? 540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 114.878 144.927 184.297 1.00 62.58  ? 541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 115.919 145.442 185.181 1.00 61.40  ? 541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 117.258 144.761 184.930 1.00 63.08  ? 541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 118.311 145.387 185.095 1.00 64.37  ? 541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 115.501 145.272 186.640 1.00 62.44  ? 541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 114.899 146.524 187.257 1.00 65.56  ? 541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 115.310 146.715 188.704 1.00 68.41  ? 541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 116.179 145.956 189.181 1.00 67.75  ? 541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 114.764 147.625 189.363 1.00 66.43  ? 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 117.241 143.483 184.544 1.00 58.16  ? 542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 118.484 142.797 184.210 1.00 57.42  ? 542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 119.157 143.439 183.002 1.00 57.67  ? 542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 120.379 143.624 182.987 1.00 56.92  ? 542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.212 141.316 183.952 1.00 54.18  ? 542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 119.336 140.592 183.230 1.00 55.88  ? 542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.171 139.086 183.324 1.00 55.00  ? 542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 120.345 138.364 182.686 1.00 52.90  ? 542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.631 138.691 183.358 1.00 56.73  ? 542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 118.371 143.787 181.982 1.00 51.42  ? 543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 118.929 144.428 180.797 1.00 48.38  ? 543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 119.383 145.846 181.115 1.00 48.11  ? 543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 120.437 146.294 180.649 1.00 50.43  ? 543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 117.904 144.401 179.650 1.00 50.08  ? 543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 117.575 142.959 179.265 1.00 53.34  ? 543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 118.429 145.166 178.452 1.00 48.81  ? 543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 118.795 142.097 179.033 1.00 50.04  ? 543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 118.596 146.577 181.911 1.00 50.04  ? 544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 118.965 147.944 182.261 1.00 50.31  ? 544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 120.263 147.991 183.054 1.00 54.15  ? 544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.019 148.962 182.950 1.00 56.68  ? 544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 117.836 148.609 183.048 1.00 51.02  ? 544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 120.540 146.955 183.852 1.00 58.25  ? 545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 121.794 146.896 184.589 1.00 58.23  ? 545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 122.999 146.736 183.670 1.00 55.77  ? 545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.110 147.113 184.056 1.00 57.03  ? 545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 121.756 145.751 185.603 1.00 58.96  ? 545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 120.892 146.070 186.807 1.00 60.15  ? 545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 120.053 146.969 186.762 1.00 61.88  ? 545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 121.094 145.332 187.892 1.00 57.47  ? 545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 122.806 146.180 182.472 1.00 49.48  ? 546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 123.906 146.078 181.521 1.00 48.70  ? 546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 124.362 147.450 181.045 1.00 50.38  ? 546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 125.562 147.665 180.837 1.00 53.57  ? 546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 123.497 145.214 180.329 1.00 48.34  ? 546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.004 143.798 180.632 1.00 48.93  ? 546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.653 143.075 179.344 1.00 49.37  ? 546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.047 143.021 181.416 1.00 43.01  ? 546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 123.430 148.385 180.873 1.00 48.97  ? 547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 123.741 149.734 180.423 1.00 47.24  ? 547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.081 150.673 181.574 1.00 48.04  ? 547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 123.974 151.895 181.417 1.00 52.83  ? 547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 122.574 150.298 179.610 1.00 46.58  ? 547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 122.334 149.576 178.317 1.00 46.57  ? 547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 123.022 149.934 177.171 1.00 47.08  ? 547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 121.426 148.535 178.248 1.00 45.51  ? 547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 122.806 149.272 175.982 1.00 43.31  ? 547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 121.206 147.867 177.060 1.00 43.55  ? 547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 121.898 148.236 175.926 1.00 42.91  ? 547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 124.482 150.135 182.723 1.00 54.58  ? 548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 124.880 150.975 183.843 1.00 56.09  ? 548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.170 151.715 183.515 1.00 57.88  ? 548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.076 151.169 182.881 1.00 59.07  ? 548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.060 150.132 185.105 1.00 55.40  ? 548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 123.768 149.861 185.859 1.00 61.23  ? 548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 123.020 151.132 186.217 1.00 60.59  ? 548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 123.676 152.127 186.595 1.00 57.65  ? 548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 121.775 151.137 186.120 1.00 56.65  ? 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.248 152.969 183.952 1.00 55.32  ? 549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.373 153.812 183.609 1.00 56.51  ? 549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.349 154.354 182.201 1.00 58.41  ? 549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.342 154.944 181.763 1.00 57.44  ? 549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.248 154.170 181.477 1.00 55.62  ? 550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.105 154.645 180.109 1.00 54.46  ? 550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 124.814 155.439 180.000 1.00 58.44  ? 550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 123.784 155.030 180.547 1.00 56.79  ? 550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.092 153.480 179.118 1.00 53.63  ? 550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.374 153.322 178.329 1.00 58.34  ? 550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.194 152.117 177.008 1.00 60.49  ? 550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.133 150.595 177.945 1.00 56.23  ? 550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 124.868 156.567 179.299 1.00 59.81  ? 551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.698 157.424 179.142 1.00 56.32  ? 551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 122.845 156.895 177.998 1.00 54.67  ? 551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.207 157.036 176.825 1.00 54.87  ? 551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 124.121 158.868 178.887 1.00 56.82  ? 551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.998 159.754 178.449 1.00 59.52  ? 551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.961 160.107 179.287 1.00 59.31  ? 551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.746 160.355 177.263 1.00 58.18  ? 551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 121.120 160.890 178.635 1.00 58.18  ? 551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.573 161.056 177.405 1.00 58.94  ? 551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.713 156.283 178.333 1.00 49.03  ? 552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 120.775 155.787 177.331 1.00 49.21  ? 552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.014 156.973 176.751 1.00 50.21  ? 552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.410 157.747 177.507 1.00 51.28  ? 552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 119.816 154.746 177.930 1.00 48.87  ? 552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 120.602 153.645 178.641 1.00 49.43  ? 552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 118.933 154.153 176.847 1.00 47.46  ? 552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 119.731 152.658 179.381 1.00 50.08  ? 552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.026 157.163 175.433 1.00 45.78  ? 553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.301 158.297 174.837 1.00 42.29  ? 553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.808 158.208 175.112 1.00 48.33  ? 553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.147 157.231 174.751 1.00 47.05  ? 553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.611 158.165 173.342 1.00 43.31  ? 553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 120.875 157.379 173.283 1.00 43.39  ? 553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 120.819 156.428 174.436 1.00 42.82  ? 553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.279 159.243 175.757 1.00 56.17  ? 554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.865 159.309 176.079 1.00 52.83  ? 554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.101 160.002 174.952 1.00 52.81  ? 554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.649 160.319 173.894 1.00 54.04  ? 554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.652 160.032 177.409 1.00 52.65  ? 554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.515 161.438 177.173 1.00 52.24  ? 554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.830 159.791 178.341 1.00 51.58  ? 554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.807 160.231 175.184 1.00 49.60  ? 555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 112.989 160.927 174.197 1.00 49.09  ? 555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.455 162.367 174.010 1.00 51.44  ? 555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.504 162.872 172.881 1.00 49.46  ? 555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.519 160.880 174.617 1.00 50.81  ? 555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 111.011 159.554 174.427 1.00 51.64  ? 555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.689 161.852 173.799 1.00 51.10  ? 555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.811 163.042 175.106 1.00 55.21  ? 556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.306 164.412 175.008 1.00 53.93  ? 556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.627 164.469 174.250 1.00 55.48  ? 556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.855 165.384 173.449 1.00 54.38  ? 556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.460 165.013 176.404 1.00 55.05  ? 556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 113.274 165.847 176.855 1.00 54.67  ? 556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 113.396 167.304 176.455 1.00 58.82  ? 556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 113.323 167.599 175.244 1.00 57.16  ? 556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 113.565 168.155 177.353 1.00 58.60  ? 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.514 163.502 174.497 1.00 53.39  ? 557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.777 163.458 173.769 1.00 49.98  ? 557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.544 163.224 172.283 1.00 48.77  ? 557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.237 163.802 171.440 1.00 51.14  ? 557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.682 162.371 174.348 1.00 48.32  ? 557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 118.953 162.567 175.824 1.00 51.41  ? 557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.152 163.727 176.244 1.00 49.85  ? 557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.967 161.563 176.564 1.00 50.24  ? 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.566 162.382 171.941 1.00 40.46  ? 558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.245 162.169 170.536 1.00 35.36  ? 558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.633 163.412 169.901 1.00 41.06  ? 558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.893 163.692 168.729 1.00 47.05  ? 558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.310 160.972 170.385 1.00 40.24  ? 558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 116.035 159.683 170.157 1.00 36.77  ? 558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.205 158.669 171.051 1.00 38.38  ? 558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.695 159.272 168.953 1.00 39.08  ? 558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.926 157.650 170.479 1.00 39.77  ? 558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.236 157.995 169.191 1.00 36.73  ? 558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 116.872 159.857 167.696 1.00 44.61  ? 558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 117.946 157.294 168.219 1.00 32.96  ? 558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.577 159.160 166.734 1.00 40.05  ? 558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.106 157.893 167.001 1.00 33.18  ? 558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.828 164.169 170.652 1.00 48.30  ? 559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.325 165.441 170.138 1.00 48.14  ? 559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.466 166.417 169.881 1.00 46.46  ? 559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.484 167.115 168.858 1.00 46.34  ? 559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 113.322 166.047 171.119 1.00 47.23  ? 559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.982 165.337 171.176 1.00 49.12  ? 559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 110.959 166.167 171.931 1.00 49.38  ? 559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 110.069 165.295 172.799 1.00 49.11  ? 559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 110.315 165.528 174.250 1.00 48.56  ? 559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.425 166.483 170.807 1.00 45.33  ? 560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.583 167.351 170.615 1.00 43.70  ? 560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 118.394 166.921 169.400 1.00 45.86  ? 560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.860 167.766 168.626 1.00 53.28  ? 560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.455 167.353 171.870 1.00 45.13  ? 560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 117.809 168.018 173.075 1.00 48.65  ? 560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.450 167.562 174.378 1.00 50.95  ? 560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 119.962 167.454 174.249 1.00 49.74  ? 560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 120.543 166.539 175.269 1.00 46.17  ? 560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.572 165.612 169.215 1.00 36.43  ? 561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 119.291 165.117 168.045 1.00 32.42  ? 561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.540 165.431 166.757 1.00 40.10  ? 561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 119.157 165.753 165.737 1.00 45.79  ? 561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.531 163.614 168.169 1.00 35.52  ? 561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.234 162.988 166.965 1.00 37.76  ? 561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.617 163.585 166.803 1.00 34.56  ? 561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.309 161.480 167.098 1.00 37.96  ? 561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 117.209 165.327 166.779 1.00 38.38  ? 562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 116.416 165.674 165.605 1.00 37.03  ? 562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.575 167.147 165.252 1.00 40.42  ? 562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.744 167.499 164.078 1.00 40.64  ? 562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.947 165.332 165.855 1.00 38.97  ? 562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.989 165.843 164.796 1.00 40.56  ? 562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.547 165.595 165.204 1.00 39.72  ? 562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.577 166.149 164.176 1.00 43.21  ? 562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 110.219 165.558 164.321 1.00 38.06  ? 562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.532 168.023 166.259 1.00 41.37  ? 563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.750 169.445 166.011 1.00 41.59  ? 563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 118.157 169.704 165.482 1.00 42.96  ? 563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 118.349 170.518 164.572 1.00 49.20  ? 563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 116.498 170.246 167.288 1.00 40.35  ? 563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 119.153 169.015 166.045 1.00 37.66  ? 564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 120.532 169.175 165.595 1.00 36.35  ? 564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.693 168.740 164.145 1.00 39.53  ? 564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 121.397 169.393 163.366 1.00 44.14  ? 564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 121.460 168.375 166.508 1.00 37.67  ? 564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.918 168.690 166.333 1.00 38.25  ? 564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 123.490 169.770 166.984 1.00 40.80  ? 564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.720 167.896 165.534 1.00 38.32  ? 564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.832 170.057 166.832 1.00 42.66  ? 564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 125.063 168.178 165.378 1.00 41.11  ? 564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.619 169.259 166.027 1.00 43.49  ? 564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 120.052 167.634 163.766 1.00 37.12  ? 565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 120.117 167.158 162.387 1.00 31.43  ? 565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 119.414 168.132 161.452 1.00 36.98  ? 565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.898 168.417 160.351 1.00 38.81  ? 565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.524 165.742 162.289 1.00 32.53  ? 565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 119.183 165.400 160.848 1.00 35.60  ? 565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.495 164.732 162.860 1.00 35.24  ? 565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 118.263 168.663 161.873 1.00 44.10  ? 566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 117.567 169.645 161.050 1.00 45.26  ? 566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 118.419 170.890 160.841 1.00 48.16  ? 566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 118.431 171.469 159.749 1.00 48.84  ? 566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 116.227 170.010 161.686 1.00 40.56  ? 566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 119.140 171.315 161.880 1.00 46.94  ? 567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.947 172.526 161.777 1.00 42.57  ? 567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 121.214 172.309 160.953 1.00 44.02  ? 567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 121.567 173.156 160.125 1.00 48.85  ? 567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 120.296 173.034 163.177 1.00 41.93  ? 567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 121.613 173.784 163.267 1.00 46.68  ? 567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.542 174.972 164.206 1.00 51.00  ? 567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.584 175.044 165.004 1.00 47.38  ? 567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.444 175.834 164.145 1.00 48.74  ? 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.905 171.184 161.151 1.00 43.79  ? 568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 123.219 170.971 160.557 1.00 42.38  ? 568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.252 169.918 159.459 1.00 38.82  ? 568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.226 169.876 158.700 1.00 42.44  ? 568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 124.234 170.587 161.644 1.00 43.02  ? 568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 124.526 171.690 162.611 1.00 42.76  ? 568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 124.552 171.499 163.974 1.00 46.64  ? 568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.817 172.997 162.409 1.00 40.38  ? 568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 124.836 172.642 164.572 1.00 42.31  ? 568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 125.003 173.567 163.645 1.00 45.38  ? 568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.235 169.076 159.347 1.00 37.12  ? 569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.221 168.066 158.311 1.00 35.73  ? 569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.888 166.771 158.725 1.00 35.52  ? 569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 123.289 166.562 159.874 1.00 40.65  ? 569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.998 165.875 157.746 1.00 31.72  ? 570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.581 164.555 157.937 1.00 27.74  ? 570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.628 164.318 156.861 1.00 31.95  ? 570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 124.350 164.503 155.674 1.00 36.93  ? 570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 122.508 163.465 157.877 1.00 33.36  ? 570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.646 163.369 159.119 1.00 32.70  ? 570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 122.137 161.997 160.171 1.00 40.94  ? 570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.069 160.654 158.994 1.00 30.30  ? 570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.828 163.906 157.275 1.00 23.75  ? 571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.899 163.695 156.307 1.00 16.90  ? 571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.716 162.400 155.527 1.00 30.52  ? 571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 127.081 162.333 154.347 1.00 34.37  ? 571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 128.256 163.697 157.008 1.00 26.87  ? 571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 129.421 163.798 156.053 1.00 29.46  ? 571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.767 165.012 155.475 1.00 32.78  ? 571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 130.170 162.679 155.719 1.00 27.78  ? 571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.828 165.110 154.599 1.00 31.14  ? 571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 131.232 162.767 154.843 1.00 31.33  ? 571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.557 163.984 154.287 1.00 38.02  ? 571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.616 164.075 153.414 1.00 39.28  ? 571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 126.164 161.366 156.155 1.00 30.83  ? 572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.021 160.054 155.539 1.00 14.94  ? 572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.558 159.790 155.218 1.00 24.17  ? 572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.688 159.968 156.077 1.00 33.94  ? 572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.556 158.952 156.456 1.00 13.60  ? 572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.904 159.245 157.035 1.00 23.33  ? 572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.074 159.982 158.187 1.00 24.89  ? 572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.145 158.894 156.626 1.00 22.27  ? 572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.363 160.076 158.460 1.00 23.54  ? 572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.035 159.424 157.529 1.00 28.30  ? 572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.292 159.371 153.979 1.00 21.36  ? 573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.945 158.937 153.624 1.00 19.12  ? 573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.564 157.671 154.379 1.00 28.55  ? 573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.431 157.542 154.858 1.00 33.72  ? 573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.846 158.718 152.117 1.00 17.51  ? 573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 123.923 157.930 151.648 1.00 28.17  ? 573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.496 156.729 154.491 1.00 27.69  ? 574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.291 155.485 155.216 1.00 17.92  ? 574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.472 155.260 156.143 1.00 16.61  ? 574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.617 155.540 155.779 1.00 21.28  ? 574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.128 154.304 154.257 1.00 18.12  ? 574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.057 154.528 153.218 1.00 16.04  ? 574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 122.354 155.139 152.008 1.00 17.59  ? 574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 120.746 154.147 153.454 1.00 16.23  ? 574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 121.380 155.355 151.061 1.00 20.35  ? 574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 119.764 154.358 152.511 1.00 12.35  ? 574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.087 154.962 151.318 1.00 14.81  ? 574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.114 155.173 150.372 1.00 29.00  ? 574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.192 154.765 157.342 1.00 17.52  ? 575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.222 154.602 158.359 1.00 9.31   ? 575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.332 153.188 158.899 1.00 18.51  ? 575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.446 152.709 159.128 1.00 30.93  ? 575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 124.964 155.564 159.523 1.00 15.39  ? 575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 124.874 157.020 159.121 1.00 17.26  ? 575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 123.946 157.781 160.044 1.00 15.93  ? 575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.563 157.341 159.910 1.00 21.51  ? 575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 121.936 156.562 160.780 1.00 18.85  ? 575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 120.666 156.235 160.560 1.00 18.23  ? 575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 122.544 156.104 161.861 1.00 14.60  ? 575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.215 152.502 159.110 1.00 15.63  ? 576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.203 151.217 159.795 1.00 13.95  ? 576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 123.787 150.113 158.834 1.00 12.29  ? 576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 122.753 150.221 158.170 1.00 27.17  ? 576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.257 151.251 160.994 1.00 12.71  ? 576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 123.531 152.325 162.045 1.00 14.42  ? 576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 122.447 152.310 163.099 1.00 20.67  ? 576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 124.894 152.125 162.677 1.00 15.54  ? 576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 124.594 149.058 158.769 1.00 14.48  ? 577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.248 147.856 158.021 1.00 13.99  ? 577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.039 146.701 158.614 1.00 28.18  ? 577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 126.257 146.803 158.777 1.00 34.37  ? 577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 124.532 148.021 156.520 1.00 13.90  ? 577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.232 147.742 155.973 1.00 29.35  ? 577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 124.347 145.621 158.954 1.00 20.92  ? 578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 124.937 144.514 159.696 1.00 21.31  ? 578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 125.309 143.430 158.691 1.00 16.68  ? 578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 124.447 142.709 158.182 1.00 19.45  ? 578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 123.993 143.995 160.782 1.00 14.09  ? 578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 123.638 145.128 161.745 1.00 2.32   ? 578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 124.633 142.853 161.542 1.00 15.61  ? 578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 122.768 144.702 162.894 1.00 16.00  ? 578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 126.602 143.318 158.406 1.00 22.86  ? 579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 127.131 142.309 157.506 1.00 17.63  ? 579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 127.369 141.001 158.253 1.00 22.37  ? 579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 127.486 140.992 159.480 1.00 38.53  ? 579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 128.428 142.807 156.875 1.00 23.12  ? 579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 127.426 139.871 157.536 1.00 22.55  ? 580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.669 138.593 158.229 1.00 26.58  ? 580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.987 138.551 158.982 1.00 29.93  ? 580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 129.046 137.979 160.078 1.00 37.13  ? 580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.624 137.563 157.091 1.00 28.34  ? 580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.842 138.346 155.844 1.00 32.28  ? 580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 127.230 139.682 156.090 1.00 25.43  ? 580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 130.042 139.151 158.428 1.00 27.21  ? 581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 131.359 139.219 159.067 1.00 38.49  ? 581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.817 137.843 159.544 1.00 38.92  ? 581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 132.206 137.652 160.697 1.00 39.27  ? 581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.357 140.222 160.220 1.00 39.43  ? 581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.664 139.664 161.343 1.00 23.54  ? 581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.672 141.509 159.797 1.00 34.77  ? 581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.767 136.869 158.633 1.00 44.80  ? 582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 132.083 135.500 158.995 1.00 46.63  ? 582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.562 135.222 159.165 1.00 50.23  ? 582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.923 134.223 159.796 1.00 55.49  ? 582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.424 136.078 158.619 1.00 41.11  ? 583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 135.864 135.857 158.658 1.00 42.75  ? 583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.548 136.623 159.784 1.00 42.80  ? 583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.317 136.040 160.552 1.00 38.48  ? 583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 136.487 136.241 157.310 1.00 47.59  ? 583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 136.162 135.292 156.309 1.00 47.10  ? 583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 136.281 137.927 159.899 1.00 46.24  ? 584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.874 138.731 160.962 1.00 42.73  ? 584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 136.308 138.408 162.334 1.00 41.69  ? 584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.851 138.872 163.342 1.00 49.58  ? 584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 136.687 140.235 160.677 1.00 42.62  ? 584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.338 140.484 160.000 1.00 42.10  ? 584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 137.834 140.763 159.830 1.00 37.97  ? 584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 134.940 141.943 159.940 1.00 38.83  ? 584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 135.223 137.631 162.399 1.00 39.71  ? 585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.651 137.266 163.690 1.00 31.85  ? 585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.611 136.397 164.492 1.00 33.32  ? 585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.666 136.495 165.724 1.00 39.79  ? 585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 133.319 136.548 163.489 1.00 37.10  ? 585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.488 135.361 162.734 1.00 39.19  ? 585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.366 135.532 163.812 1.00 43.66  ? 586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.332 134.686 164.505 1.00 40.12  ? 586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.411 135.524 165.178 1.00 40.12  ? 586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.745 135.305 166.347 1.00 41.89  ? 586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 137.960 133.697 163.523 1.00 39.46  ? 586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.011 132.645 163.005 1.00 40.42  ? 586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 136.696 131.530 163.767 1.00 44.47  ? 586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 136.432 132.762 161.748 1.00 40.35  ? 586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 135.831 130.564 163.294 1.00 46.79  ? 586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 135.565 131.803 161.268 1.00 42.93  ? 586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 135.268 130.705 162.045 1.00 48.11  ? 586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 134.405 129.743 161.573 1.00 48.68  ? 586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.952 136.507 164.454 1.00 43.30  ? 587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 140.049 137.319 164.978 1.00 38.75  ? 587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 139.599 138.104 166.202 1.00 40.01  ? 587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 140.339 138.233 167.184 1.00 41.26  ? 587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.592 138.250 163.878 1.00 35.05  ? 587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.794 139.028 164.385 1.00 36.90  ? 587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.950 137.448 162.641 1.00 40.71  ? 587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 138.383 138.639 166.165 1.00 40.58  ? 588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 137.856 139.428 167.268 1.00 36.58  ? 588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 137.275 138.575 168.383 1.00 37.89  ? 588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 136.809 139.134 169.382 1.00 39.09  ? 588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 136.791 140.397 166.752 1.00 27.31  ? 588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.348 141.536 165.922 1.00 27.58  ? 588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 137.481 142.820 166.712 1.00 37.54  ? 588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 136.620 143.155 167.524 1.00 35.53  ? 588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 138.566 143.548 166.479 1.00 41.82  ? 588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 137.297 137.250 168.241 1.00 37.32  ? 589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.697 136.331 169.204 1.00 33.45  ? 589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 135.238 136.707 169.453 1.00 36.45  ? 589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.811 136.982 170.576 1.00 39.59  ? 589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.497 136.299 170.508 1.00 39.89  ? 589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.440 135.243 170.499 1.00 42.22  ? 589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.478 136.730 168.362 1.00 35.34  ? 590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.097 137.178 168.382 1.00 29.24  ? 590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 132.254 136.266 167.506 1.00 33.44  ? 590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 132.749 135.666 166.549 1.00 33.36  ? 590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.975 138.626 167.894 1.00 29.22  ? 590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.697 138.676 166.506 1.00 35.36  ? 590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 130.974 136.157 167.850 1.00 35.34  ? 591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.035 135.447 166.998 1.00 35.19  ? 591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.737 136.271 165.749 1.00 32.19  ? 591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.692 137.502 165.785 1.00 30.34  ? 591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 128.742 135.145 167.751 1.00 32.23  ? 591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 127.948 136.334 167.841 1.00 34.81  ? 591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 129.051 134.642 169.150 1.00 28.99  ? 591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.538 135.573 164.634 1.00 31.17  ? 592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.344 136.240 163.353 1.00 34.53  ? 592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.024 137.000 163.347 1.00 31.30  ? 592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 126.963 136.412 163.579 1.00 35.21  ? 592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.382 135.223 162.217 1.00 32.76  ? 592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 128.098 138.308 163.086 1.00 27.04  ? 593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.922 139.162 162.943 1.00 21.42  ? 593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 126.041 139.124 164.184 1.00 29.56  ? 593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.501 138.769 165.274 1.00 31.71  ? 593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 126.116 138.751 161.707 1.00 30.60  ? 593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 125.097 139.692 161.422 1.00 29.12  ? 593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.772 139.494 164.028 1.00 35.29  ? 594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.803 139.415 165.113 1.00 24.60  ? 594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.088 138.074 165.027 1.00 25.56  ? 594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 122.113 137.826 165.746 1.00 26.96  ? 594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.804 140.585 165.062 1.00 21.21  ? 594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 123.524 141.904 165.289 1.00 20.60  ? 594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 122.070 140.596 163.733 1.00 23.25  ? 594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.569 137.203 164.144 1.00 29.39  ? 595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 122.986 135.883 163.996 1.00 31.23  ? 595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.319 135.011 165.206 1.00 33.84  ? 595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.371 135.172 165.829 1.00 35.30  ? 595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.501 135.208 162.728 1.00 30.27  ? 595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 122.834 135.659 161.439 1.00 29.61  ? 595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 121.064 135.942 161.599 1.00 34.49  ? 595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.014 137.730 161.579 1.00 29.54  ? 595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 122.436 134.081 165.559 1.00 33.10  ? 596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 122.782 133.088 166.579 1.00 29.16  ? 596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 123.831 132.115 166.062 1.00 34.17  ? 596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 123.989 131.905 164.857 1.00 39.49  ? 596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 121.452 132.381 166.858 1.00 30.82  ? 596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 120.633 132.615 165.637 1.00 34.33  ? 596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 121.044 133.948 165.099 1.00 32.07  ? 596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 124.560 131.518 167.005 1.00 35.52  ? 597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 125.680 130.655 166.653 1.00 37.60  ? 597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 125.174 129.387 165.978 1.00 44.06  ? 597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 124.160 128.801 166.384 1.00 46.17  ? 597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 126.519 130.331 167.900 1.00 35.64  ? 597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 125.690 129.556 168.926 1.00 37.12  ? 597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 127.055 131.608 168.520 1.00 40.34  ? 597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 126.511 128.702 169.853 1.00 36.45  ? 597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 125.870 128.969 164.920 1.00 45.94  ? 598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 125.511 127.730 164.239 1.00 47.56  ? 598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 125.887 126.514 165.076 1.00 49.33  ? 598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 125.083 125.591 165.248 1.00 49.30  ? 598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 126.189 127.669 162.871 1.00 46.64  ? 598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 125.281 128.018 161.710 1.00 47.41  ? 598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 126.179 128.753 160.332 1.00 59.57  ? 598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 127.493 127.557 160.109 1.00 47.81  ? 598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 127.109 126.497 165.606 1.00 50.00  ? 599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 127.610 125.376 166.388 1.00 46.67  ? 599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 128.303 125.902 167.634 1.00 47.33  ? 599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 128.972 126.937 167.588 1.00 52.41  ? 599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 128.589 124.513 165.579 1.00 47.02  ? 599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 128.104 124.138 164.189 1.00 52.43  ? 599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 129.187 124.270 163.139 1.00 57.57  ? 599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 129.983 123.321 162.982 1.00 58.12  ? 599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 129.244 125.324 162.472 1.00 57.60  ? 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 128.162 125.202 168.764 1.00 48.64  ? 600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 128.857 125.567 170.005 1.00 47.76  ? 600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 130.355 125.429 169.856 1.00 48.72  ? 600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 131.109 126.289 170.285 1.00 52.62  ? 600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 128.404 124.676 171.157 1.00 49.05  ? 600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 127.013 125.058 171.649 1.00 47.86  ? 600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 126.689 124.228 172.873 1.00 49.04  ? 600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 125.353 124.567 173.360 1.00 50.70  ? 600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 124.272 123.818 173.283 1.00 52.76  ? 600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 123.147 124.271 173.730 1.00 50.71  ? 600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.272 122.628 172.787 1.00 52.60  ? 600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 130.802 124.371 169.198 1.00 53.41  ? 601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 132.222 124.156 168.942 1.00 51.51  ? 601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 132.353 123.852 167.456 1.00 49.25  ? 601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 132.040 122.742 167.011 1.00 53.68  ? 601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 132.811 123.026 169.791 1.00 51.97  ? 601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 132.528 123.267 171.275 1.00 52.09  ? 601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 134.305 122.913 169.552 1.00 53.09  ? 601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 132.993 122.148 172.172 1.00 50.62  ? 601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 132.812 124.832 166.683 1.00 56.28  ? 602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 132.962 124.646 165.247 1.00 60.22  ? 602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 134.103 123.682 164.946 1.00 63.83  ? 602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 135.184 123.770 165.534 1.00 66.91  ? 602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 133.218 125.988 164.563 1.00 62.34  ? 602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 131.964 126.806 164.313 1.00 64.30  ? 602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 132.261 128.133 163.644 1.00 65.68  ? 602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.449 128.413 163.378 1.00 65.39  ? 602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 131.306 128.896 163.385 1.00 61.58  ? 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 133.855 122.759 164.024 1.00 67.89  ? 603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 134.864 121.817 163.562 1.00 68.82  ? 603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 135.374 122.282 162.204 1.00 70.47  ? 603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 134.603 122.361 161.241 1.00 69.97  ? 603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 134.292 120.403 163.468 1.00 69.34  ? 603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.241 119.314 163.938 1.00 69.86  ? 603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 134.610 117.936 163.894 1.00 72.89  ? 603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.558 117.783 163.239 1.00 70.56  ? 603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 135.166 117.006 164.514 1.00 72.95  ? 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 136.666 122.587 162.130 1.00 68.99  ? 604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 137.278 123.100 160.914 1.00 69.17  ? 604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 138.528 122.297 160.595 1.00 70.13  ? 604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 139.313 121.972 161.490 1.00 70.29  ? 604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 137.633 124.585 161.053 1.00 71.55  ? 604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 136.445 125.525 160.950 1.00 70.71  ? 604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 135.564 125.177 159.762 1.00 70.46  ? 604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 134.268 124.657 160.180 1.00 72.11  ? 604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 133.193 125.405 160.389 1.00 71.70  ? 604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 132.059 124.822 160.767 1.00 70.73  ? 604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.224 126.718 160.229 1.00 67.93  ? 604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 138.709 121.983 159.315 1.00 77.06  ? 605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 139.868 121.242 158.832 1.00 78.98  ? 605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 140.708 122.177 157.972 1.00 75.98  ? 605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 140.261 122.619 156.908 1.00 74.22  ? 605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 139.442 120.009 158.039 1.00 77.84  ? 605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 138.727 119.109 158.894 1.00 75.02  ? 605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 140.662 119.297 157.473 1.00 76.57  ? 605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 141.924 122.476 158.431 1.00 76.85  ? 606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 142.875 123.313 157.699 1.00 80.11  ? 606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 144.119 122.463 157.461 1.00 80.17  ? 606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 145.012 122.400 158.310 1.00 77.70  ? 606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 143.190 124.594 158.466 1.00 77.28  ? 606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 141.973 125.445 158.743 1.00 76.73  ? 606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 141.155 125.879 157.708 1.00 75.19  ? 606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 141.634 125.807 160.040 1.00 77.12  ? 606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 140.039 126.653 157.955 1.00 75.92  ? 606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 140.520 126.581 160.298 1.00 78.36  ? 606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 139.726 127.001 159.252 1.00 78.68  ? 606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 138.614 127.771 159.501 1.00 77.44  ? 606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 144.171 121.808 156.304 1.00 83.26  ? 607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 145.234 120.867 156.019 1.00 81.75  ? 607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 144.811 119.442 156.306 1.00 84.76  ? 607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 143.699 119.037 155.954 1.00 85.60  ? 607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 145.690 118.668 156.942 1.00 90.09  ? 608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 145.379 117.306 157.353 1.00 91.63  ? 608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 145.028 117.214 158.832 1.00 89.54  ? 608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 144.990 116.113 159.390 1.00 86.84  ? 608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 146.549 116.376 157.029 1.00 89.81  ? 608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 146.095 115.049 156.458 1.00 90.21  ? 608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 144.940 114.895 156.061 1.00 89.28  ? 608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 147.002 114.082 156.415 1.00 88.80  ? 608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 144.770 118.348 159.476 1.00 86.29  ? 609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 144.457 118.400 160.894 1.00 85.62  ? 609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 143.172 119.185 161.111 1.00 84.78  ? 609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 142.966 120.242 160.502 1.00 83.69  ? 609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 145.599 119.042 161.683 1.00 83.27  ? 609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 146.000 120.261 161.078 1.00 83.54  ? 609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 142.317 118.664 161.987 1.00 76.63  ? 610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 141.084 119.339 162.366 1.00 74.44  ? 610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 141.369 120.316 163.498 1.00 74.96  ? 610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 142.146 120.014 164.407 1.00 74.61  ? 610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 140.024 118.328 162.796 1.00 74.98  ? 610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 139.330 117.635 161.633 1.00 77.55  ? 610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 138.103 116.812 162.046 1.00 75.88  ? 610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 138.202 116.105 163.407 1.00 75.69  ? 610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 139.536 115.532 163.776 1.00 75.25  ? 610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 140.742 121.485 163.437 1.00 73.60  ? 611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 140.963 122.559 164.403 1.00 71.47  ? 611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 139.611 122.984 164.969 1.00 70.58  ? 611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 138.828 123.653 164.288 1.00 71.26  ? 611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 141.685 123.735 163.753 1.00 73.72  ? 611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 140.897 124.232 162.664 1.00 74.14  ? 611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.045 123.300 163.229 1.00 72.37  ? 611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 139.338 122.593 166.211 1.00 66.72  ? 612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 138.068 122.915 166.846 1.00 66.30  ? 612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 138.085 124.347 167.361 1.00 67.20  ? 612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 139.078 124.798 167.939 1.00 67.83  ? 612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 137.778 121.949 167.993 1.00 65.58  ? 612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 138.025 120.501 167.646 1.00 67.24  ? 612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 137.029 119.725 167.070 1.00 66.32  ? 612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 139.249 119.903 167.912 1.00 67.07  ? 612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 137.252 118.399 166.754 1.00 66.81  ? 612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 139.478 118.580 167.603 1.00 68.18  ? 612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 138.478 117.832 167.024 1.00 68.73  ? 612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 138.708 116.510 166.717 1.00 68.11  ? 612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 136.985 125.060 167.147 1.00 58.77  ? 613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 136.828 126.426 167.645 1.00 54.30  ? 613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 135.610 126.519 168.551 1.00 52.53  ? 613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 134.474 126.640 168.058 1.00 54.67  ? 613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 136.709 127.418 166.491 1.00 56.31  ? 613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 136.436 128.827 166.956 1.00 53.29  ? 613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 137.273 129.449 167.871 1.00 51.66  ? 613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 135.339 129.533 166.487 1.00 55.10  ? 613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 137.030 130.733 168.301 1.00 51.60  ? 613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 135.086 130.820 166.911 1.00 56.68  ? 613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 135.936 131.414 167.819 1.00 56.24  ? 613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 135.695 132.695 168.250 1.00 55.04  ? 613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 135.785 126.456 169.869 1.00 50.01  ? 614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 134.661 126.731 170.768 1.00 48.68  ? 614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 134.193 128.170 170.616 1.00 50.30  ? 614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 134.969 129.068 170.283 1.00 52.20  ? 614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 135.244 126.473 172.164 1.00 48.25  ? 614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 136.489 125.676 171.929 1.00 53.38  ? 614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 137.013 126.120 170.605 1.00 52.31  ? 614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 132.902 128.380 170.853 1.00 47.11  ? 615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 132.329 129.706 170.704 1.00 42.47  ? 615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 132.949 130.664 171.722 1.00 46.85  ? 615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 133.363 130.245 172.807 1.00 48.75  ? 615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 130.813 129.658 170.876 1.00 41.81  ? 615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 130.068 129.296 169.603 1.00 44.68  ? 615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 130.434 130.406 168.232 1.00 51.57  ? 615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.365 129.318 167.156 1.00 43.36  ? 615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 133.045 131.951 171.387 1.00 46.18  ? 616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 133.687 132.914 172.296 1.00 43.10  ? 616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.007 132.944 173.656 1.00 45.38  ? 616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 131.839 133.316 173.779 1.00 47.09  ? 616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 133.531 134.248 171.558 1.00 41.15  ? 616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 133.377 133.874 170.128 1.00 43.13  ? 616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 132.633 132.578 170.120 1.00 44.68  ? 616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 133.757 132.558 174.684 1.00 45.21  ? 617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 133.230 132.524 176.031 1.00 45.13  ? 617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 132.432 131.290 176.381 1.00 48.58  ? 617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 131.842 131.245 177.467 1.00 51.33  ? 617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 132.384 130.295 175.499 1.00 49.61  ? 618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 131.671 129.062 175.799 1.00 48.47  ? 618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 132.316 128.347 176.977 1.00 50.34  ? 618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 133.538 128.188 177.037 1.00 54.97  ? 618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 131.653 128.147 174.575 1.00 48.01  ? 618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 130.904 126.820 174.716 1.00 47.68  ? 618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 129.407 127.052 174.819 1.00 51.02  ? 618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 131.226 125.899 173.553 1.00 48.86  ? 618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 131.486 127.916 177.919 1.00 52.79  ? 619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 131.955 127.228 179.114 1.00 55.24  ? 619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 130.830 126.328 179.614 1.00 55.14  ? 619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 129.814 126.139 178.936 1.00 57.03  ? 619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 132.413 128.230 180.178 1.00 52.29  ? 619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 131.015 125.766 180.809 1.00 58.84  ? 620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 130.009 124.868 181.366 1.00 59.15  ? 620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 128.810 125.637 181.906 1.00 61.14  ? 620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 127.668 125.174 181.795 1.00 59.34  ? 620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 130.631 124.006 182.463 1.00 63.00  ? 620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 131.879 123.479 182.048 1.00 64.37  ? 620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 129.045 126.813 182.493 1.00 62.64  ? 621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 127.954 127.556 183.116 1.00 61.45  ? 621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 127.041 128.202 182.082 1.00 60.08  ? 621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 125.861 128.440 182.364 1.00 60.33  ? 621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 128.513 128.616 184.064 1.00 60.22  ? 621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 129.686 129.368 183.473 1.00 63.46  ? 621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 130.545 128.783 182.816 1.00 63.68  ? 621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 129.728 130.674 183.704 1.00 60.97  ? 621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 127.556 128.493 180.888 1.00 52.95  ? 622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 126.773 129.119 179.830 1.00 54.87  ? 622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 126.656 128.213 178.607 1.00 55.31  ? 622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 126.603 128.693 177.473 1.00 57.15  ? 622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 127.368 130.473 179.446 1.00 53.37  ? 622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 128.824 130.381 179.030 1.00 56.39  ? 622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 129.377 129.291 178.891 1.00 58.05  ? 622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 129.454 131.532 178.831 1.00 54.98  ? 622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 126.653 126.891 178.767 1.00 51.26  ? 623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 126.533 125.979 177.624 1.00 51.61  ? 623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 125.165 126.109 176.950 1.00 52.90  ? 623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 125.060 126.406 175.759 1.00 51.56  ? 623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 126.804 124.548 178.084 1.00 56.18  ? 623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 126.647 123.522 177.015 1.00 53.87  ? 623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 125.477 122.959 176.655 1.00 52.09  ? 623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 127.650 122.961 176.121 1.00 52.07  ? 623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 125.682 122.091 175.606 1.00 56.74  ? 623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 126.997 122.066 175.226 1.00 55.64  ? 623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 129.043 123.098 175.978 1.00 51.10  ? 623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 127.675 121.380 174.214 1.00 52.95  ? 623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 129.734 122.382 174.984 1.00 55.54  ? 623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 129.060 121.544 174.091 1.00 55.48  ? 623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 124.087 126.001 177.719 1.00 54.88  ? 624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 122.716 126.084 177.199 1.00 54.86  ? 624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 122.246 127.507 176.896 1.00 54.52  ? 624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 121.159 127.697 176.348 1.00 57.66  ? 624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 121.756 125.344 178.129 1.00 53.85  ? 624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 121.987 123.854 178.097 1.00 55.69  ? 624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 121.524 123.104 177.004 1.00 53.58  ? 624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 122.734 123.232 179.105 1.00 56.52  ? 624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 121.817 121.738 176.910 1.00 53.02  ? 624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 123.005 121.861 179.024 1.00 56.82  ? 624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 122.559 121.114 177.923 1.00 56.42  ? 624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 123.026 128.532 177.246 1.00 43.37  ? 625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 122.790 129.872 176.710 1.00 39.55  ? 625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 123.306 129.992 175.278 1.00 38.78  ? 625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 122.674 130.656 174.458 1.00 41.58  ? 625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 123.419 130.936 177.609 1.00 37.01  ? 625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 122.680 131.210 178.897 1.00 35.38  ? 625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 121.377 131.726 178.855 1.00 37.03  ? 625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 123.311 131.033 180.137 1.00 38.28  ? 625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 120.703 132.043 180.048 1.00 38.48  ? 625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 122.637 131.327 181.331 1.00 41.60  ? 625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 121.334 131.848 181.285 1.00 41.38  ? 625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 124.387 129.296 174.932 1.00 37.64  ? 626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 124.910 129.253 173.574 1.00 40.78  ? 626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 124.120 128.251 172.744 1.00 41.51  ? 626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 124.698 127.343 172.139 1.00 45.35  ? 626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 126.395 128.890 173.578 1.00 40.89  ? 626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 127.305 130.074 173.797 1.00 40.60  ? 626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 127.562 130.975 172.773 1.00 40.68  ? 626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 127.907 130.290 175.027 1.00 40.50  ? 626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 128.391 132.059 172.971 1.00 40.27  ? 626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 128.739 131.370 175.234 1.00 41.68  ? 626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 128.975 132.251 174.202 1.00 45.03  ? 626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 129.802 133.329 174.406 1.00 47.24  ? 626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 122.792 128.326 172.757 1.00 43.75  ? 627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 121.946 127.386 172.025 1.00 44.40  ? 627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 122.123 127.565 170.521 1.00 44.84  ? 627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 121.987 128.665 169.999 1.00 46.32  ? 627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 120.507 127.550 172.510 1.00 45.46  ? 627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 119.537 126.745 171.648 1.00 45.05  ? 627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 118.102 126.936 172.114 1.00 44.71  ? 627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 117.248 126.073 171.190 1.00 49.46  ? 627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 115.805 126.184 171.453 1.00 47.30  ? 627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 122.384 126.472 169.821 1.00 48.08  ? 628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 122.671 126.474 168.396 1.00 47.15  ? 628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 121.484 127.014 167.608 1.00 48.52  ? 628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 120.323 126.788 167.957 1.00 51.28  ? 628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 123.025 125.067 167.916 1.00 49.26  ? 628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 124.372 124.569 168.412 1.00 52.38  ? 628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 124.710 123.187 167.887 1.00 55.14  ? 628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 124.101 122.767 166.880 1.00 54.77  ? 628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 125.586 122.523 168.479 1.00 49.65  ? 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 121.793 127.734 166.528 1.00 45.76  ? 629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 120.760 128.417 165.758 1.00 43.07  ? 629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 119.755 127.445 165.154 1.00 50.23  ? 629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 118.587 127.802 164.964 1.00 51.44  ? 629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 121.403 129.258 164.659 1.00 40.61  ? 629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 120.186 126.222 164.841 1.00 56.60  ? 630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 119.277 125.255 164.237 1.00 50.94  ? 630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 118.228 124.768 165.229 1.00 54.08  ? 630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 117.094 124.479 164.835 1.00 56.78  ? 630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 120.067 124.077 163.672 1.00 50.53  ? 630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 121.058 124.474 162.605 1.00 49.71  ? 630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 120.636 124.790 161.322 1.00 51.44  ? 630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 122.417 124.531 162.881 1.00 49.25  ? 630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 121.539 125.153 160.344 1.00 52.10  ? 630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 123.326 124.892 161.909 1.00 50.89  ? 630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 122.882 125.202 160.642 1.00 54.14  ? 630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 123.785 125.563 159.669 1.00 52.44  ? 630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 118.585 124.670 166.509 1.00 51.71  ? 631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 117.642 124.238 167.531 1.00 50.83  ? 631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 116.693 125.345 167.968 1.00 52.94  ? 631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 115.726 125.061 168.683 1.00 53.18  ? 631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 118.397 123.707 168.752 1.00 52.39  ? 631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 119.512 122.750 168.377 1.00 58.82  ? 631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 119.405 122.094 167.319 1.00 59.32  ? 631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 120.495 122.655 169.141 1.00 58.78  ? 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 116.938 126.585 167.559 1.00 50.36  ? 632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 116.135 127.717 167.994 1.00 49.75  ? 632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 114.894 127.876 167.128 1.00 49.79  ? 632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 114.868 127.481 165.959 1.00 51.70  ? 632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 116.953 129.008 167.953 1.00 45.74  ? 632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.206 128.972 168.795 1.00 48.20  ? 632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 119.085 130.540 168.795 1.00 51.12  ? 632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 119.359 130.746 170.550 1.00 46.81  ? 632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 113.860 128.466 167.720 1.00 40.38  ? 633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 112.661 128.822 166.974 1.00 36.97  ? 633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 112.986 129.966 166.023 1.00 42.54  ? 633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 113.415 131.039 166.459 1.00 48.71  ? 633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 111.542 129.217 167.934 1.00 39.03  ? 633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 110.213 129.427 167.233 1.00 47.07  ? 633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 110.125 129.160 166.016 1.00 46.46  ? 633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 109.254 129.864 167.901 1.00 45.76  ? 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 112.788 129.737 164.724 1.00 37.28  ? 634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 113.086 130.773 163.744 1.00 30.81  ? 634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 112.168 131.978 163.877 1.00 27.89  ? 634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 112.551 133.077 163.470 1.00 32.16  ? 634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 113.005 130.205 162.329 1.00 35.50  ? 634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 114.328 129.669 161.823 1.00 38.18  ? 634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 115.572 130.968 161.717 1.00 49.29  ? 634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 116.878 130.256 162.711 1.00 36.76  ? 634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 110.971 131.799 164.439 1.00 35.16  ? 635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 110.106 132.944 164.702 1.00 35.58  ? 635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 110.731 133.872 165.737 1.00 32.86  ? 635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 110.653 135.099 165.612 1.00 35.98  ? 635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 108.728 132.468 165.160 1.00 36.94  ? 635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 107.807 132.093 164.032 1.00 31.40  ? 635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 108.300 131.493 162.884 1.00 27.12  ? 635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 106.449 132.338 164.122 1.00 33.09  ? 635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 107.455 131.149 161.849 1.00 33.76  ? 635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 105.600 131.994 163.088 1.00 37.60  ? 635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 106.104 131.399 161.951 1.00 37.51  ? 635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 111.368 133.302 166.761 1.00 32.97  ? 636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.040 134.122 167.762 1.00 34.24  ? 636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.241 134.849 167.166 1.00 35.44  ? 636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 113.514 136.002 167.518 1.00 42.34  ? 636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 112.463 133.255 168.947 1.00 36.42  ? 636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.322 132.890 169.882 1.00 35.03  ? 636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 110.437 134.090 170.166 1.00 41.00  ? 636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 108.972 133.697 170.230 1.00 41.47  ? 636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 108.085 134.886 170.359 1.00 41.25  ? 636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 113.967 134.193 166.259 1.00 30.58  ? 637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.087 134.851 165.594 1.00 27.54  ? 637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 114.588 135.977 164.696 1.00 33.67  ? 637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 115.214 137.039 164.603 1.00 36.00  ? 637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 115.921 133.821 164.811 1.00 27.62  ? 637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.172 134.470 164.251 1.00 31.56  ? 637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 116.277 132.644 165.705 1.00 33.00  ? 637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.454 135.765 164.022 1.00 35.94  ? 638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 112.845 136.831 163.231 1.00 29.99  ? 638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.455 137.997 164.127 1.00 33.52  ? 638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.646 139.164 163.771 1.00 39.72  ? 638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 111.630 136.298 162.448 1.00 28.20  ? 638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 110.835 137.452 161.873 1.00 29.12  ? 638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.071 135.357 161.344 1.00 31.15  ? 638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 111.888 137.698 165.298 1.00 31.62  ? 639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.535 138.752 166.243 1.00 29.82  ? 639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.768 139.537 166.673 1.00 32.78  ? 639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.740 140.773 166.731 1.00 39.75  ? 639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 110.835 138.147 167.460 1.00 35.37  ? 639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 109.336 138.353 167.434 1.00 42.83  ? 639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.773 138.482 166.329 1.00 43.14  ? 639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 108.721 138.384 168.520 1.00 41.29  ? 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.864 138.833 166.958 1.00 30.31  ? 640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.110 139.498 167.332 1.00 30.36  ? 640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 115.615 140.404 166.218 1.00 32.74  ? 640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.991 141.557 166.460 1.00 35.54  ? 640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.171 138.459 167.689 1.00 29.56  ? 640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 117.543 139.056 167.928 1.00 29.09  ? 640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 117.634 140.041 169.428 1.00 29.28  ? 640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.609 138.958 170.460 1.00 34.32  ? 640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.634 139.898 164.984 1.00 28.19  ? 641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 116.185 140.676 163.881 1.00 20.56  ? 641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 115.299 141.878 163.580 1.00 21.88  ? 641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 115.794 142.968 163.270 1.00 30.23  ? 641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 116.390 139.785 162.643 1.00 26.30  ? 641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 117.392 138.673 162.953 1.00 27.27  ? 641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.894 140.604 161.470 1.00 25.90  ? 641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.580 139.127 163.773 1.00 28.59  ? 641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.977 141.708 163.678 1.00 19.27  ? 642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 113.070 142.832 163.483 1.00 24.15  ? 642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 113.217 143.864 164.590 1.00 30.29  ? 642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.042 145.063 164.346 1.00 30.39  ? 642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 111.627 142.336 163.405 1.00 25.74  ? 642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 113.523 143.420 165.811 1.00 26.28  ? 643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 113.846 144.360 166.877 1.00 24.32  ? 643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 115.121 145.130 166.556 1.00 34.28  ? 643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 115.204 146.340 166.796 1.00 38.40  ? 643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 113.982 143.616 168.204 1.00 23.86  ? 643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 112.771 142.900 168.474 1.00 37.52  ? 643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 114.240 144.589 169.329 1.00 26.60  ? 643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 116.129 144.441 166.020 1.00 25.87  ? 644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 117.358 145.115 165.613 1.00 15.14  ? 644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.117 145.978 164.380 1.00 22.83  ? 644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 117.639 147.096 164.278 1.00 26.98  ? 644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 118.475 144.086 165.364 1.00 19.36  ? 644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 118.729 143.252 166.617 1.00 20.32  ? 644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 119.748 144.778 164.921 1.00 20.03  ? 644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 119.550 142.017 166.354 1.00 27.16  ? 644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 116.328 145.477 163.427 1.00 17.65  ? 645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 116.194 146.145 162.136 1.00 17.56  ? 645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 115.549 147.519 162.264 1.00 25.85  ? 645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 115.833 148.413 161.458 1.00 30.70  ? 645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 115.386 145.270 161.176 1.00 20.10  ? 645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 115.216 145.855 159.788 1.00 19.48  ? 645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 116.423 145.615 158.909 1.00 25.77  ? 645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 116.616 144.518 158.387 1.00 27.67  ? 645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.248 146.642 158.744 1.00 18.89  ? 645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 114.691 147.715 163.267 1.00 32.89  ? 646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.031 149.005 163.426 1.00 28.86  ? 646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.011 150.119 163.769 1.00 24.93  ? 646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.663 151.295 163.631 1.00 29.06  ? 646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 112.944 148.913 164.496 1.00 29.75  ? 646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 113.468 148.850 165.915 1.00 30.35  ? 646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 112.398 148.453 166.910 1.00 34.33  ? 646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.484 147.403 167.545 1.00 36.21  ? 646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 111.381 149.293 167.051 1.00 32.19  ? 646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.224 149.779 164.199 1.00 27.51  ? 647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.256 150.763 164.486 1.00 16.75  ? 647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.374 150.763 163.457 1.00 21.75  ? 647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.366 151.475 163.640 1.00 33.43  ? 647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 117.838 150.524 165.882 1.00 21.44  ? 647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 116.808 150.499 166.966 1.00 22.98  ? 647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 115.931 151.540 167.180 1.00 20.68  ? 647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 116.512 149.561 167.895 1.00 23.00  ? 647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.141 151.244 168.195 1.00 24.22  ? 647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 115.472 150.049 168.647 1.00 23.79  ? 647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.244 149.987 162.386 1.00 22.46  ? 648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.233 149.925 161.318 1.00 20.93  ? 648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 118.582 150.477 160.059 1.00 22.87  ? 648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 117.540 149.973 159.620 1.00 28.07  ? 648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 119.739 148.489 161.101 1.00 9.95   ? 648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 120.290 147.913 162.407 1.00 19.00  ? 648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 120.804 148.454 160.026 1.00 15.48  ? 648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 121.488 148.656 162.948 1.00 17.86  ? 648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.186 151.518 159.481 1.00 16.32  ? 649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 118.601 152.136 158.297 1.00 16.24  ? 649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 118.753 151.252 157.066 1.00 22.51  ? 649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 117.871 151.240 156.201 1.00 38.41  ? 649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.228 153.508 158.050 1.00 25.14  ? 649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 120.735 153.486 158.156 1.00 24.97  ? 649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 121.270 152.559 158.793 1.00 28.24  ? 649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.383 154.397 157.604 1.00 25.83  ? 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 119.856 150.520 156.965 1.00 12.54  ? 650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.034 149.532 155.914 1.00 13.66  ? 650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 119.558 148.172 156.422 1.00 14.04  ? 650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 118.886 148.068 157.450 1.00 23.80  ? 650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 121.486 149.495 155.452 1.00 15.10  ? 650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 121.994 150.804 154.881 1.00 15.23  ? 650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.418 150.699 154.386 1.00 21.68  ? 650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 123.675 150.163 153.311 1.00 17.75  ? 650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.356 151.212 155.171 1.00 19.69  ? 650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 119.894 147.110 155.694 1.00 10.92  ? 651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 119.434 145.782 156.034 1.00 18.24  ? 651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 120.353 145.049 156.990 1.00 17.58  ? 651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 121.372 145.559 157.452 1.00 20.11  ? 651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 119.960 143.814 157.290 1.00 20.84  ? 652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 120.716 142.908 158.143 1.00 21.10  ? 652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 120.843 141.583 157.409 1.00 24.45  ? 652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 119.862 141.091 156.838 1.00 26.71  ? 652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.033 142.702 159.509 1.00 13.08  ? 652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 119.771 144.045 160.190 1.00 4.36   ? 652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.878 141.809 160.402 1.00 13.35  ? 652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.060 143.917 161.505 1.00 10.10  ? 652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.042 141.005 157.418 1.00 16.85  ? 653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 122.231 139.709 156.781 1.00 13.46  ? 653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.573 138.625 157.620 1.00 29.61  ? 653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.223 137.995 158.461 1.00 33.34  ? 653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 123.714 139.407 156.579 1.00 17.87  ? 653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.142 139.822 155.296 1.00 16.84  ? 653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 120.282 138.407 157.392 1.00 24.89  ? 654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.491 137.474 158.183 1.00 14.47  ? 654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.548 136.104 157.521 1.00 15.52  ? 654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 118.971 135.897 156.450 1.00 29.76  ? 654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.055 137.974 158.309 1.00 20.70  ? 654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.185 137.123 159.184 1.00 21.66  ? 654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 117.738 136.282 160.135 1.00 25.86  ? 654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 115.810 137.169 159.060 1.00 23.80  ? 654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 116.937 135.502 160.935 1.00 21.66  ? 654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.006 136.393 159.860 1.00 28.97  ? 654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 115.570 135.559 160.801 1.00 20.83  ? 654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.237 135.168 158.165 1.00 27.01  ? 655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 120.341 133.796 157.691 1.00 31.31  ? 655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 119.317 132.938 158.421 1.00 31.94  ? 655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 119.199 133.014 159.648 1.00 34.18  ? 655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 121.750 133.247 157.918 1.00 36.73  ? 655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 122.698 134.047 157.202 1.00 43.58  ? 655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 121.847 131.810 157.443 1.00 28.48  ? 655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 118.572 132.136 157.667 1.00 36.27  ? 656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 117.603 131.218 158.247 1.00 38.18  ? 656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 118.266 129.869 158.488 1.00 39.63  ? 656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 118.807 129.261 157.560 1.00 44.88  ? 656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 116.390 131.059 157.332 1.00 37.27  ? 656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 115.493 132.290 157.203 1.00 39.37  ? 656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 114.246 131.972 156.394 1.00 39.44  ? 656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 115.122 132.831 158.573 1.00 37.76  ? 656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 118.224 129.409 159.732 1.00 36.74  ? 657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 118.827 128.142 160.130 1.00 39.83  ? 657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 117.700 127.138 160.330 1.00 45.33  ? 657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 116.942 127.232 161.302 1.00 48.36  ? 657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 119.664 128.311 161.395 1.00 43.62  ? 657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 120.651 129.441 161.319 1.00 46.68  ? 657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 120.291 130.721 161.714 1.00 46.38  ? 657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.932 129.231 160.844 1.00 44.51  ? 657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 121.193 131.762 161.647 1.00 41.33  ? 657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.838 130.272 160.770 1.00 46.14  ? 657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 122.467 131.537 161.172 1.00 45.84  ? 657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 117.594 126.182 159.414 1.00 51.67  ? 658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 116.470 125.262 159.365 1.00 51.61  ? 658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 116.937 123.837 159.612 1.00 54.68  ? 658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 118.079 123.477 159.315 1.00 58.49  ? 658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 115.759 125.340 158.011 1.00 51.17  ? 658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 115.726 126.717 157.348 1.00 52.00  ? 658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 115.464 126.576 155.861 1.00 49.63  ? 658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 114.682 127.608 157.998 1.00 51.99  ? 658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 116.041 123.029 160.166 1.00 56.66  ? 659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 116.280 121.605 160.325 1.00 58.31  ? 659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 115.755 120.846 159.111 1.00 59.63  ? 659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 114.879 121.317 158.382 1.00 56.94  ? 659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 115.619 121.081 161.600 1.00 55.83  ? 659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 116.222 121.625 162.881 1.00 55.17  ? 659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 115.936 120.703 164.054 1.00 58.38  ? 659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 116.672 121.155 165.305 1.00 57.76  ? 659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 116.870 120.034 166.265 1.00 58.23  ? 659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 116.312 119.653 158.896 1.00 68.04  ? 660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 115.871 118.818 157.785 1.00 68.84  ? 660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 114.443 118.322 157.967 1.00 67.46  ? 660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 113.787 117.982 156.977 1.00 66.52  ? 660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 116.817 117.630 157.612 1.00 67.61  ? 660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 117.668 117.741 156.363 1.00 70.80  ? 660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 117.383 118.623 155.525 1.00 67.52  ? 660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.621 116.947 156.219 1.00 70.58  ? 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 113.949 118.271 159.207 1.00 65.45  ? 661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 112.584 117.818 159.444 1.00 65.46  ? 661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 111.557 118.800 158.896 1.00 64.85  ? 661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 110.495 118.381 158.421 1.00 63.02  ? 661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 112.353 117.597 160.939 1.00 65.56  ? 661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 112.674 118.795 161.656 1.00 63.46  ? 661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 113.221 116.457 161.448 1.00 64.20  ? 661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 111.845 120.097 158.955 1.00 63.92  ? 662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 110.887 121.092 158.495 1.00 63.27  ? 662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 110.769 121.069 156.974 1.00 63.42  ? 662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 111.732 120.797 156.252 1.00 60.98  ? 662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 111.284 122.486 158.988 1.00 60.18  ? 662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 111.970 123.369 157.963 1.00 62.42  ? 662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 112.158 125.063 158.550 1.00 76.44  ? 662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 112.812 124.782 160.193 1.00 58.97  ? 662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 109.556 121.338 156.493 1.00 57.15  ? 663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 109.245 121.261 155.072 1.00 55.16  ? 663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 109.410 122.615 154.393 1.00 53.83  ? 663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 109.924 123.561 154.997 1.00 54.97  ? 663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 107.819 120.748 154.872 1.00 52.97  ? 663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 106.899 121.836 155.018 1.00 54.02  ? 663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 107.494 119.678 155.901 1.00 54.47  ? 663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 108.976 122.718 153.135 1.00 47.97  ? 664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 108.957 123.987 152.422 1.00 48.18  ? 664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 107.863 124.911 152.934 1.00 44.43  ? 664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 108.002 126.134 152.837 1.00 48.70  ? 664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 108.786 123.763 150.918 1.00 47.73  ? 664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 107.489 123.214 150.657 1.00 48.18  ? 664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 109.853 122.817 150.392 1.00 49.99  ? 664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 106.781 124.359 153.480 1.00 45.23  ? 665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 105.763 125.169 154.133 1.00 46.39  ? 665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 106.277 125.861 155.383 1.00 50.39  ? 665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 105.903 127.008 155.634 1.00 52.11  ? 665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 104.544 124.316 154.500 1.00 46.31  ? 665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 103.287 125.128 154.757 1.00 43.86  ? 665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 102.340 124.400 155.693 1.00 46.19  ? 665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 102.817 124.410 157.070 1.00 49.59  ? 665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.070 124.724 158.119 1.00 50.50  ? 665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 102.610 124.695 159.334 1.00 47.06  ? 665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 100.797 125.062 157.985 1.00 49.59  ? 665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 107.124 125.196 156.171 1.00 47.65  ? 666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 107.737 125.859 157.316 1.00 44.11  ? 666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 108.648 126.996 156.870 1.00 47.74  ? 666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 108.662 128.068 157.488 1.00 50.87  ? 666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 108.509 124.842 158.156 1.00 48.36  ? 666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 107.596 123.872 158.879 1.00 52.85  ? 666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 106.505 124.295 159.317 1.00 50.92  ? 666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 107.967 122.687 159.009 1.00 52.21  ? 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 109.413 126.781 155.798 1.00 45.24  ? 667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 110.252 127.847 155.258 1.00 39.48  ? 667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 109.408 129.017 154.772 1.00 36.29  ? 667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 109.752 130.180 155.010 1.00 42.03  ? 667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 111.120 127.302 154.124 1.00 38.79  ? 667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 112.260 128.177 153.597 1.00 41.25  ? 667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 112.835 129.063 154.690 1.00 46.27  ? 667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.346 127.315 152.981 1.00 40.01  ? 667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 108.295 128.730 154.092 1.00 37.09  ? 668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 107.404 129.797 153.646 1.00 32.88  ? 668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 106.781 130.527 154.828 1.00 39.16  ? 668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 106.592 131.746 154.781 1.00 41.99  ? 668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 106.319 129.227 152.734 1.00 36.35  ? 668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 106.747 129.177 151.284 1.00 41.32  ? 668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.563 129.983 150.837 1.00 40.67  ? 668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 106.196 128.227 150.538 1.00 43.83  ? 668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 106.441 129.795 155.890 1.00 46.04  ? 669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 105.892 130.430 157.084 1.00 43.03  ? 669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 106.910 131.361 157.727 1.00 39.65  ? 669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 106.564 132.465 158.157 1.00 44.04  ? 669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 105.434 129.370 158.083 1.00 40.29  ? 669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 104.085 128.761 157.769 1.00 41.59  ? 669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 103.643 127.818 158.874 1.00 45.18  ? 669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 103.738 128.425 160.197 1.00 42.68  ? 669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 102.958 129.404 160.638 1.00 45.42  ? 669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.149 129.883 161.863 1.00 44.75  ? 669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 101.990 129.909 159.891 1.00 46.43  ? 669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 108.170 130.931 157.801 1.00 32.51  ? 670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 109.212 131.800 158.341 1.00 35.10  ? 670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 109.402 133.022 157.452 1.00 37.37  ? 670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 109.569 134.145 157.944 1.00 39.60  ? 670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 110.526 131.020 158.525 1.00 36.53  ? 670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 110.323 129.847 159.484 1.00 41.25  ? 670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 111.616 131.934 159.049 1.00 33.94  ? 670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 111.360 128.755 159.340 1.00 37.95  ? 670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 109.373 132.828 156.129 1.00 36.51  ? 671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 109.512 133.951 155.206 1.00 28.58  ? 671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.385 134.959 155.389 1.00 33.43  ? 671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.621 136.173 155.437 1.00 40.05  ? 671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 109.529 133.438 153.766 1.00 34.18  ? 671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 110.902 132.979 153.320 1.00 44.05  ? 671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 111.889 133.277 154.022 1.00 43.50  ? 671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 110.994 132.316 152.266 1.00 41.76  ? 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.148 134.472 155.503 1.00 34.25  ? 672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.004 135.363 155.645 1.00 33.15  ? 672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 105.976 136.030 157.013 1.00 33.88  ? 672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.528 137.173 157.131 1.00 40.07  ? 672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 104.707 134.595 155.400 1.00 37.28  ? 672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 104.516 134.058 153.982 1.00 34.22  ? 672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 103.443 132.984 153.958 1.00 35.71  ? 672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.176 135.187 153.022 1.00 30.47  ? 672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.432 135.333 158.056 1.00 32.12  ? 673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.544 135.960 159.367 1.00 29.39  ? 673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.601 137.055 159.356 1.00 31.87  ? 673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.413 138.114 159.964 1.00 35.27  ? 673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 106.861 134.904 160.425 1.00 27.00  ? 673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 106.905 135.439 161.836 1.00 31.23  ? 673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 105.759 135.924 162.449 1.00 28.79  ? 673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.087 135.448 162.559 1.00 32.24  ? 673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 105.791 136.412 163.738 1.00 27.23  ? 673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.130 135.935 163.849 1.00 36.17  ? 673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 106.980 136.414 164.434 1.00 34.25  ? 673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.020 136.899 165.721 1.00 34.87  ? 673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.720 136.814 158.666 1.00 32.98  ? 674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.731 137.852 158.509 1.00 27.01  ? 674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 109.172 139.054 157.764 1.00 27.11  ? 674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 109.403 140.203 158.158 1.00 34.94  ? 674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 110.948 137.283 157.779 1.00 23.05  ? 674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 108.421 138.809 156.688 1.00 31.36  ? 675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.797 139.908 155.959 1.00 31.71  ? 675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.815 140.672 156.841 1.00 34.07  ? 675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 106.758 141.906 156.799 1.00 35.54  ? 675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 107.094 139.374 154.711 1.00 34.33  ? 675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 106.238 140.388 154.021 1.00 37.13  ? 675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.886 140.507 154.260 1.00 34.21  ? 675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 106.541 141.332 153.099 1.00 25.53  ? 675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 104.393 141.480 153.516 1.00 35.18  ? 675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 105.377 141.997 152.802 1.00 32.67  ? 675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 106.035 139.951 157.649 1.00 35.02  ? 676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 105.041 140.592 158.504 1.00 36.48  ? 676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 105.685 141.359 159.651 1.00 36.00  ? 676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 105.163 142.399 160.068 1.00 36.80  ? 676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 104.065 139.541 159.036 1.00 35.82  ? 676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.430 139.906 160.342 1.00 37.20  ? 676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.842 139.375 161.544 1.00 38.76  ? 676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 102.407 140.744 160.633 1.00 35.72  ? 676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 103.104 139.872 162.521 1.00 39.10  ? 676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.227 140.707 161.994 1.00 40.68  ? 676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.812 140.873 160.167 1.00 35.43  ? 677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 107.483 141.516 161.290 1.00 30.74  ? 677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 108.370 142.680 160.871 1.00 36.85  ? 677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 108.963 143.326 161.741 1.00 41.35  ? 677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 108.313 140.490 162.064 1.00 29.95  ? 677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.482 139.501 162.858 1.00 36.62  ? 677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 107.039 140.095 164.181 1.00 34.40  ? 677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.171 140.531 164.990 1.00 40.81  ? 677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 108.366 141.777 165.397 1.00 44.10  ? 677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 109.437 142.060 166.134 1.00 42.55  ? 677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 107.520 142.746 165.087 1.00 38.31  ? 677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 108.474 142.965 159.579 1.00 30.66  ? 678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 109.276 144.072 159.110 1.00 21.92  ? 678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 110.687 143.725 158.699 1.00 24.62  ? 678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 111.502 144.638 158.520 1.00 25.15  ? 678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.008 142.438 158.550 1.00 24.16  ? 679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.338 142.055 158.095 1.00 17.59  ? 679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 112.536 142.549 156.672 1.00 19.89  ? 679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 111.666 142.381 155.810 1.00 36.54  ? 679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 112.521 140.534 158.193 1.00 19.15  ? 679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 112.382 140.074 159.645 1.00 22.87  ? 679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.867 140.117 157.630 1.00 23.22  ? 679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 113.419 140.645 160.561 1.00 22.20  ? 679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 113.685 143.176 156.424 1.00 21.33  ? 680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 113.934 143.769 155.116 1.00 21.37  ? 680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 114.468 142.741 154.126 1.00 14.81  ? 680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 113.973 142.640 152.999 1.00 25.08  ? 680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 114.909 144.937 155.256 1.00 12.79  ? 680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 114.320 146.160 155.931 1.00 6.90   ? 680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.325 147.293 155.987 1.00 13.83  ? 680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 114.829 148.424 156.865 1.00 19.68  ? 680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 115.703 149.621 156.773 1.00 14.68  ? 680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 115.477 141.972 154.527 1.00 20.66  ? 681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 116.103 140.995 153.650 1.00 16.71  ? 681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 116.332 139.699 154.411 1.00 23.14  ? 681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 116.483 139.697 155.634 1.00 29.15  ? 681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 117.442 141.500 153.089 1.00 17.61  ? 681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 118.281 141.937 154.166 1.00 33.22  ? 681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 117.229 142.650 152.126 1.00 16.21  ? 681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.358 138.595 153.669 1.00 19.76  ? 682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.699 137.282 154.202 1.00 18.69  ? 682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.874 136.742 153.402 1.00 23.44  ? 682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.805 136.657 152.171 1.00 28.73  ? 682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.503 136.317 154.151 1.00 17.53  ? 682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.254 136.998 154.710 1.00 27.40  ? 682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 115.815 135.052 154.920 1.00 26.43  ? 682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.029 136.129 154.703 1.00 28.49  ? 682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 118.950 136.382 154.101 1.00 22.41  ? 683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.198 136.053 153.421 1.00 18.41  ? 683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.209 134.610 152.930 1.00 31.28  ? 683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.233 134.354 151.723 1.00 39.09  ? 683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.381 136.313 154.358 1.00 23.37  ? 683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.742 136.146 153.721 1.00 15.58  ? 683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.910 136.266 152.349 1.00 20.27  ? 683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.862 135.881 154.495 1.00 14.84  ? 683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.151 136.117 151.766 1.00 26.19  ? 683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.106 135.732 153.921 1.00 27.31  ? 683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.245 135.851 152.556 1.00 28.40  ? 683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.484 135.704 151.979 1.00 30.17  ? 683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.170 133.650 153.847 1.00 37.47  ? 684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 120.402 132.263 153.488 1.00 31.19  ? 684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 119.438 131.368 154.247 1.00 45.03  ? 684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 118.898 131.740 155.290 1.00 46.41  ? 684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 121.848 131.842 153.782 1.00 32.08  ? 684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 122.762 131.884 152.580 1.00 33.02  ? 684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 122.373 131.337 151.367 1.00 35.87  ? 684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.017 132.470 152.662 1.00 40.39  ? 684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 123.207 131.374 150.267 1.00 40.43  ? 684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 124.858 132.513 151.568 1.00 40.19  ? 684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 124.448 131.963 150.372 1.00 44.40  ? 684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 125.284 132.003 149.280 1.00 42.90  ? 684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 119.225 130.176 153.698 1.00 42.86  ? 685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 118.439 129.126 154.337 1.00 40.23  ? 685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 119.375 127.943 154.551 1.00 44.87  ? 685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 119.519 127.085 153.677 1.00 52.90  ? 685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 117.226 128.750 153.497 1.00 43.16  ? 685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 120.015 127.903 155.715 1.00 44.64  ? 686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 120.956 126.843 156.051 1.00 48.91  ? 686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 120.198 125.665 156.645 1.00 55.19  ? 686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 119.402 125.837 157.575 1.00 53.63  ? 686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 122.015 127.351 157.029 1.00 49.33  ? 686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 122.895 128.452 156.470 1.00 53.05  ? 686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 124.158 128.617 157.296 1.00 51.90  ? 686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 124.763 127.334 157.630 1.00 53.80  ? 686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 125.806 126.812 156.997 1.00 53.73  ? 686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 126.276 125.630 157.387 1.00 51.26  ? 686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 126.388 127.440 155.988 1.00 51.31  ? 686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 120.441 124.474 156.108 1.00 61.39  ? 687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 119.792 123.258 156.572 1.00 63.57  ? 687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 120.808 122.358 157.261 1.00 63.60  ? 687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 121.941 122.209 156.794 1.00 64.08  ? 687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 119.134 122.509 155.411 1.00 64.68  ? 687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.044 122.440 154.307 1.00 65.49  ? 687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 117.864 123.220 154.970 1.00 62.76  ? 687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 120.396 121.761 158.374 1.00 62.91  ? 688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 121.268 120.876 159.137 1.00 66.50  ? 688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 120.862 119.418 158.953 1.00 67.25  ? 688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 119.706 119.053 159.170 1.00 66.50  ? 688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 121.243 121.247 160.620 1.00 60.52  ? 688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 122.190 120.428 161.478 1.00 61.00  ? 688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 122.137 120.865 162.932 1.00 62.97  ? 688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 123.120 120.076 163.779 1.00 64.34  ? 688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 123.090 120.503 165.205 1.00 64.82  ? 688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 132.661 76.049  116.279 1.00 45.99  ? 16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 132.366 76.533  114.927 1.00 45.47  ? 16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 131.382 77.702  114.871 1.00 44.13  ? 16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 131.136 78.252  113.796 1.00 44.46  ? 16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 131.829 75.383  114.072 1.00 45.90  ? 16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 132.695 74.150  114.154 1.00 47.25  ? 16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 133.937 74.291  114.185 1.00 47.99  ? 16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 132.130 73.037  114.191 1.00 49.50  ? 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 130.824 78.084  116.017 1.00 42.17  ? 17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 129.705 79.033  116.025 1.00 40.67  ? 17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 129.770 80.194  117.024 1.00 39.46  ? 17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 129.134 81.227  116.802 1.00 39.17  ? 17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 128.372 78.278  116.178 1.00 40.24  ? 17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 128.312 77.372  117.386 1.00 39.58  ? 17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 127.913 77.867  118.628 1.00 38.78  ? 17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 128.640 76.020  117.278 1.00 39.43  ? 17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 127.844 77.034  119.745 1.00 38.07  ? 17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 128.575 75.176  118.392 1.00 39.10  ? 17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 128.178 75.686  119.628 1.00 38.63  ? 17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 130.519 80.031  118.116 1.00 38.22  ? 18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 130.520 81.034  119.195 1.00 37.09  ? 18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 130.903 82.442  118.707 1.00 36.84  ? 18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 130.229 83.426  119.054 1.00 36.13  ? 18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 131.347 80.590  120.436 1.00 36.59  ? 18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 130.618 79.585  121.147 1.00 36.50  ? 18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 131.575 81.749  121.387 1.00 36.06  ? 18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 131.960 82.529  117.894 1.00 37.01  ? 19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 132.428 83.824  117.379 1.00 37.33  ? 19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 131.365 84.577  116.597 1.00 36.63  ? 19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 131.207 85.785  116.769 1.00 36.10  ? 19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 133.695 83.683  116.536 1.00 38.24  ? 19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 134.953 83.624  117.373 1.00 41.33  ? 19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 136.137 84.312  116.722 1.00 45.15  ? 19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 136.284 84.305  115.493 1.00 47.33  ? 19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 136.995 84.911  117.545 1.00 46.51  ? 19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 130.629 83.859  115.752 1.00 36.23  ? 20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 129.559 84.485  114.988 1.00 36.40  ? 20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 128.370 84.884  115.881 1.00 34.93  ? 20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 127.741 85.913  115.641 1.00 34.20  ? 20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 129.171 83.651  113.747 1.00 37.35  ? 20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 128.132 82.561  113.926 1.00 40.49  ? 20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 127.659 81.857  112.314 1.00 48.68  ? 20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 128.914 80.589  112.095 1.00 47.17  ? 20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 128.099 84.105  116.931 1.00 33.75  ? 21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 127.092 84.505  117.925 1.00 32.62  ? 21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 127.548 85.698  118.756 1.00 32.59  ? 21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 126.750 86.591  119.058 1.00 32.23  ? 21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 126.680 83.334  118.817 1.00 32.12  ? 21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 125.653 82.438  118.191 1.00 31.04  ? 21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 126.037 81.403  117.345 1.00 30.75  ? 21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 124.295 82.633  118.439 1.00 30.99  ? 21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 125.081 80.564  116.749 1.00 30.30  ? 21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 123.332 81.804  117.854 1.00 30.74  ? 21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 123.728 80.766  117.006 1.00 30.48  ? 21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 128.831 85.716  119.113 1.00 32.33  ? 22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 129.410 86.864  119.806 1.00 32.50  ? 22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 129.195 88.139  118.994 1.00 33.01  ? 22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 128.692 89.137  119.518 1.00 32.50  ? 22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 130.905 86.657  120.116 1.00 32.53  ? 22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 131.572 87.929  120.609 1.00 33.27  ? 22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 131.456 88.332  121.942 1.00 32.34  ? 22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 132.284 88.749  119.730 1.00 33.71  ? 22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 132.048 89.512  122.392 1.00 33.58  ? 22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 132.876 89.936  120.165 1.00 35.12  ? 22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 132.758 90.308  121.499 1.00 35.30  ? 22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 133.345 91.478  121.928 1.00 36.54  ? 22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 129.563 88.091  117.711 1.00 33.80  ? 23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 129.434 89.240  116.824 1.00 34.80  ? 23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 127.978 89.662  116.639 1.00 34.40  ? 23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 127.670 90.849  116.666 1.00 33.99  ? 23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 130.103 88.971  115.467 1.00 35.46  ? 23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 131.618 88.744  115.577 1.00 38.28  ? 23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 132.274 89.185  116.533 1.00 41.01  ? 23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 132.179 88.056  114.584 1.00 39.13  ? 23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 127.087 88.684  116.471 1.00 34.49  ? 24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 125.664 88.963  116.311 1.00 34.81  ? 24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 125.064 89.587  117.577 1.00 34.68  ? 24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 124.323 90.570  117.497 1.00 34.59  ? 24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 124.903 87.698  115.900 1.00 34.83  ? 24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 123.500 87.949  115.343 1.00 36.14  ? 24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 123.489 88.805  114.073 1.00 38.04  ? 24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 124.441 88.799  113.287 1.00 38.57  ? 24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 122.401 89.550  113.875 1.00 38.67  ? 24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 125.395 89.034  118.740 1.00 34.71  ? 25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 124.884 89.573  120.000 1.00 34.99  ? 25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 125.320 91.016  120.247 1.00 35.69  ? 25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 124.493 91.877  120.566 1.00 35.41  ? 25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 125.248 88.670  121.186 1.00 34.64  ? 25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 124.303 87.496  121.327 1.00 34.71  ? 25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 123.319 87.576  122.057 1.00 35.68  ? 25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 124.574 86.409  120.599 1.00 34.71  ? 25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 126.610 91.292  120.073 1.00 36.69  ? 26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 127.113 92.643  120.330 1.00 38.00  ? 26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 126.628 93.668  119.295 1.00 38.90  ? 26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 126.448 94.836  119.628 1.00 39.46  ? 26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 128.653 92.701  120.514 1.00 38.16  ? 26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 129.077 91.800  121.658 1.00 37.75  ? 26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 129.388 92.342  119.224 1.00 38.81  ? 26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 126.384 93.226  118.061 1.00 39.67  ? 27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 125.870 94.128  117.027 1.00 40.50  ? 27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 124.369 94.392  117.195 1.00 40.02  ? 27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 123.821 95.323  116.601 1.00 40.55  ? 27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 126.190 93.604  115.613 1.00 41.23  ? 27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 125.201 92.575  115.066 1.00 42.50  ? 27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 125.534 92.141  113.631 1.00 44.92  ? 27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 125.053 93.156  112.595 1.00 46.66  ? 27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 123.574 93.348  112.639 1.00 47.26  ? 27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 123.705 93.567  117.996 1.00 39.10  ? 28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 122.295 93.757  118.265 1.00 38.22  ? 28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 122.066 94.622  119.505 1.00 37.23  ? 28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 120.917 94.887  119.852 1.00 37.40  ? 28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 121.564 92.409  118.385 1.00 38.69  ? 28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 121.355 91.690  117.043 1.00 39.57  ? 28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 120.464 90.454  117.137 1.00 41.20  ? 28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 120.280 89.744  116.148 1.00 42.94  ? 28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 119.908 90.192  118.324 1.00 41.23  ? 28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 123.145 95.077  120.151 1.00 35.83  ? 29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 123.020 95.845  121.397 1.00 34.51  ? 29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 122.107 97.068  121.262 1.00 33.81  ? 29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 122.215 97.824  120.298 1.00 33.66  ? 29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 124.380 96.264  121.964 1.00 34.59  ? 29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 124.281 97.030  123.272 1.00 34.59  ? 29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 123.931 96.378  124.459 1.00 34.34  ? 29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 124.515 98.405  123.310 1.00 35.49  ? 29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 123.830 97.082  125.669 1.00 33.88  ? 29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 124.415 99.124  124.515 1.00 34.12  ? 29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 124.073 98.463  125.694 1.00 33.87  ? 29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 121.220 97.244  122.244 1.00 32.24  ? 30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 120.261 98.347  122.255 1.00 31.28  ? 30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 119.847 98.724  123.679 1.00 31.12  ? 30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 120.083 97.958  124.621 1.00 30.71  ? 30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 119.029 97.997  121.409 1.00 30.85  ? 30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 118.250 96.808  121.915 1.00 29.31  ? 30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 118.524 95.486  121.689 1.00 29.07  ? 30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 117.087 96.837  122.748 1.00 28.33  ? 30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 117.599 94.693  122.321 1.00 28.01  ? 30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 116.703 95.495  122.978 1.00 27.67  ? 30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 116.331 97.866  123.327 1.00 27.27  ? 30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 115.600 95.156  123.760 1.00 26.54  ? 30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 115.226 97.529  124.097 1.00 27.07  ? 30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 114.876 96.183  124.313 1.00 26.52  ? 30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 119.235 99.903  123.822 1.00 30.65  ? 31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 118.647 100.363 125.083 1.00 30.38  ? 31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 117.235 100.883 124.830 1.00 30.51  ? 31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 117.000 101.518 123.801 1.00 30.77  ? 31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 119.505 101.471 125.715 1.00 30.45  ? 31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 120.910 101.056 126.161 1.00 30.29  ? 31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 121.847 102.260 126.332 1.00 30.69  ? 31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 120.855 100.197 127.434 1.00 29.91  ? 31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 116.291 100.628 125.764 1.00 30.73  ? 32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 114.900 101.067 125.565 1.00 31.17  ? 32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 114.759 102.572 125.342 1.00 32.18  ? 32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 113.846 103.002 124.618 1.00 32.66  ? 32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 114.202 100.659 126.867 1.00 30.99  ? 32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 115.314 100.392 127.854 1.00 30.50  ? 32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 116.450 99.887  127.031 1.00 30.46  ? 32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 115.662 103.354 125.940 1.00 32.62  ? 33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 115.654 104.820 125.803 1.00 33.44  ? 33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 115.857 105.305 124.362 1.00 33.59  ? 33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 115.581 106.463 124.060 1.00 34.05  ? 33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 116.695 105.478 126.726 1.00 33.72  ? 33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 116.345 105.450 128.226 1.00 34.53  ? 33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 116.536 104.073 128.863 1.00 35.09  ? 33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 117.317 103.252 128.318 1.00 34.38  ? 33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 115.901 103.813 129.911 1.00 35.53  ? 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 116.338 104.422 123.484 1.00 33.82  ? 34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 116.481 104.734 122.059 1.00 34.19  ? 34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 115.115 104.913 121.380 1.00 33.83  ? 34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 115.020 105.537 120.324 1.00 33.93  ? 34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 117.268 103.636 121.320 1.00 34.52  ? 34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 118.711 103.428 121.771 1.00 36.50  ? 34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 119.493 102.530 120.817 1.00 40.03  ? 34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 120.027 103.039 119.806 1.00 42.43  ? 34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 119.584 101.314 121.076 1.00 39.35  ? 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 114.078 104.333 121.985 1.00 33.31  ? 35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 112.710 104.352 121.462 1.00 33.14  ? 35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 111.857 105.288 122.324 1.00 32.58  ? 35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 111.681 105.041 123.512 1.00 32.12  ? 35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 112.075 102.919 121.490 1.00 33.03  ? 35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 112.986 101.869 120.818 1.00 34.76  ? 35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 110.662 102.915 120.894 1.00 33.61  ? 35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 113.168 102.015 119.305 1.00 36.75  ? 35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 111.342 106.364 121.732 1.00 32.36  ? 36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 110.439 107.271 122.447 1.00 32.17  ? 36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 109.036 106.658 122.523 1.00 31.76  ? 36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 108.503 106.188 121.516 1.00 31.95  ? 36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 110.396 108.627 121.762 1.00 33.01  ? 36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 108.441 106.664 123.712 1.00 30.68  ? 37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 107.221 105.893 123.945 1.00 30.14  ? 37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 105.939 106.714 124.010 1.00 30.21  ? 37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 104.837 106.150 123.979 1.00 29.91  ? 37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 107.371 105.029 125.203 1.00 29.46  ? 37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 108.396 103.890 125.108 1.00 29.08  ? 37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 108.588 103.223 126.458 1.00 29.23  ? 37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 107.989 102.857 124.057 1.00 28.84  ? 37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 106.081 108.035 124.076 1.00 30.50  ? 38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 104.925 108.928 124.196 1.00 31.23  ? 38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 103.950 108.852 123.009 1.00 31.03  ? 38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 102.787 109.222 123.138 1.00 30.82  ? 38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 105.364 110.375 124.493 1.00 31.98  ? 38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 106.289 110.948 123.432 1.00 33.59  ? 38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 107.338 110.369 123.121 1.00 36.48  ? 38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 105.914 112.098 122.879 1.00 34.77  ? 38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 104.426 108.340 121.877 1.00 30.88  ? 39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 103.581 108.082 120.705 1.00 31.37  ? 39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 102.507 107.016 120.890 1.00 31.05  ? 39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 101.487 107.061 120.216 1.00 31.21  ? 39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 102.726 106.066 121.803 1.00 30.63  ? 40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 101.705 105.059 122.152 1.00 30.65  ? 40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 100.594 105.561 123.080 1.00 31.00  ? 40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 99.621  104.840 123.306 1.00 30.91  ? 40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 102.343 103.834 122.820 1.00 30.00  ? 40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 103.227 103.043 121.886 1.00 30.88  ? 40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 103.385 103.430 120.704 1.00 30.42  ? 40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 103.775 102.020 122.353 1.00 31.17  ? 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 100.741 106.767 123.625 1.00 31.54  ? 41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 99.821  107.272 124.658 1.00 32.47  ? 41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 98.351  107.235 124.258 1.00 33.21  ? 41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 97.491  106.866 125.065 1.00 32.84  ? 41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 100.201 108.687 125.101 1.00 33.14  ? 41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 101.272 108.825 126.182 1.00 34.44  ? 41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 101.735 110.273 126.271 1.00 35.04  ? 41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 100.745 108.331 127.536 1.00 35.52  ? 41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 98.068  107.612 123.012 1.00 33.75  ? 42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 96.694  107.644 122.532 1.00 34.79  ? 42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 96.093  106.279 122.201 1.00 34.66  ? 42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 94.967  106.008 122.612 1.00 34.67  ? 42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 96.526  108.622 121.367 1.00 35.27  ? 42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 96.354  110.080 121.809 1.00 36.82  ? 42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 96.239  110.979 120.583 1.00 37.93  ? 42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 95.136  110.267 122.713 1.00 37.85  ? 42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 96.817  105.425 121.472 1.00 34.70  ? 43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 96.293  104.077 121.194 1.00 35.10  ? 43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 96.111  103.255 122.481 1.00 34.78  ? 43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 95.266  102.369 122.530 1.00 35.04  ? 43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 97.092  103.282 120.114 1.00 35.30  ? 43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 98.479  103.189 120.475 1.00 36.01  ? 43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 96.955  103.935 118.740 1.00 35.96  ? 43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 96.880  103.578 123.524 1.00 34.63  ? 44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 96.724  102.938 124.837 1.00 34.37  ? 44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 95.452  103.414 125.538 1.00 35.13  ? 44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 94.648  102.605 126.020 1.00 34.98  ? 44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 97.939  103.221 125.719 1.00 33.95  ? 44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 97.772  102.788 127.140 1.00 33.26  ? 44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 97.512  103.588 128.219 1.00 32.51  ? 44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 97.860  101.448 127.643 1.00 30.93  ? 44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 97.437  102.827 129.366 1.00 31.66  ? 44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 97.645  101.511 129.040 1.00 30.39  ? 44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 98.103  100.202 127.049 1.00 30.36  ? 44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 97.657  100.374 129.852 1.00 29.16  ? 44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 98.119  99.065  127.860 1.00 28.84  ? 44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 97.903  99.163  129.246 1.00 29.34  ? 44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 95.294  104.734 125.601 1.00 35.69  ? 45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 94.107  105.367 126.156 1.00 36.38  ? 45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 92.814  104.790 125.570 1.00 36.24  ? 45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 91.818  104.687 126.276 1.00 36.78  ? 45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 94.178  106.873 125.893 1.00 37.14  ? 45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 93.029  107.691 126.455 1.00 38.91  ? 45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 93.079  109.121 125.915 1.00 41.12  ? 45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 92.170  110.042 126.712 1.00 43.00  ? 45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 92.399  109.897 128.183 1.00 44.38  ? 45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 92.866  104.385 124.297 1.00 36.03  ? 46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 91.697  103.937 123.521 1.00 36.03  ? 46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 91.312  102.463 123.707 1.00 35.25  ? 46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 90.239  102.036 123.267 1.00 35.32  ? 46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 91.922  104.189 122.019 1.00 36.60  ? 46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 92.099  105.646 121.614 1.00 37.85  ? 46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 91.763  106.683 122.484 1.00 38.97  ? 46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 92.592  105.983 120.345 1.00 40.06  ? 46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 91.930  108.019 122.122 1.00 40.36  ? 46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 92.760  107.325 119.967 1.00 40.53  ? 46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 92.422  108.336 120.866 1.00 41.43  ? 46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 92.566  109.668 120.523 1.00 41.48  ? 46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 92.191  101.685 124.332 1.00 33.80  ? 47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 91.909  100.276 124.582 1.00 32.77  ? 47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 90.901  100.132 125.715 1.00 31.84  ? 47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 90.860  100.959 126.622 1.00 31.90  ? 47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 93.190  99.521  124.945 1.00 32.39  ? 47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 94.337  99.367  123.944 1.00 32.68  ? 47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 95.472  98.583  124.596 1.00 33.03  ? 47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 93.894  98.689  122.643 1.00 32.78  ? 47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 90.104  99.071  125.668 1.00 30.99  ? 48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 89.203  98.746  126.772 1.00 30.58  ? 48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 89.953  98.390  128.049 1.00 29.87  ? 48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 91.139  98.065  128.012 1.00 28.79  ? 48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 89.264  98.463  129.184 1.00 29.89  ? 49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 89.873  98.120  130.468 1.00 29.49  ? 49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 90.394  96.671  130.493 1.00 28.74  ? 49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 91.475  96.409  131.036 1.00 27.27  ? 49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 88.908  98.403  131.624 1.00 30.67  ? 49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 88.851  99.902  132.009 1.00 33.73  ? 49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 87.619  100.263 132.856 1.00 38.93  ? 49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 87.761  99.870  134.333 1.00 41.04  ? 49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 88.717  100.732 135.089 1.00 42.21  ? 49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 89.630  95.754  129.889 1.00 27.54  ? 50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 90.043  94.356  129.747 1.00 27.00  ? 50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 91.350  94.205  128.969 1.00 26.19  ? 50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 92.233  93.409  129.350 1.00 25.38  ? 50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 88.931  93.510  129.086 1.00 27.08  ? 50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 88.543  93.999  127.670 1.00 28.69  ? 50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 88.384  95.208  127.413 1.00 30.45  ? 50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 88.360  93.040  126.749 1.00 29.42  ? 50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 91.466  94.970  127.885 1.00 24.91  ? 51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 92.641  94.916  127.024 1.00 24.97  ? 51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 93.886  95.450  127.740 1.00 24.45  ? 51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 94.964  94.838  127.674 1.00 23.90  ? 51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 92.388  95.689  125.729 1.00 25.27  ? 51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 91.312  95.072  124.837 1.00 26.16  ? 51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 91.062  95.906  123.587 1.00 28.70  ? 51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 90.392  96.953  123.695 1.00 28.70  ? 51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 91.534  95.515  122.497 1.00 28.92  ? 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 93.722  96.572  128.440 1.00 23.75  ? 52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 94.818  97.171  129.197 1.00 23.94  ? 52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 95.279  96.245  130.325 1.00 23.36  ? 52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 96.470  96.137  130.588 1.00 22.95  ? 52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 94.406  98.528  129.787 1.00 24.28  ? 52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 94.285  99.680  128.769 1.00 25.22  ? 52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 93.966  101.029 129.423 1.00 29.02  ? 52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 93.818  101.123 130.640 1.00 32.08  ? 52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 93.862  102.074 128.610 1.00 29.13  ? 52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 94.319  95.608  130.999 1.00 23.02  ? 53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 94.611  94.685  132.088 1.00 23.44  ? 53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 95.450  93.503  131.586 1.00 23.00  ? 53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 96.473  93.174  132.180 1.00 22.96  ? 53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 93.312  94.173  132.727 1.00 23.31  ? 53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 93.560  93.348  133.973 1.00 25.80  ? 53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 94.139  93.882  134.954 1.00 27.95  ? 53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 93.165  92.165  133.975 1.00 26.30  ? 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 94.998  92.871  130.505 1.00 22.20  ? 54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 95.711  91.745  129.915 1.00 21.84  ? 54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 97.104  92.174  129.466 1.00 22.09  ? 54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 98.079  91.479  129.728 1.00 21.88  ? 54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 94.916  91.102  128.745 1.00 21.74  ? 54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 93.721  90.520  129.269 1.00 22.09  ? 54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 95.727  89.989  128.070 1.00 19.76  ? 54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 97.191  93.325  128.806 1.00 22.38  ? 55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 98.477  93.844  128.348 1.00 22.85  ? 55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 99.484  94.048  129.494 1.00 22.56  ? 55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 100.631 93.624  129.377 1.00 21.97  ? 55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 98.279  95.141  127.576 1.00 23.57  ? 55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 99.459  95.565  126.725 1.00 25.59  ? 55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 100.458 96.386  127.248 1.00 27.49  ? 55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 99.556  95.173  125.386 1.00 27.70  ? 55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 101.543 96.799  126.463 1.00 30.28  ? 55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 100.631 95.585  124.590 1.00 30.38  ? 55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 101.622 96.393  125.136 1.00 31.39  ? 55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 102.684 96.812  124.358 1.00 32.67  ? 55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 99.057  94.697  130.579 1.00 23.14  ? 56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 99.926  94.941  131.745 1.00 23.90  ? 56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 100.425 93.628  132.334 1.00 23.24  ? 56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 101.599 93.489  132.697 1.00 22.47  ? 56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 99.177  95.699  132.847 1.00 24.38  ? 56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 98.736  97.115  132.508 1.00 28.52  ? 56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 100.086 98.287  132.526 1.00 34.32  ? 56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 100.548 98.288  134.262 1.00 33.84  ? 56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 99.509  92.669  132.436 1.00 23.25  ? 57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 99.795  91.413  133.118 1.00 22.98  ? 57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 100.751 90.573  132.284 1.00 22.77  ? 57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 101.700 89.999  132.810 1.00 22.56  ? 57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 98.493  90.675  133.450 1.00 22.99  ? 57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 97.756  91.290  134.642 1.00 24.86  ? 57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 96.370  90.681  134.853 1.00 27.37  ? 57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 95.767  91.138  136.187 1.00 28.99  ? 57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 94.343  90.696  136.278 1.00 29.82  ? 57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 100.493 90.538  130.978 1.00 22.70  ? 58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 101.344 89.880  129.990 1.00 23.48  ? 58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 102.809 90.371  130.088 1.00 23.04  ? 58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 103.746 89.556  130.210 1.00 22.83  ? 58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 100.703 90.073  128.579 1.00 24.24  ? 58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 101.728 90.263  127.476 1.00 25.71  ? 58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 99.707  88.929  128.286 1.00 25.04  ? 58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 102.999 91.687  130.090 1.00 22.84  ? 59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 104.343 92.260  130.180 1.00 23.35  ? 59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 104.974 92.005  131.554 1.00 22.75  ? 59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 106.185 91.818  131.648 1.00 22.75  ? 59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 104.350 93.761  129.861 1.00 23.91  ? 59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 104.036 94.312  128.456 1.00 26.63  ? 59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 104.545 95.740  128.331 1.00 26.99  ? 59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 104.618 93.465  127.336 1.00 27.23  ? 59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 104.150 91.973  132.604 1.00 22.28  ? 60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 104.625 91.667  133.957 1.00 22.21  ? 60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 105.148 90.230  134.054 1.00 22.07  ? 60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 106.185 90.000  134.669 1.00 21.97  ? 60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 103.526 91.944  135.004 1.00 22.38  ? 60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 104.448 89.289  133.409 1.00 21.67  ? 61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 104.875 87.896  133.310 1.00 21.74  ? 61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 106.195 87.759  132.571 1.00 21.79  ? 61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 107.060 86.955  132.950 1.00 21.93  ? 61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 106.355 88.565  131.523 1.00 21.54  ? 62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 107.609 88.633  130.774 1.00 21.12  ? 62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 108.729 89.197  131.636 1.00 20.89  ? 62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 109.846 88.678  131.607 1.00 20.84  ? 62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 107.459 89.481  129.506 1.00 21.23  ? 62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 106.535 88.994  128.381 1.00 21.98  ? 62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 106.395 90.051  127.283 1.00 24.12  ? 62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 107.010 87.685  127.781 1.00 22.03  ? 62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 108.424 90.255  132.390 1.00 19.93  ? 63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 109.405 90.884  133.272 1.00 19.71  ? 63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 109.951 89.881  134.275 1.00 19.63  ? 63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 111.157 89.859  134.537 1.00 19.62  ? 63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 108.804 92.095  134.028 1.00 20.22  ? 63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 108.166 92.983  133.094 1.00 19.37  ? 63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 109.878 92.827  134.794 1.00 19.45  ? 63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 109.065 89.063  134.837 1.00 19.66  ? 64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 109.461 88.052  135.814 1.00 20.51  ? 64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 110.432 87.042  135.195 1.00 20.84  ? 64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 111.498 86.776  135.756 1.00 21.30  ? 64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 108.239 87.348  136.429 1.00 20.03  ? 64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 108.593 86.241  137.448 1.00 21.43  ? 64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 109.278 86.807  138.714 1.00 21.61  ? 64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 107.382 85.396  137.838 1.00 20.99  ? 64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 110.064 86.503  134.039 1.00 21.37  ? 65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 110.917 85.566  133.304 1.00 21.92  ? 65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 112.317 86.132  133.015 1.00 21.76  ? 65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 113.316 85.457  133.264 1.00 21.72  ? 65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 110.242 85.127  131.994 1.00 22.42  ? 65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 108.982 84.237  132.010 1.00 24.26  ? 65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 108.451 84.071  130.587 1.00 24.67  ? 65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 109.263 82.877  132.626 1.00 25.60  ? 65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 112.385 87.358  132.493 1.00 21.75  ? 66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 113.675 88.023  132.226 1.00 21.99  ? 66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 114.482 88.350  133.486 1.00 21.76  ? 66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 115.721 88.317  133.467 1.00 21.65  ? 66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 113.471 89.316  131.432 1.00 22.23  ? 66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 113.607 89.113  129.948 1.00 24.59  ? 66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 114.536 88.392  129.518 1.00 27.46  ? 66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 112.785 89.691  129.209 1.00 27.98  ? 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 113.781 88.699  134.562 1.00 21.50  ? 67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 114.419 88.912  135.856 1.00 21.80  ? 67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 115.210 87.661  136.282 1.00 22.04  ? 67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 116.385 87.758  136.664 1.00 22.21  ? 67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 113.386 89.311  136.925 1.00 22.15  ? 67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 112.741 90.521  136.521 1.00 22.23  ? 67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 114.042 89.535  138.290 1.00 21.19  ? 67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 114.577 86.496  136.181 1.00 21.55  ? 68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 115.212 85.257  136.611 1.00 21.81  ? 68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 116.235 84.742  135.587 1.00 21.35  ? 68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 117.265 84.186  135.962 1.00 21.34  ? 68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 114.160 84.206  136.983 1.00 22.25  ? 68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 113.554 84.435  138.398 1.00 24.02  ? 68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 114.622 84.566  139.485 1.00 25.78  ? 68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 115.568 83.750  139.510 1.00 26.69  ? 68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 114.518 85.488  140.328 1.00 28.98  ? 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 115.974 84.977  134.302 1.00 20.82  ? 69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 116.921 84.612  133.255 1.00 21.28  ? 69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 118.215 85.423  133.381 1.00 21.24  ? 69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 119.307 84.893  133.157 1.00 20.99  ? 69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 116.294 84.774  131.859 1.00 21.86  ? 69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 117.089 84.082  130.728 1.00 24.29  ? 69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 117.034 82.553  130.804 1.00 27.14  ? 69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 116.756 81.981  131.862 1.00 27.13  ? 69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 117.316 81.889  129.680 1.00 27.69  ? 69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 118.083 86.693  133.774 1.00 20.62  ? 70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 119.234 87.583  133.953 1.00 22.00  ? 70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 119.950 87.393  135.275 1.00 22.45  ? 70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 121.178 87.354  135.301 1.00 23.53  ? 70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 119.188 87.273  136.365 1.00 22.79  ? 71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 119.755 87.113  137.713 1.00 23.85  ? 71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 120.385 85.742  137.927 1.00 24.33  ? 71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 121.391 85.621  138.636 1.00 24.17  ? 71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 118.679 87.293  138.793 1.00 23.74  ? 71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 118.175 88.721  138.913 1.00 24.38  ? 71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 118.584 89.625  138.173 1.00 25.16  ? 71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 117.266 88.927  139.852 1.00 24.07  ? 71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 119.793 84.716  137.312 1.00 23.97  ? 72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 120.070 83.329  137.712 1.00 24.97  ? 72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 120.466 82.446  136.538 1.00 24.52  ? 72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 121.554 81.883  136.533 1.00 25.39  ? 72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 118.855 82.697  138.442 1.00 24.54  ? 72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 118.463 83.531  139.540 1.00 26.43  ? 72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 119.192 81.313  138.974 1.00 26.83  ? 72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 119.582 82.342  135.556 1.00 24.37  ? 73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 119.717 81.379  134.452 1.00 24.24  ? 73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 120.973 81.545  133.624 1.00 24.94  ? 73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 121.802 80.632  133.549 1.00 25.86  ? 73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 121.121 82.708  133.000 1.00 24.07  ? 74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 122.293 82.950  132.169 1.00 24.35  ? 74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 123.634 82.964  132.929 1.00 23.52  ? 74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 124.579 82.352  132.444 1.00 23.40  ? 74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 122.111 84.187  131.290 1.00 24.38  ? 74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 121.093 84.003  130.164 1.00 27.47  ? 74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 121.626 82.706  129.013 1.00 32.54  ? 74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 122.962 83.515  128.207 1.00 34.32  ? 74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 123.720 83.646  134.107 1.00 23.36  ? 75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 124.970 83.599  134.897 1.00 23.27  ? 75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 125.377 82.200  135.346 1.00 23.77  ? 75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 126.561 81.868  135.296 1.00 23.46  ? 75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 124.644 84.447  136.138 1.00 23.55  ? 75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 123.587 85.392  135.680 1.00 23.85  ? 75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 122.748 84.585  134.702 1.00 22.76  ? 75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 124.416 81.393  135.801 1.00 23.81  ? 76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 124.721 80.031  136.246 1.00 24.52  ? 76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 125.189 79.108  135.100 1.00 23.92  ? 76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 126.148 78.340  135.259 1.00 23.99  ? 76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 123.557 79.411  137.071 1.00 24.49  ? 76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 124.075 78.290  137.971 1.00 27.08  ? 76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 122.413 78.897  136.171 1.00 26.06  ? 76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 123.194 78.055  139.189 1.00 31.37  ? 76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 124.539 79.206  133.944 1.00 23.97  ? 77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 124.996 78.473  132.755 1.00 24.01  ? 77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 126.400 78.964  132.342 1.00 25.23  ? 77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 127.285 78.153  132.052 1.00 25.77  ? 77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 123.977 78.579  131.591 1.00 23.98  ? 77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 124.573 78.062  130.285 1.00 23.17  ? 77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 122.702 77.801  131.944 1.00 22.55  ? 77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 126.616 80.281  132.374 1.00 25.42  ? 78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 127.948 80.839  132.081 1.00 26.72  ? 78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 129.021 80.234  132.991 1.00 27.46  ? 78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 130.108 79.890  132.529 1.00 28.07  ? 78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 127.944 82.352  132.201 1.00 26.52  ? 78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 128.691 80.069  134.271 1.00 28.33  ? 79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 129.632 79.528  135.255 1.00 29.60  ? 79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 130.095 78.111  134.903 1.00 29.64  ? 79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 131.263 77.759  135.107 1.00 29.72  ? 79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 129.023 79.561  136.657 1.00 29.70  ? 79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 129.968 79.086  137.759 1.00 33.58  ? 79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 129.318 79.001  139.126 1.00 37.83  ? 79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 128.161 79.459  139.297 1.00 40.64  ? 79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 129.971 78.459  140.043 1.00 41.40  ? 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 129.185 77.308  134.357 1.00 29.43  ? 80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 129.459 75.893  134.143 1.00 29.74  ? 80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 129.954 75.533  132.741 1.00 30.18  ? 80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 130.495 74.454  132.537 1.00 30.30  ? 80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 128.251 75.046  134.576 1.00 29.21  ? 80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 128.044 75.036  136.059 1.00 29.60  ? 80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 127.234 75.946  136.707 1.00 30.06  ? 80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 128.577 74.253  137.027 1.00 29.49  ? 80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 127.267 75.716  138.009 1.00 29.56  ? 80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 128.073 74.693  138.229 1.00 30.20  ? 80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 129.782 76.445  131.788 1.00 30.70  ? 81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 130.237 76.236  130.416 1.00 31.47  ? 81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 131.704 76.644  130.296 1.00 32.45  ? 81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 132.084 77.733  130.743 1.00 32.50  ? 81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 129.379 77.027  129.393 1.00 31.18  ? 81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 129.991 76.968  127.992 1.00 31.20  ? 81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 127.959 76.480  129.357 1.00 31.28  ? 81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 132.510 75.772  129.687 1.00 33.38  ? 82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 133.949 76.005  129.526 1.00 34.82  ? 82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 134.291 76.817  128.283 1.00 34.74  ? 82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 133.680 76.638  127.222 1.00 35.00  ? 82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 134.715 74.674  129.502 1.00 35.82  ? 82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 134.802 74.016  130.876 1.00 38.29  ? 82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 134.854 74.737  131.901 1.00 41.49  ? 82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 134.820 72.771  130.932 1.00 41.10  ? 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 135.278 77.702  128.425 1.00 34.89  ? 83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 135.788 78.504  127.308 1.00 35.11  ? 83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 135.445 79.976  127.434 1.00 34.96  ? 83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 134.268 80.334  127.528 1.00 34.57  ? 83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 136.473 80.827  127.419 1.00 35.02  ? 84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 136.307 82.271  127.644 1.00 34.83  ? 84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 135.372 82.954  126.655 1.00 33.77  ? 84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 134.639 83.873  127.028 1.00 33.25  ? 84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 137.659 82.991  127.689 1.00 36.09  ? 84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 138.413 82.769  128.964 1.00 39.17  ? 84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 139.791 82.707  129.015 1.00 43.00  ? 84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 137.981 82.572  130.234 1.00 41.84  ? 84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 140.173 82.491  130.264 1.00 43.47  ? 84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 139.094 82.406  131.023 1.00 43.10  ? 84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 135.381 82.500  125.407 1.00 32.84  ? 85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 134.491 83.078  124.404 1.00 32.29  ? 85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 133.032 82.658  124.610 1.00 30.88  ? 85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 132.121 83.481  124.463 1.00 30.44  ? 85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 134.958 82.733  122.998 1.00 32.85  ? 85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 136.301 83.353  122.632 1.00 35.55  ? 85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 136.782 82.904  121.278 1.00 38.12  ? 85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 135.990 82.743  120.349 1.00 39.96  ? 85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 138.091 82.698  121.152 1.00 40.39  ? 85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 132.814 81.386  124.941 1.00 29.75  ? 86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 131.465 80.904  125.261 1.00 28.87  ? 86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 130.932 81.651  126.476 1.00 28.16  ? 86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 129.772 82.061  126.493 1.00 27.55  ? 86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 131.453 79.399  125.520 1.00 28.48  ? 86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 131.648 78.571  124.263 1.00 29.86  ? 86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 131.671 77.079  124.554 1.00 30.23  ? 86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 131.402 76.352  123.319 1.00 33.04  ? 86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 130.998 75.095  123.252 1.00 31.54  ? 86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 130.775 74.553  122.066 1.00 31.85  ? 86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 130.826 74.383  124.357 1.00 34.74  ? 86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 131.787 81.839  127.479 1.00 27.65  ? 87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 131.405 82.595  128.676 1.00 27.96  ? 87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 131.090 84.054  128.377 1.00 27.75  ? 87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 130.177 84.619  128.977 1.00 28.29  ? 87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 132.474 82.510  129.766 1.00 27.80  ? 87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 132.601 81.136  130.390 1.00 29.04  ? 87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 133.664 81.158  131.480 1.00 31.15  ? 87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 133.975 79.759  131.979 1.00 32.05  ? 87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 132.915 79.279  132.900 1.00 30.88  ? 87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 131.837 84.659  127.454 1.00 27.69  ? 88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 131.586 86.052  127.058 1.00 27.46  ? 88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 130.220 86.238  126.393 1.00 26.87  ? 88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 129.541 87.236  126.632 1.00 26.47  ? 88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 132.686 86.555  126.145 1.00 27.98  ? 88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 129.832 85.284  125.547 1.00 25.98  ? 89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 128.518 85.305  124.900 1.00 25.46  ? 89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 127.416 85.159  125.955 1.00 24.57  ? 89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 126.475 85.956  125.996 1.00 23.62  ? 89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 128.399 84.200  123.821 1.00 25.80  ? 89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 126.956 84.059  123.317 1.00 25.44  ? 89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 129.349 84.490  122.659 1.00 26.23  ? 89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 127.560 84.163  126.826 1.00 24.33  ? 90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 126.562 83.925  127.869 1.00 23.93  ? 90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 126.444 85.083  128.860 1.00 23.77  ? 90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 125.339 85.412  129.291 1.00 23.04  ? 90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 126.811 82.598  128.592 1.00 23.73  ? 90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 126.683 81.353  127.709 1.00 24.50  ? 90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 127.386 80.162  128.343 1.00 24.02  ? 90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 125.220 81.026  127.403 1.00 25.38  ? 90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 127.580 85.687  129.227 1.00 24.24  ? 91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 127.574 86.900  130.060 1.00 24.95  ? 91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 126.868 88.081  129.400 1.00 24.25  ? 91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 126.148 88.825  130.065 1.00 23.99  ? 91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 128.995 87.323  130.442 1.00 25.81  ? 91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 129.492 86.620  131.676 1.00 29.96  ? 91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 129.322 87.120  132.790 1.00 35.44  ? 91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 130.107 85.452  131.496 1.00 32.37  ? 91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 127.109 88.268  128.103 1.00 23.60  ? 92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 126.432 89.316  127.346 1.00 23.32  ? 92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 124.913 89.088  127.315 1.00 22.63  ? 92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 124.141 90.025  127.527 1.00 21.94  ? 92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 126.954 89.395  125.905 1.00 23.27  ? 92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 126.471 90.611  125.163 1.00 24.66  ? 92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 127.198 91.810  125.215 1.00 25.72  ? 92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 125.284 90.575  124.436 1.00 25.36  ? 92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 126.746 92.947  124.544 1.00 25.92  ? 92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 124.820 91.711  123.760 1.00 25.82  ? 92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 125.551 92.900  123.819 1.00 25.80  ? 92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 124.505 87.850  127.024 1.00 22.03  ? 93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 123.083 87.477  127.033 1.00 22.14  ? 93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 122.429 87.723  128.404 1.00 21.64  ? 93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 121.314 88.252  128.471 1.00 21.59  ? 93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 122.907 86.024  126.607 1.00 22.46  ? 93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 123.239 85.770  125.145 1.00 23.80  ? 93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 123.203 84.013  124.729 1.00 28.07  ? 93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 123.281 84.132  122.923 1.00 26.42  ? 93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 123.136 87.372  129.484 1.00 20.98  ? 94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 122.678 87.653  130.857 1.00 20.58  ? 94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 122.435 89.139  131.113 1.00 21.01  ? 94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 121.432 89.528  131.739 1.00 21.06  ? 94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 123.690 87.091  131.884 1.00 20.83  ? 94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 123.373 89.971  130.661 1.00 20.36  ? 95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 123.242 91.410  130.798 1.00 20.83  ? 95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 121.987 91.907  130.062 1.00 20.55  ? 95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 121.213 92.694  130.604 1.00 20.70  ? 95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 124.512 92.100  130.283 1.00 20.64  ? 95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 124.459 93.628  130.253 1.00 21.42  ? 95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 123.575 94.254  128.810 1.00 22.51  ? 95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 124.568 93.601  127.466 1.00 20.66  ? 95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 121.783 91.423  128.841 1.00 20.50  ? 96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 120.614 91.806  128.061 1.00 21.22  ? 96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 119.318 91.487  128.806 1.00 21.11  ? 96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 118.411 92.321  128.845 1.00 20.71  ? 96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 120.629 91.153  126.673 1.00 21.35  ? 96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 121.684 91.734  125.679 1.00 22.54  ? 96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 121.616 93.521  125.412 1.00 24.89  ? 96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 120.170 93.663  124.363 1.00 24.95  ? 96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 119.253 90.300  129.410 1.00 21.18  ? 97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 118.063 89.858  130.146 1.00 21.99  ? 97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 117.632 90.853  131.224 1.00 22.10  ? 97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 116.486 91.309  131.228 1.00 22.22  ? 97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 118.258 88.469  130.778 1.00 22.01  ? 97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 118.712 87.334  129.852 1.00 24.38  ? 97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 117.762 87.020  128.689 1.00 26.32  ? 97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 117.084 87.920  128.174 1.00 29.86  ? 97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 117.734 85.858  128.248 1.00 29.19  ? 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 118.538 91.194  132.139 1.00 22.26  ? 98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 118.140 92.031  133.271 1.00 21.91  ? 98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 118.449 93.532  133.168 1.00 22.41  ? 98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 117.734 94.348  133.747 1.00 23.07  ? 98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 118.527 91.411  134.631 1.00 21.93  ? 98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 120.020 91.263  134.825 1.00 21.31  ? 98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 120.819 91.584  133.943 1.00 21.88  ? 98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 120.409 90.781  136.004 1.00 21.73  ? 98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 119.510 93.889  132.449 1.00 22.75  ? 99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 119.876 95.294  132.269 1.00 23.12  ? 99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 119.158 95.947  131.104 1.00 23.60  ? 99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 119.011 97.173  131.090 1.00 24.14  ? 99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 121.403 95.467  132.131 1.00 23.28  ? 99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 118.704 95.145  130.134 1.00 23.23  ? 100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 118.001 95.709  128.966 1.00 23.74  ? 100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 116.536 95.282  128.865 1.00 23.62  ? 100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 115.654 96.136  128.859 1.00 24.51  ? 100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 118.739 95.427  127.640 1.00 23.19  ? 100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 117.948 95.986  126.443 1.00 24.10  ? 100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 120.152 96.030  127.680 1.00 23.48  ? 100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 116.287 93.976  128.797 1.00 23.45  ? 101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 114.932 93.461  128.588 1.00 23.81  ? 101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 113.999 93.734  129.750 1.00 24.33  ? 101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 112.946 94.348  129.557 1.00 24.80  ? 101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 114.930 91.963  128.297 1.00 23.30  ? 101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 115.658 91.585  127.046 1.00 22.96  ? 101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 115.876 90.273  126.684 1.00 22.78  ? 101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 116.246 92.346  126.093 1.00 23.25  ? 101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 116.553 90.242  125.552 1.00 22.57  ? 101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 116.790 91.485  125.172 1.00 21.75  ? 101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 114.365 93.251  130.940 1.00 24.40  ? 102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 113.515 93.418  132.121 1.00 24.00  ? 102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 113.237 94.901  132.376 1.00 24.05  ? 102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 112.115 95.270  132.716 1.00 23.89  ? 102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 114.138 92.753  133.346 1.00 23.73  ? 102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 114.253 95.742  132.190 1.00 24.36  ? 103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 114.115 97.189  132.398 1.00 24.31  ? 103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 113.195 97.884  131.388 1.00 23.84  ? 103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 112.432 98.783  131.764 1.00 24.21  ? 103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 115.478 97.885  132.469 1.00 24.93  ? 103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 115.380 99.353  132.908 1.00 26.37  ? 103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 116.745 99.975  133.148 1.00 29.42  ? 103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 116.619 101.478 133.414 1.00 31.51  ? 103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 116.107 102.222 132.224 1.00 32.37  ? 103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 113.256 97.465  130.122 1.00 23.52  ? 104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 112.397 98.013  129.067 0.50 23.23  ? 104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 110.914 97.938  129.434 1.00 22.91  ? 104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 110.138 98.822  129.094 1.00 22.33  ? 104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 112.626 97.280  127.740 0.50 23.25  ? 104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 113.968 97.395  127.308 0.50 24.57  ? 104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 110.515 96.867  130.115 1.00 22.72  ? 105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 109.110 96.730  130.502 1.00 23.34  ? 105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 108.691 97.815  131.466 1.00 23.32  ? 105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 107.564 98.282  131.393 1.00 23.17  ? 105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 108.789 95.359  131.102 1.00 23.45  ? 105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 109.132 94.195  130.202 1.00 25.16  ? 105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 108.525 94.040  128.959 1.00 26.75  ? 105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 110.071 93.245  130.604 1.00 26.36  ? 105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 108.860 92.966  128.126 1.00 28.22  ? 105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 110.412 92.179  129.786 1.00 27.17  ? 105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 109.794 92.036  128.557 1.00 29.26  ? 105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 110.124 90.965  127.751 1.00 30.76  ? 105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 109.602 98.207  132.362 1.00 23.61  ? 106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 109.344 99.308  133.282 1.00 24.40  ? 106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 109.238 100.635 132.543 1.00 24.55  ? 106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 108.474 101.495 132.954 1.00 24.74  ? 106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 110.400 99.394  134.383 1.00 24.54  ? 106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 110.177 98.401  135.378 1.00 24.69  ? 106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 110.007 100.800 131.467 1.00 25.28  ? 107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 109.893 101.997 130.627 1.00 25.88  ? 107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 108.498 102.067 130.018 1.00 25.48  ? 107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 107.864 103.120 130.012 1.00 25.23  ? 107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 110.952 102.019 129.518 1.00 26.40  ? 107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 112.336 102.412 130.020 1.00 27.90  ? 107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 112.703 102.139 131.164 1.00 30.62  ? 107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 113.116 103.045 129.151 1.00 27.91  ? 107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 108.024 100.931 129.517 1.00 25.44  ? 108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 106.666 100.857 128.977 1.00 25.48  ? 108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 105.631 101.155 130.073 1.00 25.93  ? 108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 104.772 102.023 129.884 1.00 25.54  ? 108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 106.394 99.521  128.237 1.00 25.21  ? 108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 107.347 99.388  127.037 1.00 25.96  ? 108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 104.919 99.436  127.788 1.00 24.43  ? 108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 107.386 98.007  126.384 1.00 26.11  ? 108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 105.725 100.463 131.213 1.00 26.04  ? 109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 104.798 100.687 132.338 1.00 26.66  ? 109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 104.764 102.150 132.786 1.00 27.38  ? 109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 103.682 102.718 133.012 1.00 27.22  ? 109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 105.165 99.813  133.558 1.00 26.98  ? 109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 104.893 98.339  133.384 1.00 27.46  ? 109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 103.877 97.882  132.552 1.00 28.57  ? 109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 105.656 97.402  134.082 1.00 28.51  ? 109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 103.636 96.518  132.402 1.00 29.17  ? 109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 105.418 96.028  133.945 1.00 29.27  ? 109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 104.405 95.583  133.109 1.00 28.83  ? 109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 105.941 102.763 132.915 1.00 27.52  ? 110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 106.035 104.132 133.437 1.00 29.07  ? 110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 105.443 105.172 132.502 1.00 29.58  ? 110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 105.002 106.231 132.949 1.00 30.07  ? 110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 107.473 104.501 133.791 1.00 28.96  ? 110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 107.917 103.948 135.129 1.00 31.09  ? 110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 109.635 104.331 135.545 1.00 35.43  ? 110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 110.541 103.407 134.308 1.00 33.13  ? 110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 105.433 104.858 131.212 1.00 30.25  ? 111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 104.816 105.710 130.200 1.00 30.97  ? 111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 103.288 105.597 130.220 1.00 31.36  ? 111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 102.577 106.607 130.305 1.00 31.60  ? 111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 105.369 105.359 128.790 1.00 30.88  ? 111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 106.778 105.611 128.764 1.00 29.86  ? 111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 104.694 106.190 127.687 1.00 31.44  ? 111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 102.793 104.364 130.155 1.00 31.34  ? 112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 101.365 104.111 129.952 1.00 31.68  ? 112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 100.490 104.119 131.208 1.00 31.96  ? 112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 99.315  104.478 131.144 1.00 31.69  ? 112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 101.173 102.789 129.215 1.00 31.35  ? 112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 101.941 102.595 127.903 1.00 32.14  ? 112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 101.673 101.207 127.371 1.00 32.15  ? 112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 101.565 103.661 126.875 1.00 32.39  ? 112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 101.057 103.722 132.342 1.00 32.12  ? 113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 100.256 103.443 133.526 1.00 32.53  ? 113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 100.607 104.318 134.722 1.00 33.15  ? 113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 101.765 104.688 134.899 1.00 32.47  ? 113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 100.366 101.959 133.900 1.00 32.20  ? 113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 99.599  104.636 135.559 1.00 34.27  ? 114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 99.859  105.330 136.814 1.00 35.35  ? 114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 100.510 104.387 137.820 1.00 36.17  ? 114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 100.352 103.168 137.718 1.00 35.92  ? 114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 98.466  105.768 137.280 1.00 35.48  ? 114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 97.518  104.844 136.621 1.00 34.94  ? 114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 98.165  104.344 135.364 1.00 34.50  ? 114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 101.243 104.956 138.771 1.00 37.30  ? 115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 102.023 104.189 139.748 1.00 38.49  ? 115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 101.248 103.074 140.466 1.00 38.48  ? 115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 101.804 101.996 140.706 1.00 38.74  ? 115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 102.664 105.126 140.792 1.00 38.95  ? 115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 103.380 106.160 140.108 1.00 40.08  ? 115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 103.629 104.369 141.706 1.00 39.82  ? 115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 99.982  103.334 140.798 1.00 38.89  ? 116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 99.156  102.373 141.542 1.00 38.65  ? 116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 98.866  101.119 140.724 1.00 37.38  ? 116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 98.854  100.012 141.259 1.00 37.22  ? 116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 97.847  103.005 142.064 1.00 39.52  ? 116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 96.781  103.360 141.002 1.00 41.90  ? 116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 96.413  104.853 140.956 1.00 46.43  ? 116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 97.121  105.684 141.573 1.00 47.84  ? 116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 95.403  105.194 140.293 1.00 47.52  ? 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 98.647  101.307 139.425 1.00 36.05  ? 117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 98.415  100.201 138.509 1.00 34.88  ? 117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 99.701  99.402  138.328 1.00 33.58  ? 117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 99.661  98.171  138.240 1.00 33.61  ? 117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 97.895  100.699 137.154 1.00 34.85  ? 117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 96.770  101.558 137.374 1.00 35.98  ? 117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 97.469  99.534  136.272 1.00 34.92  ? 117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 100.832 100.105 138.279 1.00 32.29  ? 118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 102.142 99.457  138.221 1.00 31.19  ? 118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 102.397 98.633  139.496 1.00 30.85  ? 118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 102.767 97.462  139.410 1.00 29.77  ? 118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 103.301 100.465 137.955 1.00 31.25  ? 118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 103.082 101.230 136.639 1.00 30.12  ? 118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 104.659 99.746  137.927 1.00 30.21  ? 118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 104.112 102.348 136.388 1.00 29.41  ? 118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 102.179 99.242  140.667 1.00 31.17  ? 119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 102.326 98.543  141.954 1.00 31.76  ? 119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 101.452 97.286  142.030 1.00 31.25  ? 119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 101.922 96.225  142.444 1.00 31.47  ? 119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 101.990 99.459  143.141 1.00 32.65  ? 119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 103.040 100.537 143.388 1.00 35.14  ? 119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 104.221 100.382 143.061 1.00 36.75  ? 119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 102.604 101.641 144.004 1.00 38.05  ? 119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 100.194 97.421  141.616 1.00 30.96  ? 120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 99.230  96.322  141.616 1.00 30.36  ? 120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 99.658  95.160  140.717 1.00 28.60  ? 120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 99.526  94.002  141.107 1.00 27.94  ? 120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 97.843  96.817  141.194 1.00 30.86  ? 120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 97.083  97.578  142.276 1.00 34.89  ? 120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 95.805  98.218  141.752 1.00 39.82  ? 120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 95.356  97.859  140.634 1.00 41.95  ? 120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 95.241  99.079  142.458 1.00 41.94  ? 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 100.166 95.457  139.523 1.00 27.29  ? 121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 100.569 94.362  138.615 1.00 25.89  ? 121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 101.793 93.593  139.126 1.00 25.11  ? 121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 101.895 92.383  138.932 1.00 24.23  ? 121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 100.708 94.806  137.117 1.00 25.99  ? 121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 102.088 95.391  136.804 1.00 25.21  ? 121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 100.429 93.632  136.192 1.00 25.78  ? 121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 102.714 94.281  139.793 1.00 24.69  ? 122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 103.864 93.586  140.391 1.00 24.77  ? 122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 103.447 92.749  141.614 1.00 24.99  ? 122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 103.998 91.676  141.861 1.00 24.73  ? 122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 105.018 94.550  140.693 1.00 24.83  ? 122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 105.820 94.919  139.464 1.00 25.12  ? 122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 106.687 93.999  138.879 1.00 26.58  ? 122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 105.693 96.172  138.883 1.00 24.49  ? 122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 107.419 94.332  137.731 1.00 26.96  ? 122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 106.415 96.514  137.749 1.00 25.79  ? 122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 107.280 95.593  137.165 1.00 26.45  ? 122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 102.456 93.233  142.360 1.00 25.22  ? 123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 101.848 92.425  143.421 1.00 25.72  ? 123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 101.146 91.201  142.834 1.00 25.08  ? 123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 101.235 90.102  143.384 1.00 24.67  ? 123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 100.890 93.259  144.267 1.00 26.23  ? 123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 101.614 94.253  145.161 1.00 29.96  ? 123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 102.675 93.586  146.020 1.00 33.82  ? 123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 102.303 92.769  146.890 1.00 36.54  ? 123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 103.877 93.860  145.815 1.00 35.84  ? 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 100.477 91.398  141.701 1.00 24.21  ? 124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 99.803  90.311  140.993 1.00 23.99  ? 124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 100.755 89.202  140.521 1.00 23.95  ? 124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 100.393 88.012  140.584 1.00 23.31  ? 124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 98.978  90.857  139.817 1.00 24.13  ? 124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 98.495  89.783  138.868 1.00 24.37  ? 124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 97.327  89.064  138.951 1.00 24.76  ? 124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 99.173  89.317  137.694 1.00 23.31  ? 124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 97.248  88.172  137.897 1.00 24.97  ? 124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 98.364  88.309  137.112 1.00 24.20  ? 124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 100.390 89.644  137.082 1.00 23.76  ? 124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 98.735  87.631  135.943 1.00 23.41  ? 124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 100.762 88.967  135.921 1.00 23.29  ? 124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 99.929  87.975  135.363 1.00 22.93  ? 124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 101.953 89.555  140.044 1.00 23.35  ? 125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 102.910 88.478  139.681 1.00 23.53  ? 125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 103.279 87.597  140.881 1.00 23.73  ? 125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 103.343 86.384  140.743 1.00 23.03  ? 125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 104.160 88.903  138.776 1.00 23.63  ? 125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 104.126 90.337  138.321 1.00 24.40  ? 125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 105.525 88.504  139.368 1.00 22.97  ? 125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 103.458 88.208  142.055 1.00 24.06  ? 126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 103.843 87.463  143.266 1.00 25.41  ? 126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 102.815 86.411  143.689 1.00 25.82  ? 126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 103.188 85.369  144.234 1.00 26.08  ? 126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 104.083 88.415  144.441 1.00 25.49  ? 126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 105.296 89.313  144.307 1.00 27.52  ? 126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 105.355 90.258  145.501 1.00 30.43  ? 126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 106.323 91.398  145.267 1.00 33.10  ? 126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 106.263 92.362  146.401 1.00 34.86  ? 126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 101.535 86.686  143.439 1.00 26.45  ? 127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 100.449 85.822  143.908 1.00 26.85  ? 127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 99.814  84.950  142.823 1.00 26.01  ? 127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 98.967  84.109  143.130 1.00 26.12  ? 127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 99.369  86.640  144.642 1.00 28.08  ? 127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 98.647  87.687  143.789 1.00 30.69  ? 127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 97.626  87.084  142.826 1.00 34.64  ? 127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 97.788  87.160  141.595 1.00 33.80  ? 127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 96.573  86.470  143.381 1.00 36.24  ? 127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 100.211 85.153  141.563 1.00 24.97  ? 128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 99.671  84.368  140.457 1.00 24.03  ? 128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 100.272 82.971  140.445 1.00 24.13  ? 128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 101.491 82.835  140.310 1.00 22.93  ? 128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 99.969  85.044  139.128 1.00 23.97  ? 128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 99.310  84.339  137.967 1.00 23.94  ? 128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 99.883  83.427  137.373 1.00 24.85  ? 128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 98.077  84.724  137.666 1.00 24.76  ? 128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 99.425  81.944  140.553 1.00 24.32  ? 129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 99.916  80.567  140.756 1.00 24.77  ? 129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 100.639 79.943  139.559 1.00 24.54  ? 129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 101.555 79.141  139.742 1.00 24.17  ? 129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 98.811  79.641  141.281 1.00 25.27  ? 129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 97.622  79.447  140.364 1.00 28.72  ? 129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 96.788  78.258  140.843 1.00 33.40  ? 129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 95.366  78.334  140.321 1.00 36.77  ? 129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 94.518  77.289  140.973 1.00 39.66  ? 129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 100.223 80.309  138.342 1.00 23.92  ? 130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 100.858 79.793  137.122 1.00 24.12  ? 130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 102.236 80.392  136.889 1.00 23.54  ? 130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 103.169 79.696  136.463 1.00 23.32  ? 130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 99.943  80.017  135.903 1.00 24.53  ? 130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 98.501  79.661  136.196 1.00 25.83  ? 130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 98.139  78.347  136.494 1.00 26.57  ? 130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 97.507  80.646  136.219 1.00 27.87  ? 130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 96.821  78.010  136.786 1.00 29.65  ? 130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 96.179  80.319  136.515 1.00 29.91  ? 130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 95.849  79.001  136.798 1.00 31.19  ? 130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 94.544  78.659  137.091 1.00 34.44  ? 130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 102.359 81.685  137.172 1.00 23.38  ? 131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 103.622 82.386  137.039 1.00 23.43  ? 131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 104.602 81.905  138.115 1.00 23.37  ? 131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 105.781 81.680  137.825 1.00 23.05  ? 131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 103.372 83.890  137.143 1.00 23.73  ? 131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 103.977 84.940  136.218 1.00 24.71  ? 131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 104.506 84.408  134.875 1.00 21.63  ? 131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 102.952 86.028  135.992 1.00 26.87  ? 131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 104.123 81.746  139.352 1.00 22.80  ? 132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 104.965 81.147  140.400 1.00 22.70  ? 132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 105.392 79.711  140.085 1.00 22.54  ? 132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 106.566 79.359  140.273 1.00 21.73  ? 132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 104.324 81.252  141.787 1.00 23.07  ? 132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 104.159 82.698  142.255 1.00 21.83  ? 132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 105.477 83.473  142.311 1.00 22.34  ? 132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 106.476 82.993  142.852 1.00 24.07  ? 132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 105.474 84.682  141.765 1.00 22.26  ? 132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 104.456 78.889  139.600 1.00 22.53  ? 133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 104.802 77.520  139.219 1.00 22.84  ? 133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 105.880 77.478  138.134 1.00 22.42  ? 133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 106.828 76.710  138.254 1.00 21.90  ? 133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 103.568 76.679  138.814 1.00 22.96  ? 133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 103.896 75.200  138.444 1.00 23.45  ? 133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 104.446 74.377  139.629 1.00 26.74  ? 133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 104.712 72.919  139.228 1.00 27.93  ? 133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 105.430 72.139  140.271 1.00 27.86  ? 133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 105.759 78.307  137.093 1.00 22.77  ? 134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 106.727 78.231  135.993 1.00 22.87  ? 134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 108.110 78.709  136.424 1.00 22.30  ? 134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 109.119 78.077  136.069 1.00 21.89  ? 134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 106.225 78.893  134.689 1.00 23.33  ? 134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 106.246 80.400  134.624 1.00 24.25  ? 134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 105.733 80.904  133.265 1.00 26.87  ? 134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 104.212 81.011  133.250 1.00 28.26  ? 134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 103.756 81.792  132.060 1.00 28.97  ? 134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 108.148 79.778  137.219 1.00 21.96  ? 135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 109.395 80.233  137.863 1.00 22.43  ? 135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 110.007 79.175  138.784 1.00 22.02  ? 135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 111.216 78.963  138.758 1.00 22.60  ? 135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 109.176 81.544  138.648 1.00 22.05  ? 135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 109.179 78.532  139.607 1.00 21.97  ? 136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 109.658 77.472  140.505 1.00 22.10  ? 136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 110.345 76.368  139.728 1.00 21.87  ? 136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 111.408 75.897  140.130 1.00 21.75  ? 136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 108.510 76.841  141.293 1.00 22.50  ? 136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 108.044 77.635  142.503 1.00 23.55  ? 136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 106.663 77.185  142.945 1.00 26.93  ? 136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 106.258 76.059  142.665 1.00 26.36  ? 136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 105.926 78.068  143.609 1.00 28.09  ? 136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 109.718 75.954  138.629 1.00 21.38  ? 137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 110.207 74.842  137.828 1.00 22.08  ? 137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 111.498 75.182  137.092 1.00 21.70  ? 137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 112.432 74.379  137.045 1.00 21.83  ? 137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 109.156 74.424  136.804 1.00 22.05  ? 137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 107.975 73.640  137.391 1.00 23.93  ? 137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 106.706 73.404  136.130 1.00 27.75  ? 137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 107.563 72.246  135.051 1.00 26.00  ? 137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 111.530 76.359  136.485 1.00 20.90  ? 138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 112.679 76.746  135.684 1.00 20.60  ? 138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 113.881 77.039  136.587 1.00 20.36  ? 138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 114.969 76.506  136.359 1.00 19.65  ? 138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 112.348 77.938  134.739 1.00 20.17  ? 138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 111.321 77.517  133.671 1.00 20.66  ? 138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 113.630 78.550  134.149 1.00 20.62  ? 138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 111.760 76.446  132.668 1.00 22.17  ? 138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 113.674 77.859  137.618 1.00 19.58  ? 139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 114.752 78.252  138.530 1.00 19.88  ? 139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 115.241 77.047  139.338 1.00 19.44  ? 139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 116.413 76.963  139.689 1.00 19.88  ? 139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 114.333 79.419  139.496 1.00 19.52  ? 139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 115.458 79.739  140.497 1.00 20.75  ? 139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 113.998 80.680  138.708 1.00 20.03  ? 139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 114.342 76.112  139.627 1.00 19.13  ? 140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 114.729 74.913  140.352 1.00 18.05  ? 140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 115.768 74.140  139.579 1.00 17.86  ? 140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 116.770 73.684  140.139 1.00 17.47  ? 140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 115.522 73.981  138.283 1.00 17.92  ? 141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 116.475 73.305  137.411 1.00 18.32  ? 141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 117.822 74.054  137.298 1.00 18.55  ? 141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 118.879 73.426  137.332 1.00 18.49  ? 141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 115.847 73.069  136.031 1.00 18.50  ? 141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 114.739 72.013  136.026 1.00 19.32  ? 141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 113.914 72.109  134.748 1.00 20.38  ? 141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 115.317 70.607  136.209 1.00 19.94  ? 141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 117.788 75.381  137.202 1.00 19.16  ? 142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 119.031 76.179  137.226 1.00 20.16  ? 142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 119.842 75.937  138.486 1.00 20.78  ? 142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 121.067 75.797  138.439 1.00 20.36  ? 142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 118.743 77.687  137.127 1.00 20.34  ? 142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 118.124 78.144  135.814 1.00 22.46  ? 142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 118.284 77.409  134.644 1.00 23.88  ? 142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 117.388 79.321  135.749 1.00 22.41  ? 142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 117.706 77.837  133.434 1.00 25.93  ? 142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 116.817 79.755  134.555 1.00 22.07  ? 142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 116.986 79.018  133.407 1.00 25.19  ? 142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 116.407 79.470  132.239 1.00 27.43  ? 142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 119.154 75.885  139.620 1.00 21.39  ? 143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 119.853 75.773  140.890 1.00 22.49  ? 143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 120.256 74.338  141.217 1.00 22.49  ? 143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 121.046 74.112  142.128 1.00 22.45  ? 143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 119.067 76.449  142.011 1.00 23.16  ? 143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 119.020 77.964  141.823 1.00 26.08  ? 143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 118.750 78.692  143.107 1.00 30.38  ? 143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 118.901 80.182  142.922 1.00 32.69  ? 143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 118.582 80.895  144.190 1.00 35.60  ? 143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 119.772 73.383  140.421 1.00 22.02  ? 144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 120.159 71.995  140.587 1.00 22.69  ? 144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 121.452 71.633  139.835 1.00 23.20  ? 144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 121.971 70.537  140.000 1.00 23.80  ? 144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 118.997 71.054  140.184 1.00 21.79  ? 144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 121.975 72.544  139.010 1.00 23.97  ? 145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 123.219 72.267  138.282 1.00 24.29  ? 145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 124.349 71.941  139.262 1.00 25.49  ? 145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 124.544 72.643  140.249 1.00 25.82  ? 145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 123.655 73.438  137.355 1.00 24.22  ? 145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 122.591 73.732  136.302 1.00 23.45  ? 145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 124.983 73.115  136.668 1.00 23.42  ? 145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 122.808 75.074  135.557 1.00 21.99  ? 145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 125.048 70.844  139.004 1.00 26.83  ? 146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 126.179 70.442  139.828 1.00 28.85  ? 146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 127.444 70.621  139.011 1.00 29.77  ? 146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 127.477 70.281  137.824 1.00 29.74  ? 146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 126.046 68.982  140.288 1.00 28.99  ? 146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 124.968 68.741  141.345 1.00 30.30  ? 146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 125.327 69.322  142.707 1.00 33.32  ? 146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 126.462 69.747  142.933 1.00 34.63  ? 146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 124.366 69.322  143.626 1.00 32.32  ? 146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 128.478 71.160  139.647 1.00 31.29  ? 147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 129.764 71.375  138.984 1.00 33.14  ? 147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 130.242 70.066  138.371 1.00 33.79  ? 147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 130.063 68.992  138.954 1.00 34.06  ? 147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 130.787 71.928  139.973 1.00 33.44  ? 147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 131.976 72.656  139.348 1.00 35.61  ? 147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 132.885 73.193  140.449 1.00 38.40  ? 147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 133.928 74.166  139.926 1.00 40.48  ? 147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 135.225 73.476  139.695 1.00 41.56  ? 147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 130.804 70.163  137.170 1.00 35.10  ? 148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 131.327 69.001  136.432 1.00 36.27  ? 148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 130.308 67.895  136.153 1.00 36.29  ? 148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 130.682 66.771  135.814 1.00 36.95  ? 148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 132.542 68.410  137.155 1.00 37.15  ? 148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 133.749 69.306  137.090 1.00 38.94  ? 148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 133.817 70.163  136.178 1.00 41.71  ? 148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 134.634 69.151  137.956 1.00 41.64  ? 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 129.025 68.203  136.299 1.00 35.87  ? 149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 127.983 67.227  136.009 1.00 35.24  ? 149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 127.192 67.736  134.811 1.00 34.12  ? 149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 126.331 68.630  134.932 1.00 33.52  ? 149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 127.106 66.978  137.240 1.00 36.09  ? 149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 125.882 66.111  136.944 1.00 38.39  ? 149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 125.814 65.452  135.879 1.00 42.06  ? 149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 124.977 66.080  137.799 1.00 42.21  ? 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 127.518 67.165  133.656 1.00 32.48  ? 150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 126.997 67.622  132.380 1.00 30.93  ? 150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 125.497 67.353  132.222 1.00 29.37  ? 150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 124.812 68.083  131.507 1.00 28.99  ? 150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 127.810 67.030  131.212 1.00 31.30  ? 150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 127.623 65.519  130.936 1.00 33.64  ? 150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 128.675 64.923  129.970 1.00 36.40  ? 150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 129.544 65.667  129.466 1.00 38.62  ? 150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 128.634 63.698  129.714 1.00 37.42  ? 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 124.996 66.310  132.884 1.00 27.68  ? 151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 123.573 65.969  132.793 1.00 26.26  ? 151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 122.705 67.022  133.488 1.00 24.85  ? 151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 121.691 67.436  132.930 1.00 23.53  ? 151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 123.268 64.540  133.317 1.00 26.53  ? 151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 124.018 63.484  132.488 1.00 27.59  ? 151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 121.752 64.264  133.358 1.00 26.51  ? 151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 123.566 63.348  131.027 1.00 26.91  ? 151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 123.102 67.463  134.684 1.00 23.58  ? 152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 122.339 68.511  135.359 1.00 22.36  ? 152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 122.388 69.811  134.554 1.00 21.79  ? 152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 121.414 70.572  134.527 1.00 20.91  ? 152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 122.796 68.719  136.808 1.00 22.43  ? 152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 124.156 69.117  136.878 1.00 24.02  ? 152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 123.526 70.055  133.903 1.00 21.65  ? 153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 123.694 71.233  133.055 1.00 21.86  ? 153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 122.773 71.165  131.834 1.00 21.98  ? 153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 122.102 72.151  131.522 1.00 21.64  ? 153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 125.167 71.440  132.645 1.00 21.71  ? 153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 125.522 72.632  131.735 1.00 22.04  ? 153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 124.988 73.961  132.268 1.00 21.99  ? 153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 127.040 72.705  131.539 1.00 23.37  ? 153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 122.739 70.009  131.163 1.00 22.17  ? 154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 121.822 69.775  130.025 1.00 22.02  ? 154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 120.372 70.069  130.391 1.00 21.86  ? 154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 119.636 70.695  129.618 1.00 21.62  ? 154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 121.917 68.322  129.534 1.00 22.08  ? 154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 120.886 67.960  128.481 1.00 21.99  ? 154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 121.105 68.267  127.135 1.00 20.87  ? 154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 119.689 67.325  128.843 1.00 20.82  ? 154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 120.149 67.963  126.164 1.00 20.27  ? 154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 118.726 67.005  127.882 1.00 20.19  ? 154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 118.958 67.319  126.532 1.00 20.93  ? 154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 119.957 69.572  131.557 1.00 21.98  ? 155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 118.580 69.756  132.023 1.00 21.79  ? 155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 118.243 71.240  132.198 1.00 21.70  ? 155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 117.163 71.692  131.790 1.00 21.10  ? 155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 118.340 68.965  133.315 1.00 22.00  ? 155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 118.398 67.454  133.136 1.00 21.93  ? 155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 118.223 66.722  134.455 1.00 23.06  ? 155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 118.217 65.220  134.261 1.00 24.91  ? 155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 118.375 64.498  135.567 1.00 25.16  ? 155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 119.170 71.994  132.799 1.00 21.49  ? 156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 119.005 73.439  132.924 1.00 20.60  ? 156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 119.002 74.171  131.564 1.00 20.37  ? 156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 118.265 75.132  131.388 1.00 19.61  ? 156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 120.060 74.033  133.853 1.00 20.88  ? 156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 119.811 73.707  130.612 1.00 20.70  ? 157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 119.828 74.296  129.261 1.00 21.06  ? 157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 118.535 74.030  128.515 1.00 20.83  ? 157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 118.104 74.859  127.706 1.00 21.28  ? 157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 121.006 73.771  128.420 1.00 20.68  ? 157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 122.396 74.221  128.866 1.00 21.61  ? 157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 123.677 73.333  127.950 1.00 24.32  ? 157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 125.135 74.302  128.389 1.00 23.64  ? 157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 117.930 72.864  128.745 1.00 20.76  ? 158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 116.618 72.561  128.160 1.00 20.14  ? 158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 115.584 73.535  128.736 1.00 20.35  ? 158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 114.772 74.107  128.004 1.00 19.82  ? 158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 116.171 71.103  128.447 1.00 20.07  ? 158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 114.706 70.901  128.050 1.00 20.07  ? 158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 117.061 70.113  127.702 1.00 20.57  ? 158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 115.635 73.713  130.052 1.00 19.89  ? 159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 114.755 74.651  130.750 1.00 20.50  ? 159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 114.919 76.071  130.183 1.00 20.67  ? 159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 113.929 76.753  129.913 1.00 21.27  ? 159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 115.062 74.636  132.231 1.00 20.03  ? 159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 116.168 76.497  129.996 1.00 20.78  ? 160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 116.476 77.808  129.413 1.00 21.26  ? 160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 115.955 77.947  127.975 1.00 21.19  ? 160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 115.341 78.953  127.638 1.00 20.89  ? 160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 117.984 78.096  129.476 1.00 21.42  ? 160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 118.279 79.400  128.995 1.00 23.69  ? 160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 116.194 76.943  127.124 1.00 20.99  ? 161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 115.605 76.978  125.781 1.00 21.18  ? 161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 114.072 77.082  125.853 1.00 21.15  ? 161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 113.463 77.873  125.115 1.00 21.18  ? 161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 116.047 75.770  124.895 1.00 21.11  ? 161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 115.254 75.739  123.591 1.00 21.75  ? 161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 117.545 75.842  124.603 1.00 20.98  ? 161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 113.440 76.307  126.745 1.00 21.10  ? 162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 111.980 76.386  126.901 1.00 21.21  ? 162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 111.504 77.761  127.368 1.00 21.38  ? 162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 110.430 78.209  126.980 1.00 20.97  ? 162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 111.418 75.293  127.833 1.00 21.50  ? 162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 111.450 73.908  127.246 1.00 22.20  ? 162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 111.535 73.715  125.868 1.00 23.80  ? 162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 111.374 72.779  128.070 1.00 23.71  ? 162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 111.565 72.427  125.320 1.00 25.52  ? 162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 111.398 71.500  127.536 1.00 24.01  ? 162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 111.504 71.328  126.166 1.00 25.47  ? 162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 111.545 70.057  125.631 1.00 25.37  ? 162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 112.295 78.412  128.207 1.00 22.12  ? 163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 112.001 79.800  128.614 1.00 23.80  ? 163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 112.168 80.755  127.424 1.00 24.21  ? 163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 111.300 81.566  127.179 1.00 24.72  ? 163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 112.887 80.229  129.788 1.00 23.52  ? 163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 112.691 81.608  130.448 1.00 24.91  ? 163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 113.000 81.516  131.921 1.00 24.81  ? 163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 113.528 82.719  129.798 1.00 26.39  ? 163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 113.276 80.631  126.680 1.00 25.17  ? 164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 113.591 81.556  125.581 1.00 25.30  ? 164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 112.620 81.450  124.393 1.00 25.07  ? 164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 112.186 82.466  123.823 1.00 24.49  ? 164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 115.026 81.319  125.053 1.00 26.17  ? 164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 116.156 81.646  126.054 1.00 27.05  ? 164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 116.432 83.149  126.185 1.00 29.23  ? 164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 115.751 83.979  125.517 1.00 28.79  ? 164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 117.364 83.518  126.937 1.00 28.65  ? 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 112.314 80.213  124.023 1.00 24.23  ? 165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 111.720 79.899  122.729 1.00 24.71  ? 165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 110.274 79.425  122.816 1.00 24.51  ? 165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 109.615 79.276  121.789 1.00 24.87  ? 165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 112.560 78.826  122.024 1.00 25.06  ? 165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 113.900 79.248  121.848 1.00 26.29  ? 165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 109.794 79.175  124.032 1.00 24.71  ? 166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 108.426 78.710  124.256 1.00 25.69  ? 166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 107.659 79.603  125.245 1.00 25.87  ? 166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 106.646 80.192  124.866 1.00 26.03  ? 166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 108.406 77.238  124.711 1.00 25.54  ? 166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 107.060 76.763  125.219 1.00 26.64  ? 166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 105.936 76.757  124.382 1.00 25.90  ? 166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 106.918 76.308  126.533 1.00 27.45  ? 166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 104.684 76.319  124.852 1.00 25.64  ? 166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 105.666 75.862  127.018 1.00 26.52  ? 166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 104.553 75.868  126.173 1.00 27.18  ? 166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 108.153 79.703  126.481 1.00 26.13  ? 167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 107.431 80.383  127.589 1.00 27.13  ? 167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 107.175 81.891  127.406 1.00 27.22  ? 167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 106.175 82.417  127.913 1.00 28.03  ? 167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 108.150 80.171  128.931 1.00 26.89  ? 167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 108.272 78.789  129.590 1.00 28.64  ? 167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 109.075 78.892  130.885 1.00 28.34  ? 167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 106.919 78.155  129.865 1.00 27.90  ? 167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 108.086 82.584  126.733 1.00 26.79  ? 168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 107.910 84.014  126.486 1.00 26.90  ? 168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 106.711 84.279  125.569 1.00 26.52  ? 168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 106.168 85.392  125.548 1.00 26.02  ? 168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 109.164 84.629  125.831 1.00 27.03  ? 168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 110.243 85.084  126.811 1.00 28.09  ? 168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 109.961 85.992  127.834 1.00 28.69  ? 168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 111.556 84.659  126.655 1.00 29.15  ? 168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 110.958 86.426  128.720 1.00 28.50  ? 168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 112.569 85.086  127.534 1.00 30.19  ? 168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 112.260 85.978  128.577 1.00 29.81  ? 168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 106.309 83.270  124.795 1.00 26.18  ? 169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 105.431 83.537  123.662 1.00 26.24  ? 169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 103.946 83.768  123.983 1.00 25.94  ? 169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 103.241 84.440  123.228 1.00 25.71  ? 169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 105.697 82.544  122.529 1.00 27.13  ? 169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 106.977 82.923  121.816 1.00 28.07  ? 169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 108.222 82.505  122.301 1.00 29.54  ? 169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 106.952 83.758  120.699 1.00 29.31  ? 169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 109.408 82.881  121.663 1.00 30.44  ? 169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 108.137 84.139  120.050 1.00 30.64  ? 169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 109.359 83.700  120.543 1.00 30.40  ? 169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 110.524 84.079  119.916 1.00 28.85  ? 169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 103.496 83.266  125.130 1.00 25.17  ? 170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 102.150 83.563  125.612 1.00 25.10  ? 170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 102.058 85.062  125.923 1.00 25.16  ? 170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 100.984 85.662  125.804 1.00 25.30  ? 170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 101.810 82.720  126.842 1.00 24.56  ? 170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 102.648 83.045  127.935 1.00 24.98  ? 170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 103.202 85.640  126.308 1.00 24.32  ? 171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 103.355 87.068  126.550 1.00 23.97  ? 171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 103.556 87.884  125.284 1.00 23.85  ? 171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 102.847 88.869  125.082 1.00 23.99  ? 171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 104.495 87.470  124.431 1.00 23.28  ? 172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 104.785 88.177  123.170 1.00 23.85  ? 172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 103.580 88.320  122.238 1.00 23.72  ? 172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 103.525 89.263  121.451 1.00 23.92  ? 172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 105.903 87.493  122.371 1.00 23.47  ? 172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 107.289 87.685  122.944 1.00 24.32  ? 172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 107.590 88.774  123.764 1.00 22.28  ? 172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 108.304 86.779  122.632 1.00 23.82  ? 172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 108.875 88.950  124.292 1.00 23.41  ? 172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 109.601 86.939  123.151 1.00 24.70  ? 172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 109.888 88.034  123.982 1.00 24.87  ? 172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 102.642 87.373  122.306 1.00 23.31  ? 173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 101.492 87.359  121.398 1.00 23.26  ? 173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 100.797 88.722  121.337 1.00 23.04  ? 173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 100.496 89.228  120.252 1.00 23.47  ? 173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 100.466 86.281  121.789 1.00 23.13  ? 173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 99.309  86.166  120.805 1.00 24.10  ? 173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 98.194  87.000  120.899 1.00 25.72  ? 173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 99.348  85.236  119.765 1.00 27.04  ? 173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 97.132  86.905  119.980 1.00 28.94  ? 173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 98.291  85.126  118.851 1.00 27.84  ? 173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 97.195  85.965  118.964 1.00 29.97  ? 173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 96.166  85.861  118.045 1.00 34.34  ? 173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 100.541 89.301  122.500 1.00 22.51  ? 174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 99.648  90.450  122.590 1.00 22.60  ? 174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 100.266 91.753  122.048 1.00 22.64  ? 174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 99.609  92.440  121.257 1.00 22.39  ? 174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 99.105  90.595  124.011 1.00 22.32  ? 174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 97.718  91.199  124.105 1.00 23.39  ? 174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 96.758  90.988  123.103 1.00 22.84  ? 174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 97.354  91.951  125.220 1.00 22.23  ? 174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 95.476  91.542  123.206 1.00 24.05  ? 174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 96.073  92.496  125.340 1.00 24.11  ? 174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 95.145  92.286  124.334 1.00 23.92  ? 174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 93.902  92.847  124.456 1.00 25.00  ? 174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 101.528 92.085  122.448 1.00 22.25  ? 175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 102.191 93.226  121.796 1.00 22.45  ? 175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 102.302 93.062  120.279 1.00 22.59  ? 175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 102.141 94.048  119.551 1.00 22.19  ? 175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 103.590 93.258  122.428 1.00 22.25  ? 175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 103.467 92.516  123.718 1.00 22.22  ? 175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 102.363 91.505  123.525 1.00 22.32  ? 175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 102.563 91.837  119.813 1.00 21.92  ? 176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 102.645 91.567  118.375 1.00 22.35  ? 176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 101.279 91.725  117.699 1.00 22.60  ? 176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 101.179 92.237  116.581 1.00 22.41  ? 176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 103.187 90.166  118.100 1.00 22.69  ? 176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 104.621 89.794  118.502 1.00 23.68  ? 176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 104.891 88.325  118.138 1.00 23.70  ? 176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 105.637 90.711  117.829 1.00 23.09  ? 176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 100.234 91.279  118.393 1.00 22.64  ? 177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 98.867  91.355  117.899 1.00 22.92  ? 177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 98.474  92.829  117.684 1.00 23.68  ? 177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 97.883  93.182  116.661 1.00 23.81  ? 177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 97.953  90.653  118.898 1.00 22.73  ? 177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 96.477  90.655  118.602 1.00 22.91  ? 177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 95.946  89.827  117.613 1.00 23.49  ? 177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 95.602  91.435  119.358 1.00 21.97  ? 177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 94.575  89.800  117.355 1.00 23.57  ? 177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 94.219  91.414  119.112 1.00 22.54  ? 177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 93.719  90.598  118.108 1.00 22.88  ? 177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 92.361  90.553  117.854 1.00 23.17  ? 177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 98.843  93.691  118.625 1.00 23.50  ? 178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 98.601  95.125  118.463 1.00 24.60  ? 178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 99.476  95.796  117.396 1.00 24.72  ? 178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 98.978  96.559  116.569 1.00 24.19  ? 178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 98.723  95.850  119.807 1.00 24.35  ? 178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 97.543  95.640  120.707 1.00 26.36  ? 178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 96.243  95.746  120.212 1.00 28.53  ? 178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 97.721  95.357  122.054 1.00 28.23  ? 178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 95.139  95.547  121.048 1.00 29.37  ? 178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 96.614  95.168  122.900 1.00 28.69  ? 178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 95.334  95.261  122.397 1.00 28.43  ? 178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 100.773 95.499  117.420 1.00 25.36  ? 179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 101.726 96.017  116.430 1.00 26.02  ? 179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 101.210 95.755  115.015 1.00 26.57  ? 179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 101.233 96.641  114.154 1.00 26.30  ? 179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 103.093 95.344  116.615 1.00 26.19  ? 179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 104.212 95.950  115.797 1.00 27.82  ? 179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 104.846 97.125  116.207 1.00 30.77  ? 179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 104.644 95.341  114.614 1.00 29.20  ? 179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 105.874 97.685  115.461 1.00 31.82  ? 179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 105.673 95.891  113.859 1.00 30.44  ? 179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 106.283 97.061  114.287 1.00 32.74  ? 179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 107.292 97.604  113.531 1.00 34.58  ? 179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 100.720 94.536  114.799 1.00 26.71  ? 180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 100.197 94.121  113.505 1.00 27.38  ? 180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 98.950  94.864  113.050 1.00 27.62  ? 180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 98.631  94.840  111.874 1.00 28.25  ? 180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 98.257  95.520  113.980 1.00 27.60  ? 181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 97.070  96.335  113.668 1.00 28.24  ? 181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 97.398  97.820  113.646 1.00 28.30  ? 181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 96.492  98.647  113.527 1.00 27.98  ? 181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 95.977  96.144  114.722 1.00 27.90  ? 181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 95.432  94.758  114.861 1.00 29.54  ? 181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 94.455  94.659  116.010 1.00 31.54  ? 181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 93.349  95.204  115.951 1.00 32.11  ? 181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 94.858  93.972  117.071 1.00 31.29  ? 181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 98.679  98.149  113.810 1.00 28.14  ? 182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 99.131  99.531  113.857 1.00 28.38  ? 182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 98.833  100.208 115.179 1.00 28.71  ? 182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 98.619  101.415 115.220 1.00 28.80  ? 182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 98.804  99.423  116.255 1.00 28.24  ? 183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 98.513  99.939  117.583 1.00 28.48  ? 183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 99.673  99.648  118.531 1.00 27.82  ? 183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 100.310 98.589  118.443 1.00 26.73  ? 183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 97.221  99.334  118.133 1.00 29.13  ? 183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 95.965  99.729  117.355 1.00 30.41  ? 183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 94.853  98.712  117.565 1.00 33.74  ? 183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 93.564  99.146  116.849 1.00 36.26  ? 183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 92.474  98.158  117.090 1.00 39.17  ? 183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 99.934  100.594 119.431 1.00 27.77  ? 184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 101.031 100.491 120.402 1.00 27.79  ? 184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 102.354 100.135 119.716 1.00 27.85  ? 184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 103.068 99.203  120.111 1.00 27.07  ? 184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 100.683 99.483  121.517 1.00 27.76  ? 184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 99.384  99.762  122.284 1.00 28.62  ? 184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 99.079  98.643  123.260 1.00 29.18  ? 184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 99.449  101.095 123.015 1.00 28.43  ? 184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 102.690 100.900 118.688 1.00 28.15  ? 185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 103.792 100.516 117.835 1.00 28.80  ? 185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 105.175 100.807 118.403 1.00 28.77  ? 185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 106.139 100.148 118.020 1.00 28.79  ? 185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 103.600 101.099 116.448 1.00 29.96  ? 185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 102.402 100.460 115.739 1.00 31.23  ? 185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 102.494 100.743 113.992 1.00 40.10  ? 185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 103.823 99.657  113.513 1.00 35.10  ? 185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 105.272 101.758 119.326 1.00 28.62  ? 186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 106.558 102.058 119.966 1.00 29.10  ? 186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 106.920 100.978 120.988 1.00 28.52  ? 186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 108.037 100.463 120.966 1.00 28.28  ? 186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 106.568 103.451 120.602 1.00 29.21  ? 186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 106.404 104.597 119.602 1.00 31.41  ? 186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 107.564 104.691 118.631 1.00 34.70  ? 186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 107.530 104.105 117.553 1.00 37.69  ? 186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 108.612 105.406 119.023 1.00 34.75  ? 186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 105.968 100.642 121.868 1.00 28.38  ? 187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 106.086 99.490  122.771 1.00 28.25  ? 187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 106.363 98.229  121.962 1.00 28.00  ? 187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 107.192 97.406  122.352 1.00 27.90  ? 187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 104.789 99.276  123.555 1.00 27.88  ? 187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 104.483 100.386 124.373 1.00 30.27  ? 187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 105.648 98.089  120.840 1.00 27.31  ? 188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 105.807 96.952  119.936 1.00 27.86  ? 188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 107.196 96.849  119.334 1.00 27.96  ? 188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 107.709 95.743  119.127 1.00 27.84  ? 188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 107.803 98.001  119.047 1.00 28.21  ? 189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 109.172 98.050  118.542 1.00 29.15  ? 189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 110.162 97.499  119.588 1.00 28.02  ? 189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 111.071 96.733  119.263 1.00 27.15  ? 189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 109.536 99.484  118.147 1.00 30.17  ? 189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 110.137 99.617  116.757 1.00 35.68  ? 189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 109.085 99.565  115.645 1.00 40.25  ? 189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 108.193 100.445 115.589 1.00 42.98  ? 189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 109.157 98.644  114.809 1.00 43.59  ? 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 109.975 97.895  120.845 1.00 27.57  ? 190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 110.769 97.352  121.953 1.00 27.47  ? 190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 110.637 95.827  122.038 1.00 26.69  ? 190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 111.635 95.097  122.086 1.00 26.56  ? 190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 110.391 98.030  123.303 1.00 27.84  ? 190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 110.898 99.481  123.315 1.00 28.56  ? 190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 110.943 97.216  124.497 1.00 27.27  ? 190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 110.632 100.234 124.613 1.00 30.09  ? 190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 109.397 95.352  122.016 1.00 26.33  ? 191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 109.105 93.925  122.102 1.00 25.96  ? 191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 109.745 93.130  120.955 1.00 25.46  ? 191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 110.271 92.044  121.185 1.00 24.84  ? 191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 107.570 93.665  122.198 1.00 26.00  ? 191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 107.008 94.237  123.510 1.00 27.16  ? 191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 107.235 92.185  122.076 1.00 26.87  ? 191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 107.548 93.593  124.775 1.00 29.84  ? 191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 109.702 93.671  119.735 1.00 25.35  ? 192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 110.349 93.031  118.584 1.00 25.60  ? 192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 111.861 92.917  118.747 1.00 25.14  ? 192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 112.473 91.920  118.333 1.00 25.61  ? 192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 110.023 93.762  117.275 1.00 26.55  ? 192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 108.736 93.278  116.645 1.00 28.10  ? 192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 108.614 92.112  116.257 1.00 31.67  ? 192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 107.770 94.172  116.527 1.00 30.36  ? 192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 112.463 93.933  119.352 1.00 24.54  ? 193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 113.897 93.885  119.652 1.00 24.40  ? 193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 114.205 92.810  120.695 1.00 23.55  ? 193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 115.156 92.041  120.531 1.00 23.09  ? 193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 114.417 95.259  120.069 1.00 24.00  ? 193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 114.516 96.305  118.938 1.00 25.69  ? 193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 114.760 97.710  119.490 1.00 26.28  ? 193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 115.613 95.953  117.929 1.00 26.05  ? 193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 113.393 92.752  121.753 1.00 23.19  ? 194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 113.496 91.691  122.762 1.00 22.88  ? 194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 113.347 90.319  122.085 1.00 23.81  ? 194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 114.159 89.421  122.312 1.00 23.83  ? 194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 112.449 91.861  123.899 1.00 22.92  ? 194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 112.660 93.187  124.633 1.00 21.11  ? 194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 112.486 90.682  124.885 1.00 21.89  ? 194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 111.664 93.448  125.745 1.00 22.26  ? 194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 112.341 90.170  121.223 1.00 24.23  ? 195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 112.082 88.884  120.565 1.00 25.41  ? 195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 113.238 88.465  119.654 1.00 25.63  ? 195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 113.638 87.291  119.644 1.00 25.46  ? 195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 110.754 88.925  119.785 1.00 26.03  ? 195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 110.238 87.678  119.053 1.00 28.00  ? 195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 108.740 87.817  118.841 1.00 31.45  ? 195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 110.953 87.446  117.717 1.00 29.83  ? 195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 113.771 89.425  118.903 1.00 25.98  ? 196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 114.942 89.199  118.063 1.00 26.73  ? 196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 116.124 88.647  118.898 1.00 25.95  ? 196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 116.785 87.696  118.466 1.00 25.75  ? 196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 115.331 90.495  117.348 1.00 27.29  ? 196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 116.368 90.349  116.226 1.00 30.12  ? 196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 117.195 91.618  116.130 1.00 35.40  ? 196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 117.575 92.029  117.482 1.00 39.87  ? 196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 118.101 93.198  117.824 1.00 40.55  ? 196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 118.377 93.421  119.103 1.00 40.77  ? 196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 118.346 94.137  116.910 1.00 41.10  ? 196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 116.364 89.230  120.078 1.00 24.70  ? 197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 117.385 88.728  121.020 1.00 24.55  ? 197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 117.073 87.296  121.500 1.00 24.23  ? 197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 117.939 86.419  121.429 1.00 23.69  ? 197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 117.557 89.641  122.252 1.00 24.50  ? 197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 118.144 91.026  121.921 1.00 25.84  ? 197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 118.842 91.196  120.898 1.00 26.91  ? 197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 117.916 91.956  122.720 1.00 25.72  ? 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 115.841 87.052  121.960 1.00 23.92  ? 198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 115.521 85.733  122.533 1.00 24.20  ? 198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 115.658 84.627  121.503 1.00 24.02  ? 198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 116.068 83.525  121.852 1.00 24.24  ? 198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 114.131 85.664  123.170 1.00 24.05  ? 198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 113.671 86.879  123.954 1.00 25.03  ? 198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 114.373 87.128  125.303 1.00 26.31  ? 198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 115.535 86.687  125.544 1.00 27.65  ? 198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 113.730 87.825  126.135 1.00 26.87  ? 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 115.317 84.916  120.246 1.00 24.00  ? 199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 115.457 83.934  119.177 1.00 24.72  ? 199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 116.905 83.432  119.042 1.00 24.80  ? 199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 117.134 82.224  118.937 1.00 25.04  ? 199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 114.934 84.489  117.828 1.00 24.66  ? 199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 117.869 84.350  119.057 1.00 24.85  ? 200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 119.288 83.960  118.985 1.00 25.07  ? 200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 119.792 83.337  120.296 1.00 23.86  ? 200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 120.639 82.441  120.263 1.00 23.72  ? 200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 120.241 85.104  118.484 1.00 25.71  ? 200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 120.447 86.182  119.553 1.00 27.10  ? 200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 119.745 85.684  117.145 1.00 27.18  ? 200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 121.512 87.233  119.218 1.00 29.63  ? 200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 119.262 83.795  121.431 1.00 22.79  ? 201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 119.588 83.183  122.739 1.00 22.48  ? 201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 119.144 81.722  122.794 1.00 22.04  ? 201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 119.880 80.875  123.287 1.00 22.06  ? 201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 118.903 83.904  123.901 1.00 21.77  ? 201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 119.368 85.303  124.127 1.00 21.76  ? 201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 118.932 86.057  125.193 1.00 20.70  ? 201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 120.229 86.088  123.439 1.00 22.07  ? 201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 119.494 87.250  125.148 1.00 22.26  ? 201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 120.279 87.297  124.089 1.00 22.52  ? 201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 117.926 81.448  122.324 1.00 22.35  ? 202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 117.381 80.082  122.270 1.00 22.01  ? 202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 118.163 79.153  121.345 1.00 22.73  ? 202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 118.388 77.976  121.672 1.00 21.99  ? 202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 118.587 79.675  120.192 1.00 22.45  ? 203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 119.415 78.893  119.271 1.00 22.54  ? 203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 120.765 78.557  119.908 1.00 22.28  ? 203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 121.175 77.399  119.921 1.00 22.44  ? 203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 119.628 79.608  117.893 1.00 23.00  ? 203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 120.673 78.857  117.049 1.00 23.10  ? 203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 118.292 79.715  117.108 1.00 23.14  ? 203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 121.430 79.568  120.463 1.00 22.41  ? 204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 122.749 79.383  121.067 1.00 22.03  ? 204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 122.741 78.365  122.207 1.00 21.66  ? 204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 123.523 77.404  122.191 1.00 21.72  ? 204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 123.348 80.717  121.539 1.00 22.22  ? 204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 124.798 80.587  121.962 1.00 21.92  ? 204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 125.795 80.321  121.023 1.00 22.36  ? 204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 125.167 80.719  123.302 1.00 21.43  ? 204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 127.128 80.183  121.409 1.00 23.82  ? 204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 126.501 80.593  123.703 1.00 21.49  ? 204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 127.468 80.326  122.753 1.00 23.58  ? 204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 128.775 80.201  123.144 1.00 25.42  ? 204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 121.858 78.566  123.188 1.00 20.95  ? 205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 121.737 77.616  124.302 1.00 20.49  ? 205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 121.340 76.219  123.792 1.00 20.84  ? 205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 121.863 75.201  124.266 1.00 21.10  ? 205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 120.794 78.134  125.424 1.00 20.57  ? 205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 120.664 77.096  126.539 1.00 20.35  ? 205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 121.341 79.451  125.994 1.00 19.60  ? 205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 120.462 76.176  122.795 1.00 21.08  ? 206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 120.124 74.911  122.123 1.00 21.43  ? 206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 121.331 74.160  121.576 1.00 21.95  ? 206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 121.441 72.932  121.736 1.00 21.84  ? 206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 122.245 74.888  120.935 1.00 22.09  ? 207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 123.464 74.267  120.406 1.00 22.96  ? 207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 124.365 73.711  121.519 1.00 22.60  ? 207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 124.940 72.627  121.375 1.00 22.04  ? 207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 124.232 75.227  119.488 1.00 23.39  ? 207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 123.565 75.633  118.161 1.00 24.35  ? 207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 124.244 76.888  117.595 1.00 25.01  ? 207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 123.588 74.509  117.131 1.00 25.11  ? 207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 124.464 74.429  122.635 1.00 22.37  ? 208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 125.224 73.930  123.797 1.00 22.62  ? 208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 124.602 72.670  124.407 1.00 22.77  ? 208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 125.317 71.722  124.773 1.00 22.57  ? 208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 125.406 75.023  124.855 1.00 22.44  ? 208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 126.101 76.308  124.382 1.00 23.54  ? 208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 126.127 77.347  125.501 1.00 23.37  ? 208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 127.523 76.028  123.863 1.00 23.91  ? 208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 123.272 72.656  124.503 1.00 22.42  ? 209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 122.543 71.483  124.982 1.00 22.02  ? 209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 122.787 70.267  124.082 1.00 22.58  ? 209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 123.051 69.177  124.574 1.00 22.14  ? 209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 121.064 71.779  125.076 1.00 22.04  ? 209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 122.717 70.473  122.769 1.00 22.96  ? 210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 122.992 69.394  121.803 1.00 24.30  ? 210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 124.393 68.823  121.926 1.00 25.11  ? 210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 124.592 67.619  121.733 1.00 24.97  ? 210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 122.753 69.871  120.374 1.00 24.38  ? 210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 121.270 70.142  120.072 1.00 25.12  ? 210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 121.049 70.613  118.651 1.00 28.08  ? 210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 121.457 69.947  117.698 1.00 27.83  ? 210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 120.415 71.777  118.497 1.00 26.38  ? 210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 125.365 69.682  122.243 1.00 25.80  ? 211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 126.736 69.224  122.488 1.00 27.16  ? 211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 126.776 68.169  123.589 1.00 26.47  ? 211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 127.445 67.138  123.453 1.00 26.10  ? 211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 127.632 70.380  122.913 1.00 27.59  ? 211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 128.326 71.086  121.789 1.00 32.55  ? 211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 129.691 71.621  122.203 1.00 36.72  ? 211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 130.052 71.521  123.400 1.00 38.32  ? 211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 130.405 72.138  121.321 1.00 40.62  ? 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 126.071 68.443  124.686 1.00 25.55  ? 212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 126.053 67.533  125.831 1.00 25.32  ? 212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 125.286 66.256  125.513 1.00 25.48  ? 212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 125.774 65.152  125.767 1.00 25.82  ? 212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 125.488 68.209  127.100 1.00 25.39  ? 212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 126.447 69.308  127.566 1.00 24.37  ? 212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 125.251 67.171  128.202 1.00 24.86  ? 212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 125.818 70.295  128.536 1.00 25.10  ? 212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 124.099 66.412  124.933 1.00 25.27  ? 213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 123.285 65.284  124.474 1.00 25.77  ? 213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 124.069 64.338  123.548 1.00 26.44  ? 213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 123.974 63.114  123.669 1.00 26.29  ? 213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 122.033 65.824  123.764 1.00 25.67  ? 213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 121.092 64.800  123.162 1.00 25.65  ? 213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 121.250 64.367  121.836 1.00 25.02  ? 213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 120.010 64.306  123.895 1.00 26.59  ? 213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 120.374 63.440  121.269 1.00 26.52  ? 213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 119.127 63.386  123.339 1.00 27.00  ? 213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 119.319 62.955  122.031 1.00 27.79  ? 213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 118.445 62.061  121.480 1.00 29.00  ? 213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 124.841 64.904  122.623 1.00 26.96  ? 214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 125.568 64.088  121.652 1.00 28.05  ? 214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 126.707 63.259  122.238 1.00 28.24  ? 214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 127.190 62.337  121.587 1.00 28.63  ? 214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 126.040 64.927  120.455 1.00 28.38  ? 214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 124.879 65.428  119.602 1.00 31.14  ? 214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 123.844 64.765  119.482 1.00 34.16  ? 214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 125.045 66.605  119.011 1.00 32.42  ? 214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 127.114 63.571  123.468 1.00 27.91  ? 215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 128.136 62.800  124.178 1.00 28.49  ? 215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 127.597 61.517  124.821 1.00 28.50  ? 215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 128.370 60.653  125.242 1.00 28.98  ? 215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 128.809 63.658  125.255 1.00 28.10  ? 215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 129.592 64.845  124.714 1.00 29.25  ? 215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 130.248 65.637  125.833 1.00 30.19  ? 215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 130.746 66.962  125.306 1.00 32.63  ? 215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 131.385 67.765  126.374 1.00 35.39  ? 215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 126.277 61.380  124.883 1.00 28.25  ? 216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 125.672 60.298  125.661 1.00 28.34  ? 216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 125.522 58.978  124.886 1.00 28.92  ? 216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 125.535 58.964  123.655 1.00 28.53  ? 216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 124.326 60.760  126.239 1.00 27.68  ? 216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 124.384 62.113  126.987 1.00 26.67  ? 216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 125.487 62.191  128.038 1.00 25.32  ? 216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 125.692 61.257  128.817 1.00 25.49  ? 216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 126.201 63.313  128.067 1.00 23.63  ? 216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 125.376 57.874  125.621 1.00 29.53  ? 217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 124.972 56.597  125.027 1.00 30.73  ? 217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 123.549 56.729  124.470 1.00 31.13  ? 217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 122.817 57.672  124.824 1.00 30.17  ? 217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 124.951 55.457  126.061 1.00 30.79  ? 217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 123.889 55.689  126.997 1.00 31.16  ? 217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 126.285 55.349  126.807 1.00 31.22  ? 217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 123.149 55.776  123.626 1.00 31.67  ? 218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 121.788 55.774  123.086 1.00 32.25  ? 218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 120.733 55.648  124.191 1.00 31.86  ? 218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 119.684 56.297  124.136 1.00 31.09  ? 218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 121.620 54.687  122.010 1.00 33.29  ? 218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 122.415 54.974  120.722 1.00 35.65  ? 218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 122.024 56.301  120.060 1.00 39.17  ? 218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 120.804 56.574  119.922 1.00 41.08  ? 218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 122.935 57.078  119.682 1.00 39.64  ? 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 121.041 54.841  125.206 1.00 31.72  ? 219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 120.165 54.650  126.354 1.00 31.76  ? 219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 119.975 55.957  127.136 1.00 30.21  ? 219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 118.847 56.319  127.501 1.00 29.63  ? 219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 120.727 53.543  127.250 1.00 32.58  ? 219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 119.794 53.081  128.358 1.00 36.93  ? 219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 120.224 51.748  128.961 1.00 42.06  ? 219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 120.180 50.722  128.243 1.00 44.09  ? 219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 120.614 51.725  130.150 1.00 44.45  ? 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 121.080 56.663  127.374 1.00 28.91  ? 220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 121.053 57.942  128.069 1.00 28.14  ? 220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 120.297 59.012  127.278 1.00 27.03  ? 220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 119.526 59.784  127.857 1.00 26.72  ? 220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 122.470 58.422  128.397 1.00 27.83  ? 220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 122.508 59.708  129.233 1.00 29.68  ? 220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 122.700 59.426  130.717 1.00 33.58  ? 220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 121.406 59.088  131.403 1.00 33.71  ? 220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 121.610 58.652  132.823 1.00 34.69  ? 220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 120.533 59.051  125.966 1.00 26.38  ? 221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 119.816 59.940  125.048 1.00 25.87  ? 221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 118.313 59.745  125.122 1.00 25.72  ? 221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 117.558 60.726  125.163 1.00 24.52  ? 221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 120.275 59.737  123.602 1.00 25.83  ? 221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 121.620 60.342  123.268 1.00 26.76  ? 221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 121.898 60.190  121.777 1.00 28.40  ? 221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 123.311 60.566  121.432 1.00 29.84  ? 221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 123.623 60.202  120.030 1.00 30.96  ? 221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 117.890 58.477  125.126 1.00 25.97  ? 222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 116.472 58.133  125.261 1.00 25.79  ? 222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 115.872 58.704  126.547 1.00 25.24  ? 222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 114.747 59.224  126.533 1.00 25.37  ? 222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 116.270 56.619  125.178 1.00 26.17  ? 222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 116.622 58.640  127.646 1.00 25.02  ? 223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 116.179 59.241  128.914 1.00 25.08  ? 223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 116.117 60.777  128.848 1.00 24.70  ? 223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 115.195 61.398  129.398 1.00 24.20  ? 223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 117.066 58.793  130.080 1.00 25.35  ? 223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 116.605 59.348  131.439 1.00 26.67  ? 223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 117.627 59.151  132.544 1.00 28.29  ? 223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 118.470 58.239  132.440 1.00 29.51  ? 223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 117.587 59.917  133.523 1.00 29.09  ? 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 117.098 61.383  128.187 1.00 24.27  ? 224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 117.130 62.841  128.047 1.00 24.54  ? 224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 115.965 63.383  127.206 1.00 24.42  ? 224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 115.410 64.439  127.520 1.00 24.10  ? 224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 118.495 63.313  127.514 1.00 23.86  ? 224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 119.684 63.109  128.463 1.00 24.78  ? 224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 120.974 63.668  127.853 1.00 25.54  ? 224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 119.440 63.727  129.847 1.00 25.29  ? 224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 115.593 62.651  126.157 1.00 25.26  ? 225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 114.409 62.986  125.352 1.00 25.97  ? 225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 113.150 62.887  126.204 1.00 25.85  ? 225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 112.279 63.755  126.122 1.00 25.01  ? 225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 114.290 62.088  124.102 1.00 26.65  ? 225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 115.401 62.306  123.077 1.00 28.90  ? 225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 115.078 61.712  121.685 1.00 31.26  ? 225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 114.841 60.267  121.719 1.00 34.01  ? 225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 115.792 59.338  121.818 1.00 35.64  ? 225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 115.458 58.053  121.838 1.00 36.11  ? 225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 117.071 59.681  121.899 1.00 37.05  ? 225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 113.064 61.839  127.027 1.00 26.01  ? 226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 111.953 61.690  127.974 1.00 26.48  ? 226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 111.879 62.886  128.922 1.00 25.72  ? 226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 110.797 63.455  129.130 1.00 25.16  ? 226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 112.075 60.403  128.794 1.00 27.18  ? 226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 110.767 59.999  129.463 1.00 30.38  ? 226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 110.933 59.383  130.840 1.00 35.77  ? 226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 111.975 58.755  131.124 1.00 38.02  ? 226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 109.994 59.526  131.654 1.00 40.39  ? 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 113.027 63.264  129.488 1.00 24.71  ? 227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 113.093 64.433  130.363 1.00 23.71  ? 227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 112.568 65.674  129.638 1.00 23.14  ? 227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 111.731 66.399  130.179 1.00 22.40  ? 227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 114.517 64.694  130.884 1.00 23.85  ? 227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 114.683 66.064  131.491 1.00 23.64  ? 227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 114.299 66.301  132.814 1.00 23.07  ? 227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 115.157 67.137  130.716 1.00 23.04  ? 227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 114.421 67.570  133.379 1.00 22.73  ? 227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 115.278 68.415  131.264 1.00 23.31  ? 227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 114.912 68.636  132.603 1.00 21.51  ? 227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 113.060 65.899  128.419 1.00 22.95  ? 228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 112.736 67.113  127.657 1.00 22.96  ? 228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 111.251 67.181  127.310 1.00 23.31  ? 228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 110.623 68.235  127.432 1.00 22.63  ? 228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 113.586 67.198  126.391 1.00 22.40  ? 228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 110.703 66.051  126.879 1.00 23.66  ? 229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 109.292 65.966  126.501 1.00 25.00  ? 229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 108.363 66.036  127.721 1.00 24.64  ? 229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 107.358 66.757  127.694 1.00 24.26  ? 229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 109.017 64.732  125.586 1.00 25.43  ? 229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 109.635 64.982  124.203 1.00 27.27  ? 229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 107.491 64.500  125.408 1.00 27.62  ? 229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 110.224 63.740  123.519 1.00 31.32  ? 229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 108.709 65.325  128.795 1.00 24.78  ? 230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 107.950 65.435  130.055 1.00 25.20  ? 230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 107.938 66.866  130.594 1.00 24.08  ? 230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 106.902 67.360  131.065 1.00 23.34  ? 230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 108.530 64.525  131.147 1.00 25.73  ? 230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 108.187 63.068  130.947 1.00 28.78  ? 230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 107.409 62.735  130.023 1.00 29.99  ? 230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 108.712 62.247  131.728 1.00 33.31  ? 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 109.095 67.522  130.539 1.00 22.98  ? 231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 109.195 68.900  131.023 1.00 21.63  ? 231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 108.365 69.831  130.147 1.00 21.66  ? 231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 107.665 70.715  130.644 1.00 19.41  ? 231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 110.648 69.373  131.049 1.00 21.89  ? 231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 110.905 70.837  131.452 1.00 21.33  ? 231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 110.347 71.153  132.857 1.00 20.89  ? 231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 112.406 71.126  131.366 1.00 20.31  ? 231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 108.456 69.632  128.835 1.00 22.28  ? 232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 107.704 70.470  127.908 1.00 23.05  ? 232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 106.205 70.346  128.160 1.00 23.36  ? 232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 105.510 71.369  128.286 1.00 22.96  ? 232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 108.047 70.138  126.454 1.00 23.53  ? 232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 107.296 70.993  125.427 1.00 25.63  ? 232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 107.678 72.470  125.532 1.00 25.88  ? 232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 107.563 70.462  124.027 1.00 27.67  ? 232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 105.717 69.105  128.252 1.00 23.55  ? 233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 104.297 68.852  128.554 1.00 24.61  ? 233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 103.832 69.461  129.879 1.00 23.57  ? 233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 102.748 70.033  129.963 1.00 23.52  ? 233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 103.979 67.355  128.514 1.00 24.99  ? 233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 103.678 66.856  127.107 1.00 28.92  ? 233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 102.771 67.350  126.434 1.00 33.75  ? 233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 104.436 65.873  126.661 1.00 30.99  ? 233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 104.659 69.341  130.914 1.00 23.22  ? 234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 104.326 69.926  132.205 1.00 22.54  ? 234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 104.237 71.465  132.127 1.00 22.00  ? 234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 103.296 72.077  132.661 1.00 21.73  ? 234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 105.336 69.490  133.266 1.00 22.85  ? 234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 104.894 69.802  134.680 1.00 23.87  ? 234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 105.919 69.394  135.732 1.00 24.95  ? 234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 106.908 68.717  135.431 1.00 24.21  ? 234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 105.696 69.832  136.973 1.00 25.97  ? 234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 105.210 72.079  131.465 1.00 21.27  ? 235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 105.202 73.524  131.262 1.00 21.37  ? 235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 104.024 73.945  130.378 1.00 21.21  ? 235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 103.381 74.963  130.624 1.00 20.75  ? 235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 106.523 73.973  130.621 1.00 20.93  ? 235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 107.797 73.959  131.469 1.00 21.74  ? 235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 109.009 74.320  130.597 1.00 20.15  ? 235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 107.701 74.898  132.671 1.00 20.90  ? 235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 103.771 73.154  129.341 1.00 21.68  ? 236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 102.684 73.410  128.396 1.00 22.40  ? 236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 101.319 73.445  129.104 1.00 23.31  ? 236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 100.552 74.414  128.938 1.00 22.99  ? 236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 102.706 72.371  127.272 1.00 22.81  ? 236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 101.542 72.446  126.304 1.00 23.76  ? 236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 101.387 73.540  125.448 1.00 24.05  ? 236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 100.589 71.431  126.255 1.00 24.04  ? 236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 100.314 73.620  124.568 1.00 24.40  ? 236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 99.513  71.501  125.373 1.00 26.30  ? 236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 99.393  72.594  124.534 1.00 25.80  ? 236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 98.341  72.655  123.664 1.00 28.42  ? 236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 101.040 72.422  129.918 1.00 22.99  ? 237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 99.765  72.333  130.638 1.00 24.46  ? 237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 99.552  73.521  131.562 1.00 23.86  ? 237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 98.451  74.064  131.636 1.00 24.01  ? 237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 99.634  71.003  131.401 1.00 25.21  ? 237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 99.481  69.771  130.479 1.00 30.12  ? 237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 98.171  69.775  129.684 1.00 35.29  ? 237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 97.163  70.340  130.167 1.00 37.71  ? 237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 98.148  69.204  128.569 1.00 39.07  ? 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 100.617 73.942  132.244 1.00 23.25  ? 238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 100.568 75.144  133.073 1.00 23.10  ? 238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 100.347 76.411  132.225 1.00 22.68  ? 238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 99.571  77.296  132.600 1.00 22.73  ? 238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 101.843 75.250  133.912 1.00 23.22  ? 238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 101.841 76.457  134.826 1.00 24.46  ? 238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 101.089 76.513  135.805 1.00 26.28  ? 238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 102.684 77.434  134.514 1.00 24.93  ? 238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 101.007 76.484  131.072 1.00 22.64  ? 239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 100.894 77.654  130.200 1.00 23.18  ? 239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 99.475  77.805  129.624 1.00 23.40  ? 239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 98.986  78.930  129.440 1.00 23.57  ? 239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 101.942 77.611  129.080 1.00 23.19  ? 239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 102.357 79.005  128.551 1.00 24.33  ? 239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 103.074 79.873  129.601 1.00 27.99  ? 239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 103.398 79.383  130.706 1.00 27.36  ? 239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 103.310 81.069  129.323 1.00 28.98  ? 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 98.820  76.675  129.354 1.00 23.35  ? 240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 97.413  76.684  128.923 1.00 23.74  ? 240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 96.504  77.392  129.931 1.00 23.80  ? 240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 95.690  78.254  129.560 1.00 23.33  ? 240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 96.902  75.262  128.677 1.00 24.09  ? 240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 97.467  74.516  127.467 1.00 24.07  ? 240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 96.861  73.121  127.394 1.00 24.77  ? 240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 97.213  75.299  126.163 1.00 24.38  ? 240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 96.640  77.020  131.198 1.00 23.41  ? 241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 95.863  77.637  132.271 1.00 24.02  ? 241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 96.185  79.131  132.431 1.00 22.91  ? 241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 95.285  79.938  132.622 1.00 22.94  ? 241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 96.109  76.893  133.585 1.00 24.92  ? 241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 95.598  75.462  133.600 1.00 27.82  ? 241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 95.839  74.778  134.934 1.00 33.08  ? 241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 96.967  74.292  135.179 1.00 36.94  ? 241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 94.893  74.718  135.741 1.00 37.48  ? 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 97.472  79.478  132.361 1.00 21.84  ? 242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 97.933  80.865  132.379 1.00 21.66  ? 242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 97.335  81.653  131.220 1.00 21.28  ? 242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 96.863  82.784  131.403 1.00 21.14  ? 242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 99.465  80.904  132.267 1.00 21.44  ? 242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 100.107 82.285  132.296 1.00 21.89  ? 242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 100.127 83.044  133.467 1.00 22.52  ? 242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 100.727 82.812  131.160 1.00 22.58  ? 242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 100.735 84.299  133.502 1.00 22.67  ? 242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 101.345 84.068  131.185 1.00 24.03  ? 242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 101.349 84.798  132.369 1.00 23.75  ? 242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 101.947 86.043  132.414 1.00 26.82  ? 242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 97.363  81.054  130.033 1.00 20.66  ? 243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 96.844  81.703  128.820 1.00 20.99  ? 243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 95.342  81.982  128.948 1.00 21.22  ? 243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 94.885  83.098  128.656 1.00 20.95  ? 243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 97.144  80.854  127.554 1.00 20.58  ? 243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 98.559  80.800  127.353 1.00 20.84  ? 243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 96.491  81.455  126.307 1.00 20.90  ? 243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 94.585  80.986  129.410 1.00 21.62  ? 244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 93.145  81.162  129.601 1.00 23.46  ? 244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 92.852  82.240  130.625 1.00 23.33  ? 244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 91.973  83.081  130.429 1.00 22.86  ? 244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 92.466  79.854  130.010 1.00 24.31  ? 244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 92.377  78.835  128.878 1.00 27.63  ? 244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 91.687  77.543  129.306 1.00 33.27  ? 244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 90.814  77.592  130.202 1.00 35.56  ? 244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 92.013  76.478  128.736 1.00 35.96  ? 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 93.602  82.215  131.716 1.00 23.36  ? 245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 93.445  83.200  132.772 1.00 24.18  ? 245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 93.632  84.641  132.261 1.00 23.96  ? 245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 92.889  85.542  132.644 1.00 24.19  ? 245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 94.439  82.900  133.892 1.00 25.14  ? 245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 94.177  83.713  135.122 1.00 27.35  ? 245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 93.044  83.652  135.644 1.00 28.45  ? 245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 95.112  84.416  135.563 1.00 31.99  ? 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 94.608  84.848  131.385 1.00 23.34  ? 246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 94.890  86.189  130.860 1.00 23.53  ? 246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 94.029  86.602  129.677 1.00 22.94  ? 246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 93.589  87.751  129.599 1.00 23.14  ? 246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 96.359  86.299  130.460 1.00 23.37  ? 246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 97.392  86.349  131.588 1.00 26.17  ? 246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 98.766  86.480  130.972 1.00 27.31  ? 246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 97.120  87.525  132.521 1.00 28.08  ? 246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 93.813  85.675  128.748 1.00 22.46  ? 247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 93.213  86.019  127.462 1.00 22.00  ? 247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 91.714  85.823  127.304 1.00 22.26  ? 247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 91.144  86.361  126.354 1.00 22.17  ? 247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 93.946  85.304  126.319 1.00 21.73  ? 247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 95.329  85.848  126.059 1.00 21.49  ? 247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 95.506  87.033  125.336 1.00 19.45  ? 247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 96.461  85.189  126.548 1.00 22.71  ? 247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 96.788  87.554  125.091 1.00 20.30  ? 247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 97.744  85.697  126.316 1.00 21.69  ? 247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 97.894  86.871  125.573 1.00 21.40  ? 247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 99.146  87.373  125.327 1.00 22.11  ? 247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 91.072  85.048  128.185 1.00 22.40  ? 248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 89.614  84.863  128.079 1.00 22.75  ? 248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 88.866  86.197  128.084 1.00 22.55  ? 248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 87.889  86.363  127.344 1.00 22.22  ? 248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 89.055  83.926  129.167 1.00 23.03  ? 248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 89.246  82.455  128.838 1.00 25.02  ? 248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 89.624  82.118  127.696 1.00 26.85  ? 248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 89.008  81.620  129.734 1.00 28.74  ? 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 89.331  87.146  128.901 1.00 22.21  ? 249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 88.665  88.466  128.991 1.00 22.39  ? 249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 88.811  89.340  127.738 1.00 21.65  ? 249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 88.112  90.345  127.605 1.00 21.70  ? 249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 89.095  89.242  130.246 1.00 22.53  ? 249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 90.602  89.597  130.338 1.00 22.73  ? 249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 90.921  90.360  131.608 1.00 25.39  ? 249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 90.127  90.372  132.550 1.00 27.88  ? 249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 92.081  91.011  131.642 1.00 24.88  ? 249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 89.714  88.959  126.832 1.00 20.91  ? 250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 89.895  89.679  125.550 1.00 20.62  ? 250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 89.557  88.792  124.338 1.00 20.53  ? 250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 89.679  89.221  123.179 1.00 20.05  ? 250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 91.314  90.347  125.412 1.00 20.32  ? 250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 91.506  91.438  126.461 1.00 20.35  ? 250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 92.452  89.321  125.509 1.00 19.32  ? 250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 89.123  87.562  124.621 1.00 20.29  ? 251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 88.584  86.659  123.601 1.00 20.51  ? 251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 89.604  85.951  122.723 1.00 20.99  ? 251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 89.268  85.497  121.618 1.00 20.22  ? 251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 90.848  85.850  123.202 1.00 20.76  ? 252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 91.945  85.404  122.338 1.00 21.38  ? 252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 92.638  84.105  122.742 1.00 21.86  ? 252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 93.628  83.719  122.124 1.00 22.45  ? 252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 92.982  86.525  122.154 1.00 21.44  ? 252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 92.525  87.863  121.567 1.00 22.02  ? 252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 93.696  88.839  121.550 1.00 22.86  ? 252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 91.931  87.681  120.153 1.00 23.88  ? 252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 92.115  83.417  123.755 1.00 22.19  ? 253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 92.834  82.296  124.356 1.00 22.47  ? 253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 93.183  81.192  123.357 1.00 22.94  ? 253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 94.308  80.705  123.337 1.00 22.07  ? 253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 92.043  81.719  125.533 1.00 22.91  ? 253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 92.015  82.655  126.592 1.00 24.25  ? 253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 92.224  80.832  122.507 1.00 24.59  ? 254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 92.431  79.767  121.519 1.00 25.66  ? 254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 93.527  80.129  120.504 1.00 26.01  ? 254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 94.351  79.280  120.120 1.00 26.23  ? 254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 91.113  79.445  120.801 1.00 26.89  ? 254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 91.212  78.299  119.843 1.00 29.10  ? 254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 91.686  77.057  120.214 1.00 32.70  ? 254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 90.894  78.202  118.531 1.00 31.68  ? 254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 91.660  76.248  119.170 1.00 33.55  ? 254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 91.170  76.913  118.141 1.00 33.71  ? 254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 93.527  81.386  120.077 1.00 25.93  ? 255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 94.534  81.903  119.155 1.00 26.65  ? 255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 95.941  81.864  119.754 1.00 25.61  ? 255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 96.888  81.423  119.089 1.00 25.34  ? 255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 94.183  83.327  118.720 1.00 27.44  ? 255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 93.825  83.411  117.253 1.00 32.09  ? 255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 94.546  82.797  116.429 1.00 36.67  ? 255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 92.817  84.076  116.918 1.00 36.30  ? 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 96.064  82.326  121.003 1.00 24.17  ? 256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 97.346  82.310  121.719 1.00 23.71  ? 256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 97.856  80.876  121.894 1.00 23.48  ? 256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 99.048  80.615  121.727 1.00 23.08  ? 256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 97.261  83.002  123.108 1.00 23.27  ? 256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 98.617  82.968  123.821 1.00 24.02  ? 256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 96.775  84.439  122.974 1.00 23.35  ? 256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 96.954  79.958  122.228 1.00 23.36  ? 257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 97.308  78.545  122.374 1.00 24.12  ? 257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 97.948  77.965  121.115 1.00 24.30  ? 257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 98.925  77.206  121.197 1.00 24.37  ? 257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 96.094  77.712  122.782 1.00 24.22  ? 257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 95.677  77.897  124.231 1.00 24.96  ? 257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 94.381  77.141  124.488 1.00 26.34  ? 257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 93.903  77.328  125.902 1.00 27.16  ? 257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 92.637  76.557  126.090 1.00 29.60  ? 257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 97.406  78.322  119.952 1.00 24.55  ? 258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 97.997  77.897  118.686 1.00 24.85  ? 258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 99.411  78.456  118.543 1.00 24.57  ? 258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 100.313 77.753  118.088 1.00 24.07  ? 258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 97.134  78.347  117.507 1.00 25.30  ? 258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 95.738  77.767  117.509 1.00 26.63  ? 258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 94.970  78.285  116.299 1.00 29.30  ? 258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 93.637  77.609  116.184 1.00 31.79  ? 258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 92.784  78.362  115.231 1.00 33.80  ? 258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 99.596  79.709  118.963 1.00 24.29  ? 259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 100.894 80.392  118.880 1.00 24.90  ? 259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 101.958 79.735  119.777 1.00 24.86  ? 259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 103.105 79.545  119.358 1.00 24.68  ? 259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 100.708 81.878  119.216 1.00 24.70  ? 259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 101.913 82.747  118.940 1.00 25.70  ? 259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 102.458 82.835  117.659 1.00 26.86  ? 259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 102.477 83.518  119.964 1.00 26.19  ? 259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 103.562 83.660  117.399 1.00 26.66  ? 259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 103.573 84.350  119.714 1.00 26.52  ? 259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 104.120 84.416  118.426 1.00 26.23  ? 259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 101.575 79.379  121.005 1.00 25.53  ? 260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 102.523 78.752  121.929 1.00 26.21  ? 260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 102.919 77.338  121.477 1.00 26.47  ? 260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 104.060 76.931  121.671 1.00 26.52  ? 260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 102.071 78.808  123.429 1.00 26.27  ? 260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 101.009 77.754  123.750 1.00 27.37  ? 260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 101.620 80.237  123.805 1.00 26.92  ? 260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 100.583 77.716  125.218 1.00 29.51  ? 260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 101.994 76.620  120.840 1.00 26.57  ? 261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 102.306 75.303  120.277 1.00 26.84  ? 261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 103.304 75.424  119.126 1.00 27.34  ? 261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 104.260 74.658  119.045 1.00 27.54  ? 261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 101.042 74.564  119.831 1.00 26.98  ? 261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 100.265 73.915  120.961 1.00 26.53  ? 261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 99.181  72.954  120.429 1.00 27.77  ? 261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 98.076  73.652  119.778 1.00 28.67  ? 261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 97.017  74.156  120.415 1.00 29.68  ? 261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 96.065  74.765  119.727 1.00 28.31  ? 261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 96.900  74.046  121.738 1.00 29.15  ? 261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 103.071 76.403  118.253 1.00 27.78  ? 262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 103.995 76.752  117.175 1.00 28.18  ? 262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 105.418 76.986  117.715 1.00 27.08  ? 262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 106.401 76.420  117.213 1.00 26.51  ? 262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 103.483 78.008  116.458 1.00 29.11  ? 262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 104.336 78.472  115.303 1.00 32.56  ? 262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 104.309 77.800  114.080 1.00 36.59  ? 262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 105.161 79.595  115.424 1.00 36.34  ? 262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 105.092 78.225  113.001 1.00 39.47  ? 262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 105.949 80.034  114.343 1.00 39.23  ? 262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 105.906 79.339  113.139 1.00 40.48  ? 262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 106.672 79.748  112.071 1.00 44.00  ? 262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 105.515 77.800  118.757 1.00 26.08  ? 263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 106.806 78.107  119.352 1.00 25.73  ? 263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 107.425 76.971  120.169 1.00 25.24  ? 263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 108.656 76.836  120.200 1.00 25.56  ? 263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 106.736 79.425  120.123 1.00 25.69  ? 263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 106.704 80.620  119.197 1.00 26.39  ? 263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 107.727 81.002  118.622 1.00 26.91  ? 263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 105.530 81.214  119.036 1.00 27.56  ? 263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 106.591 76.140  120.800 1.00 24.51  ? 264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 107.082 74.892  121.415 1.00 24.19  ? 264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 107.863 74.020  120.411 1.00 24.63  ? 264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 108.919 73.481  120.739 1.00 24.01  ? 264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 105.944 74.093  122.022 1.00 23.63  ? 264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 107.337 73.891  119.193 1.00 24.66  ? 265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 108.033 73.173  118.126 1.00 25.24  ? 265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 109.388 73.769  117.758 1.00 25.09  ? 265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 110.328 73.019  117.446 1.00 24.14  ? 265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 107.155 73.054  116.866 1.00 25.62  ? 265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 106.042 72.031  117.028 1.00 26.46  ? 265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 106.036 71.243  117.977 1.00 27.14  ? 265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 105.079 72.050  116.104 1.00 27.89  ? 265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 109.472 75.102  117.779 1.00 24.99  ? 266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 110.721 75.826  117.536 1.00 25.91  ? 266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 111.727 75.574  118.654 1.00 25.23  ? 266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 112.923 75.424  118.392 1.00 25.34  ? 266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 110.484 77.332  117.424 1.00 25.96  ? 266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 109.849 77.809  116.127 1.00 29.60  ? 266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 109.930 79.340  116.073 1.00 34.20  ? 266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 109.411 79.901  114.772 1.00 37.67  ? 266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 109.645 81.381  114.722 1.00 39.48  ? 266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 111.247 75.545  119.894 1.00 24.87  ? 267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 112.101 75.193  121.044 1.00 24.23  ? 267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 112.660 73.771  120.912 1.00 24.24  ? 267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 113.857 73.548  121.103 1.00 23.96  ? 267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 111.339 75.347  122.346 1.00 24.23  ? 267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 111.797 72.811  120.579 1.00 24.63  ? 268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 112.247 71.436  120.347 1.00 25.14  ? 268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 113.291 71.393  119.243 1.00 25.58  ? 268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 114.314 70.732  119.381 1.00 25.42  ? 268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 111.076 70.497  120.017 1.00 25.28  ? 268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 110.179 70.128  121.202 1.00 25.93  ? 268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 108.842 69.599  120.723 1.00 26.50  ? 268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 110.859 69.141  122.170 1.00 25.20  ? 268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 113.043 72.118  118.152 1.00 26.32  ? 269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 114.001 72.147  117.051 1.00 27.41  ? 269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 115.347 72.748  117.450 1.00 26.66  ? 269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 116.392 72.252  117.025 1.00 26.69  ? 269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 113.411 72.826  115.820 1.00 28.28  ? 269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 112.718 71.818  114.903 1.00 32.91  ? 269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 111.722 72.594  113.627 1.00 42.49  ? 269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 110.068 72.276  114.240 1.00 38.74  ? 269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 115.318 73.784  118.290 1.00 25.48  ? 270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 116.544 74.385  118.840 1.00 25.39  ? 270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 117.372 73.374  119.651 1.00 25.18  ? 270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 118.601 73.499  119.757 1.00 24.73  ? 270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 116.211 75.614  119.696 1.00 24.83  ? 270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 115.828 76.837  118.856 1.00 25.58  ? 270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 116.032 76.867  117.646 1.00 25.58  ? 270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 115.272 77.847  119.507 1.00 24.32  ? 270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 116.678 72.367  120.188 1.00 25.09  ? 271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 117.284 71.258  120.938 1.00 25.46  ? 271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 117.638 70.032  120.079 1.00 26.18  ? 271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 118.132 69.013  120.595 1.00 26.06  ? 271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 116.365 70.858  122.099 1.00 25.19  ? 271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 116.183 71.921  123.196 1.00 25.03  ? 271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 115.042 71.545  124.115 1.00 24.50  ? 271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 117.489 72.104  123.987 1.00 25.64  ? 271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 117.390 70.131  118.774 1.00 26.71  ? 272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 117.662 69.030  117.842 1.00 28.06  ? 272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 116.630 67.914  117.845 1.00 29.34  ? 272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 116.925 66.782  117.433 1.00 29.73  ? 272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 115.420 68.224  118.308 1.00 29.88  ? 273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 114.332 67.252  118.377 1.00 31.24  ? 273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 113.254 67.549  117.326 1.00 32.42  ? 273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 113.131 68.685  116.846 1.00 32.30  ? 273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 113.716 67.218  119.781 1.00 30.82  ? 273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 114.687 66.827  120.876 1.00 30.93  ? 273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 115.510 65.709  120.744 1.00 30.85  ? 273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 114.766 67.573  122.043 1.00 30.30  ? 273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 116.405 65.357  121.752 1.00 30.75  ? 273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 115.648 67.221  123.067 1.00 30.41  ? 273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 116.466 66.108  122.924 1.00 30.88  ? 273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 112.492 66.518  116.967 1.00 33.81  ? 274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 111.374 66.649  116.027 1.00 35.32  ? 274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 110.215 67.461  116.632 1.00 35.36  ? 274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 110.000 67.414  117.841 1.00 34.78  ? 274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 110.854 65.261  115.628 1.00 35.95  ? 274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 111.887 64.430  114.871 1.00 37.98  ? 274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 112.773 65.003  114.200 1.00 39.83  ? 274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 111.802 63.186  114.949 1.00 40.03  ? 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 109.463 68.199  115.793 1.00 36.33  ? 275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 108.256 68.903  116.280 1.00 36.92  ? 275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 107.248 67.957  116.953 1.00 37.68  ? 275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 107.097 66.809  116.525 1.00 38.07  ? 275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 107.656 69.512  115.003 1.00 36.82  ? 275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 108.377 68.830  113.847 1.00 37.42  ? 275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 109.731 68.485  114.372 1.00 36.41  ? 275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 106.572 68.442  117.995 1.00 38.10  ? 276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 105.675 67.617  118.817 1.00 38.96  ? 276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 104.192 67.923  118.573 1.00 39.71  ? 276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 103.334 67.051  118.744 1.00 40.18  ? 276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 106.015 67.827  120.297 1.00 38.94  ? 276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 105.271 66.982  121.310 1.00 39.64  ? 276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 105.674 65.676  121.597 1.00 40.43  ? 276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 104.204 67.510  122.029 1.00 41.04  ? 276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 105.001 64.905  122.546 1.00 41.69  ? 276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 103.522 66.750  122.979 1.00 41.60  ? 276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 103.928 65.452  123.236 1.00 41.92  ? 276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 103.257 64.708  124.183 1.00 42.52  ? 276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 103.892 69.159  118.190 1.00 39.85  ? 277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 102.512 69.563  117.946 1.00 40.77  ? 277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 102.247 69.688  116.453 1.00 41.95  ? 277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 103.151 70.023  115.689 1.00 41.91  ? 277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 102.209 70.890  118.650 1.00 39.94  ? 277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 102.311 70.822  120.150 1.00 39.09  ? 277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 101.325 70.188  120.902 1.00 37.84  ? 277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 103.383 71.407  120.813 1.00 38.97  ? 277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 101.412 70.129  122.287 1.00 37.46  ? 277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 103.483 71.356  122.201 1.00 38.20  ? 277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 102.494 70.716  122.940 1.00 37.91  ? 277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 101.012 69.417  116.031 1.00 43.74  ? 278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 100.658 69.561  114.615 1.00 45.61  ? 278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 100.566 71.038  114.230 1.00 46.04  ? 278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 100.229 71.885  115.057 1.00 45.88  ? 278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 99.348  68.839  114.278 1.00 46.43  ? 278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 99.297  68.313  112.833 1.00 48.82  ? 278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 97.886  68.054  112.330 1.00 51.86  ? 278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 96.914  68.266  113.093 1.00 53.35  ? 278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 97.745  67.639  111.157 1.00 53.10  ? 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 100.883 71.335  112.971 1.00 47.16  ? 279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 100.827 72.701  112.439 1.00 47.75  ? 279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 99.397  73.259  112.395 1.00 47.71  ? 279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 98.447  72.532  112.081 1.00 47.77  ? 279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 101.487 72.761  111.050 1.00 48.42  ? 279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 100.988 71.707  110.055 1.00 50.63  ? 279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 101.988 71.416  108.935 1.00 53.06  ? 279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 102.426 72.371  108.249 1.00 54.35  ? 279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 102.326 70.227  108.735 1.00 53.32  ? 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 99.262  74.542  112.731 1.00 47.40  ? 280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 97.976  75.252  112.711 1.00 47.46  ? 280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 98.149  76.661  112.130 1.00 47.31  ? 280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 99.251  77.215  112.158 1.00 47.21  ? 280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 97.390  75.360  114.126 1.00 47.19  ? 280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 97.085  74.035  114.827 1.00 47.14  ? 280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 97.006  74.184  116.343 1.00 47.21  ? 280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 98.065  74.365  116.991 1.00 46.97  ? 280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 95.883  74.131  116.886 1.00 46.13  ? 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 97.064  77.236  111.611 1.00 47.15  ? 281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 97.094  78.604  111.084 1.00 47.04  ? 281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 97.130  79.625  112.226 1.00 46.05  ? 281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 96.209  79.683  113.047 1.00 46.10  ? 281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 95.886  78.881  110.171 1.00 47.66  ? 281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 95.985  78.183  108.812 1.00 49.53  ? 281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 97.106  78.041  108.274 1.00 50.58  ? 281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 94.923  77.796  108.266 1.00 51.14  ? 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 98.203  80.412  112.276 1.00 44.96  ? 282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 98.356  81.486  113.263 1.00 43.99  ? 282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 97.667  82.756  112.753 1.00 43.53  ? 282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 97.643  83.003  111.546 1.00 43.52  ? 282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 99.857  81.778  113.556 1.00 43.84  ? 282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 100.602 80.500  113.986 1.00 43.91  ? 282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 100.024 82.912  114.583 1.00 43.55  ? 282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 100.049 79.807  115.235 1.00 42.76  ? 282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 97.101  83.545  113.668 1.00 42.51  ? 283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 96.463  84.813  113.313 1.00 41.93  ? 283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 97.397  85.654  112.428 1.00 41.78  ? 283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 98.520  85.971  112.844 1.00 41.13  ? 283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 96.076  85.588  114.581 1.00 41.83  ? 283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 95.000  86.646  114.333 1.00 41.27  ? 283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 95.057  87.403  113.367 1.00 41.28  ? 283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 94.020  86.700  115.222 1.00 40.67  ? 283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 96.947  86.001  111.197 1.00 41.74  ? 284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 97.816  86.739  110.266 1.00 41.82  ? 284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 98.211  88.126  110.784 1.00 41.56  ? 284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 99.231  88.673  110.359 1.00 41.46  ? 284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 96.971  86.844  108.982 1.00 42.14  ? 284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 95.567  86.631  109.414 1.00 42.59  ? 284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 95.633  85.695  110.596 1.00 42.05  ? 284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 97.418  88.672  111.704 1.00 41.19  ? 285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 97.738  89.934  112.371 1.00 41.47  ? 285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 99.065  89.812  113.131 1.00 41.71  ? 285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 99.929  90.681  113.029 1.00 41.38  ? 285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 96.613  90.360  113.352 1.00 41.22  ? 285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 95.297  90.599  112.599 1.00 41.27  ? 285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 97.024  91.593  114.154 1.00 40.37  ? 285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 94.073  90.649  113.503 1.00 41.85  ? 285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 99.207  88.723  113.886 1.00 42.33  ? 286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 100.427 88.438  114.650 1.00 43.36  ? 286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 101.641 88.225  113.737 1.00 44.51  ? 286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 102.754 88.615  114.087 1.00 44.57  ? 286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 100.213 87.248  115.616 1.00 42.97  ? 286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 101.547 86.707  116.157 1.00 42.86  ? 286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 99.307  87.681  116.753 1.00 41.93  ? 286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 101.406 87.631  112.568 1.00 46.21  ? 287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 102.441 87.426  111.544 1.00 47.66  ? 287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 102.900 88.740  110.913 1.00 48.82  ? 287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 104.082 88.895  110.577 1.00 49.02  ? 287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 101.950 86.450  110.466 1.00 47.95  ? 287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 102.224 84.948  110.654 1.00 48.23  ? 287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 102.380 84.522  112.121 1.00 48.10  ? 287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 101.167 84.102  109.950 1.00 48.81  ? 287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 101.963 89.676  110.754 1.00 49.80  ? 288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 102.291 91.050  110.382 1.00 51.09  ? 288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 102.987 91.815  111.512 1.00 51.08  ? 288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 103.721 92.769  111.257 1.00 51.41  ? 288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 101.049 91.803  109.899 1.00 51.37  ? 288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 100.709 91.493  108.454 1.00 53.22  ? 288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 100.696 90.331  108.037 1.00 54.39  ? 288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 100.432 92.536  107.678 1.00 54.70  ? 288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 102.751 91.390  112.753 1.00 51.25  ? 289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 103.454 91.928  113.920 1.00 51.35  ? 289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 104.943 91.609  113.927 1.00 51.86  ? 289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 105.727 92.292  114.596 1.00 51.49  ? 289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 105.332 90.570  113.187 1.00 52.45  ? 290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 106.738 90.183  113.049 1.00 52.99  ? 290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 107.417 90.940  111.905 1.00 53.65  ? 290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 107.138 90.705  110.723 1.00 54.22  ? 290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 106.866 88.671  112.834 1.00 53.08  ? 290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 106.602 87.724  114.008 1.00 53.33  ? 290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 106.410 86.301  113.506 1.00 53.79  ? 290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 107.728 87.785  115.043 1.00 53.22  ? 290 LEU C CD2   1 
ATOM   13364 N  N     . THR C 2 332 ? 144.570 108.410 110.172 1.00 29.81  ? 311 THR C N     1 
ATOM   13365 C  CA    . THR C 2 332 ? 145.241 107.983 111.393 1.00 29.93  ? 311 THR C CA    1 
ATOM   13366 C  C     . THR C 2 332 ? 145.916 109.158 112.092 1.00 29.61  ? 311 THR C C     1 
ATOM   13367 O  O     . THR C 2 332 ? 145.491 110.301 111.949 1.00 37.54  ? 311 THR C O     1 
ATOM   13368 C  CB    . THR C 2 332 ? 146.291 106.894 111.111 1.00 35.93  ? 311 THR C CB    1 
ATOM   13369 O  OG1   . THR C 2 332 ? 147.534 107.508 110.748 1.00 42.31  ? 311 THR C OG1   1 
ATOM   13370 C  CG2   . THR C 2 332 ? 145.829 105.987 109.982 1.00 32.23  ? 311 THR C CG2   1 
ATOM   13371 N  N     . VAL C 2 333 ? 146.965 108.861 112.857 1.00 26.16  ? 312 VAL C N     1 
ATOM   13372 C  CA    . VAL C 2 333 ? 147.684 109.866 113.632 1.00 21.22  ? 312 VAL C CA    1 
ATOM   13373 C  C     . VAL C 2 333 ? 149.145 109.749 113.180 1.00 25.73  ? 312 VAL C C     1 
ATOM   13374 O  O     . VAL C 2 333 ? 150.095 109.954 113.944 1.00 29.77  ? 312 VAL C O     1 
ATOM   13375 C  CB    . VAL C 2 333 ? 147.400 109.656 115.145 1.00 22.98  ? 312 VAL C CB    1 
ATOM   13376 C  CG1   . VAL C 2 333 ? 148.494 110.127 116.111 1.00 26.04  ? 312 VAL C CG1   1 
ATOM   13377 C  CG2   . VAL C 2 333 ? 146.067 110.299 115.515 1.00 25.62  ? 312 VAL C CG2   1 
ATOM   13378 N  N     . GLU C 2 334 ? 149.326 109.429 111.900 1.00 25.38  ? 313 GLU C N     1 
ATOM   13379 C  CA    . GLU C 2 334 ? 150.658 109.185 111.358 1.00 29.10  ? 313 GLU C CA    1 
ATOM   13380 C  C     . GLU C 2 334 ? 151.574 110.380 111.612 1.00 31.44  ? 313 GLU C C     1 
ATOM   13381 O  O     . GLU C 2 334 ? 151.244 111.511 111.234 1.00 31.58  ? 313 GLU C O     1 
ATOM   13382 C  CB    . GLU C 2 334 ? 150.577 108.904 109.858 1.00 30.13  ? 313 GLU C CB    1 
ATOM   13383 C  CG    . GLU C 2 334 ? 151.868 108.390 109.246 1.00 30.08  ? 313 GLU C CG    1 
ATOM   13384 C  CD    . GLU C 2 334 ? 151.716 108.038 107.779 1.00 34.97  ? 313 GLU C CD    1 
ATOM   13385 O  OE1   . GLU C 2 334 ? 150.578 108.098 107.267 1.00 29.34  ? 313 GLU C OE1   1 
ATOM   13386 O  OE2   . GLU C 2 334 ? 152.734 107.706 107.136 1.00 31.58  ? 313 GLU C OE2   1 
ATOM   13387 N  N     . PRO C 2 335 ? 152.724 110.169 112.250 1.00 24.98  ? 314 PRO C N     1 
ATOM   13388 C  CA    . PRO C 2 335 ? 153.635 111.284 112.537 1.00 29.75  ? 314 PRO C CA    1 
ATOM   13389 C  C     . PRO C 2 335 ? 154.362 111.770 111.293 1.00 28.75  ? 314 PRO C C     1 
ATOM   13390 O  O     . PRO C 2 335 ? 154.473 111.061 110.291 1.00 32.13  ? 314 PRO C O     1 
ATOM   13391 C  CB    . PRO C 2 335 ? 154.621 110.681 113.548 1.00 23.64  ? 314 PRO C CB    1 
ATOM   13392 C  CG    . PRO C 2 335 ? 153.918 109.471 114.095 1.00 23.36  ? 314 PRO C CG    1 
ATOM   13393 C  CD    . PRO C 2 335 ? 153.152 108.936 112.928 1.00 25.64  ? 314 PRO C CD    1 
ATOM   13394 N  N     . LEU C 2 336 ? 154.858 113.002 111.371 1.00 22.20  ? 315 LEU C N     1 
ATOM   13395 C  CA    . LEU C 2 336 ? 155.660 113.568 110.298 1.00 20.58  ? 315 LEU C CA    1 
ATOM   13396 C  C     . LEU C 2 336 ? 157.079 113.013 110.328 1.00 24.93  ? 315 LEU C C     1 
ATOM   13397 O  O     . LEU C 2 336 ? 157.604 112.638 111.380 1.00 24.32  ? 315 LEU C O     1 
ATOM   13398 C  CB    . LEU C 2 336 ? 155.710 115.091 110.412 1.00 19.66  ? 315 LEU C CB    1 
ATOM   13399 C  CG    . LEU C 2 336 ? 154.489 115.895 109.968 1.00 20.82  ? 315 LEU C CG    1 
ATOM   13400 C  CD1   . LEU C 2 336 ? 154.412 117.196 110.747 1.00 21.77  ? 315 LEU C CD1   1 
ATOM   13401 C  CD2   . LEU C 2 336 ? 154.556 116.166 108.479 1.00 18.31  ? 315 LEU C CD2   1 
ATOM   13402 N  N     . LYS C 2 337 ? 157.703 112.969 109.155 1.00 26.00  ? 316 LYS C N     1 
ATOM   13403 C  CA    . LYS C 2 337 ? 159.115 112.643 109.025 1.00 23.07  ? 316 LYS C CA    1 
ATOM   13404 C  C     . LYS C 2 337 ? 159.844 113.811 108.374 1.00 26.80  ? 316 LYS C C     1 
ATOM   13405 O  O     . LYS C 2 337 ? 159.241 114.816 107.989 1.00 26.38  ? 316 LYS C O     1 
ATOM   13406 C  CB    . LYS C 2 337 ? 159.327 111.353 108.218 1.00 23.23  ? 316 LYS C CB    1 
ATOM   13407 C  CG    . LYS C 2 337 ? 158.428 111.203 107.004 1.00 24.82  ? 316 LYS C CG    1 
ATOM   13408 C  CD    . LYS C 2 337 ? 158.497 109.796 106.430 1.00 20.69  ? 316 LYS C CD    1 
ATOM   13409 C  CE    . LYS C 2 337 ? 158.305 108.740 107.508 1.00 24.72  ? 316 LYS C CE    1 
ATOM   13410 N  NZ    . LYS C 2 337 ? 157.032 108.928 108.257 1.00 24.81  ? 316 LYS C NZ    1 
ATOM   13411 N  N     . ASP C 2 338 ? 161.165 113.673 108.260 1.00 23.93  ? 317 ASP C N     1 
ATOM   13412 C  CA    . ASP C 2 338 ? 161.992 114.749 107.729 1.00 19.78  ? 317 ASP C CA    1 
ATOM   13413 C  C     . ASP C 2 338 ? 161.723 115.046 106.260 1.00 21.25  ? 317 ASP C C     1 
ATOM   13414 O  O     . ASP C 2 338 ? 162.088 116.129 105.792 1.00 13.62  ? 317 ASP C O     1 
ATOM   13415 C  CB    . ASP C 2 338 ? 163.473 114.414 107.922 1.00 24.09  ? 317 ASP C CB    1 
ATOM   13416 C  CG    . ASP C 2 338 ? 163.999 114.856 109.273 1.00 26.41  ? 317 ASP C CG    1 
ATOM   13417 O  OD1   . ASP C 2 338 ? 164.360 116.043 109.413 1.00 25.77  ? 317 ASP C OD1   1 
ATOM   13418 O  OD2   . ASP C 2 338 ? 164.050 114.017 110.198 1.00 24.73  ? 317 ASP C OD2   1 
ATOM   13419 N  N     . ASP C 2 339 ? 161.096 114.127 105.524 1.00 26.19  ? 318 ASP C N     1 
ATOM   13420 C  CA    . ASP C 2 339 ? 160.888 114.304 104.094 1.00 17.33  ? 318 ASP C CA    1 
ATOM   13421 C  C     . ASP C 2 339 ? 159.567 114.977 103.748 1.00 19.67  ? 318 ASP C C     1 
ATOM   13422 O  O     . ASP C 2 339 ? 159.319 115.237 102.565 1.00 24.94  ? 318 ASP C O     1 
ATOM   13423 C  CB    . ASP C 2 339 ? 160.971 112.953 103.375 1.00 20.90  ? 318 ASP C CB    1 
ATOM   13424 C  CG    . ASP C 2 339 ? 162.269 112.781 102.610 1.00 25.28  ? 318 ASP C CG    1 
ATOM   13425 O  OD1   . ASP C 2 339 ? 163.300 113.325 103.056 1.00 27.27  ? 318 ASP C OD1   1 
ATOM   13426 O  OD2   . ASP C 2 339 ? 162.257 112.102 101.561 1.00 26.46  ? 318 ASP C OD2   1 
ATOM   13427 N  N     . ASP C 2 340 ? 158.716 115.268 104.732 1.00 15.21  ? 319 ASP C N     1 
ATOM   13428 C  CA    . ASP C 2 340 ? 157.491 116.010 104.459 1.00 12.08  ? 319 ASP C CA    1 
ATOM   13429 C  C     . ASP C 2 340 ? 157.696 117.516 104.495 1.00 12.59  ? 319 ASP C C     1 
ATOM   13430 O  O     . ASP C 2 340 ? 156.751 118.260 104.212 1.00 22.52  ? 319 ASP C O     1 
ATOM   13431 C  CB    . ASP C 2 340 ? 156.393 115.630 105.456 1.00 12.56  ? 319 ASP C CB    1 
ATOM   13432 C  CG    . ASP C 2 340 ? 156.427 114.168 105.839 1.00 22.56  ? 319 ASP C CG    1 
ATOM   13433 O  OD1   . ASP C 2 340 ? 156.031 113.321 105.011 1.00 22.79  ? 319 ASP C OD1   1 
ATOM   13434 O  OD2   . ASP C 2 340 ? 156.826 113.869 106.982 1.00 23.49  ? 319 ASP C OD2   1 
ATOM   13435 N  N     . PHE C 2 341 ? 158.896 117.982 104.837 1.00 9.55   ? 320 PHE C N     1 
ATOM   13436 C  CA    . PHE C 2 341 ? 159.184 119.408 104.922 1.00 13.62  ? 320 PHE C CA    1 
ATOM   13437 C  C     . PHE C 2 341 ? 159.929 119.921 103.697 1.00 16.13  ? 320 PHE C C     1 
ATOM   13438 O  O     . PHE C 2 341 ? 160.261 121.111 103.639 1.00 15.03  ? 320 PHE C O     1 
ATOM   13439 C  CB    . PHE C 2 341 ? 159.982 119.704 106.193 1.00 6.93   ? 320 PHE C CB    1 
ATOM   13440 C  CG    . PHE C 2 341 ? 159.188 119.528 107.455 1.00 0.01   ? 320 PHE C CG    1 
ATOM   13441 C  CD1   . PHE C 2 341 ? 158.436 120.568 107.969 1.00 8.08   ? 320 PHE C CD1   1 
ATOM   13442 C  CD2   . PHE C 2 341 ? 159.183 118.313 108.118 1.00 8.21   ? 320 PHE C CD2   1 
ATOM   13443 C  CE1   . PHE C 2 341 ? 157.703 120.404 109.128 1.00 8.05   ? 320 PHE C CE1   1 
ATOM   13444 C  CE2   . PHE C 2 341 ? 158.449 118.142 109.274 1.00 13.50  ? 320 PHE C CE2   1 
ATOM   13445 C  CZ    . PHE C 2 341 ? 157.709 119.189 109.779 1.00 10.00  ? 320 PHE C CZ    1 
ATOM   13446 N  N     . TYR C 2 342 ? 160.196 119.059 102.720 1.00 14.67  ? 321 TYR C N     1 
ATOM   13447 C  CA    . TYR C 2 342 ? 160.803 119.458 101.460 1.00 16.49  ? 321 TYR C CA    1 
ATOM   13448 C  C     . TYR C 2 342 ? 159.951 118.927 100.319 1.00 17.43  ? 321 TYR C C     1 
ATOM   13449 O  O     . TYR C 2 342 ? 159.492 117.783 100.359 1.00 18.36  ? 321 TYR C O     1 
ATOM   13450 C  CB    . TYR C 2 342 ? 162.242 118.941 101.329 1.00 14.04  ? 321 TYR C CB    1 
ATOM   13451 C  CG    . TYR C 2 342 ? 163.092 119.161 102.560 1.00 13.14  ? 321 TYR C CG    1 
ATOM   13452 C  CD1   . TYR C 2 342 ? 163.732 120.374 102.777 1.00 18.54  ? 321 TYR C CD1   1 
ATOM   13453 C  CD2   . TYR C 2 342 ? 163.258 118.155 103.503 1.00 12.64  ? 321 TYR C CD2   1 
ATOM   13454 C  CE1   . TYR C 2 342 ? 164.512 120.581 103.898 1.00 19.00  ? 321 TYR C CE1   1 
ATOM   13455 C  CE2   . TYR C 2 342 ? 164.037 118.353 104.627 1.00 18.18  ? 321 TYR C CE2   1 
ATOM   13456 C  CZ    . TYR C 2 342 ? 164.660 119.567 104.820 1.00 18.87  ? 321 TYR C CZ    1 
ATOM   13457 O  OH    . TYR C 2 342 ? 165.436 119.767 105.939 1.00 19.85  ? 321 TYR C OH    1 
ATOM   13458 N  N     . PHE C 2 343 ? 159.741 119.764 99.309  1.00 17.75  ? 322 PHE C N     1 
ATOM   13459 C  CA    . PHE C 2 343 ? 158.898 119.394 98.180  1.00 21.55  ? 322 PHE C CA    1 
ATOM   13460 C  C     . PHE C 2 343 ? 159.623 119.615 96.858  1.00 24.96  ? 322 PHE C C     1 
ATOM   13461 O  O     . PHE C 2 343 ? 160.495 120.477 96.749  1.00 18.59  ? 322 PHE C O     1 
ATOM   13462 C  CB    . PHE C 2 343 ? 157.593 120.194 98.207  1.00 23.80  ? 322 PHE C CB    1 
ATOM   13463 C  CG    . PHE C 2 343 ? 156.791 120.001 99.462  1.00 14.87  ? 322 PHE C CG    1 
ATOM   13464 C  CD1   . PHE C 2 343 ? 155.901 118.948 99.576  1.00 19.68  ? 322 PHE C CD1   1 
ATOM   13465 C  CD2   . PHE C 2 343 ? 156.928 120.875 100.529 1.00 11.74  ? 322 PHE C CD2   1 
ATOM   13466 C  CE1   . PHE C 2 343 ? 155.162 118.768 100.730 1.00 17.81  ? 322 PHE C CE1   1 
ATOM   13467 C  CE2   . PHE C 2 343 ? 156.192 120.700 101.684 1.00 12.99  ? 322 PHE C CE2   1 
ATOM   13468 C  CZ    . PHE C 2 343 ? 155.307 119.645 101.784 1.00 15.33  ? 322 PHE C CZ    1 
ATOM   13469 N  N     . ASP D 2 37  ? 119.928 104.478 147.005 1.00 32.44  ? 16  ASP D N     1 
ATOM   13470 C  CA    . ASP D 2 37  ? 120.099 105.887 146.639 1.00 32.83  ? 16  ASP D CA    1 
ATOM   13471 C  C     . ASP D 2 37  ? 120.940 106.106 145.382 1.00 31.65  ? 16  ASP D C     1 
ATOM   13472 O  O     . ASP D 2 37  ? 121.057 107.243 144.917 1.00 32.65  ? 16  ASP D O     1 
ATOM   13473 C  CB    . ASP D 2 37  ? 120.765 106.668 147.783 1.00 33.73  ? 16  ASP D CB    1 
ATOM   13474 C  CG    . ASP D 2 37  ? 119.906 106.747 149.035 1.00 36.81  ? 16  ASP D CG    1 
ATOM   13475 O  OD1   . ASP D 2 37  ? 118.676 106.525 148.955 1.00 39.69  ? 16  ASP D OD1   1 
ATOM   13476 O  OD2   . ASP D 2 37  ? 120.480 107.031 150.114 1.00 39.67  ? 16  ASP D OD2   1 
ATOM   13477 N  N     . PHE D 2 38  ? 121.527 105.044 144.834 1.00 29.55  ? 17  PHE D N     1 
ATOM   13478 C  CA    . PHE D 2 38  ? 122.600 105.232 143.856 1.00 27.75  ? 17  PHE D CA    1 
ATOM   13479 C  C     . PHE D 2 38  ? 122.614 104.304 142.630 1.00 26.21  ? 17  PHE D C     1 
ATOM   13480 O  O     . PHE D 2 38  ? 123.250 104.625 141.633 1.00 25.93  ? 17  PHE D O     1 
ATOM   13481 C  CB    . PHE D 2 38  ? 123.965 105.187 144.579 1.00 27.37  ? 17  PHE D CB    1 
ATOM   13482 C  CG    . PHE D 2 38  ? 124.225 103.891 145.300 1.00 27.32  ? 17  PHE D CG    1 
ATOM   13483 C  CD1   . PHE D 2 38  ? 124.750 102.796 144.620 1.00 27.01  ? 17  PHE D CD1   1 
ATOM   13484 C  CD2   . PHE D 2 38  ? 123.945 103.761 146.655 1.00 28.02  ? 17  PHE D CD2   1 
ATOM   13485 C  CE1   . PHE D 2 38  ? 124.986 101.591 145.280 1.00 27.66  ? 17  PHE D CE1   1 
ATOM   13486 C  CE2   . PHE D 2 38  ? 124.172 102.561 147.317 1.00 27.68  ? 17  PHE D CE2   1 
ATOM   13487 C  CZ    . PHE D 2 38  ? 124.695 101.472 146.626 1.00 27.47  ? 17  PHE D CZ    1 
ATOM   13488 N  N     . THR D 2 39  ? 121.926 103.169 142.700 1.00 24.88  ? 18  THR D N     1 
ATOM   13489 C  CA    . THR D 2 39  ? 122.031 102.144 141.649 1.00 23.81  ? 18  THR D CA    1 
ATOM   13490 C  C     . THR D 2 39  ? 121.524 102.596 140.267 1.00 23.56  ? 18  THR D C     1 
ATOM   13491 O  O     . THR D 2 39  ? 122.152 102.321 139.245 1.00 23.02  ? 18  THR D O     1 
ATOM   13492 C  CB    . THR D 2 39  ? 121.413 100.797 142.098 1.00 23.40  ? 18  THR D CB    1 
ATOM   13493 O  OG1   . THR D 2 39  ? 122.334 100.130 142.971 1.00 23.77  ? 18  THR D OG1   1 
ATOM   13494 C  CG2   . THR D 2 39  ? 121.139 99.883  140.916 1.00 22.31  ? 18  THR D CG2   1 
ATOM   13495 N  N     . GLN D 2 40  ? 120.402 103.303 140.228 1.00 23.78  ? 19  GLN D N     1 
ATOM   13496 C  CA    . GLN D 2 40  ? 119.901 103.787 138.938 1.00 23.88  ? 19  GLN D CA    1 
ATOM   13497 C  C     . GLN D 2 40  ? 120.841 104.814 138.302 1.00 24.09  ? 19  GLN D C     1 
ATOM   13498 O  O     . GLN D 2 40  ? 121.091 104.770 137.105 1.00 23.15  ? 19  GLN D O     1 
ATOM   13499 C  CB    . GLN D 2 40  ? 118.471 104.318 139.055 1.00 24.53  ? 19  GLN D CB    1 
ATOM   13500 C  CG    . GLN D 2 40  ? 117.473 103.208 139.349 1.00 24.06  ? 19  GLN D CG    1 
ATOM   13501 C  CD    . GLN D 2 40  ? 116.045 103.586 139.031 1.00 25.83  ? 19  GLN D CD    1 
ATOM   13502 O  OE1   . GLN D 2 40  ? 115.792 104.591 138.370 1.00 25.90  ? 19  GLN D OE1   1 
ATOM   13503 N  NE2   . GLN D 2 40  ? 115.098 102.763 139.482 1.00 23.56  ? 19  GLN D NE2   1 
ATOM   13504 N  N     . MET D 2 41  ? 121.397 105.706 139.112 1.00 24.07  ? 20  MET D N     1 
ATOM   13505 C  CA    . MET D 2 41  ? 122.414 106.638 138.624 1.00 25.53  ? 20  MET D CA    1 
ATOM   13506 C  C     . MET D 2 41  ? 123.643 105.918 138.035 1.00 24.24  ? 20  MET D C     1 
ATOM   13507 O  O     . MET D 2 41  ? 124.138 106.297 136.969 1.00 23.16  ? 20  MET D O     1 
ATOM   13508 C  CB    . MET D 2 41  ? 122.825 107.599 139.745 1.00 26.79  ? 20  MET D CB    1 
ATOM   13509 C  CG    . MET D 2 41  ? 123.899 108.599 139.365 1.00 32.62  ? 20  MET D CG    1 
ATOM   13510 S  SD    . MET D 2 41  ? 124.522 109.431 140.846 1.00 44.01  ? 20  MET D SD    1 
ATOM   13511 C  CE    . MET D 2 41  ? 126.163 109.918 140.305 1.00 41.93  ? 20  MET D CE    1 
ATOM   13512 N  N     . PHE D 2 42  ? 124.124 104.875 138.715 1.00 23.31  ? 21  PHE D N     1 
ATOM   13513 C  CA    . PHE D 2 42  ? 125.269 104.121 138.204 1.00 23.44  ? 21  PHE D CA    1 
ATOM   13514 C  C     . PHE D 2 42  ? 124.913 103.299 136.981 1.00 23.55  ? 21  PHE D C     1 
ATOM   13515 O  O     . PHE D 2 42  ? 125.736 103.132 136.089 1.00 23.74  ? 21  PHE D O     1 
ATOM   13516 C  CB    . PHE D 2 42  ? 125.901 103.246 139.289 1.00 22.97  ? 21  PHE D CB    1 
ATOM   13517 C  CG    . PHE D 2 42  ? 126.902 103.978 140.111 1.00 23.86  ? 21  PHE D CG    1 
ATOM   13518 C  CD1   . PHE D 2 42  ? 126.496 104.769 141.169 1.00 24.55  ? 21  PHE D CD1   1 
ATOM   13519 C  CD2   . PHE D 2 42  ? 128.258 103.914 139.799 1.00 24.06  ? 21  PHE D CD2   1 
ATOM   13520 C  CE1   . PHE D 2 42  ? 127.429 105.477 141.932 1.00 25.78  ? 21  PHE D CE1   1 
ATOM   13521 C  CE2   . PHE D 2 42  ? 129.197 104.617 140.556 1.00 25.25  ? 21  PHE D CE2   1 
ATOM   13522 C  CZ    . PHE D 2 42  ? 128.772 105.405 141.624 1.00 25.79  ? 21  PHE D CZ    1 
ATOM   13523 N  N     . TYR D 2 43  ? 123.676 102.807 136.942 1.00 24.08  ? 22  TYR D N     1 
ATOM   13524 C  CA    . TYR D 2 43  ? 123.166 102.132 135.759 1.00 24.74  ? 22  TYR D CA    1 
ATOM   13525 C  C     . TYR D 2 43  ? 123.332 103.045 134.542 1.00 25.72  ? 22  TYR D C     1 
ATOM   13526 O  O     . TYR D 2 43  ? 123.878 102.633 133.514 1.00 25.56  ? 22  TYR D O     1 
ATOM   13527 C  CB    . TYR D 2 43  ? 121.694 101.721 135.923 1.00 24.90  ? 22  TYR D CB    1 
ATOM   13528 C  CG    . TYR D 2 43  ? 121.112 101.172 134.628 1.00 24.38  ? 22  TYR D CG    1 
ATOM   13529 C  CD1   . TYR D 2 43  ? 120.535 102.023 133.682 1.00 23.96  ? 22  TYR D CD1   1 
ATOM   13530 C  CD2   . TYR D 2 43  ? 121.194 99.818  134.329 1.00 24.73  ? 22  TYR D CD2   1 
ATOM   13531 C  CE1   . TYR D 2 43  ? 120.018 101.533 132.481 1.00 23.42  ? 22  TYR D CE1   1 
ATOM   13532 C  CE2   . TYR D 2 43  ? 120.694 99.314  133.126 1.00 26.65  ? 22  TYR D CE2   1 
ATOM   13533 C  CZ    . TYR D 2 43  ? 120.107 100.177 132.213 1.00 25.68  ? 22  TYR D CZ    1 
ATOM   13534 O  OH    . TYR D 2 43  ? 119.603 99.689  131.029 1.00 26.57  ? 22  TYR D OH    1 
ATOM   13535 N  N     . ASN D 2 44  ? 122.849 104.278 134.674 1.00 26.77  ? 23  ASN D N     1 
ATOM   13536 C  CA    . ASN D 2 44  ? 122.908 105.261 133.598 1.00 28.57  ? 23  ASN D CA    1 
ATOM   13537 C  C     . ASN D 2 44  ? 124.328 105.529 133.136 1.00 28.70  ? 23  ASN D C     1 
ATOM   13538 O  O     . ASN D 2 44  ? 124.619 105.435 131.941 1.00 28.99  ? 23  ASN D O     1 
ATOM   13539 C  CB    . ASN D 2 44  ? 122.200 106.554 134.013 1.00 29.62  ? 23  ASN D CB    1 
ATOM   13540 C  CG    . ASN D 2 44  ? 120.690 106.376 134.115 1.00 32.44  ? 23  ASN D CG    1 
ATOM   13541 O  OD1   . ASN D 2 44  ? 120.116 105.458 133.514 1.00 34.30  ? 23  ASN D OD1   1 
ATOM   13542 N  ND2   . ASN D 2 44  ? 120.037 107.249 134.879 1.00 35.17  ? 23  ASN D ND2   1 
ATOM   13543 N  N     . GLN D 2 45  ? 125.214 105.816 134.087 1.00 28.97  ? 24  GLN D N     1 
ATOM   13544 C  CA    . GLN D 2 45  ? 126.607 106.106 133.770 1.00 29.99  ? 24  GLN D CA    1 
ATOM   13545 C  C     . GLN D 2 45  ? 127.319 104.912 133.117 1.00 29.69  ? 24  GLN D C     1 
ATOM   13546 O  O     . GLN D 2 45  ? 128.097 105.089 132.181 1.00 30.01  ? 24  GLN D O     1 
ATOM   13547 C  CB    . GLN D 2 45  ? 127.365 106.589 135.013 1.00 30.27  ? 24  GLN D CB    1 
ATOM   13548 C  CG    . GLN D 2 45  ? 128.778 107.136 134.709 1.00 32.29  ? 24  GLN D CG    1 
ATOM   13549 C  CD    . GLN D 2 45  ? 128.766 108.370 133.816 1.00 35.95  ? 24  GLN D CD    1 
ATOM   13550 O  OE1   . GLN D 2 45  ? 127.803 109.142 133.808 1.00 36.72  ? 24  GLN D OE1   1 
ATOM   13551 N  NE2   . GLN D 2 45  ? 129.841 108.562 133.059 1.00 37.05  ? 24  GLN D NE2   1 
ATOM   13552 N  N     . ASN D 2 46  ? 127.031 103.701 133.594 1.00 28.93  ? 25  ASN D N     1 
ATOM   13553 C  CA    . ASN D 2 46  ? 127.603 102.498 133.014 1.00 28.70  ? 25  ASN D CA    1 
ATOM   13554 C  C     . ASN D 2 46  ? 127.196 102.264 131.565 1.00 29.05  ? 25  ASN D C     1 
ATOM   13555 O  O     . ASN D 2 46  ? 128.059 102.066 130.705 1.00 28.51  ? 25  ASN D O     1 
ATOM   13556 C  CB    . ASN D 2 46  ? 127.281 101.262 133.864 1.00 28.36  ? 25  ASN D CB    1 
ATOM   13557 C  CG    . ASN D 2 46  ? 128.299 101.034 134.961 1.00 28.45  ? 25  ASN D CG    1 
ATOM   13558 O  OD1   . ASN D 2 46  ? 129.224 100.244 134.792 1.00 28.03  ? 25  ASN D OD1   1 
ATOM   13559 N  ND2   . ASN D 2 46  ? 128.153 101.746 136.077 1.00 26.53  ? 25  ASN D ND2   1 
ATOM   13560 N  N     . VAL D 2 47  ? 125.892 102.312 131.292 1.00 29.66  ? 26  VAL D N     1 
ATOM   13561 C  CA    . VAL D 2 47  ? 125.397 101.988 129.953 1.00 31.15  ? 26  VAL D CA    1 
ATOM   13562 C  C     . VAL D 2 47  ? 125.753 103.073 128.941 1.00 32.39  ? 26  VAL D C     1 
ATOM   13563 O  O     . VAL D 2 47  ? 125.955 102.782 127.763 1.00 32.80  ? 26  VAL D O     1 
ATOM   13564 C  CB    . VAL D 2 47  ? 123.872 101.636 129.911 1.00 31.08  ? 26  VAL D CB    1 
ATOM   13565 C  CG1   . VAL D 2 47  ? 123.554 100.495 130.869 1.00 31.09  ? 26  VAL D CG1   1 
ATOM   13566 C  CG2   . VAL D 2 47  ? 122.992 102.862 130.194 1.00 30.81  ? 26  VAL D CG2   1 
ATOM   13567 N  N     . LYS D 2 48  ? 125.863 104.316 129.394 1.00 33.28  ? 27  LYS D N     1 
ATOM   13568 C  CA    . LYS D 2 48  ? 126.246 105.372 128.470 1.00 34.87  ? 27  LYS D CA    1 
ATOM   13569 C  C     . LYS D 2 48  ? 127.752 105.376 128.135 1.00 34.91  ? 27  LYS D C     1 
ATOM   13570 O  O     . LYS D 2 48  ? 128.177 106.046 127.198 1.00 34.92  ? 27  LYS D O     1 
ATOM   13571 C  CB    . LYS D 2 48  ? 125.724 106.741 128.930 1.00 35.45  ? 27  LYS D CB    1 
ATOM   13572 C  CG    . LYS D 2 48  ? 126.588 107.496 129.913 1.00 37.41  ? 27  LYS D CG    1 
ATOM   13573 C  CD    . LYS D 2 48  ? 126.148 108.969 129.966 1.00 40.91  ? 27  LYS D CD    1 
ATOM   13574 C  CE    . LYS D 2 48  ? 127.221 109.841 130.622 1.00 42.46  ? 27  LYS D CE    1 
ATOM   13575 N  NZ    . LYS D 2 48  ? 126.905 111.299 130.556 1.00 45.13  ? 27  LYS D NZ    1 
ATOM   13576 N  N     . GLN D 2 49  ? 128.536 104.608 128.896 1.00 34.66  ? 28  GLN D N     1 
ATOM   13577 C  CA    . GLN D 2 49  ? 129.966 104.437 128.652 1.00 34.64  ? 28  GLN D CA    1 
ATOM   13578 C  C     . GLN D 2 49  ? 130.250 103.210 127.787 1.00 34.20  ? 28  GLN D C     1 
ATOM   13579 O  O     . GLN D 2 49  ? 131.411 102.837 127.617 1.00 34.53  ? 28  GLN D O     1 
ATOM   13580 C  CB    . GLN D 2 49  ? 130.737 104.305 129.981 1.00 34.89  ? 28  GLN D CB    1 
ATOM   13581 C  CG    . GLN D 2 49  ? 131.170 105.627 130.611 1.00 36.47  ? 28  GLN D CG    1 
ATOM   13582 C  CD    . GLN D 2 49  ? 131.755 105.470 132.017 1.00 38.37  ? 28  GLN D CD    1 
ATOM   13583 O  OE1   . GLN D 2 49  ? 131.616 106.365 132.852 1.00 40.68  ? 28  GLN D OE1   1 
ATOM   13584 N  NE2   . GLN D 2 49  ? 132.407 104.338 132.284 1.00 38.57  ? 28  GLN D NE2   1 
ATOM   13585 N  N     . PHE D 2 50  ? 129.206 102.579 127.249 1.00 33.42  ? 29  PHE D N     1 
ATOM   13586 C  CA    . PHE D 2 50  ? 129.388 101.349 126.479 1.00 32.57  ? 29  PHE D CA    1 
ATOM   13587 C  C     . PHE D 2 50  ? 130.247 101.617 125.242 1.00 32.60  ? 29  PHE D C     1 
ATOM   13588 O  O     . PHE D 2 50  ? 130.094 102.643 124.574 1.00 32.39  ? 29  PHE D O     1 
ATOM   13589 C  CB    . PHE D 2 50  ? 128.044 100.709 126.093 1.00 32.77  ? 29  PHE D CB    1 
ATOM   13590 C  CG    . PHE D 2 50  ? 128.182 99.411  125.321 1.00 32.24  ? 29  PHE D CG    1 
ATOM   13591 C  CD1   . PHE D 2 50  ? 128.542 98.232  125.967 1.00 31.50  ? 29  PHE D CD1   1 
ATOM   13592 C  CD2   . PHE D 2 50  ? 127.953 99.375  123.951 1.00 33.60  ? 29  PHE D CD2   1 
ATOM   13593 C  CE1   . PHE D 2 50  ? 128.672 97.043  125.266 1.00 33.02  ? 29  PHE D CE1   1 
ATOM   13594 C  CE2   . PHE D 2 50  ? 128.084 98.185  123.231 1.00 33.78  ? 29  PHE D CE2   1 
ATOM   13595 C  CZ    . PHE D 2 50  ? 128.436 97.017  123.890 1.00 33.13  ? 29  PHE D CZ    1 
ATOM   13596 N  N     . TRP D 2 51  ? 131.153 100.690 124.958 1.00 31.95  ? 30  TRP D N     1 
ATOM   13597 C  CA    . TRP D 2 51  ? 132.060 100.800 123.816 1.00 32.03  ? 30  TRP D CA    1 
ATOM   13598 C  C     . TRP D 2 51  ? 132.482 99.405  123.372 1.00 33.03  ? 30  TRP D C     1 
ATOM   13599 O  O     . TRP D 2 51  ? 132.246 98.422  124.077 1.00 32.54  ? 30  TRP D O     1 
ATOM   13600 C  CB    . TRP D 2 51  ? 133.282 101.668 124.155 1.00 31.19  ? 30  TRP D CB    1 
ATOM   13601 C  CG    . TRP D 2 51  ? 134.131 101.124 125.287 1.00 28.11  ? 30  TRP D CG    1 
ATOM   13602 C  CD1   . TRP D 2 51  ? 133.873 101.222 126.619 1.00 26.51  ? 30  TRP D CD1   1 
ATOM   13603 C  CD2   . TRP D 2 51  ? 135.364 100.397 125.169 1.00 25.93  ? 30  TRP D CD2   1 
ATOM   13604 N  NE1   . TRP D 2 51  ? 134.871 100.606 127.345 1.00 24.52  ? 30  TRP D NE1   1 
ATOM   13605 C  CE2   . TRP D 2 51  ? 135.796 100.089 126.480 1.00 24.42  ? 30  TRP D CE2   1 
ATOM   13606 C  CE3   . TRP D 2 51  ? 136.150 99.980  124.084 1.00 25.37  ? 30  TRP D CE3   1 
ATOM   13607 C  CZ2   . TRP D 2 51  ? 136.982 99.388  126.738 1.00 24.00  ? 30  TRP D CZ2   1 
ATOM   13608 C  CZ3   . TRP D 2 51  ? 137.326 99.275  124.341 1.00 24.99  ? 30  TRP D CZ3   1 
ATOM   13609 C  CH2   . TRP D 2 51  ? 137.728 98.986  125.657 1.00 23.72  ? 30  TRP D CH2   1 
ATOM   13610 N  N     . LEU D 2 52  ? 133.089 99.332  122.192 1.00 34.81  ? 31  LEU D N     1 
ATOM   13611 C  CA    . LEU D 2 52  ? 133.537 98.076  121.610 1.00 36.58  ? 31  LEU D CA    1 
ATOM   13612 C  C     . LEU D 2 52  ? 134.965 98.219  121.092 1.00 37.80  ? 31  LEU D C     1 
ATOM   13613 O  O     . LEU D 2 52  ? 135.346 99.294  120.637 1.00 37.92  ? 31  LEU D O     1 
ATOM   13614 C  CB    . LEU D 2 52  ? 132.591 97.640  120.478 1.00 36.95  ? 31  LEU D CB    1 
ATOM   13615 C  CG    . LEU D 2 52  ? 131.277 96.938  120.837 1.00 38.15  ? 31  LEU D CG    1 
ATOM   13616 C  CD1   . LEU D 2 52  ? 130.674 96.289  119.597 1.00 39.50  ? 31  LEU D CD1   1 
ATOM   13617 C  CD2   . LEU D 2 52  ? 131.469 95.884  121.922 1.00 37.94  ? 31  LEU D CD2   1 
ATOM   13618 N  N     . PRO D 2 53  ? 135.761 97.133  121.151 1.00 39.26  ? 32  PRO D N     1 
ATOM   13619 C  CA    . PRO D 2 53  ? 137.165 97.155  120.698 1.00 40.41  ? 32  PRO D CA    1 
ATOM   13620 C  C     . PRO D 2 53  ? 137.340 97.651  119.256 1.00 41.91  ? 32  PRO D C     1 
ATOM   13621 O  O     . PRO D 2 53  ? 138.227 98.468  118.985 1.00 42.52  ? 32  PRO D O     1 
ATOM   13622 C  CB    . PRO D 2 53  ? 137.585 95.684  120.790 1.00 40.42  ? 32  PRO D CB    1 
ATOM   13623 C  CG    . PRO D 2 53  ? 136.637 95.067  121.737 1.00 40.01  ? 32  PRO D CG    1 
ATOM   13624 C  CD    . PRO D 2 53  ? 135.345 95.789  121.588 1.00 39.30  ? 32  PRO D CD    1 
ATOM   13625 N  N     . GLU D 2 54  ? 136.486 97.172  118.356 1.00 43.27  ? 33  GLU D N     1 
ATOM   13626 C  CA    . GLU D 2 54  ? 136.531 97.505  116.923 1.00 45.17  ? 33  GLU D CA    1 
ATOM   13627 C  C     . GLU D 2 54  ? 136.535 99.007  116.596 1.00 45.57  ? 33  GLU D C     1 
ATOM   13628 O  O     . GLU D 2 54  ? 136.959 99.407  115.507 1.00 46.08  ? 33  GLU D O     1 
ATOM   13629 C  CB    . GLU D 2 54  ? 135.363 96.825  116.192 1.00 45.55  ? 33  GLU D CB    1 
ATOM   13630 C  CG    . GLU D 2 54  ? 135.595 95.355  115.835 1.00 48.19  ? 33  GLU D CG    1 
ATOM   13631 C  CD    . GLU D 2 54  ? 135.763 94.450  117.047 1.00 50.61  ? 33  GLU D CD    1 
ATOM   13632 O  OE1   . GLU D 2 54  ? 134.940 94.541  117.988 1.00 51.10  ? 33  GLU D OE1   1 
ATOM   13633 O  OE2   . GLU D 2 54  ? 136.726 93.646  117.054 1.00 52.64  ? 33  GLU D OE2   1 
ATOM   13634 N  N     . GLU D 2 55  ? 136.065 99.827  117.536 1.00 45.74  ? 34  GLU D N     1 
ATOM   13635 C  CA    . GLU D 2 55  ? 135.955 101.277 117.334 1.00 46.28  ? 34  GLU D CA    1 
ATOM   13636 C  C     . GLU D 2 55  ? 137.313 101.975 117.190 1.00 46.49  ? 34  GLU D C     1 
ATOM   13637 O  O     . GLU D 2 55  ? 137.424 102.994 116.503 1.00 46.73  ? 34  GLU D O     1 
ATOM   13638 C  CB    . GLU D 2 55  ? 135.146 101.925 118.462 1.00 46.17  ? 34  GLU D CB    1 
ATOM   13639 C  CG    . GLU D 2 55  ? 133.686 101.471 118.553 1.00 47.10  ? 34  GLU D CG    1 
ATOM   13640 C  CD    . GLU D 2 55  ? 132.920 102.195 119.658 1.00 48.43  ? 34  GLU D CD    1 
ATOM   13641 O  OE1   . GLU D 2 55  ? 132.766 103.433 119.570 1.00 49.62  ? 34  GLU D OE1   1 
ATOM   13642 O  OE2   . GLU D 2 55  ? 132.470 101.528 120.613 1.00 47.11  ? 34  GLU D OE2   1 
ATOM   13643 N  N     . ILE D 2 56  ? 138.337 101.427 117.844 1.00 46.23  ? 35  ILE D N     1 
ATOM   13644 C  CA    . ILE D 2 56  ? 139.689 101.973 117.763 1.00 46.25  ? 35  ILE D CA    1 
ATOM   13645 C  C     . ILE D 2 56  ? 140.531 101.111 116.823 1.00 46.30  ? 35  ILE D C     1 
ATOM   13646 O  O     . ILE D 2 56  ? 140.706 99.912  117.060 1.00 46.36  ? 35  ILE D O     1 
ATOM   13647 C  CB    . ILE D 2 56  ? 140.380 102.046 119.169 1.00 45.84  ? 35  ILE D CB    1 
ATOM   13648 C  CG1   . ILE D 2 56  ? 139.420 102.547 120.268 1.00 46.15  ? 35  ILE D CG1   1 
ATOM   13649 C  CG2   . ILE D 2 56  ? 141.687 102.864 119.109 1.00 45.72  ? 35  ILE D CG2   1 
ATOM   13650 C  CD1   . ILE D 2 56  ? 138.891 103.966 120.096 1.00 47.27  ? 35  ILE D CD1   1 
ATOM   13651 N  N     . ALA D 2 57  ? 141.039 101.716 115.754 1.00 46.51  ? 36  ALA D N     1 
ATOM   13652 C  CA    . ALA D 2 57  ? 141.966 101.033 114.848 1.00 46.56  ? 36  ALA D CA    1 
ATOM   13653 C  C     . ALA D 2 57  ? 143.352 100.972 115.496 1.00 46.08  ? 36  ALA D C     1 
ATOM   13654 O  O     . ALA D 2 57  ? 143.891 102.003 115.897 1.00 45.70  ? 36  ALA D O     1 
ATOM   13655 C  CB    . ALA D 2 57  ? 142.030 101.749 113.501 1.00 47.10  ? 36  ALA D CB    1 
ATOM   13656 N  N     . LEU D 2 58  ? 143.923 99.772  115.585 1.00 45.66  ? 37  LEU D N     1 
ATOM   13657 C  CA    . LEU D 2 58  ? 145.178 99.573  116.325 1.00 45.27  ? 37  LEU D CA    1 
ATOM   13658 C  C     . LEU D 2 58  ? 146.467 99.607  115.507 1.00 45.25  ? 37  LEU D C     1 
ATOM   13659 O  O     . LEU D 2 58  ? 147.548 99.840  116.060 1.00 44.82  ? 37  LEU D O     1 
ATOM   13660 C  CB    . LEU D 2 58  ? 145.122 98.275  117.131 1.00 45.05  ? 37  LEU D CB    1 
ATOM   13661 C  CG    . LEU D 2 58  ? 144.325 98.364  118.430 1.00 45.41  ? 37  LEU D CG    1 
ATOM   13662 C  CD1   . LEU D 2 58  ? 144.283 97.005  119.103 1.00 45.40  ? 37  LEU D CD1   1 
ATOM   13663 C  CD2   . LEU D 2 58  ? 144.922 99.415  119.365 1.00 44.70  ? 37  LEU D CD2   1 
ATOM   13664 N  N     . ASN D 2 59  ? 146.358 99.391  114.199 1.00 45.33  ? 38  ASN D N     1 
ATOM   13665 C  CA    . ASN D 2 59  ? 147.542 99.170  113.362 1.00 45.22  ? 38  ASN D CA    1 
ATOM   13666 C  C     . ASN D 2 59  ? 148.575 100.306 113.358 1.00 44.39  ? 38  ASN D C     1 
ATOM   13667 O  O     . ASN D 2 59  ? 149.779 100.047 113.248 1.00 44.33  ? 38  ASN D O     1 
ATOM   13668 C  CB    . ASN D 2 59  ? 147.127 98.808  111.939 1.00 46.22  ? 38  ASN D CB    1 
ATOM   13669 C  CG    . ASN D 2 59  ? 148.065 97.798  111.300 1.00 47.90  ? 38  ASN D CG    1 
ATOM   13670 O  OD1   . ASN D 2 59  ? 148.711 98.084  110.293 1.00 49.28  ? 38  ASN D OD1   1 
ATOM   13671 N  ND2   . ASN D 2 59  ? 148.143 96.603  111.888 1.00 49.18  ? 38  ASN D ND2   1 
ATOM   13672 N  N     . GLY D 2 60  ? 148.105 101.546 113.500 1.00 43.45  ? 39  GLY D N     1 
ATOM   13673 C  CA    . GLY D 2 60  ? 148.976 102.726 113.530 1.00 42.42  ? 39  GLY D CA    1 
ATOM   13674 C  C     . GLY D 2 60  ? 149.921 102.832 114.725 1.00 41.55  ? 39  GLY D C     1 
ATOM   13675 O  O     . GLY D 2 60  ? 150.787 103.712 114.764 1.00 41.29  ? 39  GLY D O     1 
ATOM   13676 N  N     . ASP D 2 61  ? 149.755 101.946 115.705 1.00 40.35  ? 40  ASP D N     1 
ATOM   13677 C  CA    . ASP D 2 61  ? 150.678 101.878 116.844 1.00 39.53  ? 40  ASP D CA    1 
ATOM   13678 C  C     . ASP D 2 61  ? 152.045 101.319 116.474 1.00 39.38  ? 40  ASP D C     1 
ATOM   13679 O  O     . ASP D 2 61  ? 153.035 101.586 117.151 1.00 38.90  ? 40  ASP D O     1 
ATOM   13680 C  CB    . ASP D 2 61  ? 150.083 101.039 117.964 1.00 38.93  ? 40  ASP D CB    1 
ATOM   13681 C  CG    . ASP D 2 61  ? 149.184 101.834 118.867 1.00 38.21  ? 40  ASP D CG    1 
ATOM   13682 O  OD1   . ASP D 2 61  ? 149.026 103.056 118.651 1.00 38.79  ? 40  ASP D OD1   1 
ATOM   13683 O  OD2   . ASP D 2 61  ? 148.640 101.233 119.807 1.00 38.02  ? 40  ASP D OD2   1 
ATOM   13684 N  N     . LEU D 2 62  ? 152.088 100.541 115.397 1.00 39.82  ? 41  LEU D N     1 
ATOM   13685 C  CA    . LEU D 2 62  ? 153.325 99.924  114.933 1.00 40.22  ? 41  LEU D CA    1 
ATOM   13686 C  C     . LEU D 2 62  ? 154.356 100.969 114.509 1.00 40.40  ? 41  LEU D C     1 
ATOM   13687 O  O     . LEU D 2 62  ? 155.553 100.682 114.467 1.00 40.91  ? 41  LEU D O     1 
ATOM   13688 C  CB    . LEU D 2 62  ? 153.030 98.942  113.796 1.00 40.52  ? 41  LEU D CB    1 
ATOM   13689 C  CG    . LEU D 2 62  ? 152.195 97.711  114.168 1.00 41.03  ? 41  LEU D CG    1 
ATOM   13690 C  CD1   . LEU D 2 62  ? 151.893 96.874  112.932 1.00 42.53  ? 41  LEU D CD1   1 
ATOM   13691 C  CD2   . LEU D 2 62  ? 152.884 96.867  115.248 1.00 41.89  ? 41  LEU D CD2   1 
ATOM   13692 N  N     . LEU D 2 63  ? 153.876 102.183 114.222 1.00 40.20  ? 42  LEU D N     1 
ATOM   13693 C  CA    . LEU D 2 63  ? 154.712 103.314 113.821 1.00 39.85  ? 42  LEU D CA    1 
ATOM   13694 C  C     . LEU D 2 63  ? 155.473 103.959 114.995 1.00 38.90  ? 42  LEU D C     1 
ATOM   13695 O  O     . LEU D 2 63  ? 156.420 104.725 114.785 1.00 39.48  ? 42  LEU D O     1 
ATOM   13696 C  CB    . LEU D 2 63  ? 153.846 104.356 113.095 1.00 40.50  ? 42  LEU D CB    1 
ATOM   13697 C  CG    . LEU D 2 63  ? 154.395 105.224 111.952 1.00 41.98  ? 42  LEU D CG    1 
ATOM   13698 C  CD1   . LEU D 2 63  ? 154.988 104.393 110.820 1.00 43.07  ? 42  LEU D CD1   1 
ATOM   13699 C  CD2   . LEU D 2 63  ? 153.283 106.100 111.402 1.00 43.17  ? 42  LEU D CD2   1 
ATOM   13700 N  N     . THR D 2 64  ? 155.062 103.668 116.227 1.00 37.28  ? 43  THR D N     1 
ATOM   13701 C  CA    . THR D 2 64  ? 155.836 104.111 117.398 1.00 35.53  ? 43  THR D CA    1 
ATOM   13702 C  C     . THR D 2 64  ? 156.440 102.938 118.160 1.00 34.57  ? 43  THR D C     1 
ATOM   13703 O  O     . THR D 2 64  ? 157.493 103.077 118.789 1.00 34.23  ? 43  THR D O     1 
ATOM   13704 C  CB    . THR D 2 64  ? 155.037 105.019 118.358 1.00 35.18  ? 43  THR D CB    1 
ATOM   13705 O  OG1   . THR D 2 64  ? 153.761 104.440 118.647 1.00 34.59  ? 43  THR D OG1   1 
ATOM   13706 C  CG2   . THR D 2 64  ? 154.840 106.381 117.752 1.00 35.48  ? 43  THR D CG2   1 
ATOM   13707 N  N     . TRP D 2 65  ? 155.771 101.788 118.088 1.00 33.62  ? 44  TRP D N     1 
ATOM   13708 C  CA    . TRP D 2 65  ? 156.230 100.549 118.736 1.00 32.87  ? 44  TRP D CA    1 
ATOM   13709 C  C     . TRP D 2 65  ? 157.634 100.145 118.266 1.00 33.46  ? 44  TRP D C     1 
ATOM   13710 O  O     . TRP D 2 65  ? 158.484 99.773  119.076 1.00 32.58  ? 44  TRP D O     1 
ATOM   13711 C  CB    . TRP D 2 65  ? 155.227 99.417  118.466 1.00 32.09  ? 44  TRP D CB    1 
ATOM   13712 C  CG    . TRP D 2 65  ? 155.618 98.076  119.022 1.00 30.42  ? 44  TRP D CG    1 
ATOM   13713 C  CD1   . TRP D 2 65  ? 156.071 96.998  118.313 1.00 29.35  ? 44  TRP D CD1   1 
ATOM   13714 C  CD2   . TRP D 2 65  ? 155.585 97.666  120.398 1.00 28.04  ? 44  TRP D CD2   1 
ATOM   13715 N  NE1   . TRP D 2 65  ? 156.322 95.944  119.160 1.00 28.44  ? 44  TRP D NE1   1 
ATOM   13716 C  CE2   . TRP D 2 65  ? 156.036 96.328  120.445 1.00 28.14  ? 44  TRP D CE2   1 
ATOM   13717 C  CE3   . TRP D 2 65  ? 155.227 98.301  121.596 1.00 27.11  ? 44  TRP D CE3   1 
ATOM   13718 C  CZ2   . TRP D 2 65  ? 156.131 95.605  121.642 1.00 27.21  ? 44  TRP D CZ2   1 
ATOM   13719 C  CZ3   . TRP D 2 65  ? 155.315 97.578  122.789 1.00 27.45  ? 44  TRP D CZ3   1 
ATOM   13720 C  CH2   . TRP D 2 65  ? 155.759 96.241  122.797 1.00 27.25  ? 44  TRP D CH2   1 
ATOM   13721 N  N     . LYS D 2 66  ? 157.855 100.233 116.955 1.00 34.52  ? 45  LYS D N     1 
ATOM   13722 C  CA    . LYS D 2 66  ? 159.139 99.909  116.339 1.00 36.41  ? 45  LYS D CA    1 
ATOM   13723 C  C     . LYS D 2 66  ? 160.300 100.769 116.835 1.00 36.26  ? 45  LYS D C     1 
ATOM   13724 O  O     . LYS D 2 66  ? 161.457 100.367 116.714 1.00 36.52  ? 45  LYS D O     1 
ATOM   13725 C  CB    . LYS D 2 66  ? 159.040 99.994  114.811 1.00 36.98  ? 45  LYS D CB    1 
ATOM   13726 C  CG    . LYS D 2 66  ? 158.920 98.638  114.120 1.00 40.03  ? 45  LYS D CG    1 
ATOM   13727 C  CD    . LYS D 2 66  ? 157.562 97.969  114.367 1.00 43.70  ? 45  LYS D CD    1 
ATOM   13728 C  CE    . LYS D 2 66  ? 157.450 96.639  113.616 1.00 45.57  ? 45  LYS D CE    1 
ATOM   13729 N  NZ    . LYS D 2 66  ? 157.545 96.799  112.135 1.00 46.59  ? 45  LYS D NZ    1 
ATOM   13730 N  N     . TYR D 2 67  ? 159.989 101.932 117.401 1.00 36.26  ? 46  TYR D N     1 
ATOM   13731 C  CA    . TYR D 2 67  ? 161.033 102.840 117.887 1.00 36.90  ? 46  TYR D CA    1 
ATOM   13732 C  C     . TYR D 2 67  ? 161.359 102.714 119.377 1.00 36.28  ? 46  TYR D C     1 
ATOM   13733 O  O     . TYR D 2 67  ? 162.236 103.416 119.871 1.00 36.44  ? 46  TYR D O     1 
ATOM   13734 C  CB    . TYR D 2 67  ? 160.717 104.296 117.524 1.00 37.15  ? 46  TYR D CB    1 
ATOM   13735 C  CG    . TYR D 2 67  ? 160.533 104.523 116.042 1.00 39.40  ? 46  TYR D CG    1 
ATOM   13736 C  CD1   . TYR D 2 67  ? 161.401 103.941 115.113 1.00 41.26  ? 46  TYR D CD1   1 
ATOM   13737 C  CD2   . TYR D 2 67  ? 159.512 105.339 115.567 1.00 41.06  ? 46  TYR D CD2   1 
ATOM   13738 C  CE1   . TYR D 2 67  ? 161.235 104.145 113.744 1.00 43.03  ? 46  TYR D CE1   1 
ATOM   13739 C  CE2   . TYR D 2 67  ? 159.341 105.557 114.198 1.00 43.05  ? 46  TYR D CE2   1 
ATOM   13740 C  CZ    . TYR D 2 67  ? 160.204 104.960 113.293 1.00 43.80  ? 46  TYR D CZ    1 
ATOM   13741 O  OH    . TYR D 2 67  ? 160.029 105.174 111.938 1.00 45.18  ? 46  TYR D OH    1 
ATOM   13742 N  N     . LEU D 2 68  ? 160.656 101.838 120.092 1.00 35.71  ? 47  LEU D N     1 
ATOM   13743 C  CA    . LEU D 2 68  ? 160.963 101.606 121.505 1.00 34.92  ? 47  LEU D CA    1 
ATOM   13744 C  C     . LEU D 2 68  ? 162.129 100.625 121.654 1.00 34.32  ? 47  LEU D C     1 
ATOM   13745 O  O     . LEU D 2 68  ? 162.301 99.721  120.831 1.00 34.50  ? 47  LEU D O     1 
ATOM   13746 C  CB    . LEU D 2 68  ? 159.733 101.095 122.270 1.00 35.00  ? 47  LEU D CB    1 
ATOM   13747 C  CG    . LEU D 2 68  ? 158.405 101.867 122.178 1.00 35.82  ? 47  LEU D CG    1 
ATOM   13748 C  CD1   . LEU D 2 68  ? 157.342 101.175 123.018 1.00 35.95  ? 47  LEU D CD1   1 
ATOM   13749 C  CD2   . LEU D 2 68  ? 158.539 103.333 122.588 1.00 35.97  ? 47  LEU D CD2   1 
ATOM   13750 N  N     . GLY D 2 69  ? 162.923 100.811 122.706 1.00 33.50  ? 48  GLY D N     1 
ATOM   13751 C  CA    . GLY D 2 69  ? 163.972 99.862  123.074 1.00 32.41  ? 48  GLY D CA    1 
ATOM   13752 C  C     . GLY D 2 69  ? 163.414 98.526  123.545 1.00 32.15  ? 48  GLY D C     1 
ATOM   13753 O  O     . GLY D 2 69  ? 162.214 98.400  123.823 1.00 30.98  ? 48  GLY D O     1 
ATOM   13754 N  N     . LYS D 2 70  ? 164.292 97.532  123.645 1.00 32.14  ? 49  LYS D N     1 
ATOM   13755 C  CA    . LYS D 2 70  ? 163.907 96.197  124.094 1.00 32.25  ? 49  LYS D CA    1 
ATOM   13756 C  C     . LYS D 2 70  ? 163.317 96.200  125.503 1.00 31.24  ? 49  LYS D C     1 
ATOM   13757 O  O     . LYS D 2 70  ? 162.320 95.523  125.740 1.00 31.34  ? 49  LYS D O     1 
ATOM   13758 C  CB    . LYS D 2 70  ? 165.091 95.230  124.019 1.00 33.07  ? 49  LYS D CB    1 
ATOM   13759 C  CG    . LYS D 2 70  ? 165.628 95.021  122.611 1.00 35.74  ? 49  LYS D CG    1 
ATOM   13760 C  CD    . LYS D 2 70  ? 166.965 94.288  122.659 1.00 39.67  ? 49  LYS D CD    1 
ATOM   13761 C  CE    . LYS D 2 70  ? 167.680 94.349  121.318 1.00 40.96  ? 49  LYS D CE    1 
ATOM   13762 N  NZ    . LYS D 2 70  ? 169.086 93.902  121.471 1.00 42.55  ? 49  LYS D NZ    1 
ATOM   13763 N  N     . ASN D 2 71  ? 163.920 96.963  126.420 1.00 29.92  ? 50  ASN D N     1 
ATOM   13764 C  CA    . ASN D 2 71  ? 163.421 97.053  127.798 1.00 29.37  ? 50  ASN D CA    1 
ATOM   13765 C  C     . ASN D 2 71  ? 162.028 97.672  127.859 1.00 28.35  ? 50  ASN D C     1 
ATOM   13766 O  O     . ASN D 2 71  ? 161.181 97.213  128.634 1.00 27.64  ? 50  ASN D O     1 
ATOM   13767 C  CB    . ASN D 2 71  ? 164.380 97.825  128.724 1.00 29.38  ? 50  ASN D CB    1 
ATOM   13768 C  CG    . ASN D 2 71  ? 165.608 97.011  129.126 1.00 31.22  ? 50  ASN D CG    1 
ATOM   13769 O  OD1   . ASN D 2 71  ? 165.559 95.783  129.234 1.00 33.03  ? 50  ASN D OD1   1 
ATOM   13770 N  ND2   . ASN D 2 71  ? 166.718 97.702  129.364 1.00 31.97  ? 50  ASN D ND2   1 
ATOM   13771 N  N     . GLU D 2 72  ? 161.797 98.698  127.036 1.00 27.72  ? 51  GLU D N     1 
ATOM   13772 C  CA    . GLU D 2 72  ? 160.478 99.344  126.961 1.00 27.70  ? 51  GLU D CA    1 
ATOM   13773 C  C     . GLU D 2 72  ? 159.412 98.385  126.423 1.00 27.62  ? 51  GLU D C     1 
ATOM   13774 O  O     . GLU D 2 72  ? 158.292 98.330  126.941 1.00 27.56  ? 51  GLU D O     1 
ATOM   13775 C  CB    . GLU D 2 72  ? 160.520 100.604 126.090 1.00 27.55  ? 51  GLU D CB    1 
ATOM   13776 C  CG    . GLU D 2 72  ? 161.491 101.691 126.568 1.00 28.77  ? 51  GLU D CG    1 
ATOM   13777 C  CD    . GLU D 2 72  ? 161.381 102.949 125.726 1.00 31.18  ? 51  GLU D CD    1 
ATOM   13778 O  OE1   . GLU D 2 72  ? 161.828 102.930 124.560 1.00 33.17  ? 51  GLU D OE1   1 
ATOM   13779 O  OE2   . GLU D 2 72  ? 160.837 103.953 126.228 1.00 31.66  ? 51  GLU D OE2   1 
ATOM   13780 N  N     . GLN D 2 73  ? 159.770 97.635  125.385 1.00 27.32  ? 52  GLN D N     1 
ATOM   13781 C  CA    . GLN D 2 73  ? 158.855 96.673  124.777 1.00 27.33  ? 52  GLN D CA    1 
ATOM   13782 C  C     . GLN D 2 73  ? 158.569 95.527  125.751 1.00 26.85  ? 52  GLN D C     1 
ATOM   13783 O  O     . GLN D 2 73  ? 157.421 95.093  125.887 1.00 26.24  ? 52  GLN D O     1 
ATOM   13784 C  CB    . GLN D 2 73  ? 159.418 96.146  123.463 1.00 27.65  ? 52  GLN D CB    1 
ATOM   13785 C  CG    . GLN D 2 73  ? 159.376 97.150  122.294 1.00 29.66  ? 52  GLN D CG    1 
ATOM   13786 C  CD    . GLN D 2 73  ? 159.768 96.525  120.955 1.00 32.60  ? 52  GLN D CD    1 
ATOM   13787 O  OE1   . GLN D 2 73  ? 160.420 95.485  120.908 1.00 34.76  ? 52  GLN D OE1   1 
ATOM   13788 N  NE2   . GLN D 2 73  ? 159.383 97.171  119.865 1.00 33.42  ? 52  GLN D NE2   1 
ATOM   13789 N  N     . ASP D 2 74  ? 159.613 95.079  126.446 1.00 26.26  ? 53  ASP D N     1 
ATOM   13790 C  CA    . ASP D 2 74  ? 159.517 94.019  127.455 1.00 26.50  ? 53  ASP D CA    1 
ATOM   13791 C  C     . ASP D 2 74  ? 158.620 94.435  128.613 1.00 25.81  ? 53  ASP D C     1 
ATOM   13792 O  O     . ASP D 2 74  ? 157.738 93.681  129.015 1.00 26.12  ? 53  ASP D O     1 
ATOM   13793 C  CB    . ASP D 2 74  ? 160.917 93.673  127.981 1.00 26.84  ? 53  ASP D CB    1 
ATOM   13794 C  CG    . ASP D 2 74  ? 160.930 92.474  128.928 1.00 29.50  ? 53  ASP D CG    1 
ATOM   13795 O  OD1   . ASP D 2 74  ? 160.597 91.348  128.499 1.00 32.08  ? 53  ASP D OD1   1 
ATOM   13796 O  OD2   . ASP D 2 74  ? 161.322 92.651  130.099 1.00 33.52  ? 53  ASP D OD2   1 
ATOM   13797 N  N     . THR D 2 75  ? 158.842 95.635  129.148 1.00 25.10  ? 54  THR D N     1 
ATOM   13798 C  CA    . THR D 2 75  ? 158.024 96.126  130.261 1.00 24.11  ? 54  THR D CA    1 
ATOM   13799 C  C     . THR D 2 75  ? 156.557 96.242  129.837 1.00 23.82  ? 54  THR D C     1 
ATOM   13800 O  O     . THR D 2 75  ? 155.664 95.774  130.543 1.00 23.81  ? 54  THR D O     1 
ATOM   13801 C  CB    . THR D 2 75  ? 158.553 97.462  130.816 1.00 23.80  ? 54  THR D CB    1 
ATOM   13802 O  OG1   . THR D 2 75  ? 159.869 97.257  131.350 1.00 24.62  ? 54  THR D OG1   1 
ATOM   13803 C  CG2   . THR D 2 75  ? 157.636 97.998  131.930 1.00 23.25  ? 54  THR D CG2   1 
ATOM   13804 N  N     . TYR D 2 76  ? 156.321 96.875  128.696 1.00 24.06  ? 55  TYR D N     1 
ATOM   13805 C  CA    . TYR D 2 76  ? 154.972 97.012  128.156 1.00 24.76  ? 55  TYR D CA    1 
ATOM   13806 C  C     . TYR D 2 76  ? 154.245 95.666  128.023 1.00 24.85  ? 55  TYR D C     1 
ATOM   13807 O  O     . TYR D 2 76  ? 153.103 95.530  128.471 1.00 24.83  ? 55  TYR D O     1 
ATOM   13808 C  CB    . TYR D 2 76  ? 154.993 97.729  126.806 1.00 24.78  ? 55  TYR D CB    1 
ATOM   13809 C  CG    . TYR D 2 76  ? 153.656 98.336  126.436 1.00 26.19  ? 55  TYR D CG    1 
ATOM   13810 C  CD1   . TYR D 2 76  ? 152.690 97.602  125.740 1.00 27.81  ? 55  TYR D CD1   1 
ATOM   13811 C  CD2   . TYR D 2 76  ? 153.351 99.649  126.799 1.00 28.03  ? 55  TYR D CD2   1 
ATOM   13812 C  CE1   . TYR D 2 76  ? 151.452 98.172  125.405 1.00 29.32  ? 55  TYR D CE1   1 
ATOM   13813 C  CE2   . TYR D 2 76  ? 152.131 100.224 126.471 1.00 29.01  ? 55  TYR D CE2   1 
ATOM   13814 C  CZ    . TYR D 2 76  ? 151.188 99.485  125.778 1.00 30.76  ? 55  TYR D CZ    1 
ATOM   13815 O  OH    . TYR D 2 76  ? 149.989 100.081 125.463 1.00 34.50  ? 55  TYR D OH    1 
ATOM   13816 N  N     . MET D 2 77  ? 154.906 94.686  127.407 1.00 25.76  ? 56  MET D N     1 
ATOM   13817 C  CA    . MET D 2 77  ? 154.339 93.342  127.257 1.00 26.81  ? 56  MET D CA    1 
ATOM   13818 C  C     . MET D 2 77  ? 153.968 92.726  128.611 1.00 26.23  ? 56  MET D C     1 
ATOM   13819 O  O     . MET D 2 77  ? 152.876 92.181  128.777 1.00 25.00  ? 56  MET D O     1 
ATOM   13820 C  CB    . MET D 2 77  ? 155.308 92.421  126.519 1.00 28.11  ? 56  MET D CB    1 
ATOM   13821 C  CG    . MET D 2 77  ? 155.513 92.744  125.035 1.00 32.52  ? 56  MET D CG    1 
ATOM   13822 S  SD    . MET D 2 77  ? 154.109 92.320  123.990 1.00 42.68  ? 56  MET D SD    1 
ATOM   13823 C  CE    . MET D 2 77  ? 153.077 93.781  124.112 1.00 38.97  ? 56  MET D CE    1 
ATOM   13824 N  N     . LYS D 2 78  ? 154.894 92.817  129.566 1.00 26.01  ? 57  LYS D N     1 
ATOM   13825 C  CA    . LYS D 2 78  ? 154.699 92.231  130.896 1.00 26.07  ? 57  LYS D CA    1 
ATOM   13826 C  C     . LYS D 2 78  ? 153.570 92.909  131.668 1.00 25.69  ? 57  LYS D C     1 
ATOM   13827 O  O     . LYS D 2 78  ? 152.783 92.242  132.350 1.00 25.58  ? 57  LYS D O     1 
ATOM   13828 C  CB    . LYS D 2 78  ? 156.001 92.263  131.708 1.00 26.08  ? 57  LYS D CB    1 
ATOM   13829 C  CG    . LYS D 2 78  ? 157.081 91.305  131.184 1.00 27.64  ? 57  LYS D CG    1 
ATOM   13830 C  CD    . LYS D 2 78  ? 158.404 91.502  131.914 1.00 29.47  ? 57  LYS D CD    1 
ATOM   13831 C  CE    . LYS D 2 78  ? 159.392 90.410  131.534 1.00 31.69  ? 57  LYS D CE    1 
ATOM   13832 N  NZ    . LYS D 2 78  ? 160.691 90.554  132.244 1.00 33.36  ? 57  LYS D NZ    1 
ATOM   13833 N  N     . VAL D 2 79  ? 153.499 94.234  131.559 1.00 25.32  ? 58  VAL D N     1 
ATOM   13834 C  CA    . VAL D 2 79  ? 152.447 95.021  132.212 1.00 25.47  ? 58  VAL D CA    1 
ATOM   13835 C  C     . VAL D 2 79  ? 151.095 94.644  131.615 1.00 25.09  ? 58  VAL D C     1 
ATOM   13836 O  O     . VAL D 2 79  ? 150.129 94.381  132.336 1.00 24.46  ? 58  VAL D O     1 
ATOM   13837 C  CB    . VAL D 2 79  ? 152.724 96.541  132.041 1.00 25.83  ? 58  VAL D CB    1 
ATOM   13838 C  CG1   . VAL D 2 79  ? 151.448 97.350  132.084 1.00 27.35  ? 58  VAL D CG1   1 
ATOM   13839 C  CG2   . VAL D 2 79  ? 153.735 97.011  133.087 1.00 26.42  ? 58  VAL D CG2   1 
ATOM   13840 N  N     . LEU D 2 80  ? 151.060 94.573  130.286 1.00 25.27  ? 59  LEU D N     1 
ATOM   13841 C  CA    . LEU D 2 80  ? 149.844 94.268  129.565 1.00 25.55  ? 59  LEU D CA    1 
ATOM   13842 C  C     . LEU D 2 80  ? 149.316 92.892  129.969 1.00 24.94  ? 59  LEU D C     1 
ATOM   13843 O  O     . LEU D 2 80  ? 148.120 92.735  130.204 1.00 24.82  ? 59  LEU D O     1 
ATOM   13844 C  CB    . LEU D 2 80  ? 150.100 94.318  128.058 1.00 25.80  ? 59  LEU D CB    1 
ATOM   13845 C  CG    . LEU D 2 80  ? 149.302 95.240  127.128 1.00 28.76  ? 59  LEU D CG    1 
ATOM   13846 C  CD1   . LEU D 2 80  ? 149.195 94.564  125.761 1.00 30.25  ? 59  LEU D CD1   1 
ATOM   13847 C  CD2   . LEU D 2 80  ? 147.922 95.614  127.642 1.00 27.79  ? 59  LEU D CD2   1 
ATOM   13848 N  N     . ALA D 2 81  ? 150.214 91.909  130.051 1.00 24.86  ? 60  ALA D N     1 
ATOM   13849 C  CA    . ALA D 2 81  ? 149.842 90.541  130.438 1.00 24.60  ? 60  ALA D CA    1 
ATOM   13850 C  C     . ALA D 2 81  ? 149.341 90.506  131.879 1.00 23.80  ? 60  ALA D C     1 
ATOM   13851 O  O     . ALA D 2 81  ? 148.400 89.788  132.199 1.00 24.07  ? 60  ALA D O     1 
ATOM   13852 C  CB    . ALA D 2 81  ? 151.024 89.590  130.259 1.00 24.48  ? 60  ALA D CB    1 
ATOM   13853 N  N     . GLY D 2 82  ? 149.974 91.292  132.741 1.00 23.54  ? 61  GLY D N     1 
ATOM   13854 C  CA    . GLY D 2 82  ? 149.537 91.433  134.126 1.00 22.53  ? 61  GLY D CA    1 
ATOM   13855 C  C     . GLY D 2 82  ? 148.107 91.925  134.211 1.00 22.23  ? 61  GLY D C     1 
ATOM   13856 O  O     . GLY D 2 82  ? 147.283 91.341  134.914 1.00 21.27  ? 61  GLY D O     1 
ATOM   13857 N  N     . LEU D 2 83  ? 147.807 93.002  133.486 1.00 22.36  ? 62  LEU D N     1 
ATOM   13858 C  CA    . LEU D 2 83  ? 146.446 93.551  133.457 1.00 22.42  ? 62  LEU D CA    1 
ATOM   13859 C  C     . LEU D 2 83  ? 145.453 92.540  132.902 1.00 22.91  ? 62  LEU D C     1 
ATOM   13860 O  O     . LEU D 2 83  ? 144.357 92.370  133.452 1.00 22.99  ? 62  LEU D O     1 
ATOM   13861 C  CB    . LEU D 2 83  ? 146.385 94.841  132.630 1.00 22.19  ? 62  LEU D CB    1 
ATOM   13862 C  CG    . LEU D 2 83  ? 147.163 96.050  133.173 1.00 22.17  ? 62  LEU D CG    1 
ATOM   13863 C  CD1   . LEU D 2 83  ? 147.290 97.121  132.081 1.00 21.55  ? 62  LEU D CD1   1 
ATOM   13864 C  CD2   . LEU D 2 83  ? 146.462 96.604  134.401 1.00 22.42  ? 62  LEU D CD2   1 
ATOM   13865 N  N     . THR D 2 84  ? 145.849 91.856  131.833 1.00 23.39  ? 63  THR D N     1 
ATOM   13866 C  CA    . THR D 2 84  ? 144.978 90.881  131.182 1.00 24.42  ? 63  THR D CA    1 
ATOM   13867 C  C     . THR D 2 84  ? 144.594 89.758  132.148 1.00 24.55  ? 63  THR D C     1 
ATOM   13868 O  O     . THR D 2 84  ? 143.414 89.428  132.297 1.00 23.68  ? 63  THR D O     1 
ATOM   13869 C  CB    . THR D 2 84  ? 145.635 90.276  129.914 1.00 24.70  ? 63  THR D CB    1 
ATOM   13870 O  OG1   . THR D 2 84  ? 145.934 91.326  128.986 1.00 25.57  ? 63  THR D OG1   1 
ATOM   13871 C  CG2   . THR D 2 84  ? 144.688 89.295  129.245 1.00 25.36  ? 63  THR D CG2   1 
ATOM   13872 N  N     . LEU D 2 85  ? 145.607 89.190  132.796 1.00 25.38  ? 64  LEU D N     1 
ATOM   13873 C  CA    . LEU D 2 85  ? 145.410 88.092  133.733 1.00 26.44  ? 64  LEU D CA    1 
ATOM   13874 C  C     . LEU D 2 85  ? 144.525 88.491  134.918 1.00 25.96  ? 64  LEU D C     1 
ATOM   13875 O  O     . LEU D 2 85  ? 143.581 87.760  135.249 1.00 25.83  ? 64  LEU D O     1 
ATOM   13876 C  CB    . LEU D 2 85  ? 146.755 87.487  134.165 1.00 26.65  ? 64  LEU D CB    1 
ATOM   13877 C  CG    . LEU D 2 85  ? 147.377 86.592  133.075 1.00 29.62  ? 64  LEU D CG    1 
ATOM   13878 C  CD1   . LEU D 2 85  ? 148.880 86.459  133.235 1.00 31.57  ? 64  LEU D CD1   1 
ATOM   13879 C  CD2   . LEU D 2 85  ? 146.727 85.196  133.034 1.00 30.96  ? 64  LEU D CD2   1 
ATOM   13880 N  N     . LEU D 2 86  ? 144.785 89.654  135.518 1.00 25.63  ? 65  LEU D N     1 
ATOM   13881 C  CA    . LEU D 2 86  ? 143.937 90.126  136.616 1.00 25.59  ? 65  LEU D CA    1 
ATOM   13882 C  C     . LEU D 2 86  ? 142.498 90.414  136.191 1.00 25.60  ? 65  LEU D C     1 
ATOM   13883 O  O     . LEU D 2 86  ? 141.555 90.143  136.940 1.00 25.47  ? 65  LEU D O     1 
ATOM   13884 C  CB    . LEU D 2 86  ? 144.542 91.349  137.332 1.00 25.76  ? 65  LEU D CB    1 
ATOM   13885 C  CG    . LEU D 2 86  ? 145.813 91.093  138.153 1.00 26.71  ? 65  LEU D CG    1 
ATOM   13886 C  CD1   . LEU D 2 86  ? 146.503 92.396  138.543 1.00 28.01  ? 65  LEU D CD1   1 
ATOM   13887 C  CD2   . LEU D 2 86  ? 145.516 90.276  139.389 1.00 28.01  ? 65  LEU D CD2   1 
ATOM   13888 N  N     . ASP D 2 87  ? 142.324 90.970  134.998 1.00 25.49  ? 66  ASP D N     1 
ATOM   13889 C  CA    . ASP D 2 87  ? 140.995 91.337  134.539 1.00 25.83  ? 66  ASP D CA    1 
ATOM   13890 C  C     . ASP D 2 87  ? 140.132 90.108  134.217 1.00 26.20  ? 66  ASP D C     1 
ATOM   13891 O  O     . ASP D 2 87  ? 138.917 90.140  134.378 1.00 25.99  ? 66  ASP D O     1 
ATOM   13892 C  CB    . ASP D 2 87  ? 141.079 92.276  133.342 1.00 25.50  ? 66  ASP D CB    1 
ATOM   13893 C  CG    . ASP D 2 87  ? 139.934 93.246  133.301 1.00 25.76  ? 66  ASP D CG    1 
ATOM   13894 O  OD1   . ASP D 2 87  ? 139.393 93.568  134.387 1.00 26.91  ? 66  ASP D OD1   1 
ATOM   13895 O  OD2   . ASP D 2 87  ? 139.567 93.692  132.197 1.00 23.11  ? 66  ASP D OD2   1 
ATOM   13896 N  N     . THR D 2 88  ? 140.780 89.028  133.787 1.00 27.12  ? 67  THR D N     1 
ATOM   13897 C  CA    . THR D 2 88  ? 140.112 87.757  133.543 1.00 28.40  ? 67  THR D CA    1 
ATOM   13898 C  C     . THR D 2 88  ? 139.534 87.180  134.825 1.00 28.28  ? 67  THR D C     1 
ATOM   13899 O  O     . THR D 2 88  ? 138.414 86.673  134.826 1.00 28.10  ? 67  THR D O     1 
ATOM   13900 C  CB    . THR D 2 88  ? 141.063 86.736  132.889 1.00 29.04  ? 67  THR D CB    1 
ATOM   13901 O  OG1   . THR D 2 88  ? 141.532 87.270  131.649 1.00 31.00  ? 67  THR D OG1   1 
ATOM   13902 C  CG2   . THR D 2 88  ? 140.335 85.423  132.608 1.00 30.16  ? 67  THR D CG2   1 
ATOM   13903 N  N     . GLU D 2 89  ? 140.290 87.258  135.919 1.00 28.28  ? 68  GLU D N     1 
ATOM   13904 C  CA    . GLU D 2 89  ? 139.772 86.824  137.211 1.00 29.16  ? 68  GLU D CA    1 
ATOM   13905 C  C     . GLU D 2 89  ? 138.529 87.635  137.573 1.00 28.65  ? 68  GLU D C     1 
ATOM   13906 O  O     . GLU D 2 89  ? 137.553 87.084  138.063 1.00 28.44  ? 68  GLU D O     1 
ATOM   13907 C  CB    . GLU D 2 89  ? 140.826 86.950  138.320 1.00 29.32  ? 68  GLU D CB    1 
ATOM   13908 C  CG    . GLU D 2 89  ? 142.095 86.115  138.095 1.00 31.95  ? 68  GLU D CG    1 
ATOM   13909 C  CD    . GLU D 2 89  ? 141.853 84.609  138.089 1.00 35.19  ? 68  GLU D CD    1 
ATOM   13910 O  OE1   . GLU D 2 89  ? 140.788 84.143  138.554 1.00 35.47  ? 68  GLU D OE1   1 
ATOM   13911 O  OE2   . GLU D 2 89  ? 142.746 83.882  137.607 1.00 38.06  ? 68  GLU D OE2   1 
ATOM   13912 N  N     . GLN D 2 90  ? 138.567 88.938  137.313 1.00 28.45  ? 69  GLN D N     1 
ATOM   13913 C  CA    . GLN D 2 90  ? 137.438 89.808  137.644 1.00 28.47  ? 69  GLN D CA    1 
ATOM   13914 C  C     . GLN D 2 90  ? 136.193 89.473  136.810 1.00 28.97  ? 69  GLN D C     1 
ATOM   13915 O  O     . GLN D 2 90  ? 135.076 89.494  137.327 1.00 28.84  ? 69  GLN D O     1 
ATOM   13916 C  CB    . GLN D 2 90  ? 137.828 91.283  137.508 1.00 28.21  ? 69  GLN D CB    1 
ATOM   13917 C  CG    . GLN D 2 90  ? 136.888 92.257  138.217 1.00 27.75  ? 69  GLN D CG    1 
ATOM   13918 C  CD    . GLN D 2 90  ? 136.988 92.222  139.738 1.00 28.91  ? 69  GLN D CD    1 
ATOM   13919 O  OE1   . GLN D 2 90  ? 137.444 91.236  140.335 1.00 27.62  ? 69  GLN D OE1   1 
ATOM   13920 N  NE2   . GLN D 2 90  ? 136.536 93.301  140.377 1.00 28.23  ? 69  GLN D NE2   1 
ATOM   13921 N  N     . GLY D 2 91  ? 136.394 89.140  135.535 1.00 29.62  ? 70  GLY D N     1 
ATOM   13922 C  CA    . GLY D 2 91  ? 135.294 88.745  134.652 1.00 30.43  ? 70  GLY D CA    1 
ATOM   13923 C  C     . GLY D 2 91  ? 134.709 87.365  134.931 1.00 31.11  ? 70  GLY D C     1 
ATOM   13924 O  O     . GLY D 2 91  ? 133.491 87.168  134.877 1.00 30.77  ? 70  GLY D O     1 
ATOM   13925 N  N     . ASN D 2 92  ? 135.572 86.402  135.219 1.00 31.69  ? 71  ASN D N     1 
ATOM   13926 C  CA    . ASN D 2 92  ? 135.105 85.043  135.467 1.00 32.72  ? 71  ASN D CA    1 
ATOM   13927 C  C     . ASN D 2 92  ? 134.599 84.779  136.878 1.00 32.60  ? 71  ASN D C     1 
ATOM   13928 O  O     . ASN D 2 92  ? 133.723 83.931  137.064 1.00 33.12  ? 71  ASN D O     1 
ATOM   13929 C  CB    . ASN D 2 92  ? 136.179 84.031  135.091 1.00 33.68  ? 71  ASN D CB    1 
ATOM   13930 C  CG    . ASN D 2 92  ? 136.363 83.919  133.592 1.00 35.15  ? 71  ASN D CG    1 
ATOM   13931 O  OD1   . ASN D 2 92  ? 137.440 83.566  133.126 1.00 40.21  ? 71  ASN D OD1   1 
ATOM   13932 N  ND2   . ASN D 2 92  ? 135.314 84.230  132.828 1.00 36.91  ? 71  ASN D ND2   1 
ATOM   13933 N  N     . THR D 2 93  ? 135.132 85.515  137.854 1.00 31.76  ? 72  THR D N     1 
ATOM   13934 C  CA    . THR D 2 93  ? 134.823 85.263  139.257 1.00 31.47  ? 72  THR D CA    1 
ATOM   13935 C  C     . THR D 2 93  ? 134.363 86.502  140.022 1.00 30.62  ? 72  THR D C     1 
ATOM   13936 O  O     . THR D 2 93  ? 133.261 86.514  140.565 1.00 30.71  ? 72  THR D O     1 
ATOM   13937 C  CB    . THR D 2 93  ? 136.019 84.637  139.970 1.00 31.60  ? 72  THR D CB    1 
ATOM   13938 O  OG1   . THR D 2 93  ? 136.408 83.449  139.269 1.00 33.14  ? 72  THR D OG1   1 
ATOM   13939 C  CG2   . THR D 2 93  ? 135.666 84.287  141.407 1.00 31.89  ? 72  THR D CG2   1 
ATOM   13940 N  N     . GLY D 2 94  ? 135.203 87.534  140.053 1.00 29.61  ? 73  GLY D N     1 
ATOM   13941 C  CA    . GLY D 2 94  ? 134.958 88.722  140.874 1.00 28.47  ? 73  GLY D CA    1 
ATOM   13942 C  C     . GLY D 2 94  ? 133.598 89.370  140.712 1.00 27.90  ? 73  GLY D C     1 
ATOM   13943 O  O     . GLY D 2 94  ? 132.862 89.558  141.691 1.00 28.27  ? 73  GLY D O     1 
ATOM   13944 N  N     . MET D 2 95  ? 133.256 89.746  139.488 1.00 26.67  ? 74  MET D N     1 
ATOM   13945 C  CA    . MET D 2 95  ? 131.961 90.391  139.287 1.00 26.00  ? 74  MET D CA    1 
ATOM   13946 C  C     . MET D 2 95  ? 130.808 89.398  139.381 1.00 25.25  ? 74  MET D C     1 
ATOM   13947 O  O     . MET D 2 95  ? 129.804 89.710  140.007 1.00 24.97  ? 74  MET D O     1 
ATOM   13948 C  CB    . MET D 2 95  ? 131.894 91.196  137.983 1.00 26.00  ? 74  MET D CB    1 
ATOM   13949 C  CG    . MET D 2 95  ? 132.557 92.549  138.065 1.00 26.40  ? 74  MET D CG    1 
ATOM   13950 S  SD    . MET D 2 95  ? 131.819 93.659  139.290 1.00 28.10  ? 74  MET D SD    1 
ATOM   13951 C  CE    . MET D 2 95  ? 132.989 95.008  139.194 1.00 28.95  ? 74  MET D CE    1 
ATOM   13952 N  N     . PRO D 2 96  ? 130.940 88.211  138.758 1.00 24.98  ? 75  PRO D N     1 
ATOM   13953 C  CA    . PRO D 2 96  ? 129.782 87.306  138.865 1.00 24.59  ? 75  PRO D CA    1 
ATOM   13954 C  C     . PRO D 2 96  ? 129.500 86.811  140.282 1.00 23.90  ? 75  PRO D C     1 
ATOM   13955 O  O     . PRO D 2 96  ? 128.342 86.581  140.610 1.00 23.45  ? 75  PRO D O     1 
ATOM   13956 C  CB    . PRO D 2 96  ? 130.162 86.123  137.964 1.00 24.80  ? 75  PRO D CB    1 
ATOM   13957 C  CG    . PRO D 2 96  ? 131.145 86.705  136.973 1.00 25.75  ? 75  PRO D CG    1 
ATOM   13958 C  CD    . PRO D 2 96  ? 131.914 87.742  137.749 1.00 25.07  ? 75  PRO D CD    1 
ATOM   13959 N  N     . ILE D 2 97  ? 130.537 86.639  141.106 1.00 23.36  ? 76  ILE D N     1 
ATOM   13960 C  CA    . ILE D 2 97  ? 130.325 86.141  142.461 1.00 23.48  ? 76  ILE D CA    1 
ATOM   13961 C  C     . ILE D 2 97  ? 129.642 87.192  143.321 1.00 23.30  ? 76  ILE D C     1 
ATOM   13962 O  O     . ILE D 2 97  ? 128.792 86.860  144.144 1.00 23.45  ? 76  ILE D O     1 
ATOM   13963 C  CB    . ILE D 2 97  ? 131.627 85.609  143.123 1.00 23.96  ? 76  ILE D CB    1 
ATOM   13964 C  CG1   . ILE D 2 97  ? 131.304 84.572  144.193 1.00 24.71  ? 76  ILE D CG1   1 
ATOM   13965 C  CG2   . ILE D 2 97  ? 132.502 86.750  143.698 1.00 24.02  ? 76  ILE D CG2   1 
ATOM   13966 C  CD1   . ILE D 2 97  ? 132.386 83.468  144.295 1.00 29.17  ? 76  ILE D CD1   1 
ATOM   13967 N  N     . VAL D 2 98  ? 130.005 88.458  143.120 1.00 22.71  ? 77  VAL D N     1 
ATOM   13968 C  CA    . VAL D 2 98  ? 129.368 89.561  143.857 1.00 22.78  ? 77  VAL D CA    1 
ATOM   13969 C  C     . VAL D 2 98  ? 127.913 89.728  143.413 1.00 22.89  ? 77  VAL D C     1 
ATOM   13970 O  O     . VAL D 2 98  ? 127.019 89.898  144.241 1.00 23.72  ? 77  VAL D O     1 
ATOM   13971 C  CB    . VAL D 2 98  ? 130.182 90.880  143.734 1.00 22.49  ? 77  VAL D CB    1 
ATOM   13972 C  CG1   . VAL D 2 98  ? 129.408 92.082  144.305 1.00 21.91  ? 77  VAL D CG1   1 
ATOM   13973 C  CG2   . VAL D 2 98  ? 131.509 90.730  144.460 1.00 23.02  ? 77  VAL D CG2   1 
ATOM   13974 N  N     . ALA D 2 99  ? 127.672 89.641  142.105 1.00 23.19  ? 78  ALA D N     1 
ATOM   13975 C  CA    . ALA D 2 99  ? 126.302 89.708  141.575 1.00 23.05  ? 78  ALA D CA    1 
ATOM   13976 C  C     . ALA D 2 99  ? 125.429 88.598  142.167 1.00 23.52  ? 78  ALA D C     1 
ATOM   13977 O  O     . ALA D 2 99  ? 124.248 88.802  142.464 1.00 23.68  ? 78  ALA D O     1 
ATOM   13978 C  CB    . ALA D 2 99  ? 126.318 89.636  140.057 1.00 22.81  ? 78  ALA D CB    1 
ATOM   13979 N  N     . GLU D 2 100 ? 126.016 87.419  142.348 1.00 23.68  ? 79  GLU D N     1 
ATOM   13980 C  CA    . GLU D 2 100 ? 125.297 86.289  142.932 1.00 24.14  ? 79  GLU D CA    1 
ATOM   13981 C  C     . GLU D 2 100 ? 124.833 86.519  144.379 1.00 23.66  ? 79  GLU D C     1 
ATOM   13982 O  O     . GLU D 2 100 ? 123.707 86.164  144.742 1.00 22.94  ? 79  GLU D O     1 
ATOM   13983 C  CB    . GLU D 2 100 ? 126.163 85.032  142.847 1.00 24.47  ? 79  GLU D CB    1 
ATOM   13984 C  CG    . GLU D 2 100 ? 125.431 83.753  143.206 1.00 27.90  ? 79  GLU D CG    1 
ATOM   13985 C  CD    . GLU D 2 100 ? 126.357 82.553  143.286 1.00 32.30  ? 79  GLU D CD    1 
ATOM   13986 O  OE1   . GLU D 2 100 ? 127.416 82.559  142.618 1.00 32.88  ? 79  GLU D OE1   1 
ATOM   13987 O  OE2   . GLU D 2 100 ? 126.021 81.606  144.025 1.00 34.74  ? 79  GLU D OE2   1 
ATOM   13988 N  N     . HIS D 2 101 ? 125.700 87.101  145.207 1.00 23.62  ? 80  HIS D N     1 
ATOM   13989 C  CA    . HIS D 2 101 ? 125.398 87.270  146.640 1.00 23.99  ? 80  HIS D CA    1 
ATOM   13990 C  C     . HIS D 2 101 ? 124.701 88.578  147.039 1.00 24.35  ? 80  HIS D C     1 
ATOM   13991 O  O     . HIS D 2 101 ? 124.128 88.662  148.126 1.00 24.21  ? 80  HIS D O     1 
ATOM   13992 C  CB    . HIS D 2 101 ? 126.661 87.043  147.483 1.00 24.13  ? 80  HIS D CB    1 
ATOM   13993 C  CG    . HIS D 2 101 ? 127.172 85.634  147.418 1.00 24.76  ? 80  HIS D CG    1 
ATOM   13994 N  ND1   . HIS D 2 101 ? 126.824 84.673  148.344 1.00 25.68  ? 80  HIS D ND1   1 
ATOM   13995 C  CD2   . HIS D 2 101 ? 127.984 85.021  146.526 1.00 25.75  ? 80  HIS D CD2   1 
ATOM   13996 C  CE1   . HIS D 2 101 ? 127.405 83.528  148.025 1.00 26.21  ? 80  HIS D CE1   1 
ATOM   13997 N  NE2   . HIS D 2 101 ? 128.115 83.712  146.927 1.00 25.35  ? 80  HIS D NE2   1 
ATOM   13998 N  N     . VAL D 2 102 ? 124.758 89.596  146.182 1.00 24.50  ? 81  VAL D N     1 
ATOM   13999 C  CA    . VAL D 2 102 ? 124.077 90.863  146.448 1.00 25.50  ? 81  VAL D CA    1 
ATOM   14000 C  C     . VAL D 2 102 ? 122.567 90.715  146.202 1.00 26.14  ? 81  VAL D C     1 
ATOM   14001 O  O     . VAL D 2 102 ? 122.162 90.149  145.190 1.00 26.96  ? 81  VAL D O     1 
ATOM   14002 C  CB    . VAL D 2 102 ? 124.660 92.011  145.573 1.00 25.30  ? 81  VAL D CB    1 
ATOM   14003 C  CG1   . VAL D 2 102 ? 123.789 93.243  145.639 1.00 27.08  ? 81  VAL D CG1   1 
ATOM   14004 C  CG2   . VAL D 2 102 ? 126.067 92.360  146.031 1.00 25.41  ? 81  VAL D CG2   1 
ATOM   14005 N  N     . ASP D 2 103 ? 121.753 91.207  147.133 1.00 26.45  ? 82  ASP D N     1 
ATOM   14006 C  CA    . ASP D 2 103 ? 120.299 91.225  146.962 1.00 27.15  ? 82  ASP D CA    1 
ATOM   14007 C  C     . ASP D 2 103 ? 119.854 92.518  146.294 1.00 26.39  ? 82  ASP D C     1 
ATOM   14008 O  O     . ASP D 2 103 ? 120.389 93.597  146.579 1.00 26.40  ? 82  ASP D O     1 
ATOM   14009 C  CB    . ASP D 2 103 ? 119.579 91.076  148.307 1.00 27.72  ? 82  ASP D CB    1 
ATOM   14010 C  CG    . ASP D 2 103 ? 119.866 89.747  148.997 1.00 31.46  ? 82  ASP D CG    1 
ATOM   14011 O  OD1   . ASP D 2 103 ? 120.078 88.712  148.308 1.00 34.26  ? 82  ASP D OD1   1 
ATOM   14012 O  OD2   . ASP D 2 103 ? 119.871 89.735  150.249 1.00 35.52  ? 82  ASP D OD2   1 
ATOM   14013 N  N     . GLY D 2 104 ? 118.859 92.404  145.419 1.00 25.52  ? 83  GLY D N     1 
ATOM   14014 C  CA    . GLY D 2 104 ? 118.298 93.565  144.731 1.00 24.31  ? 83  GLY D CA    1 
ATOM   14015 C  C     . GLY D 2 104 ? 118.388 93.352  143.224 1.00 23.27  ? 83  GLY D C     1 
ATOM   14016 O  O     . GLY D 2 104 ? 119.468 93.110  142.687 1.00 22.38  ? 83  GLY D O     1 
ATOM   14017 N  N     . HIS D 2 105 ? 117.247 93.425  142.544 1.00 22.46  ? 84  HIS D N     1 
ATOM   14018 C  CA    . HIS D 2 105 ? 117.217 93.225  141.093 1.00 22.17  ? 84  HIS D CA    1 
ATOM   14019 C  C     . HIS D 2 105 ? 118.031 94.252  140.324 1.00 21.13  ? 84  HIS D C     1 
ATOM   14020 O  O     . HIS D 2 105 ? 118.698 93.907  139.351 1.00 20.91  ? 84  HIS D O     1 
ATOM   14021 C  CB    . HIS D 2 105 ? 115.770 93.203  140.580 1.00 22.07  ? 84  HIS D CB    1 
ATOM   14022 C  CG    . HIS D 2 105 ? 114.945 92.123  141.202 1.00 23.85  ? 84  HIS D CG    1 
ATOM   14023 N  ND1   . HIS D 2 105 ? 115.354 90.807  141.231 1.00 24.86  ? 84  HIS D ND1   1 
ATOM   14024 C  CD2   . HIS D 2 105 ? 113.758 92.164  141.850 1.00 25.19  ? 84  HIS D CD2   1 
ATOM   14025 C  CE1   . HIS D 2 105 ? 114.443 90.080  141.852 1.00 24.94  ? 84  HIS D CE1   1 
ATOM   14026 N  NE2   . HIS D 2 105 ? 113.468 90.881  142.242 1.00 26.41  ? 84  HIS D NE2   1 
ATOM   14027 N  N     . GLN D 2 106 ? 117.976 95.504  140.754 1.00 20.66  ? 85  GLN D N     1 
ATOM   14028 C  CA    . GLN D 2 106 ? 118.629 96.571  140.001 1.00 20.70  ? 85  GLN D CA    1 
ATOM   14029 C  C     . GLN D 2 106 ? 120.144 96.489  140.179 1.00 20.46  ? 85  GLN D C     1 
ATOM   14030 O  O     . GLN D 2 106 ? 120.891 96.700  139.224 1.00 20.72  ? 85  GLN D O     1 
ATOM   14031 C  CB    . GLN D 2 106 ? 118.038 97.947  140.351 1.00 20.60  ? 85  GLN D CB    1 
ATOM   14032 C  CG    . GLN D 2 106 ? 116.528 98.058  140.007 1.00 20.74  ? 85  GLN D CG    1 
ATOM   14033 C  CD    . GLN D 2 106 ? 115.855 99.337  140.520 1.00 22.11  ? 85  GLN D CD    1 
ATOM   14034 O  OE1   . GLN D 2 106 ? 116.491 100.376 140.664 1.00 22.88  ? 85  GLN D OE1   1 
ATOM   14035 N  NE2   . GLN D 2 106 ? 114.553 99.259  140.783 1.00 21.64  ? 85  GLN D NE2   1 
ATOM   14036 N  N     . ARG D 2 107 ? 120.585 96.131  141.387 1.00 20.17  ? 86  ARG D N     1 
ATOM   14037 C  CA    . ARG D 2 107 ? 122.010 95.935  141.662 1.00 20.29  ? 86  ARG D CA    1 
ATOM   14038 C  C     . ARG D 2 107 ? 122.556 94.762  140.864 1.00 20.07  ? 86  ARG D C     1 
ATOM   14039 O  O     . ARG D 2 107 ? 123.647 94.845  140.315 1.00 19.53  ? 86  ARG D O     1 
ATOM   14040 C  CB    . ARG D 2 107 ? 122.253 95.682  143.147 1.00 20.88  ? 86  ARG D CB    1 
ATOM   14041 C  CG    . ARG D 2 107 ? 121.769 96.796  144.016 1.00 22.56  ? 86  ARG D CG    1 
ATOM   14042 C  CD    . ARG D 2 107 ? 121.724 96.367  145.461 1.00 27.21  ? 86  ARG D CD    1 
ATOM   14043 N  NE    . ARG D 2 107 ? 121.760 97.579  146.257 1.00 31.70  ? 86  ARG D NE    1 
ATOM   14044 C  CZ    . ARG D 2 107 ? 122.121 97.648  147.521 1.00 32.23  ? 86  ARG D CZ    1 
ATOM   14045 N  NH1   . ARG D 2 107 ? 122.121 98.832  148.107 1.00 34.27  ? 86  ARG D NH1   1 
ATOM   14046 N  NH2   . ARG D 2 107 ? 122.482 96.552  148.186 1.00 33.79  ? 86  ARG D NH2   1 
ATOM   14047 N  N     . LYS D 2 108 ? 121.799 93.665  140.817 1.00 19.61  ? 87  LYS D N     1 
ATOM   14048 C  CA    . LYS D 2 108 ? 122.216 92.509  140.024 1.00 19.92  ? 87  LYS D CA    1 
ATOM   14049 C  C     . LYS D 2 108 ? 122.366 92.864  138.541 1.00 20.08  ? 87  LYS D C     1 
ATOM   14050 O  O     . LYS D 2 108 ? 123.247 92.331  137.857 1.00 20.38  ? 87  LYS D O     1 
ATOM   14051 C  CB    . LYS D 2 108 ? 121.267 91.322  140.204 1.00 19.54  ? 87  LYS D CB    1 
ATOM   14052 C  CG    . LYS D 2 108 ? 121.281 90.717  141.596 1.00 20.55  ? 87  LYS D CG    1 
ATOM   14053 C  CD    . LYS D 2 108 ? 120.332 89.521  141.694 1.00 21.09  ? 87  LYS D CD    1 
ATOM   14054 C  CE    . LYS D 2 108 ? 120.364 88.874  143.074 1.00 22.98  ? 87  LYS D CE    1 
ATOM   14055 N  NZ    . LYS D 2 108 ? 121.658 88.120  143.290 1.00 22.30  ? 87  LYS D NZ    1 
ATOM   14056 N  N     . ALA D 2 109 ? 121.504 93.751  138.045 1.00 19.72  ? 88  ALA D N     1 
ATOM   14057 C  CA    . ALA D 2 109 ? 121.565 94.160  136.647 1.00 19.83  ? 88  ALA D CA    1 
ATOM   14058 C  C     . ALA D 2 109 ? 122.819 94.988  136.363 1.00 19.84  ? 88  ALA D C     1 
ATOM   14059 O  O     . ALA D 2 109 ? 123.520 94.747  135.374 1.00 19.96  ? 88  ALA D O     1 
ATOM   14060 C  CB    . ALA D 2 109 ? 120.290 94.918  136.241 1.00 19.65  ? 88  ALA D CB    1 
ATOM   14061 N  N     . VAL D 2 110 ? 123.115 95.944  137.242 1.00 19.33  ? 89  VAL D N     1 
ATOM   14062 C  CA    . VAL D 2 110 ? 124.319 96.775  137.095 1.00 19.22  ? 89  VAL D CA    1 
ATOM   14063 C  C     . VAL D 2 110 ? 125.564 95.872  137.168 1.00 19.45  ? 89  VAL D C     1 
ATOM   14064 O  O     . VAL D 2 110 ? 126.423 95.899  136.276 1.00 18.97  ? 89  VAL D O     1 
ATOM   14065 C  CB    . VAL D 2 110 ? 124.333 97.934  138.133 1.00 19.01  ? 89  VAL D CB    1 
ATOM   14066 C  CG1   . VAL D 2 110 ? 125.685 98.705  138.125 1.00 19.90  ? 89  VAL D CG1   1 
ATOM   14067 C  CG2   . VAL D 2 110 ? 123.201 98.891  137.834 1.00 19.69  ? 89  VAL D CG2   1 
ATOM   14068 N  N     . LEU D 2 111 ? 125.617 95.019  138.193 1.00 19.27  ? 90  LEU D N     1 
ATOM   14069 C  CA    . LEU D 2 111 ? 126.726 94.072  138.324 1.00 19.96  ? 90  LEU D CA    1 
ATOM   14070 C  C     . LEU D 2 111 ? 126.892 93.152  137.108 1.00 20.30  ? 90  LEU D C     1 
ATOM   14071 O  O     . LEU D 2 111 ? 128.018 92.913  136.665 1.00 19.88  ? 90  LEU D O     1 
ATOM   14072 C  CB    . LEU D 2 111 ? 126.635 93.282  139.637 1.00 19.87  ? 90  LEU D CB    1 
ATOM   14073 C  CG    . LEU D 2 111 ? 126.843 94.152  140.879 1.00 20.24  ? 90  LEU D CG    1 
ATOM   14074 C  CD1   . LEU D 2 111 ? 126.409 93.454  142.178 1.00 21.85  ? 90  LEU D CD1   1 
ATOM   14075 C  CD2   . LEU D 2 111 ? 128.297 94.651  140.970 1.00 20.29  ? 90  LEU D CD2   1 
ATOM   14076 N  N     . ASN D 2 112 ? 125.777 92.662  136.558 1.00 20.92  ? 91  ASN D N     1 
ATOM   14077 C  CA    . ASN D 2 112 ? 125.810 91.897  135.289 1.00 20.70  ? 91  ASN D CA    1 
ATOM   14078 C  C     . ASN D 2 112 ? 126.400 92.685  134.134 1.00 20.57  ? 91  ASN D C     1 
ATOM   14079 O  O     . ASN D 2 112 ? 127.108 92.127  133.279 1.00 20.45  ? 91  ASN D O     1 
ATOM   14080 C  CB    . ASN D 2 112 ? 124.406 91.474  134.856 1.00 21.16  ? 91  ASN D CB    1 
ATOM   14081 C  CG    . ASN D 2 112 ? 124.046 90.068  135.292 1.00 21.98  ? 91  ASN D CG    1 
ATOM   14082 O  OD1   . ASN D 2 112 ? 124.797 89.401  136.010 1.00 25.37  ? 91  ASN D OD1   1 
ATOM   14083 N  ND2   . ASN D 2 112 ? 122.875 89.619  134.877 1.00 21.12  ? 91  ASN D ND2   1 
ATOM   14084 N  N     . PHE D 2 113 ? 126.035 93.962  134.058 1.00 19.70  ? 92  PHE D N     1 
ATOM   14085 C  CA    . PHE D 2 113 ? 126.566 94.824  133.024 1.00 20.02  ? 92  PHE D CA    1 
ATOM   14086 C  C     . PHE D 2 113 ? 128.089 94.971  133.164 1.00 19.97  ? 92  PHE D C     1 
ATOM   14087 O  O     . PHE D 2 113 ? 128.824 94.875  132.175 1.00 19.22  ? 92  PHE D O     1 
ATOM   14088 C  CB    . PHE D 2 113 ? 125.876 96.199  133.003 1.00 20.09  ? 92  PHE D CB    1 
ATOM   14089 C  CG    . PHE D 2 113 ? 126.285 97.032  131.840 1.00 20.54  ? 92  PHE D CG    1 
ATOM   14090 C  CD1   . PHE D 2 113 ? 127.411 97.854  131.926 1.00 20.14  ? 92  PHE D CD1   1 
ATOM   14091 C  CD2   . PHE D 2 113 ? 125.590 96.952  130.632 1.00 20.77  ? 92  PHE D CD2   1 
ATOM   14092 C  CE1   . PHE D 2 113 ? 127.826 98.604  130.826 1.00 20.54  ? 92  PHE D CE1   1 
ATOM   14093 C  CE2   . PHE D 2 113 ? 125.995 97.704  129.532 1.00 21.23  ? 92  PHE D CE2   1 
ATOM   14094 C  CZ    . PHE D 2 113 ? 127.112 98.521  129.624 1.00 20.92  ? 92  PHE D CZ    1 
ATOM   14095 N  N     . MET D 2 114 ? 128.550 95.188  134.392 1.00 19.67  ? 93  MET D N     1 
ATOM   14096 C  CA    . MET D 2 114 ? 129.980 95.277  134.658 1.00 20.55  ? 93  MET D CA    1 
ATOM   14097 C  C     . MET D 2 114 ? 130.716 93.980  134.312 1.00 20.82  ? 93  MET D C     1 
ATOM   14098 O  O     . MET D 2 114 ? 131.783 94.045  133.718 1.00 20.43  ? 93  MET D O     1 
ATOM   14099 C  CB    . MET D 2 114 ? 130.244 95.678  136.104 1.00 20.24  ? 93  MET D CB    1 
ATOM   14100 C  CG    . MET D 2 114 ? 129.581 96.999  136.439 1.00 22.05  ? 93  MET D CG    1 
ATOM   14101 S  SD    . MET D 2 114 ? 129.669 97.454  138.156 1.00 25.85  ? 93  MET D SD    1 
ATOM   14102 C  CE    . MET D 2 114 ? 129.473 99.236  138.000 1.00 27.57  ? 93  MET D CE    1 
ATOM   14103 N  N     . ALA D 2 115 ? 130.143 92.825  134.680 1.00 21.19  ? 94  ALA D N     1 
ATOM   14104 C  CA    . ALA D 2 115 ? 130.732 91.519  134.323 1.00 21.53  ? 94  ALA D CA    1 
ATOM   14105 C  C     . ALA D 2 115 ? 130.823 91.360  132.807 1.00 21.75  ? 94  ALA D C     1 
ATOM   14106 O  O     . ALA D 2 115 ? 131.847 90.909  132.293 1.00 22.18  ? 94  ALA D O     1 
ATOM   14107 C  CB    . ALA D 2 115 ? 129.944 90.360  134.946 1.00 21.32  ? 94  ALA D CB    1 
ATOM   14108 N  N     . MET D 2 116 ? 129.766 91.760  132.097 1.00 21.47  ? 95  MET D N     1 
ATOM   14109 C  CA    . MET D 2 116 ? 129.766 91.757  130.637 1.00 21.83  ? 95  MET D CA    1 
ATOM   14110 C  C     . MET D 2 116 ? 130.944 92.568  130.062 1.00 22.15  ? 95  MET D C     1 
ATOM   14111 O  O     . MET D 2 116 ? 131.638 92.099  129.163 1.00 22.09  ? 95  MET D O     1 
ATOM   14112 C  CB    . MET D 2 116 ? 128.424 92.275  130.094 1.00 21.72  ? 95  MET D CB    1 
ATOM   14113 C  CG    . MET D 2 116 ? 128.350 92.411  128.564 1.00 22.57  ? 95  MET D CG    1 
ATOM   14114 S  SD    . MET D 2 116 ? 129.151 93.893  127.898 1.00 22.75  ? 95  MET D SD    1 
ATOM   14115 C  CE    . MET D 2 116 ? 128.101 95.195  128.543 1.00 22.96  ? 95  MET D CE    1 
ATOM   14116 N  N     . MET D 2 117 ? 131.159 93.777  130.586 1.00 22.04  ? 96  MET D N     1 
ATOM   14117 C  CA    . MET D 2 117 ? 132.255 94.641  130.116 1.00 22.45  ? 96  MET D CA    1 
ATOM   14118 C  C     . MET D 2 117 ? 133.627 93.969  130.297 1.00 22.39  ? 96  MET D C     1 
ATOM   14119 O  O     . MET D 2 117 ? 134.489 94.061  129.421 1.00 21.88  ? 96  MET D O     1 
ATOM   14120 C  CB    . MET D 2 117 ? 132.218 96.018  130.810 1.00 22.00  ? 96  MET D CB    1 
ATOM   14121 C  CG    . MET D 2 117 ? 131.049 96.923  130.339 1.00 23.25  ? 96  MET D CG    1 
ATOM   14122 S  SD    . MET D 2 117 ? 131.056 97.260  128.563 1.00 24.28  ? 96  MET D SD    1 
ATOM   14123 C  CE    . MET D 2 117 ? 132.431 98.395  128.415 1.00 24.59  ? 96  MET D CE    1 
ATOM   14124 N  N     . GLU D 2 118 ? 133.814 93.276  131.420 1.00 22.66  ? 97  GLU D N     1 
ATOM   14125 C  CA    . GLU D 2 118 ? 135.064 92.546  131.667 1.00 23.52  ? 97  GLU D CA    1 
ATOM   14126 C  C     . GLU D 2 118 ? 135.305 91.479  130.613 1.00 24.25  ? 97  GLU D C     1 
ATOM   14127 O  O     . GLU D 2 118 ? 136.385 91.431  130.020 1.00 25.05  ? 97  GLU D O     1 
ATOM   14128 C  CB    . GLU D 2 118 ? 135.103 91.896  133.070 1.00 23.11  ? 97  GLU D CB    1 
ATOM   14129 C  CG    . GLU D 2 118 ? 134.621 92.766  134.238 1.00 23.08  ? 97  GLU D CG    1 
ATOM   14130 C  CD    . GLU D 2 118 ? 135.537 93.932  134.575 1.00 24.08  ? 97  GLU D CD    1 
ATOM   14131 O  OE1   . GLU D 2 118 ? 136.393 94.285  133.750 1.00 26.39  ? 97  GLU D OE1   1 
ATOM   14132 O  OE2   . GLU D 2 118 ? 135.380 94.520  135.666 1.00 27.52  ? 97  GLU D OE2   1 
ATOM   14133 N  N     . ASN D 2 119 ? 134.292 90.649  130.374 1.00 25.47  ? 98  ASN D N     1 
ATOM   14134 C  CA    . ASN D 2 119 ? 134.416 89.441  129.534 1.00 26.32  ? 98  ASN D CA    1 
ATOM   14135 C  C     . ASN D 2 119 ? 134.271 89.674  128.033 1.00 26.22  ? 98  ASN D C     1 
ATOM   14136 O  O     . ASN D 2 119 ? 134.967 89.033  127.219 1.00 26.54  ? 98  ASN D O     1 
ATOM   14137 C  CB    . ASN D 2 119 ? 133.398 88.375  129.978 1.00 26.72  ? 98  ASN D CB    1 
ATOM   14138 C  CG    . ASN D 2 119 ? 133.680 87.850  131.386 1.00 29.12  ? 98  ASN D CG    1 
ATOM   14139 O  OD1   . ASN D 2 119 ? 134.791 87.400  131.686 1.00 32.07  ? 98  ASN D OD1   1 
ATOM   14140 N  ND2   . ASN D 2 119 ? 132.683 87.935  132.260 1.00 29.12  ? 98  ASN D ND2   1 
ATOM   14141 N  N     . ALA D 2 120 ? 133.354 90.567  127.675 1.00 25.46  ? 99  ALA D N     1 
ATOM   14142 C  CA    . ALA D 2 120 ? 133.013 90.807  126.275 1.00 25.77  ? 99  ALA D CA    1 
ATOM   14143 C  C     . ALA D 2 120 ? 133.781 91.970  125.654 1.00 25.51  ? 99  ALA D C     1 
ATOM   14144 O  O     . ALA D 2 120 ? 133.993 91.989  124.439 1.00 26.64  ? 99  ALA D O     1 
ATOM   14145 C  CB    . ALA D 2 120 ? 131.499 91.028  126.117 1.00 25.75  ? 99  ALA D CB    1 
ATOM   14146 N  N     . VAL D 2 121 ? 134.187 92.935  126.471 1.00 24.40  ? 100 VAL D N     1 
ATOM   14147 C  CA    . VAL D 2 121 ? 134.790 94.151  125.937 1.00 24.15  ? 100 VAL D CA    1 
ATOM   14148 C  C     . VAL D 2 121 ? 136.269 94.267  126.317 1.00 23.94  ? 100 VAL D C     1 
ATOM   14149 O  O     . VAL D 2 121 ? 137.138 94.315  125.441 1.00 23.75  ? 100 VAL D O     1 
ATOM   14150 C  CB    . VAL D 2 121 ? 133.988 95.424  126.348 1.00 23.68  ? 100 VAL D CB    1 
ATOM   14151 C  CG1   . VAL D 2 121 ? 134.616 96.679  125.744 1.00 23.76  ? 100 VAL D CG1   1 
ATOM   14152 C  CG2   . VAL D 2 121 ? 132.531 95.297  125.893 1.00 23.99  ? 100 VAL D CG2   1 
ATOM   14153 N  N     . HIS D 2 122 ? 136.545 94.306  127.619 1.00 23.68  ? 101 HIS D N     1 
ATOM   14154 C  CA    . HIS D 2 122 ? 137.919 94.437  128.109 1.00 24.02  ? 101 HIS D CA    1 
ATOM   14155 C  C     . HIS D 2 122 ? 138.819 93.296  127.664 1.00 24.39  ? 101 HIS D C     1 
ATOM   14156 O  O     . HIS D 2 122 ? 139.924 93.543  127.188 1.00 24.71  ? 101 HIS D O     1 
ATOM   14157 C  CB    . HIS D 2 122 ? 137.971 94.588  129.635 1.00 23.20  ? 101 HIS D CB    1 
ATOM   14158 C  CG    . HIS D 2 122 ? 137.314 95.833  130.143 1.00 22.82  ? 101 HIS D CG    1 
ATOM   14159 N  ND1   . HIS D 2 122 ? 137.202 96.116  131.487 1.00 20.48  ? 101 HIS D ND1   1 
ATOM   14160 C  CD2   . HIS D 2 122 ? 136.710 96.857  129.491 1.00 21.03  ? 101 HIS D CD2   1 
ATOM   14161 C  CE1   . HIS D 2 122 ? 136.573 97.267  131.641 1.00 19.88  ? 101 HIS D CE1   1 
ATOM   14162 N  NE2   . HIS D 2 122 ? 136.265 97.739  130.445 1.00 21.62  ? 101 HIS D NE2   1 
ATOM   14163 N  N     . ALA D 2 123 ? 138.352 92.056  127.806 1.00 25.30  ? 102 ALA D N     1 
ATOM   14164 C  CA    . ALA D 2 123 ? 139.190 90.894  127.475 1.00 25.77  ? 102 ALA D CA    1 
ATOM   14165 C  C     . ALA D 2 123 ? 139.552 90.843  125.987 1.00 26.37  ? 102 ALA D C     1 
ATOM   14166 O  O     . ALA D 2 123 ? 140.686 90.508  125.622 1.00 25.87  ? 102 ALA D O     1 
ATOM   14167 C  CB    . ALA D 2 123 ? 138.517 89.588  127.917 1.00 26.43  ? 102 ALA D CB    1 
ATOM   14168 N  N     . LYS D 2 124 ? 138.583 91.182  125.135 1.00 26.51  ? 103 LYS D N     1 
ATOM   14169 C  CA    . LYS D 2 124 ? 138.805 91.233  123.697 1.00 27.22  ? 103 LYS D CA    1 
ATOM   14170 C  C     . LYS D 2 124 ? 139.764 92.378  123.340 1.00 26.63  ? 103 LYS D C     1 
ATOM   14171 O  O     . LYS D 2 124 ? 140.587 92.236  122.435 1.00 26.07  ? 103 LYS D O     1 
ATOM   14172 C  CB    . LYS D 2 124 ? 137.467 91.371  122.944 1.00 27.51  ? 103 LYS D CB    1 
ATOM   14173 C  CG    . LYS D 2 124 ? 137.577 91.525  121.412 1.00 30.58  ? 103 LYS D CG    1 
ATOM   14174 C  CD    . LYS D 2 124 ? 138.100 90.264  120.741 1.00 35.72  ? 103 LYS D CD    1 
ATOM   14175 C  CE    . LYS D 2 124 ? 138.240 90.428  119.225 1.00 37.33  ? 103 LYS D CE    1 
ATOM   14176 N  NZ    . LYS D 2 124 ? 136.906 90.607  118.592 1.00 40.73  ? 103 LYS D NZ    1 
ATOM   14177 N  N     . SER D 2 125 ? 139.658 93.492  124.070 1.00 26.02  ? 104 SER D N     1 
ATOM   14178 C  CA    . SER D 2 125 ? 140.499 94.671  123.846 1.00 26.16  ? 104 SER D CA    1 
ATOM   14179 C  C     . SER D 2 125 ? 141.972 94.399  124.152 1.00 26.18  ? 104 SER D C     1 
ATOM   14180 O  O     . SER D 2 125 ? 142.851 94.807  123.385 1.00 26.06  ? 104 SER D O     1 
ATOM   14181 C  CB    . SER D 2 125 ? 140.007 95.863  124.671 1.00 26.10  ? 104 SER D CB    1 
ATOM   14182 O  OG    . SER D 2 125 ? 138.726 96.271  124.226 1.00 26.58  ? 104 SER D OG    1 
ATOM   14183 N  N     . TYR D 2 126 ? 142.228 93.715  125.265 1.00 25.68  ? 105 TYR D N     1 
ATOM   14184 C  CA    . TYR D 2 126 ? 143.594 93.331  125.644 1.00 26.12  ? 105 TYR D CA    1 
ATOM   14185 C  C     . TYR D 2 126 ? 144.187 92.361  124.616 1.00 26.38  ? 105 TYR D C     1 
ATOM   14186 O  O     . TYR D 2 126 ? 145.341 92.505  124.205 1.00 26.83  ? 105 TYR D O     1 
ATOM   14187 C  CB    . TYR D 2 126 ? 143.629 92.692  127.046 1.00 25.35  ? 105 TYR D CB    1 
ATOM   14188 C  CG    . TYR D 2 126 ? 143.560 93.671  128.202 1.00 25.46  ? 105 TYR D CG    1 
ATOM   14189 C  CD1   . TYR D 2 126 ? 144.481 94.714  128.312 1.00 25.41  ? 105 TYR D CD1   1 
ATOM   14190 C  CD2   . TYR D 2 126 ? 142.594 93.536  129.211 1.00 24.77  ? 105 TYR D CD2   1 
ATOM   14191 C  CE1   . TYR D 2 126 ? 144.431 95.617  129.371 1.00 25.89  ? 105 TYR D CE1   1 
ATOM   14192 C  CE2   . TYR D 2 126 ? 142.536 94.442  130.282 1.00 23.11  ? 105 TYR D CE2   1 
ATOM   14193 C  CZ    . TYR D 2 126 ? 143.467 95.468  130.360 1.00 25.38  ? 105 TYR D CZ    1 
ATOM   14194 O  OH    . TYR D 2 126 ? 143.441 96.374  131.399 1.00 23.31  ? 105 TYR D OH    1 
ATOM   14195 N  N     . SER D 2 127 ? 143.385 91.391  124.193 1.00 27.16  ? 106 SER D N     1 
ATOM   14196 C  CA    . SER D 2 127 ? 143.804 90.424  123.172 1.00 27.83  ? 106 SER D CA    1 
ATOM   14197 C  C     . SER D 2 127 ? 144.179 91.130  121.861 1.00 28.21  ? 106 SER D C     1 
ATOM   14198 O  O     . SER D 2 127 ? 145.238 90.850  121.285 1.00 28.30  ? 106 SER D O     1 
ATOM   14199 C  CB    . SER D 2 127 ? 142.707 89.370  122.946 1.00 28.37  ? 106 SER D CB    1 
ATOM   14200 O  OG    . SER D 2 127 ? 143.045 88.484  121.880 1.00 29.33  ? 106 SER D OG    1 
ATOM   14201 N  N     . ASN D 2 128 ? 143.313 92.044  121.410 1.00 28.27  ? 107 ASN D N     1 
ATOM   14202 C  CA    . ASN D 2 128 ? 143.556 92.876  120.221 1.00 28.79  ? 107 ASN D CA    1 
ATOM   14203 C  C     . ASN D 2 128 ? 144.861 93.665  120.277 1.00 28.53  ? 107 ASN D C     1 
ATOM   14204 O  O     . ASN D 2 128 ? 145.602 93.706  119.288 1.00 28.03  ? 107 ASN D O     1 
ATOM   14205 C  CB    . ASN D 2 128 ? 142.391 93.848  119.962 1.00 29.05  ? 107 ASN D CB    1 
ATOM   14206 C  CG    . ASN D 2 128 ? 141.119 93.140  119.487 1.00 30.48  ? 107 ASN D CG    1 
ATOM   14207 O  OD1   . ASN D 2 128 ? 141.137 91.956  119.159 1.00 32.19  ? 107 ASN D OD1   1 
ATOM   14208 N  ND2   . ASN D 2 128 ? 140.007 93.868  119.470 1.00 31.59  ? 107 ASN D ND2   1 
ATOM   14209 N  N     . ILE D 2 129 ? 145.128 94.312  121.414 1.00 28.21  ? 108 ILE D N     1 
ATOM   14210 C  CA    . ILE D 2 129 ? 146.395 95.034  121.593 1.00 28.76  ? 108 ILE D CA    1 
ATOM   14211 C  C     . ILE D 2 129 ? 147.594 94.084  121.435 1.00 29.83  ? 108 ILE D C     1 
ATOM   14212 O  O     . ILE D 2 129 ? 148.543 94.383  120.697 1.00 29.99  ? 108 ILE D O     1 
ATOM   14213 C  CB    . ILE D 2 129 ? 146.465 95.806  122.950 1.00 28.28  ? 108 ILE D CB    1 
ATOM   14214 C  CG1   . ILE D 2 129 ? 145.388 96.899  123.014 1.00 27.94  ? 108 ILE D CG1   1 
ATOM   14215 C  CG2   . ILE D 2 129 ? 147.853 96.434  123.141 1.00 27.52  ? 108 ILE D CG2   1 
ATOM   14216 C  CD1   . ILE D 2 129 ? 145.141 97.449  124.414 1.00 27.98  ? 108 ILE D CD1   1 
ATOM   14217 N  N     . PHE D 2 130 ? 147.548 92.944  122.120 1.00 30.86  ? 109 PHE D N     1 
ATOM   14218 C  CA    . PHE D 2 130 ? 148.611 91.947  122.023 1.00 32.76  ? 109 PHE D CA    1 
ATOM   14219 C  C     . PHE D 2 130 ? 148.865 91.469  120.590 1.00 34.37  ? 109 PHE D C     1 
ATOM   14220 O  O     . PHE D 2 130 ? 149.998 91.508  120.118 1.00 34.61  ? 109 PHE D O     1 
ATOM   14221 C  CB    . PHE D 2 130 ? 148.318 90.748  122.921 1.00 32.81  ? 109 PHE D CB    1 
ATOM   14222 C  CG    . PHE D 2 130 ? 148.980 90.820  124.267 1.00 33.84  ? 109 PHE D CG    1 
ATOM   14223 C  CD1   . PHE D 2 130 ? 150.365 90.722  124.381 1.00 34.61  ? 109 PHE D CD1   1 
ATOM   14224 C  CD2   . PHE D 2 130 ? 148.219 90.951  125.422 1.00 35.74  ? 109 PHE D CD2   1 
ATOM   14225 C  CE1   . PHE D 2 130 ? 150.988 90.775  125.628 1.00 36.99  ? 109 PHE D CE1   1 
ATOM   14226 C  CE2   . PHE D 2 130 ? 148.829 91.006  126.681 1.00 36.96  ? 109 PHE D CE2   1 
ATOM   14227 C  CZ    . PHE D 2 130 ? 150.216 90.918  126.785 1.00 36.91  ? 109 PHE D CZ    1 
ATOM   14228 N  N     . MET D 2 131 ? 147.801 91.037  119.911 1.00 35.90  ? 110 MET D N     1 
ATOM   14229 C  CA    . MET D 2 131 ? 147.887 90.510  118.548 1.00 37.94  ? 110 MET D CA    1 
ATOM   14230 C  C     . MET D 2 131 ? 148.438 91.533  117.564 1.00 38.05  ? 110 MET D C     1 
ATOM   14231 O  O     . MET D 2 131 ? 149.052 91.161  116.570 1.00 38.20  ? 110 MET D O     1 
ATOM   14232 C  CB    . MET D 2 131 ? 146.522 89.997  118.061 1.00 38.63  ? 110 MET D CB    1 
ATOM   14233 C  CG    . MET D 2 131 ? 146.011 88.741  118.786 1.00 42.34  ? 110 MET D CG    1 
ATOM   14234 S  SD    . MET D 2 131 ? 144.397 88.130  118.198 1.00 50.15  ? 110 MET D SD    1 
ATOM   14235 C  CE    . MET D 2 131 ? 143.257 89.399  118.766 1.00 48.14  ? 110 MET D CE    1 
ATOM   14236 N  N     . THR D 2 132 ? 148.217 92.816  117.846 1.00 38.12  ? 111 THR D N     1 
ATOM   14237 C  CA    . THR D 2 132 ? 148.735 93.890  116.999 1.00 38.79  ? 111 THR D CA    1 
ATOM   14238 C  C     . THR D 2 132 ? 150.252 94.085  117.166 1.00 38.81  ? 111 THR D C     1 
ATOM   14239 O  O     . THR D 2 132 ? 150.967 94.266  116.175 1.00 39.26  ? 111 THR D O     1 
ATOM   14240 C  CB    . THR D 2 132 ? 147.988 95.215  117.255 1.00 38.78  ? 111 THR D CB    1 
ATOM   14241 O  OG1   . THR D 2 132 ? 146.586 95.018  117.040 1.00 39.32  ? 111 THR D OG1   1 
ATOM   14242 C  CG2   . THR D 2 132 ? 148.472 96.310  116.311 1.00 39.75  ? 111 THR D CG2   1 
ATOM   14243 N  N     . LEU D 2 133 ? 150.729 94.030  118.411 1.00 38.34  ? 112 LEU D N     1 
ATOM   14244 C  CA    . LEU D 2 133 ? 152.113 94.376  118.749 1.00 38.36  ? 112 LEU D CA    1 
ATOM   14245 C  C     . LEU D 2 133 ? 153.103 93.211  118.721 1.00 38.94  ? 112 LEU D C     1 
ATOM   14246 O  O     . LEU D 2 133 ? 154.281 93.408  118.427 1.00 39.14  ? 112 LEU D O     1 
ATOM   14247 C  CB    . LEU D 2 133 ? 152.176 95.056  120.127 1.00 37.62  ? 112 LEU D CB    1 
ATOM   14248 C  CG    . LEU D 2 133 ? 151.310 96.294  120.373 1.00 36.50  ? 112 LEU D CG    1 
ATOM   14249 C  CD1   . LEU D 2 133 ? 151.323 96.668  121.858 1.00 35.80  ? 112 LEU D CD1   1 
ATOM   14250 C  CD2   . LEU D 2 133 ? 151.732 97.471  119.510 1.00 35.32  ? 112 LEU D CD2   1 
ATOM   14251 N  N     . ALA D 2 134 ? 152.646 92.006  119.037 1.00 39.41  ? 113 ALA D N     1 
ATOM   14252 C  CA    . ALA D 2 134 ? 153.566 90.864  119.093 1.00 40.33  ? 113 ALA D CA    1 
ATOM   14253 C  C     . ALA D 2 134 ? 153.113 89.699  118.218 1.00 41.05  ? 113 ALA D C     1 
ATOM   14254 O  O     . ALA D 2 134 ? 151.917 89.519  118.016 1.00 40.81  ? 113 ALA D O     1 
ATOM   14255 C  CB    . ALA D 2 134 ? 153.750 90.410  120.530 1.00 40.15  ? 113 ALA D CB    1 
ATOM   14256 N  N     . PRO D 2 135 ? 154.070 88.909  117.684 1.00 42.21  ? 114 PRO D N     1 
ATOM   14257 C  CA    . PRO D 2 135 ? 153.672 87.674  116.998 1.00 43.27  ? 114 PRO D CA    1 
ATOM   14258 C  C     . PRO D 2 135 ? 153.196 86.612  118.000 1.00 43.89  ? 114 PRO D C     1 
ATOM   14259 O  O     . PRO D 2 135 ? 153.523 86.694  119.188 1.00 43.31  ? 114 PRO D O     1 
ATOM   14260 C  CB    . PRO D 2 135 ? 154.958 87.224  116.302 1.00 43.69  ? 114 PRO D CB    1 
ATOM   14261 C  CG    . PRO D 2 135 ? 156.049 87.798  117.123 1.00 43.01  ? 114 PRO D CG    1 
ATOM   14262 C  CD    . PRO D 2 135 ? 155.533 89.103  117.664 1.00 42.16  ? 114 PRO D CD    1 
ATOM   14263 N  N     . THR D 2 136 ? 152.445 85.626  117.511 1.00 45.26  ? 115 THR D N     1 
ATOM   14264 C  CA    . THR D 2 136 ? 151.808 84.605  118.358 1.00 46.11  ? 115 THR D CA    1 
ATOM   14265 C  C     . THR D 2 136 ? 152.768 83.961  119.364 1.00 46.35  ? 115 THR D C     1 
ATOM   14266 O  O     . THR D 2 136 ? 152.432 83.834  120.546 1.00 46.25  ? 115 THR D O     1 
ATOM   14267 C  CB    . THR D 2 136 ? 151.092 83.516  117.512 1.00 46.59  ? 115 THR D CB    1 
ATOM   14268 O  OG1   . THR D 2 136 ? 150.188 84.146  116.599 1.00 47.80  ? 115 THR D OG1   1 
ATOM   14269 C  CG2   . THR D 2 136 ? 150.286 82.563  118.392 1.00 46.94  ? 115 THR D CG2   1 
ATOM   14270 N  N     . GLU D 2 137 ? 153.959 83.581  118.902 1.00 46.92  ? 116 GLU D N     1 
ATOM   14271 C  CA    . GLU D 2 137 ? 154.944 82.925  119.762 1.00 47.37  ? 116 GLU D CA    1 
ATOM   14272 C  C     . GLU D 2 137 ? 155.411 83.808  120.922 1.00 46.64  ? 116 GLU D C     1 
ATOM   14273 O  O     . GLU D 2 137 ? 155.606 83.312  122.033 1.00 46.89  ? 116 GLU D O     1 
ATOM   14274 C  CB    . GLU D 2 137 ? 156.142 82.411  118.948 1.00 48.04  ? 116 GLU D CB    1 
ATOM   14275 C  CG    . GLU D 2 137 ? 157.168 81.595  119.756 1.00 49.86  ? 116 GLU D CG    1 
ATOM   14276 C  CD    . GLU D 2 137 ? 156.668 80.208  120.188 1.00 52.40  ? 116 GLU D CD    1 
ATOM   14277 O  OE1   . GLU D 2 137 ? 155.589 80.108  120.814 1.00 52.97  ? 116 GLU D OE1   1 
ATOM   14278 O  OE2   . GLU D 2 137 ? 157.376 79.209  119.921 1.00 54.12  ? 116 GLU D OE2   1 
ATOM   14279 N  N     . THR D 2 138 ? 155.583 85.102  120.658 1.00 46.09  ? 117 THR D N     1 
ATOM   14280 C  CA    . THR D 2 138 ? 155.972 86.075  121.691 1.00 45.30  ? 117 THR D CA    1 
ATOM   14281 C  C     . THR D 2 138 ? 154.875 86.262  122.747 1.00 44.63  ? 117 THR D C     1 
ATOM   14282 O  O     . THR D 2 138 ? 155.169 86.365  123.942 1.00 44.51  ? 117 THR D O     1 
ATOM   14283 C  CB    . THR D 2 138 ? 156.345 87.442  121.069 1.00 45.20  ? 117 THR D CB    1 
ATOM   14284 O  OG1   . THR D 2 138 ? 157.391 87.259  120.109 1.00 45.69  ? 117 THR D OG1   1 
ATOM   14285 C  CG2   . THR D 2 138 ? 156.821 88.430  122.133 1.00 44.67  ? 117 THR D CG2   1 
ATOM   14286 N  N     . ILE D 2 139 ? 153.618 86.296  122.305 1.00 44.24  ? 118 ILE D N     1 
ATOM   14287 C  CA    . ILE D 2 139 ? 152.479 86.409  123.219 1.00 43.65  ? 118 ILE D CA    1 
ATOM   14288 C  C     . ILE D 2 139 ? 152.432 85.210  124.178 1.00 43.87  ? 118 ILE D C     1 
ATOM   14289 O  O     . ILE D 2 139 ? 152.329 85.384  125.395 1.00 43.36  ? 118 ILE D O     1 
ATOM   14290 C  CB    . ILE D 2 139 ? 151.144 86.587  122.450 1.00 43.68  ? 118 ILE D CB    1 
ATOM   14291 C  CG1   . ILE D 2 139 ? 151.127 87.945  121.732 1.00 43.30  ? 118 ILE D CG1   1 
ATOM   14292 C  CG2   . ILE D 2 139 ? 149.935 86.455  123.394 1.00 43.11  ? 118 ILE D CG2   1 
ATOM   14293 C  CD1   . ILE D 2 139 ? 150.076 88.083  120.638 1.00 43.41  ? 118 ILE D CD1   1 
ATOM   14294 N  N     . ASN D 2 140 ? 152.540 84.003  123.624 1.00 44.52  ? 119 ASN D N     1 
ATOM   14295 C  CA    . ASN D 2 140 ? 152.545 82.773  124.423 1.00 45.00  ? 119 ASN D CA    1 
ATOM   14296 C  C     . ASN D 2 140 ? 153.665 82.743  125.483 1.00 44.99  ? 119 ASN D C     1 
ATOM   14297 O  O     . ASN D 2 140 ? 153.439 82.312  126.621 1.00 44.61  ? 119 ASN D O     1 
ATOM   14298 C  CB    . ASN D 2 140 ? 152.604 81.532  123.515 1.00 45.74  ? 119 ASN D CB    1 
ATOM   14299 C  CG    . ASN D 2 140 ? 151.399 81.420  122.574 1.00 46.40  ? 119 ASN D CG    1 
ATOM   14300 O  OD1   . ASN D 2 140 ? 150.374 82.085  122.756 1.00 46.85  ? 119 ASN D OD1   1 
ATOM   14301 N  ND2   . ASN D 2 140 ? 151.522 80.561  121.564 1.00 48.16  ? 119 ASN D ND2   1 
ATOM   14302 N  N     . GLU D 2 141 ? 154.854 83.226  125.115 1.00 45.09  ? 120 GLU D N     1 
ATOM   14303 C  CA    . GLU D 2 141 ? 155.998 83.263  126.032 1.00 45.27  ? 120 GLU D CA    1 
ATOM   14304 C  C     . GLU D 2 141 ? 155.844 84.286  127.167 1.00 44.75  ? 120 GLU D C     1 
ATOM   14305 O  O     . GLU D 2 141 ? 156.176 83.994  128.321 1.00 44.37  ? 120 GLU D O     1 
ATOM   14306 C  CB    . GLU D 2 141 ? 157.302 83.511  125.272 1.00 45.75  ? 120 GLU D CB    1 
ATOM   14307 C  CG    . GLU D 2 141 ? 157.731 82.347  124.377 1.00 48.17  ? 120 GLU D CG    1 
ATOM   14308 C  CD    . GLU D 2 141 ? 159.055 82.589  123.680 1.00 50.15  ? 120 GLU D CD    1 
ATOM   14309 O  OE1   . GLU D 2 141 ? 160.035 82.965  124.357 1.00 50.90  ? 120 GLU D OE1   1 
ATOM   14310 O  OE2   . GLU D 2 141 ? 159.117 82.394  122.449 1.00 52.25  ? 120 GLU D OE2   1 
ATOM   14311 N  N     . VAL D 2 142 ? 155.358 85.480  126.829 1.00 44.31  ? 121 VAL D N     1 
ATOM   14312 C  CA    . VAL D 2 142 ? 155.096 86.524  127.822 1.00 43.91  ? 121 VAL D CA    1 
ATOM   14313 C  C     . VAL D 2 142 ? 154.068 86.045  128.851 1.00 43.71  ? 121 VAL D C     1 
ATOM   14314 O  O     . VAL D 2 142 ? 154.242 86.252  130.050 1.00 43.44  ? 121 VAL D O     1 
ATOM   14315 C  CB    . VAL D 2 142 ? 154.631 87.852  127.162 1.00 43.65  ? 121 VAL D CB    1 
ATOM   14316 C  CG1   . VAL D 2 142 ? 154.240 88.881  128.223 1.00 43.40  ? 121 VAL D CG1   1 
ATOM   14317 C  CG2   . VAL D 2 142 ? 155.732 88.419  126.272 1.00 43.96  ? 121 VAL D CG2   1 
ATOM   14318 N  N     . PHE D 2 143 ? 153.009 85.393  128.377 1.00 44.03  ? 122 PHE D N     1 
ATOM   14319 C  CA    . PHE D 2 143 ? 151.988 84.868  129.276 1.00 44.42  ? 122 PHE D CA    1 
ATOM   14320 C  C     . PHE D 2 143 ? 152.490 83.713  130.135 1.00 45.38  ? 122 PHE D C     1 
ATOM   14321 O  O     . PHE D 2 143 ? 152.109 83.603  131.297 1.00 45.50  ? 122 PHE D O     1 
ATOM   14322 C  CB    . PHE D 2 143 ? 150.702 84.511  128.527 1.00 44.27  ? 122 PHE D CB    1 
ATOM   14323 C  CG    . PHE D 2 143 ? 149.768 85.674  128.380 1.00 43.28  ? 122 PHE D CG    1 
ATOM   14324 C  CD1   . PHE D 2 143 ? 148.919 86.035  129.425 1.00 42.17  ? 122 PHE D CD1   1 
ATOM   14325 C  CD2   . PHE D 2 143 ? 149.761 86.434  127.218 1.00 42.76  ? 122 PHE D CD2   1 
ATOM   14326 C  CE1   . PHE D 2 143 ? 148.063 87.123  129.307 1.00 42.16  ? 122 PHE D CE1   1 
ATOM   14327 C  CE2   . PHE D 2 143 ? 148.910 87.525  127.089 1.00 42.77  ? 122 PHE D CE2   1 
ATOM   14328 C  CZ    . PHE D 2 143 ? 148.057 87.872  128.136 1.00 42.28  ? 122 PHE D CZ    1 
ATOM   14329 N  N     . GLU D 2 144 ? 153.359 82.878  129.572 1.00 46.18  ? 123 GLU D N     1 
ATOM   14330 C  CA    . GLU D 2 144 ? 154.048 81.846  130.345 1.00 47.19  ? 123 GLU D CA    1 
ATOM   14331 C  C     . GLU D 2 144 ? 154.885 82.464  131.476 1.00 46.99  ? 123 GLU D C     1 
ATOM   14332 O  O     . GLU D 2 144 ? 154.837 81.980  132.611 1.00 46.94  ? 123 GLU D O     1 
ATOM   14333 C  CB    . GLU D 2 144 ? 154.926 80.984  129.428 1.00 47.80  ? 123 GLU D CB    1 
ATOM   14334 C  CG    . GLU D 2 144 ? 155.589 79.775  130.096 1.00 49.54  ? 123 GLU D CG    1 
ATOM   14335 C  CD    . GLU D 2 144 ? 156.543 79.025  129.161 1.00 52.37  ? 123 GLU D CD    1 
ATOM   14336 O  OE1   . GLU D 2 144 ? 157.359 79.676  128.468 1.00 52.92  ? 123 GLU D OE1   1 
ATOM   14337 O  OE2   . GLU D 2 144 ? 156.481 77.777  129.123 1.00 53.55  ? 123 GLU D OE2   1 
ATOM   14338 N  N     . TRP D 2 145 ? 155.636 83.526  131.159 1.00 47.02  ? 124 TRP D N     1 
ATOM   14339 C  CA    . TRP D 2 145 ? 156.489 84.231  132.132 1.00 46.93  ? 124 TRP D CA    1 
ATOM   14340 C  C     . TRP D 2 145 ? 155.662 84.885  133.228 1.00 46.55  ? 124 TRP D C     1 
ATOM   14341 O  O     . TRP D 2 145 ? 155.923 84.683  134.411 1.00 46.42  ? 124 TRP D O     1 
ATOM   14342 C  CB    . TRP D 2 145 ? 157.352 85.300  131.442 1.00 47.07  ? 124 TRP D CB    1 
ATOM   14343 C  CG    . TRP D 2 145 ? 158.419 85.949  132.329 1.00 47.82  ? 124 TRP D CG    1 
ATOM   14344 C  CD1   . TRP D 2 145 ? 159.726 85.558  132.457 1.00 48.78  ? 124 TRP D CD1   1 
ATOM   14345 C  CD2   . TRP D 2 145 ? 158.266 87.105  133.179 1.00 47.80  ? 124 TRP D CD2   1 
ATOM   14346 N  NE1   . TRP D 2 145 ? 160.390 86.387  133.334 1.00 49.06  ? 124 TRP D NE1   1 
ATOM   14347 C  CE2   . TRP D 2 145 ? 159.520 87.342  133.793 1.00 48.24  ? 124 TRP D CE2   1 
ATOM   14348 C  CE3   . TRP D 2 145 ? 157.194 87.954  133.485 1.00 47.65  ? 124 TRP D CE3   1 
ATOM   14349 C  CZ2   . TRP D 2 145 ? 159.730 88.396  134.699 1.00 47.74  ? 124 TRP D CZ2   1 
ATOM   14350 C  CZ3   . TRP D 2 145 ? 157.402 89.003  134.385 1.00 46.92  ? 124 TRP D CZ3   1 
ATOM   14351 C  CH2   . TRP D 2 145 ? 158.664 89.212  134.979 1.00 47.88  ? 124 TRP D CH2   1 
ATOM   14352 N  N     . VAL D 2 146 ? 154.666 85.672  132.830 1.00 46.09  ? 125 VAL D N     1 
ATOM   14353 C  CA    . VAL D 2 146 ? 153.847 86.410  133.784 1.00 45.36  ? 125 VAL D CA    1 
ATOM   14354 C  C     . VAL D 2 146 ? 153.003 85.443  134.631 1.00 45.28  ? 125 VAL D C     1 
ATOM   14355 O  O     . VAL D 2 146 ? 152.758 85.699  135.815 1.00 45.29  ? 125 VAL D O     1 
ATOM   14356 C  CB    . VAL D 2 146 ? 153.035 87.542  133.074 1.00 45.33  ? 125 VAL D CB    1 
ATOM   14357 C  CG1   . VAL D 2 146 ? 152.072 88.214  134.018 1.00 44.97  ? 125 VAL D CG1   1 
ATOM   14358 C  CG2   . VAL D 2 146 ? 153.992 88.592  132.506 1.00 44.52  ? 125 VAL D CG2   1 
ATOM   14359 N  N     . LYS D 2 147 ? 152.609 84.316  134.038 1.00 44.98  ? 126 LYS D N     1 
ATOM   14360 C  CA    . LYS D 2 147 ? 151.888 83.262  134.765 1.00 44.65  ? 126 LYS D CA    1 
ATOM   14361 C  C     . LYS D 2 147 ? 152.726 82.628  135.887 1.00 44.06  ? 126 LYS D C     1 
ATOM   14362 O  O     . LYS D 2 147 ? 152.181 82.169  136.893 1.00 44.65  ? 126 LYS D O     1 
ATOM   14363 C  CB    . LYS D 2 147 ? 151.399 82.167  133.813 1.00 45.31  ? 126 LYS D CB    1 
ATOM   14364 C  CG    . LYS D 2 147 ? 149.960 81.742  134.063 1.00 46.54  ? 126 LYS D CG    1 
ATOM   14365 C  CD    . LYS D 2 147 ? 149.769 80.226  133.984 1.00 49.06  ? 126 LYS D CD    1 
ATOM   14366 C  CE    . LYS D 2 147 ? 150.032 79.561  135.342 1.00 50.46  ? 126 LYS D CE    1 
ATOM   14367 N  NZ    . LYS D 2 147 ? 149.295 78.271  135.507 1.00 51.33  ? 126 LYS D NZ    1 
ATOM   14368 N  N     . GLN D 2 148 ? 154.044 82.604  135.709 1.00 42.58  ? 127 GLN D N     1 
ATOM   14369 C  CA    . GLN D 2 148 ? 154.959 82.046  136.704 1.00 41.39  ? 127 GLN D CA    1 
ATOM   14370 C  C     . GLN D 2 148 ? 155.508 83.109  137.665 1.00 39.56  ? 127 GLN D C     1 
ATOM   14371 O  O     . GLN D 2 148 ? 156.051 82.772  138.716 1.00 39.77  ? 127 GLN D O     1 
ATOM   14372 C  CB    . GLN D 2 148 ? 156.091 81.277  135.995 1.00 42.11  ? 127 GLN D CB    1 
ATOM   14373 C  CG    . GLN D 2 148 ? 157.466 81.331  136.656 1.00 44.08  ? 127 GLN D CG    1 
ATOM   14374 C  CD    . GLN D 2 148 ? 158.396 82.381  136.045 1.00 46.12  ? 127 GLN D CD    1 
ATOM   14375 O  OE1   . GLN D 2 148 ? 157.982 83.506  135.736 1.00 46.47  ? 127 GLN D OE1   1 
ATOM   14376 N  NE2   . GLN D 2 148 ? 159.668 82.015  135.884 1.00 45.69  ? 127 GLN D NE2   1 
ATOM   14377 N  N     . ASN D 2 149 ? 155.351 84.384  137.301 1.00 36.99  ? 128 ASN D N     1 
ATOM   14378 C  CA    . ASN D 2 149 ? 155.882 85.497  138.088 1.00 34.54  ? 128 ASN D CA    1 
ATOM   14379 C  C     . ASN D 2 149 ? 155.343 85.568  139.519 1.00 33.13  ? 128 ASN D C     1 
ATOM   14380 O  O     . ASN D 2 149 ? 154.135 85.603  139.739 1.00 32.62  ? 128 ASN D O     1 
ATOM   14381 C  CB    . ASN D 2 149 ? 155.637 86.829  137.376 1.00 34.24  ? 128 ASN D CB    1 
ATOM   14382 C  CG    . ASN D 2 149 ? 156.276 87.995  138.103 1.00 33.83  ? 128 ASN D CG    1 
ATOM   14383 O  OD1   . ASN D 2 149 ? 155.606 88.731  138.830 1.00 32.21  ? 128 ASN D OD1   1 
ATOM   14384 N  ND2   . ASN D 2 149 ? 157.587 88.148  137.936 1.00 33.26  ? 128 ASN D ND2   1 
ATOM   14385 N  N     . LYS D 2 150 ? 156.260 85.621  140.482 1.00 31.49  ? 129 LYS D N     1 
ATOM   14386 C  CA    . LYS D 2 150 ? 155.929 85.566  141.903 1.00 30.68  ? 129 LYS D CA    1 
ATOM   14387 C  C     . LYS D 2 150 ? 155.020 86.718  142.396 1.00 28.95  ? 129 LYS D C     1 
ATOM   14388 O  O     . LYS D 2 150 ? 154.095 86.492  143.184 1.00 27.90  ? 129 LYS D O     1 
ATOM   14389 C  CB    . LYS D 2 150 ? 157.238 85.487  142.704 1.00 31.17  ? 129 LYS D CB    1 
ATOM   14390 C  CG    . LYS D 2 150 ? 157.165 85.771  144.191 1.00 33.66  ? 129 LYS D CG    1 
ATOM   14391 C  CD    . LYS D 2 150 ? 158.574 85.671  144.797 1.00 38.08  ? 129 LYS D CD    1 
ATOM   14392 C  CE    . LYS D 2 150 ? 158.718 86.514  146.069 1.00 40.20  ? 129 LYS D CE    1 
ATOM   14393 N  NZ    . LYS D 2 150 ? 158.415 85.739  147.303 1.00 42.60  ? 129 LYS D NZ    1 
ATOM   14394 N  N     . TYR D 2 151 ? 155.287 87.940  141.938 1.00 27.36  ? 130 TYR D N     1 
ATOM   14395 C  CA    . TYR D 2 151 ? 154.555 89.120  142.434 1.00 26.56  ? 130 TYR D CA    1 
ATOM   14396 C  C     . TYR D 2 151 ? 153.172 89.245  141.815 1.00 25.66  ? 130 TYR D C     1 
ATOM   14397 O  O     . TYR D 2 151 ? 152.225 89.632  142.506 1.00 25.61  ? 130 TYR D O     1 
ATOM   14398 C  CB    . TYR D 2 151 ? 155.379 90.412  142.264 1.00 26.32  ? 130 TYR D CB    1 
ATOM   14399 C  CG    . TYR D 2 151 ? 156.817 90.227  142.711 1.00 27.20  ? 130 TYR D CG    1 
ATOM   14400 C  CD1   . TYR D 2 151 ? 157.126 90.071  144.062 1.00 27.31  ? 130 TYR D CD1   1 
ATOM   14401 C  CD2   . TYR D 2 151 ? 157.855 90.151  141.783 1.00 27.22  ? 130 TYR D CD2   1 
ATOM   14402 C  CE1   . TYR D 2 151 ? 158.439 89.867  144.482 1.00 29.65  ? 130 TYR D CE1   1 
ATOM   14403 C  CE2   . TYR D 2 151 ? 159.181 89.946  142.195 1.00 28.75  ? 130 TYR D CE2   1 
ATOM   14404 C  CZ    . TYR D 2 151 ? 159.454 89.815  143.560 1.00 29.17  ? 130 TYR D CZ    1 
ATOM   14405 O  OH    . TYR D 2 151 ? 160.739 89.613  144.011 1.00 30.61  ? 130 TYR D OH    1 
ATOM   14406 N  N     . LEU D 2 152 ? 153.060 88.917  140.526 1.00 24.87  ? 131 LEU D N     1 
ATOM   14407 C  CA    . LEU D 2 152 ? 151.756 88.863  139.873 1.00 24.37  ? 131 LEU D CA    1 
ATOM   14408 C  C     . LEU D 2 152 ? 150.888 87.770  140.509 1.00 24.18  ? 131 LEU D C     1 
ATOM   14409 O  O     . LEU D 2 152 ? 149.751 88.035  140.899 1.00 23.16  ? 131 LEU D O     1 
ATOM   14410 C  CB    . LEU D 2 152 ? 151.857 88.655  138.358 1.00 24.45  ? 131 LEU D CB    1 
ATOM   14411 C  CG    . LEU D 2 152 ? 150.409 88.674  137.834 1.00 26.33  ? 131 LEU D CG    1 
ATOM   14412 C  CD1   . LEU D 2 152 ? 149.848 90.102  137.825 1.00 25.00  ? 131 LEU D CD1   1 
ATOM   14413 C  CD2   . LEU D 2 152 ? 150.227 87.992  136.509 1.00 29.15  ? 131 LEU D CD2   1 
ATOM   14414 N  N     . GLN D 2 153 ? 151.438 86.561  140.640 1.00 24.07  ? 132 GLN D N     1 
ATOM   14415 C  CA    . GLN D 2 153 ? 150.708 85.458  141.299 1.00 24.99  ? 132 GLN D CA    1 
ATOM   14416 C  C     . GLN D 2 153 ? 150.284 85.773  142.731 1.00 24.24  ? 132 GLN D C     1 
ATOM   14417 O  O     . GLN D 2 153 ? 149.138 85.496  143.127 1.00 23.75  ? 132 GLN D O     1 
ATOM   14418 C  CB    . GLN D 2 153 ? 151.493 84.137  141.237 1.00 25.84  ? 132 GLN D CB    1 
ATOM   14419 C  CG    . GLN D 2 153 ? 151.555 83.519  139.814 1.00 28.48  ? 132 GLN D CG    1 
ATOM   14420 C  CD    . GLN D 2 153 ? 150.177 83.172  139.229 1.00 30.95  ? 132 GLN D CD    1 
ATOM   14421 O  OE1   . GLN D 2 153 ? 149.277 82.750  139.945 1.00 31.78  ? 132 GLN D OE1   1 
ATOM   14422 N  NE2   . GLN D 2 153 ? 150.023 83.341  137.914 1.00 32.81  ? 132 GLN D NE2   1 
ATOM   14423 N  N     . LYS D 2 154 ? 151.184 86.360  143.516 1.00 24.00  ? 133 LYS D N     1 
ATOM   14424 C  CA    . LYS D 2 154 ? 150.827 86.664  144.902 1.00 24.43  ? 133 LYS D CA    1 
ATOM   14425 C  C     . LYS D 2 154 ? 149.537 87.495  144.976 1.00 23.40  ? 133 LYS D C     1 
ATOM   14426 O  O     . LYS D 2 154 ? 148.589 87.115  145.667 1.00 22.68  ? 133 LYS D O     1 
ATOM   14427 C  CB    . LYS D 2 154 ? 151.949 87.377  145.664 1.00 24.64  ? 133 LYS D CB    1 
ATOM   14428 C  CG    . LYS D 2 154 ? 151.542 87.641  147.125 1.00 28.01  ? 133 LYS D CG    1 
ATOM   14429 C  CD    . LYS D 2 154 ? 152.654 88.182  147.992 1.00 32.56  ? 133 LYS D CD    1 
ATOM   14430 C  CE    . LYS D 2 154 ? 153.710 87.135  148.252 1.00 34.45  ? 133 LYS D CE    1 
ATOM   14431 N  NZ    . LYS D 2 154 ? 154.806 87.695  149.103 1.00 36.11  ? 133 LYS D NZ    1 
ATOM   14432 N  N     . LYS D 2 155 ? 149.501 88.620  144.263 1.00 23.07  ? 134 LYS D N     1 
ATOM   14433 C  CA    . LYS D 2 155 ? 148.306 89.460  144.289 1.00 22.70  ? 134 LYS D CA    1 
ATOM   14434 C  C     . LYS D 2 155 ? 147.102 88.785  143.633 1.00 21.96  ? 134 LYS D C     1 
ATOM   14435 O  O     . LYS D 2 155 ? 146.005 88.851  144.177 1.00 22.25  ? 134 LYS D O     1 
ATOM   14436 C  CB    . LYS D 2 155 ? 148.563 90.871  143.729 1.00 22.70  ? 134 LYS D CB    1 
ATOM   14437 C  CG    . LYS D 2 155 ? 148.921 90.965  142.260 1.00 23.62  ? 134 LYS D CG    1 
ATOM   14438 C  CD    . LYS D 2 155 ? 149.061 92.435  141.871 1.00 25.32  ? 134 LYS D CD    1 
ATOM   14439 C  CE    . LYS D 2 155 ? 150.148 92.609  140.815 1.00 27.09  ? 134 LYS D CE    1 
ATOM   14440 N  NZ    . LYS D 2 155 ? 150.235 94.035  140.382 1.00 26.65  ? 134 LYS D NZ    1 
ATOM   14441 N  N     . ALA D 2 156 ? 147.291 88.113  142.497 1.00 21.76  ? 135 ALA D N     1 
ATOM   14442 C  CA    . ALA D 2 156 ? 146.151 87.454  141.833 1.00 21.83  ? 135 ALA D CA    1 
ATOM   14443 C  C     . ALA D 2 156 ? 145.484 86.430  142.767 1.00 22.30  ? 135 ALA D C     1 
ATOM   14444 O  O     . ALA D 2 156 ? 144.257 86.416  142.911 1.00 21.92  ? 135 ALA D O     1 
ATOM   14445 C  CB    . ALA D 2 156 ? 146.578 86.788  140.514 1.00 22.30  ? 135 ALA D CB    1 
ATOM   14446 N  N     . GLN D 2 157 ? 146.294 85.596  143.422 1.00 22.15  ? 136 GLN D N     1 
ATOM   14447 C  CA    . GLN D 2 157 ? 145.749 84.559  144.305 1.00 22.38  ? 136 GLN D CA    1 
ATOM   14448 C  C     . GLN D 2 157 ? 145.173 85.103  145.619 1.00 21.59  ? 136 GLN D C     1 
ATOM   14449 O  O     . GLN D 2 157 ? 144.225 84.534  146.160 1.00 21.44  ? 136 GLN D O     1 
ATOM   14450 C  CB    . GLN D 2 157 ? 146.776 83.445  144.576 1.00 22.94  ? 136 GLN D CB    1 
ATOM   14451 C  CG    . GLN D 2 157 ? 147.304 82.729  143.322 1.00 25.31  ? 136 GLN D CG    1 
ATOM   14452 C  CD    . GLN D 2 157 ? 146.210 82.341  142.323 1.00 28.02  ? 136 GLN D CD    1 
ATOM   14453 O  OE1   . GLN D 2 157 ? 145.114 81.914  142.699 1.00 27.14  ? 136 GLN D OE1   1 
ATOM   14454 N  NE2   . GLN D 2 157 ? 146.519 82.483  141.035 1.00 29.47  ? 136 GLN D NE2   1 
ATOM   14455 N  N     . MET D 2 158 ? 145.740 86.187  146.136 1.00 21.52  ? 137 MET D N     1 
ATOM   14456 C  CA    . MET D 2 158 ? 145.172 86.844  147.327 1.00 22.20  ? 137 MET D CA    1 
ATOM   14457 C  C     . MET D 2 158 ? 143.735 87.321  147.084 1.00 21.84  ? 137 MET D C     1 
ATOM   14458 O  O     . MET D 2 158 ? 142.854 87.119  147.923 1.00 21.91  ? 137 MET D O     1 
ATOM   14459 C  CB    . MET D 2 158 ? 146.036 88.020  147.782 1.00 22.52  ? 137 MET D CB    1 
ATOM   14460 C  CG    . MET D 2 158 ? 147.304 87.601  148.540 1.00 25.81  ? 137 MET D CG    1 
ATOM   14461 S  SD    . MET D 2 158 ? 148.326 89.004  149.067 1.00 31.19  ? 137 MET D SD    1 
ATOM   14462 C  CE    . MET D 2 158 ? 147.172 89.769  150.175 1.00 23.91  ? 137 MET D CE    1 
ATOM   14463 N  N     . ILE D 2 159 ? 143.516 87.949  145.931 1.00 21.41  ? 138 ILE D N     1 
ATOM   14464 C  CA    . ILE D 2 159 ? 142.205 88.471  145.559 1.00 21.51  ? 138 ILE D CA    1 
ATOM   14465 C  C     . ILE D 2 159 ? 141.211 87.318  145.341 1.00 21.77  ? 138 ILE D C     1 
ATOM   14466 O  O     . ILE D 2 159 ? 140.101 87.332  145.896 1.00 21.44  ? 138 ILE D O     1 
ATOM   14467 C  CB    . ILE D 2 159 ? 142.319 89.417  144.301 1.00 21.49  ? 138 ILE D CB    1 
ATOM   14468 C  CG1   . ILE D 2 159 ? 143.195 90.643  144.604 1.00 21.16  ? 138 ILE D CG1   1 
ATOM   14469 C  CG2   . ILE D 2 159 ? 140.944 89.845  143.775 1.00 22.34  ? 138 ILE D CG2   1 
ATOM   14470 C  CD1   . ILE D 2 159 ? 142.659 91.571  145.715 1.00 23.85  ? 138 ILE D CD1   1 
ATOM   14471 N  N     . VAL D 2 160 ? 141.629 86.326  144.546 1.00 21.96  ? 139 VAL D N     1 
ATOM   14472 C  CA    . VAL D 2 160 ? 140.810 85.152  144.208 1.00 22.59  ? 139 VAL D CA    1 
ATOM   14473 C  C     . VAL D 2 160 ? 140.445 84.359  145.472 1.00 22.36  ? 139 VAL D C     1 
ATOM   14474 O  O     . VAL D 2 160 ? 139.325 83.850  145.587 1.00 21.64  ? 139 VAL D O     1 
ATOM   14475 C  CB    . VAL D 2 160 ? 141.528 84.241  143.156 1.00 23.08  ? 139 VAL D CB    1 
ATOM   14476 C  CG1   . VAL D 2 160 ? 140.897 82.838  143.066 1.00 24.33  ? 139 VAL D CG1   1 
ATOM   14477 C  CG2   . VAL D 2 160 ? 141.528 84.911  141.772 1.00 22.87  ? 139 VAL D CG2   1 
ATOM   14478 N  N     . GLY D 2 161 ? 141.390 84.269  146.411 1.00 22.21  ? 140 GLY D N     1 
ATOM   14479 C  CA    . GLY D 2 161 ? 141.149 83.609  147.692 1.00 22.50  ? 140 GLY D CA    1 
ATOM   14480 C  C     . GLY D 2 161 ? 139.965 84.210  148.443 1.00 22.88  ? 140 GLY D C     1 
ATOM   14481 O  O     . GLY D 2 161 ? 139.127 83.477  148.986 1.00 23.54  ? 140 GLY D O     1 
ATOM   14482 N  N     . LEU D 2 162 ? 139.884 85.540  148.468 1.00 22.25  ? 141 LEU D N     1 
ATOM   14483 C  CA    . LEU D 2 162 ? 138.765 86.218  149.130 1.00 22.48  ? 141 LEU D CA    1 
ATOM   14484 C  C     . LEU D 2 162 ? 137.429 86.023  148.409 1.00 22.27  ? 141 LEU D C     1 
ATOM   14485 O  O     . LEU D 2 162 ? 136.391 85.916  149.064 1.00 22.31  ? 141 LEU D O     1 
ATOM   14486 C  CB    . LEU D 2 162 ? 139.069 87.706  149.394 1.00 22.07  ? 141 LEU D CB    1 
ATOM   14487 C  CG    . LEU D 2 162 ? 140.060 87.948  150.553 1.00 22.81  ? 141 LEU D CG    1 
ATOM   14488 C  CD1   . LEU D 2 162 ? 140.725 89.320  150.466 1.00 21.65  ? 141 LEU D CD1   1 
ATOM   14489 C  CD2   . LEU D 2 162 ? 139.434 87.710  151.932 1.00 23.35  ? 141 LEU D CD2   1 
ATOM   14490 N  N     . TYR D 2 163 ? 137.447 85.978  147.075 1.00 22.63  ? 142 TYR D N     1 
ATOM   14491 C  CA    . TYR D 2 163 ? 136.227 85.656  146.307 1.00 23.30  ? 142 TYR D CA    1 
ATOM   14492 C  C     . TYR D 2 163 ? 135.740 84.239  146.582 1.00 23.40  ? 142 TYR D C     1 
ATOM   14493 O  O     . TYR D 2 163 ? 134.545 84.006  146.689 1.00 23.75  ? 142 TYR D O     1 
ATOM   14494 C  CB    . TYR D 2 163 ? 136.451 85.767  144.805 1.00 23.22  ? 142 TYR D CB    1 
ATOM   14495 C  CG    . TYR D 2 163 ? 136.832 87.128  144.290 1.00 24.01  ? 142 TYR D CG    1 
ATOM   14496 C  CD1   . TYR D 2 163 ? 136.527 88.280  145.004 1.00 24.47  ? 142 TYR D CD1   1 
ATOM   14497 C  CD2   . TYR D 2 163 ? 137.494 87.256  143.073 1.00 24.62  ? 142 TYR D CD2   1 
ATOM   14498 C  CE1   . TYR D 2 163 ? 136.876 89.527  144.526 1.00 26.33  ? 142 TYR D CE1   1 
ATOM   14499 C  CE2   . TYR D 2 163 ? 137.839 88.503  142.577 1.00 26.07  ? 142 TYR D CE2   1 
ATOM   14500 C  CZ    . TYR D 2 163 ? 137.520 89.635  143.315 1.00 26.65  ? 142 TYR D CZ    1 
ATOM   14501 O  OH    . TYR D 2 163 ? 137.863 90.883  142.848 1.00 31.13  ? 142 TYR D OH    1 
ATOM   14502 N  N     . LYS D 2 164 ? 136.667 83.296  146.684 1.00 23.70  ? 143 LYS D N     1 
ATOM   14503 C  CA    . LYS D 2 164 ? 136.315 81.896  146.969 1.00 24.47  ? 143 LYS D CA    1 
ATOM   14504 C  C     . LYS D 2 164 ? 135.798 81.670  148.399 1.00 24.55  ? 143 LYS D C     1 
ATOM   14505 O  O     . LYS D 2 164 ? 135.169 80.649  148.684 1.00 24.49  ? 143 LYS D O     1 
ATOM   14506 C  CB    . LYS D 2 164 ? 137.517 80.990  146.697 1.00 24.98  ? 143 LYS D CB    1 
ATOM   14507 C  CG    . LYS D 2 164 ? 137.808 80.740  145.209 1.00 27.10  ? 143 LYS D CG    1 
ATOM   14508 C  CD    . LYS D 2 164 ? 138.941 79.733  145.069 1.00 30.75  ? 143 LYS D CD    1 
ATOM   14509 C  CE    . LYS D 2 164 ? 139.219 79.355  143.615 1.00 32.81  ? 143 LYS D CE    1 
ATOM   14510 N  NZ    . LYS D 2 164 ? 140.420 78.435  143.488 1.00 33.68  ? 143 LYS D NZ    1 
ATOM   14511 N  N     . ALA D 2 165 ? 136.075 82.613  149.295 1.00 24.18  ? 144 ALA D N     1 
ATOM   14512 C  CA    . ALA D 2 165 ? 135.698 82.478  150.705 1.00 25.04  ? 144 ALA D CA    1 
ATOM   14513 C  C     . ALA D 2 165 ? 134.324 83.067  151.057 1.00 25.00  ? 144 ALA D C     1 
ATOM   14514 O  O     . ALA D 2 165 ? 133.893 82.976  152.216 1.00 25.50  ? 144 ALA D O     1 
ATOM   14515 C  CB    . ALA D 2 165 ? 136.785 83.076  151.614 1.00 25.02  ? 144 ALA D CB    1 
ATOM   14516 N  N     . ILE D 2 166 ? 133.641 83.669  150.081 1.00 24.60  ? 145 ILE D N     1 
ATOM   14517 C  CA    . ILE D 2 166 ? 132.293 84.188  150.313 1.00 24.40  ? 145 ILE D CA    1 
ATOM   14518 C  C     . ILE D 2 166 ? 131.353 83.024  150.656 1.00 25.75  ? 145 ILE D C     1 
ATOM   14519 O  O     . ILE D 2 166 ? 131.358 81.988  149.982 1.00 25.84  ? 145 ILE D O     1 
ATOM   14520 C  CB    . ILE D 2 166 ? 131.714 84.959  149.092 1.00 24.15  ? 145 ILE D CB    1 
ATOM   14521 C  CG1   . ILE D 2 166 ? 132.696 86.017  148.591 1.00 23.15  ? 145 ILE D CG1   1 
ATOM   14522 C  CG2   . ILE D 2 166 ? 130.378 85.607  149.456 1.00 22.72  ? 145 ILE D CG2   1 
ATOM   14523 C  CD1   . ILE D 2 166 ? 132.301 86.643  147.270 1.00 21.70  ? 145 ILE D CD1   1 
ATOM   14524 N  N     . GLN D 2 167 ? 130.582 83.190  151.723 1.00 26.52  ? 146 GLN D N     1 
ATOM   14525 C  CA    . GLN D 2 167 ? 129.603 82.187  152.122 1.00 28.77  ? 146 GLN D CA    1 
ATOM   14526 C  C     . GLN D 2 167 ? 128.188 82.719  151.942 1.00 29.20  ? 146 GLN D C     1 
ATOM   14527 O  O     . GLN D 2 167 ? 127.916 83.898  152.212 1.00 28.89  ? 146 GLN D O     1 
ATOM   14528 C  CB    . GLN D 2 167 ? 129.829 81.776  153.574 1.00 29.04  ? 146 GLN D CB    1 
ATOM   14529 C  CG    . GLN D 2 167 ? 131.152 81.069  153.798 1.00 31.87  ? 146 GLN D CG    1 
ATOM   14530 C  CD    . GLN D 2 167 ? 131.850 81.558  155.039 1.00 35.35  ? 146 GLN D CD    1 
ATOM   14531 O  OE1   . GLN D 2 167 ? 131.394 81.316  156.159 1.00 36.91  ? 146 GLN D OE1   1 
ATOM   14532 N  NE2   . GLN D 2 167 ? 132.971 82.253  154.851 1.00 36.19  ? 146 GLN D NE2   1 
ATOM   14533 N  N     . LYS D 2 168 ? 127.290 81.847  151.488 1.00 30.29  ? 147 LYS D N     1 
ATOM   14534 C  CA    . LYS D 2 168 ? 125.883 82.207  151.330 1.00 31.24  ? 147 LYS D CA    1 
ATOM   14535 C  C     . LYS D 2 168 ? 125.324 82.837  152.606 1.00 31.73  ? 147 LYS D C     1 
ATOM   14536 O  O     . LYS D 2 168 ? 125.591 82.350  153.705 1.00 31.46  ? 147 LYS D O     1 
ATOM   14537 C  CB    . LYS D 2 168 ? 125.058 80.987  150.929 1.00 31.92  ? 147 LYS D CB    1 
ATOM   14538 C  CG    . LYS D 2 168 ? 123.594 81.305  150.662 1.00 33.23  ? 147 LYS D CG    1 
ATOM   14539 C  CD    . LYS D 2 168 ? 122.867 80.125  150.038 1.00 36.06  ? 147 LYS D CD    1 
ATOM   14540 C  CE    . LYS D 2 168 ? 121.396 80.426  149.844 1.00 35.46  ? 147 LYS D CE    1 
ATOM   14541 N  NZ    . LYS D 2 168 ? 121.163 81.420  148.763 1.00 38.24  ? 147 LYS D NZ    1 
ATOM   14542 N  N     . ASP D 2 169 ? 124.574 83.930  152.446 1.00 32.28  ? 148 ASP D N     1 
ATOM   14543 C  CA    . ASP D 2 169 ? 123.954 84.659  153.567 1.00 33.45  ? 148 ASP D CA    1 
ATOM   14544 C  C     . ASP D 2 169 ? 124.914 85.148  154.651 1.00 33.30  ? 148 ASP D C     1 
ATOM   14545 O  O     . ASP D 2 169 ? 124.508 85.349  155.798 1.00 34.32  ? 148 ASP D O     1 
ATOM   14546 C  CB    . ASP D 2 169 ? 122.856 83.814  154.234 1.00 34.63  ? 148 ASP D CB    1 
ATOM   14547 C  CG    . ASP D 2 169 ? 121.604 83.696  153.391 1.00 36.09  ? 148 ASP D CG    1 
ATOM   14548 O  OD1   . ASP D 2 169 ? 121.445 84.441  152.401 1.00 37.80  ? 148 ASP D OD1   1 
ATOM   14549 O  OD2   . ASP D 2 169 ? 120.765 82.840  153.741 1.00 40.47  ? 148 ASP D OD2   1 
ATOM   14550 N  N     . ASP D 2 170 ? 126.183 85.319  154.314 1.00 32.58  ? 149 ASP D N     1 
ATOM   14551 C  CA    . ASP D 2 170 ? 127.127 85.899  155.267 1.00 32.01  ? 149 ASP D CA    1 
ATOM   14552 C  C     . ASP D 2 170 ? 127.678 87.196  154.687 1.00 30.59  ? 149 ASP D C     1 
ATOM   14553 O  O     . ASP D 2 170 ? 128.532 87.181  153.800 1.00 29.11  ? 149 ASP D O     1 
ATOM   14554 C  CB    . ASP D 2 170 ? 128.240 84.910  155.622 1.00 32.93  ? 149 ASP D CB    1 
ATOM   14555 C  CG    . ASP D 2 170 ? 129.373 85.549  156.413 1.00 35.05  ? 149 ASP D CG    1 
ATOM   14556 O  OD1   . ASP D 2 170 ? 129.151 86.526  157.162 1.00 39.25  ? 149 ASP D OD1   1 
ATOM   14557 O  OD2   . ASP D 2 170 ? 130.503 85.056  156.300 1.00 39.22  ? 149 ASP D OD2   1 
ATOM   14558 N  N     . GLU D 2 171 ? 127.162 88.311  155.198 1.00 29.34  ? 150 GLU D N     1 
ATOM   14559 C  CA    . GLU D 2 171 ? 127.506 89.634  154.686 1.00 28.51  ? 150 GLU D CA    1 
ATOM   14560 C  C     . GLU D 2 171 ? 128.932 90.075  155.040 1.00 27.27  ? 150 GLU D C     1 
ATOM   14561 O  O     . GLU D 2 171 ? 129.496 90.919  154.361 1.00 26.62  ? 150 GLU D O     1 
ATOM   14562 C  CB    . GLU D 2 171 ? 126.471 90.673  155.136 1.00 29.09  ? 150 GLU D CB    1 
ATOM   14563 C  CG    . GLU D 2 171 ? 126.477 91.002  156.628 1.00 30.68  ? 150 GLU D CG    1 
ATOM   14564 C  CD    . GLU D 2 171 ? 125.315 91.896  157.031 1.00 33.92  ? 150 GLU D CD    1 
ATOM   14565 O  OE1   . GLU D 2 171 ? 124.527 92.295  156.138 1.00 36.31  ? 150 GLU D OE1   1 
ATOM   14566 O  OE2   . GLU D 2 171 ? 125.182 92.212  158.234 1.00 34.02  ? 150 GLU D OE2   1 
ATOM   14567 N  N     . ILE D 2 172 ? 129.517 89.487  156.083 1.00 26.19  ? 151 ILE D N     1 
ATOM   14568 C  CA    . ILE D 2 172 ? 130.898 89.794  156.456 1.00 25.49  ? 151 ILE D CA    1 
ATOM   14569 C  C     . ILE D 2 172 ? 131.870 89.286  155.387 1.00 24.61  ? 151 ILE D C     1 
ATOM   14570 O  O     . ILE D 2 172 ? 132.753 90.026  154.937 1.00 24.09  ? 151 ILE D O     1 
ATOM   14571 C  CB    . ILE D 2 172 ? 131.261 89.244  157.864 1.00 25.98  ? 151 ILE D CB    1 
ATOM   14572 C  CG1   . ILE D 2 172 ? 130.408 89.911  158.945 1.00 26.86  ? 151 ILE D CG1   1 
ATOM   14573 C  CG2   . ILE D 2 172 ? 132.771 89.401  158.187 1.00 26.50  ? 151 ILE D CG2   1 
ATOM   14574 C  CD1   . ILE D 2 172 ? 130.579 91.420  159.037 1.00 27.81  ? 151 ILE D CD1   1 
ATOM   14575 N  N     . SER D 2 173 ? 131.684 88.037  154.970 1.00 23.71  ? 152 SER D N     1 
ATOM   14576 C  CA    . SER D 2 173 ? 132.519 87.443  153.927 1.00 23.38  ? 152 SER D CA    1 
ATOM   14577 C  C     . SER D 2 173 ? 132.297 88.144  152.575 1.00 22.41  ? 152 SER D C     1 
ATOM   14578 O  O     . SER D 2 173 ? 133.227 88.292  151.777 1.00 21.43  ? 152 SER D O     1 
ATOM   14579 C  CB    . SER D 2 173 ? 132.282 85.930  153.825 1.00 23.90  ? 152 SER D CB    1 
ATOM   14580 O  OG    . SER D 2 173 ? 131.006 85.595  153.283 1.00 23.74  ? 152 SER D OG    1 
ATOM   14581 N  N     . LEU D 2 174 ? 131.068 88.591  152.334 1.00 21.63  ? 153 LEU D N     1 
ATOM   14582 C  CA    . LEU D 2 174 ? 130.775 89.351  151.116 1.00 20.75  ? 153 LEU D CA    1 
ATOM   14583 C  C     . LEU D 2 174 ? 131.522 90.684  151.143 1.00 20.96  ? 153 LEU D C     1 
ATOM   14584 O  O     . LEU D 2 174 ? 132.123 91.081  150.145 1.00 20.41  ? 153 LEU D O     1 
ATOM   14585 C  CB    . LEU D 2 174 ? 129.259 89.578  150.947 1.00 20.62  ? 153 LEU D CB    1 
ATOM   14586 C  CG    . LEU D 2 174 ? 128.817 90.403  149.719 1.00 19.55  ? 153 LEU D CG    1 
ATOM   14587 C  CD1   . LEU D 2 174 ? 129.401 89.820  148.427 1.00 20.44  ? 153 LEU D CD1   1 
ATOM   14588 C  CD2   . LEU D 2 174 ? 127.284 90.471  149.656 1.00 20.99  ? 153 LEU D CD2   1 
ATOM   14589 N  N     . PHE D 2 175 ? 131.486 91.365  152.287 1.00 21.07  ? 154 PHE D N     1 
ATOM   14590 C  CA    . PHE D 2 175 ? 132.179 92.643  152.438 1.00 21.32  ? 154 PHE D CA    1 
ATOM   14591 C  C     . PHE D 2 175 ? 133.681 92.503  152.165 1.00 21.08  ? 154 PHE D C     1 
ATOM   14592 O  O     . PHE D 2 175 ? 134.272 93.321  151.458 1.00 20.85  ? 154 PHE D O     1 
ATOM   14593 C  CB    . PHE D 2 175 ? 131.949 93.216  153.841 1.00 21.20  ? 154 PHE D CB    1 
ATOM   14594 C  CG    . PHE D 2 175 ? 132.835 94.380  154.173 1.00 22.46  ? 154 PHE D CG    1 
ATOM   14595 C  CD1   . PHE D 2 175 ? 134.085 94.182  154.766 1.00 21.21  ? 154 PHE D CD1   1 
ATOM   14596 C  CD2   . PHE D 2 175 ? 132.419 95.683  153.903 1.00 22.53  ? 154 PHE D CD2   1 
ATOM   14597 C  CE1   . PHE D 2 175 ? 134.909 95.263  155.068 1.00 22.11  ? 154 PHE D CE1   1 
ATOM   14598 C  CE2   . PHE D 2 175 ? 133.222 96.762  154.215 1.00 23.26  ? 154 PHE D CE2   1 
ATOM   14599 C  CZ    . PHE D 2 175 ? 134.476 96.557  154.798 1.00 22.08  ? 154 PHE D CZ    1 
ATOM   14600 N  N     . LYS D 2 176 ? 134.291 91.472  152.740 1.00 21.14  ? 155 LYS D N     1 
ATOM   14601 C  CA    . LYS D 2 176 ? 135.720 91.210  152.541 1.00 20.93  ? 155 LYS D CA    1 
ATOM   14602 C  C     . LYS D 2 176 ? 136.073 91.021  151.068 1.00 20.61  ? 155 LYS D C     1 
ATOM   14603 O  O     . LYS D 2 176 ? 137.084 91.545  150.587 1.00 20.62  ? 155 LYS D O     1 
ATOM   14604 C  CB    . LYS D 2 176 ? 136.142 89.997  153.356 1.00 21.27  ? 155 LYS D CB    1 
ATOM   14605 C  CG    . LYS D 2 176 ? 136.205 90.303  154.827 1.00 22.04  ? 155 LYS D CG    1 
ATOM   14606 C  CD    . LYS D 2 176 ? 136.523 89.077  155.667 1.00 25.24  ? 155 LYS D CD    1 
ATOM   14607 C  CE    . LYS D 2 176 ? 136.630 89.485  157.114 1.00 25.83  ? 155 LYS D CE    1 
ATOM   14608 N  NZ    . LYS D 2 176 ? 136.960 88.344  158.018 1.00 26.64  ? 155 LYS D NZ    1 
ATOM   14609 N  N     . ALA D 2 177 ? 135.220 90.294  150.353 1.00 20.02  ? 156 ALA D N     1 
ATOM   14610 C  CA    . ALA D 2 177 ? 135.381 90.122  148.911 1.00 19.86  ? 156 ALA D CA    1 
ATOM   14611 C  C     . ALA D 2 177 ? 135.203 91.443  148.148 1.00 19.61  ? 156 ALA D C     1 
ATOM   14612 O  O     . ALA D 2 177 ? 135.869 91.685  147.139 1.00 19.69  ? 156 ALA D O     1 
ATOM   14613 C  CB    . ALA D 2 177 ? 134.405 89.103  148.422 1.00 19.99  ? 156 ALA D CB    1 
ATOM   14614 N  N     . MET D 2 178 ? 134.294 92.291  148.624 1.00 19.75  ? 157 MET D N     1 
ATOM   14615 C  CA    . MET D 2 178 ? 134.048 93.594  147.971 1.00 18.89  ? 157 MET D CA    1 
ATOM   14616 C  C     . MET D 2 178 ? 135.255 94.503  148.142 1.00 18.62  ? 157 MET D C     1 
ATOM   14617 O  O     . MET D 2 178 ? 135.635 95.225  147.212 1.00 18.10  ? 157 MET D O     1 
ATOM   14618 C  CB    . MET D 2 178 ? 132.798 94.261  148.538 1.00 18.82  ? 157 MET D CB    1 
ATOM   14619 C  CG    . MET D 2 178 ? 131.506 93.625  148.053 1.00 20.20  ? 157 MET D CG    1 
ATOM   14620 S  SD    . MET D 2 178 ? 130.097 94.372  148.884 1.00 23.78  ? 157 MET D SD    1 
ATOM   14621 C  CE    . MET D 2 178 ? 128.759 93.631  147.952 1.00 22.62  ? 157 MET D CE    1 
ATOM   14622 N  N     . VAL D 2 179 ? 135.865 94.441  149.327 1.00 18.34  ? 158 VAL D N     1 
ATOM   14623 C  CA    . VAL D 2 179 ? 137.099 95.161  149.601 1.00 18.75  ? 158 VAL D CA    1 
ATOM   14624 C  C     . VAL D 2 179 ? 138.195 94.718  148.640 1.00 18.86  ? 158 VAL D C     1 
ATOM   14625 O  O     . VAL D 2 179 ? 138.890 95.567  148.057 1.00 18.79  ? 158 VAL D O     1 
ATOM   14626 C  CB    . VAL D 2 179 ? 137.581 94.988  151.066 1.00 19.02  ? 158 VAL D CB    1 
ATOM   14627 C  CG1   . VAL D 2 179 ? 138.990 95.576  151.233 1.00 19.10  ? 158 VAL D CG1   1 
ATOM   14628 C  CG2   . VAL D 2 179 ? 136.594 95.641  152.045 1.00 18.94  ? 158 VAL D CG2   1 
ATOM   14629 N  N     . ALA D 2 180 ? 138.349 93.396  148.491 1.00 18.96  ? 159 ALA D N     1 
ATOM   14630 C  CA    . ALA D 2 180 ? 139.289 92.826  147.524 1.00 19.05  ? 159 ALA D CA    1 
ATOM   14631 C  C     . ALA D 2 180 ? 138.997 93.331  146.108 1.00 18.67  ? 159 ALA D C     1 
ATOM   14632 O  O     . ALA D 2 180 ? 139.917 93.739  145.387 1.00 17.72  ? 159 ALA D O     1 
ATOM   14633 C  CB    . ALA D 2 180 ? 139.259 91.288  147.570 1.00 19.43  ? 159 ALA D CB    1 
ATOM   14634 N  N     . SER D 2 181 ? 137.715 93.332  145.733 1.00 18.49  ? 160 SER D N     1 
ATOM   14635 C  CA    . SER D 2 181 ? 137.311 93.807  144.408 1.00 18.51  ? 160 SER D CA    1 
ATOM   14636 C  C     . SER D 2 181 ? 137.642 95.283  144.189 1.00 18.23  ? 160 SER D C     1 
ATOM   14637 O  O     . SER D 2 181 ? 138.191 95.652  143.160 1.00 18.18  ? 160 SER D O     1 
ATOM   14638 C  CB    . SER D 2 181 ? 135.818 93.570  144.164 1.00 18.51  ? 160 SER D CB    1 
ATOM   14639 O  OG    . SER D 2 181 ? 135.509 93.883  142.820 1.00 19.42  ? 160 SER D OG    1 
ATOM   14640 N  N     . VAL D 2 182 ? 137.312 96.124  145.168 1.00 18.43  ? 161 VAL D N     1 
ATOM   14641 C  CA    . VAL D 2 182 ? 137.659 97.547  145.089 1.00 18.09  ? 161 VAL D CA    1 
ATOM   14642 C  C     . VAL D 2 182 ? 139.176 97.743  144.995 1.00 18.41  ? 161 VAL D C     1 
ATOM   14643 O  O     . VAL D 2 182 ? 139.650 98.557  144.200 1.00 18.52  ? 161 VAL D O     1 
ATOM   14644 C  CB    . VAL D 2 182 ? 137.065 98.348  146.255 1.00 17.71  ? 161 VAL D CB    1 
ATOM   14645 C  CG1   . VAL D 2 182 ? 137.617 99.793  146.269 1.00 16.02  ? 161 VAL D CG1   1 
ATOM   14646 C  CG2   . VAL D 2 182 ? 135.534 98.363  146.134 1.00 17.78  ? 161 VAL D CG2   1 
ATOM   14647 N  N     . TYR D 2 183 ? 139.934 96.965  145.769 1.00 19.06  ? 162 TYR D N     1 
ATOM   14648 C  CA    . TYR D 2 183 ? 141.389 97.057  145.697 1.00 19.73  ? 162 TYR D CA    1 
ATOM   14649 C  C     . TYR D 2 183 ? 141.904 96.684  144.314 1.00 19.90  ? 162 TYR D C     1 
ATOM   14650 O  O     . TYR D 2 183 ? 142.858 97.281  143.842 1.00 20.73  ? 162 TYR D O     1 
ATOM   14651 C  CB    . TYR D 2 183 ? 142.094 96.232  146.790 1.00 19.84  ? 162 TYR D CB    1 
ATOM   14652 C  CG    . TYR D 2 183 ? 141.994 96.823  148.181 1.00 20.24  ? 162 TYR D CG    1 
ATOM   14653 C  CD1   . TYR D 2 183 ? 141.549 98.127  148.380 1.00 21.51  ? 162 TYR D CD1   1 
ATOM   14654 C  CD2   . TYR D 2 183 ? 142.371 96.079  149.306 1.00 20.45  ? 162 TYR D CD2   1 
ATOM   14655 C  CE1   . TYR D 2 183 ? 141.464 98.674  149.667 1.00 21.68  ? 162 TYR D CE1   1 
ATOM   14656 C  CE2   . TYR D 2 183 ? 142.310 96.625  150.595 1.00 19.97  ? 162 TYR D CE2   1 
ATOM   14657 C  CZ    . TYR D 2 183 ? 141.851 97.920  150.765 1.00 21.83  ? 162 TYR D CZ    1 
ATOM   14658 O  OH    . TYR D 2 183 ? 141.776 98.467  152.031 1.00 21.96  ? 162 TYR D OH    1 
ATOM   14659 N  N     . LEU D 2 184 ? 141.273 95.722  143.655 1.00 20.22  ? 163 LEU D N     1 
ATOM   14660 C  CA    . LEU D 2 184 ? 141.696 95.365  142.304 1.00 20.89  ? 163 LEU D CA    1 
ATOM   14661 C  C     . LEU D 2 184 ? 141.337 96.489  141.321 1.00 20.72  ? 163 LEU D C     1 
ATOM   14662 O  O     . LEU D 2 184 ? 142.207 97.000  140.622 1.00 21.07  ? 163 LEU D O     1 
ATOM   14663 C  CB    . LEU D 2 184 ? 141.135 93.995  141.875 1.00 21.16  ? 163 LEU D CB    1 
ATOM   14664 C  CG    . LEU D 2 184 ? 141.439 93.466  140.459 1.00 22.77  ? 163 LEU D CG    1 
ATOM   14665 C  CD1   . LEU D 2 184 ? 142.946 93.490  140.120 1.00 22.44  ? 163 LEU D CD1   1 
ATOM   14666 C  CD2   . LEU D 2 184 ? 140.879 92.066  140.260 1.00 24.75  ? 163 LEU D CD2   1 
ATOM   14667 N  N     . GLU D 2 185 ? 140.068 96.891  141.310 1.00 20.65  ? 164 GLU D N     1 
ATOM   14668 C  CA    . GLU D 2 185 ? 139.561 97.916  140.384 1.00 20.69  ? 164 GLU D CA    1 
ATOM   14669 C  C     . GLU D 2 185 ? 140.226 99.284  140.527 1.00 20.64  ? 164 GLU D C     1 
ATOM   14670 O  O     . GLU D 2 185 ? 140.487 99.967  139.525 1.00 20.25  ? 164 GLU D O     1 
ATOM   14671 C  CB    . GLU D 2 185 ? 138.047 98.098  140.568 1.00 21.03  ? 164 GLU D CB    1 
ATOM   14672 C  CG    . GLU D 2 185 ? 137.211 96.833  140.348 1.00 22.19  ? 164 GLU D CG    1 
ATOM   14673 C  CD    . GLU D 2 185 ? 136.885 96.554  138.883 1.00 24.19  ? 164 GLU D CD    1 
ATOM   14674 O  OE1   . GLU D 2 185 ? 137.366 97.263  137.981 1.00 27.97  ? 164 GLU D OE1   1 
ATOM   14675 O  OE2   . GLU D 2 185 ? 136.117 95.627  138.623 1.00 25.47  ? 164 GLU D OE2   1 
ATOM   14676 N  N     . SER D 2 186 ? 140.467 99.694  141.768 1.00 20.42  ? 165 SER D N     1 
ATOM   14677 C  CA    . SER D 2 186 ? 140.864 101.071 142.061 1.00 20.70  ? 165 SER D CA    1 
ATOM   14678 C  C     . SER D 2 186 ? 142.322 101.224 142.493 1.00 20.88  ? 165 SER D C     1 
ATOM   14679 O  O     . SER D 2 186 ? 142.768 102.337 142.771 1.00 21.21  ? 165 SER D O     1 
ATOM   14680 C  CB    . SER D 2 186 ? 139.945 101.681 143.134 1.00 21.25  ? 165 SER D CB    1 
ATOM   14681 O  OG    . SER D 2 186 ? 138.572 101.542 142.796 1.00 20.97  ? 165 SER D OG    1 
ATOM   14682 N  N     . PHE D 2 187 ? 143.074 100.124 142.547 1.00 20.94  ? 166 PHE D N     1 
ATOM   14683 C  CA    . PHE D 2 187 ? 144.410 100.186 143.121 1.00 21.19  ? 166 PHE D CA    1 
ATOM   14684 C  C     . PHE D 2 187 ? 145.398 99.270  142.399 1.00 21.22  ? 166 PHE D C     1 
ATOM   14685 O  O     . PHE D 2 187 ? 146.358 99.771  141.803 1.00 21.10  ? 166 PHE D O     1 
ATOM   14686 C  CB    . PHE D 2 187 ? 144.337 99.974  144.659 1.00 21.63  ? 166 PHE D CB    1 
ATOM   14687 C  CG    . PHE D 2 187 ? 145.625 99.541  145.308 1.00 24.05  ? 166 PHE D CG    1 
ATOM   14688 C  CD1   . PHE D 2 187 ? 146.778 100.322 145.220 1.00 25.52  ? 166 PHE D CD1   1 
ATOM   14689 C  CD2   . PHE D 2 187 ? 145.671 98.368  146.056 1.00 27.03  ? 166 PHE D CD2   1 
ATOM   14690 C  CE1   . PHE D 2 187 ? 147.953 99.924  145.844 1.00 26.73  ? 166 PHE D CE1   1 
ATOM   14691 C  CE2   . PHE D 2 187 ? 146.860 97.958  146.678 1.00 27.36  ? 166 PHE D CE2   1 
ATOM   14692 C  CZ    . PHE D 2 187 ? 147.994 98.738  146.566 1.00 27.87  ? 166 PHE D CZ    1 
ATOM   14693 N  N     . LEU D 2 188 ? 145.142 97.965  142.400 1.00 20.78  ? 167 LEU D N     1 
ATOM   14694 C  CA    . LEU D 2 188 ? 146.096 96.987  141.838 1.00 21.78  ? 167 LEU D CA    1 
ATOM   14695 C  C     . LEU D 2 188 ? 146.356 97.123  140.332 1.00 21.91  ? 167 LEU D C     1 
ATOM   14696 O  O     . LEU D 2 188 ? 147.462 96.838  139.873 1.00 22.87  ? 167 LEU D O     1 
ATOM   14697 C  CB    . LEU D 2 188 ? 145.663 95.555  142.153 1.00 22.32  ? 167 LEU D CB    1 
ATOM   14698 C  CG    . LEU D 2 188 ? 145.670 95.047  143.594 1.00 23.33  ? 167 LEU D CG    1 
ATOM   14699 C  CD1   . LEU D 2 188 ? 145.172 93.612  143.605 1.00 22.43  ? 167 LEU D CD1   1 
ATOM   14700 C  CD2   . LEU D 2 188 ? 147.052 95.146  144.252 1.00 25.71  ? 167 LEU D CD2   1 
ATOM   14701 N  N     . PHE D 2 189 ? 145.341 97.533  139.568 1.00 21.56  ? 168 PHE D N     1 
ATOM   14702 C  CA    . PHE D 2 189 ? 145.498 97.769  138.130 1.00 21.86  ? 168 PHE D CA    1 
ATOM   14703 C  C     . PHE D 2 189 ? 146.486 98.913  137.818 1.00 21.87  ? 168 PHE D C     1 
ATOM   14704 O  O     . PHE D 2 189 ? 147.056 98.970  136.725 1.00 21.79  ? 168 PHE D O     1 
ATOM   14705 C  CB    . PHE D 2 189 ? 144.150 98.123  137.476 1.00 21.79  ? 168 PHE D CB    1 
ATOM   14706 C  CG    . PHE D 2 189 ? 143.256 96.939  137.192 1.00 21.88  ? 168 PHE D CG    1 
ATOM   14707 C  CD1   . PHE D 2 189 ? 143.777 95.726  136.735 1.00 21.44  ? 168 PHE D CD1   1 
ATOM   14708 C  CD2   . PHE D 2 189 ? 141.875 97.057  137.351 1.00 22.82  ? 168 PHE D CD2   1 
ATOM   14709 C  CE1   . PHE D 2 189 ? 142.936 94.638  136.468 1.00 22.35  ? 168 PHE D CE1   1 
ATOM   14710 C  CE2   . PHE D 2 189 ? 141.022 95.984  137.088 1.00 22.08  ? 168 PHE D CE2   1 
ATOM   14711 C  CZ    . PHE D 2 189 ? 141.554 94.766  136.655 1.00 22.60  ? 168 PHE D CZ    1 
ATOM   14712 N  N     . TYR D 2 190 ? 146.668 99.832  138.760 1.00 21.91  ? 169 TYR D N     1 
ATOM   14713 C  CA    . TYR D 2 190 ? 147.338 101.099 138.432 1.00 22.52  ? 169 TYR D CA    1 
ATOM   14714 C  C     . TYR D 2 190 ? 148.860 101.040 138.298 1.00 22.75  ? 169 TYR D C     1 
ATOM   14715 O  O     . TYR D 2 190 ? 149.427 101.849 137.577 1.00 21.93  ? 169 TYR D O     1 
ATOM   14716 C  CB    . TYR D 2 190 ? 146.865 102.238 139.341 1.00 22.67  ? 169 TYR D CB    1 
ATOM   14717 C  CG    . TYR D 2 190 ? 145.485 102.710 138.932 1.00 24.77  ? 169 TYR D CG    1 
ATOM   14718 C  CD1   . TYR D 2 190 ? 144.346 101.958 139.240 1.00 25.65  ? 169 TYR D CD1   1 
ATOM   14719 C  CD2   . TYR D 2 190 ? 145.323 103.881 138.196 1.00 25.94  ? 169 TYR D CD2   1 
ATOM   14720 C  CE1   . TYR D 2 190 ? 143.076 102.378 138.833 1.00 26.62  ? 169 TYR D CE1   1 
ATOM   14721 C  CE2   . TYR D 2 190 ? 144.060 104.316 137.801 1.00 26.91  ? 169 TYR D CE2   1 
ATOM   14722 C  CZ    . TYR D 2 190 ? 142.946 103.563 138.117 1.00 27.39  ? 169 TYR D CZ    1 
ATOM   14723 O  OH    . TYR D 2 190 ? 141.703 104.009 137.708 1.00 27.50  ? 169 TYR D OH    1 
ATOM   14724 N  N     . SER D 2 191 ? 149.510 100.072 138.954 1.00 22.74  ? 170 SER D N     1 
ATOM   14725 C  CA    . SER D 2 191 ? 150.932 99.822  138.690 1.00 23.43  ? 170 SER D CA    1 
ATOM   14726 C  C     . SER D 2 191 ? 151.108 99.422  137.226 1.00 23.08  ? 170 SER D C     1 
ATOM   14727 O  O     . SER D 2 191 ? 152.137 99.680  136.625 1.00 23.67  ? 170 SER D O     1 
ATOM   14728 C  CB    . SER D 2 191 ? 151.511 98.743  139.618 1.00 23.39  ? 170 SER D CB    1 
ATOM   14729 O  OG    . SER D 2 191 ? 150.856 97.495  139.439 1.00 24.10  ? 170 SER D OG    1 
ATOM   14730 N  N     . GLY D 2 192 ? 150.072 98.824  136.653 1.00 22.82  ? 171 GLY D N     1 
ATOM   14731 C  CA    . GLY D 2 192 ? 150.060 98.438  135.247 1.00 22.08  ? 171 GLY D CA    1 
ATOM   14732 C  C     . GLY D 2 192 ? 149.645 99.560  134.311 1.00 22.12  ? 171 GLY D C     1 
ATOM   14733 O  O     . GLY D 2 192 ? 150.336 99.831  133.327 1.00 22.86  ? 171 GLY D O     1 
ATOM   14734 N  N     . PHE D 2 193 ? 148.526 100.217 134.612 1.00 21.48  ? 172 PHE D N     1 
ATOM   14735 C  CA    . PHE D 2 193 ? 148.025 101.337 133.794 1.00 21.06  ? 172 PHE D CA    1 
ATOM   14736 C  C     . PHE D 2 193 ? 149.070 102.437 133.606 1.00 21.13  ? 172 PHE D C     1 
ATOM   14737 O  O     . PHE D 2 193 ? 149.058 103.134 132.591 1.00 21.18  ? 172 PHE D O     1 
ATOM   14738 C  CB    . PHE D 2 193 ? 146.778 101.962 134.417 1.00 21.33  ? 172 PHE D CB    1 
ATOM   14739 C  CG    . PHE D 2 193 ? 145.532 101.112 134.321 1.00 20.93  ? 172 PHE D CG    1 
ATOM   14740 C  CD1   . PHE D 2 193 ? 145.333 100.226 133.262 1.00 20.88  ? 172 PHE D CD1   1 
ATOM   14741 C  CD2   . PHE D 2 193 ? 144.533 101.245 135.275 1.00 19.83  ? 172 PHE D CD2   1 
ATOM   14742 C  CE1   . PHE D 2 193 ? 144.162 99.463  133.185 1.00 22.31  ? 172 PHE D CE1   1 
ATOM   14743 C  CE2   . PHE D 2 193 ? 143.353 100.495 135.197 1.00 20.67  ? 172 PHE D CE2   1 
ATOM   14744 C  CZ    . PHE D 2 193 ? 143.170 99.604  134.151 1.00 21.00  ? 172 PHE D CZ    1 
ATOM   14745 N  N     . TYR D 2 194 ? 149.975 102.578 134.577 1.00 20.48  ? 173 TYR D N     1 
ATOM   14746 C  CA    . TYR D 2 194 ? 150.990 103.629 134.542 1.00 20.76  ? 173 TYR D CA    1 
ATOM   14747 C  C     . TYR D 2 194 ? 151.694 103.706 133.183 1.00 20.53  ? 173 TYR D C     1 
ATOM   14748 O  O     . TYR D 2 194 ? 151.804 104.775 132.575 1.00 19.89  ? 173 TYR D O     1 
ATOM   14749 C  CB    . TYR D 2 194 ? 152.031 103.443 135.675 1.00 20.94  ? 173 TYR D CB    1 
ATOM   14750 C  CG    . TYR D 2 194 ? 152.961 104.635 135.812 1.00 21.56  ? 173 TYR D CG    1 
ATOM   14751 C  CD1   . TYR D 2 194 ? 154.048 104.805 134.947 1.00 22.23  ? 173 TYR D CD1   1 
ATOM   14752 C  CD2   . TYR D 2 194 ? 152.742 105.607 136.792 1.00 22.00  ? 173 TYR D CD2   1 
ATOM   14753 C  CE1   . TYR D 2 194 ? 154.887 105.898 135.058 1.00 21.58  ? 173 TYR D CE1   1 
ATOM   14754 C  CE2   . TYR D 2 194 ? 153.579 106.715 136.905 1.00 20.52  ? 173 TYR D CE2   1 
ATOM   14755 C  CZ    . TYR D 2 194 ? 154.649 106.849 136.035 1.00 21.66  ? 173 TYR D CZ    1 
ATOM   14756 O  OH    . TYR D 2 194 ? 155.469 107.948 136.127 1.00 21.37  ? 173 TYR D OH    1 
ATOM   14757 N  N     . TYR D 2 195 ? 152.143 102.562 132.694 1.00 20.77  ? 174 TYR D N     1 
ATOM   14758 C  CA    . TYR D 2 195 ? 153.007 102.558 131.526 1.00 21.12  ? 174 TYR D CA    1 
ATOM   14759 C  C     . TYR D 2 195 ? 152.287 102.987 130.234 1.00 21.49  ? 174 TYR D C     1 
ATOM   14760 O  O     . TYR D 2 195 ? 152.778 103.886 129.545 1.00 21.60  ? 174 TYR D O     1 
ATOM   14761 C  CB    . TYR D 2 195 ? 153.738 101.218 131.407 1.00 21.23  ? 174 TYR D CB    1 
ATOM   14762 C  CG    . TYR D 2 195 ? 155.099 101.288 130.753 1.00 21.77  ? 174 TYR D CG    1 
ATOM   14763 C  CD1   . TYR D 2 195 ? 155.966 102.361 130.990 1.00 23.28  ? 174 TYR D CD1   1 
ATOM   14764 C  CD2   . TYR D 2 195 ? 155.532 100.265 129.913 1.00 22.87  ? 174 TYR D CD2   1 
ATOM   14765 C  CE1   . TYR D 2 195 ? 157.230 102.410 130.382 1.00 23.81  ? 174 TYR D CE1   1 
ATOM   14766 C  CE2   . TYR D 2 195 ? 156.789 100.305 129.314 1.00 24.09  ? 174 TYR D CE2   1 
ATOM   14767 C  CZ    . TYR D 2 195 ? 157.626 101.377 129.547 1.00 23.51  ? 174 TYR D CZ    1 
ATOM   14768 O  OH    . TYR D 2 195 ? 158.868 101.415 128.942 1.00 25.36  ? 174 TYR D OH    1 
ATOM   14769 N  N     . PRO D 2 196 ? 151.125 102.365 129.904 1.00 21.86  ? 175 PRO D N     1 
ATOM   14770 C  CA    . PRO D 2 196 ? 150.356 102.841 128.744 1.00 22.03  ? 175 PRO D CA    1 
ATOM   14771 C  C     . PRO D 2 196 ? 149.987 104.321 128.841 1.00 22.18  ? 175 PRO D C     1 
ATOM   14772 O  O     . PRO D 2 196 ? 150.025 105.018 127.824 1.00 23.00  ? 175 PRO D O     1 
ATOM   14773 C  CB    . PRO D 2 196 ? 149.081 101.989 128.773 1.00 21.50  ? 175 PRO D CB    1 
ATOM   14774 C  CG    . PRO D 2 196 ? 149.415 100.808 129.540 1.00 22.47  ? 175 PRO D CG    1 
ATOM   14775 C  CD    . PRO D 2 196 ? 150.594 101.092 130.423 1.00 20.91  ? 175 PRO D CD    1 
ATOM   14776 N  N     . LEU D 2 197 ? 149.648 104.797 130.041 1.00 21.70  ? 176 LEU D N     1 
ATOM   14777 C  CA    . LEU D 2 197 ? 149.355 106.223 130.246 1.00 22.40  ? 176 LEU D CA    1 
ATOM   14778 C  C     . LEU D 2 197 ? 150.587 107.109 130.039 1.00 22.58  ? 176 LEU D C     1 
ATOM   14779 O  O     . LEU D 2 197 ? 150.480 108.219 129.503 1.00 22.15  ? 176 LEU D O     1 
ATOM   14780 C  CB    . LEU D 2 197 ? 148.792 106.474 131.639 1.00 22.15  ? 176 LEU D CB    1 
ATOM   14781 C  CG    . LEU D 2 197 ? 147.374 105.994 131.973 1.00 23.08  ? 176 LEU D CG    1 
ATOM   14782 C  CD1   . LEU D 2 197 ? 147.200 106.036 133.482 1.00 21.62  ? 176 LEU D CD1   1 
ATOM   14783 C  CD2   . LEU D 2 197 ? 146.311 106.857 131.263 1.00 21.94  ? 176 LEU D CD2   1 
ATOM   14784 N  N     . TYR D 2 198 ? 151.742 106.603 130.478 1.00 22.76  ? 177 TYR D N     1 
ATOM   14785 C  CA    . TYR D 2 198 ? 153.036 107.262 130.286 1.00 23.23  ? 177 TYR D CA    1 
ATOM   14786 C  C     . TYR D 2 198 ? 153.354 107.428 128.800 1.00 23.91  ? 177 TYR D C     1 
ATOM   14787 O  O     . TYR D 2 198 ? 153.743 108.521 128.362 1.00 24.20  ? 177 TYR D O     1 
ATOM   14788 C  CB    . TYR D 2 198 ? 154.141 106.482 131.018 1.00 23.19  ? 177 TYR D CB    1 
ATOM   14789 C  CG    . TYR D 2 198 ? 155.534 107.077 130.938 1.00 23.52  ? 177 TYR D CG    1 
ATOM   14790 C  CD1   . TYR D 2 198 ? 155.832 108.284 131.553 1.00 24.85  ? 177 TYR D CD1   1 
ATOM   14791 C  CD2   . TYR D 2 198 ? 156.568 106.398 130.279 1.00 25.30  ? 177 TYR D CD2   1 
ATOM   14792 C  CE1   . TYR D 2 198 ? 157.119 108.827 131.499 1.00 26.05  ? 177 TYR D CE1   1 
ATOM   14793 C  CE2   . TYR D 2 198 ? 157.867 106.932 130.223 1.00 26.38  ? 177 TYR D CE2   1 
ATOM   14794 C  CZ    . TYR D 2 198 ? 158.126 108.143 130.837 1.00 26.68  ? 177 TYR D CZ    1 
ATOM   14795 O  OH    . TYR D 2 198 ? 159.391 108.687 130.800 1.00 30.01  ? 177 TYR D OH    1 
ATOM   14796 N  N     . PHE D 2 199 ? 153.183 106.363 128.015 1.00 24.84  ? 178 PHE D N     1 
ATOM   14797 C  CA    . PHE D 2 199 ? 153.342 106.483 126.562 1.00 25.81  ? 178 PHE D CA    1 
ATOM   14798 C  C     . PHE D 2 199 ? 152.302 107.393 125.920 1.00 26.23  ? 178 PHE D C     1 
ATOM   14799 O  O     . PHE D 2 199 ? 152.640 108.237 125.090 1.00 26.58  ? 178 PHE D O     1 
ATOM   14800 C  CB    . PHE D 2 199 ? 153.339 105.117 125.888 1.00 26.08  ? 178 PHE D CB    1 
ATOM   14801 C  CG    . PHE D 2 199 ? 154.619 104.358 126.068 1.00 28.71  ? 178 PHE D CG    1 
ATOM   14802 C  CD1   . PHE D 2 199 ? 155.846 104.982 125.878 1.00 32.03  ? 178 PHE D CD1   1 
ATOM   14803 C  CD2   . PHE D 2 199 ? 154.607 103.022 126.433 1.00 31.77  ? 178 PHE D CD2   1 
ATOM   14804 C  CE1   . PHE D 2 199 ? 157.051 104.285 126.056 1.00 32.29  ? 178 PHE D CE1   1 
ATOM   14805 C  CE2   . PHE D 2 199 ? 155.804 102.318 126.603 1.00 32.72  ? 178 PHE D CE2   1 
ATOM   14806 C  CZ    . PHE D 2 199 ? 157.024 102.958 126.412 1.00 31.91  ? 178 PHE D CZ    1 
ATOM   14807 N  N     . TYR D 2 200 ? 151.047 107.205 126.319 1.00 26.46  ? 179 TYR D N     1 
ATOM   14808 C  CA    . TYR D 2 200 ? 149.899 107.972 125.809 1.00 27.43  ? 179 TYR D CA    1 
ATOM   14809 C  C     . TYR D 2 200 ? 150.105 109.468 126.022 1.00 27.68  ? 179 TYR D C     1 
ATOM   14810 O  O     . TYR D 2 200 ? 149.783 110.273 125.149 1.00 28.71  ? 179 TYR D O     1 
ATOM   14811 C  CB    . TYR D 2 200 ? 148.649 107.506 126.549 1.00 27.27  ? 179 TYR D CB    1 
ATOM   14812 C  CG    . TYR D 2 200 ? 147.310 107.848 125.944 1.00 28.90  ? 179 TYR D CG    1 
ATOM   14813 C  CD1   . TYR D 2 200 ? 147.044 107.630 124.599 1.00 29.00  ? 179 TYR D CD1   1 
ATOM   14814 C  CD2   . TYR D 2 200 ? 146.277 108.331 126.754 1.00 30.14  ? 179 TYR D CD2   1 
ATOM   14815 C  CE1   . TYR D 2 200 ? 145.793 107.920 124.058 1.00 31.26  ? 179 TYR D CE1   1 
ATOM   14816 C  CE2   . TYR D 2 200 ? 145.026 108.613 126.232 1.00 31.86  ? 179 TYR D CE2   1 
ATOM   14817 C  CZ    . TYR D 2 200 ? 144.790 108.411 124.882 1.00 32.51  ? 179 TYR D CZ    1 
ATOM   14818 O  OH    . TYR D 2 200 ? 143.550 108.695 124.363 1.00 33.77  ? 179 TYR D OH    1 
ATOM   14819 N  N     . GLY D 2 201 ? 150.647 109.833 127.182 1.00 27.68  ? 180 GLY D N     1 
ATOM   14820 C  CA    . GLY D 2 201 ? 150.957 111.224 127.493 1.00 28.02  ? 180 GLY D CA    1 
ATOM   14821 C  C     . GLY D 2 201 ? 152.121 111.819 126.706 1.00 28.60  ? 180 GLY D C     1 
ATOM   14822 O  O     . GLY D 2 201 ? 152.296 113.030 126.701 1.00 28.44  ? 180 GLY D O     1 
ATOM   14823 N  N     . GLN D 2 202 ? 152.918 110.959 126.064 1.00 29.34  ? 181 GLN D N     1 
ATOM   14824 C  CA    . GLN D 2 202 ? 154.076 111.358 125.245 1.00 30.39  ? 181 GLN D CA    1 
ATOM   14825 C  C     . GLN D 2 202 ? 153.804 111.312 123.741 1.00 30.55  ? 181 GLN D C     1 
ATOM   14826 O  O     . GLN D 2 202 ? 154.691 111.637 122.944 1.00 31.23  ? 181 GLN D O     1 
ATOM   14827 C  CB    . GLN D 2 202 ? 155.239 110.386 125.457 1.00 30.31  ? 181 GLN D CB    1 
ATOM   14828 C  CG    . GLN D 2 202 ? 155.907 110.374 126.779 1.00 32.40  ? 181 GLN D CG    1 
ATOM   14829 C  CD    . GLN D 2 202 ? 157.019 109.345 126.795 1.00 33.85  ? 181 GLN D CD    1 
ATOM   14830 O  OE1   . GLN D 2 202 ? 156.888 108.278 127.389 1.00 33.94  ? 181 GLN D OE1   1 
ATOM   14831 N  NE2   . GLN D 2 202 ? 158.103 109.643 126.100 1.00 34.92  ? 181 GLN D NE2   1 
ATOM   14832 N  N     . GLY D 2 203 ? 152.626 110.846 123.345 1.00 30.57  ? 182 GLY D N     1 
ATOM   14833 C  CA    . GLY D 2 203 ? 152.303 110.701 121.924 1.00 30.83  ? 182 GLY D CA    1 
ATOM   14834 C  C     . GLY D 2 203 ? 152.696 109.357 121.329 1.00 30.80  ? 182 GLY D C     1 
ATOM   14835 O  O     . GLY D 2 203 ? 152.664 109.183 120.108 1.00 30.86  ? 182 GLY D O     1 
ATOM   14836 N  N     . LYS D 2 204 ? 153.061 108.406 122.189 1.00 30.14  ? 183 LYS D N     1 
ATOM   14837 C  CA    . LYS D 2 204 ? 153.429 107.057 121.748 1.00 30.35  ? 183 LYS D CA    1 
ATOM   14838 C  C     . LYS D 2 204 ? 152.317 106.047 122.020 1.00 29.52  ? 183 LYS D C     1 
ATOM   14839 O  O     . LYS D 2 204 ? 151.599 106.168 123.010 1.00 28.60  ? 183 LYS D O     1 
ATOM   14840 C  CB    . LYS D 2 204 ? 154.724 106.610 122.423 1.00 30.76  ? 183 LYS D CB    1 
ATOM   14841 C  CG    . LYS D 2 204 ? 155.946 107.436 122.011 1.00 32.95  ? 183 LYS D CG    1 
ATOM   14842 C  CD    . LYS D 2 204 ? 157.110 107.128 122.922 1.00 36.37  ? 183 LYS D CD    1 
ATOM   14843 C  CE    . LYS D 2 204 ? 158.351 107.921 122.554 1.00 38.47  ? 183 LYS D CE    1 
ATOM   14844 N  NZ    . LYS D 2 204 ? 159.357 107.746 123.645 1.00 40.21  ? 183 LYS D NZ    1 
ATOM   14845 N  N     . LEU D 2 205 ? 152.191 105.050 121.141 1.00 29.47  ? 184 LEU D N     1 
ATOM   14846 C  CA    . LEU D 2 205 ? 151.165 104.002 121.254 1.00 29.06  ? 184 LEU D CA    1 
ATOM   14847 C  C     . LEU D 2 205 ? 149.790 104.587 121.641 1.00 28.96  ? 184 LEU D C     1 
ATOM   14848 O  O     . LEU D 2 205 ? 149.164 104.180 122.628 1.00 27.68  ? 184 LEU D O     1 
ATOM   14849 C  CB    . LEU D 2 205 ? 151.604 102.902 122.234 1.00 28.63  ? 184 LEU D CB    1 
ATOM   14850 C  CG    . LEU D 2 205 ? 152.937 102.188 121.964 1.00 29.00  ? 184 LEU D CG    1 
ATOM   14851 C  CD1   . LEU D 2 205 ? 153.240 101.189 123.084 1.00 28.90  ? 184 LEU D CD1   1 
ATOM   14852 C  CD2   . LEU D 2 205 ? 152.930 101.480 120.616 1.00 28.67  ? 184 LEU D CD2   1 
ATOM   14853 N  N     . MET D 2 206 ? 149.349 105.546 120.832 1.00 29.02  ? 185 MET D N     1 
ATOM   14854 C  CA    . MET D 2 206 ? 148.126 106.301 121.056 1.00 29.72  ? 185 MET D CA    1 
ATOM   14855 C  C     . MET D 2 206 ? 146.830 105.511 120.908 1.00 29.54  ? 185 MET D C     1 
ATOM   14856 O  O     . MET D 2 206 ? 145.857 105.805 121.600 1.00 29.47  ? 185 MET D O     1 
ATOM   14857 C  CB    . MET D 2 206 ? 148.095 107.521 120.127 1.00 30.69  ? 185 MET D CB    1 
ATOM   14858 C  CG    . MET D 2 206 ? 149.283 108.449 120.329 1.00 32.03  ? 185 MET D CG    1 
ATOM   14859 S  SD    . MET D 2 206 ? 149.369 109.049 122.025 1.00 36.63  ? 185 MET D SD    1 
ATOM   14860 C  CE    . MET D 2 206 ? 148.256 110.441 121.936 1.00 33.80  ? 185 MET D CE    1 
ATOM   14861 N  N     . GLN D 2 207 ? 146.807 104.538 119.999 1.00 29.56  ? 186 GLN D N     1 
ATOM   14862 C  CA    . GLN D 2 207 ? 145.603 103.736 119.756 1.00 29.17  ? 186 GLN D CA    1 
ATOM   14863 C  C     . GLN D 2 207 ? 145.354 102.777 120.917 1.00 28.26  ? 186 GLN D C     1 
ATOM   14864 O  O     . GLN D 2 207 ? 144.238 102.694 121.422 1.00 27.98  ? 186 GLN D O     1 
ATOM   14865 C  CB    . GLN D 2 207 ? 145.699 102.964 118.430 1.00 29.80  ? 186 GLN D CB    1 
ATOM   14866 C  CG    . GLN D 2 207 ? 146.005 103.830 117.209 1.00 31.75  ? 186 GLN D CG    1 
ATOM   14867 C  CD    . GLN D 2 207 ? 145.062 105.011 117.094 1.00 34.93  ? 186 GLN D CD    1 
ATOM   14868 O  OE1   . GLN D 2 207 ? 143.876 104.854 116.778 1.00 36.91  ? 186 GLN D OE1   1 
ATOM   14869 N  NE2   . GLN D 2 207 ? 145.583 106.203 117.361 1.00 36.09  ? 186 GLN D NE2   1 
ATOM   14870 N  N     . SER D 2 208 ? 146.392 102.058 121.339 0.50 27.75  ? 187 SER D N     1 
ATOM   14871 C  CA    . SER D 2 208 ? 146.270 101.155 122.476 0.50 27.12  ? 187 SER D CA    1 
ATOM   14872 C  C     . SER D 2 208 ? 146.101 101.939 123.775 0.50 26.72  ? 187 SER D C     1 
ATOM   14873 O  O     . SER D 2 208 ? 145.423 101.475 124.690 0.50 26.30  ? 187 SER D O     1 
ATOM   14874 C  CB    . SER D 2 208 ? 147.467 100.208 122.566 0.50 26.88  ? 187 SER D CB    1 
ATOM   14875 O  OG    . SER D 2 208 ? 148.678 100.931 122.533 0.50 26.59  ? 187 SER D OG    1 
ATOM   14876 N  N     . GLY D 2 209 ? 146.715 103.121 123.843 1.00 26.64  ? 188 GLY D N     1 
ATOM   14877 C  CA    . GLY D 2 209 ? 146.554 104.026 124.999 1.00 26.43  ? 188 GLY D CA    1 
ATOM   14878 C  C     . GLY D 2 209 ? 145.130 104.548 125.139 1.00 26.66  ? 188 GLY D C     1 
ATOM   14879 O  O     . GLY D 2 209 ? 144.626 104.722 126.249 1.00 26.57  ? 188 GLY D O     1 
ATOM   14880 N  N     . GLU D 2 210 ? 144.478 104.807 124.009 1.00 27.42  ? 189 GLU D N     1 
ATOM   14881 C  CA    . GLU D 2 210 ? 143.071 105.204 124.014 1.00 27.73  ? 189 GLU D CA    1 
ATOM   14882 C  C     . GLU D 2 210 ? 142.206 104.054 124.552 1.00 27.04  ? 189 GLU D C     1 
ATOM   14883 O  O     . GLU D 2 210 ? 141.342 104.263 125.404 1.00 26.57  ? 189 GLU D O     1 
ATOM   14884 C  CB    . GLU D 2 210 ? 142.611 105.645 122.613 1.00 28.28  ? 189 GLU D CB    1 
ATOM   14885 C  CG    . GLU D 2 210 ? 141.166 106.167 122.579 1.00 30.71  ? 189 GLU D CG    1 
ATOM   14886 C  CD    . GLU D 2 210 ? 140.774 106.850 121.271 1.00 35.43  ? 189 GLU D CD    1 
ATOM   14887 O  OE1   . GLU D 2 210 ? 141.551 106.806 120.284 1.00 36.89  ? 189 GLU D OE1   1 
ATOM   14888 O  OE2   . GLU D 2 210 ? 139.674 107.447 121.238 1.00 37.04  ? 189 GLU D OE2   1 
ATOM   14889 N  N     . ILE D 2 211 ? 142.456 102.845 124.059 1.00 26.80  ? 190 ILE D N     1 
ATOM   14890 C  CA    . ILE D 2 211 ? 141.777 101.657 124.568 1.00 26.92  ? 190 ILE D CA    1 
ATOM   14891 C  C     . ILE D 2 211 ? 141.980 101.509 126.070 1.00 26.45  ? 190 ILE D C     1 
ATOM   14892 O  O     . ILE D 2 211 ? 141.014 101.294 126.800 1.00 26.65  ? 190 ILE D O     1 
ATOM   14893 C  CB    . ILE D 2 211 ? 142.203 100.371 123.815 1.00 27.00  ? 190 ILE D CB    1 
ATOM   14894 C  CG1   . ILE D 2 211 ? 141.642 100.403 122.388 1.00 28.77  ? 190 ILE D CG1   1 
ATOM   14895 C  CG2   . ILE D 2 211 ? 141.708 99.116  124.553 1.00 26.82  ? 190 ILE D CG2   1 
ATOM   14896 C  CD1   . ILE D 2 211 ? 142.115 99.270  121.486 1.00 30.88  ? 190 ILE D CD1   1 
ATOM   14897 N  N     . ILE D 2 212 ? 143.223 101.651 126.539 1.00 26.49  ? 191 ILE D N     1 
ATOM   14898 C  CA    . ILE D 2 212 ? 143.517 101.479 127.962 1.00 25.73  ? 191 ILE D CA    1 
ATOM   14899 C  C     . ILE D 2 212 ? 142.783 102.529 128.799 1.00 25.48  ? 191 ILE D C     1 
ATOM   14900 O  O     . ILE D 2 212 ? 142.265 102.224 129.877 1.00 24.95  ? 191 ILE D O     1 
ATOM   14901 C  CB    . ILE D 2 212 ? 145.046 101.490 128.259 1.00 26.44  ? 191 ILE D CB    1 
ATOM   14902 C  CG1   . ILE D 2 212 ? 145.735 100.278 127.616 1.00 26.71  ? 191 ILE D CG1   1 
ATOM   14903 C  CG2   . ILE D 2 212 ? 145.320 101.538 129.779 1.00 26.01  ? 191 ILE D CG2   1 
ATOM   14904 C  CD1   . ILE D 2 212 ? 145.284 98.918  128.115 1.00 30.50  ? 191 ILE D CD1   1 
ATOM   14905 N  N     . ASN D 2 213 ? 142.721 103.753 128.284 1.00 24.79  ? 192 ASN D N     1 
ATOM   14906 C  CA    . ASN D 2 213 ? 142.016 104.829 128.966 1.00 24.80  ? 192 ASN D CA    1 
ATOM   14907 C  C     . ASN D 2 213 ? 140.507 104.545 129.119 1.00 24.44  ? 192 ASN D C     1 
ATOM   14908 O  O     . ASN D 2 213 ? 139.894 104.918 130.126 1.00 23.25  ? 192 ASN D O     1 
ATOM   14909 C  CB    . ASN D 2 213 ? 142.261 106.158 128.248 1.00 25.68  ? 192 ASN D CB    1 
ATOM   14910 C  CG    . ASN D 2 213 ? 142.399 107.324 129.208 1.00 27.89  ? 192 ASN D CG    1 
ATOM   14911 O  OD1   . ASN D 2 213 ? 142.858 107.170 130.337 1.00 31.05  ? 192 ASN D OD1   1 
ATOM   14912 N  ND2   . ASN D 2 213 ? 142.005 108.506 128.754 1.00 31.70  ? 192 ASN D ND2   1 
ATOM   14913 N  N     . LEU D 2 214 ? 139.921 103.873 128.128 1.00 23.60  ? 193 LEU D N     1 
ATOM   14914 C  CA    . LEU D 2 214 ? 138.504 103.511 128.188 1.00 23.84  ? 193 LEU D CA    1 
ATOM   14915 C  C     . LEU D 2 214 ? 138.289 102.405 129.206 1.00 23.48  ? 193 LEU D C     1 
ATOM   14916 O  O     . LEU D 2 214 ? 137.323 102.442 129.973 1.00 24.12  ? 193 LEU D O     1 
ATOM   14917 C  CB    . LEU D 2 214 ? 137.997 103.073 126.815 1.00 23.71  ? 193 LEU D CB    1 
ATOM   14918 C  CG    . LEU D 2 214 ? 137.805 104.200 125.791 1.00 25.29  ? 193 LEU D CG    1 
ATOM   14919 C  CD1   . LEU D 2 214 ? 137.441 103.623 124.422 1.00 25.41  ? 193 LEU D CD1   1 
ATOM   14920 C  CD2   . LEU D 2 214 ? 136.749 105.195 126.243 1.00 25.80  ? 193 LEU D CD2   1 
ATOM   14921 N  N     . ILE D 2 215 ? 139.201 101.433 129.212 1.00 22.89  ? 194 ILE D N     1 
ATOM   14922 C  CA    . ILE D 2 215 ? 139.170 100.344 130.177 1.00 22.25  ? 194 ILE D CA    1 
ATOM   14923 C  C     . ILE D 2 215 ? 139.286 100.920 131.584 1.00 22.55  ? 194 ILE D C     1 
ATOM   14924 O  O     . ILE D 2 215 ? 138.475 100.610 132.468 1.00 22.53  ? 194 ILE D O     1 
ATOM   14925 C  CB    . ILE D 2 215 ? 140.306 99.330  129.935 1.00 22.37  ? 194 ILE D CB    1 
ATOM   14926 C  CG1   . ILE D 2 215 ? 140.091 98.596  128.605 1.00 21.89  ? 194 ILE D CG1   1 
ATOM   14927 C  CG2   . ILE D 2 215 ? 140.418 98.349  131.120 1.00 20.25  ? 194 ILE D CG2   1 
ATOM   14928 C  CD1   . ILE D 2 215 ? 141.179 97.570  128.263 1.00 20.48  ? 194 ILE D CD1   1 
ATOM   14929 N  N     . LEU D 2 216 ? 140.287 101.774 131.782 1.00 22.35  ? 195 LEU D N     1 
ATOM   14930 C  CA    . LEU D 2 216 ? 140.549 102.364 133.092 1.00 22.51  ? 195 LEU D CA    1 
ATOM   14931 C  C     . LEU D 2 216 ? 139.322 103.136 133.585 1.00 22.30  ? 195 LEU D C     1 
ATOM   14932 O  O     . LEU D 2 216 ? 138.971 103.051 134.769 1.00 21.62  ? 195 LEU D O     1 
ATOM   14933 C  CB    . LEU D 2 216 ? 141.780 103.280 133.007 1.00 23.06  ? 195 LEU D CB    1 
ATOM   14934 C  CG    . LEU D 2 216 ? 142.270 104.157 134.169 1.00 23.98  ? 195 LEU D CG    1 
ATOM   14935 C  CD1   . LEU D 2 216 ? 143.678 104.595 133.864 1.00 24.44  ? 195 LEU D CD1   1 
ATOM   14936 C  CD2   . LEU D 2 216 ? 141.379 105.392 134.386 1.00 25.00  ? 195 LEU D CD2   1 
ATOM   14937 N  N     . ARG D 2 217 ? 138.686 103.887 132.679 1.00 21.64  ? 196 ARG D N     1 
ATOM   14938 C  CA    . ARG D 2 217 ? 137.470 104.639 133.010 1.00 22.49  ? 196 ARG D CA    1 
ATOM   14939 C  C     . ARG D 2 217 ? 136.331 103.704 133.486 1.00 21.56  ? 196 ARG D C     1 
ATOM   14940 O  O     . ARG D 2 217 ? 135.609 104.044 134.414 1.00 21.32  ? 196 ARG D O     1 
ATOM   14941 C  CB    . ARG D 2 217 ? 137.015 105.542 131.847 1.00 23.07  ? 196 ARG D CB    1 
ATOM   14942 C  CG    . ARG D 2 217 ? 135.845 106.486 132.202 1.00 25.64  ? 196 ARG D CG    1 
ATOM   14943 C  CD    . ARG D 2 217 ? 135.263 107.215 130.977 1.00 32.11  ? 196 ARG D CD    1 
ATOM   14944 N  NE    . ARG D 2 217 ? 134.766 106.283 129.955 1.00 35.06  ? 196 ARG D NE    1 
ATOM   14945 C  CZ    . ARG D 2 217 ? 134.027 106.631 128.907 1.00 37.65  ? 196 ARG D CZ    1 
ATOM   14946 N  NH1   . ARG D 2 217 ? 133.638 105.707 128.032 1.00 40.20  ? 196 ARG D NH1   1 
ATOM   14947 N  NH2   . ARG D 2 217 ? 133.662 107.896 128.731 1.00 38.20  ? 196 ARG D NH2   1 
ATOM   14948 N  N     . ASP D 2 218 ? 136.181 102.537 132.857 1.00 21.34  ? 197 ASP D N     1 
ATOM   14949 C  CA    . ASP D 2 218 ? 135.250 101.510 133.349 1.00 21.09  ? 197 ASP D CA    1 
ATOM   14950 C  C     . ASP D 2 218 ? 135.655 100.986 134.742 1.00 20.65  ? 197 ASP D C     1 
ATOM   14951 O  O     . ASP D 2 218 ? 134.808 100.885 135.633 1.00 20.16  ? 197 ASP D O     1 
ATOM   14952 C  CB    . ASP D 2 218 ? 135.138 100.333 132.368 1.00 21.58  ? 197 ASP D CB    1 
ATOM   14953 C  CG    . ASP D 2 218 ? 134.480 100.715 131.043 1.00 22.60  ? 197 ASP D CG    1 
ATOM   14954 O  OD1   . ASP D 2 218 ? 133.719 101.709 130.988 1.00 24.72  ? 197 ASP D OD1   1 
ATOM   14955 O  OD2   . ASP D 2 218 ? 134.741 100.010 130.041 1.00 22.64  ? 197 ASP D OD2   1 
ATOM   14956 N  N     . GLU D 2 219 ? 136.931 100.649 134.939 1.00 20.59  ? 198 GLU D N     1 
ATOM   14957 C  CA    . GLU D 2 219 ? 137.361 100.101 136.244 1.00 20.66  ? 198 GLU D CA    1 
ATOM   14958 C  C     . GLU D 2 219 ? 137.150 101.107 137.379 1.00 20.45  ? 198 GLU D C     1 
ATOM   14959 O  O     . GLU D 2 219 ? 136.794 100.721 138.497 1.00 20.59  ? 198 GLU D O     1 
ATOM   14960 C  CB    . GLU D 2 219 ? 138.818 99.611  136.229 1.00 20.55  ? 198 GLU D CB    1 
ATOM   14961 C  CG    . GLU D 2 219 ? 139.266 98.819  134.961 1.00 21.99  ? 198 GLU D CG    1 
ATOM   14962 C  CD    . GLU D 2 219 ? 138.495 97.522  134.687 1.00 24.00  ? 198 GLU D CD    1 
ATOM   14963 O  OE1   . GLU D 2 219 ? 137.334 97.358  135.122 1.00 25.06  ? 198 GLU D OE1   1 
ATOM   14964 O  OE2   . GLU D 2 219 ? 139.048 96.653  133.992 1.00 24.49  ? 198 GLU D OE2   1 
ATOM   14965 N  N     . ALA D 2 220 ? 137.353 102.388 137.084 1.00 20.47  ? 199 ALA D N     1 
ATOM   14966 C  CA    . ALA D 2 220 ? 137.105 103.463 138.068 1.00 21.10  ? 199 ALA D CA    1 
ATOM   14967 C  C     . ALA D 2 220 ? 135.669 103.446 138.585 1.00 21.34  ? 199 ALA D C     1 
ATOM   14968 O  O     . ALA D 2 220 ? 135.453 103.383 139.794 1.00 21.19  ? 199 ALA D O     1 
ATOM   14969 C  CB    . ALA D 2 220 ? 137.466 104.836 137.496 1.00 21.09  ? 199 ALA D CB    1 
ATOM   14970 N  N     . ILE D 2 221 ? 134.695 103.472 137.673 1.00 21.31  ? 200 ILE D N     1 
ATOM   14971 C  CA    . ILE D 2 221 ? 133.294 103.372 138.076 1.00 21.80  ? 200 ILE D CA    1 
ATOM   14972 C  C     . ILE D 2 221 ? 132.935 102.020 138.732 1.00 20.90  ? 200 ILE D C     1 
ATOM   14973 O  O     . ILE D 2 221 ? 132.142 101.988 139.671 1.00 20.54  ? 200 ILE D O     1 
ATOM   14974 C  CB    . ILE D 2 221 ? 132.303 103.774 136.947 1.00 22.75  ? 200 ILE D CB    1 
ATOM   14975 C  CG1   . ILE D 2 221 ? 130.927 104.049 137.544 1.00 24.63  ? 200 ILE D CG1   1 
ATOM   14976 C  CG2   . ILE D 2 221 ? 132.189 102.688 135.879 1.00 23.38  ? 200 ILE D CG2   1 
ATOM   14977 C  CD1   . ILE D 2 221 ? 130.052 104.916 136.688 1.00 26.91  ? 200 ILE D CD1   1 
ATOM   14978 N  N     . HIS D 2 222 ? 133.543 100.921 138.272 1.00 20.31  ? 201 HIS D N     1 
ATOM   14979 C  CA    . HIS D 2 222 ? 133.335 99.626  138.927 1.00 20.25  ? 201 HIS D CA    1 
ATOM   14980 C  C     . HIS D 2 222 ? 133.763 99.699  140.391 1.00 20.51  ? 201 HIS D C     1 
ATOM   14981 O  O     . HIS D 2 222 ? 133.009 99.307  141.290 1.00 20.99  ? 201 HIS D O     1 
ATOM   14982 C  CB    . HIS D 2 222 ? 134.088 98.491  138.224 1.00 19.79  ? 201 HIS D CB    1 
ATOM   14983 C  CG    . HIS D 2 222 ? 133.664 98.243  136.809 1.00 19.25  ? 201 HIS D CG    1 
ATOM   14984 N  ND1   . HIS D 2 222 ? 134.341 97.371  135.984 1.00 18.35  ? 201 HIS D ND1   1 
ATOM   14985 C  CD2   . HIS D 2 222 ? 132.651 98.755  136.066 1.00 17.64  ? 201 HIS D CD2   1 
ATOM   14986 C  CE1   . HIS D 2 222 ? 133.758 97.341  134.798 1.00 18.28  ? 201 HIS D CE1   1 
ATOM   14987 N  NE2   . HIS D 2 222 ? 132.735 98.179  134.819 1.00 20.01  ? 201 HIS D NE2   1 
ATOM   14988 N  N     . GLY D 2 223 ? 134.967 100.223 140.627 1.00 20.33  ? 202 GLY D N     1 
ATOM   14989 C  CA    . GLY D 2 223 ? 135.496 100.402 141.985 1.00 19.94  ? 202 GLY D CA    1 
ATOM   14990 C  C     . GLY D 2 223 ? 134.618 101.272 142.875 1.00 19.80  ? 202 GLY D C     1 
ATOM   14991 O  O     . GLY D 2 223 ? 134.360 100.918 144.025 1.00 19.96  ? 202 GLY D O     1 
ATOM   14992 N  N     . VAL D 2 224 ? 134.130 102.394 142.343 1.00 19.49  ? 203 VAL D N     1 
ATOM   14993 C  CA    . VAL D 2 224 ? 133.239 103.284 143.107 1.00 18.88  ? 203 VAL D CA    1 
ATOM   14994 C  C     . VAL D 2 224 ? 131.923 102.588 143.481 1.00 18.55  ? 203 VAL D C     1 
ATOM   14995 O  O     . VAL D 2 224 ? 131.459 102.677 144.630 1.00 17.65  ? 203 VAL D O     1 
ATOM   14996 C  CB    . VAL D 2 224 ? 132.955 104.634 142.353 1.00 19.22  ? 203 VAL D CB    1 
ATOM   14997 C  CG1   . VAL D 2 224 ? 131.997 105.528 143.166 1.00 18.51  ? 203 VAL D CG1   1 
ATOM   14998 C  CG2   . VAL D 2 224 ? 134.270 105.390 142.069 1.00 19.69  ? 203 VAL D CG2   1 
ATOM   14999 N  N     . TYR D 2 225 ? 131.342 101.876 142.519 1.00 18.17  ? 204 TYR D N     1 
ATOM   15000 C  CA    . TYR D 2 225 ? 130.065 101.187 142.721 1.00 18.76  ? 204 TYR D CA    1 
ATOM   15001 C  C     . TYR D 2 225 ? 130.178 100.061 143.763 1.00 18.93  ? 204 TYR D C     1 
ATOM   15002 O  O     . TYR D 2 225 ? 129.406 100.011 144.731 1.00 18.77  ? 204 TYR D O     1 
ATOM   15003 C  CB    . TYR D 2 225 ? 129.509 100.641 141.390 1.00 18.96  ? 204 TYR D CB    1 
ATOM   15004 C  CG    . TYR D 2 225 ? 128.118 100.041 141.559 1.00 20.06  ? 204 TYR D CG    1 
ATOM   15005 C  CD1   . TYR D 2 225 ? 127.027 100.856 141.891 1.00 21.79  ? 204 TYR D CD1   1 
ATOM   15006 C  CD2   . TYR D 2 225 ? 127.900 98.667  141.423 1.00 19.51  ? 204 TYR D CD2   1 
ATOM   15007 C  CE1   . TYR D 2 225 ? 125.753 100.317 142.077 1.00 20.38  ? 204 TYR D CE1   1 
ATOM   15008 C  CE2   . TYR D 2 225 ? 126.612 98.114  141.604 1.00 19.38  ? 204 TYR D CE2   1 
ATOM   15009 C  CZ    . TYR D 2 225 ? 125.552 98.955  141.935 1.00 20.84  ? 204 TYR D CZ    1 
ATOM   15010 O  OH    . TYR D 2 225 ? 124.287 98.450  142.133 1.00 20.77  ? 204 TYR D OH    1 
ATOM   15011 N  N     . VAL D 2 226 ? 131.142 99.163  143.571 1.00 18.76  ? 205 VAL D N     1 
ATOM   15012 C  CA    . VAL D 2 226 ? 131.351 98.080  144.528 1.00 18.85  ? 205 VAL D CA    1 
ATOM   15013 C  C     . VAL D 2 226 ? 131.679 98.657  145.904 1.00 19.19  ? 205 VAL D C     1 
ATOM   15014 O  O     . VAL D 2 226 ? 131.240 98.114  146.920 1.00 19.87  ? 205 VAL D O     1 
ATOM   15015 C  CB    . VAL D 2 226 ? 132.425 97.093  144.054 1.00 19.28  ? 205 VAL D CB    1 
ATOM   15016 C  CG1   . VAL D 2 226 ? 132.674 95.990  145.118 1.00 18.22  ? 205 VAL D CG1   1 
ATOM   15017 C  CG2   . VAL D 2 226 ? 131.984 96.479  142.715 1.00 18.40  ? 205 VAL D CG2   1 
ATOM   15018 N  N     . GLY D 2 227 ? 132.420 99.766  145.925 1.00 18.53  ? 206 GLY D N     1 
ATOM   15019 C  CA    . GLY D 2 227 ? 132.705 100.495 147.176 1.00 18.74  ? 206 GLY D CA    1 
ATOM   15020 C  C     . GLY D 2 227 ? 131.466 100.929 147.939 1.00 19.17  ? 206 GLY D C     1 
ATOM   15021 O  O     . GLY D 2 227 ? 131.417 100.838 149.174 1.00 18.66  ? 206 GLY D O     1 
ATOM   15022 N  N     . LEU D 2 228 ? 130.465 101.420 147.211 1.00 19.00  ? 207 LEU D N     1 
ATOM   15023 C  CA    . LEU D 2 228 ? 129.206 101.830 147.836 1.00 19.73  ? 207 LEU D CA    1 
ATOM   15024 C  C     . LEU D 2 228 ? 128.450 100.621 148.402 1.00 19.76  ? 207 LEU D C     1 
ATOM   15025 O  O     . LEU D 2 228 ? 127.891 100.696 149.495 1.00 20.07  ? 207 LEU D O     1 
ATOM   15026 C  CB    . LEU D 2 228 ? 128.345 102.630 146.856 1.00 19.36  ? 207 LEU D CB    1 
ATOM   15027 C  CG    . LEU D 2 228 ? 128.882 104.025 146.494 1.00 20.50  ? 207 LEU D CG    1 
ATOM   15028 C  CD1   . LEU D 2 228 ? 128.106 104.610 145.328 1.00 19.87  ? 207 LEU D CD1   1 
ATOM   15029 C  CD2   . LEU D 2 228 ? 128.840 104.988 147.715 1.00 22.38  ? 207 LEU D CD2   1 
ATOM   15030 N  N     . LEU D 2 229 ? 128.473 99.499  147.682 1.00 19.27  ? 208 LEU D N     1 
ATOM   15031 C  CA    . LEU D 2 229 ? 127.878 98.249  148.189 1.00 19.47  ? 208 LEU D CA    1 
ATOM   15032 C  C     . LEU D 2 229 ? 128.572 97.730  149.455 1.00 19.67  ? 208 LEU D C     1 
ATOM   15033 O  O     . LEU D 2 229 ? 127.916 97.189  150.353 1.00 19.82  ? 208 LEU D O     1 
ATOM   15034 C  CB    . LEU D 2 229 ? 127.874 97.152  147.104 1.00 19.51  ? 208 LEU D CB    1 
ATOM   15035 C  CG    . LEU D 2 229 ? 127.099 97.383  145.796 1.00 19.48  ? 208 LEU D CG    1 
ATOM   15036 C  CD1   . LEU D 2 229 ? 127.366 96.233  144.808 1.00 20.14  ? 208 LEU D CD1   1 
ATOM   15037 C  CD2   . LEU D 2 229 ? 125.583 97.582  146.016 1.00 19.95  ? 208 LEU D CD2   1 
ATOM   15038 N  N     . ALA D 2 230 ? 129.895 97.884  149.524 1.00 19.43  ? 209 ALA D N     1 
ATOM   15039 C  CA    . ALA D 2 230 ? 130.657 97.519  150.726 1.00 20.29  ? 209 ALA D CA    1 
ATOM   15040 C  C     . ALA D 2 230 ? 130.327 98.423  151.915 1.00 21.17  ? 209 ALA D C     1 
ATOM   15041 O  O     . ALA D 2 230 ? 130.154 97.941  153.030 1.00 21.73  ? 209 ALA D O     1 
ATOM   15042 C  CB    . ALA D 2 230 ? 132.156 97.536  150.438 1.00 19.99  ? 209 ALA D CB    1 
ATOM   15043 N  N     . GLN D 2 231 ? 130.235 99.731  151.676 1.00 22.26  ? 210 GLN D N     1 
ATOM   15044 C  CA    . GLN D 2 231 ? 129.864 100.692 152.732 1.00 23.33  ? 210 GLN D CA    1 
ATOM   15045 C  C     . GLN D 2 231 ? 128.471 100.406 153.305 1.00 23.85  ? 210 GLN D C     1 
ATOM   15046 O  O     . GLN D 2 231 ? 128.250 100.560 154.503 1.00 24.91  ? 210 GLN D O     1 
ATOM   15047 C  CB    . GLN D 2 231 ? 129.913 102.133 152.216 1.00 23.49  ? 210 GLN D CB    1 
ATOM   15048 C  CG    . GLN D 2 231 ? 131.306 102.649 151.840 1.00 23.05  ? 210 GLN D CG    1 
ATOM   15049 C  CD    . GLN D 2 231 ? 131.259 104.081 151.311 1.00 24.65  ? 210 GLN D CD    1 
ATOM   15050 O  OE1   . GLN D 2 231 ? 130.683 104.961 151.950 1.00 25.85  ? 210 GLN D OE1   1 
ATOM   15051 N  NE2   . GLN D 2 231 ? 131.851 104.315 150.139 1.00 22.30  ? 210 GLN D NE2   1 
ATOM   15052 N  N     . GLU D 2 232 ? 127.537 100.011 152.445 1.00 24.36  ? 211 GLU D N     1 
ATOM   15053 C  CA    . GLU D 2 232 ? 126.211 99.587  152.889 1.00 24.83  ? 211 GLU D CA    1 
ATOM   15054 C  C     . GLU D 2 232 ? 126.286 98.454  153.918 1.00 24.34  ? 211 GLU D C     1 
ATOM   15055 O  O     . GLU D 2 232 ? 125.605 98.507  154.944 1.00 24.20  ? 211 GLU D O     1 
ATOM   15056 C  CB    . GLU D 2 232 ? 125.359 99.156  151.701 1.00 25.15  ? 211 GLU D CB    1 
ATOM   15057 C  CG    . GLU D 2 232 ? 123.903 98.955  152.032 1.00 28.55  ? 211 GLU D CG    1 
ATOM   15058 C  CD    . GLU D 2 232 ? 123.115 98.555  150.815 1.00 33.83  ? 211 GLU D CD    1 
ATOM   15059 O  OE1   . GLU D 2 232 ? 123.067 97.343  150.506 1.00 35.09  ? 211 GLU D OE1   1 
ATOM   15060 O  OE2   . GLU D 2 232 ? 122.580 99.461  150.144 1.00 35.51  ? 211 GLU D OE2   1 
ATOM   15061 N  N     . ILE D 2 233 ? 127.111 97.443  153.651 1.00 23.39  ? 212 ILE D N     1 
ATOM   15062 C  CA    . ILE D 2 233 ? 127.313 96.345  154.612 1.00 23.42  ? 212 ILE D CA    1 
ATOM   15063 C  C     . ILE D 2 233 ? 128.007 96.848  155.879 1.00 23.74  ? 212 ILE D C     1 
ATOM   15064 O  O     . ILE D 2 233 ? 127.556 96.579  156.992 1.00 24.61  ? 212 ILE D O     1 
ATOM   15065 C  CB    . ILE D 2 233 ? 128.088 95.150  153.992 1.00 22.81  ? 212 ILE D CB    1 
ATOM   15066 C  CG1   . ILE D 2 233 ? 127.254 94.486  152.887 1.00 22.94  ? 212 ILE D CG1   1 
ATOM   15067 C  CG2   . ILE D 2 233 ? 128.447 94.112  155.064 1.00 22.45  ? 212 ILE D CG2   1 
ATOM   15068 C  CD1   . ILE D 2 233 ? 128.059 93.529  151.981 1.00 22.21  ? 212 ILE D CD1   1 
ATOM   15069 N  N     . TYR D 2 234 ? 129.093 97.595  155.702 1.00 24.19  ? 213 TYR D N     1 
ATOM   15070 C  CA    . TYR D 2 234 ? 129.859 98.157  156.805 1.00 24.59  ? 213 TYR D CA    1 
ATOM   15071 C  C     . TYR D 2 234 ? 128.968 98.942  157.774 1.00 25.15  ? 213 TYR D C     1 
ATOM   15072 O  O     . TYR D 2 234 ? 129.112 98.812  158.992 1.00 24.94  ? 213 TYR D O     1 
ATOM   15073 C  CB    . TYR D 2 234 ? 130.964 99.064  156.257 1.00 24.41  ? 213 TYR D CB    1 
ATOM   15074 C  CG    . TYR D 2 234 ? 131.831 99.731  157.304 1.00 25.93  ? 213 TYR D CG    1 
ATOM   15075 C  CD1   . TYR D 2 234 ? 132.937 99.075  157.836 1.00 24.70  ? 213 TYR D CD1   1 
ATOM   15076 C  CD2   . TYR D 2 234 ? 131.547 101.026 157.756 1.00 26.11  ? 213 TYR D CD2   1 
ATOM   15077 C  CE1   . TYR D 2 234 ? 133.742 99.685  158.794 1.00 27.90  ? 213 TYR D CE1   1 
ATOM   15078 C  CE2   . TYR D 2 234 ? 132.349 101.643 158.707 1.00 27.70  ? 213 TYR D CE2   1 
ATOM   15079 C  CZ    . TYR D 2 234 ? 133.444 100.969 159.219 1.00 27.89  ? 213 TYR D CZ    1 
ATOM   15080 O  OH    . TYR D 2 234 ? 134.240 101.573 160.164 1.00 32.34  ? 213 TYR D OH    1 
ATOM   15081 N  N     . ASN D 2 235 ? 128.062 99.750  157.221 1.00 25.43  ? 214 ASN D N     1 
ATOM   15082 C  CA    . ASN D 2 235 ? 127.179 100.613 158.024 1.00 26.77  ? 214 ASN D CA    1 
ATOM   15083 C  C     . ASN D 2 235 ? 126.095 99.857  158.791 1.00 27.06  ? 214 ASN D C     1 
ATOM   15084 O  O     . ASN D 2 235 ? 125.442 100.419 159.665 1.00 27.42  ? 214 ASN D O     1 
ATOM   15085 C  CB    . ASN D 2 235 ? 126.514 101.685 157.157 1.00 26.80  ? 214 ASN D CB    1 
ATOM   15086 C  CG    . ASN D 2 235 ? 127.503 102.642 156.549 1.00 28.19  ? 214 ASN D CG    1 
ATOM   15087 O  OD1   . ASN D 2 235 ? 128.524 102.972 157.149 1.00 29.35  ? 214 ASN D OD1   1 
ATOM   15088 N  ND2   . ASN D 2 235 ? 127.199 103.106 155.348 1.00 30.84  ? 214 ASN D ND2   1 
ATOM   15089 N  N     . LYS D 2 236 ? 125.906 98.589  158.458 1.00 26.87  ? 215 LYS D N     1 
ATOM   15090 C  CA    . LYS D 2 236 ? 124.941 97.755  159.162 1.00 27.86  ? 215 LYS D CA    1 
ATOM   15091 C  C     . LYS D 2 236 ? 125.572 97.072  160.384 1.00 28.07  ? 215 LYS D C     1 
ATOM   15092 O  O     . LYS D 2 236 ? 124.890 96.368  161.127 1.00 28.22  ? 215 LYS D O     1 
ATOM   15093 C  CB    . LYS D 2 236 ? 124.342 96.714  158.216 1.00 27.52  ? 215 LYS D CB    1 
ATOM   15094 C  CG    . LYS D 2 236 ? 123.521 97.298  157.092 1.00 29.60  ? 215 LYS D CG    1 
ATOM   15095 C  CD    . LYS D 2 236 ? 122.482 96.313  156.581 1.00 34.24  ? 215 LYS D CD    1 
ATOM   15096 C  CE    . LYS D 2 236 ? 122.906 95.594  155.315 1.00 36.75  ? 215 LYS D CE    1 
ATOM   15097 N  NZ    . LYS D 2 236 ? 124.069 94.711  155.548 1.00 40.41  ? 215 LYS D NZ    1 
ATOM   15098 N  N     . GLN D 2 237 ? 126.868 97.292  160.590 1.00 28.33  ? 216 GLN D N     1 
ATOM   15099 C  CA    . GLN D 2 237 ? 127.611 96.586  161.638 1.00 29.60  ? 216 GLN D CA    1 
ATOM   15100 C  C     . GLN D 2 237 ? 127.708 97.387  162.931 1.00 30.69  ? 216 GLN D C     1 
ATOM   15101 O  O     . GLN D 2 237 ? 127.564 98.614  162.925 1.00 30.85  ? 216 GLN D O     1 
ATOM   15102 C  CB    . GLN D 2 237 ? 129.029 96.215  161.157 1.00 29.08  ? 216 GLN D CB    1 
ATOM   15103 C  CG    . GLN D 2 237 ? 129.103 95.450  159.832 1.00 27.78  ? 216 GLN D CG    1 
ATOM   15104 C  CD    . GLN D 2 237 ? 128.170 94.251  159.774 1.00 28.38  ? 216 GLN D CD    1 
ATOM   15105 O  OE1   . GLN D 2 237 ? 128.162 93.411  160.672 1.00 29.30  ? 216 GLN D OE1   1 
ATOM   15106 N  NE2   . GLN D 2 237 ? 127.385 94.162  158.705 1.00 26.88  ? 216 GLN D NE2   1 
ATOM   15107 N  N     . THR D 2 238 ? 127.968 96.682  164.031 1.00 32.02  ? 217 THR D N     1 
ATOM   15108 C  CA    . THR D 2 238 ? 128.258 97.319  165.320 1.00 33.47  ? 217 THR D CA    1 
ATOM   15109 C  C     . THR D 2 238 ? 129.577 98.095  165.267 1.00 34.29  ? 217 THR D C     1 
ATOM   15110 O  O     . THR D 2 238 ? 130.353 97.974  164.305 1.00 33.78  ? 217 THR D O     1 
ATOM   15111 C  CB    . THR D 2 238 ? 128.335 96.271  166.466 1.00 34.00  ? 217 THR D CB    1 
ATOM   15112 O  OG1   . THR D 2 238 ? 129.458 95.402  166.254 1.00 34.33  ? 217 THR D OG1   1 
ATOM   15113 C  CG2   . THR D 2 238 ? 127.046 95.434  166.535 1.00 33.53  ? 217 THR D CG2   1 
ATOM   15114 N  N     . GLU D 2 239 ? 129.845 98.881  166.305 1.00 35.45  ? 218 GLU D N     1 
ATOM   15115 C  CA    . GLU D 2 239 ? 131.085 99.649  166.363 1.00 36.37  ? 218 GLU D CA    1 
ATOM   15116 C  C     . GLU D 2 239 ? 132.321 98.759  166.477 1.00 36.29  ? 218 GLU D C     1 
ATOM   15117 O  O     . GLU D 2 239 ? 133.344 99.035  165.843 1.00 36.18  ? 218 GLU D O     1 
ATOM   15118 C  CB    . GLU D 2 239 ? 131.042 100.694 167.482 1.00 37.27  ? 218 GLU D CB    1 
ATOM   15119 C  CG    . GLU D 2 239 ? 130.061 101.848 167.204 1.00 39.45  ? 218 GLU D CG    1 
ATOM   15120 C  CD    . GLU D 2 239 ? 130.336 102.572 165.888 1.00 41.22  ? 218 GLU D CD    1 
ATOM   15121 O  OE1   . GLU D 2 239 ? 131.509 102.902 165.608 1.00 42.62  ? 218 GLU D OE1   1 
ATOM   15122 O  OE2   . GLU D 2 239 ? 129.373 102.813 165.128 1.00 41.24  ? 218 GLU D OE2   1 
ATOM   15123 N  N     . GLU D 2 240 ? 132.221 97.689  167.263 1.00 36.66  ? 219 GLU D N     1 
ATOM   15124 C  CA    . GLU D 2 240 ? 133.331 96.743  167.407 1.00 37.01  ? 219 GLU D CA    1 
ATOM   15125 C  C     . GLU D 2 240 ? 133.592 96.001  166.096 1.00 35.85  ? 219 GLU D C     1 
ATOM   15126 O  O     . GLU D 2 240 ? 134.749 95.811  165.711 1.00 35.62  ? 219 GLU D O     1 
ATOM   15127 C  CB    . GLU D 2 240 ? 133.081 95.743  168.546 1.00 37.98  ? 219 GLU D CB    1 
ATOM   15128 C  CG    . GLU D 2 240 ? 134.271 94.803  168.795 1.00 40.87  ? 219 GLU D CG    1 
ATOM   15129 C  CD    . GLU D 2 240 ? 134.049 93.787  169.913 1.00 44.58  ? 219 GLU D CD    1 
ATOM   15130 O  OE1   . GLU D 2 240 ? 132.880 93.427  170.197 1.00 45.86  ? 219 GLU D OE1   1 
ATOM   15131 O  OE2   . GLU D 2 240 ? 135.063 93.346  170.508 1.00 45.75  ? 219 GLU D OE2   1 
ATOM   15132 N  N     . LYS D 2 241 ? 132.515 95.587  165.428 1.00 34.54  ? 220 LYS D N     1 
ATOM   15133 C  CA    . LYS D 2 241 ? 132.612 94.893  164.143 1.00 33.65  ? 220 LYS D CA    1 
ATOM   15134 C  C     . LYS D 2 241 ? 133.179 95.819  163.059 1.00 32.67  ? 220 LYS D C     1 
ATOM   15135 O  O     . LYS D 2 241 ? 133.967 95.375  162.228 1.00 32.05  ? 220 LYS D O     1 
ATOM   15136 C  CB    . LYS D 2 241 ? 131.255 94.315  163.725 1.00 33.30  ? 220 LYS D CB    1 
ATOM   15137 C  CG    . LYS D 2 241 ? 131.270 93.428  162.466 1.00 34.50  ? 220 LYS D CG    1 
ATOM   15138 C  CD    . LYS D 2 241 ? 132.166 92.191  162.613 1.00 36.30  ? 220 LYS D CD    1 
ATOM   15139 C  CE    . LYS D 2 241 ? 131.571 91.172  163.578 1.00 38.44  ? 220 LYS D CE    1 
ATOM   15140 N  NZ    . LYS D 2 241 ? 132.624 90.283  164.138 1.00 39.28  ? 220 LYS D NZ    1 
ATOM   15141 N  N     . LYS D 2 242 ? 132.776 97.093  163.080 1.00 31.90  ? 221 LYS D N     1 
ATOM   15142 C  CA    . LYS D 2 242 ? 133.323 98.099  162.169 1.00 31.28  ? 221 LYS D CA    1 
ATOM   15143 C  C     . LYS D 2 242 ? 134.835 98.238  162.331 1.00 31.32  ? 221 LYS D C     1 
ATOM   15144 O  O     . LYS D 2 242 ? 135.563 98.191  161.347 1.00 30.72  ? 221 LYS D O     1 
ATOM   15145 C  CB    . LYS D 2 242 ? 132.652 99.466  162.371 1.00 31.38  ? 221 LYS D CB    1 
ATOM   15146 C  CG    . LYS D 2 242 ? 131.312 99.630  161.663 1.00 30.64  ? 221 LYS D CG    1 
ATOM   15147 C  CD    . LYS D 2 242 ? 130.742 101.024 161.923 1.00 32.51  ? 221 LYS D CD    1 
ATOM   15148 C  CE    . LYS D 2 242 ? 129.425 101.218 161.203 1.00 32.66  ? 221 LYS D CE    1 
ATOM   15149 N  NZ    . LYS D 2 242 ? 128.762 102.465 161.644 1.00 35.31  ? 221 LYS D NZ    1 
ATOM   15150 N  N     . ALA D 2 243 ? 135.297 98.412  163.574 1.00 31.62  ? 222 ALA D N     1 
ATOM   15151 C  CA    . ALA D 2 243 ? 136.730 98.515  163.871 1.00 31.66  ? 222 ALA D CA    1 
ATOM   15152 C  C     . ALA D 2 243 ? 137.509 97.293  163.370 1.00 31.52  ? 222 ALA D C     1 
ATOM   15153 O  O     . ALA D 2 243 ? 138.645 97.413  162.903 1.00 31.41  ? 222 ALA D O     1 
ATOM   15154 C  CB    . ALA D 2 243 ? 136.951 98.726  165.374 1.00 31.89  ? 222 ALA D CB    1 
ATOM   15155 N  N     . GLU D 2 244 ? 136.869 96.130  163.454 1.00 31.35  ? 223 GLU D N     1 
ATOM   15156 C  CA    . GLU D 2 244 ? 137.430 94.864  163.012 1.00 31.54  ? 223 GLU D CA    1 
ATOM   15157 C  C     . GLU D 2 244 ? 137.518 94.785  161.470 1.00 30.63  ? 223 GLU D C     1 
ATOM   15158 O  O     . GLU D 2 244 ? 138.504 94.284  160.911 1.00 29.47  ? 223 GLU D O     1 
ATOM   15159 C  CB    . GLU D 2 244 ? 136.550 93.755  163.567 1.00 32.45  ? 223 GLU D CB    1 
ATOM   15160 C  CG    . GLU D 2 244 ? 137.094 92.361  163.501 1.00 35.31  ? 223 GLU D CG    1 
ATOM   15161 C  CD    . GLU D 2 244 ? 136.279 91.419  164.364 1.00 38.36  ? 223 GLU D CD    1 
ATOM   15162 O  OE1   . GLU D 2 244 ? 136.327 91.554  165.605 1.00 41.93  ? 223 GLU D OE1   1 
ATOM   15163 O  OE2   . GLU D 2 244 ? 135.579 90.549  163.808 1.00 39.37  ? 223 GLU D OE2   1 
ATOM   15164 N  N     . LEU D 2 245 ? 136.485 95.288  160.801 1.00 29.62  ? 224 LEU D N     1 
ATOM   15165 C  CA    . LEU D 2 245 ? 136.475 95.382  159.344 1.00 29.44  ? 224 LEU D CA    1 
ATOM   15166 C  C     . LEU D 2 245 ? 137.474 96.414  158.818 1.00 28.99  ? 224 LEU D C     1 
ATOM   15167 O  O     . LEU D 2 245 ? 138.068 96.207  157.763 1.00 28.63  ? 224 LEU D O     1 
ATOM   15168 C  CB    . LEU D 2 245 ? 135.062 95.682  158.831 1.00 29.06  ? 224 LEU D CB    1 
ATOM   15169 C  CG    . LEU D 2 245 ? 134.019 94.574  159.013 1.00 29.27  ? 224 LEU D CG    1 
ATOM   15170 C  CD1   . LEU D 2 245 ? 132.694 95.020  158.403 1.00 30.76  ? 224 LEU D CD1   1 
ATOM   15171 C  CD2   . LEU D 2 245 ? 134.468 93.258  158.386 1.00 28.11  ? 224 LEU D CD2   1 
ATOM   15172 N  N     . ARG D 2 246 ? 137.655 97.515  159.550 1.00 29.31  ? 225 ARG D N     1 
ATOM   15173 C  CA    . ARG D 2 246 ? 138.678 98.508  159.210 1.00 29.86  ? 225 ARG D CA    1 
ATOM   15174 C  C     . ARG D 2 246 ? 140.075 97.909  159.305 1.00 29.23  ? 225 ARG D C     1 
ATOM   15175 O  O     . ARG D 2 246 ? 140.902 98.125  158.430 1.00 28.95  ? 225 ARG D O     1 
ATOM   15176 C  CB    . ARG D 2 246 ? 138.613 99.740  160.121 1.00 30.56  ? 225 ARG D CB    1 
ATOM   15177 C  CG    . ARG D 2 246 ? 137.492 100.702 159.804 1.00 33.71  ? 225 ARG D CG    1 
ATOM   15178 C  CD    . ARG D 2 246 ? 137.770 102.121 160.336 1.00 37.42  ? 225 ARG D CD    1 
ATOM   15179 N  NE    . ARG D 2 246 ? 138.048 102.165 161.776 1.00 39.17  ? 225 ARG D NE    1 
ATOM   15180 C  CZ    . ARG D 2 246 ? 137.130 102.101 162.742 1.00 40.68  ? 225 ARG D CZ    1 
ATOM   15181 N  NH1   . ARG D 2 246 ? 137.513 102.153 164.014 1.00 40.28  ? 225 ARG D NH1   1 
ATOM   15182 N  NH2   . ARG D 2 246 ? 135.837 101.974 162.453 1.00 41.65  ? 225 ARG D NH2   1 
ATOM   15183 N  N     . GLU D 2 247 ? 140.330 97.174  160.380 1.00 28.89  ? 226 GLU D N     1 
ATOM   15184 C  CA    . GLU D 2 247 ? 141.611 96.498  160.557 1.00 29.27  ? 226 GLU D CA    1 
ATOM   15185 C  C     . GLU D 2 247 ? 141.858 95.502  159.424 1.00 27.84  ? 226 GLU D C     1 
ATOM   15186 O  O     . GLU D 2 247 ? 142.971 95.444  158.894 1.00 27.37  ? 226 GLU D O     1 
ATOM   15187 C  CB    . GLU D 2 247 ? 141.700 95.812  161.931 1.00 30.21  ? 226 GLU D CB    1 
ATOM   15188 C  CG    . GLU D 2 247 ? 142.973 94.973  162.156 1.00 34.46  ? 226 GLU D CG    1 
ATOM   15189 C  CD    . GLU D 2 247 ? 144.258 95.789  162.032 1.00 40.77  ? 226 GLU D CD    1 
ATOM   15190 O  OE1   . GLU D 2 247 ? 144.453 96.719  162.850 1.00 44.03  ? 226 GLU D OE1   1 
ATOM   15191 O  OE2   . GLU D 2 247 ? 145.074 95.505  161.119 1.00 42.98  ? 226 GLU D OE2   1 
ATOM   15192 N  N     . PHE D 2 248 ? 140.826 94.741  159.050 1.00 26.73  ? 227 PHE D N     1 
ATOM   15193 C  CA    . PHE D 2 248 ? 140.909 93.829  157.902 1.00 26.15  ? 227 PHE D CA    1 
ATOM   15194 C  C     . PHE D 2 248 ? 141.334 94.565  156.628 1.00 25.33  ? 227 PHE D C     1 
ATOM   15195 O  O     . PHE D 2 248 ? 142.244 94.120  155.934 1.00 24.70  ? 227 PHE D O     1 
ATOM   15196 C  CB    . PHE D 2 248 ? 139.591 93.079  157.628 1.00 26.02  ? 227 PHE D CB    1 
ATOM   15197 C  CG    . PHE D 2 248 ? 139.537 92.434  156.243 1.00 25.61  ? 227 PHE D CG    1 
ATOM   15198 C  CD1   . PHE D 2 248 ? 140.069 91.167  156.028 1.00 26.51  ? 227 PHE D CD1   1 
ATOM   15199 C  CD2   . PHE D 2 248 ? 138.988 93.120  155.156 1.00 26.21  ? 227 PHE D CD2   1 
ATOM   15200 C  CE1   . PHE D 2 248 ? 140.048 90.579  154.763 1.00 26.16  ? 227 PHE D CE1   1 
ATOM   15201 C  CE2   . PHE D 2 248 ? 138.963 92.544  153.878 1.00 26.07  ? 227 PHE D CE2   1 
ATOM   15202 C  CZ    . PHE D 2 248 ? 139.500 91.267  153.686 1.00 25.82  ? 227 PHE D CZ    1 
ATOM   15203 N  N     . ALA D 2 249 ? 140.653 95.673  156.328 1.00 24.83  ? 228 ALA D N     1 
ATOM   15204 C  CA    . ALA D 2 249 ? 140.889 96.443  155.099 1.00 24.08  ? 228 ALA D CA    1 
ATOM   15205 C  C     . ALA D 2 249 ? 142.310 97.025  155.050 1.00 23.93  ? 228 ALA D C     1 
ATOM   15206 O  O     . ALA D 2 249 ? 142.974 96.969  154.013 1.00 22.51  ? 228 ALA D O     1 
ATOM   15207 C  CB    . ALA D 2 249 ? 139.854 97.567  154.978 1.00 24.18  ? 228 ALA D CB    1 
ATOM   15208 N  N     . ILE D 2 250 ? 142.762 97.584  156.173 1.00 24.20  ? 229 ILE D N     1 
ATOM   15209 C  CA    . ILE D 2 250 ? 144.098 98.176  156.255 1.00 24.86  ? 229 ILE D CA    1 
ATOM   15210 C  C     . ILE D 2 250 ? 145.182 97.095  156.175 1.00 24.68  ? 229 ILE D C     1 
ATOM   15211 O  O     . ILE D 2 250 ? 146.183 97.271  155.492 1.00 24.30  ? 229 ILE D O     1 
ATOM   15212 C  CB    . ILE D 2 250 ? 144.270 99.073  157.531 1.00 25.44  ? 229 ILE D CB    1 
ATOM   15213 C  CG1   . ILE D 2 250 ? 143.240 100.219 157.567 1.00 26.49  ? 229 ILE D CG1   1 
ATOM   15214 C  CG2   . ILE D 2 250 ? 145.697 99.626  157.647 1.00 27.13  ? 229 ILE D CG2   1 
ATOM   15215 C  CD1   . ILE D 2 250 ? 143.188 101.103 156.319 1.00 28.58  ? 229 ILE D CD1   1 
ATOM   15216 N  N     . ASP D 2 251 ? 144.972 95.977  156.873 1.00 24.90  ? 230 ASP D N     1 
ATOM   15217 C  CA    . ASP D 2 251 ? 145.899 94.852  156.837 1.00 25.04  ? 230 ASP D CA    1 
ATOM   15218 C  C     . ASP D 2 251 ? 146.032 94.296  155.407 1.00 24.25  ? 230 ASP D C     1 
ATOM   15219 O  O     . ASP D 2 251 ? 147.144 94.066  154.925 1.00 23.60  ? 230 ASP D O     1 
ATOM   15220 C  CB    . ASP D 2 251 ? 145.430 93.761  157.806 1.00 26.23  ? 230 ASP D CB    1 
ATOM   15221 C  CG    . ASP D 2 251 ? 146.268 92.504  157.732 1.00 28.91  ? 230 ASP D CG    1 
ATOM   15222 O  OD1   . ASP D 2 251 ? 147.452 92.533  158.127 1.00 32.03  ? 230 ASP D OD1   1 
ATOM   15223 O  OD2   . ASP D 2 251 ? 145.726 91.468  157.297 1.00 33.16  ? 230 ASP D OD2   1 
ATOM   15224 N  N     . LEU D 2 252 ? 144.898 94.080  154.745 1.00 23.43  ? 231 LEU D N     1 
ATOM   15225 C  CA    . LEU D 2 252 ? 144.897 93.636  153.354 1.00 22.79  ? 231 LEU D CA    1 
ATOM   15226 C  C     . LEU D 2 252 ? 145.621 94.641  152.452 1.00 22.71  ? 231 LEU D C     1 
ATOM   15227 O  O     . LEU D 2 252 ? 146.439 94.252  151.610 1.00 21.58  ? 231 LEU D O     1 
ATOM   15228 C  CB    . LEU D 2 252 ? 143.468 93.413  152.847 1.00 22.48  ? 231 LEU D CB    1 
ATOM   15229 C  CG    . LEU D 2 252 ? 143.346 92.938  151.386 1.00 21.05  ? 231 LEU D CG    1 
ATOM   15230 C  CD1   . LEU D 2 252 ? 144.109 91.617  151.145 1.00 22.94  ? 231 LEU D CD1   1 
ATOM   15231 C  CD2   . LEU D 2 252 ? 141.887 92.774  150.986 1.00 19.31  ? 231 LEU D CD2   1 
ATOM   15232 N  N     . LEU D 2 253 ? 145.312 95.926  152.629 1.00 22.90  ? 232 LEU D N     1 
ATOM   15233 C  CA    . LEU D 2 253 ? 145.962 96.974  151.828 1.00 23.78  ? 232 LEU D CA    1 
ATOM   15234 C  C     . LEU D 2 253 ? 147.486 96.923  151.991 1.00 23.75  ? 232 LEU D C     1 
ATOM   15235 O  O     . LEU D 2 253 ? 148.221 96.996  151.005 1.00 23.26  ? 232 LEU D O     1 
ATOM   15236 C  CB    . LEU D 2 253 ? 145.454 98.366  152.210 1.00 24.03  ? 232 LEU D CB    1 
ATOM   15237 C  CG    . LEU D 2 253 ? 146.249 99.530  151.589 1.00 26.46  ? 232 LEU D CG    1 
ATOM   15238 C  CD1   . LEU D 2 253 ? 145.952 99.631  150.111 1.00 26.52  ? 232 LEU D CD1   1 
ATOM   15239 C  CD2   . LEU D 2 253 ? 145.944 100.861 152.281 1.00 27.50  ? 232 LEU D CD2   1 
ATOM   15240 N  N     . ASN D 2 254 ? 147.941 96.824  153.241 1.00 24.63  ? 233 ASN D N     1 
ATOM   15241 C  CA    . ASN D 2 254 ? 149.369 96.699  153.547 1.00 25.49  ? 233 ASN D CA    1 
ATOM   15242 C  C     . ASN D 2 254 ? 150.051 95.515  152.845 1.00 24.94  ? 233 ASN D C     1 
ATOM   15243 O  O     . ASN D 2 254 ? 151.145 95.674  152.299 1.00 24.64  ? 233 ASN D O     1 
ATOM   15244 C  CB    . ASN D 2 254 ? 149.596 96.598  155.052 1.00 26.98  ? 233 ASN D CB    1 
ATOM   15245 C  CG    . ASN D 2 254 ? 149.686 97.952  155.719 1.00 29.94  ? 233 ASN D CG    1 
ATOM   15246 O  OD1   . ASN D 2 254 ? 150.290 98.891  155.183 1.00 34.55  ? 233 ASN D OD1   1 
ATOM   15247 N  ND2   . ASN D 2 254 ? 149.098 98.063  156.903 1.00 33.81  ? 233 ASN D ND2   1 
ATOM   15248 N  N     . GLN D 2 255 ? 149.413 94.344  152.875 1.00 24.08  ? 234 GLN D N     1 
ATOM   15249 C  CA    . GLN D 2 255 ? 149.976 93.156  152.227 1.00 24.35  ? 234 GLN D CA    1 
ATOM   15250 C  C     . GLN D 2 255 ? 150.106 93.389  150.733 1.00 23.26  ? 234 GLN D C     1 
ATOM   15251 O  O     . GLN D 2 255 ? 151.164 93.118  150.156 1.00 23.12  ? 234 GLN D O     1 
ATOM   15252 C  CB    . GLN D 2 255 ? 149.115 91.907  152.454 1.00 24.84  ? 234 GLN D CB    1 
ATOM   15253 C  CG    . GLN D 2 255 ? 149.148 91.324  153.849 1.00 27.45  ? 234 GLN D CG    1 
ATOM   15254 C  CD    . GLN D 2 255 ? 150.551 90.986  154.321 1.00 32.02  ? 234 GLN D CD    1 
ATOM   15255 O  OE1   . GLN D 2 255 ? 151.022 91.542  155.311 1.00 35.80  ? 234 GLN D OE1   1 
ATOM   15256 N  NE2   . GLN D 2 255 ? 151.225 90.072  153.620 1.00 32.12  ? 234 GLN D NE2   1 
ATOM   15257 N  N     . LEU D 2 256 ? 149.032 93.893  150.122 1.00 21.77  ? 235 LEU D N     1 
ATOM   15258 C  CA    . LEU D 2 256 ? 149.015 94.152  148.680 1.00 21.68  ? 235 LEU D CA    1 
ATOM   15259 C  C     . LEU D 2 256 ? 150.012 95.245  148.309 1.00 21.49  ? 235 LEU D C     1 
ATOM   15260 O  O     . LEU D 2 256 ? 150.707 95.136  147.305 1.00 20.89  ? 235 LEU D O     1 
ATOM   15261 C  CB    . LEU D 2 256 ? 147.607 94.540  148.187 1.00 20.49  ? 235 LEU D CB    1 
ATOM   15262 C  CG    . LEU D 2 256 ? 146.536 93.441  148.227 1.00 21.52  ? 235 LEU D CG    1 
ATOM   15263 C  CD1   . LEU D 2 256 ? 145.133 93.999  147.929 1.00 20.71  ? 235 LEU D CD1   1 
ATOM   15264 C  CD2   . LEU D 2 256 ? 146.857 92.306  147.265 1.00 20.74  ? 235 LEU D CD2   1 
ATOM   15265 N  N     . TYR D 2 257 ? 150.077 96.292  149.131 1.00 21.42  ? 236 TYR D N     1 
ATOM   15266 C  CA    . TYR D 2 257 ? 150.991 97.402  148.864 1.00 22.02  ? 236 TYR D CA    1 
ATOM   15267 C  C     . TYR D 2 257 ? 152.458 96.971  148.885 1.00 22.61  ? 236 TYR D C     1 
ATOM   15268 O  O     . TYR D 2 257 ? 153.235 97.365  148.014 1.00 22.19  ? 236 TYR D O     1 
ATOM   15269 C  CB    . TYR D 2 257 ? 150.750 98.558  149.830 1.00 22.06  ? 236 TYR D CB    1 
ATOM   15270 C  CG    . TYR D 2 257 ? 151.764 99.673  149.716 1.00 23.44  ? 236 TYR D CG    1 
ATOM   15271 C  CD1   . TYR D 2 257 ? 151.834 100.470 148.567 1.00 24.01  ? 236 TYR D CD1   1 
ATOM   15272 C  CD2   . TYR D 2 257 ? 152.647 99.938  150.761 1.00 25.22  ? 236 TYR D CD2   1 
ATOM   15273 C  CE1   . TYR D 2 257 ? 152.766 101.501 148.466 1.00 25.14  ? 236 TYR D CE1   1 
ATOM   15274 C  CE2   . TYR D 2 257 ? 153.589 100.959 150.666 1.00 26.71  ? 236 TYR D CE2   1 
ATOM   15275 C  CZ    . TYR D 2 257 ? 153.639 101.736 149.522 1.00 25.35  ? 236 TYR D CZ    1 
ATOM   15276 O  OH    . TYR D 2 257 ? 154.563 102.745 149.447 1.00 26.77  ? 236 TYR D OH    1 
ATOM   15277 N  N     . GLU D 2 258 ? 152.836 96.156  149.866 1.00 23.09  ? 237 GLU D N     1 
ATOM   15278 C  CA    . GLU D 2 258 ? 154.230 95.717  149.957 1.00 23.98  ? 237 GLU D CA    1 
ATOM   15279 C  C     . GLU D 2 258 ? 154.621 94.838  148.769 1.00 23.13  ? 237 GLU D C     1 
ATOM   15280 O  O     . GLU D 2 258 ? 155.728 94.955  148.250 1.00 23.02  ? 237 GLU D O     1 
ATOM   15281 C  CB    . GLU D 2 258 ? 154.521 95.034  151.301 1.00 25.20  ? 237 GLU D CB    1 
ATOM   15282 C  CG    . GLU D 2 258 ? 154.416 95.983  152.508 1.00 28.82  ? 237 GLU D CG    1 
ATOM   15283 C  CD    . GLU D 2 258 ? 155.538 97.027  152.590 1.00 34.48  ? 237 GLU D CD    1 
ATOM   15284 O  OE1   . GLU D 2 258 ? 156.673 96.765  152.112 1.00 37.75  ? 237 GLU D OE1   1 
ATOM   15285 O  OE2   . GLU D 2 258 ? 155.288 98.121  153.153 1.00 37.16  ? 237 GLU D OE2   1 
ATOM   15286 N  N     . ASN D 2 259 ? 153.702 93.991  148.325 1.00 22.12  ? 238 ASN D N     1 
ATOM   15287 C  CA    . ASN D 2 259 ? 153.897 93.216  147.099 1.00 22.35  ? 238 ASN D CA    1 
ATOM   15288 C  C     . ASN D 2 259 ? 153.927 94.087  145.815 1.00 22.11  ? 238 ASN D C     1 
ATOM   15289 O  O     . ASN D 2 259 ? 154.693 93.799  144.892 1.00 22.24  ? 238 ASN D O     1 
ATOM   15290 C  CB    . ASN D 2 259 ? 152.841 92.110  146.992 1.00 21.69  ? 238 ASN D CB    1 
ATOM   15291 C  CG    . ASN D 2 259 ? 153.028 91.242  145.760 1.00 23.38  ? 238 ASN D CG    1 
ATOM   15292 O  OD1   . ASN D 2 259 ? 153.960 90.426  145.689 1.00 23.95  ? 238 ASN D OD1   1 
ATOM   15293 N  ND2   . ASN D 2 259 ? 152.155 91.420  144.779 1.00 21.14  ? 238 ASN D ND2   1 
ATOM   15294 N  N     . GLU D 2 260 ? 153.104 95.141  145.767 1.00 21.95  ? 239 GLU D N     1 
ATOM   15295 C  CA    . GLU D 2 260 ? 153.120 96.105  144.647 1.00 22.50  ? 239 GLU D CA    1 
ATOM   15296 C  C     . GLU D 2 260 ? 154.473 96.800  144.499 1.00 22.03  ? 239 GLU D C     1 
ATOM   15297 O  O     . GLU D 2 260 ? 154.914 97.073  143.387 1.00 22.03  ? 239 GLU D O     1 
ATOM   15298 C  CB    . GLU D 2 260 ? 152.051 97.201  144.810 1.00 22.90  ? 239 GLU D CB    1 
ATOM   15299 C  CG    . GLU D 2 260 ? 150.633 96.843  144.336 1.00 25.84  ? 239 GLU D CG    1 
ATOM   15300 C  CD    . GLU D 2 260 ? 150.584 96.214  142.948 1.00 28.59  ? 239 GLU D CD    1 
ATOM   15301 O  OE1   . GLU D 2 260 ? 150.853 95.001  142.838 1.00 28.18  ? 239 GLU D OE1   1 
ATOM   15302 O  OE2   . GLU D 2 260 ? 150.236 96.922  141.974 1.00 30.32  ? 239 GLU D OE2   1 
ATOM   15303 N  N     . LEU D 2 261 ? 155.106 97.118  145.623 1.00 21.50  ? 240 LEU D N     1 
ATOM   15304 C  CA    . LEU D 2 261 ? 156.418 97.757  145.588 1.00 22.03  ? 240 LEU D CA    1 
ATOM   15305 C  C     . LEU D 2 261 ? 157.427 96.830  144.935 1.00 21.52  ? 240 LEU D C     1 
ATOM   15306 O  O     . LEU D 2 261 ? 158.214 97.268  144.095 1.00 21.44  ? 240 LEU D O     1 
ATOM   15307 C  CB    . LEU D 2 261 ? 156.890 98.160  146.982 1.00 21.57  ? 240 LEU D CB    1 
ATOM   15308 C  CG    . LEU D 2 261 ? 156.045 99.166  147.763 1.00 23.22  ? 240 LEU D CG    1 
ATOM   15309 C  CD1   . LEU D 2 261 ? 156.677 99.393  149.124 1.00 23.06  ? 240 LEU D CD1   1 
ATOM   15310 C  CD2   . LEU D 2 261 ? 155.907 100.485 147.002 1.00 23.52  ? 240 LEU D CD2   1 
ATOM   15311 N  N     . GLU D 2 262 ? 157.383 95.551  145.306 1.00 21.69  ? 241 GLU D N     1 
ATOM   15312 C  CA    . GLU D 2 262 ? 158.266 94.541  144.700 1.00 22.31  ? 241 GLU D CA    1 
ATOM   15313 C  C     . GLU D 2 262 ? 157.935 94.309  143.225 1.00 21.69  ? 241 GLU D C     1 
ATOM   15314 O  O     . GLU D 2 262 ? 158.832 94.213  142.384 1.00 21.75  ? 241 GLU D O     1 
ATOM   15315 C  CB    . GLU D 2 262 ? 158.189 93.212  145.458 1.00 22.46  ? 241 GLU D CB    1 
ATOM   15316 C  CG    . GLU D 2 262 ? 158.624 93.256  146.925 1.00 25.63  ? 241 GLU D CG    1 
ATOM   15317 C  CD    . GLU D 2 262 ? 158.600 91.867  147.548 1.00 29.83  ? 241 GLU D CD    1 
ATOM   15318 O  OE1   . GLU D 2 262 ? 157.505 91.390  147.915 1.00 33.22  ? 241 GLU D OE1   1 
ATOM   15319 O  OE2   . GLU D 2 262 ? 159.668 91.236  147.646 1.00 33.36  ? 241 GLU D OE2   1 
ATOM   15320 N  N     . TYR D 2 263 ? 156.643 94.196  142.919 1.00 21.42  ? 242 TYR D N     1 
ATOM   15321 C  CA    . TYR D 2 263 ? 156.160 94.057  141.540 1.00 21.04  ? 242 TYR D CA    1 
ATOM   15322 C  C     . TYR D 2 263 ? 156.673 95.223  140.683 1.00 21.15  ? 242 TYR D C     1 
ATOM   15323 O  O     . TYR D 2 263 ? 157.105 95.034  139.546 1.00 20.32  ? 242 TYR D O     1 
ATOM   15324 C  CB    . TYR D 2 263 ? 154.624 94.034  141.536 1.00 20.95  ? 242 TYR D CB    1 
ATOM   15325 C  CG    . TYR D 2 263 ? 153.968 93.994  140.168 1.00 21.86  ? 242 TYR D CG    1 
ATOM   15326 C  CD1   . TYR D 2 263 ? 153.857 92.796  139.462 1.00 23.53  ? 242 TYR D CD1   1 
ATOM   15327 C  CD2   . TYR D 2 263 ? 153.459 95.156  139.578 1.00 21.20  ? 242 TYR D CD2   1 
ATOM   15328 C  CE1   . TYR D 2 263 ? 153.257 92.753  138.213 1.00 23.34  ? 242 TYR D CE1   1 
ATOM   15329 C  CE2   . TYR D 2 263 ? 152.856 95.120  138.325 1.00 23.11  ? 242 TYR D CE2   1 
ATOM   15330 C  CZ    . TYR D 2 263 ? 152.765 93.916  137.648 1.00 23.27  ? 242 TYR D CZ    1 
ATOM   15331 O  OH    . TYR D 2 263 ? 152.168 93.876  136.406 1.00 27.07  ? 242 TYR D OH    1 
ATOM   15332 N  N     . THR D 2 264 ? 156.597 96.424  141.253 1.00 21.12  ? 243 THR D N     1 
ATOM   15333 C  CA    . THR D 2 264 ? 156.980 97.659  140.575 1.00 21.98  ? 243 THR D CA    1 
ATOM   15334 C  C     . THR D 2 264 ? 158.469 97.675  140.240 1.00 22.32  ? 243 THR D C     1 
ATOM   15335 O  O     . THR D 2 264 ? 158.839 97.911  139.091 1.00 21.78  ? 243 THR D O     1 
ATOM   15336 C  CB    . THR D 2 264 ? 156.574 98.895  141.408 1.00 21.68  ? 243 THR D CB    1 
ATOM   15337 O  OG1   . THR D 2 264 ? 155.146 98.957  141.478 1.00 23.29  ? 243 THR D OG1   1 
ATOM   15338 C  CG2   . THR D 2 264 ? 157.114 100.206 140.805 1.00 23.16  ? 243 THR D CG2   1 
ATOM   15339 N  N     . GLU D 2 265 ? 159.316 97.399  141.232 1.00 22.48  ? 244 GLU D N     1 
ATOM   15340 C  CA    . GLU D 2 265 ? 160.760 97.365  140.986 1.00 23.73  ? 244 GLU D CA    1 
ATOM   15341 C  C     . GLU D 2 265 ? 161.125 96.308  139.955 1.00 23.85  ? 244 GLU D C     1 
ATOM   15342 O  O     . GLU D 2 265 ? 161.957 96.557  139.092 1.00 24.40  ? 244 GLU D O     1 
ATOM   15343 C  CB    . GLU D 2 265 ? 161.531 97.134  142.277 1.00 23.19  ? 244 GLU D CB    1 
ATOM   15344 C  CG    . GLU D 2 265 ? 161.538 98.357  143.154 1.00 25.08  ? 244 GLU D CG    1 
ATOM   15345 C  CD    . GLU D 2 265 ? 162.147 98.106  144.518 1.00 27.30  ? 244 GLU D CD    1 
ATOM   15346 O  OE1   . GLU D 2 265 ? 162.754 97.038  144.727 1.00 27.77  ? 244 GLU D OE1   1 
ATOM   15347 O  OE2   . GLU D 2 265 ? 162.013 98.991  145.383 1.00 28.63  ? 244 GLU D OE2   1 
ATOM   15348 N  N     . ASP D 2 266 ? 160.467 95.151  140.035 1.00 24.13  ? 245 ASP D N     1 
ATOM   15349 C  CA    . ASP D 2 266 ? 160.704 94.030  139.120 1.00 25.22  ? 245 ASP D CA    1 
ATOM   15350 C  C     . ASP D 2 266 ? 160.469 94.409  137.641 1.00 24.84  ? 245 ASP D C     1 
ATOM   15351 O  O     . ASP D 2 266 ? 161.199 93.949  136.757 1.00 25.64  ? 245 ASP D O     1 
ATOM   15352 C  CB    . ASP D 2 266 ? 159.818 92.844  139.533 1.00 25.79  ? 245 ASP D CB    1 
ATOM   15353 C  CG    . ASP D 2 266 ? 160.093 91.582  138.727 1.00 27.71  ? 245 ASP D CG    1 
ATOM   15354 O  OD1   . ASP D 2 266 ? 161.249 91.134  138.699 1.00 31.57  ? 245 ASP D OD1   1 
ATOM   15355 O  OD2   . ASP D 2 266 ? 159.145 91.018  138.139 1.00 30.29  ? 245 ASP D OD2   1 
ATOM   15356 N  N     . LEU D 2 267 ? 159.475 95.254  137.385 1.00 24.07  ? 246 LEU D N     1 
ATOM   15357 C  CA    . LEU D 2 267 ? 159.105 95.640  136.020 1.00 23.98  ? 246 LEU D CA    1 
ATOM   15358 C  C     . LEU D 2 267 ? 159.713 96.959  135.543 1.00 22.83  ? 246 LEU D C     1 
ATOM   15359 O  O     . LEU D 2 267 ? 160.098 97.076  134.373 1.00 23.00  ? 246 LEU D O     1 
ATOM   15360 C  CB    . LEU D 2 267 ? 157.575 95.723  135.875 1.00 23.82  ? 246 LEU D CB    1 
ATOM   15361 C  CG    . LEU D 2 267 ? 156.805 94.396  135.936 1.00 26.05  ? 246 LEU D CG    1 
ATOM   15362 C  CD1   . LEU D 2 267 ? 155.374 94.596  135.520 1.00 26.74  ? 246 LEU D CD1   1 
ATOM   15363 C  CD2   . LEU D 2 267 ? 157.448 93.333  135.065 1.00 28.00  ? 246 LEU D CD2   1 
ATOM   15364 N  N     . TYR D 2 268 ? 159.789 97.939  136.444 1.00 21.68  ? 247 TYR D N     1 
ATOM   15365 C  CA    . TYR D 2 268 ? 160.100 99.320  136.061 1.00 20.95  ? 247 TYR D CA    1 
ATOM   15366 C  C     . TYR D 2 268 ? 161.533 99.806  136.311 1.00 21.43  ? 247 TYR D C     1 
ATOM   15367 O  O     . TYR D 2 268 ? 161.925 100.829 135.751 1.00 20.73  ? 247 TYR D O     1 
ATOM   15368 C  CB    . TYR D 2 268 ? 159.118 100.298 136.715 1.00 20.27  ? 247 TYR D CB    1 
ATOM   15369 C  CG    . TYR D 2 268 ? 157.708 100.246 136.157 1.00 19.54  ? 247 TYR D CG    1 
ATOM   15370 C  CD1   . TYR D 2 268 ? 157.393 100.864 134.937 1.00 18.52  ? 247 TYR D CD1   1 
ATOM   15371 C  CD2   . TYR D 2 268 ? 156.694 99.581  136.839 1.00 20.62  ? 247 TYR D CD2   1 
ATOM   15372 C  CE1   . TYR D 2 268 ? 156.078 100.827 134.417 1.00 18.33  ? 247 TYR D CE1   1 
ATOM   15373 C  CE2   . TYR D 2 268 ? 155.370 99.538  136.330 1.00 20.79  ? 247 TYR D CE2   1 
ATOM   15374 C  CZ    . TYR D 2 268 ? 155.081 100.172 135.126 1.00 20.23  ? 247 TYR D CZ    1 
ATOM   15375 O  OH    . TYR D 2 268 ? 153.802 100.143 134.607 1.00 20.50  ? 247 TYR D OH    1 
ATOM   15376 N  N     . ASP D 2 269 ? 162.308 99.110  137.150 1.00 21.65  ? 248 ASP D N     1 
ATOM   15377 C  CA    . ASP D 2 269 ? 163.717 99.487  137.308 1.00 22.30  ? 248 ASP D CA    1 
ATOM   15378 C  C     . ASP D 2 269 ? 164.484 99.508  135.964 1.00 22.54  ? 248 ASP D C     1 
ATOM   15379 O  O     . ASP D 2 269 ? 165.317 100.390 135.742 1.00 22.49  ? 248 ASP D O     1 
ATOM   15380 C  CB    . ASP D 2 269 ? 164.437 98.598  138.324 1.00 22.83  ? 248 ASP D CB    1 
ATOM   15381 C  CG    . ASP D 2 269 ? 164.182 99.024  139.766 1.00 23.55  ? 248 ASP D CG    1 
ATOM   15382 O  OD1   . ASP D 2 269 ? 163.577 100.093 139.985 1.00 24.95  ? 248 ASP D OD1   1 
ATOM   15383 O  OD2   . ASP D 2 269 ? 164.589 98.282  140.688 1.00 24.47  ? 248 ASP D OD2   1 
ATOM   15384 N  N     . GLN D 2 270 ? 164.194 98.552  135.079 1.00 22.79  ? 249 GLN D N     1 
ATOM   15385 C  CA    . GLN D 2 270 ? 164.892 98.459  133.790 1.00 23.41  ? 249 GLN D CA    1 
ATOM   15386 C  C     . GLN D 2 270 ? 164.599 99.628  132.844 1.00 22.83  ? 249 GLN D C     1 
ATOM   15387 O  O     . GLN D 2 270 ? 165.322 99.829  131.871 1.00 23.75  ? 249 GLN D O     1 
ATOM   15388 C  CB    . GLN D 2 270 ? 164.614 97.125  133.089 1.00 24.02  ? 249 GLN D CB    1 
ATOM   15389 C  CG    . GLN D 2 270 ? 163.179 96.957  132.560 1.00 25.40  ? 249 GLN D CG    1 
ATOM   15390 C  CD    . GLN D 2 270 ? 162.867 95.525  132.161 1.00 29.23  ? 249 GLN D CD    1 
ATOM   15391 O  OE1   . GLN D 2 270 ? 163.400 94.578  132.743 1.00 31.31  ? 249 GLN D OE1   1 
ATOM   15392 N  NE2   . GLN D 2 270 ? 161.990 95.357  131.174 1.00 30.04  ? 249 GLN D NE2   1 
ATOM   15393 N  N     . VAL D 2 271 ? 163.533 100.381 133.120 1.00 21.93  ? 250 VAL D N     1 
ATOM   15394 C  CA    . VAL D 2 271 ? 163.223 101.587 132.347 1.00 21.29  ? 250 VAL D CA    1 
ATOM   15395 C  C     . VAL D 2 271 ? 163.258 102.861 133.212 1.00 21.16  ? 250 VAL D C     1 
ATOM   15396 O  O     . VAL D 2 271 ? 162.814 103.928 132.778 1.00 21.54  ? 250 VAL D O     1 
ATOM   15397 C  CB    . VAL D 2 271 ? 161.868 101.443 131.580 1.00 21.62  ? 250 VAL D CB    1 
ATOM   15398 C  CG1   . VAL D 2 271 ? 161.965 100.335 130.533 1.00 21.36  ? 250 VAL D CG1   1 
ATOM   15399 C  CG2   . VAL D 2 271 ? 160.700 101.180 132.548 1.00 21.17  ? 250 VAL D CG2   1 
ATOM   15400 N  N     . GLY D 2 272 ? 163.767 102.733 134.443 1.00 20.92  ? 251 GLY D N     1 
ATOM   15401 C  CA    . GLY D 2 272 ? 164.045 103.879 135.332 1.00 20.61  ? 251 GLY D CA    1 
ATOM   15402 C  C     . GLY D 2 272 ? 162.858 104.656 135.898 1.00 20.77  ? 251 GLY D C     1 
ATOM   15403 O  O     . GLY D 2 272 ? 162.990 105.840 136.244 1.00 20.28  ? 251 GLY D O     1 
ATOM   15404 N  N     . LEU D 2 273 ? 161.709 103.997 136.021 1.00 19.85  ? 252 LEU D N     1 
ATOM   15405 C  CA    . LEU D 2 273 ? 160.479 104.711 136.371 1.00 20.09  ? 252 LEU D CA    1 
ATOM   15406 C  C     . LEU D 2 273 ? 159.895 104.419 137.756 1.00 19.88  ? 252 LEU D C     1 
ATOM   15407 O  O     . LEU D 2 273 ? 158.920 105.054 138.145 1.00 20.04  ? 252 LEU D O     1 
ATOM   15408 C  CB    . LEU D 2 273 ? 159.402 104.421 135.312 1.00 19.97  ? 252 LEU D CB    1 
ATOM   15409 C  CG    . LEU D 2 273 ? 159.727 104.803 133.875 1.00 20.26  ? 252 LEU D CG    1 
ATOM   15410 C  CD1   . LEU D 2 273 ? 158.501 104.534 133.032 1.00 18.98  ? 252 LEU D CD1   1 
ATOM   15411 C  CD2   . LEU D 2 273 ? 160.171 106.287 133.751 1.00 21.03  ? 252 LEU D CD2   1 
ATOM   15412 N  N     . SER D 2 274 ? 160.500 103.482 138.488 0.50 19.54  ? 253 SER D N     1 
ATOM   15413 C  CA    . SER D 2 274 ? 159.892 102.922 139.705 0.50 19.34  ? 253 SER D CA    1 
ATOM   15414 C  C     . SER D 2 274 ? 159.487 103.950 140.767 0.50 20.05  ? 253 SER D C     1 
ATOM   15415 O  O     . SER D 2 274 ? 158.418 103.831 141.363 0.50 20.31  ? 253 SER D O     1 
ATOM   15416 C  CB    . SER D 2 274 ? 160.786 101.837 140.320 0.50 18.97  ? 253 SER D CB    1 
ATOM   15417 O  OG    . SER D 2 274 ? 161.076 100.815 139.384 0.50 15.35  ? 253 SER D OG    1 
ATOM   15418 N  N     . HIS D 2 275 ? 160.341 104.945 141.007 1.00 20.77  ? 254 HIS D N     1 
ATOM   15419 C  CA    . HIS D 2 275 ? 160.034 106.021 141.970 1.00 21.18  ? 254 HIS D CA    1 
ATOM   15420 C  C     . HIS D 2 275 ? 158.676 106.687 141.685 1.00 21.50  ? 254 HIS D C     1 
ATOM   15421 O  O     . HIS D 2 275 ? 157.835 106.822 142.589 1.00 19.88  ? 254 HIS D O     1 
ATOM   15422 C  CB    . HIS D 2 275 ? 161.149 107.079 142.013 1.00 21.60  ? 254 HIS D CB    1 
ATOM   15423 C  CG    . HIS D 2 275 ? 160.822 108.257 142.882 1.00 22.43  ? 254 HIS D CG    1 
ATOM   15424 N  ND1   . HIS D 2 275 ? 161.108 108.294 144.232 1.00 22.77  ? 254 HIS D ND1   1 
ATOM   15425 C  CD2   . HIS D 2 275 ? 160.215 109.435 142.592 1.00 22.50  ? 254 HIS D CD2   1 
ATOM   15426 C  CE1   . HIS D 2 275 ? 160.697 109.447 144.733 1.00 24.05  ? 254 HIS D CE1   1 
ATOM   15427 N  NE2   . HIS D 2 275 ? 160.146 110.154 143.760 1.00 23.22  ? 254 HIS D NE2   1 
ATOM   15428 N  N     . ASP D 2 276 ? 158.468 107.080 140.428 1.00 22.34  ? 255 ASP D N     1 
ATOM   15429 C  CA    . ASP D 2 276 ? 157.226 107.737 140.028 1.00 23.19  ? 255 ASP D CA    1 
ATOM   15430 C  C     . ASP D 2 276 ? 156.036 106.788 140.031 1.00 22.17  ? 255 ASP D C     1 
ATOM   15431 O  O     . ASP D 2 276 ? 154.929 107.203 140.343 1.00 21.87  ? 255 ASP D O     1 
ATOM   15432 C  CB    . ASP D 2 276 ? 157.355 108.396 138.646 1.00 24.33  ? 255 ASP D CB    1 
ATOM   15433 C  CG    . ASP D 2 276 ? 157.901 109.825 138.710 1.00 27.58  ? 255 ASP D CG    1 
ATOM   15434 O  OD1   . ASP D 2 276 ? 157.766 110.495 139.758 1.00 31.10  ? 255 ASP D OD1   1 
ATOM   15435 O  OD2   . ASP D 2 276 ? 158.474 110.276 137.692 1.00 29.88  ? 255 ASP D OD2   1 
ATOM   15436 N  N     . VAL D 2 277 ? 156.256 105.531 139.647 1.00 21.21  ? 256 VAL D N     1 
ATOM   15437 C  CA    . VAL D 2 277 ? 155.185 104.530 139.693 1.00 20.51  ? 256 VAL D CA    1 
ATOM   15438 C  C     . VAL D 2 277 ? 154.692 104.312 141.128 1.00 20.32  ? 256 VAL D C     1 
ATOM   15439 O  O     . VAL D 2 277 ? 153.491 104.197 141.358 1.00 19.81  ? 256 VAL D O     1 
ATOM   15440 C  CB    . VAL D 2 277 ? 155.604 103.176 139.053 1.00 20.30  ? 256 VAL D CB    1 
ATOM   15441 C  CG1   . VAL D 2 277 ? 154.491 102.151 139.190 1.00 21.16  ? 256 VAL D CG1   1 
ATOM   15442 C  CG2   . VAL D 2 277 ? 155.951 103.367 137.587 1.00 19.06  ? 256 VAL D CG2   1 
ATOM   15443 N  N     . LYS D 2 278 ? 155.626 104.278 142.078 1.00 19.84  ? 257 LYS D N     1 
ATOM   15444 C  CA    . LYS D 2 278 ? 155.287 104.132 143.494 1.00 20.27  ? 257 LYS D CA    1 
ATOM   15445 C  C     . LYS D 2 278 ? 154.380 105.260 144.002 1.00 20.16  ? 257 LYS D C     1 
ATOM   15446 O  O     . LYS D 2 278 ? 153.434 104.991 144.738 1.00 19.88  ? 257 LYS D O     1 
ATOM   15447 C  CB    . LYS D 2 278 ? 156.544 103.993 144.357 1.00 20.20  ? 257 LYS D CB    1 
ATOM   15448 C  CG    . LYS D 2 278 ? 157.223 102.635 144.214 1.00 21.60  ? 257 LYS D CG    1 
ATOM   15449 C  CD    . LYS D 2 278 ? 158.603 102.619 144.859 1.00 21.53  ? 257 LYS D CD    1 
ATOM   15450 C  CE    . LYS D 2 278 ? 159.300 101.317 144.547 1.00 24.52  ? 257 LYS D CE    1 
ATOM   15451 N  NZ    . LYS D 2 278 ? 160.647 101.265 145.204 1.00 26.32  ? 257 LYS D NZ    1 
ATOM   15452 N  N     . LYS D 2 279 ? 154.653 106.502 143.589 1.00 19.67  ? 258 LYS D N     1 
ATOM   15453 C  CA    . LYS D 2 279 ? 153.773 107.630 143.930 1.00 20.10  ? 258 LYS D CA    1 
ATOM   15454 C  C     . LYS D 2 279 ? 152.354 107.408 143.392 1.00 19.12  ? 258 LYS D C     1 
ATOM   15455 O  O     . LYS D 2 279 ? 151.377 107.699 144.085 1.00 18.59  ? 258 LYS D O     1 
ATOM   15456 C  CB    . LYS D 2 279 ? 154.330 108.972 143.418 1.00 20.54  ? 258 LYS D CB    1 
ATOM   15457 C  CG    . LYS D 2 279 ? 155.690 109.366 143.991 1.00 22.84  ? 258 LYS D CG    1 
ATOM   15458 C  CD    . LYS D 2 279 ? 155.938 110.891 143.927 1.00 24.16  ? 258 LYS D CD    1 
ATOM   15459 C  CE    . LYS D 2 279 ? 156.061 111.408 142.496 1.00 25.61  ? 258 LYS D CE    1 
ATOM   15460 N  NZ    . LYS D 2 279 ? 156.309 112.901 142.443 1.00 24.70  ? 258 LYS D NZ    1 
ATOM   15461 N  N     . PHE D 2 280 ? 152.263 106.872 142.171 1.00 19.04  ? 259 PHE D N     1 
ATOM   15462 C  CA    . PHE D 2 280 ? 150.981 106.594 141.497 1.00 19.31  ? 259 PHE D CA    1 
ATOM   15463 C  C     . PHE D 2 280 ? 150.181 105.476 142.173 1.00 19.25  ? 259 PHE D C     1 
ATOM   15464 O  O     . PHE D 2 280 ? 148.950 105.550 142.275 1.00 19.71  ? 259 PHE D O     1 
ATOM   15465 C  CB    . PHE D 2 280 ? 151.235 106.234 140.033 1.00 19.04  ? 259 PHE D CB    1 
ATOM   15466 C  CG    . PHE D 2 280 ? 150.009 106.307 139.142 1.00 20.15  ? 259 PHE D CG    1 
ATOM   15467 C  CD1   . PHE D 2 280 ? 149.263 107.472 139.046 1.00 21.63  ? 259 PHE D CD1   1 
ATOM   15468 C  CD2   . PHE D 2 280 ? 149.645 105.210 138.359 1.00 19.95  ? 259 PHE D CD2   1 
ATOM   15469 C  CE1   . PHE D 2 280 ? 148.147 107.544 138.183 1.00 22.56  ? 259 PHE D CE1   1 
ATOM   15470 C  CE2   . PHE D 2 280 ? 148.547 105.264 137.502 1.00 20.29  ? 259 PHE D CE2   1 
ATOM   15471 C  CZ    . PHE D 2 280 ? 147.793 106.435 137.415 1.00 21.30  ? 259 PHE D CZ    1 
ATOM   15472 N  N     . ILE D 2 281 ? 150.874 104.433 142.619 1.00 19.36  ? 260 ILE D N     1 
ATOM   15473 C  CA    . ILE D 2 281 ? 150.255 103.377 143.426 1.00 19.45  ? 260 ILE D CA    1 
ATOM   15474 C  C     . ILE D 2 281 ? 149.616 103.925 144.721 1.00 19.61  ? 260 ILE D C     1 
ATOM   15475 O  O     . ILE D 2 281 ? 148.468 103.594 145.025 1.00 19.72  ? 260 ILE D O     1 
ATOM   15476 C  CB    . ILE D 2 281 ? 151.291 102.265 143.734 1.00 19.49  ? 260 ILE D CB    1 
ATOM   15477 C  CG1   . ILE D 2 281 ? 151.690 101.561 142.434 1.00 20.10  ? 260 ILE D CG1   1 
ATOM   15478 C  CG2   . ILE D 2 281 ? 150.789 101.270 144.805 1.00 20.53  ? 260 ILE D CG2   1 
ATOM   15479 C  CD1   . ILE D 2 281 ? 152.944 100.694 142.601 1.00 21.17  ? 260 ILE D CD1   1 
ATOM   15480 N  N     . ARG D 2 282 ? 150.348 104.761 145.462 1.00 19.75  ? 261 ARG D N     1 
ATOM   15481 C  CA    . ARG D 2 282 ? 149.852 105.298 146.744 1.00 20.34  ? 261 ARG D CA    1 
ATOM   15482 C  C     . ARG D 2 282 ? 148.654 106.220 146.548 1.00 21.18  ? 261 ARG D C     1 
ATOM   15483 O  O     . ARG D 2 282 ? 147.685 106.185 147.320 1.00 21.68  ? 261 ARG D O     1 
ATOM   15484 C  CB    . ARG D 2 282 ? 150.966 106.016 147.517 1.00 20.20  ? 261 ARG D CB    1 
ATOM   15485 C  CG    . ARG D 2 282 ? 152.017 105.083 148.088 1.00 20.57  ? 261 ARG D CG    1 
ATOM   15486 C  CD    . ARG D 2 282 ? 153.002 105.836 148.986 1.00 23.15  ? 261 ARG D CD    1 
ATOM   15487 N  NE    . ARG D 2 282 ? 153.950 106.671 148.245 1.00 23.46  ? 261 ARG D NE    1 
ATOM   15488 C  CZ    . ARG D 2 282 ? 155.126 106.251 147.781 1.00 22.84  ? 261 ARG D CZ    1 
ATOM   15489 N  NH1   . ARG D 2 282 ? 155.922 107.099 147.143 1.00 23.37  ? 261 ARG D NH1   1 
ATOM   15490 N  NH2   . ARG D 2 282 ? 155.506 104.990 147.939 1.00 22.27  ? 261 ARG D NH2   1 
ATOM   15491 N  N     . TYR D 2 283 ? 148.741 107.057 145.520 1.00 21.46  ? 262 TYR D N     1 
ATOM   15492 C  CA    . TYR D 2 283 ? 147.654 107.958 145.143 1.00 22.97  ? 262 TYR D CA    1 
ATOM   15493 C  C     . TYR D 2 283 ? 146.375 107.151 144.821 1.00 22.12  ? 262 TYR D C     1 
ATOM   15494 O  O     . TYR D 2 283 ? 145.277 107.509 145.254 1.00 22.00  ? 262 TYR D O     1 
ATOM   15495 C  CB    . TYR D 2 283 ? 148.122 108.822 143.967 1.00 23.37  ? 262 TYR D CB    1 
ATOM   15496 C  CG    . TYR D 2 283 ? 147.054 109.570 143.206 1.00 27.31  ? 262 TYR D CG    1 
ATOM   15497 C  CD1   . TYR D 2 283 ? 146.633 110.835 143.618 1.00 30.79  ? 262 TYR D CD1   1 
ATOM   15498 C  CD2   . TYR D 2 283 ? 146.496 109.032 142.047 1.00 30.31  ? 262 TYR D CD2   1 
ATOM   15499 C  CE1   . TYR D 2 283 ? 145.646 111.536 142.906 1.00 33.18  ? 262 TYR D CE1   1 
ATOM   15500 C  CE2   . TYR D 2 283 ? 145.520 109.723 141.322 1.00 33.20  ? 262 TYR D CE2   1 
ATOM   15501 C  CZ    . TYR D 2 283 ? 145.107 110.977 141.758 1.00 34.74  ? 262 TYR D CZ    1 
ATOM   15502 O  OH    . TYR D 2 283 ? 144.148 111.662 141.036 1.00 37.63  ? 262 TYR D OH    1 
ATOM   15503 N  N     . ASN D 2 284 ? 146.527 106.037 144.110 1.00 21.63  ? 263 ASN D N     1 
ATOM   15504 C  CA    . ASN D 2 284 ? 145.375 105.205 143.772 1.00 21.41  ? 263 ASN D CA    1 
ATOM   15505 C  C     . ASN D 2 284 ? 144.887 104.334 144.934 1.00 20.86  ? 263 ASN D C     1 
ATOM   15506 O  O     . ASN D 2 284 ? 143.696 104.059 145.033 1.00 20.92  ? 263 ASN D O     1 
ATOM   15507 C  CB    . ASN D 2 284 ? 145.627 104.396 142.498 1.00 21.15  ? 263 ASN D CB    1 
ATOM   15508 C  CG    . ASN D 2 284 ? 145.546 105.261 141.247 1.00 22.59  ? 263 ASN D CG    1 
ATOM   15509 O  OD1   . ASN D 2 284 ? 144.461 105.689 140.846 1.00 22.35  ? 263 ASN D OD1   1 
ATOM   15510 N  ND2   . ASN D 2 284 ? 146.695 105.536 140.636 1.00 22.93  ? 263 ASN D ND2   1 
ATOM   15511 N  N     . ALA D 2 285 ? 145.801 103.916 145.809 1.00 20.92  ? 264 ALA D N     1 
ATOM   15512 C  CA    . ALA D 2 285 ? 145.425 103.272 147.079 1.00 20.77  ? 264 ALA D CA    1 
ATOM   15513 C  C     . ALA D 2 285 ? 144.497 104.162 147.913 1.00 21.13  ? 264 ALA D C     1 
ATOM   15514 O  O     . ALA D 2 285 ? 143.497 103.684 148.465 1.00 19.92  ? 264 ALA D O     1 
ATOM   15515 C  CB    . ALA D 2 285 ? 146.672 102.881 147.886 1.00 20.68  ? 264 ALA D CB    1 
ATOM   15516 N  N     . ASN D 2 286 ? 144.830 105.455 147.993 1.00 21.38  ? 265 ASN D N     1 
ATOM   15517 C  CA    . ASN D 2 286 ? 143.995 106.442 148.682 1.00 21.94  ? 265 ASN D CA    1 
ATOM   15518 C  C     . ASN D 2 286 ? 142.597 106.571 148.050 1.00 22.13  ? 265 ASN D C     1 
ATOM   15519 O  O     . ASN D 2 286 ? 141.608 106.704 148.760 1.00 21.95  ? 265 ASN D O     1 
ATOM   15520 C  CB    . ASN D 2 286 ? 144.675 107.812 148.710 1.00 22.22  ? 265 ASN D CB    1 
ATOM   15521 C  CG    . ASN D 2 286 ? 145.755 107.931 149.781 1.00 22.80  ? 265 ASN D CG    1 
ATOM   15522 O  OD1   . ASN D 2 286 ? 145.874 107.097 150.686 1.00 22.57  ? 265 ASN D OD1   1 
ATOM   15523 N  ND2   . ASN D 2 286 ? 146.556 108.984 149.671 1.00 23.91  ? 265 ASN D ND2   1 
ATOM   15524 N  N     . LYS D 2 287 ? 142.521 106.524 146.722 1.00 22.51  ? 266 LYS D N     1 
ATOM   15525 C  CA    . LYS D 2 287 ? 141.220 106.557 146.039 1.00 22.91  ? 266 LYS D CA    1 
ATOM   15526 C  C     . LYS D 2 287 ? 140.381 105.319 146.381 1.00 22.33  ? 266 LYS D C     1 
ATOM   15527 O  O     . LYS D 2 287 ? 139.187 105.435 146.627 1.00 22.24  ? 266 LYS D O     1 
ATOM   15528 C  CB    . LYS D 2 287 ? 141.388 106.690 144.519 1.00 23.65  ? 266 LYS D CB    1 
ATOM   15529 C  CG    . LYS D 2 287 ? 141.797 108.091 144.064 1.00 26.50  ? 266 LYS D CG    1 
ATOM   15530 C  CD    . LYS D 2 287 ? 141.931 108.148 142.531 1.00 31.30  ? 266 LYS D CD    1 
ATOM   15531 C  CE    . LYS D 2 287 ? 141.835 109.584 142.046 1.00 35.08  ? 266 LYS D CE    1 
ATOM   15532 N  NZ    . LYS D 2 287 ? 141.920 109.725 140.561 1.00 37.66  ? 266 LYS D NZ    1 
ATOM   15533 N  N     . ALA D 2 288 ? 141.023 104.150 146.408 1.00 21.41  ? 267 ALA D N     1 
ATOM   15534 C  CA    . ALA D 2 288 ? 140.378 102.886 146.765 1.00 21.53  ? 267 ALA D CA    1 
ATOM   15535 C  C     . ALA D 2 288 ? 139.814 102.922 148.196 1.00 21.77  ? 267 ALA D C     1 
ATOM   15536 O  O     . ALA D 2 288 ? 138.672 102.501 148.449 1.00 21.59  ? 267 ALA D O     1 
ATOM   15537 C  CB    . ALA D 2 288 ? 141.358 101.718 146.590 1.00 21.33  ? 267 ALA D CB    1 
ATOM   15538 N  N     . LEU D 2 289 ? 140.605 103.446 149.123 1.00 21.71  ? 268 LEU D N     1 
ATOM   15539 C  CA    . LEU D 2 289 ? 140.139 103.633 150.491 1.00 22.36  ? 268 LEU D CA    1 
ATOM   15540 C  C     . LEU D 2 289 ? 138.951 104.584 150.542 1.00 23.01  ? 268 LEU D C     1 
ATOM   15541 O  O     . LEU D 2 289 ? 137.949 104.297 151.201 1.00 23.14  ? 268 LEU D O     1 
ATOM   15542 C  CB    . LEU D 2 289 ? 141.278 104.108 151.402 1.00 22.61  ? 268 LEU D CB    1 
ATOM   15543 C  CG    . LEU D 2 289 ? 142.370 103.059 151.699 1.00 21.22  ? 268 LEU D CG    1 
ATOM   15544 C  CD1   . LEU D 2 289 ? 143.590 103.711 152.334 1.00 20.77  ? 268 LEU D CD1   1 
ATOM   15545 C  CD2   . LEU D 2 289 ? 141.844 101.911 152.590 1.00 21.40  ? 268 LEU D CD2   1 
ATOM   15546 N  N     . MET D 2 290 ? 139.037 105.702 149.829 1.00 23.87  ? 269 MET D N     1 
ATOM   15547 C  CA    . MET D 2 290 ? 137.909 106.630 149.814 1.00 25.26  ? 269 MET D CA    1 
ATOM   15548 C  C     . MET D 2 290 ? 136.643 105.987 149.222 1.00 24.37  ? 269 MET D C     1 
ATOM   15549 O  O     . MET D 2 290 ? 135.553 106.219 149.736 1.00 23.97  ? 269 MET D O     1 
ATOM   15550 C  CB    . MET D 2 290 ? 138.289 107.960 149.172 1.00 25.94  ? 269 MET D CB    1 
ATOM   15551 C  CG    . MET D 2 290 ? 139.077 108.846 150.157 1.00 31.08  ? 269 MET D CG    1 
ATOM   15552 S  SD    . MET D 2 290 ? 139.603 110.437 149.481 1.00 41.28  ? 269 MET D SD    1 
ATOM   15553 C  CE    . MET D 2 290 ? 138.039 111.093 148.844 1.00 38.56  ? 269 MET D CE    1 
ATOM   15554 N  N     . ASN D 2 291 ? 136.795 105.146 148.194 1.00 23.66  ? 270 ASN D N     1 
ATOM   15555 C  CA    . ASN D 2 291 ? 135.662 104.348 147.669 1.00 23.17  ? 270 ASN D CA    1 
ATOM   15556 C  C     . ASN D 2 291 ? 134.973 103.467 148.717 1.00 23.22  ? 270 ASN D C     1 
ATOM   15557 O  O     . ASN D 2 291 ? 133.775 103.203 148.620 1.00 22.68  ? 270 ASN D O     1 
ATOM   15558 C  CB    . ASN D 2 291 ? 136.086 103.474 146.479 1.00 22.41  ? 270 ASN D CB    1 
ATOM   15559 C  CG    . ASN D 2 291 ? 136.400 104.285 145.243 1.00 21.93  ? 270 ASN D CG    1 
ATOM   15560 O  OD1   . ASN D 2 291 ? 136.077 105.475 145.165 1.00 20.94  ? 270 ASN D OD1   1 
ATOM   15561 N  ND2   . ASN D 2 291 ? 137.036 103.647 144.263 1.00 19.20  ? 270 ASN D ND2   1 
ATOM   15562 N  N     . LEU D 2 292 ? 135.748 103.020 149.704 1.00 23.53  ? 271 LEU D N     1 
ATOM   15563 C  CA    . LEU D 2 292 ? 135.242 102.188 150.798 1.00 24.21  ? 271 LEU D CA    1 
ATOM   15564 C  C     . LEU D 2 292 ? 134.836 103.022 152.017 1.00 25.14  ? 271 LEU D C     1 
ATOM   15565 O  O     . LEU D 2 292 ? 134.559 102.476 153.097 1.00 25.14  ? 271 LEU D O     1 
ATOM   15566 C  CB    . LEU D 2 292 ? 136.288 101.121 151.187 1.00 23.71  ? 271 LEU D CB    1 
ATOM   15567 C  CG    . LEU D 2 292 ? 136.654 100.066 150.132 1.00 23.37  ? 271 LEU D CG    1 
ATOM   15568 C  CD1   . LEU D 2 292 ? 137.956 99.351  150.500 1.00 23.28  ? 271 LEU D CD1   1 
ATOM   15569 C  CD2   . LEU D 2 292 ? 135.513 99.051  149.921 1.00 23.06  ? 271 LEU D CD2   1 
ATOM   15570 N  N     . GLY D 2 293 ? 134.791 104.343 151.834 1.00 25.82  ? 272 GLY D N     1 
ATOM   15571 C  CA    . GLY D 2 293 ? 134.411 105.267 152.896 1.00 27.13  ? 272 GLY D CA    1 
ATOM   15572 C  C     . GLY D 2 293 ? 135.442 105.420 153.996 1.00 27.99  ? 272 GLY D C     1 
ATOM   15573 O  O     . GLY D 2 293 ? 135.113 105.875 155.087 1.00 27.97  ? 272 GLY D O     1 
ATOM   15574 N  N     . PHE D 2 294 ? 136.690 105.038 153.711 1.00 28.02  ? 273 PHE D N     1 
ATOM   15575 C  CA    . PHE D 2 294 ? 137.788 105.144 154.681 1.00 28.75  ? 273 PHE D CA    1 
ATOM   15576 C  C     . PHE D 2 294 ? 138.696 106.350 154.408 1.00 29.00  ? 273 PHE D C     1 
ATOM   15577 O  O     . PHE D 2 294 ? 138.719 106.876 153.297 1.00 28.74  ? 273 PHE D O     1 
ATOM   15578 C  CB    . PHE D 2 294 ? 138.632 103.859 154.678 1.00 28.32  ? 273 PHE D CB    1 
ATOM   15579 C  CG    . PHE D 2 294 ? 137.889 102.637 155.144 1.00 28.66  ? 273 PHE D CG    1 
ATOM   15580 C  CD1   . PHE D 2 294 ? 137.028 102.699 156.240 1.00 30.23  ? 273 PHE D CD1   1 
ATOM   15581 C  CD2   . PHE D 2 294 ? 138.063 101.421 154.496 1.00 26.94  ? 273 PHE D CD2   1 
ATOM   15582 C  CE1   . PHE D 2 294 ? 136.338 101.561 156.673 1.00 31.04  ? 273 PHE D CE1   1 
ATOM   15583 C  CE2   . PHE D 2 294 ? 137.389 100.284 154.917 1.00 27.39  ? 273 PHE D CE2   1 
ATOM   15584 C  CZ    . PHE D 2 294 ? 136.528 100.344 156.006 1.00 29.80  ? 273 PHE D CZ    1 
ATOM   15585 N  N     . ASP D 2 295 ? 139.436 106.777 155.428 1.00 29.60  ? 274 ASP D N     1 
ATOM   15586 C  CA    . ASP D 2 295 ? 140.391 107.874 155.293 1.00 30.40  ? 274 ASP D CA    1 
ATOM   15587 C  C     . ASP D 2 295 ? 141.607 107.466 154.438 1.00 29.58  ? 274 ASP D C     1 
ATOM   15588 O  O     . ASP D 2 295 ? 141.969 106.290 154.396 1.00 28.68  ? 274 ASP D O     1 
ATOM   15589 C  CB    . ASP D 2 295 ? 140.869 108.352 156.671 1.00 31.44  ? 274 ASP D CB    1 
ATOM   15590 C  CG    . ASP D 2 295 ? 139.756 108.977 157.504 1.00 34.27  ? 274 ASP D CG    1 
ATOM   15591 O  OD1   . ASP D 2 295 ? 138.794 109.541 156.929 1.00 36.43  ? 274 ASP D OD1   1 
ATOM   15592 O  OD2   . ASP D 2 295 ? 139.854 108.901 158.748 1.00 38.03  ? 274 ASP D OD2   1 
ATOM   15593 N  N     . PRO D 2 296 ? 142.246 108.444 153.766 1.00 29.59  ? 275 PRO D N     1 
ATOM   15594 C  CA    . PRO D 2 296 ? 143.462 108.108 153.020 1.00 29.09  ? 275 PRO D CA    1 
ATOM   15595 C  C     . PRO D 2 296 ? 144.552 107.594 153.960 1.00 29.26  ? 275 PRO D C     1 
ATOM   15596 O  O     . PRO D 2 296 ? 144.653 108.043 155.102 1.00 29.36  ? 275 PRO D O     1 
ATOM   15597 C  CB    . PRO D 2 296 ? 143.882 109.443 152.390 1.00 29.49  ? 275 PRO D CB    1 
ATOM   15598 C  CG    . PRO D 2 296 ? 143.163 110.504 153.177 1.00 30.28  ? 275 PRO D CG    1 
ATOM   15599 C  CD    . PRO D 2 296 ? 141.891 109.872 153.648 1.00 29.63  ? 275 PRO D CD    1 
ATOM   15600 N  N     . TYR D 2 297 ? 145.344 106.644 153.486 1.00 28.97  ? 276 TYR D N     1 
ATOM   15601 C  CA    . TYR D 2 297 ? 146.391 106.037 154.298 1.00 29.63  ? 276 TYR D CA    1 
ATOM   15602 C  C     . TYR D 2 297 ? 147.740 106.748 154.097 1.00 29.55  ? 276 TYR D C     1 
ATOM   15603 O  O     . TYR D 2 297 ? 148.546 106.867 155.029 1.00 30.12  ? 276 TYR D O     1 
ATOM   15604 C  CB    . TYR D 2 297 ? 146.516 104.563 153.915 1.00 29.49  ? 276 TYR D CB    1 
ATOM   15605 C  CG    . TYR D 2 297 ? 147.321 103.715 154.864 1.00 31.19  ? 276 TYR D CG    1 
ATOM   15606 C  CD1   . TYR D 2 297 ? 146.910 103.537 156.189 1.00 31.93  ? 276 TYR D CD1   1 
ATOM   15607 C  CD2   . TYR D 2 297 ? 148.481 103.068 154.436 1.00 31.98  ? 276 TYR D CD2   1 
ATOM   15608 C  CE1   . TYR D 2 297 ? 147.641 102.750 157.069 1.00 33.86  ? 276 TYR D CE1   1 
ATOM   15609 C  CE2   . TYR D 2 297 ? 149.221 102.270 155.311 1.00 33.88  ? 276 TYR D CE2   1 
ATOM   15610 C  CZ    . TYR D 2 297 ? 148.786 102.117 156.622 1.00 34.42  ? 276 TYR D CZ    1 
ATOM   15611 O  OH    . TYR D 2 297 ? 149.502 101.343 157.500 1.00 37.63  ? 276 TYR D OH    1 
ATOM   15612 N  N     . PHE D 2 298 ? 147.964 107.209 152.872 1.00 29.10  ? 277 PHE D N     1 
ATOM   15613 C  CA    . PHE D 2 298 ? 149.237 107.784 152.450 1.00 28.97  ? 277 PHE D CA    1 
ATOM   15614 C  C     . PHE D 2 298 ? 149.134 109.309 152.328 1.00 29.77  ? 277 PHE D C     1 
ATOM   15615 O  O     . PHE D 2 298 ? 148.073 109.841 151.991 1.00 29.07  ? 277 PHE D O     1 
ATOM   15616 C  CB    . PHE D 2 298 ? 149.660 107.190 151.102 1.00 27.99  ? 277 PHE D CB    1 
ATOM   15617 C  CG    . PHE D 2 298 ? 149.866 105.694 151.124 1.00 27.61  ? 277 PHE D CG    1 
ATOM   15618 C  CD1   . PHE D 2 298 ? 150.984 105.140 151.750 1.00 25.91  ? 277 PHE D CD1   1 
ATOM   15619 C  CD2   . PHE D 2 298 ? 148.958 104.844 150.507 1.00 27.32  ? 277 PHE D CD2   1 
ATOM   15620 C  CE1   . PHE D 2 298 ? 151.191 103.772 151.768 1.00 26.65  ? 277 PHE D CE1   1 
ATOM   15621 C  CE2   . PHE D 2 298 ? 149.151 103.474 150.519 1.00 25.38  ? 277 PHE D CE2   1 
ATOM   15622 C  CZ    . PHE D 2 298 ? 150.275 102.933 151.163 1.00 26.20  ? 277 PHE D CZ    1 
ATOM   15623 N  N     . GLU D 2 299 ? 150.240 109.997 152.608 1.00 31.10  ? 278 GLU D N     1 
ATOM   15624 C  CA    . GLU D 2 299 ? 150.331 111.446 152.407 1.00 32.86  ? 278 GLU D CA    1 
ATOM   15625 C  C     . GLU D 2 299 ? 150.127 111.779 150.922 1.00 33.04  ? 278 GLU D C     1 
ATOM   15626 O  O     . GLU D 2 299 ? 150.453 110.973 150.046 1.00 32.23  ? 278 GLU D O     1 
ATOM   15627 C  CB    . GLU D 2 299 ? 151.684 111.983 152.905 1.00 33.45  ? 278 GLU D CB    1 
ATOM   15628 C  CG    . GLU D 2 299 ? 152.892 111.398 152.158 1.00 36.27  ? 278 GLU D CG    1 
ATOM   15629 C  CD    . GLU D 2 299 ? 154.230 112.014 152.538 1.00 40.47  ? 278 GLU D CD    1 
ATOM   15630 O  OE1   . GLU D 2 299 ? 154.472 112.276 153.738 1.00 41.72  ? 278 GLU D OE1   1 
ATOM   15631 O  OE2   . GLU D 2 299 ? 155.055 112.205 151.617 1.00 42.65  ? 278 GLU D OE2   1 
ATOM   15632 N  N     . GLU D 2 300 ? 149.583 112.965 150.660 1.00 34.09  ? 279 GLU D N     1 
ATOM   15633 C  CA    . GLU D 2 300 ? 149.348 113.444 149.305 1.00 35.06  ? 279 GLU D CA    1 
ATOM   15634 C  C     . GLU D 2 300 ? 150.678 113.687 148.590 1.00 34.97  ? 279 GLU D C     1 
ATOM   15635 O  O     . GLU D 2 300 ? 151.605 114.264 149.161 1.00 34.96  ? 279 GLU D O     1 
ATOM   15636 C  CB    . GLU D 2 300 ? 148.499 114.727 149.336 1.00 35.81  ? 279 GLU D CB    1 
ATOM   15637 C  CG    . GLU D 2 300 ? 148.033 115.209 147.961 1.00 38.58  ? 279 GLU D CG    1 
ATOM   15638 C  CD    . GLU D 2 300 ? 146.770 116.064 148.019 1.00 43.09  ? 279 GLU D CD    1 
ATOM   15639 O  OE1   . GLU D 2 300 ? 146.763 117.089 148.740 1.00 44.69  ? 279 GLU D OE1   1 
ATOM   15640 O  OE2   . GLU D 2 300 ? 145.777 115.702 147.347 1.00 44.94  ? 279 GLU D OE2   1 
ATOM   15641 N  N     . GLU D 2 301 ? 150.762 113.217 147.350 1.00 34.73  ? 280 GLU D N     1 
ATOM   15642 C  CA    . GLU D 2 301 ? 151.945 113.395 146.517 1.00 35.16  ? 280 GLU D CA    1 
ATOM   15643 C  C     . GLU D 2 301 ? 151.512 113.874 145.142 1.00 35.23  ? 280 GLU D C     1 
ATOM   15644 O  O     . GLU D 2 301 ? 150.396 113.584 144.698 1.00 34.92  ? 280 GLU D O     1 
ATOM   15645 C  CB    . GLU D 2 301 ? 152.709 112.072 146.378 1.00 35.10  ? 280 GLU D CB    1 
ATOM   15646 C  CG    . GLU D 2 301 ? 153.612 111.723 147.558 1.00 36.62  ? 280 GLU D CG    1 
ATOM   15647 C  CD    . GLU D 2 301 ? 154.136 110.288 147.502 1.00 37.59  ? 280 GLU D CD    1 
ATOM   15648 O  OE1   . GLU D 2 301 ? 153.318 109.346 147.447 1.00 38.10  ? 280 GLU D OE1   1 
ATOM   15649 O  OE2   . GLU D 2 301 ? 155.367 110.098 147.539 1.00 38.93  ? 280 GLU D OE2   1 
ATOM   15650 N  N     . ASP D 2 302 ? 152.389 114.605 144.465 1.00 35.60  ? 281 ASP D N     1 
ATOM   15651 C  CA    . ASP D 2 302 ? 152.116 115.009 143.091 1.00 35.96  ? 281 ASP D CA    1 
ATOM   15652 C  C     . ASP D 2 302 ? 152.425 113.835 142.171 1.00 35.01  ? 281 ASP D C     1 
ATOM   15653 O  O     . ASP D 2 302 ? 153.250 112.985 142.507 1.00 35.52  ? 281 ASP D O     1 
ATOM   15654 C  CB    . ASP D 2 302 ? 152.905 116.274 142.711 1.00 36.82  ? 281 ASP D CB    1 
ATOM   15655 C  CG    . ASP D 2 302 ? 154.432 116.074 142.733 1.00 39.01  ? 281 ASP D CG    1 
ATOM   15656 O  OD1   . ASP D 2 302 ? 154.944 115.138 143.397 1.00 40.83  ? 281 ASP D OD1   1 
ATOM   15657 O  OD2   . ASP D 2 302 ? 155.125 116.889 142.091 1.00 41.13  ? 281 ASP D OD2   1 
ATOM   15658 N  N     . ILE D 2 303 ? 151.744 113.760 141.037 1.00 33.94  ? 282 ILE D N     1 
ATOM   15659 C  CA    . ILE D 2 303 ? 151.959 112.661 140.098 1.00 33.00  ? 282 ILE D CA    1 
ATOM   15660 C  C     . ILE D 2 303 ? 152.743 113.108 138.856 1.00 31.59  ? 282 ILE D C     1 
ATOM   15661 O  O     . ILE D 2 303 ? 152.683 114.275 138.463 1.00 31.14  ? 282 ILE D O     1 
ATOM   15662 C  CB    . ILE D 2 303 ? 150.618 111.942 139.743 1.00 33.44  ? 282 ILE D CB    1 
ATOM   15663 C  CG1   . ILE D 2 303 ? 150.639 111.353 138.327 1.00 34.29  ? 282 ILE D CG1   1 
ATOM   15664 C  CG2   . ILE D 2 303 ? 149.438 112.881 139.935 1.00 35.47  ? 282 ILE D CG2   1 
ATOM   15665 C  CD1   . ILE D 2 303 ? 149.301 110.821 137.855 1.00 36.30  ? 282 ILE D CD1   1 
ATOM   15666 N  N     . ASN D 2 304 ? 153.493 112.178 138.265 1.00 29.53  ? 283 ASN D N     1 
ATOM   15667 C  CA    . ASN D 2 304 ? 154.220 112.438 137.025 1.00 28.49  ? 283 ASN D CA    1 
ATOM   15668 C  C     . ASN D 2 304 ? 153.333 113.162 135.989 1.00 27.87  ? 283 ASN D C     1 
ATOM   15669 O  O     . ASN D 2 304 ? 152.253 112.676 135.657 1.00 27.02  ? 283 ASN D O     1 
ATOM   15670 C  CB    . ASN D 2 304 ? 154.756 111.126 136.449 1.00 28.20  ? 283 ASN D CB    1 
ATOM   15671 C  CG    . ASN D 2 304 ? 155.595 111.340 135.217 1.00 28.17  ? 283 ASN D CG    1 
ATOM   15672 O  OD1   . ASN D 2 304 ? 155.071 111.427 134.111 1.00 29.01  ? 283 ASN D OD1   1 
ATOM   15673 N  ND2   . ASN D 2 304 ? 156.903 111.425 135.397 1.00 27.24  ? 283 ASN D ND2   1 
ATOM   15674 N  N     . PRO D 2 305 ? 153.782 114.332 135.492 1.00 28.00  ? 284 PRO D N     1 
ATOM   15675 C  CA    . PRO D 2 305 ? 152.943 115.140 134.592 1.00 27.58  ? 284 PRO D CA    1 
ATOM   15676 C  C     . PRO D 2 305 ? 152.657 114.495 133.234 1.00 27.01  ? 284 PRO D C     1 
ATOM   15677 O  O     . PRO D 2 305 ? 151.651 114.814 132.610 1.00 26.66  ? 284 PRO D O     1 
ATOM   15678 C  CB    . PRO D 2 305 ? 153.750 116.433 134.409 1.00 28.21  ? 284 PRO D CB    1 
ATOM   15679 C  CG    . PRO D 2 305 ? 155.128 116.096 134.776 1.00 28.80  ? 284 PRO D CG    1 
ATOM   15680 C  CD    . PRO D 2 305 ? 155.022 115.043 135.857 1.00 28.11  ? 284 PRO D CD    1 
ATOM   15681 N  N     . ILE D 2 306 ? 153.529 113.595 132.788 1.00 26.52  ? 285 ILE D N     1 
ATOM   15682 C  CA    . ILE D 2 306 ? 153.305 112.888 131.532 1.00 26.50  ? 285 ILE D CA    1 
ATOM   15683 C  C     . ILE D 2 306 ? 152.134 111.907 131.684 1.00 26.43  ? 285 ILE D C     1 
ATOM   15684 O  O     . ILE D 2 306 ? 151.213 111.876 130.856 1.00 26.00  ? 285 ILE D O     1 
ATOM   15685 C  CB    . ILE D 2 306 ? 154.593 112.192 131.024 1.00 26.88  ? 285 ILE D CB    1 
ATOM   15686 C  CG1   . ILE D 2 306 ? 155.692 113.243 130.783 1.00 26.98  ? 285 ILE D CG1   1 
ATOM   15687 C  CG2   . ILE D 2 306 ? 154.287 111.385 129.762 1.00 24.94  ? 285 ILE D CG2   1 
ATOM   15688 C  CD1   . ILE D 2 306 ? 157.052 112.683 130.467 1.00 26.65  ? 285 ILE D CD1   1 
ATOM   15689 N  N     . VAL D 2 307 ? 152.163 111.137 132.767 1.00 26.36  ? 286 VAL D N     1 
ATOM   15690 C  CA    . VAL D 2 307 ? 151.042 110.278 133.128 1.00 26.71  ? 286 VAL D CA    1 
ATOM   15691 C  C     . VAL D 2 307 ? 149.760 111.087 133.354 1.00 27.68  ? 286 VAL D C     1 
ATOM   15692 O  O     . VAL D 2 307 ? 148.696 110.677 132.891 1.00 27.92  ? 286 VAL D O     1 
ATOM   15693 C  CB    . VAL D 2 307 ? 151.387 109.363 134.334 1.00 26.37  ? 286 VAL D CB    1 
ATOM   15694 C  CG1   . VAL D 2 307 ? 150.139 108.645 134.874 1.00 25.48  ? 286 VAL D CG1   1 
ATOM   15695 C  CG2   . VAL D 2 307 ? 152.404 108.355 133.905 1.00 25.55  ? 286 VAL D CG2   1 
ATOM   15696 N  N     . LEU D 2 308 ? 149.857 112.242 134.019 1.00 28.80  ? 287 LEU D N     1 
ATOM   15697 C  CA    . LEU D 2 308 ? 148.688 113.126 134.159 1.00 30.07  ? 287 LEU D CA    1 
ATOM   15698 C  C     . LEU D 2 308 ? 148.112 113.558 132.807 1.00 30.38  ? 287 LEU D C     1 
ATOM   15699 O  O     . LEU D 2 308 ? 146.891 113.587 132.620 1.00 30.71  ? 287 LEU D O     1 
ATOM   15700 C  CB    . LEU D 2 308 ? 149.011 114.357 135.012 1.00 30.86  ? 287 LEU D CB    1 
ATOM   15701 C  CG    . LEU D 2 308 ? 148.902 114.166 136.528 1.00 32.62  ? 287 LEU D CG    1 
ATOM   15702 C  CD1   . LEU D 2 308 ? 149.439 115.376 137.261 1.00 33.97  ? 287 LEU D CD1   1 
ATOM   15703 C  CD2   . LEU D 2 308 ? 147.454 113.867 136.958 1.00 34.73  ? 287 LEU D CD2   1 
ATOM   15704 N  N     . ASN D 2 309 ? 148.988 113.883 131.863 1.00 30.81  ? 288 ASN D N     1 
ATOM   15705 C  CA    . ASN D 2 309 ? 148.546 114.260 130.525 1.00 31.25  ? 288 ASN D CA    1 
ATOM   15706 C  C     . ASN D 2 309 ? 147.848 113.101 129.812 1.00 31.83  ? 288 ASN D C     1 
ATOM   15707 O  O     . ASN D 2 309 ? 146.905 113.312 129.044 1.00 31.73  ? 288 ASN D O     1 
ATOM   15708 C  CB    . ASN D 2 309 ? 149.702 114.813 129.684 1.00 31.21  ? 288 ASN D CB    1 
ATOM   15709 C  CG    . ASN D 2 309 ? 149.227 115.395 128.362 1.00 31.41  ? 288 ASN D CG    1 
ATOM   15710 O  OD1   . ASN D 2 309 ? 148.228 116.123 128.317 1.00 31.88  ? 288 ASN D OD1   1 
ATOM   15711 N  ND2   . ASN D 2 309 ? 149.930 115.074 127.282 1.00 29.12  ? 288 ASN D ND2   1 
ATOM   15712 N  N     . GLY D 2 310 ? 148.315 111.880 130.079 1.00 32.04  ? 289 GLY D N     1 
ATOM   15713 C  CA    . GLY D 2 310 ? 147.655 110.672 129.597 1.00 33.04  ? 289 GLY D CA    1 
ATOM   15714 C  C     . GLY D 2 310 ? 146.276 110.502 130.223 1.00 33.85  ? 289 GLY D C     1 
ATOM   15715 O  O     . GLY D 2 310 ? 145.301 110.246 129.518 1.00 34.05  ? 289 GLY D O     1 
ATOM   15716 N  N     . LEU D 2 311 ? 146.201 110.651 131.545 1.00 34.33  ? 290 LEU D N     1 
ATOM   15717 C  CA    . LEU D 2 311 ? 144.951 110.496 132.294 1.00 35.77  ? 290 LEU D CA    1 
ATOM   15718 C  C     . LEU D 2 311 ? 143.877 111.501 131.890 1.00 37.01  ? 290 LEU D C     1 
ATOM   15719 O  O     . LEU D 2 311 ? 142.700 111.152 131.790 1.00 37.18  ? 290 LEU D O     1 
ATOM   15720 C  CB    . LEU D 2 311 ? 145.204 110.633 133.801 1.00 35.50  ? 290 LEU D CB    1 
ATOM   15721 C  CG    . LEU D 2 311 ? 145.535 109.423 134.670 1.00 35.45  ? 290 LEU D CG    1 
ATOM   15722 C  CD1   . LEU D 2 311 ? 145.918 109.904 136.079 1.00 35.28  ? 290 LEU D CD1   1 
ATOM   15723 C  CD2   . LEU D 2 311 ? 144.376 108.425 134.743 1.00 34.16  ? 290 LEU D CD2   1 
ATOM   15724 N  N     . THR D 2 332 ? 111.212 118.594 151.135 1.00 32.51  ? 311 THR D N     1 
ATOM   15725 C  CA    . THR D 2 332 ? 109.846 118.158 151.398 1.00 32.98  ? 311 THR D CA    1 
ATOM   15726 C  C     . THR D 2 332 ? 108.848 119.255 151.048 1.00 28.33  ? 311 THR D C     1 
ATOM   15727 O  O     . THR D 2 332 ? 108.598 120.155 151.845 1.00 34.06  ? 311 THR D O     1 
ATOM   15728 C  CB    . THR D 2 332 ? 109.646 117.766 152.875 1.00 32.80  ? 311 THR D CB    1 
ATOM   15729 O  OG1   . THR D 2 332 ? 110.809 117.085 153.357 1.00 35.39  ? 311 THR D OG1   1 
ATOM   15730 C  CG2   . THR D 2 332 ? 108.444 116.843 153.017 1.00 27.32  ? 311 THR D CG2   1 
ATOM   15731 N  N     . VAL D 2 333 ? 108.277 119.170 149.846 1.00 21.04  ? 312 VAL D N     1 
ATOM   15732 C  CA    . VAL D 2 333 ? 107.326 120.180 149.398 1.00 23.06  ? 312 VAL D CA    1 
ATOM   15733 C  C     . VAL D 2 333 ? 105.999 119.993 150.115 1.00 24.35  ? 312 VAL D C     1 
ATOM   15734 O  O     . VAL D 2 333 ? 105.345 118.954 149.987 1.00 27.51  ? 312 VAL D O     1 
ATOM   15735 C  CB    . VAL D 2 333 ? 107.154 120.117 147.869 1.00 21.66  ? 312 VAL D CB    1 
ATOM   15736 C  CG1   . VAL D 2 333 ? 106.175 121.184 147.391 1.00 19.37  ? 312 VAL D CG1   1 
ATOM   15737 C  CG2   . VAL D 2 333 ? 108.509 120.265 147.182 1.00 24.14  ? 312 VAL D CG2   1 
ATOM   15738 N  N     . GLU D 2 334 ? 105.601 121.007 150.880 1.00 22.97  ? 313 GLU D N     1 
ATOM   15739 C  CA    . GLU D 2 334 ? 104.309 121.030 151.556 1.00 25.24  ? 313 GLU D CA    1 
ATOM   15740 C  C     . GLU D 2 334 ? 103.589 122.292 151.097 1.00 26.98  ? 313 GLU D C     1 
ATOM   15741 O  O     . GLU D 2 334 ? 104.126 123.406 151.269 1.00 30.39  ? 313 GLU D O     1 
ATOM   15742 C  CB    . GLU D 2 334 ? 104.486 120.990 153.078 1.00 25.19  ? 313 GLU D CB    1 
ATOM   15743 C  CG    . GLU D 2 334 ? 103.264 120.503 153.834 1.00 25.82  ? 313 GLU D CG    1 
ATOM   15744 C  CD    . GLU D 2 334 ? 103.233 120.993 155.270 1.00 23.31  ? 313 GLU D CD    1 
ATOM   15745 O  OE1   . GLU D 2 334 ? 104.314 121.213 155.847 1.00 22.88  ? 313 GLU D OE1   1 
ATOM   15746 O  OE2   . GLU D 2 334 ? 102.122 121.153 155.822 1.00 23.92  ? 313 GLU D OE2   1 
ATOM   15747 N  N     . PRO D 2 335 ? 102.387 122.186 150.526 1.00 13.93  ? 314 PRO D N     1 
ATOM   15748 C  CA    . PRO D 2 335 ? 101.748 123.364 149.929 1.00 25.32  ? 314 PRO D CA    1 
ATOM   15749 C  C     . PRO D 2 335 ? 101.266 124.344 150.989 1.00 22.50  ? 314 PRO D C     1 
ATOM   15750 O  O     . PRO D 2 335 ? 100.812 123.952 152.066 1.00 23.90  ? 314 PRO D O     1 
ATOM   15751 C  CB    . PRO D 2 335 ? 100.570 122.757 149.138 1.00 20.68  ? 314 PRO D CB    1 
ATOM   15752 C  CG    . PRO D 2 335 ? 100.844 121.207 149.205 1.00 23.47  ? 314 PRO D CG    1 
ATOM   15753 C  CD    . PRO D 2 335 ? 101.376 121.136 150.596 1.00 23.46  ? 314 PRO D CD    1 
ATOM   15754 N  N     . LEU D 2 336 ? 101.382 125.632 150.678 1.00 14.61  ? 315 LEU D N     1 
ATOM   15755 C  CA    . LEU D 2 336 ? 100.816 126.664 151.535 1.00 10.57  ? 315 LEU D CA    1 
ATOM   15756 C  C     . LEU D 2 336 ? 99.300  126.520 151.575 1.00 14.80  ? 315 LEU D C     1 
ATOM   15757 O  O     . LEU D 2 336 ? 98.628  126.540 150.538 1.00 26.75  ? 315 LEU D O     1 
ATOM   15758 C  CB    . LEU D 2 336 ? 101.209 128.054 151.027 1.00 14.40  ? 315 LEU D CB    1 
ATOM   15759 C  CG    . LEU D 2 336 ? 102.523 128.619 151.567 1.00 12.28  ? 315 LEU D CG    1 
ATOM   15760 C  CD1   . LEU D 2 336 ? 102.886 129.918 150.870 1.00 10.98  ? 315 LEU D CD1   1 
ATOM   15761 C  CD2   . LEU D 2 336 ? 102.465 128.808 153.068 1.00 14.92  ? 315 LEU D CD2   1 
ATOM   15762 N  N     . LYS D 2 337 ? 98.761  126.377 152.784 1.00 13.54  ? 316 LYS D N     1 
ATOM   15763 C  CA    . LYS D 2 337 ? 97.365  126.009 152.993 1.00 30.01  ? 316 LYS D CA    1 
ATOM   15764 C  C     . LYS D 2 337 ? 96.543  127.169 153.548 1.00 25.79  ? 316 LYS D C     1 
ATOM   15765 O  O     . LYS D 2 337 ? 95.460  126.959 154.101 1.00 33.47  ? 316 LYS D O     1 
ATOM   15766 C  CB    . LYS D 2 337 ? 97.277  124.792 153.913 1.00 28.27  ? 316 LYS D CB    1 
ATOM   15767 C  CG    . LYS D 2 337 ? 97.511  125.102 155.390 1.00 24.51  ? 316 LYS D CG    1 
ATOM   15768 C  CD    . LYS D 2 337 ? 97.665  123.836 156.224 1.00 27.44  ? 316 LYS D CD    1 
ATOM   15769 C  CE    . LYS D 2 337 ? 96.920  122.655 155.619 1.00 29.88  ? 316 LYS D CE    1 
ATOM   15770 N  NZ    . LYS D 2 337 ? 97.188  121.395 156.368 1.00 29.09  ? 316 LYS D NZ    1 
ATOM   15771 N  N     . ASP D 2 338 ? 97.044  128.397 153.394 1.00 13.62  ? 317 ASP D N     1 
ATOM   15772 C  CA    . ASP D 2 338 ? 96.477  129.585 154.028 1.00 23.84  ? 317 ASP D CA    1 
ATOM   15773 C  C     . ASP D 2 338 ? 96.554  129.454 155.546 1.00 29.46  ? 317 ASP D C     1 
ATOM   15774 O  O     . ASP D 2 338 ? 96.957  128.405 156.060 1.00 33.27  ? 317 ASP D O     1 
ATOM   15775 C  CB    . ASP D 2 338 ? 95.037  129.830 153.565 1.00 26.92  ? 317 ASP D CB    1 
ATOM   15776 C  CG    . ASP D 2 338 ? 94.569  131.245 153.836 1.00 26.65  ? 317 ASP D CG    1 
ATOM   15777 O  OD1   . ASP D 2 338 ? 95.392  132.072 154.281 1.00 23.79  ? 317 ASP D OD1   1 
ATOM   15778 O  OD2   . ASP D 2 338 ? 93.377  131.531 153.596 1.00 27.60  ? 317 ASP D OD2   1 
ATOM   15779 N  N     . ASP D 2 339 ? 96.220  130.532 156.266 1.00 23.80  ? 318 ASP D N     1 
ATOM   15780 C  CA    . ASP D 2 339 ? 96.382  130.635 157.716 1.00 22.70  ? 318 ASP D CA    1 
ATOM   15781 C  C     . ASP D 2 339 ? 97.870  130.681 158.057 1.00 23.02  ? 318 ASP D C     1 
ATOM   15782 O  O     . ASP D 2 339 ? 98.254  130.896 159.213 1.00 26.98  ? 318 ASP D O     1 
ATOM   15783 C  CB    . ASP D 2 339 ? 95.658  129.483 158.435 1.00 24.00  ? 318 ASP D CB    1 
ATOM   15784 C  CG    . ASP D 2 339 ? 95.915  129.462 159.930 1.00 30.89  ? 318 ASP D CG    1 
ATOM   15785 O  OD1   . ASP D 2 339 ? 95.800  130.529 160.568 1.00 33.02  ? 318 ASP D OD1   1 
ATOM   15786 O  OD2   . ASP D 2 339 ? 96.238  128.379 160.464 1.00 30.00  ? 318 ASP D OD2   1 
ATOM   15787 N  N     . ASP D 2 340 ? 98.719  130.520 157.042 1.00 14.41  ? 319 ASP D N     1 
ATOM   15788 C  CA    . ASP D 2 340 ? 100.152 130.729 157.168 1.00 13.17  ? 319 ASP D CA    1 
ATOM   15789 C  C     . ASP D 2 340 ? 100.564 132.144 156.794 1.00 13.84  ? 319 ASP D C     1 
ATOM   15790 O  O     . ASP D 2 340 ? 101.702 132.538 157.068 1.00 19.23  ? 319 ASP D O     1 
ATOM   15791 C  CB    . ASP D 2 340 ? 100.915 129.727 156.292 1.00 10.03  ? 319 ASP D CB    1 
ATOM   15792 C  CG    . ASP D 2 340 ? 100.490 128.295 156.544 1.00 22.05  ? 319 ASP D CG    1 
ATOM   15793 O  OD1   . ASP D 2 340 ? 99.705  128.066 157.489 1.00 26.18  ? 319 ASP D OD1   1 
ATOM   15794 O  OD2   . ASP D 2 340 ? 100.937 127.399 155.799 1.00 26.11  ? 319 ASP D OD2   1 
ATOM   15795 N  N     . PHE D 2 341 ? 99.670  132.905 156.168 1.00 16.86  ? 320 PHE D N     1 
ATOM   15796 C  CA    . PHE D 2 341 ? 99.874  134.320 155.901 1.00 12.88  ? 320 PHE D CA    1 
ATOM   15797 C  C     . PHE D 2 341 ? 99.373  135.195 157.038 1.00 12.06  ? 320 PHE D C     1 
ATOM   15798 O  O     . PHE D 2 341 ? 99.553  136.416 156.992 1.00 15.68  ? 320 PHE D O     1 
ATOM   15799 C  CB    . PHE D 2 341 ? 99.175  134.716 154.597 1.00 14.37  ? 320 PHE D CB    1 
ATOM   15800 C  CG    . PHE D 2 341 ? 99.722  134.026 153.379 1.00 12.00  ? 320 PHE D CG    1 
ATOM   15801 C  CD1   . PHE D 2 341 ? 99.318  132.742 153.051 1.00 7.83   ? 320 PHE D CD1   1 
ATOM   15802 C  CD2   . PHE D 2 341 ? 100.632 134.665 152.555 1.00 12.15  ? 320 PHE D CD2   1 
ATOM   15803 C  CE1   . PHE D 2 341 ? 99.819  132.109 151.932 1.00 9.70   ? 320 PHE D CE1   1 
ATOM   15804 C  CE2   . PHE D 2 341 ? 101.134 134.037 151.432 1.00 8.26   ? 320 PHE D CE2   1 
ATOM   15805 C  CZ    . PHE D 2 341 ? 100.727 132.757 151.122 1.00 8.55   ? 320 PHE D CZ    1 
ATOM   15806 N  N     . TYR D 2 342 ? 98.750  134.599 158.053 1.00 7.62   ? 321 TYR D N     1 
ATOM   15807 C  CA    . TYR D 2 342 ? 98.246  135.317 159.214 1.00 11.59  ? 321 TYR D CA    1 
ATOM   15808 C  C     . TYR D 2 342 ? 98.923  134.758 160.456 1.00 18.48  ? 321 TYR D C     1 
ATOM   15809 O  O     . TYR D 2 342 ? 99.066  133.540 160.590 1.00 23.59  ? 321 TYR D O     1 
ATOM   15810 C  CB    . TYR D 2 342 ? 96.724  135.184 159.332 1.00 9.15   ? 321 TYR D CB    1 
ATOM   15811 C  CG    . TYR D 2 342 ? 95.962  135.797 158.180 1.00 14.71  ? 321 TYR D CG    1 
ATOM   15812 C  CD1   . TYR D 2 342 ? 95.669  137.153 158.157 1.00 13.92  ? 321 TYR D CD1   1 
ATOM   15813 C  CD2   . TYR D 2 342 ? 95.535  135.017 157.113 1.00 21.77  ? 321 TYR D CD2   1 
ATOM   15814 C  CE1   . TYR D 2 342 ? 94.973  137.715 157.105 1.00 13.51  ? 321 TYR D CE1   1 
ATOM   15815 C  CE2   . TYR D 2 342 ? 94.839  135.570 156.056 1.00 15.51  ? 321 TYR D CE2   1 
ATOM   15816 C  CZ    . TYR D 2 342 ? 94.561  136.920 156.057 1.00 17.94  ? 321 TYR D CZ    1 
ATOM   15817 O  OH    . TYR D 2 342 ? 93.868  137.475 155.007 1.00 24.54  ? 321 TYR D OH    1 
ATOM   15818 N  N     . PHE D 2 343 ? 99.336  135.646 161.353 1.00 11.50  ? 322 PHE D N     1 
ATOM   15819 C  CA    . PHE D 2 343 ? 100.051 135.230 162.554 1.00 15.15  ? 322 PHE D CA    1 
ATOM   15820 C  C     . PHE D 2 343 ? 99.415  135.821 163.808 1.00 24.40  ? 322 PHE D C     1 
ATOM   15821 O  O     . PHE D 2 343 ? 98.842  136.910 163.774 1.00 21.09  ? 322 PHE D O     1 
ATOM   15822 C  CB    . PHE D 2 343 ? 101.521 135.638 162.461 1.00 15.27  ? 322 PHE D CB    1 
ATOM   15823 C  CG    . PHE D 2 343 ? 102.196 135.183 161.200 1.00 12.42  ? 322 PHE D CG    1 
ATOM   15824 C  CD1   . PHE D 2 343 ? 102.718 133.905 161.100 1.00 11.68  ? 322 PHE D CD1   1 
ATOM   15825 C  CD2   . PHE D 2 343 ? 102.302 136.031 160.111 1.00 10.73  ? 322 PHE D CD2   1 
ATOM   15826 C  CE1   . PHE D 2 343 ? 103.337 133.483 159.940 1.00 5.83   ? 322 PHE D CE1   1 
ATOM   15827 C  CE2   . PHE D 2 343 ? 102.919 135.614 158.949 1.00 7.52   ? 322 PHE D CE2   1 
ATOM   15828 C  CZ    . PHE D 2 343 ? 103.436 134.339 158.864 1.00 8.62   ? 322 PHE D CZ    1 
ATOM   15829 N  N     . VAL E 3 19  ? 115.712 110.164 197.069 1.00 95.16  ? 19  VAL E N     1 
ATOM   15830 C  CA    . VAL E 3 19  ? 116.243 109.806 195.749 1.00 95.16  ? 19  VAL E CA    1 
ATOM   15831 C  C     . VAL E 3 19  ? 115.414 110.483 194.668 1.00 95.16  ? 19  VAL E C     1 
ATOM   15832 O  O     . VAL E 3 19  ? 114.197 110.289 194.577 1.00 95.16  ? 19  VAL E O     1 
ATOM   15833 C  CB    . VAL E 3 19  ? 116.326 108.284 195.548 1.00 95.16  ? 19  VAL E CB    1 
ATOM   15834 C  CG1   . VAL E 3 19  ? 116.983 107.936 194.205 1.00 95.16  ? 19  VAL E CG1   1 
ATOM   15835 C  CG2   . VAL E 3 19  ? 117.178 107.653 196.656 1.00 95.16  ? 19  VAL E CG2   1 
ATOM   15836 N  N     . VAL E 3 20  ? 116.086 111.275 193.837 1.00 96.12  ? 20  VAL E N     1 
ATOM   15837 C  CA    . VAL E 3 20  ? 115.465 112.074 192.783 1.00 96.12  ? 20  VAL E CA    1 
ATOM   15838 C  C     . VAL E 3 20  ? 116.117 111.768 191.440 1.00 96.12  ? 20  VAL E C     1 
ATOM   15839 O  O     . VAL E 3 20  ? 117.335 111.818 191.314 1.00 96.12  ? 20  VAL E O     1 
ATOM   15840 C  CB    . VAL E 3 20  ? 115.508 113.579 193.113 1.00 96.12  ? 20  VAL E CB    1 
ATOM   15841 C  CG1   . VAL E 3 20  ? 114.670 114.370 192.103 1.00 96.12  ? 20  VAL E CG1   1 
ATOM   15842 C  CG2   . VAL E 3 20  ? 114.967 113.849 194.527 1.00 96.12  ? 20  VAL E CG2   1 
ATOM   15843 N  N     . LEU E 3 21  ? 115.307 111.482 190.423 1.00 96.32  ? 21  LEU E N     1 
ATOM   15844 C  CA    . LEU E 3 21  ? 115.743 111.400 189.032 1.00 96.32  ? 21  LEU E CA    1 
ATOM   15845 C  C     . LEU E 3 21  ? 115.415 112.725 188.339 1.00 96.32  ? 21  LEU E C     1 
ATOM   15846 O  O     . LEU E 3 21  ? 114.251 113.008 188.049 1.00 96.32  ? 21  LEU E O     1 
ATOM   15847 C  CB    . LEU E 3 21  ? 115.080 110.188 188.360 1.00 96.32  ? 21  LEU E CB    1 
ATOM   15848 C  CG    . LEU E 3 21  ? 115.531 109.947 186.909 1.00 96.32  ? 21  LEU E CG    1 
ATOM   15849 C  CD1   . LEU E 3 21  ? 117.000 109.524 186.838 1.00 96.32  ? 21  LEU E CD1   1 
ATOM   15850 C  CD2   . LEU E 3 21  ? 114.695 108.823 186.299 1.00 96.32  ? 21  LEU E CD2   1 
ATOM   15851 N  N     . ALA E 3 22  ? 116.436 113.540 188.099 1.00 97.01  ? 22  ALA E N     1 
ATOM   15852 C  CA    . ALA E 3 22  ? 116.309 114.814 187.408 1.00 97.01  ? 22  ALA E CA    1 
ATOM   15853 C  C     . ALA E 3 22  ? 116.580 114.651 185.906 1.00 97.01  ? 22  ALA E C     1 
ATOM   15854 O  O     . ALA E 3 22  ? 117.670 114.243 185.516 1.00 97.01  ? 22  ALA E O     1 
ATOM   15855 C  CB    . ALA E 3 22  ? 117.235 115.843 188.057 1.00 97.01  ? 22  ALA E CB    1 
ATOM   15856 N  N     . ASP E 3 23  ? 115.606 115.003 185.072 1.00 96.28  ? 23  ASP E N     1 
ATOM   15857 C  CA    . ASP E 3 23  ? 115.678 114.983 183.612 1.00 96.28  ? 23  ASP E CA    1 
ATOM   15858 C  C     . ASP E 3 23  ? 115.862 116.390 183.046 1.00 96.28  ? 23  ASP E C     1 
ATOM   15859 O  O     . ASP E 3 23  ? 114.954 117.227 183.092 1.00 96.28  ? 23  ASP E O     1 
ATOM   15860 C  CB    . ASP E 3 23  ? 114.424 114.295 183.056 1.00 96.28  ? 23  ASP E CB    1 
ATOM   15861 C  CG    . ASP E 3 23  ? 114.302 114.372 181.528 1.00 96.28  ? 23  ASP E CG    1 
ATOM   15862 O  OD1   . ASP E 3 23  ? 115.329 114.284 180.825 1.00 96.28  ? 23  ASP E OD1   1 
ATOM   15863 O  OD2   . ASP E 3 23  ? 113.146 114.491 181.053 1.00 96.28  ? 23  ASP E OD2   1 
ATOM   15864 N  N     . PHE E 3 24  ? 117.051 116.631 182.503 1.00 96.18  ? 24  PHE E N     1 
ATOM   15865 C  CA    . PHE E 3 24  ? 117.393 117.827 181.749 1.00 96.18  ? 24  PHE E CA    1 
ATOM   15866 C  C     . PHE E 3 24  ? 117.010 117.610 180.293 1.00 96.18  ? 24  PHE E C     1 
ATOM   15867 O  O     . PHE E 3 24  ? 117.602 116.779 179.600 1.00 96.18  ? 24  PHE E O     1 
ATOM   15868 C  CB    . PHE E 3 24  ? 118.889 118.124 181.886 1.00 96.18  ? 24  PHE E CB    1 
ATOM   15869 C  CG    . PHE E 3 24  ? 119.296 118.568 183.273 1.00 96.18  ? 24  PHE E CG    1 
ATOM   15870 C  CD1   . PHE E 3 24  ? 119.406 117.631 184.318 1.00 96.18  ? 24  PHE E CD1   1 
ATOM   15871 C  CD2   . PHE E 3 24  ? 119.542 119.929 183.530 1.00 96.18  ? 24  PHE E CD2   1 
ATOM   15872 C  CE1   . PHE E 3 24  ? 119.734 118.058 185.614 1.00 96.18  ? 24  PHE E CE1   1 
ATOM   15873 C  CE2   . PHE E 3 24  ? 119.891 120.350 184.823 1.00 96.18  ? 24  PHE E CE2   1 
ATOM   15874 C  CZ    . PHE E 3 24  ? 119.989 119.416 185.867 1.00 96.18  ? 24  PHE E CZ    1 
ATOM   15875 N  N     . TRP E 3 25  ? 116.032 118.375 179.822 1.00 94.24  ? 25  TRP E N     1 
ATOM   15876 C  CA    . TRP E 3 25  ? 115.395 118.165 178.525 1.00 94.24  ? 25  TRP E CA    1 
ATOM   15877 C  C     . TRP E 3 25  ? 115.142 119.493 177.809 1.00 94.24  ? 25  TRP E C     1 
ATOM   15878 O  O     . TRP E 3 25  ? 115.297 120.555 178.402 1.00 94.24  ? 25  TRP E O     1 
ATOM   15879 C  CB    . TRP E 3 25  ? 114.095 117.376 178.745 1.00 94.24  ? 25  TRP E CB    1 
ATOM   15880 C  CG    . TRP E 3 25  ? 112.956 118.145 179.336 1.00 94.24  ? 25  TRP E CG    1 
ATOM   15881 C  CD1   . TRP E 3 25  ? 112.876 118.570 180.614 1.00 94.24  ? 25  TRP E CD1   1 
ATOM   15882 C  CD2   . TRP E 3 25  ? 111.765 118.659 178.668 1.00 94.24  ? 25  TRP E CD2   1 
ATOM   15883 N  NE1   . TRP E 3 25  ? 111.762 119.369 180.771 1.00 94.24  ? 25  TRP E NE1   1 
ATOM   15884 C  CE2   . TRP E 3 25  ? 111.029 119.440 179.608 1.00 94.24  ? 25  TRP E CE2   1 
ATOM   15885 C  CE3   . TRP E 3 25  ? 111.246 118.562 177.359 1.00 94.24  ? 25  TRP E CE3   1 
ATOM   15886 C  CZ2   . TRP E 3 25  ? 109.849 120.112 179.262 1.00 94.24  ? 25  TRP E CZ2   1 
ATOM   15887 C  CZ3   . TRP E 3 25  ? 110.054 119.221 177.004 1.00 94.24  ? 25  TRP E CZ3   1 
ATOM   15888 C  CH2   . TRP E 3 25  ? 109.363 120.003 177.948 1.00 94.24  ? 25  TRP E CH2   1 
ATOM   15889 N  N     . ALA E 3 26  ? 114.735 119.432 176.540 1.00 92.23  ? 26  ALA E N     1 
ATOM   15890 C  CA    . ALA E 3 26  ? 114.236 120.593 175.804 1.00 92.23  ? 26  ALA E CA    1 
ATOM   15891 C  C     . ALA E 3 26  ? 113.097 120.202 174.841 1.00 92.23  ? 26  ALA E C     1 
ATOM   15892 O  O     . ALA E 3 26  ? 113.064 119.057 174.365 1.00 92.23  ? 26  ALA E O     1 
ATOM   15893 C  CB    . ALA E 3 26  ? 115.378 121.258 175.027 1.00 92.23  ? 26  ALA E CB    1 
ATOM   15894 N  N     . PRO E 3 27  ? 112.197 121.130 174.462 1.00 86.64  ? 27  PRO E N     1 
ATOM   15895 C  CA    . PRO E 3 27  ? 111.051 120.838 173.595 1.00 86.64  ? 27  PRO E CA    1 
ATOM   15896 C  C     . PRO E 3 27  ? 111.426 120.437 172.162 1.00 86.64  ? 27  PRO E C     1 
ATOM   15897 O  O     . PRO E 3 27  ? 110.661 119.753 171.475 1.00 86.64  ? 27  PRO E O     1 
ATOM   15898 C  CB    . PRO E 3 27  ? 110.215 122.125 173.586 1.00 86.64  ? 27  PRO E CB    1 
ATOM   15899 C  CG    . PRO E 3 27  ? 110.630 122.853 174.862 1.00 86.64  ? 27  PRO E CG    1 
ATOM   15900 C  CD    . PRO E 3 27  ? 112.102 122.488 174.982 1.00 86.64  ? 27  PRO E CD    1 
ATOM   15901 N  N     . TRP E 3 28  ? 112.592 120.867 171.683 1.00 80.08  ? 28  TRP E N     1 
ATOM   15902 C  CA    . TRP E 3 28  ? 113.102 120.555 170.345 1.00 80.08  ? 28  TRP E CA    1 
ATOM   15903 C  C     . TRP E 3 28  ? 113.890 119.240 170.287 1.00 80.08  ? 28  TRP E C     1 
ATOM   15904 O  O     . TRP E 3 28  ? 114.098 118.705 169.200 1.00 80.08  ? 28  TRP E O     1 
ATOM   15905 C  CB    . TRP E 3 28  ? 113.936 121.742 169.855 1.00 80.08  ? 28  TRP E CB    1 
ATOM   15906 C  CG    . TRP E 3 28  ? 114.983 122.215 170.809 1.00 80.08  ? 28  TRP E CG    1 
ATOM   15907 C  CD1   . TRP E 3 28  ? 114.856 123.251 171.668 1.00 80.08  ? 28  TRP E CD1   1 
ATOM   15908 C  CD2   . TRP E 3 28  ? 116.323 121.678 171.036 1.00 80.08  ? 28  TRP E CD2   1 
ATOM   15909 N  NE1   . TRP E 3 28  ? 116.008 123.381 172.411 1.00 80.08  ? 28  TRP E NE1   1 
ATOM   15910 C  CE2   . TRP E 3 28  ? 116.943 122.436 172.073 1.00 80.08  ? 28  TRP E CE2   1 
ATOM   15911 C  CE3   . TRP E 3 28  ? 117.076 120.627 170.475 1.00 80.08  ? 28  TRP E CE3   1 
ATOM   15912 C  CZ2   . TRP E 3 28  ? 118.228 122.160 172.553 1.00 80.08  ? 28  TRP E CZ2   1 
ATOM   15913 C  CZ3   . TRP E 3 28  ? 118.382 120.362 170.927 1.00 80.08  ? 28  TRP E CZ3   1 
ATOM   15914 C  CH2   . TRP E 3 28  ? 118.956 121.116 171.964 1.00 80.08  ? 28  TRP E CH2   1 
ATOM   15915 N  N     . CYS E 3 29  ? 114.275 118.681 171.434 1.00 85.92  ? 29  CYS E N     1 
ATOM   15916 C  CA    . CYS E 3 29  ? 115.091 117.475 171.519 1.00 85.92  ? 29  CYS E CA    1 
ATOM   15917 C  C     . CYS E 3 29  ? 114.252 116.211 171.258 1.00 85.92  ? 29  CYS E C     1 
ATOM   15918 O  O     . CYS E 3 29  ? 113.418 115.809 172.073 1.00 85.92  ? 29  CYS E O     1 
ATOM   15919 C  CB    . CYS E 3 29  ? 115.758 117.488 172.894 1.00 85.92  ? 29  CYS E CB    1 
ATOM   15920 S  SG    . CYS E 3 29  ? 116.907 116.145 173.261 1.00 85.92  ? 29  CYS E SG    1 
ATOM   15921 N  N     . GLY E 3 30  ? 114.487 115.554 170.118 1.00 84.06  ? 30  GLY E N     1 
ATOM   15922 C  CA    . GLY E 3 30  ? 113.816 114.302 169.741 1.00 84.06  ? 30  GLY E CA    1 
ATOM   15923 C  C     . GLY E 3 30  ? 113.964 113.190 170.791 1.00 84.06  ? 30  GLY E C     1 
ATOM   15924 O  O     . GLY E 3 30  ? 112.946 112.692 171.276 1.00 84.06  ? 30  GLY E O     1 
ATOM   15925 N  N     . PRO E 3 31  ? 115.192 112.844 171.226 1.00 89.12  ? 31  PRO E N     1 
ATOM   15926 C  CA    . PRO E 3 31  ? 115.406 111.845 172.277 1.00 89.12  ? 31  PRO E CA    1 
ATOM   15927 C  C     . PRO E 3 31  ? 114.724 112.179 173.610 1.00 89.12  ? 31  PRO E C     1 
ATOM   15928 O  O     . PRO E 3 31  ? 114.196 111.294 174.279 1.00 89.12  ? 31  PRO E O     1 
ATOM   15929 C  CB    . PRO E 3 31  ? 116.929 111.721 172.404 1.00 89.12  ? 31  PRO E CB    1 
ATOM   15930 C  CG    . PRO E 3 31  ? 117.436 112.102 171.016 1.00 89.12  ? 31  PRO E CG    1 
ATOM   15931 C  CD    . PRO E 3 31  ? 116.464 113.207 170.610 1.00 89.12  ? 31  PRO E CD    1 
ATOM   15932 N  N     . CYS E 3 32  ? 114.623 113.462 173.954 1.00 91.95  ? 32  CYS E N     1 
ATOM   15933 C  CA    . CYS E 3 32  ? 113.913 113.918 175.145 1.00 91.95  ? 32  CYS E CA    1 
ATOM   15934 C  C     . CYS E 3 32  ? 112.401 113.656 175.063 1.00 91.95  ? 32  CYS E C     1 
ATOM   15935 O  O     . CYS E 3 32  ? 111.757 113.362 176.068 1.00 91.95  ? 32  CYS E O     1 
ATOM   15936 C  CB    . CYS E 3 32  ? 114.171 115.409 175.339 1.00 91.95  ? 32  CYS E CB    1 
ATOM   15937 S  SG    . CYS E 3 32  ? 115.881 115.891 175.702 1.00 91.95  ? 32  CYS E SG    1 
ATOM   15938 N  N     . LYS E 3 33  ? 111.809 113.716 173.863 1.00 89.47  ? 33  LYS E N     1 
ATOM   15939 C  CA    . LYS E 3 33  ? 110.407 113.317 173.656 1.00 89.47  ? 33  LYS E CA    1 
ATOM   15940 C  C     . LYS E 3 33  ? 110.214 111.813 173.814 1.00 89.47  ? 33  LYS E C     1 
ATOM   15941 O  O     . LYS E 3 33  ? 109.174 111.395 174.305 1.00 89.47  ? 33  LYS E O     1 
ATOM   15942 C  CB    . LYS E 3 33  ? 109.903 113.766 172.280 1.00 89.47  ? 33  LYS E CB    1 
ATOM   15943 C  CG    . LYS E 3 33  ? 109.824 115.289 172.182 1.00 89.47  ? 33  LYS E CG    1 
ATOM   15944 C  CD    . LYS E 3 33  ? 109.430 115.720 170.767 1.00 89.47  ? 33  LYS E CD    1 
ATOM   15945 C  CE    . LYS E 3 33  ? 109.404 117.244 170.778 1.00 89.47  ? 33  LYS E CE    1 
ATOM   15946 N  NZ    . LYS E 3 33  ? 109.278 117.840 169.430 1.00 89.47  ? 33  LYS E NZ    1 
ATOM   15947 N  N     . MET E 3 34  ? 111.207 111.011 173.428 1.00 91.65  ? 34  MET E N     1 
ATOM   15948 C  CA    . MET E 3 34  ? 111.155 109.554 173.584 1.00 91.65  ? 34  MET E CA    1 
ATOM   15949 C  C     . MET E 3 34  ? 111.261 109.121 175.048 1.00 91.65  ? 34  MET E C     1 
ATOM   15950 O  O     . MET E 3 34  ? 110.641 108.134 175.430 1.00 91.65  ? 34  MET E O     1 
ATOM   15951 C  CB    . MET E 3 34  ? 112.256 108.871 172.761 1.00 91.65  ? 34  MET E CB    1 
ATOM   15952 C  CG    . MET E 3 34  ? 112.112 109.130 171.260 1.00 91.65  ? 34  MET E CG    1 
ATOM   15953 S  SD    . MET E 3 34  ? 113.144 108.066 170.215 1.00 91.65  ? 34  MET E SD    1 
ATOM   15954 C  CE    . MET E 3 34  ? 114.811 108.657 170.607 1.00 91.65  ? 34  MET E CE    1 
ATOM   15955 N  N     . ILE E 3 35  ? 112.011 109.855 175.877 1.00 92.57  ? 35  ILE E N     1 
ATOM   15956 C  CA    . ILE E 3 35  ? 112.183 109.508 177.296 1.00 92.57  ? 35  ILE E CA    1 
ATOM   15957 C  C     . ILE E 3 35  ? 110.981 109.904 178.161 1.00 92.57  ? 35  ILE E C     1 
ATOM   15958 O  O     . ILE E 3 35  ? 110.748 109.296 179.198 1.00 92.57  ? 35  ILE E O     1 
ATOM   15959 C  CB    . ILE E 3 35  ? 113.525 110.075 177.817 1.00 92.57  ? 35  ILE E CB    1 
ATOM   15960 C  CG1   . ILE E 3 35  ? 114.172 109.068 178.787 1.00 92.57  ? 35  ILE E CG1   1 
ATOM   15961 C  CG2   . ILE E 3 35  ? 113.403 111.464 178.469 1.00 92.57  ? 35  ILE E CG2   1 
ATOM   15962 C  CD1   . ILE E 3 35  ? 115.640 109.401 179.066 1.00 92.57  ? 35  ILE E CD1   1 
ATOM   15963 N  N     . ALA E 3 36  ? 110.185 110.888 177.731 1.00 91.47  ? 36  ALA E N     1 
ATOM   15964 C  CA    . ALA E 3 36  ? 109.015 111.358 178.472 1.00 91.47  ? 36  ALA E CA    1 
ATOM   15965 C  C     . ALA E 3 36  ? 108.034 110.235 178.889 1.00 91.47  ? 36  ALA E C     1 
ATOM   15966 O  O     . ALA E 3 36  ? 107.787 110.125 180.090 1.00 91.47  ? 36  ALA E O     1 
ATOM   15967 C  CB    . ALA E 3 36  ? 108.341 112.488 177.681 1.00 91.47  ? 36  ALA E CB    1 
ATOM   15968 N  N     . PRO E 3 37  ? 107.537 109.357 177.988 1.00 93.27  ? 37  PRO E N     1 
ATOM   15969 C  CA    . PRO E 3 37  ? 106.652 108.255 178.385 1.00 93.27  ? 37  PRO E CA    1 
ATOM   15970 C  C     . PRO E 3 37  ? 107.341 107.230 179.297 1.00 93.27  ? 37  PRO E C     1 
ATOM   15971 O  O     . PRO E 3 37  ? 106.708 106.667 180.183 1.00 93.27  ? 37  PRO E O     1 
ATOM   15972 C  CB    . PRO E 3 37  ? 106.191 107.612 177.072 1.00 93.27  ? 37  PRO E CB    1 
ATOM   15973 C  CG    . PRO E 3 37  ? 107.305 107.958 176.085 1.00 93.27  ? 37  PRO E CG    1 
ATOM   15974 C  CD    . PRO E 3 37  ? 107.720 109.351 176.543 1.00 93.27  ? 37  PRO E CD    1 
ATOM   15975 N  N     . VAL E 3 38  ? 108.652 107.024 179.132 1.00 94.14  ? 38  VAL E N     1 
ATOM   15976 C  CA    . VAL E 3 38  ? 109.431 106.111 179.984 1.00 94.14  ? 38  VAL E CA    1 
ATOM   15977 C  C     . VAL E 3 38  ? 109.456 106.609 181.431 1.00 94.14  ? 38  VAL E C     1 
ATOM   15978 O  O     . VAL E 3 38  ? 109.317 105.818 182.361 1.00 94.14  ? 38  VAL E O     1 
ATOM   15979 C  CB    . VAL E 3 38  ? 110.868 105.947 179.445 1.00 94.14  ? 38  VAL E CB    1 
ATOM   15980 C  CG1   . VAL E 3 38  ? 111.666 104.940 180.270 1.00 94.14  ? 38  VAL E CG1   1 
ATOM   15981 C  CG2   . VAL E 3 38  ? 110.877 105.457 177.990 1.00 94.14  ? 38  VAL E CG2   1 
ATOM   15982 N  N     . LEU E 3 39  ? 109.598 107.922 181.629 1.00 94.75  ? 39  LEU E N     1 
ATOM   15983 C  CA    . LEU E 3 39  ? 109.558 108.537 182.956 1.00 94.75  ? 39  LEU E CA    1 
ATOM   15984 C  C     . LEU E 3 39  ? 108.156 108.487 183.577 1.00 94.75  ? 39  LEU E C     1 
ATOM   15985 O  O     . LEU E 3 39  ? 108.044 108.333 184.789 1.00 94.75  ? 39  LEU E O     1 
ATOM   15986 C  CB    . LEU E 3 39  ? 110.067 109.985 182.868 1.00 94.75  ? 39  LEU E CB    1 
ATOM   15987 C  CG    . LEU E 3 39  ? 111.545 110.135 182.464 1.00 94.75  ? 39  LEU E CG    1 
ATOM   15988 C  CD1   . LEU E 3 39  ? 111.876 111.623 182.339 1.00 94.75  ? 39  LEU E CD1   1 
ATOM   15989 C  CD2   . LEU E 3 39  ? 112.504 109.511 183.475 1.00 94.75  ? 39  LEU E CD2   1 
ATOM   15990 N  N     . GLU E 3 40  ? 107.093 108.587 182.777 1.00 93.96  ? 40  GLU E N     1 
ATOM   15991 C  CA    . GLU E 3 40  ? 105.713 108.444 183.265 1.00 93.96  ? 40  GLU E CA    1 
ATOM   15992 C  C     . GLU E 3 40  ? 105.426 107.021 183.758 1.00 93.96  ? 40  GLU E C     1 
ATOM   15993 O  O     . GLU E 3 40  ? 104.848 106.852 184.831 1.00 93.96  ? 40  GLU E O     1 
ATOM   15994 C  CB    . GLU E 3 40  ? 104.709 108.842 182.173 1.00 93.96  ? 40  GLU E CB    1 
ATOM   15995 C  CG    . GLU E 3 40  ? 104.701 110.354 181.902 1.00 93.96  ? 40  GLU E CG    1 
ATOM   15996 C  CD    . GLU E 3 40  ? 103.757 110.774 180.759 1.00 93.96  ? 40  GLU E CD    1 
ATOM   15997 O  OE1   . GLU E 3 40  ? 103.009 109.916 180.234 1.00 93.96  ? 40  GLU E OE1   1 
ATOM   15998 O  OE2   . GLU E 3 40  ? 103.779 111.981 180.419 1.00 93.96  ? 40  GLU E OE2   1 
ATOM   15999 N  N     . GLU E 3 41  ? 105.868 105.993 183.029 1.00 94.15  ? 41  GLU E N     1 
ATOM   16000 C  CA    . GLU E 3 41  ? 105.775 104.603 183.497 1.00 94.15  ? 41  GLU E CA    1 
ATOM   16001 C  C     . GLU E 3 41  ? 106.613 104.369 184.758 1.00 94.15  ? 41  GLU E C     1 
ATOM   16002 O  O     . GLU E 3 41  ? 106.166 103.709 185.697 1.00 94.15  ? 41  GLU E O     1 
ATOM   16003 C  CB    . GLU E 3 41  ? 106.256 103.633 182.413 1.00 94.15  ? 41  GLU E CB    1 
ATOM   16004 C  CG    . GLU E 3 41  ? 105.296 103.506 181.224 1.00 94.15  ? 41  GLU E CG    1 
ATOM   16005 C  CD    . GLU E 3 41  ? 105.747 102.420 180.230 1.00 94.15  ? 41  GLU E CD    1 
ATOM   16006 O  OE1   . GLU E 3 41  ? 106.545 101.527 180.626 1.00 94.15  ? 41  GLU E OE1   1 
ATOM   16007 O  OE2   . GLU E 3 41  ? 105.252 102.447 179.081 1.00 94.15  ? 41  GLU E OE2   1 
ATOM   16008 N  N     . LEU E 3 42  ? 107.822 104.935 184.804 1.00 93.46  ? 42  LEU E N     1 
ATOM   16009 C  CA    . LEU E 3 42  ? 108.694 104.821 185.967 1.00 93.46  ? 42  LEU E CA    1 
ATOM   16010 C  C     . LEU E 3 42  ? 108.068 105.469 187.210 1.00 93.46  ? 42  LEU E C     1 
ATOM   16011 O  O     . LEU E 3 42  ? 108.162 104.903 188.298 1.00 93.46  ? 42  LEU E O     1 
ATOM   16012 C  CB    . LEU E 3 42  ? 110.057 105.441 185.622 1.00 93.46  ? 42  LEU E CB    1 
ATOM   16013 C  CG    . LEU E 3 42  ? 111.143 105.171 186.676 1.00 93.46  ? 42  LEU E CG    1 
ATOM   16014 C  CD1   . LEU E 3 42  ? 111.535 103.696 186.704 1.00 93.46  ? 42  LEU E CD1   1 
ATOM   16015 C  CD2   . LEU E 3 42  ? 112.397 105.976 186.339 1.00 93.46  ? 42  LEU E CD2   1 
ATOM   16016 N  N     . ASP E 3 43  ? 107.394 106.613 187.060 1.00 93.38  ? 43  ASP E N     1 
ATOM   16017 C  CA    . ASP E 3 43  ? 106.665 107.247 188.162 1.00 93.38  ? 43  ASP E CA    1 
ATOM   16018 C  C     . ASP E 3 43  ? 105.495 106.388 188.660 1.00 93.38  ? 43  ASP E C     1 
ATOM   16019 O  O     . ASP E 3 43  ? 105.235 106.320 189.861 1.00 93.38  ? 43  ASP E O     1 
ATOM   16020 C  CB    . ASP E 3 43  ? 106.135 108.634 187.763 1.00 93.38  ? 43  ASP E CB    1 
ATOM   16021 C  CG    . ASP E 3 43  ? 105.523 109.305 188.995 1.00 93.38  ? 43  ASP E CG    1 
ATOM   16022 O  OD1   . ASP E 3 43  ? 106.219 109.337 190.035 1.00 93.38  ? 43  ASP E OD1   1 
ATOM   16023 O  OD2   . ASP E 3 43  ? 104.337 109.716 188.973 1.00 93.38  ? 43  ASP E OD2   1 
ATOM   16024 N  N     . GLN E 3 44  ? 104.799 105.691 187.761 1.00 92.26  ? 44  GLN E N     1 
ATOM   16025 C  CA    . GLN E 3 44  ? 103.706 104.797 188.152 1.00 92.26  ? 44  GLN E CA    1 
ATOM   16026 C  C     . GLN E 3 44  ? 104.200 103.585 188.947 1.00 92.26  ? 44  GLN E C     1 
ATOM   16027 O  O     . GLN E 3 44  ? 103.522 103.142 189.873 1.00 92.26  ? 44  GLN E O     1 
ATOM   16028 C  CB    . GLN E 3 44  ? 102.938 104.326 186.911 1.00 92.26  ? 44  GLN E CB    1 
ATOM   16029 C  CG    . GLN E 3 44  ? 102.109 105.457 186.293 1.00 92.26  ? 44  GLN E CG    1 
ATOM   16030 C  CD    . GLN E 3 44  ? 101.402 105.030 185.012 1.00 92.26  ? 44  GLN E CD    1 
ATOM   16031 O  OE1   . GLN E 3 44  ? 101.185 103.866 184.718 1.00 92.26  ? 44  GLN E OE1   1 
ATOM   16032 N  NE2   . GLN E 3 44  ? 100.973 105.971 184.204 1.00 92.26  ? 44  GLN E NE2   1 
ATOM   16033 N  N     . GLU E 3 45  ? 105.370 103.046 188.601 1.00 91.79  ? 45  GLU E N     1 
ATOM   16034 C  CA    . GLU E 3 45  ? 105.916 101.845 189.242 1.00 91.79  ? 45  GLU E CA    1 
ATOM   16035 C  C     . GLU E 3 45  ? 106.733 102.149 190.506 1.00 91.79  ? 45  GLU E C     1 
ATOM   16036 O  O     . GLU E 3 45  ? 106.760 101.342 191.437 1.00 91.79  ? 45  GLU E O     1 
ATOM   16037 C  CB    . GLU E 3 45  ? 106.776 101.072 188.229 1.00 91.79  ? 45  GLU E CB    1 
ATOM   16038 C  CG    . GLU E 3 45  ? 105.927 100.425 187.120 1.00 91.79  ? 45  GLU E CG    1 
ATOM   16039 C  CD    . GLU E 3 45  ? 106.761 99.624  186.106 1.00 91.79  ? 45  GLU E CD    1 
ATOM   16040 O  OE1   . GLU E 3 45  ? 107.896 99.210  186.431 1.00 91.79  ? 45  GLU E OE1   1 
ATOM   16041 O  OE2   . GLU E 3 45  ? 106.273 99.393  184.973 1.00 91.79  ? 45  GLU E OE2   1 
ATOM   16042 N  N     . MET E 3 46  ? 107.421 103.291 190.545 1.00 90.55  ? 46  MET E N     1 
ATOM   16043 C  CA    . MET E 3 46  ? 108.417 103.605 191.577 1.00 90.55  ? 46  MET E CA    1 
ATOM   16044 C  C     . MET E 3 46  ? 108.188 104.941 192.283 1.00 90.55  ? 46  MET E C     1 
ATOM   16045 O  O     . MET E 3 46  ? 108.971 105.299 193.165 1.00 90.55  ? 46  MET E O     1 
ATOM   16046 C  CB    . MET E 3 46  ? 109.828 103.550 190.977 1.00 90.55  ? 46  MET E CB    1 
ATOM   16047 C  CG    . MET E 3 46  ? 110.159 102.169 190.403 1.00 90.55  ? 46  MET E CG    1 
ATOM   16048 S  SD    . MET E 3 46  ? 111.888 101.974 189.912 1.00 90.55  ? 46  MET E SD    1 
ATOM   16049 C  CE    . MET E 3 46  ? 112.712 101.969 191.518 1.00 90.55  ? 46  MET E CE    1 
ATOM   16050 N  N     . GLY E 3 47  ? 107.117 105.662 191.956 1.00 85.77  ? 47  GLY E N     1 
ATOM   16051 C  CA    . GLY E 3 47  ? 106.859 107.019 192.436 1.00 85.77  ? 47  GLY E CA    1 
ATOM   16052 C  C     . GLY E 3 47  ? 106.649 107.181 193.945 1.00 85.77  ? 47  GLY E C     1 
ATOM   16053 O  O     . GLY E 3 47  ? 106.515 108.313 194.401 1.00 85.77  ? 47  GLY E O     1 
ATOM   16054 N  N     . ASP E 3 48  ? 106.599 106.085 194.710 1.00 86.79  ? 48  ASP E N     1 
ATOM   16055 C  CA    . ASP E 3 48  ? 106.568 106.091 196.183 1.00 86.79  ? 48  ASP E CA    1 
ATOM   16056 C  C     . ASP E 3 48  ? 107.970 106.178 196.809 1.00 86.79  ? 48  ASP E C     1 
ATOM   16057 O  O     . ASP E 3 48  ? 108.115 106.548 197.974 1.00 86.79  ? 48  ASP E O     1 
ATOM   16058 C  CB    . ASP E 3 48  ? 105.897 104.805 196.689 1.00 86.79  ? 48  ASP E CB    1 
ATOM   16059 C  CG    . ASP E 3 48  ? 104.404 104.694 196.369 1.00 86.79  ? 48  ASP E CG    1 
ATOM   16060 O  OD1   . ASP E 3 48  ? 103.754 105.742 196.154 1.00 86.79  ? 48  ASP E OD1   1 
ATOM   16061 O  OD2   . ASP E 3 48  ? 103.922 103.540 196.393 1.00 86.79  ? 48  ASP E OD2   1 
ATOM   16062 N  N     . LYS E 3 49  ? 109.008 105.796 196.057 1.00 90.32  ? 49  LYS E N     1 
ATOM   16063 C  CA    . LYS E 3 49  ? 110.411 105.760 196.510 1.00 90.32  ? 49  LYS E CA    1 
ATOM   16064 C  C     . LYS E 3 49  ? 111.318 106.688 195.710 1.00 90.32  ? 49  LYS E C     1 
ATOM   16065 O  O     . LYS E 3 49  ? 112.412 107.008 196.160 1.00 90.32  ? 49  LYS E O     1 
ATOM   16066 C  CB    . LYS E 3 49  ? 110.954 104.332 196.420 1.00 90.32  ? 49  LYS E CB    1 
ATOM   16067 C  CG    . LYS E 3 49  ? 110.152 103.316 197.239 1.00 90.32  ? 49  LYS E CG    1 
ATOM   16068 C  CD    . LYS E 3 49  ? 110.862 101.964 197.164 1.00 90.32  ? 49  LYS E CD    1 
ATOM   16069 C  CE    . LYS E 3 49  ? 110.029 100.894 197.865 1.00 90.32  ? 49  LYS E CE    1 
ATOM   16070 N  NZ    . LYS E 3 49  ? 110.708 99.581  197.769 1.00 90.32  ? 49  LYS E NZ    1 
ATOM   16071 N  N     . LEU E 3 50  ? 110.871 107.081 194.523 1.00 93.16  ? 50  LEU E N     1 
ATOM   16072 C  CA    . LEU E 3 50  ? 111.590 107.919 193.582 1.00 93.16  ? 50  LEU E CA    1 
ATOM   16073 C  C     . LEU E 3 50  ? 110.754 109.155 193.278 1.00 93.16  ? 50  LEU E C     1 
ATOM   16074 O  O     . LEU E 3 50  ? 109.596 109.046 192.882 1.00 93.16  ? 50  LEU E O     1 
ATOM   16075 C  CB    . LEU E 3 50  ? 111.840 107.102 192.303 1.00 93.16  ? 50  LEU E CB    1 
ATOM   16076 C  CG    . LEU E 3 50  ? 112.583 107.890 191.210 1.00 93.16  ? 50  LEU E CG    1 
ATOM   16077 C  CD1   . LEU E 3 50  ? 113.996 108.247 191.670 1.00 93.16  ? 50  LEU E CD1   1 
ATOM   16078 C  CD2   . LEU E 3 50  ? 112.594 107.080 189.914 1.00 93.16  ? 50  LEU E CD2   1 
ATOM   16079 N  N     . LYS E 3 51  ? 111.370 110.327 193.377 1.00 94.28  ? 51  LYS E N     1 
ATOM   16080 C  CA    . LYS E 3 51  ? 110.801 111.552 192.820 1.00 94.28  ? 51  LYS E CA    1 
ATOM   16081 C  C     . LYS E 3 51  ? 111.393 111.797 191.441 1.00 94.28  ? 51  LYS E C     1 
ATOM   16082 O  O     . LYS E 3 51  ? 112.607 111.727 191.271 1.00 94.28  ? 51  LYS E O     1 
ATOM   16083 C  CB    . LYS E 3 51  ? 111.070 112.686 193.800 1.00 94.28  ? 51  LYS E CB    1 
ATOM   16084 C  CG    . LYS E 3 51  ? 110.348 113.980 193.424 1.00 94.28  ? 51  LYS E CG    1 
ATOM   16085 C  CD    . LYS E 3 51  ? 110.704 115.013 194.490 1.00 94.28  ? 51  LYS E CD    1 
ATOM   16086 C  CE    . LYS E 3 51  ? 110.009 116.342 194.236 1.00 94.28  ? 51  LYS E CE    1 
ATOM   16087 N  NZ    . LYS E 3 51  ? 110.456 117.316 195.249 1.00 94.28  ? 51  LYS E NZ    1 
ATOM   16088 N  N     . ILE E 3 52  ? 110.561 112.113 190.456 1.00 96.24  ? 52  ILE E N     1 
ATOM   16089 C  CA    . ILE E 3 52  ? 111.035 112.494 189.123 1.00 96.24  ? 52  ILE E CA    1 
ATOM   16090 C  C     . ILE E 3 52  ? 110.843 113.997 188.951 1.00 96.24  ? 52  ILE E C     1 
ATOM   16091 O  O     . ILE E 3 52  ? 109.740 114.522 189.127 1.00 96.24  ? 52  ILE E O     1 
ATOM   16092 C  CB    . ILE E 3 52  ? 110.370 111.650 188.020 1.00 96.24  ? 52  ILE E CB    1 
ATOM   16093 C  CG1   . ILE E 3 52  ? 110.610 110.143 188.289 1.00 96.24  ? 52  ILE E CG1   1 
ATOM   16094 C  CG2   . ILE E 3 52  ? 110.919 112.061 186.639 1.00 96.24  ? 52  ILE E CG2   1 
ATOM   16095 C  CD1   . ILE E 3 52  ? 110.074 109.211 187.199 1.00 96.24  ? 52  ILE E CD1   1 
ATOM   16096 N  N     . VAL E 3 53  ? 111.925 114.688 188.608 1.00 96.81  ? 53  VAL E N     1 
ATOM   16097 C  CA    . VAL E 3 53  ? 111.955 116.134 188.373 1.00 96.81  ? 53  VAL E CA    1 
ATOM   16098 C  C     . VAL E 3 53  ? 112.374 116.374 186.928 1.00 96.81  ? 53  VAL E C     1 
ATOM   16099 O  O     . VAL E 3 53  ? 113.372 115.834 186.478 1.00 96.81  ? 53  VAL E O     1 
ATOM   16100 C  CB    . VAL E 3 53  ? 112.896 116.835 189.372 1.00 96.81  ? 53  VAL E CB    1 
ATOM   16101 C  CG1   . VAL E 3 53  ? 113.022 118.332 189.069 1.00 96.81  ? 53  VAL E CG1   1 
ATOM   16102 C  CG2   . VAL E 3 53  ? 112.380 116.703 190.812 1.00 96.81  ? 53  VAL E CG2   1 
ATOM   16103 N  N     . LYS E 3 54  ? 111.639 117.192 186.179 1.00 96.68  ? 54  LYS E N     1 
ATOM   16104 C  CA    . LYS E 3 54  ? 112.006 117.626 184.825 1.00 96.68  ? 54  LYS E CA    1 
ATOM   16105 C  C     . LYS E 3 54  ? 112.384 119.098 184.848 1.00 96.68  ? 54  LYS E C     1 
ATOM   16106 O  O     . LYS E 3 54  ? 111.653 119.903 185.423 1.00 96.68  ? 54  LYS E O     1 
ATOM   16107 C  CB    . LYS E 3 54  ? 110.854 117.368 183.843 1.00 96.68  ? 54  LYS E CB    1 
ATOM   16108 C  CG    . LYS E 3 54  ? 110.626 115.873 183.575 1.00 96.68  ? 54  LYS E CG    1 
ATOM   16109 C  CD    . LYS E 3 54  ? 109.496 115.637 182.563 1.00 96.68  ? 54  LYS E CD    1 
ATOM   16110 C  CE    . LYS E 3 54  ? 109.901 115.949 181.114 1.00 96.68  ? 54  LYS E CE    1 
ATOM   16111 N  NZ    . LYS E 3 54  ? 110.604 114.807 180.484 1.00 96.68  ? 54  LYS E NZ    1 
ATOM   16112 N  N     . ILE E 3 55  ? 113.467 119.460 184.173 1.00 96.24  ? 55  ILE E N     1 
ATOM   16113 C  CA    . ILE E 3 55  ? 113.911 120.847 184.019 1.00 96.24  ? 55  ILE E CA    1 
ATOM   16114 C  C     . ILE E 3 55  ? 114.211 121.141 182.550 1.00 96.24  ? 55  ILE E C     1 
ATOM   16115 O  O     . ILE E 3 55  ? 114.979 120.429 181.902 1.00 96.24  ? 55  ILE E O     1 
ATOM   16116 C  CB    . ILE E 3 55  ? 115.082 121.152 184.973 1.00 96.24  ? 55  ILE E CB    1 
ATOM   16117 C  CG1   . ILE E 3 55  ? 115.418 122.655 184.899 1.00 96.24  ? 55  ILE E CG1   1 
ATOM   16118 C  CG2   . ILE E 3 55  ? 116.317 120.269 184.715 1.00 96.24  ? 55  ILE E CG2   1 
ATOM   16119 C  CD1   . ILE E 3 55  ? 116.326 123.116 186.036 1.00 96.24  ? 55  ILE E CD1   1 
ATOM   16120 N  N     . ASP E 3 56  ? 113.546 122.162 182.011 1.00 95.13  ? 56  ASP E N     1 
ATOM   16121 C  CA    . ASP E 3 56  ? 113.748 122.594 180.629 1.00 95.13  ? 56  ASP E CA    1 
ATOM   16122 C  C     . ASP E 3 56  ? 115.008 123.462 180.542 1.00 95.13  ? 56  ASP E C     1 
ATOM   16123 O  O     . ASP E 3 56  ? 115.054 124.548 181.125 1.00 95.13  ? 56  ASP E O     1 
ATOM   16124 C  CB    . ASP E 3 56  ? 112.504 123.336 180.116 1.00 95.13  ? 56  ASP E CB    1 
ATOM   16125 C  CG    . ASP E 3 56  ? 112.557 123.592 178.604 1.00 95.13  ? 56  ASP E CG    1 
ATOM   16126 O  OD1   . ASP E 3 56  ? 113.674 123.614 178.037 1.00 95.13  ? 56  ASP E OD1   1 
ATOM   16127 O  OD2   . ASP E 3 56  ? 111.463 123.690 178.006 1.00 95.13  ? 56  ASP E OD2   1 
ATOM   16128 N  N     . VAL E 3 57  ? 116.049 122.991 179.855 1.00 94.14  ? 57  VAL E N     1 
ATOM   16129 C  CA    . VAL E 3 57  ? 117.310 123.737 179.762 1.00 94.14  ? 57  VAL E CA    1 
ATOM   16130 C  C     . VAL E 3 57  ? 117.127 125.045 178.994 1.00 94.14  ? 57  VAL E C     1 
ATOM   16131 O  O     . VAL E 3 57  ? 117.755 126.043 179.332 1.00 94.14  ? 57  VAL E O     1 
ATOM   16132 C  CB    . VAL E 3 57  ? 118.449 122.910 179.145 1.00 94.14  ? 57  VAL E CB    1 
ATOM   16133 C  CG1   . VAL E 3 57  ? 118.665 121.617 179.928 1.00 94.14  ? 57  VAL E CG1   1 
ATOM   16134 C  CG2   . VAL E 3 57  ? 118.225 122.561 177.674 1.00 94.14  ? 57  VAL E CG2   1 
ATOM   16135 N  N     . ASP E 3 58  ? 116.202 125.111 178.029 1.00 91.19  ? 58  ASP E N     1 
ATOM   16136 C  CA    . ASP E 3 58  ? 115.988 126.336 177.250 1.00 91.19  ? 58  ASP E CA    1 
ATOM   16137 C  C     . ASP E 3 58  ? 115.470 127.493 178.112 1.00 91.19  ? 58  ASP E C     1 
ATOM   16138 O  O     . ASP E 3 58  ? 115.643 128.657 177.742 1.00 91.19  ? 58  ASP E O     1 
ATOM   16139 C  CB    . ASP E 3 58  ? 114.961 126.099 176.135 1.00 91.19  ? 58  ASP E CB    1 
ATOM   16140 C  CG    . ASP E 3 58  ? 115.484 125.429 174.871 1.00 91.19  ? 58  ASP E CG    1 
ATOM   16141 O  OD1   . ASP E 3 58  ? 116.707 125.240 174.680 1.00 91.19  ? 58  ASP E OD1   1 
ATOM   16142 O  OD2   . ASP E 3 58  ? 114.652 125.265 173.953 1.00 91.19  ? 58  ASP E OD2   1 
ATOM   16143 N  N     . GLU E 3 59  ? 114.815 127.190 179.231 1.00 92.47  ? 59  GLU E N     1 
ATOM   16144 C  CA    . GLU E 3 59  ? 114.261 128.189 180.154 1.00 92.47  ? 59  GLU E CA    1 
ATOM   16145 C  C     . GLU E 3 59  ? 115.060 128.298 181.459 1.00 92.47  ? 59  GLU E C     1 
ATOM   16146 O  O     . GLU E 3 59  ? 114.876 129.262 182.197 1.00 92.47  ? 59  GLU E O     1 
ATOM   16147 C  CB    . GLU E 3 59  ? 112.777 127.887 180.434 1.00 92.47  ? 59  GLU E CB    1 
ATOM   16148 C  CG    . GLU E 3 59  ? 111.905 127.943 179.167 1.00 92.47  ? 59  GLU E CG    1 
ATOM   16149 C  CD    . GLU E 3 59  ? 110.391 127.946 179.458 1.00 92.47  ? 59  GLU E CD    1 
ATOM   16150 O  OE1   . GLU E 3 59  ? 109.973 127.491 180.548 1.00 92.47  ? 59  GLU E OE1   1 
ATOM   16151 O  OE2   . GLU E 3 59  ? 109.644 128.448 178.580 1.00 92.47  ? 59  GLU E OE2   1 
ATOM   16152 N  N     . ASN E 3 60  ? 115.927 127.320 181.743 1.00 94.69  ? 60  ASN E N     1 
ATOM   16153 C  CA    . ASN E 3 60  ? 116.637 127.179 183.014 1.00 94.69  ? 60  ASN E CA    1 
ATOM   16154 C  C     . ASN E 3 60  ? 118.124 126.860 182.788 1.00 94.69  ? 60  ASN E C     1 
ATOM   16155 O  O     . ASN E 3 60  ? 118.636 125.782 183.123 1.00 94.69  ? 60  ASN E O     1 
ATOM   16156 C  CB    . ASN E 3 60  ? 115.929 126.133 183.882 1.00 94.69  ? 60  ASN E CB    1 
ATOM   16157 C  CG    . ASN E 3 60  ? 114.466 126.445 184.085 1.00 94.69  ? 60  ASN E CG    1 
ATOM   16158 O  OD1   . ASN E 3 60  ? 114.078 127.217 184.946 1.00 94.69  ? 60  ASN E OD1   1 
ATOM   16159 N  ND2   . ASN E 3 60  ? 113.607 125.839 183.299 1.00 94.69  ? 60  ASN E ND2   1 
ATOM   16160 N  N     . GLN E 3 61  ? 118.820 127.766 182.119 1.00 94.07  ? 61  GLN E N     1 
ATOM   16161 C  CA    . GLN E 3 61  ? 120.212 127.554 181.765 1.00 94.07  ? 61  GLN E CA    1 
ATOM   16162 C  C     . GLN E 3 61  ? 121.165 127.589 182.966 1.00 94.07  ? 61  GLN E C     1 
ATOM   16163 O  O     . GLN E 3 61  ? 122.217 126.966 182.898 1.00 94.07  ? 61  GLN E O     1 
ATOM   16164 C  CB    . GLN E 3 61  ? 120.596 128.632 180.764 1.00 94.07  ? 61  GLN E CB    1 
ATOM   16165 C  CG    . GLN E 3 61  ? 120.127 128.351 179.341 1.00 94.07  ? 61  GLN E CG    1 
ATOM   16166 C  CD    . GLN E 3 61  ? 118.814 128.969 178.879 1.00 94.07  ? 61  GLN E CD    1 
ATOM   16167 O  OE1   . GLN E 3 61  ? 117.948 129.380 179.650 1.00 94.07  ? 61  GLN E OE1   1 
ATOM   16168 N  NE2   . GLN E 3 61  ? 118.664 129.085 177.573 1.00 94.07  ? 61  GLN E NE2   1 
ATOM   16169 N  N     . GLU E 3 62  ? 120.815 128.263 184.068 1.00 94.65  ? 62  GLU E N     1 
ATOM   16170 C  CA    . GLU E 3 62  ? 121.714 128.369 185.224 1.00 94.65  ? 62  GLU E CA    1 
ATOM   16171 C  C     . GLU E 3 62  ? 121.905 127.010 185.902 1.00 94.65  ? 62  GLU E C     1 
ATOM   16172 O  O     . GLU E 3 62  ? 123.038 126.603 186.172 1.00 94.65  ? 62  GLU E O     1 
ATOM   16173 C  CB    . GLU E 3 62  ? 121.224 129.411 186.247 1.00 94.65  ? 62  GLU E CB    1 
ATOM   16174 C  CG    . GLU E 3 62  ? 121.185 130.845 185.689 1.00 94.65  ? 62  GLU E CG    1 
ATOM   16175 C  CD    . GLU E 3 62  ? 120.844 131.922 186.739 1.00 94.65  ? 62  GLU E CD    1 
ATOM   16176 O  OE1   . GLU E 3 62  ? 120.544 131.563 187.902 1.00 94.65  ? 62  GLU E OE1   1 
ATOM   16177 O  OE2   . GLU E 3 62  ? 120.948 133.124 186.382 1.00 94.65  ? 62  GLU E OE2   1 
ATOM   16178 N  N     . THR E 3 63  ? 120.826 126.254 186.106 1.00 95.30  ? 63  THR E N     1 
ATOM   16179 C  CA    . THR E 3 63  ? 120.882 124.907 186.688 1.00 95.30  ? 63  THR E CA    1 
ATOM   16180 C  C     . THR E 3 63  ? 121.600 123.949 185.756 1.00 95.30  ? 63  THR E C     1 
ATOM   16181 O  O     . THR E 3 63  ? 122.488 123.217 186.198 1.00 95.30  ? 63  THR E O     1 
ATOM   16182 C  CB    . THR E 3 63  ? 119.484 124.363 186.993 1.00 95.30  ? 63  THR E CB    1 
ATOM   16183 O  OG1   . THR E 3 63  ? 118.850 125.215 187.899 1.00 95.30  ? 63  THR E OG1   1 
ATOM   16184 C  CG2   . THR E 3 63  ? 119.523 123.010 187.689 1.00 95.30  ? 63  THR E CG2   1 
ATOM   16185 N  N     . ALA E 3 64  ? 121.296 123.968 184.459 1.00 93.68  ? 64  ALA E N     1 
ATOM   16186 C  CA    . ALA E 3 64  ? 121.996 123.109 183.508 1.00 93.68  ? 64  ALA E CA    1 
ATOM   16187 C  C     . ALA E 3 64  ? 123.510 123.405 183.485 1.00 93.68  ? 64  ALA E C     1 
ATOM   16188 O  O     . ALA E 3 64  ? 124.331 122.484 183.486 1.00 93.68  ? 64  ALA E O     1 
ATOM   16189 C  CB    . ALA E 3 64  ? 121.319 123.278 182.147 1.00 93.68  ? 64  ALA E CB    1 
ATOM   16190 N  N     . GLY E 3 65  ? 123.879 124.691 183.573 1.00 91.87  ? 65  GLY E N     1 
ATOM   16191 C  CA    . GLY E 3 65  ? 125.268 125.114 183.720 1.00 91.87  ? 65  GLY E CA    1 
ATOM   16192 C  C     . GLY E 3 65  ? 125.915 124.667 185.035 1.00 91.87  ? 65  GLY E C     1 
ATOM   16193 O  O     . GLY E 3 65  ? 127.037 124.156 185.019 1.00 91.87  ? 65  GLY E O     1 
ATOM   16194 N  N     . LYS E 3 66  ? 125.211 124.796 186.168 1.00 93.09  ? 66  LYS E N     1 
ATOM   16195 C  CA    . LYS E 3 66  ? 125.679 124.385 187.506 1.00 93.09  ? 66  LYS E CA    1 
ATOM   16196 C  C     . LYS E 3 66  ? 126.036 122.901 187.560 1.00 93.09  ? 66  LYS E C     1 
ATOM   16197 O  O     . LYS E 3 66  ? 127.056 122.541 188.142 1.00 93.09  ? 66  LYS E O     1 
ATOM   16198 C  CB    . LYS E 3 66  ? 124.591 124.721 188.541 1.00 93.09  ? 66  LYS E CB    1 
ATOM   16199 C  CG    . LYS E 3 66  ? 124.996 124.370 189.983 1.00 93.09  ? 66  LYS E CG    1 
ATOM   16200 C  CD    . LYS E 3 66  ? 123.820 124.596 190.941 1.00 93.09  ? 66  LYS E CD    1 
ATOM   16201 C  CE    . LYS E 3 66  ? 124.197 124.165 192.364 1.00 93.09  ? 66  LYS E CE    1 
ATOM   16202 N  NZ    . LYS E 3 66  ? 123.014 124.182 193.262 1.00 93.09  ? 66  LYS E NZ    1 
ATOM   16203 N  N     . TYR E 3 67  ? 125.209 122.021 187.013 1.00 91.99  ? 67  TYR E N     1 
ATOM   16204 C  CA    . TYR E 3 67  ? 125.488 120.588 187.099 1.00 91.99  ? 67  TYR E CA    1 
ATOM   16205 C  C     . TYR E 3 67  ? 126.573 120.110 186.123 1.00 91.99  ? 67  TYR E C     1 
ATOM   16206 O  O     . TYR E 3 67  ? 126.947 118.928 186.127 1.00 91.99  ? 67  TYR E O     1 
ATOM   16207 C  CB    . TYR E 3 67  ? 124.176 119.815 186.995 1.00 91.99  ? 67  TYR E CB    1 
ATOM   16208 C  CG    . TYR E 3 67  ? 123.434 119.828 188.311 1.00 91.99  ? 67  TYR E CG    1 
ATOM   16209 C  CD1   . TYR E 3 67  ? 123.934 119.065 189.383 1.00 91.99  ? 67  TYR E CD1   1 
ATOM   16210 C  CD2   . TYR E 3 67  ? 122.318 120.657 188.504 1.00 91.99  ? 67  TYR E CD2   1 
ATOM   16211 C  CE1   . TYR E 3 67  ? 123.306 119.116 190.637 1.00 91.99  ? 67  TYR E CE1   1 
ATOM   16212 C  CE2   . TYR E 3 67  ? 121.687 120.713 189.762 1.00 91.99  ? 67  TYR E CE2   1 
ATOM   16213 C  CZ    . TYR E 3 67  ? 122.176 119.939 190.830 1.00 91.99  ? 67  TYR E CZ    1 
ATOM   16214 O  OH    . TYR E 3 67  ? 121.586 119.984 192.051 1.00 91.99  ? 67  TYR E OH    1 
ATOM   16215 N  N     . GLY E 3 68  ? 127.119 121.000 185.287 1.00 87.95  ? 68  GLY E N     1 
ATOM   16216 C  CA    . GLY E 3 68  ? 128.048 120.622 184.228 1.00 87.95  ? 68  GLY E CA    1 
ATOM   16217 C  C     . GLY E 3 68  ? 127.374 119.678 183.230 1.00 87.95  ? 68  GLY E C     1 
ATOM   16218 O  O     . GLY E 3 68  ? 127.966 118.680 182.811 1.00 87.95  ? 68  GLY E O     1 
ATOM   16219 N  N     . VAL E 3 69  ? 126.097 119.933 182.928 1.00 88.85  ? 69  VAL E N     1 
ATOM   16220 C  CA    . VAL E 3 69  ? 125.397 119.321 181.796 1.00 88.85  ? 69  VAL E CA    1 
ATOM   16221 C  C     . VAL E 3 69  ? 125.884 120.022 180.527 1.00 88.85  ? 69  VAL E C     1 
ATOM   16222 O  O     . VAL E 3 69  ? 125.980 121.246 180.498 1.00 88.85  ? 69  VAL E O     1 
ATOM   16223 C  CB    . VAL E 3 69  ? 123.867 119.427 181.952 1.00 88.85  ? 69  VAL E CB    1 
ATOM   16224 C  CG1   . VAL E 3 69  ? 123.141 118.679 180.832 1.00 88.85  ? 69  VAL E CG1   1 
ATOM   16225 C  CG2   . VAL E 3 69  ? 123.394 118.824 183.278 1.00 88.85  ? 69  VAL E CG2   1 
ATOM   16226 N  N     . MET E 3 70  ? 126.222 119.257 179.489 1.00 88.20  ? 70  MET E N     1 
ATOM   16227 C  CA    . MET E 3 70  ? 126.773 119.769 178.223 1.00 88.20  ? 70  MET E CA    1 
ATOM   16228 C  C     . MET E 3 70  ? 126.171 119.031 177.010 1.00 88.20  ? 70  MET E C     1 
ATOM   16229 O  O     . MET E 3 70  ? 126.737 119.038 175.917 1.00 88.20  ? 70  MET E O     1 
ATOM   16230 C  CB    . MET E 3 70  ? 128.313 119.702 178.237 1.00 88.20  ? 70  MET E CB    1 
ATOM   16231 C  CG    . MET E 3 70  ? 128.950 120.328 179.485 1.00 88.20  ? 70  MET E CG    1 
ATOM   16232 S  SD    . MET E 3 70  ? 130.749 120.196 179.587 1.00 88.20  ? 70  MET E SD    1 
ATOM   16233 C  CE    . MET E 3 70  ? 131.207 121.847 179.014 1.00 88.20  ? 70  MET E CE    1 
ATOM   16234 N  N     . SER E 3 71  ? 125.049 118.331 177.223 1.00 88.10  ? 71  SER E N     1 
ATOM   16235 C  CA    . SER E 3 71  ? 124.190 117.705 176.206 1.00 88.10  ? 71  SER E CA    1 
ATOM   16236 C  C     . SER E 3 71  ? 122.851 117.261 176.825 1.00 88.10  ? 71  SER E C     1 
ATOM   16237 O  O     . SER E 3 71  ? 122.730 117.098 178.042 1.00 88.10  ? 71  SER E O     1 
ATOM   16238 C  CB    . SER E 3 71  ? 124.874 116.484 175.574 1.00 88.10  ? 71  SER E CB    1 
ATOM   16239 O  OG    . SER E 3 71  ? 125.145 115.479 176.540 1.00 88.10  ? 71  SER E OG    1 
ATOM   16240 N  N     . ILE E 3 72  ? 121.849 117.004 175.985 1.00 90.57  ? 72  ILE E N     1 
ATOM   16241 C  CA    . ILE E 3 72  ? 120.542 116.455 176.389 1.00 90.57  ? 72  ILE E CA    1 
ATOM   16242 C  C     . ILE E 3 72  ? 120.110 115.264 175.508 1.00 90.57  ? 72  ILE E C     1 
ATOM   16243 O  O     . ILE E 3 72  ? 120.589 115.135 174.378 1.00 90.57  ? 72  ILE E O     1 
ATOM   16244 C  CB    . ILE E 3 72  ? 119.462 117.555 176.433 1.00 90.57  ? 72  ILE E CB    1 
ATOM   16245 C  CG1   . ILE E 3 72  ? 119.352 118.329 175.105 1.00 90.57  ? 72  ILE E CG1   1 
ATOM   16246 C  CG2   . ILE E 3 72  ? 119.699 118.481 177.636 1.00 90.57  ? 72  ILE E CG2   1 
ATOM   16247 C  CD1   . ILE E 3 72  ? 118.119 119.231 175.058 1.00 90.57  ? 72  ILE E CD1   1 
ATOM   16248 N  N     . PRO E 3 73  ? 119.233 114.369 176.007 1.00 93.49  ? 73  PRO E N     1 
ATOM   16249 C  CA    . PRO E 3 73  ? 118.763 114.268 177.387 1.00 93.49  ? 73  PRO E CA    1 
ATOM   16250 C  C     . PRO E 3 73  ? 119.880 113.888 178.365 1.00 93.49  ? 73  PRO E C     1 
ATOM   16251 O  O     . PRO E 3 73  ? 120.744 113.067 178.070 1.00 93.49  ? 73  PRO E O     1 
ATOM   16252 C  CB    . PRO E 3 73  ? 117.662 113.201 177.380 1.00 93.49  ? 73  PRO E CB    1 
ATOM   16253 C  CG    . PRO E 3 73  ? 117.975 112.357 176.152 1.00 93.49  ? 73  PRO E CG    1 
ATOM   16254 C  CD    . PRO E 3 73  ? 118.581 113.367 175.191 1.00 93.49  ? 73  PRO E CD    1 
ATOM   16255 N  N     . THR E 3 74  ? 119.852 114.483 179.556 1.00 93.65  ? 74  THR E N     1 
ATOM   16256 C  CA    . THR E 3 74  ? 120.736 114.114 180.667 1.00 93.65  ? 74  THR E CA    1 
ATOM   16257 C  C     . THR E 3 74  ? 119.923 113.826 181.917 1.00 93.65  ? 74  THR E C     1 
ATOM   16258 O  O     . THR E 3 74  ? 119.166 114.670 182.386 1.00 93.65  ? 74  THR E O     1 
ATOM   16259 C  CB    . THR E 3 74  ? 121.793 115.192 180.943 1.00 93.65  ? 74  THR E CB    1 
ATOM   16260 O  OG1   . THR E 3 74  ? 122.768 115.143 179.933 1.00 93.65  ? 74  THR E OG1   1 
ATOM   16261 C  CG2   . THR E 3 74  ? 122.536 114.972 182.266 1.00 93.65  ? 74  THR E CG2   1 
ATOM   16262 N  N     . LEU E 3 75  ? 120.122 112.635 182.478 1.00 95.19  ? 75  LEU E N     1 
ATOM   16263 C  CA    . LEU E 3 75  ? 119.472 112.181 183.690 1.00 95.19  ? 75  LEU E CA    1 
ATOM   16264 C  C     . LEU E 3 75  ? 120.483 112.173 184.832 1.00 95.19  ? 75  LEU E C     1 
ATOM   16265 O  O     . LEU E 3 75  ? 121.492 111.466 184.765 1.00 95.19  ? 75  LEU E O     1 
ATOM   16266 C  CB    . LEU E 3 75  ? 118.885 110.789 183.460 1.00 95.19  ? 75  LEU E CB    1 
ATOM   16267 C  CG    . LEU E 3 75  ? 117.800 110.703 182.376 1.00 95.19  ? 75  LEU E CG    1 
ATOM   16268 C  CD1   . LEU E 3 75  ? 117.372 109.253 182.296 1.00 95.19  ? 75  LEU E CD1   1 
ATOM   16269 C  CD2   . LEU E 3 75  ? 116.570 111.540 182.687 1.00 95.19  ? 75  LEU E CD2   1 
ATOM   16270 N  N     . LEU E 3 76  ? 120.206 112.935 185.884 1.00 95.47  ? 76  LEU E N     1 
ATOM   16271 C  CA    . LEU E 3 76  ? 120.978 112.914 187.122 1.00 95.47  ? 76  LEU E CA    1 
ATOM   16272 C  C     . LEU E 3 76  ? 120.190 112.159 188.185 1.00 95.47  ? 76  LEU E C     1 
ATOM   16273 O  O     . LEU E 3 76  ? 119.033 112.486 188.442 1.00 95.47  ? 76  LEU E O     1 
ATOM   16274 C  CB    . LEU E 3 76  ? 121.321 114.342 187.583 1.00 95.47  ? 76  LEU E CB    1 
ATOM   16275 C  CG    . LEU E 3 76  ? 122.037 115.218 186.543 1.00 95.47  ? 76  LEU E CG    1 
ATOM   16276 C  CD1   . LEU E 3 76  ? 122.423 116.556 187.171 1.00 95.47  ? 76  LEU E CD1   1 
ATOM   16277 C  CD2   . LEU E 3 76  ? 123.315 114.574 186.018 1.00 95.47  ? 76  LEU E CD2   1 
ATOM   16278 N  N     . VAL E 3 77  ? 120.820 111.177 188.826 1.00 96.40  ? 77  VAL E N     1 
ATOM   16279 C  CA    . VAL E 3 77  ? 120.308 110.619 190.080 1.00 96.40  ? 77  VAL E CA    1 
ATOM   16280 C  C     . VAL E 3 77  ? 120.918 111.435 191.199 1.00 96.40  ? 77  VAL E C     1 
ATOM   16281 O  O     . VAL E 3 77  ? 122.143 111.468 191.348 1.00 96.40  ? 77  VAL E O     1 
ATOM   16282 C  CB    . VAL E 3 77  ? 120.620 109.127 190.258 1.00 96.40  ? 77  VAL E CB    1 
ATOM   16283 C  CG1   . VAL E 3 77  ? 119.946 108.572 191.521 1.00 96.40  ? 77  VAL E CG1   1 
ATOM   16284 C  CG2   . VAL E 3 77  ? 120.092 108.319 189.078 1.00 96.40  ? 77  VAL E CG2   1 
ATOM   16285 N  N     . LEU E 3 78  ? 120.068 112.103 191.966 1.00 96.12  ? 78  LEU E N     1 
ATOM   16286 C  CA    . LEU E 3 78  ? 120.455 112.812 193.171 1.00 96.12  ? 78  LEU E CA    1 
ATOM   16287 C  C     . LEU E 3 78  ? 119.979 112.035 194.394 1.00 96.12  ? 78  LEU E C     1 
ATOM   16288 O  O     . LEU E 3 78  ? 118.874 111.492 194.392 1.00 96.12  ? 78  LEU E O     1 
ATOM   16289 C  CB    . LEU E 3 78  ? 119.956 114.267 193.175 1.00 96.12  ? 78  LEU E CB    1 
ATOM   16290 C  CG    . LEU E 3 78  ? 120.438 115.085 191.959 1.00 96.12  ? 78  LEU E CG    1 
ATOM   16291 C  CD1   . LEU E 3 78  ? 119.363 115.169 190.872 1.00 96.12  ? 78  LEU E CD1   1 
ATOM   16292 C  CD2   . LEU E 3 78  ? 120.799 116.516 192.362 1.00 96.12  ? 78  LEU E CD2   1 
ATOM   16293 N  N     . LYS E 3 79  ? 120.807 112.004 195.434 1.00 95.93  ? 79  LYS E N     1 
ATOM   16294 C  CA    . LYS E 3 79  ? 120.454 111.494 196.754 1.00 95.93  ? 79  LYS E CA    1 
ATOM   16295 C  C     . LYS E 3 79  ? 120.757 112.569 197.784 1.00 95.93  ? 79  LYS E C     1 
ATOM   16296 O  O     . LYS E 3 79  ? 121.904 112.994 197.891 1.00 95.93  ? 79  LYS E O     1 
ATOM   16297 C  CB    . LYS E 3 79  ? 121.195 110.181 197.023 1.00 95.93  ? 79  LYS E CB    1 
ATOM   16298 C  CG    . LYS E 3 79  ? 120.726 109.556 198.343 1.00 95.93  ? 79  LYS E CG    1 
ATOM   16299 C  CD    . LYS E 3 79  ? 121.241 108.121 198.465 1.00 95.93  ? 79  LYS E CD    1 
ATOM   16300 C  CE    . LYS E 3 79  ? 120.637 107.464 199.709 1.00 95.93  ? 79  LYS E CE    1 
ATOM   16301 N  NZ    . LYS E 3 79  ? 120.650 105.985 199.586 1.00 95.93  ? 79  LYS E NZ    1 
ATOM   16302 N  N     . ASP E 3 80  ? 119.728 113.028 198.489 1.00 94.33  ? 80  ASP E N     1 
ATOM   16303 C  CA    . ASP E 3 80  ? 119.841 114.063 199.527 1.00 94.33  ? 80  ASP E CA    1 
ATOM   16304 C  C     . ASP E 3 80  ? 120.611 115.316 199.041 1.00 94.33  ? 80  ASP E C     1 
ATOM   16305 O  O     . ASP E 3 80  ? 121.469 115.868 199.729 1.00 94.33  ? 80  ASP E O     1 
ATOM   16306 C  CB    . ASP E 3 80  ? 120.374 113.442 200.831 1.00 94.33  ? 80  ASP E CB    1 
ATOM   16307 C  CG    . ASP E 3 80  ? 119.524 112.251 201.295 1.00 94.33  ? 80  ASP E CG    1 
ATOM   16308 O  OD1   . ASP E 3 80  ? 118.276 112.391 201.309 1.00 94.33  ? 80  ASP E OD1   1 
ATOM   16309 O  OD2   . ASP E 3 80  ? 120.113 111.187 201.608 1.00 94.33  ? 80  ASP E OD2   1 
ATOM   16310 N  N     . GLY E 3 81  ? 120.332 115.740 197.802 1.00 93.05  ? 81  GLY E N     1 
ATOM   16311 C  CA    . GLY E 3 81  ? 120.947 116.907 197.163 1.00 93.05  ? 81  GLY E CA    1 
ATOM   16312 C  C     . GLY E 3 81  ? 122.257 116.659 196.405 1.00 93.05  ? 81  GLY E C     1 
ATOM   16313 O  O     . GLY E 3 81  ? 122.636 117.509 195.594 1.00 93.05  ? 81  GLY E O     1 
ATOM   16314 N  N     . GLU E 3 82  ? 122.931 115.520 196.590 1.00 95.02  ? 82  GLU E N     1 
ATOM   16315 C  CA    . GLU E 3 82  ? 124.180 115.202 195.883 1.00 95.02  ? 82  GLU E CA    1 
ATOM   16316 C  C     . GLU E 3 82  ? 123.957 114.319 194.655 1.00 95.02  ? 82  GLU E C     1 
ATOM   16317 O  O     . GLU E 3 82  ? 123.184 113.365 194.690 1.00 95.02  ? 82  GLU E O     1 
ATOM   16318 C  CB    . GLU E 3 82  ? 125.226 114.565 196.806 1.00 95.02  ? 82  GLU E CB    1 
ATOM   16319 C  CG    . GLU E 3 82  ? 125.750 115.549 197.868 1.00 95.02  ? 82  GLU E CG    1 
ATOM   16320 C  CD    . GLU E 3 82  ? 127.231 115.337 198.237 1.00 95.02  ? 82  GLU E CD    1 
ATOM   16321 O  OE1   . GLU E 3 82  ? 127.797 114.262 197.931 1.00 95.02  ? 82  GLU E OE1   1 
ATOM   16322 O  OE2   . GLU E 3 82  ? 127.821 116.289 198.799 1.00 95.02  ? 82  GLU E OE2   1 
ATOM   16323 N  N     . VAL E 3 83  ? 124.661 114.610 193.557 1.00 95.68  ? 83  VAL E N     1 
ATOM   16324 C  CA    . VAL E 3 83  ? 124.615 113.786 192.338 1.00 95.68  ? 83  VAL E CA    1 
ATOM   16325 C  C     . VAL E 3 83  ? 125.428 112.514 192.560 1.00 95.68  ? 83  VAL E C     1 
ATOM   16326 O  O     . VAL E 3 83  ? 126.646 112.572 192.711 1.00 95.68  ? 83  VAL E O     1 
ATOM   16327 C  CB    . VAL E 3 83  ? 125.136 114.543 191.103 1.00 95.68  ? 83  VAL E CB    1 
ATOM   16328 C  CG1   . VAL E 3 83  ? 125.052 113.682 189.833 1.00 95.68  ? 83  VAL E CG1   1 
ATOM   16329 C  CG2   . VAL E 3 83  ? 124.326 115.816 190.849 1.00 95.68  ? 83  VAL E CG2   1 
ATOM   16330 N  N     . VAL E 3 84  ? 124.755 111.365 192.531 1.00 95.67  ? 84  VAL E N     1 
ATOM   16331 C  CA    . VAL E 3 84  ? 125.366 110.044 192.752 1.00 95.67  ? 84  VAL E CA    1 
ATOM   16332 C  C     . VAL E 3 84  ? 125.576 109.258 191.460 1.00 95.67  ? 84  VAL E C     1 
ATOM   16333 O  O     . VAL E 3 84  ? 126.483 108.431 191.385 1.00 95.67  ? 84  VAL E O     1 
ATOM   16334 C  CB    . VAL E 3 84  ? 124.559 109.217 193.770 1.00 95.67  ? 84  VAL E CB    1 
ATOM   16335 C  CG1   . VAL E 3 84  ? 124.629 109.851 195.162 1.00 95.67  ? 84  VAL E CG1   1 
ATOM   16336 C  CG2   . VAL E 3 84  ? 123.083 109.043 193.393 1.00 95.67  ? 84  VAL E CG2   1 
ATOM   16337 N  N     . GLU E 3 85  ? 124.780 109.521 190.422 1.00 94.20  ? 85  GLU E N     1 
ATOM   16338 C  CA    . GLU E 3 85  ? 124.942 108.893 189.107 1.00 94.20  ? 85  GLU E CA    1 
ATOM   16339 C  C     . GLU E 3 85  ? 124.475 109.850 188.001 1.00 94.20  ? 85  GLU E C     1 
ATOM   16340 O  O     . GLU E 3 85  ? 123.612 110.706 188.202 1.00 94.20  ? 85  GLU E O     1 
ATOM   16341 C  CB    . GLU E 3 85  ? 124.240 107.511 189.086 1.00 94.20  ? 85  GLU E CB    1 
ATOM   16342 C  CG    . GLU E 3 85  ? 124.809 106.519 188.037 1.00 94.20  ? 85  GLU E CG    1 
ATOM   16343 C  CD    . GLU E 3 85  ? 124.615 105.010 188.372 1.00 94.20  ? 85  GLU E CD    1 
ATOM   16344 O  OE1   . GLU E 3 85  ? 124.216 104.672 189.502 1.00 94.20  ? 85  GLU E OE1   1 
ATOM   16345 O  OE2   . GLU E 3 85  ? 124.900 104.127 187.520 1.00 94.20  ? 85  GLU E OE2   1 
ATOM   16346 N  N     . THR E 3 86  ? 125.077 109.741 186.819 1.00 92.29  ? 86  THR E N     1 
ATOM   16347 C  CA    . THR E 3 86  ? 124.746 110.554 185.641 1.00 92.29  ? 86  THR E CA    1 
ATOM   16348 C  C     . THR E 3 86  ? 124.613 109.636 184.440 1.00 92.29  ? 86  THR E C     1 
ATOM   16349 O  O     . THR E 3 86  ? 125.495 108.821 184.172 1.00 92.29  ? 86  THR E O     1 
ATOM   16350 C  CB    . THR E 3 86  ? 125.819 111.620 185.379 1.00 92.29  ? 86  THR E CB    1 
ATOM   16351 O  OG1   . THR E 3 86  ? 125.862 112.510 186.467 1.00 92.29  ? 86  THR E OG1   1 
ATOM   16352 C  CG2   . THR E 3 86  ? 125.575 112.437 184.108 1.00 92.29  ? 86  THR E CG2   1 
ATOM   16353 N  N     . SER E 3 87  ? 123.518 109.777 183.701 1.00 91.65  ? 87  SER E N     1 
ATOM   16354 C  CA    . SER E 3 87  ? 123.250 109.034 182.477 1.00 91.65  ? 87  SER E CA    1 
ATOM   16355 C  C     . SER E 3 87  ? 122.905 110.003 181.358 1.00 91.65  ? 87  SER E C     1 
ATOM   16356 O  O     . SER E 3 87  ? 122.029 110.848 181.508 1.00 91.65  ? 87  SER E O     1 
ATOM   16357 C  CB    . SER E 3 87  ? 122.130 108.025 182.719 1.00 91.65  ? 87  SER E CB    1 
ATOM   16358 O  OG    . SER E 3 87  ? 121.802 107.375 181.504 1.00 91.65  ? 87  SER E OG    1 
ATOM   16359 N  N     . VAL E 3 88  ? 123.574 109.861 180.220 1.00 89.96  ? 88  VAL E N     1 
ATOM   16360 C  CA    . VAL E 3 88  ? 123.386 110.722 179.048 1.00 89.96  ? 88  VAL E CA    1 
ATOM   16361 C  C     . VAL E 3 88  ? 122.738 109.919 177.925 1.00 89.96  ? 88  VAL E C     1 
ATOM   16362 O  O     . VAL E 3 88  ? 123.078 108.749 177.722 1.00 89.96  ? 88  VAL E O     1 
ATOM   16363 C  CB    . VAL E 3 88  ? 124.727 111.342 178.615 1.00 89.96  ? 88  VAL E CB    1 
ATOM   16364 C  CG1   . VAL E 3 88  ? 124.564 112.239 177.387 1.00 89.96  ? 88  VAL E CG1   1 
ATOM   16365 C  CG2   . VAL E 3 88  ? 125.337 112.188 179.742 1.00 89.96  ? 88  VAL E CG2   1 
ATOM   16366 N  N     . GLY E 3 89  ? 121.829 110.564 177.196 1.00 88.38  ? 89  GLY E N     1 
ATOM   16367 C  CA    . GLY E 3 89  ? 121.102 109.974 176.077 1.00 88.38  ? 89  GLY E CA    1 
ATOM   16368 C  C     . GLY E 3 89  ? 119.864 109.197 176.511 1.00 88.38  ? 89  GLY E C     1 
ATOM   16369 O  O     . GLY E 3 89  ? 119.501 109.144 177.691 1.00 88.38  ? 89  GLY E O     1 
ATOM   16370 N  N     . PHE E 3 90  ? 119.181 108.605 175.535 1.00 89.87  ? 90  PHE E N     1 
ATOM   16371 C  CA    . PHE E 3 90  ? 117.973 107.839 175.802 1.00 89.87  ? 90  PHE E CA    1 
ATOM   16372 C  C     . PHE E 3 90  ? 118.297 106.556 176.580 1.00 89.87  ? 90  PHE E C     1 
ATOM   16373 O  O     . PHE E 3 90  ? 119.299 105.877 176.339 1.00 89.87  ? 90  PHE E O     1 
ATOM   16374 C  CB    . PHE E 3 90  ? 117.240 107.564 174.485 1.00 89.87  ? 90  PHE E CB    1 
ATOM   16375 C  CG    . PHE E 3 90  ? 116.032 106.665 174.641 1.00 89.87  ? 90  PHE E CG    1 
ATOM   16376 C  CD1   . PHE E 3 90  ? 114.807 107.188 175.097 1.00 89.87  ? 90  PHE E CD1   1 
ATOM   16377 C  CD2   . PHE E 3 90  ? 116.152 105.288 174.376 1.00 89.87  ? 90  PHE E CD2   1 
ATOM   16378 C  CE1   . PHE E 3 90  ? 113.707 106.332 175.283 1.00 89.87  ? 90  PHE E CE1   1 
ATOM   16379 C  CE2   . PHE E 3 90  ? 115.051 104.435 174.560 1.00 89.87  ? 90  PHE E CE2   1 
ATOM   16380 C  CZ    . PHE E 3 90  ? 113.828 104.958 175.012 1.00 89.87  ? 90  PHE E CZ    1 
ATOM   16381 N  N     . LYS E 3 91  ? 117.418 106.193 177.518 1.00 90.76  ? 91  LYS E N     1 
ATOM   16382 C  CA    . LYS E 3 91  ? 117.488 104.932 178.259 1.00 90.76  ? 91  LYS E CA    1 
ATOM   16383 C  C     . LYS E 3 91  ? 116.099 104.298 178.340 1.00 90.76  ? 91  LYS E C     1 
ATOM   16384 O  O     . LYS E 3 91  ? 115.135 105.014 178.613 1.00 90.76  ? 91  LYS E O     1 
ATOM   16385 C  CB    . LYS E 3 91  ? 118.039 105.167 179.670 1.00 90.76  ? 91  LYS E CB    1 
ATOM   16386 C  CG    . LYS E 3 91  ? 119.494 105.647 179.747 1.00 90.76  ? 91  LYS E CG    1 
ATOM   16387 C  CD    . LYS E 3 91  ? 120.503 104.614 179.230 1.00 90.76  ? 91  LYS E CD    1 
ATOM   16388 C  CE    . LYS E 3 91  ? 121.906 105.218 179.301 1.00 90.76  ? 91  LYS E CE    1 
ATOM   16389 N  NZ    . LYS E 3 91  ? 122.894 104.386 178.583 1.00 90.76  ? 91  LYS E NZ    1 
ATOM   16390 N  N     . PRO E 3 92  ? 115.988 102.975 178.131 1.00 92.45  ? 92  PRO E N     1 
ATOM   16391 C  CA    . PRO E 3 92  ? 114.744 102.253 178.365 1.00 92.45  ? 92  PRO E CA    1 
ATOM   16392 C  C     . PRO E 3 92  ? 114.431 102.184 179.864 1.00 92.45  ? 92  PRO E C     1 
ATOM   16393 O  O     . PRO E 3 92  ? 115.311 102.398 180.706 1.00 92.45  ? 92  PRO E O     1 
ATOM   16394 C  CB    . PRO E 3 92  ? 114.969 100.868 177.756 1.00 92.45  ? 92  PRO E CB    1 
ATOM   16395 C  CG    . PRO E 3 92  ? 116.465 100.643 177.966 1.00 92.45  ? 92  PRO E CG    1 
ATOM   16396 C  CD    . PRO E 3 92  ? 117.051 102.042 177.779 1.00 92.45  ? 92  PRO E CD    1 
ATOM   16397 N  N     . LYS E 3 93  ? 113.182 101.845 180.194 1.00 93.12  ? 93  LYS E N     1 
ATOM   16398 C  CA    . LYS E 3 93  ? 112.685 101.824 181.575 1.00 93.12  ? 93  LYS E CA    1 
ATOM   16399 C  C     . LYS E 3 93  ? 113.533 100.938 182.478 1.00 93.12  ? 93  LYS E C     1 
ATOM   16400 O  O     . LYS E 3 93  ? 113.946 101.379 183.543 1.00 93.12  ? 93  LYS E O     1 
ATOM   16401 C  CB    . LYS E 3 93  ? 111.226 101.346 181.580 1.00 93.12  ? 93  LYS E CB    1 
ATOM   16402 C  CG    . LYS E 3 93  ? 110.621 101.462 182.989 1.00 93.12  ? 93  LYS E CG    1 
ATOM   16403 C  CD    . LYS E 3 93  ? 109.125 101.151 182.992 1.00 93.12  ? 93  LYS E CD    1 
ATOM   16404 C  CE    . LYS E 3 93  ? 108.823 99.697  182.627 1.00 93.12  ? 93  LYS E CE    1 
ATOM   16405 N  NZ    . LYS E 3 93  ? 107.361 99.531  182.486 1.00 93.12  ? 93  LYS E NZ    1 
ATOM   16406 N  N     . GLU E 3 94  ? 113.849 99.728  182.033 1.00 93.86  ? 94  GLU E N     1 
ATOM   16407 C  CA    . GLU E 3 94  ? 114.579 98.729  182.818 1.00 93.86  ? 94  GLU E CA    1 
ATOM   16408 C  C     . GLU E 3 94  ? 115.974 99.239  183.200 1.00 93.86  ? 94  GLU E C     1 
ATOM   16409 O  O     . GLU E 3 94  ? 116.417 99.065  184.334 1.00 93.86  ? 94  GLU E O     1 
ATOM   16410 C  CB    . GLU E 3 94  ? 114.715 97.418  182.021 1.00 93.86  ? 94  GLU E CB    1 
ATOM   16411 C  CG    . GLU E 3 94  ? 113.386 96.747  181.622 1.00 93.86  ? 94  GLU E CG    1 
ATOM   16412 C  CD    . GLU E 3 94  ? 112.607 97.470  180.507 1.00 93.86  ? 94  GLU E CD    1 
ATOM   16413 O  OE1   . GLU E 3 94  ? 113.226 98.268  179.760 1.00 93.86  ? 94  GLU E OE1   1 
ATOM   16414 O  OE2   . GLU E 3 94  ? 111.379 97.257  180.425 1.00 93.86  ? 94  GLU E OE2   1 
ATOM   16415 N  N     . ALA E 3 95  ? 116.641 99.945  182.281 1.00 94.25  ? 95  ALA E N     1 
ATOM   16416 C  CA    . ALA E 3 95  ? 117.943 100.545 182.543 1.00 94.25  ? 95  ALA E CA    1 
ATOM   16417 C  C     . ALA E 3 95  ? 117.850 101.701 183.552 1.00 94.25  ? 95  ALA E C     1 
ATOM   16418 O  O     . ALA E 3 95  ? 118.744 101.858 184.381 1.00 94.25  ? 95  ALA E O     1 
ATOM   16419 C  CB    . ALA E 3 95  ? 118.552 101.009 181.216 1.00 94.25  ? 95  ALA E CB    1 
ATOM   16420 N  N     . LEU E 3 96  ? 116.776 102.499 183.510 1.00 93.58  ? 96  LEU E N     1 
ATOM   16421 C  CA    . LEU E 3 96  ? 116.537 103.557 184.498 1.00 93.58  ? 96  LEU E CA    1 
ATOM   16422 C  C     . LEU E 3 96  ? 116.196 102.994 185.874 1.00 93.58  ? 96  LEU E C     1 
ATOM   16423 O  O     . LEU E 3 96  ? 116.683 103.509 186.878 1.00 93.58  ? 96  LEU E O     1 
ATOM   16424 C  CB    . LEU E 3 96  ? 115.422 104.499 184.013 1.00 93.58  ? 96  LEU E CB    1 
ATOM   16425 C  CG    . LEU E 3 96  ? 115.778 105.288 182.748 1.00 93.58  ? 96  LEU E CG    1 
ATOM   16426 C  CD1   . LEU E 3 96  ? 114.656 106.266 182.407 1.00 93.58  ? 96  LEU E CD1   1 
ATOM   16427 C  CD2   . LEU E 3 96  ? 117.073 106.070 182.946 1.00 93.58  ? 96  LEU E CD2   1 
ATOM   16428 N  N     . GLN E 3 97  ? 115.423 101.911 185.927 1.00 93.40  ? 97  GLN E N     1 
ATOM   16429 C  CA    . GLN E 3 97  ? 115.135 101.198 187.168 1.00 93.40  ? 97  GLN E CA    1 
ATOM   16430 C  C     . GLN E 3 97  ? 116.413 100.656 187.795 1.00 93.40  ? 97  GLN E C     1 
ATOM   16431 O  O     . GLN E 3 97  ? 116.638 100.865 188.982 1.00 93.40  ? 97  GLN E O     1 
ATOM   16432 C  CB    . GLN E 3 97  ? 114.160 100.046 186.909 1.00 93.40  ? 97  GLN E CB    1 
ATOM   16433 C  CG    . GLN E 3 97  ? 112.764 100.581 186.606 1.00 93.40  ? 97  GLN E CG    1 
ATOM   16434 C  CD    . GLN E 3 97  ? 111.724 99.492  186.426 1.00 93.40  ? 97  GLN E CD    1 
ATOM   16435 O  OE1   . GLN E 3 97  ? 111.990 98.416  185.913 1.00 93.40  ? 97  GLN E OE1   1 
ATOM   16436 N  NE2   . GLN E 3 97  ? 110.510 99.781  186.836 1.00 93.40  ? 97  GLN E NE2   1 
ATOM   16437 N  N     . GLU E 3 98  ? 117.274 99.998  187.018 1.00 93.61  ? 98  GLU E N     1 
ATOM   16438 C  CA    . GLU E 3 98  ? 118.576 99.534  187.510 1.00 93.61  ? 98  GLU E CA    1 
ATOM   16439 C  C     . GLU E 3 98  ? 119.438 100.687 188.024 1.00 93.61  ? 98  GLU E C     1 
ATOM   16440 O  O     . GLU E 3 98  ? 120.070 100.561 189.070 1.00 93.61  ? 98  GLU E O     1 
ATOM   16441 C  CB    . GLU E 3 98  ? 119.337 98.785  186.403 1.00 93.61  ? 98  GLU E CB    1 
ATOM   16442 C  CG    . GLU E 3 98  ? 119.457 97.291  186.725 1.00 93.61  ? 98  GLU E CG    1 
ATOM   16443 C  CD    . GLU E 3 98  ? 120.371 96.540  185.743 1.00 93.61  ? 98  GLU E CD    1 
ATOM   16444 O  OE1   . GLU E 3 98  ? 120.781 97.131  184.717 1.00 93.61  ? 98  GLU E OE1   1 
ATOM   16445 O  OE2   . GLU E 3 98  ? 120.701 95.373  186.058 1.00 93.61  ? 98  GLU E OE2   1 
ATOM   16446 N  N     . LEU E 3 99  ? 119.455 101.813 187.308 1.00 92.43  ? 99  LEU E N     1 
ATOM   16447 C  CA    . LEU E 3 99  ? 120.233 102.993 187.675 1.00 92.43  ? 99  LEU E CA    1 
ATOM   16448 C  C     . LEU E 3 99  ? 119.754 103.594 189.006 1.00 92.43  ? 99  LEU E C     1 
ATOM   16449 O  O     . LEU E 3 99  ? 120.569 103.900 189.867 1.00 92.43  ? 99  LEU E O     1 
ATOM   16450 C  CB    . LEU E 3 99  ? 120.143 103.989 186.508 1.00 92.43  ? 99  LEU E CB    1 
ATOM   16451 C  CG    . LEU E 3 99  ? 121.223 105.086 186.543 1.00 92.43  ? 99  LEU E CG    1 
ATOM   16452 C  CD1   . LEU E 3 99  ? 122.213 104.905 185.389 1.00 92.43  ? 99  LEU E CD1   1 
ATOM   16453 C  CD2   . LEU E 3 99  ? 120.589 106.461 186.366 1.00 92.43  ? 99  LEU E CD2   1 
ATOM   16454 N  N     . VAL E 3 100 ? 118.439 103.705 189.209 1.00 93.10  ? 100 VAL E N     1 
ATOM   16455 C  CA    . VAL E 3 100 ? 117.852 104.258 190.441 1.00 93.10  ? 100 VAL E CA    1 
ATOM   16456 C  C     . VAL E 3 100 ? 117.924 103.269 191.607 1.00 93.10  ? 100 VAL E C     1 
ATOM   16457 O  O     . VAL E 3 100 ? 118.264 103.665 192.720 1.00 93.10  ? 100 VAL E O     1 
ATOM   16458 C  CB    . VAL E 3 100 ? 116.403 104.708 190.182 1.00 93.10  ? 100 VAL E CB    1 
ATOM   16459 C  CG1   . VAL E 3 100 ? 115.696 105.117 191.478 1.00 93.10  ? 100 VAL E CG1   1 
ATOM   16460 C  CG2   . VAL E 3 100 ? 116.371 105.913 189.227 1.00 93.10  ? 100 VAL E CG2   1 
ATOM   16461 N  N     . ASN E 3 101 ? 117.647 101.981 191.376 1.00 93.56  ? 101 ASN E N     1 
ATOM   16462 C  CA    . ASN E 3 101 ? 117.604 100.952 192.426 1.00 93.56  ? 101 ASN E CA    1 
ATOM   16463 C  C     . ASN E 3 101 ? 118.934 100.792 193.171 1.00 93.56  ? 101 ASN E C     1 
ATOM   16464 O  O     . ASN E 3 101 ? 118.933 100.361 194.322 1.00 93.56  ? 101 ASN E O     1 
ATOM   16465 C  CB    . ASN E 3 101 ? 117.197 99.600  191.814 1.00 93.56  ? 101 ASN E CB    1 
ATOM   16466 C  CG    . ASN E 3 101 ? 115.700 99.441  191.622 1.00 93.56  ? 101 ASN E CG    1 
ATOM   16467 O  OD1   . ASN E 3 101 ? 114.889 99.880  192.416 1.00 93.56  ? 101 ASN E OD1   1 
ATOM   16468 N  ND2   . ASN E 3 101 ? 115.276 98.740  190.599 1.00 93.56  ? 101 ASN E ND2   1 
ATOM   16469 N  N     . LYS E 3 102 ? 120.059 101.154 192.547 1.00 92.85  ? 102 LYS E N     1 
ATOM   16470 C  CA    . LYS E 3 102 ? 121.373 101.182 193.207 1.00 92.85  ? 102 LYS E CA    1 
ATOM   16471 C  C     . LYS E 3 102 ? 121.444 102.161 194.383 1.00 92.85  ? 102 LYS E C     1 
ATOM   16472 O  O     . LYS E 3 102 ? 122.324 102.004 195.225 1.00 92.85  ? 102 LYS E O     1 
ATOM   16473 C  CB    . LYS E 3 102 ? 122.435 101.582 192.182 1.00 92.85  ? 102 LYS E CB    1 
ATOM   16474 C  CG    . LYS E 3 102 ? 122.705 100.505 191.124 1.00 92.85  ? 102 LYS E CG    1 
ATOM   16475 C  CD    . LYS E 3 102 ? 123.545 101.158 190.026 1.00 92.85  ? 102 LYS E CD    1 
ATOM   16476 C  CE    . LYS E 3 102 ? 123.647 100.333 188.750 1.00 92.85  ? 102 LYS E CE    1 
ATOM   16477 N  NZ    . LYS E 3 102 ? 124.410 101.127 187.752 1.00 92.85  ? 102 LYS E NZ    1 
ATOM   16478 N  N     . HIS E 3 103 ? 120.555 103.154 194.434 1.00 92.02  ? 103 HIS E N     1 
ATOM   16479 C  CA    . HIS E 3 103 ? 120.624 104.280 195.372 1.00 92.02  ? 103 HIS E CA    1 
ATOM   16480 C  C     . HIS E 3 103 ? 119.422 104.395 196.313 1.00 92.02  ? 103 HIS E C     1 
ATOM   16481 O  O     . HIS E 3 103 ? 119.427 105.290 197.164 1.00 92.02  ? 103 HIS E O     1 
ATOM   16482 C  CB    . HIS E 3 103 ? 120.834 105.574 194.575 1.00 92.02  ? 103 HIS E CB    1 
ATOM   16483 C  CG    . HIS E 3 103 ? 122.075 105.524 193.728 1.00 92.02  ? 103 HIS E CG    1 
ATOM   16484 N  ND1   . HIS E 3 103 ? 123.385 105.515 194.213 1.00 92.02  ? 103 HIS E ND1   1 
ATOM   16485 C  CD2   . HIS E 3 103 ? 122.099 105.395 192.374 1.00 92.02  ? 103 HIS E CD2   1 
ATOM   16486 C  CE1   . HIS E 3 103 ? 124.169 105.393 193.131 1.00 92.02  ? 103 HIS E CE1   1 
ATOM   16487 N  NE2   . HIS E 3 103 ? 123.421 105.311 192.020 1.00 92.02  ? 103 HIS E NE2   1 
ATOM   16488 N  N     . LEU E 3 104 ? 118.428 103.510 196.180 1.00 89.57  ? 104 LEU E N     1 
ATOM   16489 C  CA    . LEU E 3 104 ? 117.247 103.441 197.053 1.00 89.57  ? 104 LEU E CA    1 
ATOM   16490 C  C     . LEU E 3 104 ? 117.547 102.908 198.464 1.00 89.57  ? 104 LEU E C     1 
ATOM   16491 O  O     . LEU E 3 104 ? 118.566 102.205 198.645 1.00 89.57  ? 104 LEU E O     1 
ATOM   16492 C  CB    . LEU E 3 104 ? 116.138 102.628 196.352 1.00 89.57  ? 104 LEU E CB    1 
ATOM   16493 C  CG    . LEU E 3 104 ? 115.492 103.310 195.139 1.00 89.57  ? 104 LEU E CG    1 
ATOM   16494 C  CD1   . LEU E 3 104 ? 114.418 102.388 194.580 1.00 89.57  ? 104 LEU E CD1   1 
ATOM   16495 C  CD2   . LEU E 3 104 ? 114.809 104.629 195.495 1.00 89.57  ? 104 LEU E CD2   1 
ATOM   16496 O  OXT   . LEU E 3 104 ? 116.723 103.231 199.348 1.00 89.57  ? 104 LEU E OXT   1 
HETATM 16497 P  PA    . TTP F 4 .   ? 145.409 144.674 133.546 1.00 38.66  ? 801 TTP A PA    1 
HETATM 16498 O  O1A   . TTP F 4 .   ? 144.034 145.277 133.416 1.00 42.70  ? 801 TTP A O1A   1 
HETATM 16499 O  O2A   . TTP F 4 .   ? 146.400 145.397 132.666 1.00 43.26  ? 801 TTP A O2A   1 
HETATM 16500 O  O3A   . TTP F 4 .   ? 145.875 144.643 135.084 1.00 48.32  ? 801 TTP A O3A   1 
HETATM 16501 P  PB    . TTP F 4 .   ? 147.068 145.581 135.613 1.00 46.19  ? 801 TTP A PB    1 
HETATM 16502 O  O1B   . TTP F 4 .   ? 147.232 146.829 134.782 1.00 46.96  ? 801 TTP A O1B   1 
HETATM 16503 O  O2B   . TTP F 4 .   ? 146.837 145.936 137.061 1.00 44.37  ? 801 TTP A O2B   1 
HETATM 16504 O  O3B   . TTP F 4 .   ? 148.324 144.590 135.445 1.00 42.96  ? 801 TTP A O3B   1 
HETATM 16505 P  PG    . TTP F 4 .   ? 149.760 145.145 134.982 1.00 47.86  ? 801 TTP A PG    1 
HETATM 16506 O  O1G   . TTP F 4 .   ? 149.993 146.527 135.546 1.00 48.77  ? 801 TTP A O1G   1 
HETATM 16507 O  O2G   . TTP F 4 .   ? 149.805 145.184 133.476 1.00 48.58  ? 801 TTP A O2G   1 
HETATM 16508 O  O3G   . TTP F 4 .   ? 150.837 144.207 135.470 1.00 45.20  ? 801 TTP A O3G   1 
HETATM 16509 O  "O5'" . TTP F 4 .   ? 145.388 143.110 133.180 1.00 31.26  ? 801 TTP A "O5'" 1 
HETATM 16510 C  "C5'" . TTP F 4 .   ? 146.327 142.624 132.227 1.00 41.84  ? 801 TTP A "C5'" 1 
HETATM 16511 C  "C4'" . TTP F 4 .   ? 146.121 141.139 131.978 1.00 43.19  ? 801 TTP A "C4'" 1 
HETATM 16512 O  "O4'" . TTP F 4 .   ? 145.779 140.479 133.194 1.00 41.64  ? 801 TTP A "O4'" 1 
HETATM 16513 C  "C3'" . TTP F 4 .   ? 144.980 140.879 131.014 1.00 41.37  ? 801 TTP A "C3'" 1 
HETATM 16514 O  "O3'" . TTP F 4 .   ? 145.473 140.628 129.696 1.00 38.80  ? 801 TTP A "O3'" 1 
HETATM 16515 C  "C2'" . TTP F 4 .   ? 144.284 139.645 131.552 1.00 45.87  ? 801 TTP A "C2'" 1 
HETATM 16516 C  "C1'" . TTP F 4 .   ? 144.897 139.391 132.920 1.00 46.86  ? 801 TTP A "C1'" 1 
HETATM 16517 N  N1    . TTP F 4 .   ? 143.852 139.313 133.942 1.00 38.94  ? 801 TTP A N1    1 
HETATM 16518 C  C2    . TTP F 4 .   ? 143.250 138.068 134.218 1.00 42.98  ? 801 TTP A C2    1 
HETATM 16519 O  O2    . TTP F 4 .   ? 143.624 137.055 133.591 1.00 46.36  ? 801 TTP A O2    1 
HETATM 16520 N  N3    . TTP F 4 .   ? 142.293 137.947 135.146 1.00 45.81  ? 801 TTP A N3    1 
HETATM 16521 C  C4    . TTP F 4 .   ? 141.877 139.013 135.832 1.00 44.47  ? 801 TTP A C4    1 
HETATM 16522 O  O4    . TTP F 4 .   ? 140.983 138.901 136.697 1.00 47.60  ? 801 TTP A O4    1 
HETATM 16523 C  C5    . TTP F 4 .   ? 142.490 140.334 135.558 1.00 45.17  ? 801 TTP A C5    1 
HETATM 16524 C  C5M   . TTP F 4 .   ? 142.048 141.555 136.314 1.00 44.48  ? 801 TTP A C5M   1 
HETATM 16525 C  C6    . TTP F 4 .   ? 143.479 140.420 134.591 1.00 43.33  ? 801 TTP A C6    1 
HETATM 16526 MG MG    . MG  G 5 .   ? 147.486 147.040 131.887 1.00 39.74  ? 802 MG  A MG    1 
HETATM 16527 P  PG    . ATP H 6 .   ? 107.925 136.448 79.450  1.00 89.84  ? 803 ATP A PG    1 
HETATM 16528 O  O1G   . ATP H 6 .   ? 109.397 136.253 79.317  1.00 77.50  ? 803 ATP A O1G   1 
HETATM 16529 O  O2G   . ATP H 6 .   ? 107.538 137.646 80.324  1.00 75.92  ? 803 ATP A O2G   1 
HETATM 16530 O  O3G   . ATP H 6 .   ? 107.192 136.550 78.108  1.00 76.37  ? 803 ATP A O3G   1 
HETATM 16531 P  PB    . ATP H 6 .   ? 105.827 134.673 80.636  1.00 86.04  ? 803 ATP A PB    1 
HETATM 16532 O  O1B   . ATP H 6 .   ? 104.853 135.777 80.745  1.00 78.66  ? 803 ATP A O1B   1 
HETATM 16533 O  O2B   . ATP H 6 .   ? 105.439 133.525 79.706  1.00 74.68  ? 803 ATP A O2B   1 
HETATM 16534 O  O3B   . ATP H 6 .   ? 107.257 135.192 80.179  1.00 80.83  ? 803 ATP A O3B   1 
HETATM 16535 P  PA    . ATP H 6 .   ? 106.007 132.624 82.761  1.00 83.90  ? 803 ATP A PA    1 
HETATM 16536 O  O1A   . ATP H 6 .   ? 107.113 131.716 82.394  1.00 73.36  ? 803 ATP A O1A   1 
HETATM 16537 O  O2A   . ATP H 6 .   ? 104.609 132.105 82.429  1.00 78.01  ? 803 ATP A O2A   1 
HETATM 16538 O  O3A   . ATP H 6 .   ? 106.156 134.041 82.059  1.00 77.55  ? 803 ATP A O3A   1 
HETATM 16539 O  "O5'" . ATP H 6 .   ? 106.046 133.001 84.293  1.00 77.37  ? 803 ATP A "O5'" 1 
HETATM 16540 C  "C5'" . ATP H 6 .   ? 105.474 134.235 84.775  1.00 74.63  ? 803 ATP A "C5'" 1 
HETATM 16541 C  "C4'" . ATP H 6 .   ? 106.502 134.960 85.607  1.00 74.40  ? 803 ATP A "C4'" 1 
HETATM 16542 O  "O4'" . ATP H 6 .   ? 107.094 134.041 86.551  1.00 75.89  ? 803 ATP A "O4'" 1 
HETATM 16543 C  "C3'" . ATP H 6 .   ? 107.673 135.546 84.828  1.00 75.44  ? 803 ATP A "C3'" 1 
HETATM 16544 O  "O3'" . ATP H 6 .   ? 107.371 136.853 84.356  1.00 73.55  ? 803 ATP A "O3'" 1 
HETATM 16545 C  "C2'" . ATP H 6 .   ? 108.784 135.566 85.879  1.00 75.53  ? 803 ATP A "C2'" 1 
HETATM 16546 O  "O2'" . ATP H 6 .   ? 108.688 136.706 86.726  1.00 74.32  ? 803 ATP A "O2'" 1 
HETATM 16547 C  "C1'" . ATP H 6 .   ? 108.486 134.287 86.666  1.00 72.95  ? 803 ATP A "C1'" 1 
HETATM 16548 N  N9    . ATP H 6 .   ? 109.203 133.110 86.188  1.00 71.48  ? 803 ATP A N9    1 
HETATM 16549 C  C8    . ATP H 6 .   ? 108.687 132.057 85.479  1.00 73.72  ? 803 ATP A C8    1 
HETATM 16550 N  N7    . ATP H 6 .   ? 109.564 131.130 85.181  1.00 73.74  ? 803 ATP A N7    1 
HETATM 16551 C  C5    . ATP H 6 .   ? 110.743 131.605 85.736  1.00 77.26  ? 803 ATP A C5    1 
HETATM 16552 C  C6    . ATP H 6 .   ? 112.052 131.089 85.773  1.00 75.28  ? 803 ATP A C6    1 
HETATM 16553 N  N6    . ATP H 6 .   ? 112.410 129.927 85.216  1.00 72.17  ? 803 ATP A N6    1 
HETATM 16554 N  N1    . ATP H 6 .   ? 112.997 131.815 86.409  1.00 70.82  ? 803 ATP A N1    1 
HETATM 16555 C  C2    . ATP H 6 .   ? 112.648 132.977 86.965  1.00 69.72  ? 803 ATP A C2    1 
HETATM 16556 N  N3    . ATP H 6 .   ? 111.450 133.564 86.996  1.00 71.91  ? 803 ATP A N3    1 
HETATM 16557 C  C4    . ATP H 6 .   ? 110.535 132.825 86.360  1.00 73.82  ? 803 ATP A C4    1 
HETATM 16558 P  PB    . GDP I 7 .   ? 104.370 151.615 83.984  1.00 86.77  ? 804 GDP A PB    1 
HETATM 16559 O  O1B   . GDP I 7 .   ? 104.160 150.341 83.201  1.00 69.94  ? 804 GDP A O1B   1 
HETATM 16560 O  O2B   . GDP I 7 .   ? 104.699 152.736 83.028  1.00 71.43  ? 804 GDP A O2B   1 
HETATM 16561 O  O3B   . GDP I 7 .   ? 103.115 151.946 84.754  1.00 72.91  ? 804 GDP A O3B   1 
HETATM 16562 O  O3A   . GDP I 7 .   ? 105.600 151.413 84.998  1.00 73.18  ? 804 GDP A O3A   1 
HETATM 16563 P  PA    . GDP I 7 .   ? 105.409 150.685 86.420  1.00 77.70  ? 804 GDP A PA    1 
HETATM 16564 O  O1A   . GDP I 7 .   ? 105.356 151.685 87.550  1.00 71.30  ? 804 GDP A O1A   1 
HETATM 16565 O  O2A   . GDP I 7 .   ? 104.181 149.807 86.418  1.00 70.91  ? 804 GDP A O2A   1 
HETATM 16566 O  "O5'" . GDP I 7 .   ? 106.744 149.796 86.504  1.00 72.45  ? 804 GDP A "O5'" 1 
HETATM 16567 C  "C5'" . GDP I 7 .   ? 107.977 150.351 86.954  1.00 70.07  ? 804 GDP A "C5'" 1 
HETATM 16568 C  "C4'" . GDP I 7 .   ? 109.010 149.237 86.959  1.00 65.18  ? 804 GDP A "C4'" 1 
HETATM 16569 O  "O4'" . GDP I 7 .   ? 109.130 148.734 88.289  1.00 67.00  ? 804 GDP A "O4'" 1 
HETATM 16570 C  "C3'" . GDP I 7 .   ? 108.542 148.091 86.075  1.00 69.06  ? 804 GDP A "C3'" 1 
HETATM 16571 O  "O3'" . GDP I 7 .   ? 109.546 147.758 85.115  1.00 70.95  ? 804 GDP A "O3'" 1 
HETATM 16572 C  "C2'" . GDP I 7 .   ? 108.319 146.914 86.998  1.00 70.71  ? 804 GDP A "C2'" 1 
HETATM 16573 O  "O2'" . GDP I 7 .   ? 108.919 145.738 86.451  1.00 74.21  ? 804 GDP A "O2'" 1 
HETATM 16574 C  "C1'" . GDP I 7 .   ? 108.995 147.313 88.299  1.00 70.10  ? 804 GDP A "C1'" 1 
HETATM 16575 N  N9    . GDP I 7 .   ? 108.228 146.875 89.493  1.00 66.83  ? 804 GDP A N9    1 
HETATM 16576 C  C8    . GDP I 7 .   ? 108.775 146.318 90.588  1.00 67.54  ? 804 GDP A C8    1 
HETATM 16577 N  N7    . GDP I 7 .   ? 107.832 146.029 91.516  1.00 68.66  ? 804 GDP A N7    1 
HETATM 16578 C  C5    . GDP I 7 .   ? 106.646 146.419 91.020  1.00 70.74  ? 804 GDP A C5    1 
HETATM 16579 C  C6    . GDP I 7 .   ? 105.242 146.407 91.490  1.00 69.86  ? 804 GDP A C6    1 
HETATM 16580 O  O6    . GDP I 7 .   ? 104.946 145.945 92.612  1.00 70.16  ? 804 GDP A O6    1 
HETATM 16581 N  N1    . GDP I 7 .   ? 104.303 146.903 90.677  1.00 69.83  ? 804 GDP A N1    1 
HETATM 16582 C  C2    . GDP I 7 .   ? 104.596 147.407 89.465  1.00 67.15  ? 804 GDP A C2    1 
HETATM 16583 N  N2    . GDP I 7 .   ? 103.587 147.892 88.703  1.00 66.79  ? 804 GDP A N2    1 
HETATM 16584 N  N3    . GDP I 7 .   ? 105.859 147.452 88.972  1.00 66.64  ? 804 GDP A N3    1 
HETATM 16585 C  C4    . GDP I 7 .   ? 106.908 146.981 89.688  1.00 68.58  ? 804 GDP A C4    1 
HETATM 16586 MG MG    . MG  J 5 .   ? 118.005 150.685 124.093 1.00 23.04  ? 801 MG  B MG    1 
HETATM 16587 P  PA    . TTP K 4 .   ? 119.430 147.544 122.956 1.00 38.14  ? 802 TTP B PA    1 
HETATM 16588 O  O1A   . TTP K 4 .   ? 120.933 147.558 122.822 1.00 32.84  ? 802 TTP B O1A   1 
HETATM 16589 O  O2A   . TTP K 4 .   ? 118.951 148.711 123.785 1.00 36.02  ? 802 TTP B O2A   1 
HETATM 16590 O  O3A   . TTP K 4 .   ? 118.721 147.521 121.514 1.00 38.55  ? 802 TTP B O3A   1 
HETATM 16591 P  PB    . TTP K 4 .   ? 118.552 148.859 120.641 1.00 40.67  ? 802 TTP B PB    1 
HETATM 16592 O  O1B   . TTP K 4 .   ? 118.917 150.096 121.424 1.00 39.27  ? 802 TTP B O1B   1 
HETATM 16593 O  O2B   . TTP K 4 .   ? 119.386 148.769 119.386 1.00 39.33  ? 802 TTP B O2B   1 
HETATM 16594 O  O3B   . TTP K 4 .   ? 116.986 148.830 120.271 1.00 37.78  ? 802 TTP B O3B   1 
HETATM 16595 P  PG    . TTP K 4 .   ? 115.860 149.129 121.385 1.00 33.98  ? 802 TTP B PG    1 
HETATM 16596 O  O1G   . TTP K 4 .   ? 115.630 147.881 122.202 1.00 30.17  ? 802 TTP B O1G   1 
HETATM 16597 O  O2G   . TTP K 4 .   ? 114.566 149.509 120.709 1.00 39.80  ? 802 TTP B O2G   1 
HETATM 16598 O  O3G   . TTP K 4 .   ? 116.298 150.250 122.294 1.00 41.40  ? 802 TTP B O3G   1 
HETATM 16599 O  "O5'" . TTP K 4 .   ? 118.931 146.162 123.604 1.00 30.68  ? 802 TTP B "O5'" 1 
HETATM 16600 C  "C5'" . TTP K 4 .   ? 118.227 146.190 124.840 1.00 31.77  ? 802 TTP B "C5'" 1 
HETATM 16601 C  "C4'" . TTP K 4 .   ? 117.985 144.775 125.337 1.00 30.48  ? 802 TTP B "C4'" 1 
HETATM 16602 O  "O4'" . TTP K 4 .   ? 118.077 143.845 124.260 1.00 34.93  ? 802 TTP B "O4'" 1 
HETATM 16603 C  "C3'" . TTP K 4 .   ? 119.030 144.352 126.350 1.00 33.58  ? 802 TTP B "C3'" 1 
HETATM 16604 O  "O3'" . TTP K 4 .   ? 118.532 144.498 127.682 1.00 35.23  ? 802 TTP B "O3'" 1 
HETATM 16605 C  "C2'" . TTP K 4 .   ? 119.300 142.892 126.052 1.00 35.50  ? 802 TTP B "C2'" 1 
HETATM 16606 C  "C1'" . TTP K 4 .   ? 118.576 142.599 124.747 1.00 39.81  ? 802 TTP B "C1'" 1 
HETATM 16607 N  N1    . TTP K 4 .   ? 119.495 141.993 123.783 1.00 37.48  ? 802 TTP B N1    1 
HETATM 16608 C  C2    . TTP K 4 .   ? 119.701 140.595 123.813 1.00 36.50  ? 802 TTP B C2    1 
HETATM 16609 O  O2    . TTP K 4 .   ? 119.090 139.904 124.655 1.00 36.23  ? 802 TTP B O2    1 
HETATM 16610 N  N3    . TTP K 4 .   ? 120.529 139.994 122.951 1.00 35.69  ? 802 TTP B N3    1 
HETATM 16611 C  C4    . TTP K 4 .   ? 121.191 140.708 122.039 1.00 37.87  ? 802 TTP B C4    1 
HETATM 16612 O  O4    . TTP K 4 .   ? 121.964 140.149 121.236 1.00 37.46  ? 802 TTP B O4    1 
HETATM 16613 C  C5    . TTP K 4 .   ? 120.996 142.176 121.990 1.00 35.26  ? 802 TTP B C5    1 
HETATM 16614 C  C5M   . TTP K 4 .   ? 121.727 143.005 120.972 1.00 32.09  ? 802 TTP B C5M   1 
HETATM 16615 C  C6    . TTP K 4 .   ? 120.131 142.765 122.897 1.00 35.20  ? 802 TTP B C6    1 
HETATM 16616 P  PG    . ATP L 6 .   ? 153.530 138.625 180.017 1.00 82.63  ? 803 ATP B PG    1 
HETATM 16617 O  O1G   . ATP L 6 .   ? 153.092 137.671 181.074 1.00 70.62  ? 803 ATP B O1G   1 
HETATM 16618 O  O2G   . ATP L 6 .   ? 154.522 139.684 180.515 1.00 71.91  ? 803 ATP B O2G   1 
HETATM 16619 O  O3G   . ATP L 6 .   ? 152.370 139.323 179.298 1.00 69.78  ? 803 ATP B O3G   1 
HETATM 16620 P  PB    . ATP L 6 .   ? 155.644 137.990 177.989 1.00 78.57  ? 803 ATP B PB    1 
HETATM 16621 O  O1B   . ATP L 6 .   ? 155.742 139.308 177.332 1.00 69.20  ? 803 ATP B O1B   1 
HETATM 16622 O  O2B   . ATP L 6 .   ? 156.817 137.610 178.892 1.00 66.79  ? 803 ATP B O2B   1 
HETATM 16623 O  O3B   . ATP L 6 .   ? 154.316 137.855 178.855 1.00 75.48  ? 803 ATP B O3B   1 
HETATM 16624 P  PA    . ATP L 6 .   ? 154.798 135.368 176.911 1.00 74.49  ? 803 ATP B PA    1 
HETATM 16625 O  O1A   . ATP L 6 .   ? 153.429 135.393 177.463 1.00 68.26  ? 803 ATP B O1A   1 
HETATM 16626 O  O2A   . ATP L 6 .   ? 155.765 134.419 177.618 1.00 70.83  ? 803 ATP B O2A   1 
HETATM 16627 O  O3A   . ATP L 6 .   ? 155.460 136.814 176.933 1.00 74.54  ? 803 ATP B O3A   1 
HETATM 16628 O  "O5'" . ATP L 6 .   ? 154.785 135.013 175.373 1.00 70.55  ? 803 ATP B "O5'" 1 
HETATM 16629 C  "C5'" . ATP L 6 .   ? 155.862 135.418 174.503 1.00 68.64  ? 803 ATP B "C5'" 1 
HETATM 16630 C  "C4'" . ATP L 6 .   ? 155.303 136.271 173.391 1.00 68.94  ? 803 ATP B "C4'" 1 
HETATM 16631 O  "O4'" . ATP L 6 .   ? 154.476 135.459 172.528 1.00 71.15  ? 803 ATP B "O4'" 1 
HETATM 16632 C  "C3'" . ATP L 6 .   ? 154.411 137.423 173.841 1.00 68.08  ? 803 ATP B "C3'" 1 
HETATM 16633 O  "O3'" . ATP L 6 .   ? 155.178 138.593 174.103 1.00 68.97  ? 803 ATP B "O3'" 1 
HETATM 16634 C  "C2'" . ATP L 6 .   ? 153.489 137.609 172.635 1.00 70.53  ? 803 ATP B "C2'" 1 
HETATM 16635 O  "O2'" . ATP L 6 .   ? 154.106 138.380 171.611 1.00 69.49  ? 803 ATP B "O2'" 1 
HETATM 16636 C  "C1'" . ATP L 6 .   ? 153.295 136.162 172.177 1.00 69.43  ? 803 ATP B "C1'" 1 
HETATM 16637 N  N9    . ATP L 6 .   ? 152.160 135.489 172.799 1.00 67.69  ? 803 ATP B N9    1 
HETATM 16638 C  C8    . ATP L 6 .   ? 152.199 134.427 173.664 1.00 69.32  ? 803 ATP B C8    1 
HETATM 16639 N  N7    . ATP L 6 .   ? 151.019 134.024 174.069 1.00 69.89  ? 803 ATP B N7    1 
HETATM 16640 C  C5    . ATP L 6 .   ? 150.141 134.883 173.426 1.00 72.52  ? 803 ATP B C5    1 
HETATM 16641 C  C6    . ATP L 6 .   ? 148.736 134.986 173.432 1.00 70.17  ? 803 ATP B C6    1 
HETATM 16642 N  N6    . ATP L 6 .   ? 147.934 134.185 174.140 1.00 67.68  ? 803 ATP B N6    1 
HETATM 16643 N  N1    . ATP L 6 .   ? 148.174 135.955 172.678 1.00 67.83  ? 803 ATP B N1    1 
HETATM 16644 C  C2    . ATP L 6 .   ? 148.969 136.763 171.971 1.00 66.24  ? 803 ATP B C2    1 
HETATM 16645 N  N3    . ATP L 6 .   ? 150.300 136.759 171.885 1.00 66.05  ? 803 ATP B N3    1 
HETATM 16646 C  C4    . ATP L 6 .   ? 150.830 135.792 172.640 1.00 69.17  ? 803 ATP B C4    1 
HETATM 16647 P  PB    . GDP M 7 .   ? 162.574 151.477 172.175 1.00 79.35  ? 804 GDP B PB    1 
HETATM 16648 O  O1B   . GDP M 7 .   ? 162.169 150.310 173.042 1.00 67.14  ? 804 GDP B O1B   1 
HETATM 16649 O  O2B   . GDP M 7 .   ? 162.940 152.648 173.055 1.00 67.24  ? 804 GDP B O2B   1 
HETATM 16650 O  O3B   . GDP M 7 .   ? 163.758 151.087 171.324 1.00 68.08  ? 804 GDP B O3B   1 
HETATM 16651 O  O3A   . GDP M 7 .   ? 161.338 151.883 171.230 1.00 69.78  ? 804 GDP B O3A   1 
HETATM 16652 P  PA    . GDP M 7 .   ? 160.984 151.002 169.929 1.00 71.02  ? 804 GDP B PA    1 
HETATM 16653 O  O1A   . GDP M 7 .   ? 161.698 151.539 168.711 1.00 68.62  ? 804 GDP B O1A   1 
HETATM 16654 O  O2A   . GDP M 7 .   ? 161.337 149.552 170.155 1.00 67.18  ? 804 GDP B O2A   1 
HETATM 16655 O  "O5'" . GDP M 7 .   ? 159.393 151.186 169.782 1.00 65.98  ? 804 GDP B "O5'" 1 
HETATM 16656 C  "C5'" . GDP M 7 .   ? 158.742 150.829 168.568 1.00 65.54  ? 804 GDP B "C5'" 1 
HETATM 16657 C  "C4'" . GDP M 7 .   ? 157.420 150.146 168.885 1.00 63.92  ? 804 GDP B "C4'" 1 
HETATM 16658 O  "O4'" . GDP M 7 .   ? 156.945 149.507 167.700 1.00 64.17  ? 804 GDP B "O4'" 1 
HETATM 16659 C  "C3'" . GDP M 7 .   ? 157.614 149.081 169.950 1.00 68.21  ? 804 GDP B "C3'" 1 
HETATM 16660 O  "O3'" . GDP M 7 .   ? 156.725 149.311 171.047 1.00 68.16  ? 804 GDP B "O3'" 1 
HETATM 16661 C  "C2'" . GDP M 7 .   ? 157.285 147.758 169.291 1.00 66.45  ? 804 GDP B "C2'" 1 
HETATM 16662 O  "O2'" . GDP M 7 .   ? 156.327 147.042 170.074 1.00 64.69  ? 804 GDP B "O2'" 1 
HETATM 16663 C  "C1'" . GDP M 7 .   ? 156.712 148.116 167.929 1.00 64.51  ? 804 GDP B "C1'" 1 
HETATM 16664 N  N9    . GDP M 7 .   ? 157.330 147.317 166.837 1.00 64.21  ? 804 GDP B N9    1 
HETATM 16665 C  C8    . GDP M 7 .   ? 156.660 146.785 165.798 1.00 64.58  ? 804 GDP B C8    1 
HETATM 16666 N  N7    . GDP M 7 .   ? 157.497 146.119 164.964 1.00 65.95  ? 804 GDP B N7    1 
HETATM 16667 C  C5    . GDP M 7 .   ? 158.741 146.233 165.463 1.00 66.21  ? 804 GDP B C5    1 
HETATM 16668 C  C6    . GDP M 7 .   ? 160.093 145.769 165.074 1.00 65.68  ? 804 GDP B C6    1 
HETATM 16669 O  O6    . GDP M 7 .   ? 160.266 145.090 164.040 1.00 68.03  ? 804 GDP B O6    1 
HETATM 16670 N  N1    . GDP M 7 .   ? 161.124 146.098 165.860 1.00 66.68  ? 804 GDP B N1    1 
HETATM 16671 C  C2    . GDP M 7 .   ? 160.967 146.828 166.978 1.00 65.75  ? 804 GDP B C2    1 
HETATM 16672 N  N2    . GDP M 7 .   ? 162.059 147.122 167.723 1.00 65.25  ? 804 GDP B N2    1 
HETATM 16673 N  N3    . GDP M 7 .   ? 159.759 147.286 167.393 1.00 65.49  ? 804 GDP B N3    1 
HETATM 16674 C  C4    . GDP M 7 .   ? 158.628 147.027 166.694 1.00 65.33  ? 804 GDP B C4    1 
HETATM 16675 MN MN    . MN  N 8 .   ? 117.009 85.398  126.486 0.85 25.05  ? 401 MN  C MN    1 
HETATM 16676 MN MN    . MN  O 8 .   ? 115.124 88.434  127.575 0.85 26.37  ? 402 MN  C MN    1 
HETATM 16677 MN MN    . MN  P 8 .   ? 136.247 96.079  136.353 1.00 22.51  ? 401 MN  D MN    1 
HETATM 16678 MN MN    . MN  Q 8 .   ? 138.120 95.020  133.088 1.00 24.72  ? 402 MN  D MN    1 
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